ID A0AYW1_BURCH Unreviewed; 194 AA. AC A0AYW1; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 50. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bcen2424_3850; OS Burkholderia cenocepacia (strain HI2424). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=331272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI2424; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F., RA Konstantinidis K., Tiedje J.M., Richardson P.; RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia RT HI2424."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000459; ABK10587.1; -; Genomic_DNA. DR RefSeq; YP_837480.1; NC_008543.1. DR ProteinModelPortal; A0AYW1; -. DR STRING; 331272.Bcen2424_3850; -. DR EnsemblBacteria; ABK10587; ABK10587; Bcen2424_3850. DR GeneID; 4451806; -. DR KEGG; bch:Bcen2424_3850; -. DR PATRIC; 19065214; VBIBurCen15205_3935. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCEN331272:GHR7-3923-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 19918 MW; C6EB413E18D31159 CRC64; MNAPLPRCCV ITPEPASASA ADRAAFLDRL SAVLARGETL VQLRVKSLDA AAFASLAAAA LARCAAAGAH LMLNGPIDAA GVMRLDGAGW HLDGTALRAA AQRPLPAARW VSAACHTQDD LLLAARAGAD FVTLSPVLPT LSHPGAPALG WARFDALAAQ AAMPVFALGG MTRAHLDDAR RHGAYGIAGI RGFW // ID A0K3U0_BURCH Unreviewed; 375 AA. AC A0K3U0; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 14-MAY-2014, entry version 57. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Bcen2424_0413; OS Burkholderia cenocepacia (strain HI2424). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=331272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI2424; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F., RA Konstantinidis K., Tiedje J.M., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia RT HI2424."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000458; ABK07167.1; -; Genomic_DNA. DR RefSeq; YP_834060.1; NC_008542.1. DR ProteinModelPortal; A0K3U0; -. DR STRING; 331272.Bcen2424_0413; -. DR EnsemblBacteria; ABK07167; ABK07167; Bcen2424_0413. DR GeneID; 4449967; -. DR KEGG; bch:Bcen2424_0413; -. DR PATRIC; 19058014; VBIBurCen15205_0408. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BCEN331272:GHR7-428-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 375 AA; 39196 MW; 4EC4FA8333C5D3FC CRC64; MSAARFADAF WPPADELAEA AERIRARLGD WPEGAAPWRL CVAAPDVPAD GDVLIVSAGD RAAQARASAV SRPASPDAVA IEFDEQGAVL HAAGGRYALD AAHPLADDWI AALAAFLDCG FAPVDALVLA LAWRDGDETR AADAWPVDAA RFPRVAGLPP APEPAFAPCP ARLGLYPVVP SAEWVERVLD GGARTVQLRV KEATPDALRR EIARAVAAGR RYPDARVFIN DHWEIAAEAG AYGVHLGQED LETADLAAIA GAGLRLGLSS HGYYEMLRAL HERPSYLALG PVYATATKAV AAPPQGLARI ARYARFAGAR APLVAIGGVG LDTLPAVLAT GVGSVAVVSA VTGAADYRTV LIALQQCFTG QFDNH // ID A0KFE7_AERHH Unreviewed; 538 AA. AC A0KFE7; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=AHA_0440; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7966 / NCIB 9240; RX PubMed=16980456; DOI=10.1128/JB.00621-06; RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., RA Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., RA Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.; RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all RT trades."; RL J. Bacteriol. 188:8272-8282(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000462; ABK38267.1; -; Genomic_DNA. DR RefSeq; YP_854969.1; NC_008570.1. DR ProteinModelPortal; A0KFE7; -. DR STRING; 380703.AHA_0440; -. DR EnsemblBacteria; ABK38267; ABK38267; AHA_0440. DR GeneID; 4490403; -. DR KEGG; aha:AHA_0440; -. DR PATRIC; 20778370; VBIAerHyd135212_0430. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; AHYD380703:GH2M-441-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 538 AA; 56979 MW; 723D773D14D5F54D CRC64; MSSASGAVSP ADLSPVTDSR PVVWTIAGSD SGGGAGIQAD LHTLHDLGVH GCSVISAITA QNSVAVKMVD PVLMQTFTAQ IDALGLDLPP AAIKVGLLPT RLHVEVLARR LPTVDAPFVV YDPVAIASTG TPMAEPNMLE AVREQLLPRL SLITPNGPEL EALTGLPATS PELVRLAARR LRELGARAVL VKGGHLAWSG DLCLDYYQDE TREFWLTAPR LDTRHGHGTG CCYASAIAAV VAQDYPVEDA ITLARAYLQQ GLAAAQGVGA GPGPIAHLGW PADLAHFPRA VLAGSALDRR FGLYETSSAR LPQGPFAPTE HNLGLYPVVD SVKWLKRLLG AGVKTIQLRI KDLPAAQVAP AIRDAVALGR RHGARLFIND YWQQAIEAGA WGVHLGQEDM ETADLAAIQA AGLRLGISTH GYFELMRARE LAPSYIALGH IFPTNTKAMP SRPQGLKRLH RYRALMCDWP TVAIGGISEE RVAAVKESGV GSIALVSAIT ASDDWQGATE RLLAAVGAGD EPRSALLMTD MQEAAHAL // ID A0KWJ9_SHESA Unreviewed; 560 AA. AC A0KWJ9; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 14-MAY-2014, entry version 60. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Shewana3_1937; OS Shewanella sp. (strain ANA-3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=94122; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANA-3; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J., RA Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000469; ABK48168.1; -; Genomic_DNA. DR RefSeq; YP_869574.1; NC_008577.1. DR ProteinModelPortal; A0KWJ9; -. DR STRING; 94122.Shewana3_1937; -. DR EnsemblBacteria; ABK48168; ABK48168; Shewana3_1937. DR GeneID; 4479734; -. DR KEGG; shn:Shewana3_1937; -. DR PATRIC; 23571679; VBISheSp134792_2241. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SSP94122:GJ9K-2015-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 560 AA; 59145 MW; FB9231BF54495960 CRC64; MTSAKHVSHL APKPIVWTIA GSDSGGGAGI QADLATIKDL GGHGCSVITT LTAQSSVAVD LVEPVSEAML LTQLSTLLAD LPPQAIKIGL LANQQQLHLV ADWLAGFKTQ FPLVPVILDP VMVASCGDEL GDKSTASQPL DFTPFKGLIS LITPNVQELA KLTVTTDKQV SPIHTKAAFA AAAMQLSEQL DCSVLAKGGD VDFAAQASVG INTRDSLSGH KSDITSHRSA TDNQRMAEDL LICHQVTGCT PLDANGCFWL SSARINTRHN HGSGCTLSSA IASVLAFGFV LQDAVVVAKA YVNQGLTYAG GIGQGPGPLA RTAWPHNLTA YPHITAYSEN SLSESSDVQC GAFKRLEPDL GIYPVVDNLL LLEQLLAAGV KTVQLRIKSN ALKSDELEAQ IQTAIALGKH YEAQLFINDH WQLAIKHGAF GVHLGQEDLA VTDLNAIHAA GLALGISSHG YFELLRAHQH APSYIALGHI FPTTTKQMPS APQGLFKLTH YVELLNTHYP LVAIGGIGPS NLLLVKATGV SNIAVVRAIT EANDPVMALA ELTRAWESSL // ID A0L5B1_MAGSM Unreviewed; 206 AA. AC A0L5B1; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Mmc1_0633; OS Magnetococcus sp. (strain MC-1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales; OC Magnetococcaceae; Magnetococcus. OX NCBI_TaxID=156889; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Goodwin L.A., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Richardson P.; RT "Complete sequence of Magnetococcus sp. MC-1."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000471; ABK43154.1; -; Genomic_DNA. DR RefSeq; YP_864560.1; NC_008576.1. DR ProteinModelPortal; A0L5B1; -. DR STRING; 156889.Mmc1_0633; -. DR EnsemblBacteria; ABK43154; ABK43154; Mmc1_0633. DR GeneID; 4481926; -. DR KEGG; mgm:Mmc1_0633; -. DR PATRIC; 22427776; VBIMagSp23654_0655. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSCHTL; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MSP156889:GH36-638-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 21806 MW; FEFA727562AF9667 CRC64; MRAPRLLIIA DLQACPPWSQ WLPAALAGGA RHLLFRAPGM EDASYLQIAQ QLHAQLTPHG AMLLLHNRPH LLPKLPGAGL HMSDGPPSLT AIRHQIGPQV WLGRSCHTLH GGQHAFAQGA DYITLSPLFP TLSHPGAAHL GVAQWQQWAA QLPGPVLALG GITADNAHLA RAAGAYGVAL IRGICGVSDP QTMTARLLGR EIGAKE // ID A0LCT3_MAGSM Unreviewed; 214 AA. AC A0LCT3; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 19-FEB-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mmc1_3286; OS Magnetococcus sp. (strain MC-1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales; OC Magnetococcaceae; Magnetococcus. OX NCBI_TaxID=156889; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Goodwin L.A., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Richardson P.; RT "Complete sequence of Magnetococcus sp. MC-1."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000471; ABK45776.1; -; Genomic_DNA. DR RefSeq; YP_867182.1; NC_008576.1. DR ProteinModelPortal; A0LCT3; -. DR STRING; 156889.Mmc1_3286; -. DR EnsemblBacteria; ABK45776; ABK45776; Mmc1_3286. DR GeneID; 4482256; -. DR KEGG; mgm:Mmc1_3286; -. DR PATRIC; 22433233; VBIMagSp23654_3344. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AMISALW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MSP156889:GH36-3331-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23507 MW; 23B054BBA482D88F CRC64; MSFPTHTLYP ILDQAWLDQS GFHISAEAVA QQFNTLQLPL IQLRSKGEAG AQWAFMQPWA AAFRRHAPNC RLIINDRVDI ALALAADGVH VGQEDLPVAV CRQILGNQAW VGLSTHNAEE IALARQSGCD YIGFGPVHTT DTKQNTYRVQ GYARLAEACH LAAHLPVIAI GGIGKDRITP CMQAGAAGVA MISALWRQED WIERLTDAQH RVHK // ID A0LJA7_SYNFM Unreviewed; 222 AA. AC A0LJA7; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sfum_1824; OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB). OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophobacteraceae; Syntrophobacter. OX NCBI_TaxID=335543; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10017 / MPOB; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G., RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R., RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., RA Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.; RT "Complete sequence of Syntrophobacter fumaroxidans MPOB."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000478; ABK17509.1; -; Genomic_DNA. DR RefSeq; YP_845944.1; NC_008554.1. DR ProteinModelPortal; A0LJA7; -. DR STRING; 335543.Sfum_1824; -. DR EnsemblBacteria; ABK17509; ABK17509; Sfum_1824. DR GeneID; 4459869; -. DR KEGG; sfu:Sfum_1824; -. DR PATRIC; 23849137; VBISynFum78438_2140. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SFUM335543:GH6P-1860-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 24094 MW; 28141F7C77730284 CRC64; MKTTIKAART ALLLDADIYP VTCEKLSNGR TDLEVLDAVI EGGARMIQLR EKDLSKRGLY HLALKFREVT ARARVLFIIN DHLDIALAAE ADGVHLGQDD LPLAAARRLA PDLILGASTH SLEEALRAKH DGADYVNIGP IFPTKTKAGV DRLLGPEAIA AISPHLDIPF TVMGGINASN IDRVLENGAR RIAMVSAITM APDIAETVRA FRKKIRSYSR PS // ID A0LP27_SYNFM Unreviewed; 223 AA. AC A0LP27; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 14-MAY-2014, entry version 57. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sfum_3508; OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB). OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophobacteraceae; Syntrophobacter. OX NCBI_TaxID=335543; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10017 / MPOB; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G., RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R., RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., RA Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.; RT "Complete sequence of Syntrophobacter fumaroxidans MPOB."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000478; ABK19179.1; -; Genomic_DNA. DR RefSeq; YP_847614.1; NC_008554.1. DR ProteinModelPortal; A0LP27; -. DR STRING; 335543.Sfum_3508; -. DR EnsemblBacteria; ABK19179; ABK19179; Sfum_3508. DR GeneID; 4458175; -. DR KEGG; sfu:Sfum_3508; -. DR PATRIC; 23853217; VBISynFum78438_4161. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SFUM335543:GH6P-3564-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23215 MW; 9DA5BCDB416DEC76 CRC64; MGTVSPPVDY TLYLVTDRGL AAGRSFEDIV REGVEGGVTL VQLREKDLAV RDFVACAVAL RNLLGEYRVP LIVNDRVDVA LACGAAGVHL GQDDMDCASA RRIVGRGRIV GVSVSCVEEA VKAEAQGADY LGVSPVFSTP TKTDTPPAVG LEGLRAIRMA VRLPLVAIGG IKAENAADVI RAGADGLAVV SAIMACPEPR VAARTLKAAI AEARARVRTA RIG // ID A0NNF8_9RHOB Unreviewed; 213 AA. AC A0NNF8; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 19-FEB-2014, entry version 32. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=SIAM614_23757; OS Labrenzia aggregata IAM 12614. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=384765; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IAM 12614; RA King G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAUW01000002; EAV45689.1; -; Genomic_DNA. DR ProteinModelPortal; A0NNF8; -. DR EnsemblBacteria; EAV45689; EAV45689; SIAM614_23757. DR PATRIC; 30161553; VBILabAgg74751_0723. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 213 AA; 22675 MW; 11A7B588287D8C28 CRC64; MNRPRLFLVT PPEFDTADMA VKLKQAFTGG DIACVMIYRP GASTKDLQAV ASELVPIIQD GGAAAIVYRD TQAAGRSGAD GVHVDTSLED LKLAVESFKP DRIVGTGGTK LKHDSMEWAE TGVDYILFGK LDLPEKAEAH DRTLASASWW AELFETPCVA LAGNTVETLA DVAATGADFV AVKDAVWQSG SDIATVIAEA NRILDAHPFP EAE // ID A0NTS3_9RHOB Unreviewed; 201 AA. AC A0NTS3; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SIAM614_11928; OS Labrenzia aggregata IAM 12614. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=384765; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IAM 12614; RA King G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAUW01000008; EAV43832.1; -; Genomic_DNA. DR ProteinModelPortal; A0NTS3; -. DR EnsemblBacteria; EAV43832; EAV43832; SIAM614_11928. DR PATRIC; 30165307; VBILabAgg74751_2571. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22346 MW; 217EA52633D0849D CRC64; MKLDPFYPIV DSSDWIERLV PLGIKLVQLR IKDTSDDILR KEIAASRSVC VKHGCHLVVN DYWQLAIEEG CDFVHLGQED LAEADVAAIR KAGLKLGVST HDGEELQTAL STEPDYVALG PVYPTILKEL KWAPQGVEKI GRWRQQIGSL PLVAIGGLNP ERLPGVFENG ADIAAVATDI TRNADPEART REWIEATQRW R // ID A0PYY3_CLONN Unreviewed; 207 AA. AC A0PYY3; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=NT01CX_1504; OS Clostridium novyi (strain NT). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=386415; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NT; RX PubMed=17115055; DOI=10.1038/nbt1256; RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., RA Zhang X., Diaz L.A.Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., RA Vogelstein B., Zhou S.; RT "The genome and transcriptomes of the anti-tumor agent Clostridium RT novyi-NT."; RL Nat. Biotechnol. 24:1573-1580(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000382; ABK61380.1; -; Genomic_DNA. DR RefSeq; YP_877585.1; NC_008593.1. DR ProteinModelPortal; A0PYY3; -. DR STRING; 386415.NT01CX_1504; -. DR EnsemblBacteria; ABK61380; ABK61380; NT01CX_1504. DR GeneID; 4540424; -. DR KEGG; cno:NT01CX_1504; -. DR PATRIC; 19478666; VBICloNov112828_0611. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CNOV386415:GH98-636-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 207 AA; 22973 MW; 36D20928BCE2C774 CRC64; MTLFKGGIQI LYIVTNRKLV QNEEFYDVIE RVAKNKVDYL ALREKDLNDE ELFSLAKDIK IITDKYNVPL IINGNLKVAE DINAYGCQLS YNVLMESSLW KKSKLKVGAS VHSLEEAINA EKAGADYIVA GHIFETDCKK GLKGRGLNFV SNISNHINIP LIAIGGINEN NASSVIKAGA SGVAIMSTAM RKDNVHKIEE ILYKIRT // ID A0RA05_BACAH Unreviewed; 208 AA. AC A0RA05; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=BALH_0666; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=412694; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Al Hakam; RX PubMed=17337577; DOI=10.1128/JB.00241-07; RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Green L.D., Han C.S., Hill K.K., Hitchcock P., RA Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., RA Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., RA Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., RA Wills P.L., Gilna P., Brettin T.S.; RT "The complete genome sequence of Bacillus thuringiensis Al Hakam."; RL J. Bacteriol. 189:3680-3681(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000485; ABK84048.1; -; Genomic_DNA. DR RefSeq; YP_893555.1; NC_008600.1. DR ProteinModelPortal; A0RA05; -. DR STRING; 412694.BALH_0666; -. DR EnsemblBacteria; ABK84048; ABK84048; BALH_0666. DR GeneID; 4546387; -. DR KEGG; btl:BALH_0666; -. DR PATRIC; 18993554; VBIBacThu63319_0781. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BTHU412694:GH1W-739-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 208 AA; 23182 MW; 4046F1BAF5992FB6 CRC64; MNMKNELHVI SNGNMSFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLKKGFPP SKLVINDRID IAILLNIPRV QLGYRSTDVR SVKEKFSYLH AGYSVHSLEE AIEAFKNGAD SLVYGHVFPT DCKKDVPARG LEEISDIARS LSIPIIAIGG ITPENTKDIL ASEVSGIAVM SGIVSSSNPY SKAKSYKESI RKWAEKHV // ID A0RP15_CAMFF Unreviewed; 178 AA. AC A0RP15; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 46. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=CFF8240_0773; OS Campylobacter fetus subsp. fetus (strain 82-40). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=82-40; RA Fouts D.E., Nelson K.E.; RT "Sequence of Campylobacter fetus subsp. fetus 82-40."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000487; ABK82414.1; -; Genomic_DNA. DR RefSeq; YP_891948.1; NC_008599.1. DR ProteinModelPortal; A0RP15; -. DR STRING; 360106.CFF8240_0773; -. DR EnsemblBacteria; ABK82414; ABK82414; CFF8240_0773. DR GeneID; 4538835; -. DR KEGG; cff:CFF8240_0773; -. DR PATRIC; 20036062; VBICamFet25865_0747. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FATPNKG; -. DR OrthoDB; EOG6FJNJD; -. DR BioCyc; CFET360106:GHTH-772-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 178 AA; 19956 MW; 2A7AF017D0996F86 CRC64; MLSYAITDPK LYSNLKDSFF KFERLQTADF ILFRDKICSD YVKKAEIFMS LKPNFKAKFI IHNDLNLALN LKADGIHFSS NLIANLKNTP QSLIKFASTH NEKEIEDAIK LGADFITFSP IFSTPNKGEP VGIETLKKIV LNSSVKVFGL GGITTKKHIK MVELAKAAGF ASIRYFAN // ID A0RQA8_CAMFF Unreviewed; 202 AA. AC A0RQA8; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CFF8240_1234; OS Campylobacter fetus subsp. fetus (strain 82-40). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=82-40; RA Fouts D.E., Nelson K.E.; RT "Sequence of Campylobacter fetus subsp. fetus 82-40."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000487; ABK81976.1; -; Genomic_DNA. DR RefSeq; YP_892391.1; NC_008599.1. DR ProteinModelPortal; A0RQA8; -. DR STRING; 360106.CFF8240_1234; -. DR EnsemblBacteria; ABK81976; ABK81976; CFF8240_1234. DR GeneID; 4538552; -. DR KEGG; cff:CFF8240_1234; -. DR PATRIC; 20036988; VBICamFet25865_1207. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FQFRVKG; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CFET360106:GHTH-1232-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 202 AA; 22067 MW; 4BB9596E0193B20C CRC64; MCQLYVLTDK ELTPQNSISQ QILELLNSGI KLIQYRNKTQ DHDIKLLKSI ANLCDDFNAK FIINDDPFLA KACGAHGVHI GKDDEDIKKA KELLGKNSII GVSCYNDINL ALKAQKDGAS YVAFGAMYPS QTKPNAPLCD HNTIKKAKEN LNVPICVIGG INALNLKEAS ALMPDLIAIV SAAYSPKSIS ENITNLNNII RN // ID A0XZA1_9GAMM Unreviewed; 508 AA. AC A0XZA1; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 19-FEB-2014, entry version 42. DE SubName: Full=Putative phosphomethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase; GN ORFNames=ATW7_18620; OS Alteromonadales bacterium TW-7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales. OX NCBI_TaxID=156578; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TW-7; RA Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVS01000005; EAW28658.1; -; Genomic_DNA. DR ProteinModelPortal; A0XZA1; -. DR EnsemblBacteria; EAW28658; EAW28658; ATW7_18620. DR PATRIC; 24463099; VBIAltBac127053_0907. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 508 AA; 54941 MW; 3ACD4C4FC3A3E0A0 CRC64; MNNVVWTIAG SDSGGGAGIQ ADIKAMQSFG VHGCTAITAL TAQNSLGVEA INAVSTDIIE SQLLALEKDM KAKVIKIGML ANVQQIQLIS EHISHYKAKW PVPPVIVYDP VAIASSGDVL TEEDTVSAIK ECLLPLVDVI TPNTHETQLL TGVYLIGPSA VKDAANKLLS WGAKSVVIKG GHWDFPSGYC IDYCIQNNEE YWLGNKKIQT PHNHGTGCSM ASVIAACLAK DYPLKDAFIL AKAYINQGLK QSVRYGEGIG PVAQTSFPTH LDDYPQVIEP GSWLGDELDF DVPLEFNMAA DFAPCESKQL GLYAVVDSND WLEKCLQQGI KTAQLRVKNK TDTELDELIK QAVDLGNKYR AHVFINDYWQ LAIKHGAYGV HLGQEDLDIA NLAAIKEAGL RLGLSTHGFY EMLRAHNYRP SYMAFGAIYP TTTKDMTGQI QGLDKLKKCV PLMQSYPTVA IGGIDLTRAN EVANTGVGSV AVVRAISEAD DYIAAISSLQ SAINQPNG // ID A0YI47_LYNSP Unreviewed; 360 AA. AC A0YI47; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=L8106_04606; OS Lyngbya sp. (strain PCC 8106) (Lyngbya aestuarii (strain CCY9616)). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Lyngbya. OX NCBI_TaxID=313612; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 8106; RA Stal L., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVU01000001; EAW39193.1; -; Genomic_DNA. DR ProteinModelPortal; A0YI47; -. DR EnsemblBacteria; EAW39193; EAW39193; L8106_04606. DR PATRIC; 30985475; VBILynSp34733_0077. DR OMA; ANCARVQ; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 129 Unknown (By similarity). FT REGION 130 360 Thiamine-phosphate synthase (By FT similarity). FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 360 AA; 40997 MW; D6E1712F81A62503 CRC64; MADQQSWDKR VQPALYRILD ANLDRAREGL RIIEEWCRFG LNSAELAEEC KQLRQELAHW HTMKLRLSRD TPGDLGTELT HPQEEKRDGI DSVLQANFCR VEEALRVLEE YGKIYHPDMG VSFKQMRYRV YTLESRLLAY QRYQLLDDAY LYLVTSPSDK MFSIVEAALQ GGLKLIQYRD KQNDDETRLQ NAEKLCELCH RYNALFIMND RVDLAIASNA DGVHLGQKDI PISLARQLLG PQRIIGRSTT NPQEMQKAVE QGADYVGVGP VYATPTKADK PAAGLDYVRH AAQNCTIPWF AIGGIDMNNF DDVMSVGGER IAVVRAIMQA EQPTLVTQYF LSQLTRVQTL RAYNILPNPS // ID A0ZEK1_NODSP Unreviewed; 368 AA. AC A0ZEK1; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 19-FEB-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=N9414_18273; OS Nodularia spumigena CCY9414. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nodularia. OX NCBI_TaxID=313624; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCY9414; RA Stal L., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVW01000023; EAW45660.1; -; Genomic_DNA. DR ProteinModelPortal; A0ZEK1; -. DR EnsemblBacteria; EAW45660; EAW45660; N9414_18273. DR PATRIC; 25517257; VBINodSpu128623_1851. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 148 Unknown (By similarity). FT REGION 149 368 Thiamine-phosphate synthase (By FT similarity). FT REGION 196 200 HMP-PP binding (By similarity). FT REGION 293 295 THZ-P binding (By similarity). FT METAL 229 229 Magnesium (By similarity). FT METAL 248 248 Magnesium (By similarity). FT BINDING 228 228 HMP-PP (By similarity). FT BINDING 267 267 HMP-PP (By similarity). FT BINDING 296 296 HMP-PP (By similarity). FT BINDING 323 323 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 368 AA; 41405 MW; 7DDAA535D35A4868 CRC64; MSKSVEITSF KESNNRVVVM VEPHSQKAQI QQVVYRILDA NLDRAREGLR IIEEWCRFGL NNAQLLGECK YLRQELAHWH TAELRAARDT PGDPGTELTH PQEEQRSSIK ALLQANFCRV QEAMRVLEEY GKLYHPNMGK AFKQMRYRVY TLESSLMGYE RYQLLWRSHL YLVTSPSETL FKTVEAALKG GLTLVQYRDK TADDTVRVEQ ATKLRQLCHS YGALFIINDR VDLALAVDAD GVHLGQQDMP IAMARQLLGH QRLIGRSTTN AEEMQKAIAE GADYIGVGPV YETPTKADKA AAGLEYVSYA AQNSSIPWFA IGGIDANNIN DVISAGAERV AVVRAIIQAE QPTLVTQYLV SQLHRIKL // ID A1A2J3_BIFAA Unreviewed; 251 AA. AC A1A2J3; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BAD_1145; OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC OS 11814 / E194a). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=367928; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a; RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., RA Hirai S., Tanaka K., Watanabe K.; RT "Bifidobacterium adolescentis complete genome sequence."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009256; BAF39926.1; -; Genomic_DNA. DR RefSeq; YP_910008.1; NC_008618.1. DR ProteinModelPortal; A1A2J3; -. DR STRING; 367928.BAD_1145; -. DR DNASU; 4556116; -. DR EnsemblBacteria; BAF39926; BAF39926; BAD_1145. DR GeneID; 4556116; -. DR KEGG; bad:BAD_1145; -. DR PATRIC; 21101727; VBIBifAdo27973_1227. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; RPTPTKN; -. DR OrthoDB; EOG6NWBM5; -. DR BioCyc; BADO367928:GHPT-1192-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 156 158 THZ-P binding (By similarity). FT REGION 215 216 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 108 108 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 127 127 HMP-PP (By similarity). FT BINDING 159 159 HMP-PP (By similarity). FT BINDING 195 195 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 251 AA; 26736 MW; EC3CC4F106F49CB1 CRC64; MNNYPFASMR DCFDMSAYFV VGPQDCKGRP VTDVVDDALR GGATFIQLRA KNADAKDITE MARDIAQVIK NSGKSDSVAF VIDDRVDVVW QARDKGIKVD GVHIGQTDME PQEARALLGE DAIVGLSAET ESLVKLINEL PSGCIDYIGA GPLHVSTTKP EASVGGNDGS GHTLDEEQIN AICAASEFPV VVGGGVHADD MEMLARSKAA GWFVVSAIAG ADDPEAATRE MVTRWKAVRG DAKHGYAPRV K // ID A1AS79_PELPD Unreviewed; 494 AA. AC A1AS79; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 56. DE SubName: Full=Phosphomethylpyrimidine kinase; GN OrderedLocusNames=Ppro_2595; OS Pelobacter propionicus (strain DSM 2379). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Pelobacteraceae; Pelobacter. OX NCBI_TaxID=338966; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2379; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Lovley D., Richardson P.; RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000482; ABL00200.1; -; Genomic_DNA. DR RefSeq; YP_902257.1; NC_008609.1. DR ProteinModelPortal; A1AS79; -. DR STRING; 338966.Ppro_2595; -. DR EnsemblBacteria; ABL00200; ABL00200; Ppro_2595. DR GeneID; 4572928; -. DR KEGG; ppd:Ppro_2595; -. DR PATRIC; 22898291; VBIPelPro64470_2751. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OMA; YLAQGEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PPRO338966:GHL0-2636-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 494 AA; 52257 MW; 6693304A5CEEC04D CRC64; MSDSGKPFRL VVNRNTHSSP ITGVYLVTDQ DDDLVERVST ALKGGVSALQ YRAKGKERCH CLSEAAELKR LCRDFGVAFI VNDDMLLAKV LEADGVHLGQ DDGSVAQARA LLGPDSIIGK STHDLREALE AEAEGADYIG FGSMYPTTSK SVSHLPGTTG LMEIRDRIRL PIVAIGGITP ANACRVVDAG ADALAVISSV LSSPRPDVAV TELKLLFNRR RPLPRGAVLT VAGSDSGGGA GIQADIKTIT LLGSYAASVL TALTAQNTRG VSSIHGLPPS FVMDQLDSVL ADIPIDVIKT GMLHTPAIVS ALAERLGERT TLLPLVIDPV MIAKGGAALM EREAAQTFLE QLMPLAYLLT PNIPETERLL GRTIQNEAET EQAARDLHAL GAANVLIKGG HMGGRLSTDI LFDGRECHHF SVERVFTSNT HGTGCTYASA IAAFLAQGEP LRTAVERAKQ FITAAIQLAR PLGRGHSPVN HFAAAQQTAA HPLS // ID A1AUP8_PELPD Unreviewed; 223 AA. AC A1AUP8; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 59. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ppro_3476; OS Pelobacter propionicus (strain DSM 2379). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Pelobacteraceae; Pelobacter. OX NCBI_TaxID=338966; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2379; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Lovley D., Richardson P.; RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000482; ABL01069.1; -; Genomic_DNA. DR RefSeq; YP_903126.1; NC_008609.1. DR ProteinModelPortal; A1AUP8; -. DR STRING; 338966.Ppro_3476; -. DR EnsemblBacteria; ABL01069; ABL01069; Ppro_3476. DR GeneID; 4572504; -. DR KEGG; ppd:Ppro_3476; -. DR PATRIC; 22900097; VBIPelPro64470_3634. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPRO338966:GHL0-3534-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23438 MW; 052B27D94F23C177 CRC64; MSTVSRGEGQ SRCVDFSLYL ITDRRQTAGR PLLDVVAAAL RGGVGAVQLR EKDLPDNELL ELARDLRRLT HEHHARLLIN RRVDVCQAVG ADGVQLGIEG LSIVEARRLL GDGPLIGYSA HAVEEARRAE ASGADFVTLS PVYHTPSKAP FGEPLGPDRL GEACGALGIP VFALGGIKGS TIARVMAAGA HGVALISAIT AAANPETEAA SLLQTIEQHE TLS // ID A1AVC4_RUTMC Unreviewed; 193 AA. AC A1AVC4; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 54. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rmag_0082; OS Ruthia magnifica subsp. Calyptogena magnifica. OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=413404; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Cm; RX PubMed=17303757; DOI=10.1126/science.1138438; RA Newton I.L., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., RA Cavanaugh C.M.; RT "The Calyptogena magnifica chemoautotrophic symbiont genome."; RL Science 315:998-1000(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000488; ABL01881.1; -; Genomic_DNA. DR RefSeq; YP_903352.1; NC_008610.1. DR ProteinModelPortal; A1AVC4; -. DR STRING; 413404.Rmag_0082; -. DR EnsemblBacteria; ABL01881; ABL01881; Rmag_0082. DR GeneID; 4554704; -. DR KEGG; rma:Rmag_0082; -. DR PATRIC; 31999729; VBICanRut45856_0097. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CIGGINE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CRUT413404:GHM7-86-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 193 AA; 21498 MW; 4996F2817D3319B0 CRC64; MVFNKKISNI YAVTPNTFLN SALIKRVIIE HQISILQYRH KINDDNIKLK EAYALRLLCL EYNTLFIIND DINLAEKIHA DGVHLGKDDD SIQQARQQLG DAAIIGMSCY DNIDLALQAQ NQGASYVAFG ALFDSNTKPN APYCPFSLIT KVKKILNIPI VGIGGIDLHN QQQAFDAGCD AVAMINTLFK KHH // ID A1AXR5_RUTMC Unreviewed; 307 AA. AC A1AXR5; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 62. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=Rmag_1016; OS Ruthia magnifica subsp. Calyptogena magnifica. OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=413404; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Cm; RX PubMed=17303757; DOI=10.1126/science.1138438; RA Newton I.L., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., RA Cavanaugh C.M.; RT "The Calyptogena magnifica chemoautotrophic symbiont genome."; RL Science 315:998-1000(2007). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000488; ABL02722.1; -; Genomic_DNA. DR RefSeq; YP_904193.1; NC_008610.1. DR ProteinModelPortal; A1AXR5; -. DR STRING; 413404.Rmag_1016; -. DR EnsemblBacteria; ABL02722; ABL02722; Rmag_1016. DR GeneID; 4555006; -. DR KEGG; rma:Rmag_1016; -. DR PATRIC; 32001843; VBICanRut45856_1121. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CRUT413404:GHM7-1056-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 307 AA; 34755 MW; 3664C50833F7C945 CRC64; MEIIKTVVGV LRNKNQEILI SKRKKEQFMG GFWELPGGKI ETGESLKQAI IRELKEELGI QVNQLTLHKT MMHKYEDRAV QLSIYNINEH QNTPLGIEGQ AISWASVDEL NNYKLLPTMK AFISSITLPN KYWITPSSNH QSDEWMGKFN QKLNSDITLL QLRSKIELDN SFIRELNNKC KKNNIKLLLN TINKTFNEPY CDGWHLTTTE MLKLSKRPCA DNKLLGVSTH NLTEALKAQT MGADFVVISP VQTTKTHPDT ISLGWDIAKE IVDKLNIPVY FLGGMALKDL EKTQQLGAQG IAGISAF // ID A1AY11_PARDP Unreviewed; 198 AA. AC A1AY11; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Pden_0038; OS Paracoccus denitrificans (strain Pd 1222). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paracoccus. OX NCBI_TaxID=318586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pd 1222; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., RA van Spanning R.J.M., Richardson P.; RT "Complete sequence of chromosome 1 of Paracoccus denitrificans RT PD1222."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000489; ABL68155.1; -; Genomic_DNA. DR RefSeq; YP_913851.1; NC_008686.1. DR ProteinModelPortal; A1AY11; -. DR STRING; 318586.Pden_0038; -. DR EnsemblBacteria; ABL68155; ABL68155; Pden_0038. DR GeneID; 4578892; -. DR KEGG; pde:Pden_0038; -. DR PATRIC; 22851251; VBIParDen97112_0038. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PDEN318586:GCVQ-38-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 198 AA; 22146 MW; FF6C2EF27D3404CB CRC64; MRLPRFYPIF DSSDWLRRAL PLGVKLVQIR IKDQPPARLL GELALCQELC REHGAMLVVN DHWQAAIDLG CDFIHLGQED LDEADIPAIR KAGLRLGIST HDHAELDRAL ALRPDYVALG PVWPTILKKM KWEQQGLDRV REWRRLVGAT PLVAIGGVTP ERALEAFTAG ADVASAVTDI TLNPDPEGRI REWLRVAA // ID A1B8C0_PARDP Unreviewed; 203 AA. AC A1B8C0; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Pden_3697; OS Paracoccus denitrificans (strain Pd 1222). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paracoccus. OX NCBI_TaxID=318586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pd 1222; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., RA van Spanning R.J.M., Richardson P.; RT "Complete sequence of chromosome 2 of Paracoccus denitrificans RT PD1222."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000490; ABL71764.1; -; Genomic_DNA. DR RefSeq; YP_917460.1; NC_008687.1. DR ProteinModelPortal; A1B8C0; -. DR STRING; 318586.Pden_3697; -. DR EnsemblBacteria; ABL71764; ABL71764; Pden_3697. DR GeneID; 4582249; -. DR KEGG; pde:Pden_3697; -. DR PATRIC; 22858554; VBIParDen97112_3635. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; PDEN318586:GCVQ-3740-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 203 AA; 21381 MW; 6F44D94134083706 CRC64; MTDQPNSPQL YLITPVGAAA STLGPMLAEV MDRFPVACLR IPGAGTEDEL GRIADLAREI AHARDVAVVI EDHVQLAQRH GLDGVHLTNG ARGVRHARKE LGQDAIVGTF CGASRHDGMN AAEAGADYVS FGPCGATALG HGEIAPLELF QWWSEVIEIP VIAEGALTPA LIGQLAPVAD FIALGAEIWS EPDPAEALGI LWR // ID A1BGM6_CHLPD Unreviewed; 212 AA. AC A1BGM6; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Cpha266_1531; OS Chlorobium phaeobacteroides (strain DSM 266). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290317; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 266; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., RA Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobium phaeobacteroides DSM 266."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000492; ABL65553.1; -; Genomic_DNA. DR RefSeq; YP_911977.1; NC_008639.1. DR ProteinModelPortal; A1BGM6; -. DR STRING; 290317.Cpha266_1531; -. DR EnsemblBacteria; ABL65553; ABL65553; Cpha266_1531. DR GeneID; 4569581; -. DR KEGG; cph:Cpha266_1531; -. DR PATRIC; 21391267; VBIChlPha122104_1803. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FGPPQGL; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPHA290317:GHX4-1561-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 212 AA; 22761 MW; BE509992619F3703 CRC64; MTPPSPQLPR LYLVSSGFNS RDSYTQLENQ VTCFSSSCPC IVQIREKMLD AKTLFELSCS IAPAIIAAGS MVVINERVDI ALAAALNGVH FPENSSPPER FRAMTKGKIL GQSTHSLKTA RISQQAGVDY ILFGPVFDTP SKRGFGPPQG LLNLAAVCEA TSLPVYAIGG VTPENASLCL DSGAYGVAAL SLFMDTTRLV NTLDKFHRLL YS // ID A1CSW0_ASPCL Unreviewed; 519 AA. AC A1CSW0; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 16-APR-2014, entry version 40. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative; GN ORFNames=ACLA_080810; OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC OS 3887 / NRRL 1). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=344612; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1; RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046; RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., RA Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., RA Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., RA Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R., RA Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., RA Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., RA Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., RA Jiang B., Denning D.W., Nierman W.C.; RT "Genomic islands in the pathogenic filamentous fungus Aspergillus RT fumigatus."; RL PLoS Genet. 4:E1000046-E1000046(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS027060; EAW06397.1; -; Genomic_DNA. DR RefSeq; XP_001267823.1; XM_001267822.1. DR ProteinModelPortal; A1CSW0; -. DR STRING; 5057.CADACLAP00007678; -. DR EnsemblFungi; CADACLAT00007869; CADACLAP00007678; CADACLAG00007869. DR GeneID; 4700142; -. DR KEGG; act:ACLA_080810; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 519 AA; 55142 MW; E37E2ECA43ECFC02 CRC64; MPLDLSVYLV TDSTPAILKG QDLCTVVEEA LKGGVTLVQY RDKKSDTGDL IKTAKALHKI TQAYGVPLLI NDRVDVALAV GAEGVHLGQD DMYIAEAKQL LPKDAIIGIT ASSIEEAQKA IEAGADYLGI GTMFATSTKT NTKNILGTAG TQTILEAISD SGRNVGTVAI GGISLSNVQR VLYQAKAPRK GLDGVAIVSA IVGADDPRAA AEEFVKRVNT PPTFAWEPKA PRANETSALL EEVPQIVQKM VKAHPLVHNM INYVVANFVA NIALSMGASP IMSPYGEEAA DLAKFDGALV INMGTLNSES VPNYLKAIKS YNERGNPVIY DPVGAAATHI RRGAVNELMR GGYFDLIKGN EGEIKQVSGT SNTVQRGVDS GPSSLDGREK ATLARDLARR ERNVVLLTGA VDYLSDGERV IAVENGHEYL GQVTGTGCAV GMVSGCFLAT HRSDKLLAVL AGILMYEIAA ENAASKDYVR GPGSFVPAFL DELYAIRQAA LKGDDSWFVG RAKIQEIRL // ID A1DGJ4_NEOFI Unreviewed; 523 AA. AC A1DGJ4; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 16-APR-2014, entry version 41. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative; GN ORFNames=NFIA_084530; OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL OS 181) (Aspergillus fischerianus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Neosartorya. OX NCBI_TaxID=331117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181; RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046; RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., RA Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., RA Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., RA Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R., RA Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., RA Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., RA Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., RA Jiang B., Denning D.W., Nierman W.C.; RT "Genomic islands in the pathogenic filamentous fungus Aspergillus RT fumigatus."; RL PLoS Genet. 4:E1000046-E1000046(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS027696; EAW18501.1; -; Genomic_DNA. DR RefSeq; XP_001260398.1; XM_001260397.1. DR ProteinModelPortal; A1DGJ4; -. DR STRING; 36630.CADNFIAP00006650; -. DR EnsemblFungi; CADNFIAT00006817; CADNFIAP00006650; CADNFIAG00006817. DR GeneID; 4586956; -. DR KEGG; nfi:NFIA_084530; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 523 AA; 55774 MW; 344A8C0913D25A9E CRC64; MPLDLSVYLV TDSTPAILKG RDLCTVVEEA LKGGVTIVQY RDKTSDTGDL IRTAKELHRI TKAYEVPLLI NDRVDVALAV GAEGVHLGQD DMYIEEAKKL LPKDAIIGIS ASSVEEAQRA IEAGADYLGI GTMFATPTKT NTKHILGTAG TQAILDAISD SGRKVGTVAI GGINLSNVQR VMYQSKAPRK GLDGVAIVSA IMAADDPRAA AEEFVKRINS PPSFAWEPKA PRASEAAALV EEVAQIVQKM VKAHPLVHNM INYVVANFVA NVALAMGASP IMSPYGEEAV DLAKFDGALV INMGTLSRES IPNYLQAIKS YNERGNPVVY DPVGAAATQV RRGAVKELMS GGYFDLIKGN EGEIRQVSGS SNAVQRGVDS GPSTLDGQEK ARLARDLARR ERNVVLLTGA VDYLSDGERV IAVENGHEFL GQVTGTGCAV GMVSGCFLAV HPSDKLLAVL SGILMYEIAA ENAASKDYVR GPGSFVPAFL DELYAIRQAA LKGDDSWFSG RAKIQEIKLF QEL // ID A1EMW0_VIBCL Unreviewed; 440 AA. AC A1EMW0; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 19-FEB-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCV52_0066; OS Vibrio cholerae V52. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=345076; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=V52; RA Heidelberg J., Sebastian Y.; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAKJ02000027; EAX62324.1; -; Genomic_DNA. DR ProteinModelPortal; A1EMW0; -. DR EnsemblBacteria; EAX62324; EAX62324; VCV52_0066. DR PATRIC; 38606496; VBIVibCho49684_1752. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID A1F6D0_VIBCL Unreviewed; 440 AA. AC A1F6D0; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 19-FEB-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VC274080_0065; OS Vibrio cholerae 2740-80. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=412614; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2740-80; RA Heidelberg J., Sebastian Y.; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAUT01000034; EAX58175.1; -; Genomic_DNA. DR ProteinModelPortal; A1F6D0; -. DR EnsemblBacteria; EAX58175; EAX58175; VC274080_0065. DR PATRIC; 28012370; VBIVibCho84837_2061. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48979 MW; EA66272C0BDA63C6 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC YQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID A1HPQ3_9FIRM Unreviewed; 215 AA. AC A1HPQ3; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 19-FEB-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TcarDRAFT_1901; OS Thermosinus carboxydivorans Nor1. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Thermosinus. OX NCBI_TaxID=401526; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Nor1; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M., Hauser L.; RT "Annotation of the draft genome assembly of Thermosinus RT carboxydivorans Nor1."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Nor1; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Bruce D., Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of Thermosinus RT carboxydivorans Nor1."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWL01000005; EAX48023.1; -; Genomic_DNA. DR ProteinModelPortal; A1HPQ3; -. DR EnsemblBacteria; EAX48023; EAX48023; TcarDRAFT_1901. DR PATRIC; 30836222; VBITheCar126673_1169. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23445 MW; C48DD611A8CE3F8B CRC64; MDRQTALANL RRADIYGITS EEHSLGRSNV EVAQLMIAAG IKVIQYREKE KKARRMYEEC CKIRELTRAA GVTFIVNDHI DLAMLVEADG VHIGQDDLPP EKVRQLVGKE MLIGLSTHAP AEAQAAENSG VVDYIGVGPI YATQTKKDVC APVGLEYLSY VAKNISLPFV AIGGIKEHNL AEVIRHGART VALVTEIVGA PDIKAKVQAL RAKFT // ID A1JII7_YERE8 Unreviewed; 203 AA. AC A1JII7; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 55. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=YE0292; OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / OS 8081). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=393305; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 13174 / 8081; RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206; RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J., RA Prentice M.B.; RT "The complete genome sequence and comparative genome analysis of the RT high pathogenicity Yersinia enterocolitica strain 8081."; RL PLoS Genet. 2:2039-2051(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM286415; CAL10425.1; -; Genomic_DNA. DR RefSeq; YP_001008366.1; NC_008800.1. DR ProteinModelPortal; A1JII7; -. DR STRING; 393305.YE0292; -. DR EnsemblBacteria; CAL10425; CAL10425; YE0292. DR GeneID; 4714404; -. DR KEGG; yen:YE0292; -. DR PATRIC; 18559968; VBIYerEnt11519_0385. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 23 27 HMP-PP binding (By similarity). FT REGION 120 122 THZ-P binding (By similarity). FT REGION 172 173 THZ-P binding (By similarity). FT METAL 56 56 Magnesium (By similarity). FT METAL 75 75 Magnesium (By similarity). FT BINDING 55 55 HMP-PP (By similarity). FT BINDING 94 94 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 152 152 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 22020 MW; 1E8F2C98A0626340 CRC64; MYPVVDSVLW IERLLAAGVT TIQLRIKDLD DAQVEQDIAA AIALGKRYQA RLFINDYWRL AIKHGAYGVH LGQEDLETTD LAAIQQAGLR LGVSTHDEHE LAIAKAVRPS YIAMGHIFPT QTKQMPSSPQ GLAVLKQMVE NTPDYPTVAI GGISIERVPA VLAAGVGSVA VVSAITQAED WQQATAQLLR LIEGKELSDD KQA // ID A1K3E0_AZOSB Unreviewed; 318 AA. AC A1K3E0; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 59. DE SubName: Full=Bifunctional DGTP-pyrophosphohydrolase/Thiamine-phosphate diphosphorylase; DE EC=3.6.1.-; GN OrderedLocusNames=azo0728; OS Azoarcus sp. (strain BH72). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azoarcus. OX NCBI_TaxID=62928; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BH72; RX PubMed=17057704; DOI=10.1038/nbt1243; RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.; RT "Complete genome of the mutualistic, N2-fixing grass endophyte RT Azoarcus sp. strain BH72."; RL Nat. Biotechnol. 24:1385-1391(2006). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM406670; CAL93345.1; -; Genomic_DNA. DR RefSeq; YP_932232.1; NC_008702.1. DR ProteinModelPortal; A1K3E0; -. DR STRING; 62928.azo0728; -. DR EnsemblBacteria; CAL93345; CAL93345; azo0728. DR GeneID; 4606536; -. DR KEGG; azo:azo0728; -. DR PATRIC; 21009742; VBIAzoSp26047_0741. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 318 AA; 33828 MW; A182AFFE216C43B0 CRC64; MAEVGARKIV NVAAGVILER GRVLLGQRAP DTFYPGYWEF PGGKVEPGES AADALKRELA EELGIVVPHV RPWLTREHDY EHAHVRLHFF EVPAWSGAPV AHVHAALRWA EPELIATACA PMLPANGPIL KALQLPRRMG ITQAAERGVA RQLDELEQAL GAGLRLVQVR EAALPRRQQI EFAQEVVRRV AAAGGIVVIN GDLDLARAVG APGVHLPSAA LLDCTVRPAF EWVGASCHSE EELRAAAALG LDYAVLGPVR PTASHPGQAA LGWARFGELA GTLPFPVFAL GGLGWGDMDC ARDHGAHGVA AIRGAWGA // ID A1KWE8_NEIMF Unreviewed; 205 AA. AC A1KWE8; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 59. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NMC2050; OS Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / OS DSM 15464 / FAM18). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=272831; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700532 / DSM 15464 / FAM18; RX PubMed=17305430; DOI=10.1371/journal.pgen.0030023; RA Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., RA Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., RA Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., RA Unwin L., Whitehead S., Quail M.A., Achtman M., Barrell B.G., RA Saunders N.J., Parkhill J.; RT "Meningococcal genetic variation mechanisms viewed through comparative RT analysis of serogroup C strain FAM18."; RL PLoS Genet. 3:230-240(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM421808; CAM11205.1; -; Genomic_DNA. DR RefSeq; YP_975972.1; NC_008767.1. DR ProteinModelPortal; A1KWE8; -. DR STRING; 272831.NMC2050; -. DR EnsemblBacteria; CAM11205; CAM11205; NMC2050. DR GeneID; 4676349; -. DR KEGG; nmc:NMC2050; -. DR PATRIC; 20354680; VBINeiMen17609_2562. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NMEN272831:GJDX-1947-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21654 MW; 28E6A2E0137A5C49 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGDELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAE NPEAVVKAFQ ALWDG // ID A1R8B5_ARTAT Unreviewed; 243 AA. AC A1R8B5; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 62. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AAur_2765; OS Arthrobacter aurescens (strain TC1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=290340; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TC1; RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214; RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B., RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., RA Khouri H., Wackett L.P., Nelson K.E., Sadowsky M.J.; RT "Secrets of soil survival revealed by the genome sequence of RT Arthrobacter aurescens TC1."; RL PLoS Genet. 2:2094-2106(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000474; ABM06701.1; -; Genomic_DNA. DR RefSeq; YP_948477.1; NC_008711.1. DR ProteinModelPortal; A1R8B5; -. DR STRING; 290340.AAur_2765; -. DR EnsemblBacteria; ABM06701; ABM06701; AAur_2765. DR GeneID; 4638155; -. DR KEGG; aau:AAur_2765; -. DR PATRIC; 20980996; VBIArtAur67810_2807. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AAUR290340:GI59-2764-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 61 65 HMP-PP binding (By similarity). FT REGION 163 165 THZ-P binding (By similarity). FT METAL 94 94 Magnesium (By similarity). FT METAL 113 113 Magnesium (By similarity). FT BINDING 93 93 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 166 166 HMP-PP (By similarity). FT BINDING 200 200 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 243 AA; 25604 MW; D9DFD6FC24C79B2B CRC64; MTNVAAPAVR AQFRGTTLVS MTQPDALASA RLYLCTDARQ RQGDFEDFVD AAFAGGVDII QLRDKTLEAA EELELLAVLR SVAQRHGRLW AVNDRADVAS ISGAPVFHIG QKDLPLTAAR TLLPNVTGIG LSTHTQEQID AAVATSQGPL GLDYFCVGPV WATPTKPGRS AVGLDLVTYA AEAEKRSGNA VTLPWFAIGG IDLSNVEQVV EAGASRIVVV RAITEATDPT AAAKSLLQAL DTV // ID A1RJR8_SHESW Unreviewed; 624 AA. AC A1RJR8; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 63. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=Sputw3181_2085; OS Shewanella sp. (strain W3-18-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=351745; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W3-18-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Tiedje J., RA Richardson P.; RT "Complete sequence of Shewanella sp. W3-18-1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000503; ABM24913.1; -; Genomic_DNA. DR RefSeq; YP_963467.1; NC_008750.1. DR ProteinModelPortal; A1RJR8; -. DR STRING; 351745.Sputw3181_2085; -. DR EnsemblBacteria; ABM24913; ABM24913; Sputw3181_2085. DR GeneID; 4661217; -. DR KEGG; shw:Sputw3181_2085; -. DR PATRIC; 23597821; VBISheSp103602_2168. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SSP351745:GCOY-2150-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 624 AA; 65778 MW; 7F053972DA949DBD CRC64; MSTARPAIVW TIAGSDSGGG AGIQADLATI QDLGCHGCSV ITTVTAQSSV AVTLVEPVSA AMLMAQLTTL LSDLPPKAIK IGLLADQSQV ALLADWIASF KIHYPSVPVI VDPVMVASCG DALAVDNCQD IKSTAKSALD FNPFKGLIEL ITPNVLELGR LTHSDVSTKA QFAAAAQALS QSLDCSVLAK GGDVSFGCTD ILDDTQTHDS TYAQTQANVH VSTLDSNGWD HGLAEDYLVC HQVRASSELH QNGCFWLASQ RVNTRHNHGS GCTLSSAIAA VLAQGSVLQD AVVVAKAYVS QGLSAAIGLG QGPGPLARTG WPNDLSRYAK INLCDGNFIS HHLNQHLDVR SDLVATVLSA TDQANTTSTP AQYISSHGFK VLDADLGVYP VVSDLIMLES LLAAGVKTVQ LRIKTDISEL SSAAPAESDL GKCESGKSEL VGSELEVQIQ TAIALGKHFN AQLFINDHWQ LAIKYHAFGI HLGQEDLAVT DLAAIQSAGL ALGISSHSYF ELLLAHQYSP SYIALGHIFP TTTKQMPSAP QGLAKLKHYV ALLQDHYPLV AIGGIDLDNL AKVKATGVGN IAVVRAITEA QDPLAAFAEL SQAWEQCSLS EELAVKHELV AKHE // ID A1S6Q8_SHEAM Unreviewed; 525 AA. AC A1S6Q8; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Phosphomethylpyrimidine kinase., Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=Sama_1859; OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=326297; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1098 / SB2B; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Fredrickson J., Richardson P.; RT "Complete sequence of Shewanella amazonensis SB2B."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000507; ABM00065.1; -; Genomic_DNA. DR RefSeq; YP_927734.1; NC_008700.1. DR ProteinModelPortal; A1S6Q8; -. DR STRING; 326297.Sama_1859; -. DR EnsemblBacteria; ABM00065; ABM00065; Sama_1859. DR GeneID; 4604109; -. DR KEGG; saz:Sama_1859; -. DR PATRIC; 23452449; VBISheAma74963_1914. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SAMA326297:GH0T-1935-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 525 AA; 55136 MW; CF4E2C072D898A13 CRC64; MAKINDMAAK PIVWTIAGSD SGGGAGIQAD LLTLQDLGCY GCSVITAITA QNSVAVTAVE PVTPRMLRAQ LETLKADLYP SAVKIGLIAN QPQLDFLADW LGENLPGVPV ILDPVMVASC GGDLQSPDNT CPDKTGERSG LDFSPFAGKI SLITPNKAEL SRLIGRLLND DDALEWAANV LWQAFGGSIL AKGGDCPWQQ SKARDLLLLG DIATISPLHR RQGFWLSNER VATVHNHGSG CTLSSAIAAF VAKGLVLPDA VLLAKAYVFE GLRQASAVGS GPGPLARTGM PESLAAMASI HRLHESRSHR LPTKGFTRLG HDLGVYPVVA DIDMLETLLE AGANPIQLRI KGEIGPGSAA EADIIRAIAL GRQHRARVFI NDHWRLAISH GAFGVHLGQE DIEAVPLDAI AEAGMALGLS SHGLFEALLA LELNPSYLAL GHIFPTTTKE MPSKPQGLET LALLAKIVST AVPTVAIGGI EAGNLPEVAA TGVDSIAVVR AVTEASEPAT AFRALADAWE MRNAR // ID A1SM67_NOCSJ Unreviewed; 197 AA. AC A1SM67; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN OrderedLocusNames=Noca_3402; OS Nocardioides sp. (strain BAA-499 / JS614). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Nocardioidaceae; Nocardioides. OX NCBI_TaxID=196162; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAA-499 / JS614; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Mattes T., Gossett J., Richardson P.; RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000509; ABL82902.1; -; Genomic_DNA. DR RefSeq; YP_924589.1; NC_008699.1. DR ProteinModelPortal; A1SM67; -. DR STRING; 196162.Noca_3402; -. DR EnsemblBacteria; ABL82902; ABL82902; Noca_3402. DR GeneID; 4598200; -. DR KEGG; nca:Noca_3402; -. DR PATRIC; 22748907; VBINocSp122728_3687. DR eggNOG; NOG131844; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VMRAEDP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NSP196162:GH4V-3449-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 197 AA; 19969 MW; 769837E63F875159 CRC64; MTGVDLPRLL VLTDRHQLPA GRDLVGALAD CVAAGLEAVL LRELDLPGQE RQALARALGA TGVTVILART WLPGAAAVHL AAAQSPHDAG AAPFHGRSCH DDHEIRRAVA GGASYLTISP VAASASKPGY GPILGEDGVR RAVALAGEVP VFALGGVKVQ NAAAMRAAGA HGVAVMGAVM RAPDPADVVE RVLGEAR // ID A1SM71_NOCSJ Unreviewed; 203 AA. AC A1SM71; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Noca_3406; OS Nocardioides sp. (strain BAA-499 / JS614). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Nocardioidaceae; Nocardioides. OX NCBI_TaxID=196162; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAA-499 / JS614; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Mattes T., Gossett J., Richardson P.; RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000509; ABL82906.1; -; Genomic_DNA. DR RefSeq; YP_924593.1; NC_008699.1. DR ProteinModelPortal; A1SM71; -. DR STRING; 196162.Noca_3406; -. DR EnsemblBacteria; ABL82906; ABL82906; Noca_3406. DR GeneID; 4598204; -. DR KEGG; nca:Noca_3406; -. DR PATRIC; 22748915; VBINocSp122728_3691. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NSP196162:GH4V-3453-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 20907 MW; D4C9995858B1D4E9 CRC64; MLPRIHCITD FSSYGDRAIT LLEAVVREGV DAVQVRAKSV SDREVVAFTR ALVDRLAGTS AAVIVNDRVD IALIAGAQGV HLGRDDLAVA EARRLAPQGF LVGGTCRNAD QAREARAQGA DYIGVGPVYA TTTKSGLPDP IGLDALRDAA RVLPAIAISG INAERAPEVM AAGAYGIAVA SAICRSPQPG LAARELVGAV ALA // ID A1SRV8_PSYIN Unreviewed; 500 AA. AC A1SRV8; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 62. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Ping_0361; OS Psychromonas ingrahamii (strain 37). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Psychromonadaceae; Psychromonas. OX NCBI_TaxID=357804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=37; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., RA Staley J., Richardson P.; RT "Complete sequence of Psychromonas ingrahamii 37."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000510; ABM02223.1; -; Genomic_DNA. DR RefSeq; YP_941822.1; NC_008709.1. DR ProteinModelPortal; A1SRV8; -. DR STRING; 357804.Ping_0361; -. DR EnsemblBacteria; ABM02223; ABM02223; Ping_0361. DR GeneID; 4624145; -. DR KEGG; pin:Ping_0361; -. DR PATRIC; 23065462; VBIPsyIng103130_0394. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PING357804:GJBJ-381-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 500 AA; 53690 MW; 9033AC88CF46DD6E CRC64; MNKLVWSIGA SDCTGGGGIQ ADLHTFKDLG ADGCSVISAV TAQNSATVSL VESVSEQMFT DQLACLTADM QAKVIKIGLI TSVKHVQILA EKLAEFKQTW AVPPFVIYDP VAVALTGEKM AEEGLVELIR TALLPCIDLL TANAGEVLTL SGHALISGES LKPAALKLIS LGCQSVLIKG GDFELVDKIA LDYWTDGKRE IALSSARLTR MESHGTGGIL ASAIGATIAL GYFIEDALVV AKAYLNQELK AAKKLGFYGI AHLGWPTNKT DFPEVVLPES KIGYELDLPG TLEAGPGFAS CGTLKLGLYP VLDSVEWLDK VLKLGVKTLQ LRIKDKQPEQ VEQQIIEAIA LGRKYNARLF INDYWQLAIK HQAYGVHLGQ EDMDVADLPM IADAGLRLGL STHGYYEILR AQQLKPSYIA LGHIFPTQTK QMPSDPQGLS RLGKYAQLLS DIPTVAIGGI NLERATTVWK TGVGSIAVVS AITHADSPKI AIESFNQVIQ // ID A1SX94_PSYIN Unreviewed; 205 AA. AC A1SX94; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 57. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ping_2372; OS Psychromonas ingrahamii (strain 37). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Psychromonadaceae; Psychromonas. OX NCBI_TaxID=357804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=37; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., RA Staley J., Richardson P.; RT "Complete sequence of Psychromonas ingrahamii 37."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000510; ABM04109.1; -; Genomic_DNA. DR RefSeq; YP_943708.1; NC_008709.1. DR ProteinModelPortal; A1SX94; -. DR STRING; 357804.Ping_2372; -. DR EnsemblBacteria; ABM04109; ABM04109; Ping_2372. DR GeneID; 4623706; -. DR KEGG; pin:Ping_2372; -. DR PATRIC; 23070033; VBIPsyIng103130_2614. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PING357804:GJBJ-2462-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21836 MW; 9CFA22DD84456EA1 CRC64; MNPYRLYLVT DDQQNLETLK RVVAEAVVGG VTMVQVREKQ GDLRVFIERV LAVKAILHGT GVPLIVNDRV DVALAVDADG VHLGQSDMPV ETARRLIGKD KLLGLSIENP QQLIEAESLP VDYLGLSAIF STATKTNIKK EWGIEGLTNA VAQSSLPIVA IGGINVSNLD EVIASNVAGV ALVSAICHAP SPKQAAINLL KQMGK // ID A1TRP9_ACIAC Unreviewed; 302 AA. AC A1TRP9; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 59. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Aave_3071; OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. OS citrulli). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=397945; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAC00-1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., RA Richardson P.; RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000512; ABM33637.1; -; Genomic_DNA. DR RefSeq; YP_971411.1; NC_008752.1. DR ProteinModelPortal; A1TRP9; -. DR STRING; 397945.Aave_3071; -. DR EnsemblBacteria; ABM33637; ABM33637; Aave_3071. DR GeneID; 4667399; -. DR KEGG; aav:Aave_3071; -. DR PATRIC; 20681299; VBIAciCit38535_3125. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ACIT397945:GI5W-3107-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 302 AA; 31595 MW; A15C2A4A5FB1EE0C CRC64; MAEDSTLQAM AEAIVQAHAA AFAGFPAQPA PAPAHGGAAY GAALRACSQL GFIAVDADCL ARAWQARTDR TGHFDASHWP DEPVDFGLQP RPHARPFATC PDRLGLYAVL PDAHWVGRMA RAGVPTVQLR FKSEDGAAVE REVRAAVEAV RGTSALLFIN DHWQAAIGAG AYGVHLGQED LDALPPGSLE TLRASGLRLG VSTHGYAEMV RADAAAPSYV AMGAVFPTTL KKMATVPQGL ARLAGYARLM RGYPQVAIGG IGAEQFADVL ATGVGSIAVV RALVNAPDPE AAARDLMQRM GR // ID A1U3E7_MARAV Unreviewed; 329 AA. AC A1U3E7; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 13-NOV-2013, entry version 60. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=Maqu_2441; OS Marinobacter aquaeolei (strain ATCC 700491 / DSM 11845 / VT8) OS (Marinobacter hydrocarbonoclasticus (strain DSM 11845)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=351348; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700491 / DSM 11845 / VT8; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Edwards K., Richardson P.; RT "Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000514; ABM19516.1; -; Genomic_DNA. DR RefSeq; YP_959703.1; NC_008740.1. DR ProteinModelPortal; A1U3E7; -. DR STRING; 351348.Maqu_2441; -. DR EnsemblBacteria; ABM19516; ABM19516; Maqu_2441. DR GeneID; 4656717; -. DR KEGG; maq:Maqu_2441; -. DR PATRIC; 22460224; VBIMarAqu65105_2861. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MHYD351348:GHYZ-2492-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 329 AA; 34816 MW; F258D02EA5BA4C75 CRC64; MPNTVPESVE GLSANRKTVH VAVGVIVRDG RVLIARRPDT AHQGGLLEFP GGKVEPGETV QQALCREIAE ETGLVLTEDS LEPVIGIRHD YGDKCVFLDV WSSHSAQGEP EGKEGQPVSW LAPEALKDEE FPAANRPIIR ALRLPHRLAV TGTIEDAPAG LARLGAALDR GQPDSLVVLR APTLSGAAYL ELAAAALGGC RERGVGLILH GAADLCRAVP DVQGVHLPWC EAQLHSERPV SDDYWLGVSC HSAEQLRYAE RLGADYVVLG NVLETPSHPG QPGIGWAAFQ ALAATANVPV YGIGGLGPEH QSRARALGGQ GVAGIGFWW // ID A1UR90_BARBK Unreviewed; 225 AA. AC A1UR90; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE SubName: Full=ThiE/TenI family protein; GN OrderedLocusNames=BARBAKC583_0155; OS Bartonella bacilliformis (strain ATCC 35685 / KC583). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=360095; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35685 / KC583; RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., RA Fraser-Ligget C., Seshadri R.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000524; ABM44921.1; -; Genomic_DNA. DR RefSeq; YP_988493.1; NC_008783.1. DR ProteinModelPortal; A1UR90; -. DR STRING; 360095.BARBAKC583_0155; -. DR EnsemblBacteria; ABM44921; ABM44921; BARBAKC583_0155. DR GeneID; 4684794; -. DR KEGG; bbk:BARBAKC583_0155; -. DR PATRIC; 20536587; VBIBarBac6912_0155. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FACVILY; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BBAC360095:GHRY-155-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 225 AA; 25169 MW; FE9147CC0A35B45B CRC64; MTKQKSKPIE SCLYPQLVLT VDVRRTLNPS LLRTLLQTQS FTCVIIYDSL IHQGDENFLQ NKAQSYVDDV QHSGAALIIA DHSQIVGRIK ADGLHVEGNR EALKIFKDQT KENKIVGFGN LRDRHSAMTV AEAGVDYLFF GKLGADQKAQ AHPRNLSLAT WWAEIMEIPA IIQAGNDYAT VDEAFKTACE FIAVEDMLLS HEDPLPLLQE MVKKCKKFPL LMGKA // ID A1US07_BARBK Unreviewed; 201 AA. AC A1US07; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=BARBAKC583_0442; OS Bartonella bacilliformis (strain ATCC 35685 / KC583). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=360095; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35685 / KC583; RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., RA Fraser-Ligget C., Seshadri R.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000524; ABM45287.1; -; Genomic_DNA. DR RefSeq; YP_988760.1; NC_008783.1. DR ProteinModelPortal; A1US07; -. DR STRING; 360095.BARBAKC583_0442; -. DR EnsemblBacteria; ABM45287; ABM45287; BARBAKC583_0442. DR GeneID; 4684091; -. DR KEGG; bbk:BARBAKC583_0442; -. DR PATRIC; 20537151; VBIBarBac6912_0424. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BBAC360095:GHRY-442-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 201 AA; 23100 MW; E5733D682B710B26 CRC64; MKLDPFYLIV DNADWIERCV PLGIKLVQLR IKNKDTELIR HHIKRAKNIC DQFGAQFIVN DYWEIAIDEK CDFIHLGQED LNNADIPAIR KNGIKFGLST HDEYELDIAL SFCPEYIALG PIYPTILKKM KWPPQGLEKI KQWKKLIGPL PLVGIGGLTP ERAINVLQVG ANSAAAITDI ILHKKPKERV QQWIKVTQKW R // ID A1UYL0_BURMS Unreviewed; 209 AA. AC A1UYL0; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN OrderedLocusNames=BMASAVP1_1467; OS Burkholderia mallei (strain SAVP1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320388; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAVP1; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000525; ABM49180.1; -; Genomic_DNA. DR RefSeq; YP_991063.1; NC_008784.1. DR ProteinModelPortal; A1UYL0; -. DR STRING; 320388.BMASAVP1_1467; -. DR EnsemblBacteria; ABM49180; ABM49180; BMASAVP1_1467. DR GeneID; 4676897; -. DR KEGG; bmv:BMASAVP1_1467; -. DR PATRIC; 19152205; VBIBurMal134057_1381. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BMAL320388:GHFL-4998-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID A1V8F7_BURMS Unreviewed; 367 AA. AC A1V8F7; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=BMASAVP1_A3227; OS Burkholderia mallei (strain SAVP1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320388; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAVP1; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000526; ABM51389.1; -; Genomic_DNA. DR RefSeq; YP_994510.1; NC_008785.1. DR ProteinModelPortal; A1V8F7; -. DR STRING; 320388.BMASAVP1_A3227; -. DR EnsemblBacteria; ABM51389; ABM51389; BMASAVP1_A3227. DR GeneID; 4680486; -. DR KEGG; bmv:BMASAVP1_A3227; -. DR PATRIC; 19159137; VBIBurMal134057_4798. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BMAL320388:GHFL-3226-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 367 AA; 38315 MW; 3E9B351CCB7F5C2B CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGARAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID A1VBV5_DESVV Unreviewed; 219 AA. AC A1VBV5; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 59. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dvul_0900; OS Desulfovibrio vulgaris subsp. vulgaris (strain DP4). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=391774; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DP4; RX PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x; RA Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., RA Dehal P.S., He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., RA Hazen T.C., Arkin A.P., Stahl D.A.; RT "Contribution of mobile genetic elements to Desulfovibrio vulgaris RT genome plasticity."; RL Environ. Microbiol. 11:2244-2252(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000527; ABM27921.1; -; Genomic_DNA. DR RefSeq; YP_966348.1; NC_008751.1. DR ProteinModelPortal; A1VBV5; -. DR STRING; 391774.Dvul_0900; -. DR EnsemblBacteria; ABM27921; ABM27921; Dvul_0900. DR GeneID; 4663290; -. DR KEGG; dvl:Dvul_0900; -. DR PATRIC; 21765573; VBIDesVul62463_1082. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DVUL391774:GHS0-933-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22397 MW; 08AD220A9563C8CB CRC64; MTRVRKAAVD YGLYLVTDAG LTDARLHEVV TAAISGGVGI VQLREKATPT RAFVDRARAL VALLRPRGIP LLINDRVDVA LASGADGVHV GQSDMHVGDV RALMGPDAIV GLSVETPAQA KAAEHAPVDY LGVSPVFATA TKPDAAPPWG VAGLCGLRRT TRHVLVGIGG IGPVNAADVL HAGAEGIAVV SAICGAADPL AAARALRAVV DEVRVPVRI // ID A1VCJ3_DESVV Unreviewed; 226 AA. AC A1VCJ3; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 56. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dvul_1139; OS Desulfovibrio vulgaris subsp. vulgaris (strain DP4). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=391774; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DP4; RX PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x; RA Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., RA Dehal P.S., He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., RA Hazen T.C., Arkin A.P., Stahl D.A.; RT "Contribution of mobile genetic elements to Desulfovibrio vulgaris RT genome plasticity."; RL Environ. Microbiol. 11:2244-2252(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000527; ABM28159.1; -; Genomic_DNA. DR RefSeq; YP_966586.1; NC_008751.1. DR ProteinModelPortal; A1VCJ3; -. DR STRING; 391774.Dvul_1139; -. DR EnsemblBacteria; ABM28159; ABM28159; Dvul_1139. DR GeneID; 4662380; -. DR KEGG; dvl:Dvul_1139; -. DR PATRIC; 21766089; VBIDesVul62463_1333. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DVUL391774:GHS0-1179-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23885 MW; 482382EA0D7FB3B7 CRC64; MPVILPGTTP DADIYCLTDS GLCLGRPTVD VVDAMLQAGA RIIQYREKEK KAGEMLRECL ELRRMTREAG ACFIVNDHVD IAILCDADGV HIGQEDLPVG EVRRLIGPDR AIGLSTHSPE QAMAAVAAGA DYIGVGPIFA TKTKKDVCDP VGYAYLDWVV THLDIPFVAI GGIKLHNIGE VAAHGARCCA LVSEIVGAVD IVAQVQTVRR AMRGVAAAGT DSPQAG // ID A1VI71_POLNA Unreviewed; 213 AA. AC A1VI71; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 59. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Pnap_0023; OS Polaromonas naphthalenivorans (strain CJ2). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=365044; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CJ2; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D.R., Brettin T., Bruce D., Han C., Tapia R., RA Brainard J., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Madsen E.L., Richardson P.; RT "Complete sequence of chromosome 1 of Polaromonas naphthalenivorans RT CJ2."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000529; ABM35349.1; -; Genomic_DNA. DR RefSeq; YP_980270.1; NC_008781.1. DR ProteinModelPortal; A1VI71; -. DR STRING; 365044.Pnap_0023; -. DR EnsemblBacteria; ABM35349; ABM35349; Pnap_0023. DR GeneID; 4687098; -. DR KEGG; pna:Pnap_0023; -. DR PATRIC; 22944513; VBIPolNap76733_0827. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PNAP365044:GJ8X-23-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22217 MW; FBCCBF8A75B57DBF CRC64; MTASAPFAPL TGPIGFYPVV HDAAWVQRLL GWGVRTVQLR FKAAGHTPAE IEREVNAAVE AGSKVPGAQV FINDHWQLAL AAGAYGVHLG QEDLDTADIE ALRNAGLRLG LSTHTPAELA RAHAVQPSYL AIGPIYPTTL KVMPYAPVGL TQLKEWATLA VPYPVVAIGG ISLERLPGVL ACGVDGVAVV SAVTLAANPQ QAALQGLALV GKR // ID A1W033_CAMJJ Unreviewed; 201 AA. AC A1W033; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 50. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=CJJ81176_1064; OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=354242; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=81-176; RA Fouts D.E., Nelson K.E., Sebastian Y.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000538; EAQ72165.1; -; Genomic_DNA. DR RefSeq; YP_001000724.1; NC_008787.1. DR ProteinModelPortal; A1W033; -. DR STRING; 354242.CJJ81176_1064; -. DR EnsemblBacteria; EAQ72165; EAQ72165; CJJ81176_1064. DR GeneID; 4683305; -. DR KEGG; cjj:CJJ81176_1064; -. DR PATRIC; 20052099; VBICamJej103413_1062. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CJEJ354242:GC51-1040-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 23461 MW; 48AC77B39ECB01F4 CRC64; MWDKKIIAIS DRKCVQIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID A1W6U6_ACISJ Unreviewed; 309 AA. AC A1W6U6; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 55. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Ajs_1783; OS Acidovorax sp. (strain JS42). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=232721; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS42; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., RA Richardson P.; RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000539; ABM41971.1; -; Genomic_DNA. DR RefSeq; YP_986047.1; NC_008782.1. DR ProteinModelPortal; A1W6U6; -. DR STRING; 232721.Ajs_1783; -. DR EnsemblBacteria; ABM41971; ABM41971; Ajs_1783. DR GeneID; 4672601; -. DR KEGG; ajs:Ajs_1783; -. DR PATRIC; 20688894; VBIAciSp27161_1983. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ASP232721:GHWE-1806-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 309 AA; 32624 MW; 90F7FD4F3AC52B03 CRC64; MPQAAAPLPS AAAMEQAIRQ HHASAFADFP PQPMPATTVE DPVYRAALAA CSALGFIAHD ADCLARAWAA QTRRTGRFDP AQWPDEPADF GLQPRPHAHP FAACPQNLGL YAVLPDAQWV GRMAQAGVPT VQLRFKSDDP AAITREVRAA VQAVQGTASL LFINDHWRQA IAAGAYGVHL GQEDLDALSP EELRTLRESG VRLGVSTHGY AEMVRADAAS PSYIAMGAVF PTTLKKMATV PQGVARLAGY ARLMRGYPLV AIGGIGLAQF PQVLATGVGS IAVVRAVVAA DQPEAAAAQL MRAIDAGRR // ID A1WQV7_VEREI Unreviewed; 314 AA. AC A1WQV7; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 55. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Veis_4311; OS Verminephrobacter eiseniae (strain EF01-2). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Verminephrobacter. OX NCBI_TaxID=391735; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EF01-2; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., RA Richardson P.; RT "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01- RT 2."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000542; ABM60014.1; -; Genomic_DNA. DR RefSeq; YP_999032.1; NC_008786.1. DR ProteinModelPortal; A1WQV7; -. DR STRING; 391735.Veis_4311; -. DR EnsemblBacteria; ABM60014; ABM60014; Veis_4311. DR GeneID; 4693454; -. DR KEGG; vei:Veis_4311; -. DR PATRIC; 24022513; VBIVerEis120356_4632. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RFKSEDR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; VEIS391735:GHY5-4359-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 314 AA; 33520 MW; 79C4539CF4177FF3 CRC64; MRSTDSMAQA IVAQHRAAFT GFAPAPMPES TAQDPVYLAA LQACSALGFI APDAQCLARA WQARTQRTGS FQAEPWPDDP RDFGLQPEPR AHRFAPCPER LGLYAVLPDA GWVARMARAG VPTVQLRYKS CDTRAIEQEV AAAVQAVQGT GALLFINDHW QAAITAGAYG IHLGQEDLDA LTPQDLQTLR HCGLRLGLST HGYAEMLRAD AVGPSYIALG AVFPTTLKTM ATAPQGIGRL GRYARLLRHY PQVAIGGIGA EQFPQVLATG VGSIAVVRAL VNAPDPDEAA RQLMGRIALS ANERLAHSND ELAP // ID A1WYM7_HALHL Unreviewed; 322 AA. AC A1WYM7; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 13-NOV-2013, entry version 61. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=Hhal_2025; OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira OS halophila (strain DSM 244 / SL1)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Halorhodospira. OX NCBI_TaxID=349124; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 244 / SL1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Hoff W., Richardson P.; RT "Complete sequence of Halorhodospira halophila SL1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000544; ABM62789.1; -; Genomic_DNA. DR RefSeq; YP_001003591.1; NC_008789.1. DR ProteinModelPortal; A1WYM7; -. DR STRING; 349124.Hhal_2025; -. DR EnsemblBacteria; ABM62789; ABM62789; Hhal_2025. DR GeneID; 4710378; -. DR KEGG; hha:Hhal_2025; -. DR PATRIC; 22098345; VBIHalHal112047_2000. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HHAL349124:GI3I-2074-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 322 AA; 35051 MW; B08D5F366293BCE4 CRC64; MHTASPAAPI HVAAAVVRGE DQRVLVQCRP DHLDHGGLWE FPGGKIEPGE SVADALVREL DEELGIRVRP GALRIRVPWD YGHRRVVLHV LDVNEWTGRP IGREGQAVDW LTPEAMAERA WPAANWPIIR SLQLPDRYLI TPVEPADADA WLARLDAALA RGVRLVQLRR PDLDVEAWVR LGRALRRRCD AHGAWLLANG PAEQARAVGA DGVHWSSRVL AEGPQRPGWA RWVGASCHNG DELERAAACG ADFALLSPVQ WTASHPEQSG MGWERFAAWV AGARLPVYAL GGVGPADIHR ARACGGQGVA AIRGLLAEAG RR // ID A1ZKW6_9BACT Unreviewed; 208 AA. AC A1ZKW6; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 19-FEB-2014, entry version 31. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=M23134_00086; OS Microscilla marina ATCC 23134. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Microscilla. OX NCBI_TaxID=313606; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23134; RA Haygood M., Podell S., Anderson C., Hopkinson B., Roe K., Barbeau K., RA Gaasterland T., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWS01000013; EAY28932.1; -; Genomic_DNA. DR ProteinModelPortal; A1ZKW6; -. DR EnsemblBacteria; EAY28932; EAY28932; M23134_00086. DR PATRIC; 26275710; VBIMicMar10703_3013. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 208 AA; 23633 MW; 9CDC68A18BF5FF15 CRC64; MNIIVISSPQ QELNEASIIG ALFEHGLEVF HLRKPTYSIY DTEALIQAIE PKFRDRVVLH HHYALAEKYN LRGIHFTGHY VKSHSDQLTN WYDKAKQQAM TVSGSKHQLK ELETLEVPYN YVFLSPVFDS ISKAGYKSNF ADLKSIEKYK SATQLIALGG ISLDKIDQVK RMGFDGAAVL GTVWEKPAQA IAVFMELKAA WEKKDQIF // ID A1ZKW8_9BACT Unreviewed; 214 AA. AC A1ZKW8; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 19-FEB-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=M23134_00088; OS Microscilla marina ATCC 23134. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Microscilla. OX NCBI_TaxID=313606; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23134; RA Haygood M., Podell S., Anderson C., Hopkinson B., Roe K., Barbeau K., RA Gaasterland T., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWS01000013; EAY28934.1; -; Genomic_DNA. DR ProteinModelPortal; A1ZKW8; -. DR EnsemblBacteria; EAY28934; EAY28934; M23134_00088. DR PATRIC; 26275714; VBIMicMar10703_3015. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22926 MW; 6E6D4ADA097D388B CRC64; MKKEIAKLQY ITQQTDTLSH VQAAQKACEA GCNWVQLRVK DTPEAEVQAI ALKVKAICAL YGATFILNDH VAVAKAVHAD GVHLGKEDMS PKEARKILGK DAIIGGTANT FEDVQRLAKA GVDYIGAGPF RFTTTKKKLS PVLGAQGYTT LMANCYEQNI DTPIVAIGGI VAEDMSIIRQ TGVYGVAVSS VITHHQAPAQ VVETIQTTFD SSKV // ID A2BXY1_PROM5 Unreviewed; 353 AA. AC A2BXY1; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=P9515_14351; OS Prochlorococcus marinus (strain MIT 9515). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=167542; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9515; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., RA Steglich C., Church G.M., Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000552; ABM72642.1; -; Genomic_DNA. DR RefSeq; YP_001011749.1; NC_008817.1. DR ProteinModelPortal; A2BXY1; -. DR STRING; 167542.P9515_14351; -. DR EnsemblBacteria; ABM72642; ABM72642; P9515_14351. DR GeneID; 4718721; -. DR KEGG; pmc:P9515_14351; -. DR PATRIC; 23016518; VBIProMar113831_1476. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR167542:GI3N-1474-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 128 Unknown (By similarity). FT REGION 129 353 Thiamine-phosphate synthase (By FT similarity). FT REGION 180 184 HMP-PP binding (By similarity). FT METAL 213 213 Magnesium (By similarity). FT METAL 232 232 Magnesium (By similarity). FT BINDING 212 212 HMP-PP (By similarity). FT BINDING 251 251 HMP-PP (By similarity). FT BINDING 280 280 HMP-PP (By similarity). FT BINDING 307 307 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 353 AA; 40020 MW; 3E587577A46C4156 CRC64; MEQPKINQPE DLRISQIIDA NLDRAREGLR VLEDWARFGL GNEDFVIRIK NLRQILGKNH LEIYKKSRNH IEDQCKGLSH IEQIHRKSPS KIISSNSARV QEALRVIEEF SRNHNNKLSK IASDIRYEIY TLEIELLNLN TRKRAELIIR ENNLYSITDH RDNLLQIIEK ILLGGVKIIQ HRFKEGNDKN HLKEAIQVKN LCEKYNSLFI VNDRVDIAMA SNADGVHLGQ EDIDVKTARK LLGSSKIIGV SANNSTDINK AIKDGCDYIG IGPVFQSLTK KGKEPLGVEK IKTLIKDINI PCFAIGGINK LNISCLKSHR ISKVAVVSGL LNSEDPKEEA IIILKKLSNE NYS // ID A2C440_PROM1 Unreviewed; 350 AA. AC A2C440; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NATL1_16941; OS Prochlorococcus marinus (strain NATL1A). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=167555; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NATL1A; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., RA Steglich C., Church G.M., Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000553; ABM76250.1; -; Genomic_DNA. DR RefSeq; YP_001015514.1; NC_008819.1. DR ProteinModelPortal; A2C440; -. DR STRING; 167555.NATL1_16941; -. DR EnsemblBacteria; ABM76250; ABM76250; NATL1_16941. DR GeneID; 4779849; -. DR KEGG; pme:NATL1_16941; -. DR PATRIC; 23021017; VBIProMar31285_1727. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR167555:GI3K-1727-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 128 Unknown (By similarity). FT REGION 129 350 Thiamine-phosphate synthase (By FT similarity). FT REGION 180 184 HMP-PP binding (By similarity). FT METAL 213 213 Magnesium (By similarity). FT METAL 232 232 Magnesium (By similarity). FT BINDING 212 212 HMP-PP (By similarity). FT BINDING 251 251 HMP-PP (By similarity). FT BINDING 280 280 HMP-PP (By similarity). FT BINDING 307 307 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 350 AA; 39515 MW; F6A946D5D2CA2EB0 CRC64; MKSIPVTPPS DNRIAQLIDA NLDRAREGLR VMEDWCRFGL KRSDFSIQIK DWRQQLGVHH HNIYRKERLT SIDPAMGISH PLQTVRSTPE DVFIANSSRV QEALRVIEEF TRKTDPNLCE IASKIRYETY EIEIKVLKST EGVNKRETLK YCSVYLITSN RRDIEEVVLH ALKAGVKIVQ YREKFLNDNE KISQAKCLAS LCKKFNSLFI VNDRIDIALA VDADGIHLGQ EDMPTKIARQ LLGAEKIIGR STHCLEDIKN AEGEGCDYIG IGPIFPSETK KQLNPIGIDN LKKGLSETIL PAFAIGGINK SNITKLNQIN NLRIAVSNAI INSNDPFSTT EELIKFLICN // ID A2P7Z2_VIBCL Unreviewed; 440 AA. AC A2P7Z2; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 19-FEB-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=A55_0083; OS Vibrio cholerae 1587. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=412966; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1587; RA Heidelberg J., Sebastian Y.; RT "Annotation of Vibrio cholerae 1587."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAUR01000034; EAY34048.1; -; Genomic_DNA. DR ProteinModelPortal; A2P7Z2; -. DR EnsemblBacteria; EAY34048; EAY34048; A55_0083. DR PATRIC; 29700028; VBIVibCho116800_1980. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48905 MW; 82730D3F75276B45 CRC64; MVRLVFPRHL SALIGLVQYA LLQAKEQGFA IQHIRLDVGS EARFILEKSE ESLRIGSSLC SQEETSEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGNAAEQLII YSSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQC DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLASYQRLV NQIPYQGQHG IPTVAIGGID CSNIRDVLDC GVTAVAVVRA ITESSDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAREVADAHR // ID A2PS79_VIBCL Unreviewed; 440 AA. AC A2PS79; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 19-FEB-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=A51_B0062; OS Vibrio cholerae MZO-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=412883; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MZO-3; RA Heidelberg J., Sebastian Y.; RT "Annotation of Vibrio cholerae MZO-3."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAUU01000027; EAY41507.1; -; Genomic_DNA. DR ProteinModelPortal; A2PS79; -. DR EnsemblBacteria; EAY41507; EAY41507; A51_B0062. DR PATRIC; 28079255; VBIVibCho17340_1410. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48823 MW; 391AD1FB7A647ECC CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGFA IQHIRLDVGS DAQFILEKSE ESLRIGSSLC SQEETSEPCD YYLDYVSENR VSPEAIMCNA RCTVTVGFHD KYAFTLDKWQ YGNAAEQLII YPSENHRLNS KVNQHLAWVL ASLALGFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPA MQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QVDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CSNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID A2QZE7_ASPNC Unreviewed; 519 AA. AC A2QZE7; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 16-APR-2014, entry version 44. DE SubName: Full=Putative uncharacterized protein An12g04660; DE EC=2.5.1.3; DE EC=2.7.1.50; GN ORFNames=An12g04660; OS Aspergillus niger (strain CBS 513.88 / FGSC A1513). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=425011; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 513.88 / FGSC A1513; RX PubMed=17259976; DOI=10.1038/nbt1282; RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., RA Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., RA Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., RA Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M., RA Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., RA van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., RA Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., RA Henrissat B., Herweijer M., van den Hombergh J.P.T.W., RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., RA van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., RA van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., RA Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., RA Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., RA Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., RA Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., RA Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.; RT "Genome sequencing and analysis of the versatile cell factory RT Aspergillus niger CBS 513.88."; RL Nat. Biotechnol. 25:221-231(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM270269; CAK97157.1; -; Genomic_DNA. DR RefSeq; XP_001395536.1; XM_001395499.1. DR ProteinModelPortal; A2QZE7; -. DR STRING; 5061.CADANGAP00009718; -. DR EnsemblFungi; CADANGAT00009909; CADANGAP00009718; CADANGAG00009909. DR GeneID; 4985815; -. DR KEGG; ang:ANI_1_588104; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 519 AA; 54530 MW; 9894F9DCA20AD49E CRC64; MTLDLSVYLV TDSTPAILKG RDLCAVVEEA VKGGVTIVQY RDKKSDTGVQ VETAKKLHQI TKKYNVPLLI NDRVDVALAA GVEGVHLGQD DMAIEVARKL LPENSIIGIS ASSIEEAQKA VAAGADYLGI GTMFATPTKT NTKSIIGTAG TQAILEAISE SGRTVGTVSI GGINASNVQR VLYQSRAPNK ALDGVAIVSA IMAADDPKAA AAEFVKLVSS PPPFVRSDAT TPARDTSALL EQVPQVVQEV VKGHPLVHNM INYVVANFVA NVALSMGASP IMSPYGDEAV DLCQFDGALV INMGTLTSES IPNYLKAQKA YNMRGNPVVY DPVGAAATSI RRGAVTQLMS GGYFDLIKGN EGEIRQVFGS SGVTQRGVDS GPSNLDSHGK ARLARDLARR EHNIVLLTGA TDYLSDGERV VAVSNGHELL GQVTGTGCAV GTVSGAFLTT HPKDKFLAVL AGILMYEIAA ENAASADNVR GPGSFVPAFL DELYAIRQAA LKGDHSWFAG RAKVEEIQL // ID A2RPZ0_HERSE Unreviewed; 210 AA. AC A2RPZ0; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 19-FEB-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OS Herbaspirillum seropedicae. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Herbaspirillum. OX NCBI_TaxID=964; RN [1] RP NUCLEOTIDE SEQUENCE. RA Chaves D.F.S., Ferrer P.P., Monteiro R.A., Souza E.M., Cruz L.M., RA Pedrosa F.O.; RT "A two-dimensional proteome reference map of Herbaspirillum RT seropedicae proteins."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RG Genopar Consortium; RA Pedrosa F.O.; RT "Genome sequence of the nitrogen fixing bacterium Herbaspirillum RT seropedicae."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM490552; CAM32647.1; -; Genomic_DNA. DR ProteinModelPortal; A2RPZ0; -. DR PRIDE; A2RPZ0; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22941 MW; DDD6FBB377EFC14A CRC64; MKPEYAKHLR GLYIVTPDWD DTAQLLAATE LALQQGAALV QYRHKTADAQ QRQAQASALL ALCRQYQVPL IINDHVDLCL DIDADGIHVG GTDASIAEVR KAVGPDRIVG ASCYGTLELA HAAYRDGASY VAFGGFYPSR VKKYDFRTAP EIIAHSKREI PLPVVVIGGI TLENAPPLVE QGADMVAVIS SVYLVPVEER KTRELADLYR // ID A2S0J4_BURM9 Unreviewed; 209 AA. AC A2S0J4; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 2. DT 14-MAY-2014, entry version 45. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN OrderedLocusNames=BMA10229_1663; OS Burkholderia mallei (strain NCTC 10229). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=412022; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 10229; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000545; ABM99055.2; -; Genomic_DNA. DR RefSeq; YP_001025464.1; NC_008835.1. DR ProteinModelPortal; A2S0J4; -. DR STRING; 412022.BMA10229_1663; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EnsemblBacteria; ABM99055; ABM99055; BMA10229_1663. DR GeneID; 4789369; -. DR KEGG; bml:BMA10229_1664; -. DR PATRIC; 19129785; VBIBurMal46188_1623. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155668; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BMAL412022:GJI8-5071-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID A2S736_BURM9 Unreviewed; 367 AA. AC A2S736; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=BMA10229_A1776; OS Burkholderia mallei (strain NCTC 10229). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=412022; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 10229; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000546; ABN03615.1; -; Genomic_DNA. DR RefSeq; YP_001027755.1; NC_008836.1. DR ProteinModelPortal; A2S736; -. DR STRING; 412022.BMA10229_A1776; -. DR EnsemblBacteria; ABN03615; ABN03615; BMA10229_A1776. DR GeneID; 4792843; -. DR KEGG; bml:BMA10229_A1776; -. DR PATRIC; 19134518; VBIBurMal46188_3975. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BMAL412022:GJI8-1776-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 367 AA; 38315 MW; 3E9B351CCB7F5C2B CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGARAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID A2SG79_METPP Unreviewed; 532 AA. AC A2SG79; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE SubName: Full=Phosphomethylpyrimidine kinase / thiamine-phosphate pyrophosphorylase; DE EC=2.7.4.7; GN OrderedLocusNames=Mpe_A1606; OS Methylibium petroleiphilum (strain PM1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Methylibium. OX NCBI_TaxID=420662; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PM1; RX PubMed=17158667; DOI=10.1128/JB.01259-06; RA Kane S.R., Chakicherla A.Y., Chain P.S., Schmidt R., Shin M.W., RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., RA Hristova K.R.; RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta- RT proteobacterium Methylibium petroleiphilum PM1."; RL J. Bacteriol. 189:1931-1945(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000555; ABM94568.1; -; Genomic_DNA. DR RefSeq; YP_001020803.1; NC_008825.1. DR ProteinModelPortal; A2SG79; -. DR STRING; 420662.Mpe_A1606; -. DR EnsemblBacteria; ABM94568; ABM94568; Mpe_A1606. DR GeneID; 4787230; -. DR KEGG; mpt:Mpe_A1606; -. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; MPET420662:GHBE-1629-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 532 AA; 54901 MW; 59B5E386C9C5A7B3 CRC64; MTAERTTRPV VWSIAGTDSG GGAGLSADQR AADAFGVHLC PVVSAVTAQN SLAVTRIERL PPLALEAQLE ALADDLPPQV VKTGLLGGAE HVRRVAHWID RLRRRQPVAL VVDPVLAASS GATFADPDTL AAYRELLLPR ATLITPNRRE AAALLGQPEA GTAGLPAQAL ALRRRGAQAV CITGGDAADL DGRVLDWMAT EQADGWLAAP RIATPHHHGS GCTFASSAAA ALALGFVPAD ALVLAKMATG HALRHAHPAG AGRGPVRAAA GFASDPSLMP WLSWGAAPVF APAAESEAPP ASLGLYAIVD SAARAEQVLA AGVRTLQLRL KTPAVPDAGW HPALRATLQR GIAAARGTGA ALFVNDHWQL AAELGAPGVH LGQEDLLALG DEGRARLRAS GLALGISSHS LWELARARTL APHYVACGPV WPTLTKAMPW RPQGLDNLAW WCAMAGRPVV AIGGILTPER VEAAARCGAD GVCAVRVLGD DPARVLPSLQ RALQAGRQAP TPAPVPALPH PSLALSVAPR PS // ID A2SQ46_METLZ Unreviewed; 212 AA. AC A2SQ46; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mlab_0276; OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z). OC Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales; OC Methanocorpusculaceae; Methanocorpusculum. OX NCBI_TaxID=410358; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43576 / DSM 4855 / Z; RX PubMed=21304657; DOI=10.4056.sigs.35575; RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., RA Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., RA Pitluck S., Hauser L., Land M., Lucas S., Richardson P., Whitman W.B., RA Kyrpides N.C.; RT "Complete genome sequence of Methanocorpusculum labreanum type strain RT Z."; RL Stand. Genomic Sci. 1:197-203(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000559; ABN06452.1; -; Genomic_DNA. DR RefSeq; YP_001029719.1; NC_008942.1. DR ProteinModelPortal; A2SQ46; -. DR STRING; 410358.Mlab_0276; -. DR EnsemblBacteria; ABN06452; ABN06452; Mlab_0276. DR GeneID; 4795430; -. DR KEGG; mla:Mlab_0276; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; HRFYFIT; -. DR BioCyc; MLAB410358:GH7C-280-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23329 MW; F7895E0CC8FACDC2 CRC64; MTANNFGLYL IITKPSFSYR KIAETAVKYN VQYLQLREKS LSDREILKAA DEIMQVTNGT GTKFILNDRA DLAFICGADG LHLGQDDISL CDAKKICGEK VFRFGLSTHN LEQVKEAVQL KPDYIGFGPI FTTPTKAKPD PVVGTEMIPE AVKLAGDIPV VAIGGIDGEN LISVLDAGAR NVCMVRYFMN SMHFETRVKE TVKILNDYGI CG // ID A2SU12_METLZ Unreviewed; 210 AA. AC A2SU12; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mlab_1657; OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z). OC Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales; OC Methanocorpusculaceae; Methanocorpusculum. OX NCBI_TaxID=410358; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43576 / DSM 4855 / Z; RX PubMed=21304657; DOI=10.4056.sigs.35575; RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., RA Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., RA Pitluck S., Hauser L., Land M., Lucas S., Richardson P., Whitman W.B., RA Kyrpides N.C.; RT "Complete genome sequence of Methanocorpusculum labreanum type strain RT Z."; RL Stand. Genomic Sci. 1:197-203(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000559; ABN07818.1; -; Genomic_DNA. DR RefSeq; YP_001031085.1; NC_008942.1. DR ProteinModelPortal; A2SU12; -. DR STRING; 410358.Mlab_1657; -. DR EnsemblBacteria; ABN07818; ABN07818; Mlab_1657. DR GeneID; 4795251; -. DR KEGG; mla:Mlab_1657; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; MLAB410358:GH7C-1717-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22135 MW; 4142768F33B1CC30 CRC64; MKYDLYVVTD ENLSNGYSHA EIAKLAVDGG ANVIQLRDKD MDSASLFTEA VKIRMITKDK ALFIVNDRLD IALASKADGV HLGQSDLPVD VVRRLVPENF IIGISIGSVE EALKGVKDGA DYVAVSPVFS TGSKPDAGTG HGISCISAVR QAVEKDIPVL GIGGINCDNI PEVIKAGLDG ICVISAVVSA PDITKAAEDL CQKIRSAKNE // ID A2TRP1_9FLAO Unreviewed; 200 AA. AC A2TRP1; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 16-OCT-2013, entry version 34. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=MED134_07931; OS Dokdonia donghaensis MED134. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Dokdonia. OX NCBI_TaxID=313590; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED134; RX PubMed=17215843; DOI=10.1038/nature05381; RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., RA Pascher T., Neutze R., Pedros-Alio C., Pinhassi J.; RT "Light stimulates growth of proteorhodopsin-containing marine RT Flavobacteria."; RL Nature 445:210-213(2007). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED134; RA Gonzalez J., Fernandez-Gomez B., Fernandez-Guerra A., RA Gomez-Consarnau L., Pedro-Alio C., Pinhassi J., Jaenicke S., RA Goesmann A., Puigbo P.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMZ01000002; EAQ39403.1; -; Genomic_DNA. DR ProteinModelPortal; A2TRP1; -. DR EnsemblBacteria; EAQ39403; EAQ39403; MED134_07931. DR PATRIC; 36978925; VBIDokDon50125_0104. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 200 AA; 22428 MW; 56EFAD255D305CF4 CRC64; MILLISPEQT TPDEVETLHH LFEAGLAHYH FRKPEASLDE HITYLNRVDA QYHNRIMTHN YHEELCKKFD LRGVHLEEAK WRAQETRLEG YVSAFAKANK KVSSSYHELE DLEAQSVTFD YTILSPVFAA ISKSDMQGRG FNVRASEKFI VGMGGINAVT TPEAVALGFK GVGALGGIWN AQNPVAAFVE MQEAFKEANT // ID A2VFA3_MYCTX Unreviewed; 222 AA. AC A2VFA3; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TBCG_00406; OS Mycobacterium tuberculosis C. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=348776; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C; RG The Broad Institute Genome Sequencing Platform; RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L., RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., RA Mauceli E., Brockman W., Rounsley S., Young S., LaButti K., RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., RA Montgomery P., Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., RA Oleary S., Alvarado L., Murray M., Kreiswirth B.; RT "The Genome Sequence of Mycobacterium tuberculosis (strain C)."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH482373; EAY58834.1; -; Genomic_DNA. DR ProteinModelPortal; A2VFA3; -. DR SMR; A2VFA3; 1-221. DR EnsemblBacteria; EAY58834; EAY58834; TBCG_00406. DR PATRIC; 26044368; VBIMycTub57268_2389. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID A2VTI6_9BURK Unreviewed; 375 AA. AC A2VTI6; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 19-FEB-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BCPG_01290; OS Burkholderia cenocepacia PC184. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=350702; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PC184; RG The Broad Institute Genome Sequencing Platform; RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L., RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., RA Mauceli E., Brockman W., Young S., LaButti K., DeCaprio D., RA Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., RA Howarth C., White J., Larson L., Alvarado L., Kodira C., Zeng Q., RA Yandava C., Oleary S., LiPuma J., Lory S.; RT "The Genome Sequence of Burkholderia cenocepacia (strain PC184)."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH482377; EAY63032.1; -; Genomic_DNA. DR ProteinModelPortal; A2VTI6; -. DR EnsemblBacteria; EAY63032; EAY63032; BCPG_01290. DR PATRIC; 26849358; VBIBurCen79288_1284. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 375 AA; 39309 MW; B51F10E30A099A1B CRC64; MSAARFADAF WPPADELAEA AERIRARLGD WPEGAAPWRL CVAAPDVPAD GDVLIVSAGD RAAQARASAV SRPASPDAVA IEFDEQGAVL HAVGVRYALA AAHPLADDWI AALAAFLDCG FAPVDALVLA LAWRDGDETR AADAWPVDAA RFPQVAGLPP APEPAFAPCP ARLGLYPVVP SAEWVERVLD GGARTVQLRV KDATPDALRR EIARAVAAGR RYPDARVFIN DHWQIAAEEG AYGVHLGQED LETADLAAIA RAGLRLGLSS HGYYEMLRAL HERPSYLALG PVYATATKAV AAPPQGLARI ARYARFAGAR APLVAIGGVG LDTLPAVLAT GVGSVAVVSA VTGAADYRTA LIALQQCFTG QFDNH // ID A2W006_9BURK Unreviewed; 194 AA. AC A2W006; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 16-OCT-2013, entry version 31. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=BCPG_03661; OS Burkholderia cenocepacia PC184. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=350702; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PC184; RG The Broad Institute Genome Sequencing Platform; RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L., RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., RA Mauceli E., Brockman W., Young S., LaButti K., DeCaprio D., RA Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., RA Howarth C., White J., Larson L., Alvarado L., Kodira C., Zeng Q., RA Yandava C., Oleary S., LiPuma J., Lory S.; RT "The Genome Sequence of Burkholderia cenocepacia (strain PC184)."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH482378; EAY65302.1; -; Genomic_DNA. DR ProteinModelPortal; A2W006; -. DR EnsemblBacteria; EAY65302; EAY65302; BCPG_03661. DR PATRIC; 26854847; VBIBurCen79288_3732. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 19947 MW; E3E35DBBF3447AD7 CRC64; MNAPLPRCCV ITPEPASASA ADRVAFLDRL SAVLARGETL VQLRVKSLDA AAFASLAAAA LARCDAAGAH LMLNGPIDAT GVIRLDGAGW HLDGAALRAA AQRPLPADRW VSAACHTQDD LLLAAGAGAD FVTLSPVLPT LSHPGAPALG WTRFDALAAQ AAMPVFALGG MTRAHLDDAR RHGAYGIAGI RGFW // ID A2WDA5_9BURK Unreviewed; 365 AA. AC A2WDA5; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 16-OCT-2013, entry version 29. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=BDAG_02726; OS Burkholderia dolosa AUO158. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=350701; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AUO158; RG The Broad Institute Genome Sequencing Platform; RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L., RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., RA Mauceli E., Brockman W., Young S., LaButti K., DeCaprio D., RA Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., RA Howarth C., White J., Larson L., Alvarado L., Kodira C., Zeng Q., RA Yandava C., Oleary S., LiPuma J., Lory S.; RT "The Genome Sequence of Burkholderia dolosa (strain AU0158)."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH482380; EAY69951.1; -; Genomic_DNA. DR ProteinModelPortal; A2WDA5; -. DR EnsemblBacteria; EAY69951; EAY69951; BDAG_02726. DR PATRIC; 26866440; VBIBurDol134514_0970. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 365 AA; 38464 MW; 788194541086D940 CRC64; MHSGRRPMNW PKAAERIRAR LGDWPRGSAP WRLCLATPDA PADGDVLIVS AGDRAGQARA SAVSRPVSPD AVAIEFGEQH AMLHAAGARH ALEAAHPLAD DWIAALAAFL DCGFAPVDAL VLALAWCDGD ETRSADAWPI DAARFPRIAG LPAAPEPPFP PCPAQLGLYP VVPTADWVER VLDCGVRTVQ LRMKSATPDV LRREIARAVA AGRRYPDARV FVNDHWQIAA EEGAYGVHLG QEDVETADLA AIARAGLRLG LSSHGYYEML RALHERPSYL ALGPVFATAT KAVAAPPQGL ARIARYARFA GARAPLVAIG GVALDTLPDV LATGVGSVAV VSAVTERAGL SGGDRCVAAM FSLTI // ID A2WDL6_9BURK Unreviewed; 646 AA. AC A2WDL6; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 16-OCT-2013, entry version 33. DE SubName: Full=Hemolysin; GN ORFNames=BDAG_02841; OS Burkholderia dolosa AUO158. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=350701; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AUO158; RG The Broad Institute Genome Sequencing Platform; RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L., RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., RA Mauceli E., Brockman W., Young S., LaButti K., DeCaprio D., RA Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., RA Howarth C., White J., Larson L., Alvarado L., Kodira C., Zeng Q., RA Yandava C., Oleary S., LiPuma J., Lory S.; RT "The Genome Sequence of Burkholderia dolosa (strain AU0158)."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH482381; EAY70062.1; -; Genomic_DNA. DR ProteinModelPortal; A2WDL6; -. DR EnsemblBacteria; EAY70062; EAY70062; BDAG_02841. DR PATRIC; 26866725; VBIBurDol134514_3696. DR GO; GO:0030554; F:adenyl nucleotide binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR002550; DUF21. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00571; CBS; 2. DR Pfam; PF01595; DUF21; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SMART; SM00116; CBS; 2. DR SUPFAM; SSF51391; SSF51391; 1. DR PROSITE; PS51371; CBS; 2. PE 4: Predicted; SQ SEQUENCE 646 AA; 70258 MW; 085F61E83B3FC3A9 CRC64; MALNGFFVAA EFGLVKLRTT RVKTLARKHG LRGRILGVVH GRLDAYLSAC QLGITLASLG LGWIGEPAFA ELIGPLLDLL GVESERVVHL ISLVFAFSLI SFLHIVVGEL APKSMAIRQP EKVGLWVALP LYAFYWAMYP AIWLLNTSAN AVLRLAGLSA DHGSDAHYST DELKLILRSR RSTAGGAAQP TRGSYSNDEW NTLAHSLDFS SMTVSDLMRP AHEMIGLRRD LPLPDNMEIV ARHRFSRYPL FADASRERVF GLIHLKDLLL ARHAGAALDD LSDYVRPVQY VKPDMPALDL FRRFRKGAPH FALVGNKREK PIGFLTLDNL LGALVGQIHD EFHQGDADWS RLDDGTLMGK GSLPVVSLEQ ALGIDIDEGR AESRRRAGDP GAERSAVRRA ARVVRSLRRR REEDEWASDR ARARLSEDDE GKPTNDGLVT ARAMNATLPR CCVITPEPAS ASAADCRAFV DRLEAVLARG DTLVQLRAKS LDAAAFARLA ADALARCDAA GAQLMLNGPI DAAGVMRLDG AGWHLDGAAL RTVAQRPLPA DTPVSAACHT ADDLLLAARA GADFVTLSPV RPTLSHPGAP TLGWEKFDAL GRAGRDARLR ARRDDARASR RRASASRIRN RGYSRVLVSR GAAARG // ID A3D462_SHEB5 Unreviewed; 650 AA. AC A3D462; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 14-MAY-2014, entry version 63. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=Sbal_2023; OS Shewanella baltica (strain OS155 / ATCC BAA-1091). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=325240; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS155 / ATCC BAA-1091; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D.R., Brettin T., Bruce D., Han C., Tapia R., RA Brainard J., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Brettar I., Klappenbach J., Konstantinidis K., RA Rodrigues J., Tiedje J., Richardson P.; RT "Complete sequence of chromosome of Shewanella baltica OS155."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000563; ABN61525.1; -; Genomic_DNA. DR RefSeq; YP_001050394.1; NC_009052.1. DR ProteinModelPortal; A3D462; -. DR STRING; 325240.Sbal_2023; -. DR EnsemblBacteria; ABN61525; ABN61525; Sbal_2023. DR GeneID; 4844261; -. DR KEGG; sbl:Sbal_2023; -. DR PATRIC; 37182973; VBISheBal55297_2324. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SBAL325240:GCTA-2062-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 650 AA; 68610 MW; 1F1747E4725471E7 CRC64; MLGIHGDNAP MNTEHPAFVW TIAGSDSGGG AGIQADLATI QDLGCHGCSV VTTVTAQSSV AVTLVEPVSA AMLMAQLTTL LSDLPPKAIK IGLLADQTQV ALLADWIASF KIHYPSVPVI VDPVMVASCG DALAVDNCQD IKSAAKSALD FKPFKGLIEL ITPNVLELGR LTHSDVSTKA QFAAAALALS QSLDCSVLAK GGDVSFGSTD ILDDTHAQTH DNTYAQTQAN VHVIALDSNG WDLELAEDYL VCRQVRASSK LHQNGRFWLA SQRVNTPHNH GSGCTLSSAI AAVLAQGFVL QDAVVVAKAY VSQGLSAAIG LGQGPGPLAR TGWPNDVSRY AKINLCDSNF ISHQLNQHLD VGNDLVATVL SATDQATAQV RIASTQPQNI LSHGFKVLDA DLGVYPVVND LTMLESLLAA GVKTLQLRIK TDISELTTAG LAESDLGKSA LSRCESGKSK SGEPELIGSE LEAQIQTAIA LGKHFNAQLF INDHWQLAIK YHAFGVHLGQ EDLAVTDLAA IQAAGLALGI SSHSYFELLL AHQYSPSYIA LGHIFPTTTK QMPSAPQGLA KLKHYVALLQ DHYPLVAIGG IDLTNLAKVK ATGVGNIAVV RAITKAKDPL AAFAELSQAW EQCSLSEELA VKHELDAKHE // ID A3DD07_CLOTH Unreviewed; 356 AA. AC A3DD07; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cthe_0601; OS Clostridium thermocellum (strain ATCC 27405 / DSM 1237). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=203119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.; RT "Complete sequence of Clostridium thermocellum ATCC 27405."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000568; ABN51836.1; -; Genomic_DNA. DR RefSeq; YP_001037029.1; NC_009012.1. DR ProteinModelPortal; A3DD07; -. DR STRING; 203119.Cthe_0601; -. DR DNASU; 4808203; -. DR EnsemblBacteria; ABN51836; ABN51836; Cthe_0601. DR GeneID; 4808203; -. DR KEGG; cth:Cthe_0601; -. DR PATRIC; 19514871; VBICloThe47081_0627. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CTHE203119:GIW8-620-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 183 187 HMP-PP binding (By similarity). FT REGION 280 282 THZ-P binding (By similarity). FT REGION 331 332 THZ-P binding (By similarity). FT METAL 216 216 Magnesium (By similarity). FT METAL 235 235 Magnesium (By similarity). FT BINDING 215 215 HMP-PP (By similarity). FT BINDING 254 254 HMP-PP (By similarity). FT BINDING 283 283 HMP-PP (By similarity). FT BINDING 311 311 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 356 AA; 40444 MW; 3C88F277A3F463FC CRC64; MGLDNLYRVL DANVNRTSEG LRVLEDLARF CYNDRLLSKR IKELRHSVRK NIAGLVPNLI SSRDSVNDVG LKTSMEMDID RKASLLDLAR ANFKRVQEAL RTVEESLKVL NENDLSKFYE SCRFETYSIE KEYFKVLTFE NKKGRLNEII TGLYCITSEE HSKGRSNIEV VEKMIKAGVK IIQYREKKKS LLEKYNECKK IREMTLDSGV TFIVNDNIDI AMMVKADGVH IGQDDLPIEK VRELVGDEMI IGISTHSPTQ AEDAVRRGAD YIGVGPLYRT YTKEDVCEPV GLEYLDYVVK NINIPYVAIG GIKEHNMDEV LARGARCIAM VTEIVGADDI EEKISKVKSK FSRGVL // ID A3EJS9_VIBCL Unreviewed; 440 AA. AC A3EJS9; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 19-FEB-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCV51_0045; OS Vibrio cholerae V51. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=345075; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=V51; RA Heidelberg J., Sebastian Y.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS179721; EAZ50228.1; -; Genomic_DNA. DR ProteinModelPortal; A3EJS9; -. DR EnsemblBacteria; EAZ50228; EAZ50228; VCV51_0045. DR PATRIC; 38598579; VBIVibCho81623_1348. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 49227 MW; 4E43E77B01A27C43 CRC64; MVRLVFPRHL SALIAHVQYA LLQAKEQGFA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQEETSEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGNAAEQLII YSSETHRLNS KLNQHLAWVL ATLTLDFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPV VQSNIRFLYT QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQC DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID RSNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSVFAD FVDAEYKLMP ASESCEPLSC LAREVADAHR // ID A3EQ31_9BACT Unreviewed; 215 AA. AC A3EQ31; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=UBAL2_82410338; OS Leptospirillum rubarum. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=419542; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=17344860; DOI=10.1038/nature05624; RA Lo I., Denef V.J., Verberkmoes N.C., Shah M.B., Goltsman D., RA DiBartolo G., Tyson G.W., Allen E.E., Ram R.J., Detter J.C., RA Richardson P., Thelen M.P., Hettich R.L., Banfield J.F.; RT "Strain-resolved community proteomics reveals recombining genomes of RT acidophilic bacteria."; RL Nature 446:537-541(2007). RN [2] RP NUCLEOTIDE SEQUENCE. RX PubMed=19429552; DOI=10.1128/AEM.02943-08; RA Goltsman D.S., Denef V.J., Singer S.W., VerBerkmoes N.C., Lefsrud M., RA Mueller R.S., Dick G.J., Sun C.L., Wheeler K.E., Zemla A., Baker B.J., RA Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., RA Banfield J.F.; RT "Community genomic and proteomic analyses of chemoautotrophic iron- RT oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum RT ferrodiazotrophum" (Group III) bacteria in acid mine drainage RT biofilms."; RL Appl. Environ. Microbiol. 75:4599-4615(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS180869; EAY57935.1; -; Genomic_DNA. DR ProteinModelPortal; A3EQ31; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23168 MW; BD52AC7BEFC5FF15 CRC64; MIKSLVSPLF PLMYVTPEDI PVKPLVQRAL EAVAGGVTSI QVRRKGGSAK ELFDLAILLA ESLPSGFPLI VNSRLDVALE AGAWGLHFPD DHIPLPFFRD RAPNLRLGVS CHSLESARKA FSEGADYLVA GPVFDTPSKR SYGPPPGPAF LGKVTKFVPL PVLAIGGVTE EGIPEVWRSG ASGFAVMGAL AYEEDTRSRA FSLRKCWSRQ GDVRP // ID A3EVK0_9BACT Unreviewed; 212 AA. AC A3EVK0; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 19-FEB-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=UBAL2_86920039; OS Leptospirillum rubarum. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=419542; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=17344860; DOI=10.1038/nature05624; RA Lo I., Denef V.J., Verberkmoes N.C., Shah M.B., Goltsman D., RA DiBartolo G., Tyson G.W., Allen E.E., Ram R.J., Detter J.C., RA Richardson P., Thelen M.P., Hettich R.L., Banfield J.F.; RT "Strain-resolved community proteomics reveals recombining genomes of RT acidophilic bacteria."; RL Nature 446:537-541(2007). RN [2] RP NUCLEOTIDE SEQUENCE. RX PubMed=19429552; DOI=10.1128/AEM.02943-08; RA Goltsman D.S., Denef V.J., Singer S.W., VerBerkmoes N.C., Lefsrud M., RA Mueller R.S., Dick G.J., Sun C.L., Wheeler K.E., Zemla A., Baker B.J., RA Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., RA Banfield J.F.; RT "Community genomic and proteomic analyses of chemoautotrophic iron- RT oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum RT ferrodiazotrophum" (Group III) bacteria in acid mine drainage RT biofilms."; RL Appl. Environ. Microbiol. 75:4599-4615(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS180874; EAY55885.1; -; Genomic_DNA. DR ProteinModelPortal; A3EVK0; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23543 MW; 8235E27593C48F74 CRC64; MTERSWSFPS LLYLAGTQDF PSPDHLFSHV EKACQGGLKW FQYREKVLPD RLLYETARRL REITREYGTL LTINDRTDIA LLVGADGVHL GQDDLPSVRE FRKLFPSEVL HLGISTHSPY EVRRALLLKP DYLGVGPIFQ TSTKDTGVEP RGVAAVEETR KLTSLPLVAI GGITAEHAGV LYRAGSHAVA LSGAITSSPD PLPVLEMFFR SR // ID A3GMS8_VIBCL Unreviewed; 440 AA. AC A3GMS8; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=A5C_0079; OS Vibrio cholerae NCTC 8457. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=417399; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 8457; RA Heidelberg J., Sebastian Y.; RT "Annotation of Vibrio cholerae NCTC 8457."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWD01000025; EAZ73830.1; -; Genomic_DNA. DR ProteinModelPortal; A3GMS8; -. DR EnsemblBacteria; EAZ73830; EAZ73830; A5C_0079. DR PATRIC; 30066215; VBIVibCho106694_1365. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID A3GZ04_VIBCL Unreviewed; 440 AA. AC A3GZ04; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-MAR-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=A5E_0093, VCE_000376; OS Vibrio cholerae B33. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=417400; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B33; RA Heidelberg J., Sebastian Y.; RT "Annotation of Vibrio cholerae B33."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B33; RX PubMed=19850044; DOI=10.1016/j.febslet.2009.10.041; RA Taviani E., Grim C.J., Chun J., Huq A., Colwell R.R.; RT "Genomic analysis of a novel integrative conjugative element in Vibrio RT cholerae."; RL FEBS Lett. 583:3630-3636(2009). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B33; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D., RA Vonstein V.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWE01000027; EAZ77581.1; -; Genomic_DNA. DR EMBL; ACHZ01000009; EEO19022.1; -; Genomic_DNA. DR EnsemblBacteria; EAZ77581; EAZ77581; A5E_0093. DR EnsemblBacteria; EEO19022; EEO19022; VCE_000376. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48888 MW; 0F07EC45EC75720D CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWL YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID A3HUE5_9BACT Unreviewed; 214 AA. AC A3HUE5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-MAR-2014, entry version 34. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=ALPR1_00960; OS Algoriphagus machipongonensis. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae; OC Algoriphagus. OX NCBI_TaxID=388413; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PR1; RG The Broad Institute Genome Sequencing Platform; RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B., RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Burger G., Gray M.W., RA Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I., RA Lander E., Nusbaum C.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PR1; RX PubMed=21183675; DOI=10.1128/JB.01421-10; RA Alegado R.A., Ferriera S., Nusbaum C., Young S.K., Zeng Q., RA Imamovic A., Fairclough S.R., King N.; RT "Complete genome sequence of Algoriphagus sp. PR1, bacterial prey of a RT colony-forming choanoflagellate."; RL J. Bacteriol. 193:1485-1486(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXU02000001; EAZ81767.1; -; Genomic_DNA. DR ProteinModelPortal; A3HUE5; -. DR EnsemblBacteria; EAZ81767; EAZ81767; ALPR1_00960. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 214 AA; 23516 MW; AC5675DF804772A5 CRC64; MKTSATISGG LYLVIDPSKE ETLLLKSLKQ ALSAKPCAVQ IWDNFPEKPP VAGLIGKIKV LCKAAKVPLL INNHPEWVEL FDLDGVHFDE INQFSEKCLK TFHDMRKIVG VTVNNDLKTI KKAVDFGVDY LSFCSMFPSS TSTSCELVDF ETVRKTREMT QNPIFLAGGI SPQNLADLES LSFDGIAVVS GVMSSEDPKA AILNYQQSLS TLNK // ID A3I925_9BACI Unreviewed; 213 AA. AC A3I925; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BB14905_12335; OS Bacillus sp. B14905. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=388400; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B14905; RA Edwards R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXV01000009; EAZ85967.1; -; Genomic_DNA. DR ProteinModelPortal; A3I925; -. DR EnsemblBacteria; EAZ85967; EAZ85967; BB14905_12335. DR PATRIC; 25221363; VBIBacSp135347_1893. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23359 MW; 52A342551DDC59B2 CRC64; MKREDLQLYF IMGTSNISQQ EPLAVLEQAL RAGITMFQLR EKGPNALTGL AYEQFARQCQ KRCQHYRVPF IINDDVDLAV RLGADGVHIG QDDEQIAIAR KKMANRLLGV SVHSQEELQT AIDHHADYVG IGPIFATTSK SDAQPPCGTI FLQQASKLQP NLPIVAIGGI NWTNANIVLQ AGADGVAVIS AICDSKDIEQ TVSMFKSLSR IKK // ID A3IVP9_9CHRO Unreviewed; 339 AA. AC A3IVP9; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CY0110_27064; OS Cyanothece sp. CCY0110. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=391612; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCY0110; RA Stal L., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXW01000044; EAZ89439.1; -; Genomic_DNA. DR ProteinModelPortal; A3IVP9; -. DR EnsemblBacteria; EAZ89439; EAZ89439; CY0110_27064. DR PATRIC; 27730623; VBICyaSp137568_4197. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 121 Unknown (By similarity). FT REGION 122 339 Thiamine-phosphate synthase (By FT similarity). FT REGION 169 173 HMP-PP binding (By similarity). FT REGION 266 268 THZ-P binding (By similarity). FT METAL 202 202 Magnesium (By similarity). FT METAL 221 221 Magnesium (By similarity). FT BINDING 201 201 HMP-PP (By similarity). FT BINDING 240 240 HMP-PP (By similarity). FT BINDING 269 269 HMP-PP (By similarity). FT BINDING 296 296 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 339 AA; 38085 MW; F0B74E5C3E1D9269 CRC64; MDKNLAISRI LDANLDRARE GLRVVEEWCR LGLENSNWAE NCKQMRQEIA HWHTSELRMS RDTPNDPGVQ LSHPQEEKRE SINQLLQANL CRVQEALRVL EEYGKLYDPK MGSACKKIRY QVYTLESELL QTDRYQKLKR ASLYLVTSST ENLLAIVESA LQGGLTLVQY REKKIDDIMR FNMAQKLCEL CHKYDALFIV NDRVDIALGV DADGIHLGQQ DIPIALARRI LGPNKIIGCS TTNPQEMEKA IAEKPDYIGV GPVYATPTKP DKKAAGLDYV KYAAETSPIP WFAIGGIDDN NVTEVMASGG TQVALVRAIM EAANPKIATQ ELLKKLTVK // ID A3JA89_9ALTE Unreviewed; 314 AA. AC A3JA89; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 44. DE SubName: Full=Uncharacterized protein; GN ORFNames=MELB17_19239; OS Marinobacter sp. ELB17. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=270374; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ELB17; RA Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXY01000002; EBA01219.1; -; Genomic_DNA. DR ProteinModelPortal; A3JA89; -. DR EnsemblBacteria; EBA01219; EBA01219; MELB17_19239. DR PATRIC; 30999596; VBIMarSp19762_0879. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 314 AA; 33733 MW; 1A71076952E4AD93 CRC64; MHVAVGVIIR DGRVLIARRL EHAHQGGLLE FPGGKVEPGE TVQQALVREI AEETGLKLIE SALQPVIGVR HDYGDKRVFL DVWSTDAAAG EAHGREGQPI QWLLPQDLRD ADFPAANRPI IRALQLPSQL ALTGCDVADG ESGLKRLQTA LQVSQPPLIV LRAPDLAEQA IAYNRLAQSA LALCQSNGSE LMLHGVPELI DRHPQAAGVH LPWRHASQCQ QRPVAECYKL GVSCHNAEQL AHAASMGADY AILGHVLDTP SHPNEAPLGW YAFSQLVSAA RLPVYGIGGL SPADLPKARQ CGAQGIAGIG FWWA // ID A3JDT8_9ALTE Unreviewed; 220 AA. AC A3JDT8; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MELB17_20346; OS Marinobacter sp. ELB17. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=270374; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ELB17; RA Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXY01000007; EAZ99504.1; -; Genomic_DNA. DR ProteinModelPortal; A3JDT8; -. DR EnsemblBacteria; EAZ99504; EAZ99504; MELB17_20346. DR PATRIC; 31002073; VBIMarSp19762_2104. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22933 MW; ACE7975635562A06 CRC64; MGTLTLKPGL YAITDGHLTP GDTLIAAVEA ALEGGAVLVQ YREKHLPAAE QLRQASALQS ACSNAGVPLL INDNIELALR VQAAGVHLGQ GDTALADARR LLGEQAIIGI TCHADLALAQ AACEQGANYL AFGRFYPSTT KPNASAADTQ VLGLAKQFKL PVTAIGGITL GNAEPLIQAG ADLLAVAGGL FSTDMDATAK RAREFSRLFV QHRSQFFQSI // ID A3JSH2_9RHOB Unreviewed; 203 AA. AC A3JSH2; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-MAR-2014, entry version 33. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=RB2150_01919; OS Rhodobacteraceae bacterium HTCC2150. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=388401; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2150; RA Giovannoni S., Vergin K., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2150; RX PubMed=20889754; DOI=10.1128/JB.01088-10; RA Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.; RT "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned RT to the Roseobacter clade."; RL J. Bacteriol. 192:6315-6316(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXZ01000003; EBA03373.1; -; Genomic_DNA. DR ProteinModelPortal; A3JSH2; -. DR EnsemblBacteria; EBA03373; EBA03373; RB2150_01919. DR PATRIC; 28465099; VBIRhoBac104552_2103. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 203 AA; 21677 MW; 6D881D7F8B62FC43 CRC64; MSQENQPQLY LITPPEFELE SFSKQLQDVF AVMDVSCLRL ALSSQDADYV SRTADALREI CHAAEVAIVI EDHVNLVEAL GLDGVHLSDG ARSVGKVRRE LGTDAIIGAY CGASRHDGIS AAEASADYVA FGPITETPLG TGDVAEMDLF DWWSAMIEVP VVAEGGLSAE LVKGLSTKTD FYGVGMEIWE QADPAASLKA LLG // ID A3K256_9RHOB Unreviewed; 207 AA. AC A3K256; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 30. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=SSE37_05130; OS Sagittula stellata E-37. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sagittula. OX NCBI_TaxID=388399; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E-37; RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYA01000004; EBA09002.1; -; Genomic_DNA. DR ProteinModelPortal; A3K256; -. DR EnsemblBacteria; EBA09002; EBA09002; SSE37_05130. DR PATRIC; 29859148; VBISagSte54459_1866. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 207 AA; 21988 MW; 54BABB7DBE64F259 CRC64; MTQPETPQIY LVTPPEIELS RFPDALSRVL NGAGIACLRL SLATRDEDRL MRAADAVREI AHAADVALVI DTHVVLAERL GLDGVHLPDG ARGVRAARKT LGPDAIVGCH CGQSRHEGMT AGEAGADYVA FGPVGGALGD GAHAETELFQ WWSEVIEVPV VAEGGLDTDR IATLAPFTDF FAVGEEIWND EDPLAALKRL QSAMTPA // ID A3K894_9RHOB Unreviewed; 203 AA. AC A3K894; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSE37_09968; OS Sagittula stellata E-37. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sagittula. OX NCBI_TaxID=388399; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E-37; RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYA01000014; EBA06573.1; -; Genomic_DNA. DR ProteinModelPortal; A3K894; -. DR EnsemblBacteria; EBA06573; EBA06573; SSE37_09968. DR PATRIC; 29863533; VBISagSte54459_4043. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 20313 MW; 39CA4F9684C3E577 CRC64; MIPPLCFVTE ASAPAPVPDQ ATAAARGGAG WVQLRDKTSS DADLIPLAQR VIASLAPLGA RLIVNDRVDV AIAAGAYGLH IGQGDGDPAA IRARIGPDMF LGLSIEHADQ LAAVPKGVDY LGVGPVYATG SKPDHAAPIG LDGFAQIAAR TALPCLAIGG LTTRDAAALK ASGGAGMAVV SAISRAADMT GAARALCDSW RTA // ID A3KYN0_PSEAI Unreviewed; 209 AA. AC A3KYN0; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PACG_02889; OS Pseudomonas aeruginosa C3719. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=350704; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C3719; RX PubMed=18287045; DOI=10.1073/pnas.0711982105; RA Mathee K., Narasimhan G., Valdes C., Qiu X., Matewish J.M., RA Koehrsen M., Rokas A., Yandava C.N., Engels R., Zeng E., RA Olavarietta R., Doud M., Smith R.S., Montgomery P., White J.R., RA Godfrey P.A., Kodira C., Birren B., Galagan J.E., Lory S.; RT "Dynamics of Pseudomonas aeruginosa genome evolution."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3100-3105(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH482383; EAZ54311.1; -; Genomic_DNA. DR ProteinModelPortal; A3KYN0; -. DR SMR; A3KYN0; 24-200. DR EnsemblBacteria; EAZ54311; EAZ54311; PACG_02889. DR PATRIC; 25569278; VBIPseAer51129_3907. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22146 MW; 898DA261D0AFA265 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER HGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAQ LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID A3L4J8_PSEAI Unreviewed; 315 AA. AC A3L4J8; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 16-OCT-2013, entry version 42. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=PACG_05106; OS Pseudomonas aeruginosa C3719. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=350704; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C3719; RX PubMed=18287045; DOI=10.1073/pnas.0711982105; RA Mathee K., Narasimhan G., Valdes C., Qiu X., Matewish J.M., RA Koehrsen M., Rokas A., Yandava C.N., Engels R., Zeng E., RA Olavarietta R., Doud M., Smith R.S., Montgomery P., White J.R., RA Godfrey P.A., Kodira C., Birren B., Galagan J.E., Lory S.; RT "Dynamics of Pseudomonas aeruginosa genome evolution."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3100-3105(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH482383; EAZ56379.1; -; Genomic_DNA. DR ProteinModelPortal; A3L4J8; -. DR EnsemblBacteria; EAZ56379; EAZ56379; PACG_05106. DR PATRIC; 25574007; VBIPseAer51129_0988. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34041 MW; FBCE869C3EE6B47B CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EDGEPVRAAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEAHGAEGQ PLAWVEPREL ADYEFPAANA PIVQAARLPA HYLITPDGLE PGELISGVRK AVEAGIRLIQ LRAPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDADELAL AASMGVEFVT LSPVQPTESH PGEPALGWDK AAELIAGFNQ PVYLLGGLGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID A3LF72_PSEAI Unreviewed; 209 AA. AC A3LF72; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PA2G_03424; OS Pseudomonas aeruginosa 2192. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=350703; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2192; RX PubMed=18287045; DOI=10.1073/pnas.0711982105; RA Mathee K., Narasimhan G., Valdes C., Qiu X., Matewish J.M., RA Koehrsen M., Rokas A., Yandava C.N., Engels R., Zeng E., RA Olavarietta R., Doud M., Smith R.S., Montgomery P., White J.R., RA Godfrey P.A., Kodira C., Birren B., Galagan J.E., Lory S.; RT "Dynamics of Pseudomonas aeruginosa genome evolution."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3100-3105(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH482384; EAZ60103.1; -; Genomic_DNA. DR ProteinModelPortal; A3LF72; -. DR EnsemblBacteria; EAZ60103; EAZ60103; PA2G_03424. DR PATRIC; 25557132; VBIPseAer126331_3022. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22200 MW; 647D8D7222003226 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER YGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAR LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID A3LL99_PSEAI Unreviewed; 315 AA. AC A3LL99; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 47. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=PA2G_05661; OS Pseudomonas aeruginosa 2192. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=350703; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2192; RX PubMed=18287045; DOI=10.1073/pnas.0711982105; RA Mathee K., Narasimhan G., Valdes C., Qiu X., Matewish J.M., RA Koehrsen M., Rokas A., Yandava C.N., Engels R., Zeng E., RA Olavarietta R., Doud M., Smith R.S., Montgomery P., White J.R., RA Godfrey P.A., Kodira C., Birren B., Galagan J.E., Lory S.; RT "Dynamics of Pseudomonas aeruginosa genome evolution."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3100-3105(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH482384; EAZ62230.1; -; Genomic_DNA. DR ProteinModelPortal; A3LL99; -. DR SMR; A3LL99; 6-123, 127-313. DR EnsemblBacteria; EAZ62230; EAZ62230; PA2G_05661. DR PATRIC; 25561880; VBIPseAer126331_5728. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34055 MW; 9165F7469596B47A CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EDGEPVRAAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEAHGAEGQ PLAWVEPREL ADYEFPAANA PIVQAARLPA HYLITPDGLE PGELISGVRK AVEAGIRLIQ LRAPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDAEELAL AASMGVEFVT LSPVQPTESH PGEPALGWDK AAELIAGFNQ PVYLLGGLGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID A3LUC4_PICST Unreviewed; 533 AA. AC A3LUC4; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 2. DT 16-APR-2014, entry version 44. DE SubName: Full=Thiamin biosynthetic bifunctional enzyme; GN ORFNames=PICST_77822; OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / OS NRRL Y-11545) (Yeast) (Pichia stipitis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; OC Scheffersomyces. OX NCBI_TaxID=322104; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545; RX PubMed=17334359; DOI=10.1038/nbt1290; RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., RA Passoth V., Richardson P.M.; RT "Genome sequence of the lignocellulose-bioconverting and xylose- RT fermenting yeast Pichia stipitis."; RL Nat. Biotechnol. 25:319-326(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000498; ABN66215.2; -; Genomic_DNA. DR RefSeq; XP_001384244.2; XM_001384207.1. DR ProteinModelPortal; A3LUC4; -. DR STRING; 4924.PICST_77822; -. DR GeneID; 4838878; -. DR KEGG; pic:PICST_77822; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 533 AA; 57095 MW; E32BC9E1FD5F6A75 CRC64; MATDGQGKSA RAPNDNVDYS LYLVTDSTMI PESSTFIKQV QEAVDSGVTL VQLREKSLST LEFVKRAEEV HSITKKKGIP LIINDRIDVA LAIDAEGVHV GQDDMPAELA RKLLGPNKIL GVTCSNPEEV DVVVKQKVAD YVGLGTVYKT NTKKNVSDPE GTGPIGIRKM LRVLGDYNKE ADYKIKCVAI GGINHSNADK VLYQCQVTEQ KLDGVAVVSC IMASADARKA TLDLAKIIAS EPAFSITTRL SESNLDSFSK LQPLVHHITN NVVKNFSANV TLSIGASPIM SELAEEFDEL VGNAKHIALV LNLGTPSSDM MSVFKQAIQV YNKYGKHIIF DPVACGATKA RLECARILLN TGHVSVIKGN VGEIMSVWKL TTFYIAKSVG ESNTMRGVDS IFNLSEHILL ERARQVASEF KTVVVVTGKK NFTVSPTGIV RSCLGGSPLM GKITGTGCSL GSTIAAFLAA GADGELEQDS TCVFDAATIA VEMYNSAGKQ AAVSVSTPGS FSTKFLDHLS RGQDLIPTLF SRP // ID A3M715_ACIBT Unreviewed; 299 AA. AC A3M715; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 2. DT 14-MAY-2014, entry version 56. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=A1S_2286; OS Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=400667; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17978 / NCDC KC 755; RX PubMed=17344419; DOI=10.1101/gad.1510307; RA Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., RA Gerstein M., Snyder M.; RT "New insights into Acinetobacter baumannii pathogenesis revealed by RT high-density pyrosequencing and transposon mutagenesis."; RL Genes Dev. 21:601-614(2007). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000521; ABO12709.2; -; Genomic_DNA. DR ProteinModelPortal; A3M715; -. DR STRING; 400667.A1S_2286; -. DR EnsemblBacteria; ABO12709; ABO12709; A1S_2286. DR PATRIC; 20720862; VBIAciBau103176_2333. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ABAU400667:GI0Q-2274-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 299 AA; 34180 MW; A7E3C647A5E5F417 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLSSELK KQIKTVHLKQ SQLMSLHKGD LEVGIRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID A3M7I9_ACIBT Unreviewed; 203 AA. AC A3M7I9; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 60. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=A1S_2465; OS Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=400667; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17978 / NCDC KC 755; RX PubMed=17344419; DOI=10.1101/gad.1510307; RA Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., RA Gerstein M., Snyder M.; RT "New insights into Acinetobacter baumannii pathogenesis revealed by RT high-density pyrosequencing and transposon mutagenesis."; RL Genes Dev. 21:601-614(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000521; ABO12883.1; -; Genomic_DNA. DR RefSeq; YP_001085485.1; NC_009085.1. DR ProteinModelPortal; A3M7I9; -. DR STRING; 400667.A1S_2465; -. DR EnsemblBacteria; ABO12883; ABO12883; A1S_2465. DR GeneID; 4918230; -. DR KEGG; acb:A1S_2465; -. DR PATRIC; 20721227; VBIAciBau103176_2510. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ABAU400667:GI0Q-2453-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21750 MW; C30389D6687A22BE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKVD KADQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID A3MB88_BURM7 Unreviewed; 209 AA. AC A3MB88; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN OrderedLocusNames=BMA10247_A0319; OS Burkholderia mallei (strain NCTC 10247). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320389; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 10247; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000547; ABO02874.1; -; Genomic_DNA. DR RefSeq; YP_001077524.1; NC_009079.1. DR ProteinModelPortal; A3MB88; -. DR STRING; 320389.BMA10247_A0319; -. DR EnsemblBacteria; ABO02874; ABO02874; BMA10247_A0319. DR GeneID; 4889768; -. DR KEGG; bmn:BMA10247_A0319; -. DR PATRIC; 19138441; VBIBurMal96640_0300. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BMAL320389:GH97-3854-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID A3MPW2_BURM7 Unreviewed; 367 AA. AC A3MPW2; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=BMA10247_2777; OS Burkholderia mallei (strain NCTC 10247). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320389; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 10247; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000548; ABO04731.1; -; Genomic_DNA. DR RefSeq; YP_001082298.1; NC_009080.1. DR ProteinModelPortal; A3MPW2; -. DR STRING; 320389.BMA10247_2777; -. DR EnsemblBacteria; ABO04731; ABO04731; BMA10247_2777. DR GeneID; 4891463; -. DR KEGG; bmn:BMA10247_2777; -. DR PATRIC; 19147900; VBIBurMal96640_4982. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BMAL320389:GH97-2768-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 367 AA; 38315 MW; 3E9B351CCB7F5C2B CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGARAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID A3MZQ6_ACTP2 Unreviewed; 137 AA. AC A3MZQ6; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=APL_0540; OS Actinobacillus pleuropneumoniae serotype 5b (strain L20). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=416269; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L20; RX PubMed=18065534; DOI=10.1128/JB.01845-07; RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., RA Nash J.H.; RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20 RT (serotype 5b)."; RL J. Bacteriol. 190:1495-1496(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000569; ABN73642.1; -; Genomic_DNA. DR RefSeq; YP_001053247.1; NC_009053.1. DR ProteinModelPortal; A3MZQ6; -. DR STRING; 416269.APL_0540; -. DR EnsemblBacteria; ABN73642; ABN73642; APL_0540. DR GeneID; 4849688; -. DR KEGG; apl:APL_0540; -. DR PATRIC; 20745934; VBIActPle94089_0569. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; APLE416269:GHV7-549-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 137 AA; 14799 MW; 73E9F1F7B0C860AF CRC64; MDDNVALAIE IDADGVHVGQ KDMSPIMIRQ MTDKPLIIGL SNNTLEDLWR SEQMIEVDYC GLGPVFPTNS KEKHNPPIGL DFVKKAREAG IRKPIVSIGG VKAEHVATLK QNGVDGIAVI TAISLASDVS QAVKRLL // ID A3NEB1_BURP6 Unreviewed; 367 AA. AC A3NEB1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 55. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=BURPS668_3678; OS Burkholderia pseudomallei (strain 668). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320373; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=668; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000570; ABN84180.1; -; Genomic_DNA. DR RefSeq; YP_001060682.1; NC_009074.1. DR ProteinModelPortal; A3NEB1; -. DR STRING; 320373.BURPS668_3678; -. DR EnsemblBacteria; ABN84180; ABN84180; BURPS668_3678. DR GeneID; 4883104; -. DR KEGG; bpd:BURPS668_3678; -. DR PATRIC; 19252986; VBIBurPse82117_3418. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BPSE320373:GJ9C-3671-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 367 AA; 38287 MW; 3639BE8C7D3D38BA CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGAQAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID A3NMJ8_BURP6 Unreviewed; 209 AA. AC A3NMJ8; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=BURPS668_A2576; OS Burkholderia pseudomallei (strain 668). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320373; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=668; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000571; ABN86460.1; -; Genomic_DNA. DR RefSeq; YP_001063569.1; NC_009075.1. DR ProteinModelPortal; A3NMJ8; -. DR STRING; 320373.BURPS668_A2576; -. DR EnsemblBacteria; ABN86460; ABN86460; BURPS668_A2576. DR GeneID; 4885923; -. DR KEGG; bpd:BURPS668_A2576; -. DR PATRIC; 19258228; VBIBurPse82117_6016. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPSE320373:GJ9C-6495-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 209 AA; 21746 MW; EF2632A0C174B664 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR PQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID A3P045_BURP0 Unreviewed; 367 AA. AC A3P045; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 55. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=BURPS1106A_3736; OS Burkholderia pseudomallei (strain 1106a). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=357348; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1106a; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000572; ABN90474.1; -; Genomic_DNA. DR RefSeq; YP_001067966.1; NC_009076.1. DR ProteinModelPortal; A3P045; -. DR STRING; 357348.BURPS1106A_3736; -. DR EnsemblBacteria; ABN90474; ABN90474; BURPS1106A_3736. DR GeneID; 4900941; -. DR KEGG; bpl:BURPS1106A_3736; -. DR PATRIC; 19225775; VBIBurPse14980_3524. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BPSE357348:GHVF-3737-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 367 AA; 38266 MW; 130C8EEBCCFAAA13 CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PQPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAQIARL NAAGAQAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEVE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA ATDYREAIVA LQQNFGR // ID A3P5P2_BURP0 Unreviewed; 199 AA. AC A3P5P2; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 2. DT 14-MAY-2014, entry version 48. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BURPS1106A_A1618; OS Burkholderia pseudomallei (strain 1106a). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=357348; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1106a; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000573; ABN95326.2; -; Genomic_DNA. DR RefSeq; YP_001075652.2; NC_009078.1. DR ProteinModelPortal; A3P5P2; -. DR STRING; 357348.BURPS1106A_A1618; -. DR EnsemblBacteria; ABN95326; ABN95326; BURPS1106A_A1618. DR GeneID; 4904236; -. DR KEGG; bpl:BURPS1106A_A1618; -. DR PATRIC; 19229327; VBIBurPse14980_5280. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPSE357348:GHVF-5701-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 199 AA; 21380 MW; BAC4456E90187CCB CRC64; MNKSANLPSE YLITPEPPGD EALSDYLATL ERTLKAGISL VQLRAKAVTA PYYARLTEYA LACCRRYNAR LLVNAAPEVA LGLHTDGVHL TSTRLMTCST RPLPAGLLVS AACHDEDQVR HADSIGVDLI TISPVMPTAT HTTAEPLGWP RFRELATLTS VPVYALGGMS VDSLAEARNA GAYGIAAIRA FWESNVDRS // ID A3P811_BURP0 Unreviewed; 209 AA. AC A3P811; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN OrderedLocusNames=BURPS1106A_A2440; OS Burkholderia pseudomallei (strain 1106a). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=357348; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1106a; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000573; ABN93008.1; -; Genomic_DNA. DR RefSeq; YP_001076471.1; NC_009078.1. DR ProteinModelPortal; A3P811; -. DR STRING; 357348.BURPS1106A_A2440; -. DR EnsemblBacteria; ABN93008; ABN93008; BURPS1106A_A2440. DR GeneID; 4904383; -. DR KEGG; bpl:BURPS1106A_A2440; -. DR PATRIC; 19230812; VBIBurPse14980_6020. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPSE357348:GHVF-6522-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID A3PEA7_PROM0 Unreviewed; 351 AA. AC A3PEA7; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=P9301_14591; OS Prochlorococcus marinus (strain MIT 9301). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=167546; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9301; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., RA Steglich C., Church G.M., Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000576; ABO18082.1; -; Genomic_DNA. DR RefSeq; YP_001091683.1; NC_009091.1. DR ProteinModelPortal; A3PEA7; -. DR STRING; 167546.P9301_14591; -. DR EnsemblBacteria; ABO18082; ABO18082; P9301_14591. DR GeneID; 4911099; -. DR KEGG; pmg:P9301_14591; -. DR PATRIC; 22996429; VBIProMar103344_1393. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; NFNRARE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR167546:GH1Y-1495-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 128 Unknown (By similarity). FT REGION 129 351 Thiamine-phosphate synthase (By FT similarity). FT REGION 180 184 HMP-PP binding (By similarity). FT REGION 277 279 THZ-P binding (By similarity). FT METAL 213 213 Magnesium (By similarity). FT METAL 232 232 Magnesium (By similarity). FT BINDING 212 212 HMP-PP (By similarity). FT BINDING 251 251 HMP-PP (By similarity). FT BINDING 280 280 HMP-PP (By similarity). FT BINDING 307 307 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 351 AA; 40292 MW; 83CF9D1EB9C73C1D CRC64; MLNSNTTNTE DLRIYQIIDA NLDRAREGLR VLEDWARFGL GKEKYVEKIK NFRQILGKNH LEIYKLSRNH VEDKCKGLTH QEQINRKTSE QIISSNSARV QEALRVIEEF SRLQNHELSK IASEIRYEIY TIEIDLLSYS KFKKSEEILK ENDLYVITDQ KDNLLEIIEE ILIAGVRIIQ HRFKTGTDQD HLQEAIQIKN LCKRYNSLFI VNDRLDIALA SNADGIHLGK DDLDFKTARR LLGYSKIIGI SANNEIDISN ALKEGCDYIG IGPVFETATK KDKKPIGIEK IKTLTKDLDI PWFAIGGIKS NNISYLKSNG FKKVALVSQL MNSEDPKEDA MIILKKLSHE N // ID A3PM37_RHOS1 Unreviewed; 203 AA. AC A3PM37; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 55. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rsph17029_2301; OS Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=349101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17029 / ATH 2.4.9; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P., Mackenzie C., Choudhary M., RA Donohue T.J., Kaplan S.; RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC RT 17029."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000577; ABN77403.1; -; Genomic_DNA. DR RefSeq; YP_001044175.1; NC_009049.1. DR ProteinModelPortal; A3PM37; -. DR STRING; 349101.Rsph17029_2301; -. DR EnsemblBacteria; ABN77403; ABN77403; Rsph17029_2301. DR GeneID; 4896628; -. DR KEGG; rsh:Rsph17029_2301; -. DR PATRIC; 23172453; VBIRhoSph114483_2519. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RSPH349101:GHC8-2338-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 20314 MW; 7E48C76474FAF26D CRC64; MNLSLYFVTP DGAEGLEQLV AAAVRGGATL VQLRDKHRSD AELIPLARRL VAALDAQGVP LIVNDRIEVV LASGAAGLHV GQGDLGVAEA RRRIGPDRLL GLSVEAPEHL EALPLGIVDY VGAGPVRATA SKPDHAPPIG FEGLARLVAA APVPAVAIGG LGAGDAHAVK AAGAAGMAIV SAIGAAADPE AAARALALEW GRA // ID A3PQJ7_RHOS1 Unreviewed; 226 AA. AC A3PQJ7; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 43. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Rsph17029_3521; OS Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=349101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17029 / ATH 2.4.9; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P., Mackenzie C., Choudhary M., RA Donohue T.J., Kaplan S.; RT "Complete sequence of chromosome 2 of Rhodobacter sphaeroides ATCC RT 17029."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000578; ABN78613.1; -; Genomic_DNA. DR RefSeq; YP_001045385.1; NC_009050.1. DR ProteinModelPortal; A3PQJ7; -. DR STRING; 349101.Rsph17029_3521; -. DR EnsemblBacteria; ABN78613; ABN78613; Rsph17029_3521. DR GeneID; 4898317; -. DR KEGG; rsh:Rsph17029_3521; -. DR PATRIC; 23175015; VBIRhoSph114483_3782. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RSPH349101:GHC8-3576-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 226 AA; 24394 MW; ADC5FA9CEC5584E6 CRC64; MPFPSARPSA IGFAIRRRPI MAEVERPQLY LVTPPEIDLE IFPDRLAAVL DSTEVACLRL ALAGKDEDRI ARTGDALREV AHARDVALVI ENHVLMVERL GLDGVHLTDG ARLVRKLRKD LGPDAILGAF CGRTRHEGIN AAEAGADYVA FGPVGTTALG DGSLAEAELF GWWSEMIEVP VVAEGALTPE KVAELAPLTD FFAVGEEIWR EEDAAAALRR LLAPLG // ID A3QER3_SHELP Unreviewed; 581 AA. AC A3QER3; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 57. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=Shew_2095; OS Shewanella loihica (strain ATCC BAA-1088 / PV-4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=323850; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1088 / PV-4; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Romine M.F., Serres G., Fredrickson J., Tiedje J., Richardson P.; RT "Complete sequence of Shewanella loihica PV-4."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000606; ABO23961.1; -; Genomic_DNA. DR RefSeq; YP_001094220.1; NC_009092.1. DR ProteinModelPortal; A3QER3; -. DR STRING; 323850.Shew_2095; -. DR EnsemblBacteria; ABO23961; ABO23961; Shew_2095. DR GeneID; 4923631; -. DR KEGG; slo:Shew_2095; -. DR PATRIC; 23516057; VBISheLoi132094_2094. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SLOI323850:GHQJ-2172-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 581 AA; 61127 MW; B567AFCEFBA281A2 CRC64; MSAEKPIVWT IAGSDSGGGA GIQADLATMA DLDCHGCSVI TCVTAQNSVA VNGVEPVSEA ILLAQLDTLL VDLPPRAIKI GLLANQRQIN LVADWLATHM APLKTDDGQP IPIILDPVMV ASCGDALTGE SAVQASAQTK TKPKTKLKTK PKTELKTEPK HLAGLDFTPF AKLLTLVTPN ASEFGKLVGS EASSSDEMLA QASALSRRLV CNLLITGGDK GSLWYSDKAE DLFICNAVAH TSPLHQHTSF RLSGERVDNP NHHGSGCTLS SAIASFLAQG LVLHDAILLA KTYVGQGIAP AKALGAGAGP LARCGWPSGL VSLPRITELA GITSISSSDR ASSGSSILSF PRLSFPGLSF PRLKRPIGVY PVVDNLMHLE QVLAAGATTA QLRIKLEDDR QAASKQEEGA GAAALEAQIQ AAIALGRKYD AQVFINDHWQ LALKHGAFGI HLGQEDLFEA DLDRIAKAGI ALGVSSHGVF ELALASQLNP SYLALGHIFP TPTKSMPSNP QGLSRLARMV ALWTPDCPRV AIGGIDASRL EQVKATNVEA VAVVRAVTQA DSPGEAYKQL ARMWENAYVT Q // ID A3RP20_RALSL Unreviewed; 198 AA. AC A3RP20; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 34. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=RRSL_04785; OS Ralstonia solanacearum UW551. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=342110; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UW551; RX PubMed=16404955; DOI=10.1094/MPMI-19-0069; RA Gabriel D.W., Allen C., Schell M., Denny T.P., Greenberg J.T., RA Duan Y.P., Flores-Cruz Z., Huang Q., Clifford J.M., Presting G., RA Gonzalez E.T., Reddy J., Elphinstone J., Swanson J., Yao J., RA Mulholland V., Liu L., Farmerie W., Patnaikuni M., Balogh B., RA Norman D., Alvarez A., Castillo J.A., Jones J., Saddler G., RA Walunas T., Zhukov A., Mikhailova N.; RT "Identification of open reading frames unique to a select agent: RT Ralstonia solanacearum race 3 biovar 2."; RL Mol. Plant Microbe Interact. 19:69-79(2006). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAKL01000001; EAP74913.1; -; Genomic_DNA. DR ProteinModelPortal; A3RP20; -. DR EnsemblBacteria; EAP74913; EAP74913; RRSL_04785. DR PATRIC; 38538417; VBIRalSol34715_0199. DR OMA; SCHSEAD; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 198 AA; 21562 MW; 4B5720A83B29EF5F CRC64; MKDISLPDFY QITPEPVGSP HFETFFAELT DTLRSGIRLL QLRAKQLGPR EHLDVARRTL DLCRQSGAIL ILNGPIDMAL EVGCDGVHLS SDALMSLRSR PVPDTVLLSA ACHSAEQLEQ AASMAVDFVT LSPVLRTRTH PDADPLGWER FTELAQRARV PVFALGGMHP DMLAQAKRAG AWGVAAISAT WCHRSVGA // ID A3SB30_9RHOB Unreviewed; 206 AA. AC A3SB30; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 30. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=EE36_15832; OS Sulfitobacter sp. EE-36. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sulfitobacter. OX NCBI_TaxID=52598; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EE-36; RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALV01000002; EAP84494.1; -; Genomic_DNA. DR ProteinModelPortal; A3SB30; -. DR EnsemblBacteria; EAP84494; EAP84494; EE36_15832. DR PATRIC; 28307393; VBISulSp6348_1406. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22247 MW; E9553586892EE856 CRC64; MDTPEQPQLY LITPPELELS SFPDQLARVL DAHDVACVRL ALSTRDEDRV MRAADALRGV TDARDIALVI ADHTLLAERL GLDGVHLSDA ARSVRHARKT LGDDAIVGSF CNGSRHDGMA AGEAGADYIS FGPVNASLLD DGTHAEQDLF QWWSEVIEVP VVAEGGLNTD LIRTLTPVTD FFGIGDEIWT SETPQQALAD LIAAMK // ID A3SD69_9RHOB Unreviewed; 198 AA. AC A3SD69; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 32. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=EE36_13828; OS Sulfitobacter sp. EE-36. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sulfitobacter. OX NCBI_TaxID=52598; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EE-36; RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALV01000003; EAP84150.1; -; Genomic_DNA. DR ProteinModelPortal; A3SD69; -. DR EnsemblBacteria; EAP84150; EAP84150; EE36_13828. DR PATRIC; 28306581; VBISulSp6348_2826. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 198 AA; 22003 MW; D3009D0ECB0D3E13 CRC64; MTLDRFYPIF DSAAWLERLV PLGIKLVQLR IKDMPAPALR RDIRQAKALC AKHDCTLVIN DHWRIALDEG CDFIHLGQED LDSADLNAIR NAGARLGIST HDKVELTRAL DLRPDYIALG PIYPTILKQM KWHAQGLDRL RDWRERVGQT PLVAIGGMSV DRAAGAFDAG ADCVAAVTDI TLNPSPEDRV TAWLGATR // ID A3SPL1_9RHOB Unreviewed; 206 AA. AC A3SPL1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 31. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=ISM_16085; OS Roseovarius nubinhibens ISM. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=89187; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ISM; RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALY01000002; EAP76401.1; -; Genomic_DNA. DR ProteinModelPortal; A3SPL1; -. DR EnsemblBacteria; EAP76401; EAP76401; ISM_16085. DR PATRIC; 28132014; VBIRosNub115512_3218. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 21877 MW; 6DCB5D3BF5864184 CRC64; MAEPDTPKLY LITPAEIELS RFPDQLAAAL DAHETACLRL ALASHDEDRI ARVADACREV TLPRDVALVI DNHVMLVERL GLDGVHLTDG TRSVRSARKT LGPDAIVGAF CGTSRHDGMS AGEAGADYIS FGPAGVTSLG DGAQAEHELF DWWSQMIEVP VVAEGALDAE RIAALAPVTD FFAIGDEIWA SDDPLAELSR LAAAMG // ID A3SR16_9RHOB Unreviewed; 203 AA. AC A3SR16; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=ISM_10641; OS Roseovarius nubinhibens ISM. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=89187; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ISM; RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALY01000003; EAP75575.1; -; Genomic_DNA. DR ProteinModelPortal; A3SR16; -. DR EnsemblBacteria; EAP75575; EAP75575; ISM_10641. DR PATRIC; 28129791; VBIRosNub115512_2123. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22220 MW; 439AD8CD09F5D889 CRC64; MDRFYLIVSD VLWLRALVPL GVRLVQLRIK DRDAAETRAQ IRAAREVCAA HNCQLVVNDY WQIALEEGCD FVHLGQEDMD SADFTALRRA GVRFGLSTHD ETELDRALDK GPAYVALGPV YPTLLKKMKW GPQGLDRVRD WKARAGKVPL VAIGGLTPER LPGVFAAGAD SAAVVTDIQR AADPLARTAE WIAACDAADL TPA // ID A3SWF9_9RHOB Unreviewed; 206 AA. AC A3SWF9; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 30. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=NAS141_05963; OS Sulfitobacter sp. NAS-14.1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sulfitobacter. OX NCBI_TaxID=314267; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAS-14.1; RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALZ01000003; EAP80860.1; -; Genomic_DNA. DR ProteinModelPortal; A3SWF9; -. DR EnsemblBacteria; EAP80860; EAP80860; NAS141_05963. DR PATRIC; 28308590; VBISulSp100835_0213. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22217 MW; F4E3EEF6892EE856 CRC64; MDTPEQPQLY LITPPELELS SFPDQLARVL DAHDVACVRL ALSTRDEDRV MRAADALRGV TDARDIALVI ADHTLLAERL GLDGVHLSDA ARSVRHARKT LGDDAIVGSF CNGSRHDGMA AGEAGADYIS FGPVNASLLD DGTHAEQDLF QWWSEVIEVP VVAEGGLNTD LIRALTPVTD FFGIGDEIWT SETPQQALAD LIAAMK // ID A3SYB0_9RHOB Unreviewed; 198 AA. AC A3SYB0; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 32. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=NAS141_18869; OS Sulfitobacter sp. NAS-14.1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sulfitobacter. OX NCBI_TaxID=314267; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAS-14.1; RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALZ01000004; EAP80605.1; -; Genomic_DNA. DR ProteinModelPortal; A3SYB0; -. DR EnsemblBacteria; EAP80605; EAP80605; NAS141_18869. DR PATRIC; 28313810; VBISulSp100835_2781. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 198 AA; 21929 MW; 060E6FC758E06237 CRC64; MTLDRFYPIF DSAAWLERLV PLGIKLVQLR IKDTPAPALR RDIRQAKAIC AKHDSTLVIN DHWQIALDEG CDFIHLGQED LDSADLTAIR DAGVRLGIST HDKAELIRAL DLRPDYIALG PIYPTILKQM KWHAQGLDRL RDWRERVGQT PLVAIGGMSV DRAAGAFDAG ADCVAAVTDI TLNPSPEDRV TAWLGATR // ID A3TXE3_9RHOB Unreviewed; 198 AA. AC A3TXE3; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 33. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=OB2597_02747; OS Oceanicola batsensis HTCC2597. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Oceanicola. OX NCBI_TaxID=252305; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2597; RX PubMed=20418400; DOI=10.1128/JB.00412-10; RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.; RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola RT batsensis HTCC2597(TDelta)."; RL J. Bacteriol. 192:3549-3550(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMO01000004; EAQ03503.1; -; Genomic_DNA. DR ProteinModelPortal; A3TXE3; -. DR EnsemblBacteria; EAQ03503; EAQ03503; OB2597_02747. DR PATRIC; 28490883; VBIOceBat2886_2268. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 198 AA; 22031 MW; 7318AB0546CB6F53 CRC64; MTLDRFYPIF DNVAWLERTL PLGVKLVQLR IKTLSASDLR PAVARARALC RSHGAVLVVN DHWQTAIDED CDWIHLGQED LDEADLPAIR RAGLKIGIST HDHAELDRAL SLTPDYVALG PVYPTILKKM KWERQGLERV TEWKRLIGAL PLVAIGGMNV DRAAGAFAAG ADIVSAVTDI TLHDDPEARV RQWIEATR // ID A3TXH3_9RHOB Unreviewed; 204 AA. AC A3TXH3; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 33. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=OB2597_02897; OS Oceanicola batsensis HTCC2597. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Oceanicola. OX NCBI_TaxID=252305; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2597; RX PubMed=20418400; DOI=10.1128/JB.00412-10; RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.; RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola RT batsensis HTCC2597(TDelta)."; RL J. Bacteriol. 192:3549-3550(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMO01000004; EAQ03533.1; -; Genomic_DNA. DR ProteinModelPortal; A3TXH3; -. DR EnsemblBacteria; EAQ03533; EAQ03533; OB2597_02897. DR PATRIC; 28490941; VBIOceBat2886_2296. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 204 AA; 21625 MW; 3C4A635720124B51 CRC64; MADTEQPQLY LISPPDFDLS GFAETLGRVL DGAEVACVRL ALASHDEGEI ARAADTLRDV CHQRDVAIVI DNHILLAERH GLDGVHLTDG ARSVRKARKQ LGPDAIVGSY CGTSRHDGMT AGESGADYVS FGPVGASSLA AGETAEIEIF DWWSQMIELP VVAEGGMTPE LIAQLRPVTD FFGIGTEIWA EDDPAAGLAA LLSP // ID A3U008_9RHOB Unreviewed; 201 AA. AC A3U008; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=OB2597_18022; OS Oceanicola batsensis HTCC2597. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Oceanicola. OX NCBI_TaxID=252305; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2597; RX PubMed=20418400; DOI=10.1128/JB.00412-10; RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.; RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola RT batsensis HTCC2597(TDelta)."; RL J. Bacteriol. 192:3549-3550(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMO01000007; EAQ02639.1; -; Genomic_DNA. DR ProteinModelPortal; A3U008; -. DR EnsemblBacteria; EAQ02639; EAQ02639; OB2597_18022. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 125 127 THZ-P binding (By similarity). FT REGION 176 177 THZ-P binding (By similarity). FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 156 156 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 201 AA; 19745 MW; B31DAF9BD0F1D4BC CRC64; MLDPGLCAGV GIVETARAAV AGGAMVVQLR DKMADTARMI ETGLALKAVL AGTGAALIVN DDVEAAVAIG ADGLHIGQGD MAVAEARARI GAGMVLGLSV ETPALAASVD AGQVDYIGAG PVFATLSKLD HKTPVGFEGL AAQVAASPVP AVAIGGLKAQ HVGAVLKTGA RGVAVVSAIC GQPDPEVAAR ALRQEIDALG R // ID A3U9P4_CROAH Unreviewed; 208 AA. AC A3U9P4; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CA2559_10858; OS Croceibacter atlanticus (strain ATCC BAA-628 / HTCC2559 / KCTC 12090). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Croceibacter. OX NCBI_TaxID=216432; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-628 / HTCC2559 / KCTC 12090; RX PubMed=20639333; DOI=10.1128/JB.00733-10; RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.; RT "Complete genome sequence of Croceibacter atlanticus HTCC2559T."; RL J. Bacteriol. 192:4796-4797(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002046; EAP86530.1; -; Genomic_DNA. DR RefSeq; YP_003716913.1; NC_014230.1. DR ProteinModelPortal; A3U9P4; -. DR EnsemblBacteria; EAP86530; EAP86530; CA2559_10858. DR GeneID; 9297659; -. DR KEGG; cat:CA2559_10858; -. DR PATRIC; 38159903; VBICroAtl46233_2142. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; CATL216432:GHTE-2185-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22347 MW; EDEB2DAB7279CC90 CRC64; MNNATLSLMY VTDDSITNDI KFFEILEAAL IGGASCIQLR EKTCDTKTFY NRALQAKSLC EIYKVPLIIN DRVDIALAVN ADGVHLGQTD MPFKVARNLL GSTKIIGLSV SNVSQAIQAQ TASEIDYIGV SPIFATQTKT RDLDAPLGIA GLIKICEVYK KPIVCIGGIH IYNATEIIKN GATGIAVVSA ISKAENPEIA TKTLKTKV // ID A3UH95_9RHOB Unreviewed; 203 AA. AC A3UH95; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-MAR-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=OA2633_08129; OS Oceanicaulis sp. HTCC2633. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Oceanicaulis. OX NCBI_TaxID=314254; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2633; RX PubMed=21036991; DOI=10.1128/JB.01267-10; RA Oh H.M., Kang I., Vergin K.L., Lee K., Giovannoni S.J., Cho J.C.; RT "Genome sequence of Oceanicaulis sp. strain HTCC2633, isolated from RT the Western Sargasso Sea."; RL J. Bacteriol. 193:317-318(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMQ01000003; EAP90166.1; -; Genomic_DNA. DR ProteinModelPortal; A3UH95; -. DR EnsemblBacteria; EAP90166; EAP90166; OA2633_08129. DR PATRIC; 25535396; VBIOceAle934_2437. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21403 MW; 781D165FEC4FDDAF CRC64; MAELYLLTPP KIDADFADVL ARTLDAGRVS ALQLRLKDQG QDEIEALAPR LIEIAHQRGV SVIMNDDPVL AAKLGCDGVH IGQEDGSIKQ ARAAVGPKGI VGVTCHDSRH LAMLAGEQGA DYVAFGAFFD TATKSPKTRA DLDILVWWTE LFELPCVAIG GITLENASEV IAAGADYIAV CGGVWSHPEG PEAACAGLSQ LLD // ID A3UIE3_9RHOB Unreviewed; 178 AA. AC A3UIE3; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-MAR-2014, entry version 32. DE SubName: Full=Uncharacterized protein; GN ORFNames=OA2633_10129; OS Oceanicaulis sp. HTCC2633. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Oceanicaulis. OX NCBI_TaxID=314254; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2633; RX PubMed=21036991; DOI=10.1128/JB.01267-10; RA Oh H.M., Kang I., Vergin K.L., Lee K., Giovannoni S.J., Cho J.C.; RT "Genome sequence of Oceanicaulis sp. strain HTCC2633, isolated from RT the Western Sargasso Sea."; RL J. Bacteriol. 193:317-318(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMQ01000004; EAP89616.1; -; Genomic_DNA. DR ProteinModelPortal; A3UIE3; -. DR EnsemblBacteria; EAP89616; EAP89616; OA2633_10129. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 178 AA; 18775 MW; 9ED73FCED7646F18 CRC64; MPALFCLSDP DRTPDLMALA HALPAGVGLI LRTFGKPEIR QQADDVVRLR HQAGGMCLIS ADPDLARQAG ADGVHWPERL LTGANVRRTQ GLVSTSAHSP QALRRAGRLA DLAFVSTVFP SHSPSATRPM GPFRLAAHAA RSTLPVYALG GMTSRTIRRL ENLGISGAGA VGALTVSR // ID A3UKX5_VIBSP Unreviewed; 205 AA. AC A3UKX5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=V12B01_15866; OS Vibrio splendidus 12B01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=314291; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=12B01; RA Polz M., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMR01000001; EAP96610.1; -; Genomic_DNA. DR ProteinModelPortal; A3UKX5; -. DR EnsemblBacteria; EAP96610; EAP96610; V12B01_15866. DR PATRIC; 25651397; VBIVibSpl92012_0335. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22104 MW; CA11AF1FD9032403 CRC64; MNPYKLYLVT DDQQDLETLK FVVEQAVAGG VTMVQVREKH GDVRAFIERA QAVKSILVGS GVPLIINDRV DVALAVDADG LHLGQSDMPA ELARQLIGPD KILGLSIETE QQLQEADSLP IDYIGLSALF TTPTKTNLKK HWGYEGIQMA LETTKLPIVG IGGINESNIP QLVKTGIHGL ALVSAICHAE SPKQATQDLL SLMGE // ID A3UY00_VIBSP Unreviewed; 430 AA. AC A3UY00; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=V12B01_06447; OS Vibrio splendidus 12B01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=314291; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=12B01; RA Polz M., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMR01000046; EAP92632.1; -; Genomic_DNA. DR ProteinModelPortal; A3UY00; -. DR EnsemblBacteria; EAP92632; EAP92632; V12B01_06447. DR PATRIC; 25659426; VBIVibSpl92012_4692. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 430 AA; 47362 MW; ED20ED75EC447676 CRC64; MTVKVLIPSQ NIELTGEVQN CLLVANRQGL ATDAVELGVS PTQYFSIVDS QQALSIGFAH DLDSLTVCQL AELNHVVDYS NSVALADVCD AFTQTPNTIY IGVSDDSAVL DIWSHLDASR VIKNDTTAHQ ELDHHAHFAW LLTLLALEFP LEDALVLARA ASNVSRGTWP AHYQNFPIPV LEDQRLDISV GWANQGTSLS FPELSKSSLG LYPVVDDVEW IERLLKLGIN TVQLRIKNPQ QTDLELQVAR SIELGREYNA QVFINDYWQL ALKHDAFGVH LGQEDIEESN LSQLSLAGIK IGLSTHGYYE LLRIVQINPS YIALGHIFPT TTKQMPSKPQ GLVRLSLYQQ LIDTIPYTEQ LTGYPTVAIG GIDQSTAAQV WSCGVSSLAV VRAITLAEDP KQVIEFFEAL MADSSTSAVK EVTRELSHAE // ID A3V5X4_9RHOB Unreviewed; 208 AA. AC A3V5X4; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 29. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=SKA53_04403; OS Loktanella vestfoldensis SKA53. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Loktanella. OX NCBI_TaxID=314232; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SKA53; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMS01000005; EAQ06298.1; -; Genomic_DNA. DR ProteinModelPortal; A3V5X4; -. DR EnsemblBacteria; EAQ06298; EAQ06298; SKA53_04403. DR PATRIC; 30245271; VBILokVes90427_2133. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 208 AA; 22119 MW; 3DE796BD6DF595A6 CRC64; MSDAADTPQI YLITPSDFDL TSFPDRLAAC LDSNDIGCVR LALATKDDSK IARAADALRA VTHARDVALV IESHVLMVDR LGLDGVHLLD AARSVNKIRK DLGDDAIIGA FCGNSRHDGM TAGELGADYV SFGPVGASAL GDGRTADLEL FTWWSEMIEV PVVAEGALDA ALIRLLTPHT DFFGFGDEIW REDDAAAALG TLLKAMTS // ID A3VKD6_9RHOB Unreviewed; 206 AA. AC A3VKD6; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 16-OCT-2013, entry version 30. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=RB2654_04506; OS Maritimibacter alkaliphilus HTCC2654. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Maritimibacter. OX NCBI_TaxID=314271; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2654; RX PubMed=20729358; DOI=10.1128/JB.00873-10; RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L., RA Giovannoni S.J.; RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and RT Maritimibacter alkaliphilus HTCC2654T, the type strains of two marine RT Roseobacter genera."; RL J. Bacteriol. 192:5552-5553(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMT01000017; EAQ11260.1; -; Genomic_DNA. DR ProteinModelPortal; A3VKD6; -. DR EnsemblBacteria; EAQ11260; EAQ11260; RB2654_04506. DR PATRIC; 28474288; VBIRhoBac6565_3751. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22266 MW; BD26AFC7C30E6134 CRC64; MAETDLPQLY LVTPPQFELS SFPDQLARAL DAVEIACLRL ELATRDEDTI ARAADACREV AHARDIAIVI ADHVLMVERL GLDGVHFTDG SRQVRKTRKD LGKDAIVGAF CGTSRHDGMT AGEQDADYVA FGPVGTSNLG TGEIAGRDLF QWWTEMIEVP IVAEGGLTEA LVRDFAPVTD FFSFGEEIWT AEDPTAALTA LAAARA // ID A3VW94_9RHOB Unreviewed; 206 AA. AC A3VW94; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 30. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=ROS217_19397; OS Roseovarius sp. 217. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=314264; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=217; RA Murrell J.C., Schafer H., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMV01000001; EAQ26724.1; -; Genomic_DNA. DR ProteinModelPortal; A3VW94; -. DR EnsemblBacteria; EAQ26724; EAQ26724; ROS217_19397. DR PATRIC; 28139021; VBIRosSp94902_1885. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 21961 MW; 0619734D38CB07A0 CRC64; MAETEQPQIY LITPPDFELS VFPDTLARVL DSHPVACVRL GLATRDEDRI ARAADACREV THARDVALVI DSHLMLVEPH GLDGVHLPDA ARSVRAARKA LGEDAIVGSF CGTSRHDGMS AGEAGADYIS FGPIGATALD TGACVDLDVF DWWSKVIELP VVAEGALNEA LVAQLAPMTD FFAFGDEIWR DEDAAAALGR FIAAMG // ID A3W4X7_9RHOB Unreviewed; 198 AA. AC A3W4X7; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 33. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=ROS217_09285; OS Roseovarius sp. 217. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=314264; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=217; RA Murrell J.C., Schafer H., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMV01000009; EAQ24433.1; -; Genomic_DNA. DR ProteinModelPortal; A3W4X7; -. DR EnsemblBacteria; EAQ24433; EAQ24433; ROS217_09285. DR PATRIC; 28134963; VBIRosSp94902_3654. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 198 AA; 21665 MW; 2B97570433806D30 CRC64; MTLPRFYPIF DHADWLHRLL PLGVGLVQLR IKDVPNGMLK QQIALAQGLC RAHGAILVVN DHWQAAIDAG CTWVHLGQED LDTADIPALR RAGIKIGLST HDHAELDRAL SYAPDYVALG PVYPTILKKM KWHEQGLGKL TEWKHLIGDI PLIAIGGMSV ERAQGALSAG ADVVSAVTDI TLNPDPEARV RQWLDVTG // ID A3WCR8_9SPHN Unreviewed; 211 AA. AC A3WCR8; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NAP1_04485; OS Erythrobacter sp. NAP1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=237727; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAP1; RA Falkowski P., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAP1; RX PubMed=21952547; DOI=10.1128/JB.05845-11; RA Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S., RA Falkowski P.G.; RT "Genome Sequence of the Marine Photoheterotrophic Bacterium RT Erythrobacter sp. Strain NAP1."; RL J. Bacteriol. 193:5881-5882(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMW01000001; EAQ30003.1; -; Genomic_DNA. DR ProteinModelPortal; A3WCR8; -. DR EnsemblBacteria; EAQ30003; EAQ30003; NAP1_04485. DR PATRIC; 30314476; VBIErySp29781_0894. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22546 MW; B0B798796CC132BB CRC64; MTDPTTQLYL ISPSQVDGDF PDRLERALDA GEGLVTAFQF RVKGVDQHEA ARLAEPLMAI CARHEVAFIV NDSVPLAKRL KADGVHLGQD DGDPKEAREV LGRDAQIGVT CHASKHLAME AGEAGADYVA FGAFFESMTK DKGDAERPTP DTIEWWVKLF EIPVVAIGGI TPENCAPLVR AGADFLAVSG GVWNGDEAAA VKAFAEAIEK A // ID A3WH55_9SPHN Unreviewed; 176 AA. AC A3WH55; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 16-OCT-2013, entry version 30. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=NAP1_14223; OS Erythrobacter sp. NAP1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=237727; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAP1; RA Falkowski P., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAP1; RX PubMed=21952547; DOI=10.1128/JB.05845-11; RA Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S., RA Falkowski P.G.; RT "Genome Sequence of the Marine Photoheterotrophic Bacterium RT Erythrobacter sp. Strain NAP1."; RL J. Bacteriol. 193:5881-5882(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMW01000002; EAQ28762.1; -; Genomic_DNA. DR ProteinModelPortal; A3WH55; -. DR EnsemblBacteria; EAQ28762; EAQ28762; NAP1_14223. DR PATRIC; 30318386; VBIErySp29781_2829. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 176 AA; 19165 MW; 00466B7F879DD771 CRC64; MAHIKPLPEL WLISDARNDA VLEDAIARLP KGSGFVFRHY HLWPDERATR FAALLPMLRD GGHWAIVSDS VSTAEEWGAD GVYGALDAIP TSDLRWIATA HNEGEIVDAN RYGADAVMLS PVFPTRSHPG GDTLGVDRFR QLAALSKVPV IALGGMNTSR AEQLGWPRWA AIDGLS // ID A3WTN1_9BRAD Unreviewed; 233 AA. AC A3WTN1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 31. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=NB311A_15697; OS Nitrobacter sp. Nb-311A. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=314253; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Nb-311A; RA Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMY01000003; EAQ36725.1; -; Genomic_DNA. DR ProteinModelPortal; A3WTN1; -. DR EnsemblBacteria; EAQ36725; EAQ36725; NB311A_15697. DR PATRIC; 25477762; VBINitSp102674_0812. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 233 AA; 23890 MW; CBD599B53E3E1AE9 CRC64; MLAKSASLRP APRLYLATPV ICDPTGIMTP LADALASADI AAVLMRLALS DPRTMISRIK ALAPLIQNSG AALLLDGHAD LVARSGADGA HLASIEALQE AMPALKPDRI VGAGGLPTRH DSMVAGETGA DYVLFGEPDK TGDRPSAEAI ADRLAWWAEL FEPPCVAHAA NLDEAQLFAA SGADFVLVGD IIWNDPRGAA AALADIATAI GQGYGPQGGA QRANHPHGVR GAG // ID A3WY76_9BRAD Unreviewed; 202 AA. AC A3WY76; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NB311A_14230; OS Nitrobacter sp. Nb-311A. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=314253; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Nb-311A; RA Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMY01000014; EAQ35060.1; -; Genomic_DNA. DR ProteinModelPortal; A3WY76; -. DR EnsemblBacteria; EAQ35060; EAQ35060; NB311A_14230. DR PATRIC; 25477135; VBINitSp102674_0500. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 29 33 HMP-PP binding (By similarity). FT REGION 178 179 THZ-P binding (By similarity). FT METAL 62 62 Magnesium (By similarity). FT METAL 81 81 Magnesium (By similarity). FT BINDING 61 61 HMP-PP (By similarity). FT BINDING 100 100 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 202 AA; 21895 MW; 1F907E6DCDB6AF92 CRC64; MPYPDRFYPV IDTLDWVRRL IGLGVGTVQL RLKDLNDGEA LQLVSDALEI VKGTQTRLVV NDYWRAAIVA GAKHVHLGQE DLAAADVHEI RKAGLTLGLS THDDAELDSA LAAEPDYIAL GPIFPTTLKA MRFAPQGIPK ITEWKRRVGN IPLVAIGGIK LEQAAEIFAA GADSIAVVSD VTQNPDPDAR VKAWLEQVTE TA // ID A3X8R2_9RHOB Unreviewed; 196 AA. AC A3X8R2; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=MED193_07748; OS Roseobacter sp. MED193. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=314262; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED193; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANB01000004; EAQ45529.1; -; Genomic_DNA. DR ProteinModelPortal; A3X8R2; -. DR EnsemblBacteria; EAQ45529; EAQ45529; MED193_07748. DR PATRIC; 28110582; VBIRosSp92751_3038. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 196 AA; 21628 MW; E000BE440B5A8245 CRC64; MERFYLIVGH VGRLELLVPQ GAKLVQLRIK DEPEAELRRQ IARARDFCAV HGAQLVVNDH WQLALDLNCN FVHLGQEDME TADFAALRRA GIRFGLSTHD EAELERALSH DPAYVALGPV YPTLLKKMKW DPQGLDRVSR WKGLAGNTPL VAIGGLTPER LPGVFAAGAD SAAVVTDIQL ADDPEARCRQ WAEACA // ID A3XAU9_9RHOB Unreviewed; 210 AA. AC A3XAU9; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 31. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=MED193_04461; OS Roseobacter sp. MED193. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=314262; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED193; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANB01000006; EAQ45052.1; -; Genomic_DNA. DR ProteinModelPortal; A3XAU9; -. DR EnsemblBacteria; EAQ45052; EAQ45052; MED193_04461. DR PATRIC; 28109352; VBIRosSp92751_2430. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 210 AA; 22540 MW; 2ADBA79D55E75C01 CRC64; MDNAAEAPEA PQIYLISPPS FELGRYPDML ARVLDSTEIS CLRLNMASRD EDTLSRAGDA LREVCHARDV AIVISDHQIL AERLGLDGVH LNDASKSVRT ARKALGPDAI VGSFCGASRH DGISAGEAGA DYVSFGPVGT SGLGDGAVAE TELFEWWSQM IEVPVVAEGG LTEDLIRTVA PFTDFFGLGE EIWNTEDPVA TLNRFMAAMR // ID A3XJN1_LEEBM Unreviewed; 220 AA. AC A3XJN1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MED217_04397; OS Leeuwenhoekiella blandensis (strain CECT 7118 / CCUG 51940 / MED217) OS (Flavobacterium sp. (strain MED217)). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Leeuwenhoekiella. OX NCBI_TaxID=398720; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MED217; RX PubMed=17215843; DOI=10.1038/nature05381; RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., RA Pascher T., Neutze R., Pedros-Alio C., Pinhassi J.; RT "Light stimulates growth of proteorhodopsin-containing marine RT Flavobacteria."; RL Nature 445:210-213(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANC01000002; EAQ50241.1; -; Genomic_DNA. DR ProteinModelPortal; A3XJN1; -. DR EnsemblBacteria; EAQ50241; EAQ50241; MED217_04397. DR PATRIC; 29226354; VBILeeBla91056_2398. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). SQ SEQUENCE 220 AA; 24371 MW; 3C4ABAA91A9EF990 CRC64; MEKPFPYQLY LVISEEACLG RNFLEVAEAA VQGGVDLVQL REKNDTPQAF LNKAFELKEL LDRYEVPLII NDNLEIATQC KAAGIHVGNS DMPPTTIRKS WESCRLLGYS IEYLEQLYNE QTYTSDYLGI SPVFSTSTKT DTVTTWGFDG VRKVRSITQK PLVAIGNMNA SNARQVVEAG ADCIAVVSAI CAAPKPKNAA QLLRKEIQKG LKNRANLLNL // ID A3XVX5_9VIBR Unreviewed; 205 AA. AC A3XVX5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MED222_04055; OS Vibrio sp. MED222. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=314290; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED222; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAND01000004; EAQ54628.1; -; Genomic_DNA. DR ProteinModelPortal; A3XVX5; -. DR EnsemblBacteria; EAQ54628; EAQ54628; MED222_04055. DR PATRIC; 28406405; VBIVibSp50596_0111. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22121 MW; D5A73C6F9CF08735 CRC64; MNPYKLYLVT DDQQDLETLK FVVEQAIAGG VTMVQVREKH GDVRAFIERA QAVKSILAGS GVPMIINDRV DVTLAVDADG LHLGQSDMPA ELARQLIGPD KILGLSIETE QQLREADSLP IDYIGLSALF ATPTKTNLKK HWGYDGIKMA LETTKLPIVG IGGINESNIP QLVESGIHGL ALVSAICHAE DPKQATQDLL ALMGE // ID A3Y344_9VIBR Unreviewed; 430 AA. AC A3Y344; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=MED222_19096; OS Vibrio sp. MED222. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=314290; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED222; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAND01000037; EAQ52102.1; -; Genomic_DNA. DR ProteinModelPortal; A3Y344; -. DR EnsemblBacteria; EAQ52102; EAQ52102; MED222_19096. DR PATRIC; 28413048; VBIVibSp50596_3035. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 430 AA; 47629 MW; 4F3DCF754F3AEAF3 CRC64; MTVKILTPSQ NIELTGEVQN CLLVAKRQGL ATDAVELGVS PTQYFSIVDS QQALSIGFAH DLDSLTVCQL AELNHVVDYS NSVALADVCD AFTQTPNTIY IGVSDDSAVL DIWSHRDANR AIKSETTAHQ ELDNRGHFAW LLTLLALEFP LEDALVLARA SSNVSRGTWP AHYQNFPIPA LEDQRLNISV GWANQGTVLS FPELGKNSLG LYPVVDDVEW IERLLKLGIN TVQLRIKNPQ QVDLEQQVAR SIELGREHNA QVFINDYWQL ALKHDAFGVH LGQEDIEESN LSQLSQAGIK IGLSTHGYYE LLRIVQINPS YIALGHIFPT TTKQMPSKPQ GLVRLSLYQQ LIDTIPYTDQ LTGYPTVAIG GIDQSTAEQV WECGVSSLAV VRAITLAEDP QKVIEFFEKL MAPKSPTLKE EVIQEPSYAE // ID A3YAF0_9GAMM Unreviewed; 203 AA. AC A3YAF0; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=MED121_01595; OS Marinomonas sp. MED121. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=314277; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED121; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANE01000004; EAQ65864.1; -; Genomic_DNA. DR ProteinModelPortal; A3YAF0; -. DR EnsemblBacteria; EAQ65864; EAQ65864; MED121_01595. DR PATRIC; 28820246; VBIMarSp20187_3353. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22920 MW; 3CD66B4AAC4416CB CRC64; MSSAMTQLDR FYPIFDSYDW LERLVPLGIK LVQLRIKDES QERIKAQIVE AKALCYQYDC QLVINDYWQL AIELGCDYVH LGQEDLDVAD IEAIKSAGIK LGISTHCEEE LERALALNPD YIALGPVYPT ILKKMKWHQQ GVEKLTLWKA QIGQIPLIAI GGMTIERSKG AFEAKADSVA AVTDITLNQN PERQVQAWLA ATR // ID A3YMG0_CAMJU Unreviewed; 210 AA. AC A3YMG0; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CJJCF936_1169; OS Campylobacter jejuni subsp. jejuni CF93-6. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360111; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CF93-6; RA Fouts D., Nelson K.; RT "Sequence of Campylobacter jejuni subsp. jejuni CF93-6."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANJ01000007; EAQ56378.1; -; Genomic_DNA. DR ProteinModelPortal; A3YMG0; -. DR EnsemblBacteria; EAQ56378; EAQ56378; CJJCF936_1169. DR PATRIC; 27751533; VBICamJej28969_1494. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID A3YMY6_CAMJU Unreviewed; 201 AA. AC A3YMY6; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=CJJCF936_1126; OS Campylobacter jejuni subsp. jejuni CF93-6. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360111; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CF93-6; RA Fouts D., Nelson K.; RT "Sequence of Campylobacter jejuni subsp. jejuni CF93-6."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANJ01000008; EAQ56302.1; -; Genomic_DNA. DR ProteinModelPortal; A3YMY6; -. DR EnsemblBacteria; EAQ56302; EAQ56302; CJJCF936_1126. DR PATRIC; 27751644; VBICamJej28969_1548. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID A3YP00_CAMJU Unreviewed; 201 AA. AC A3YP00; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 33. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=CJJ26094_1108; OS Campylobacter jejuni subsp. jejuni 260.94. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360108; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=260.94; RA Fouts D., Nelson K.; RT "Sequence of Campylobacter jejuni subsp. jejuni 260.94."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANK01000001; EAQ59485.1; -; Genomic_DNA. DR ProteinModelPortal; A3YP00; -. DR EnsemblBacteria; EAQ59485; EAQ59485; CJJ26094_1108. DR PATRIC; 30471023; VBICamJej101115_0325. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23390 MW; 081449B92607D5F2 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RGCLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID A3YP41_CAMJU Unreviewed; 210 AA. AC A3YP41; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CJJ26094_1144; OS Campylobacter jejuni subsp. jejuni 260.94. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360108; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=260.94; RA Fouts D., Nelson K.; RT "Sequence of Campylobacter jejuni subsp. jejuni 260.94."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANK01000001; EAQ59562.1; -; Genomic_DNA. DR ProteinModelPortal; A3YP41; -. DR EnsemblBacteria; EAQ59562; EAQ59562; CJJ26094_1144. DR PATRIC; 30470949; VBICamJej101115_0288. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID A3YV80_9SYNE Unreviewed; 339 AA. AC A3YV80; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=WH5701_14536; OS Synechococcus sp. WH 5701. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=69042; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 5701; RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANO01000002; EAQ76032.1; -; Genomic_DNA. DR ProteinModelPortal; A3YV80; -. DR EnsemblBacteria; EAQ76032; EAQ76032; WH5701_14536. DR PATRIC; 29896781; VBISynSp31756_0424. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 115 Unknown (By similarity). FT REGION 116 339 Thiamine-phosphate synthase (By FT similarity). FT REGION 168 172 HMP-PP binding (By similarity). FT REGION 265 267 THZ-P binding (By similarity). FT METAL 201 201 Magnesium (By similarity). FT METAL 220 220 Magnesium (By similarity). FT BINDING 200 200 HMP-PP (By similarity). FT BINDING 239 239 HMP-PP (By similarity). FT BINDING 268 268 HMP-PP (By similarity). FT BINDING 295 295 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 339 AA; 36504 MW; 3B44DC5084B523AF CRC64; MLRLLDANLD RAREGLRVLE DWCRFGLDRQ DLVARLKDLR QRLGRCHLPA YKAARHTASD GGAGLAHPAQ AERQQPSQVV AANAGRAQEA LRVLEEFGRA GDPLLAAEAA AIRYALYDLE VDLMRACGAA AGRRELLLRC HLYLITSPSP RLLETVAAAL EAGVRLVQYR AKQADDLERW QEARALRQLC SSHGALFIVN DRVDLALAVE ADGVHLGQGD LPPAEARRLL GPDRLIGRST QRIEQLRQAV ADGCDYVGVG PINATPTKPG REPVGLAYER EAAAESPIPF FAIGGLDAGA VAPVVAAGGR RVAVVRAIME ASDPHAASRE LLAALQEEA // ID A3ZAC2_9SYNE Unreviewed; 348 AA. AC A3ZAC2; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RS9917_01871; OS Synechococcus sp. RS9917. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=221360; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RS9917; RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANP01000007; EAQ68043.1; -; Genomic_DNA. DR ProteinModelPortal; A3ZAC2; -. DR EnsemblBacteria; EAQ68043; EAQ68043; RS9917_01871. DR PATRIC; 29888783; VBISynSp107221_0369. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 128 Unknown (By similarity). FT REGION 129 348 Thiamine-phosphate synthase (By FT similarity). FT REGION 180 184 HMP-PP binding (By similarity). FT REGION 277 279 THZ-P binding (By similarity). FT METAL 213 213 Magnesium (By similarity). FT METAL 232 232 Magnesium (By similarity). FT BINDING 212 212 HMP-PP (By similarity). FT BINDING 251 251 HMP-PP (By similarity). FT BINDING 280 280 HMP-PP (By similarity). FT BINDING 307 307 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 348 AA; 38290 MW; 64EC77829A8C0851 CRC64; MKSMLAAASG DQRVARLIDA NLDRAREGLR VVEDWCRFGL DRQDLVIRLK DWRQRLGAHH HRAYKEARST ATDSGAGLAH PAQQKRDHAE QIVAANCGRI QEALRVLEEF GRDSNPELAA TAAAIRYGIY DLEVTILQAG DHQERLRRLH ESRLYLVTSP VPNLVAQVAA ALQAGLSLVQ YRAKEGHDLQ RLEEARALAD LCKRHQALFI VNDRIDLALL VDADGVHLGQ EDLPTREARA LIGPHRLLGR STHQLEQLLT AQNEGCDYVG VGPVYATATK PDRSARGLHW VEEASRHASI PWFAIGGIDA GRLDAVRAAG AHRVAVVRAI MDATDAQAAS HELLTALL // ID A3ZBD1_CAMJU Unreviewed; 201 AA. AC A3ZBD1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 33. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=CJJHB9313_1060; OS Campylobacter jejuni subsp. jejuni HB93-13. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360112; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HB93-13; RA Fouts D., Nelson W.C., Mongodin E., Schobel S., Sebastian Y., RA Shomokin I., Nelson K.; RT "Sequence of Campylobacter jejuni subsp jejuni HB93-13."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANQ01000001; EAQ60816.1; -; Genomic_DNA. DR ProteinModelPortal; A3ZBD1; -. DR EnsemblBacteria; EAQ60816; EAQ60816; CJJHB9313_1060. DR PATRIC; 27761026; VBICamJej65950_0632. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23461 MW; 48AC77B39ECB01F4 CRC64; MWDKKIIAIS DRKCVQIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID A3ZBH0_CAMJU Unreviewed; 210 AA. AC A3ZBH0; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CJJHB9313_1095; OS Campylobacter jejuni subsp. jejuni HB93-13. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360112; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HB93-13; RA Fouts D., Nelson W.C., Mongodin E., Schobel S., Sebastian Y., RA Shomokin I., Nelson K.; RT "Sequence of Campylobacter jejuni subsp jejuni HB93-13."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANQ01000001; EAQ61106.1; -; Genomic_DNA. DR ProteinModelPortal; A3ZBH0; -. DR EnsemblBacteria; EAQ61106; EAQ61106; CJJHB9313_1095. DR PATRIC; 27760954; VBICamJej65950_0596. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22980 MW; 25138187D1AAA731 CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKAVLD ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLPLK // ID A3ZHS7_CAMJU Unreviewed; 210 AA. AC A3ZHS7; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CJJ8425_1109; OS Campylobacter jejuni subsp. jejuni 84-25. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360110; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=84-25; RA Fouts D., Nelson K.; RT "Sequence of Campylobacter jejuni subsp. jejuni 84-25."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANT02000001; EAQ95569.1; -; Genomic_DNA. DR ProteinModelPortal; A3ZHS7; -. DR EnsemblBacteria; EAQ95569; EAQ95569; CJJ8425_1109. DR PATRIC; 27745826; VBICamJej92970_0675. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23001 MW; 753C83D43B0EB44A CRC64; MKNKLDLSLY LVATKGSKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID A3ZHW5_CAMJU Unreviewed; 201 AA. AC A3ZHW5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=CJJ8425_1071; OS Campylobacter jejuni subsp. jejuni 84-25. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360110; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=84-25; RA Fouts D., Nelson K.; RT "Sequence of Campylobacter jejuni subsp. jejuni 84-25."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANT02000001; EAQ94850.1; -; Genomic_DNA. DR ProteinModelPortal; A3ZHW5; -. DR EnsemblBacteria; EAQ94850; EAQ94850; CJJ8425_1071. DR PATRIC; 27745904; VBICamJej92970_0714. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID A3ZUE5_9PLAN Unreviewed; 357 AA. AC A3ZUE5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DSM3645_21984; OS Blastopirellula marina DSM 3645. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Blastopirellula. OX NCBI_TaxID=314230; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3645; RA Amann R., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANZ01000012; EAQ79855.1; -; Genomic_DNA. DR ProteinModelPortal; A3ZUE5; -. DR EnsemblBacteria; EAQ79855; EAQ79855; DSM3645_21984. DR PATRIC; 36949529; VBIBlaMar90471_1315. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 186 190 HMP-PP binding (By similarity). FT REGION 283 285 THZ-P binding (By similarity). FT METAL 219 219 Magnesium (By similarity). FT METAL 238 238 Magnesium (By similarity). FT BINDING 218 218 HMP-PP (By similarity). FT BINDING 257 257 HMP-PP (By similarity). FT BINDING 286 286 HMP-PP (By similarity). FT BINDING 313 313 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 357 AA; 38534 MW; B0BD4BA05636BA33 CRC64; MPDEQQPPNA QSTIAAWRAI DAAANRAAEG LRVVEDFVRF GLDDRHLTTL VKNMRHDLAS ALQQFSSETL HSARDTQADV GVTLSTNGEQ SRTNLTQIAT SNLKRAQQSL RTLEEFSKLV HPAVSAYFEQ LRYRSYTLEK GLTTTQANSE RLAGARLYVL IDGCQNAEKF SQIVAELIAG GVDIVQLRDK SLDDRTLLER ARQLREITAA TSTFAIVNDR CDIAALADAD GVHVGQEELS VKEARAILGV GKLIGVSTHS IDQARRAVLD GADYIGVGPT FPSQTKSFDQ FPGLDLVRQV AGEIRLPAFA IGGITLENIG QVVEAGLSRV AVSGAIAGAN DPREAAEAMR QSLRGAN // ID A4AHQ4_9ACTN Unreviewed; 234 AA. AC A4AHQ4; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=A20C1_01691; OS marine actinobacterium PHSC20C1. OC Bacteria; Actinobacteria. OX NCBI_TaxID=312284; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PHSC20C1; RA Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOB01000004; EAR25260.1; -; Genomic_DNA. DR ProteinModelPortal; A4AHQ4; -. DR EnsemblBacteria; EAR25260; EAR25260; A20C1_01691. DR PATRIC; 25919431; VBIMarAct105506_2303. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 51 55 HMP-PP binding (By similarity). FT REGION 154 156 THZ-P binding (By similarity). FT REGION 205 206 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 107 107 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 126 126 HMP-PP (By similarity). FT BINDING 157 157 HMP-PP (By similarity). FT BINDING 185 185 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 234 AA; 23965 MW; 3C774EBAEE953FB9 CRC64; MSTEASPVSG YRASFDLSTY LVTDSAQARA AGHDLVELIY EAVAGGVTIV QLREKDLPAR AFLDLVLRVS TAVGLKVPVL VNDRVDVYLA AREMGARVAG VHVGQHDLPP SAVRALVGPD AIVGLSAATE DQLYEASVRS AGVDYVGIGA LHPTTSKKDA PEQLGHARMA ELIALSTLPS VAIGGIGPDD LPLLRAAGAD GAAVVSAICG AADPRVAARA LADAWAGESV GERV // ID A4BCN5_9GAMM Unreviewed; 479 AA. AC A4BCN5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=MED297_07761; OS Reinekea blandensis MED297. OC Bacteria; Proteobacteria; Gammaproteobacteria; Reinekea. OX NCBI_TaxID=314283; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED297; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOE01000006; EAR09967.1; -; Genomic_DNA. DR ProteinModelPortal; A4BCN5; -. DR EnsemblBacteria; EAR09967; EAR09967; MED297_07761. DR PATRIC; 28433310; VBIReiBla99298_2623. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 479 AA; 51536 MW; EA96C92B06328B0A CRC64; MSLLILSGFE ANGMAGLLAD DRLANGLNIP AAAIATGQTA QTASALMHAS ATDPNVMQQQ LSSLNQPPSV IKIGAVFDVA TAQVIANWLS TLPHRPTVVL DPVGLSSGDH RPLSTMTLGE RLAPLLPWVS LLTPNTDEAK ALAGTTESVQ ILRVLQAQYD FRGTLLLKGG HSVSEQDDVV TDELLVPDDP RRWQLQQPKR LSKLRGTGCR LSTAIACALT DGYALTDACV LGSAVLHRYW RLAPKPTAPG WPDTLSDYPV VSTDTHPTSP DRTFPALDWP SGLYPVVDSA QWVQRLANTG IRTLQLRIKH ARSDVLSDQI RQAIEIANAH QLQLFINDHW QQAIELGAYG VHLGQEDLDT ADLAAIANAG LRLGISTHGD TELLRALALK PSYLAVGAVF PTQTKDMSGQ IQGIGRLRRY VRLSKGTPVV AIGGINVQNL ADVLDTNVDM VAVVSAVTAS TAPERDAHLL NERVMRCRH // ID A4BQH5_9GAMM Unreviewed; 316 AA. AC A4BQH5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 45. DE SubName: Full=Uncharacterized protein; GN ORFNames=NB231_05541; OS Nitrococcus mobilis Nb-231. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Nitrococcus. OX NCBI_TaxID=314278; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Nb-231; RA Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOF01000005; EAR21825.1; -; Genomic_DNA. DR ProteinModelPortal; A4BQH5; -. DR EnsemblBacteria; EAR21825; EAR21825; NB231_05541. DR PATRIC; 25483060; VBINitMob112042_0559. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34052 MW; 1C7B59C9BDA4612E CRC64; MSASKPVHVA VGVVTDAAAR VLICRRGAHR HQGGLWEFPG GKVEPGEDVC AALDRELTEE VGIRPELAWP LIRVPYRYPD KEVLLDVWRV SRFTGAAQGR EGQCCQWVMP PALADFRFPP ANHPIVLAAG LPARYLITPS LAGAEGLLRG VQQGLSLGCK LVQLRTDGLS EVQLEKLAHT LLAVVRAAGG KLLVSRRVDI ARRVGADGVH LSTAQLWALR ARPLPASLLV GASCHNPEDL ARACTIGVDF AVLSPVRATL SHPGREPLGW QTFAAWIRDV SIPVYALGGV GPADMERAWR ARAQGVAGIR KFWRAG // ID A4BSF2_9GAMM Unreviewed; 211 AA. AC A4BSF2; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NB231_13496; OS Nitrococcus mobilis Nb-231. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Nitrococcus. OX NCBI_TaxID=314278; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Nb-231; RA Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOF01000009; EAR21412.1; -; Genomic_DNA. DR ProteinModelPortal; A4BSF2; -. DR EnsemblBacteria; EAR21412; EAR21412; NB231_13496. DR PATRIC; 25486379; VBINitMob112042_2305. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22053 MW; 8D1D5991A71CC64B CRC64; MSAERRRALH GLYALTDSGL QRPQDLPTRV EAVLSGGAHL LQYRDKSARP QRRQEALQLA ALCRAYGAVF IVNDDVELAV TVAADGVHLG RDDLSLSAAR ARLGPAAIIG ISCYNELGRA RAAAAGGADY VAFGSVFPSP TKPRAVHAPL ELLAAAREVL SLPIVAIGGI TPDNARRVVA TGVDAVAVVR GVFGVPDPAS AARRVACLFD D // ID A4BZI8_9FLAO Unreviewed; 214 AA. AC A4BZI8; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PI23P_08145; OS Polaribacter irgensii 23-P. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Polaribacter. OX NCBI_TaxID=313594; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=23-P; RA Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOG01000002; EAR12581.1; -; Genomic_DNA. DR ProteinModelPortal; A4BZI8; -. DR EnsemblBacteria; EAR12581; EAR12581; PI23P_08145. DR PATRIC; 29509504; VBIPolIrg130144_1641. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23542 MW; D3E08044B7D4CA08 CRC64; MYNTTYALMY VTDDGITDDT AFFKILEDTL KGGASIIQLR EKSCKTISFY NRSLKAKTLC HAYRVPFIIN DRIDIALAVD ADGVHLGQTD MPYRKARELL GPNKIIGLSV SNTEQAIEAE NLKVDYIGIS PIFNTVTKTS DLAPSLGIEG LQMIRPLFSK PIICIGGIHQ NNVAEIIKNG ANGVAIISAI SKAQYPEKET KNLKEIICQT GFIQ // ID A4C0H4_9FLAO Unreviewed; 212 AA. AC A4C0H4; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 16-OCT-2013, entry version 33. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=PI23P_09825; OS Polaribacter irgensii 23-P. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Polaribacter. OX NCBI_TaxID=313594; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=23-P; RA Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOG01000002; EAR12917.1; -; Genomic_DNA. DR ProteinModelPortal; A4C0H4; -. DR EnsemblBacteria; EAR12917; EAR12917; PI23P_09825. DR PATRIC; 29510148; VBIPolIrg130144_1960. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 212 AA; 23344 MW; A1E1D70FC19CAB6C CRC64; MIPKLHYISQ GTTPKEHIEN IQKACSAGAE LVQLNVKNLS EKKYLKLAKE AREITAYFQT RLIISGDYKI AKAVKADGVH LEQKGSCPTA ARIHLYTWQI IGADANTLAA CKILIDKQVD YITLSPFKAE KNKDTEQTIL GLLGYTAIVE ALNTKTPIIG VGKITTKDIS DILKTGIVGV AVADEITLDF DIIKKFNQLL SASSTEEQRH TF // ID A4C196_9FLAO Unreviewed; 217 AA. AC A4C196; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PI23P_11217; OS Polaribacter irgensii 23-P. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Polaribacter. OX NCBI_TaxID=313594; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=23-P; RA Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOG01000003; EAR11899.1; -; Genomic_DNA. DR ProteinModelPortal; A4C196; -. DR EnsemblBacteria; EAR11899; EAR11899; PI23P_11217. DR PATRIC; 29510706; VBIPolIrg130144_2239. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23746 MW; E98BC5115E4AE816 CRC64; MIGKLQYISQ GETPEEHLEN IEQACISGAV WVQLRLKNLD ANSILETAKK ARRITQHYKA KLIVNDHYKI AKEVQADGVH LGKKDCCPQE VRGYLGSEFI IGGTANTLED CENLLAKKVD YIGLGPYQFT KTKKQLSPIL GVDGYKRILA ALHTKTPIIA IGGIEFSAVP EIVNTGVYGI AFSGALTKDF KSIPIVTKLI SVSSKEAQAN KTANTQF // ID A4C198_9FLAO Unreviewed; 213 AA. AC A4C198; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 16-OCT-2013, entry version 29. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase; GN ORFNames=PI23P_11227; OS Polaribacter irgensii 23-P. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Polaribacter. OX NCBI_TaxID=313594; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=23-P; RA Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOG01000003; EAR11901.1; -; Genomic_DNA. DR ProteinModelPortal; A4C198; -. DR EnsemblBacteria; EAR11901; EAR11901; PI23P_11227. DR PATRIC; 29510710; VBIPolIrg130144_2241. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 213 AA; 24405 MW; 45FDF1B43DB26609 CRC64; MLILLAPEKD IVGEIEILTQ LFKEGLSCYH LRKPAKNQQE HCAFLDKIPP EYHHRILLHH CHELLQDYNL KGLHFTAKKR ADVLTKGPQL FLDLQKKGKT ISSSFHEIKE VLDCTVAFDY HFLSPVFSSI SKKGYLGRSF KVHEIDKRMI GMGGITANNL EETIALGFHG VGVLGGVWYA ENPVESFKSI QQQYEQCVQN YTQLSENRHT RIN // ID A4C8L1_9GAMM Unreviewed; 504 AA. AC A4C8L1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 43. DE SubName: Full=Putative phosphomethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase; GN ORFNames=PTD2_07779; OS Pseudoalteromonas tunicata D2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=87626; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D2; RA Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., RA Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K., RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOH01000003; EAR28926.1; -; Genomic_DNA. DR ProteinModelPortal; A4C8L1; -. DR EnsemblBacteria; EAR28926; EAR28926; PTD2_07779. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 504 AA; 53861 MW; 396BDBA6A66650F2 CRC64; MKSIIWTIAG SDSGGGAGIA ADIKAIESFG GHACTIITAL TAQNSMGVEA INAVTIEVLE SQFAALESDM PAKVIKIGLL ANIQQVEFVA AKLAHFKANW PLPPLVVYDP VAVASSGETL TEDDIIPTLK NTLLPLVDVI TPNTQETQIL TGHYLIGPSA VRDASEAFFN LGVGAAVIKG GHWDYPQGYC VDYCAVPGQE YWLGNEKIIA PHNHGTGCSY ASSMAACLGL GYPLKDAFIL AKAYINQGLK VSVRIGQGIG PVAHKGFPHD LADFPTVIEA GSWLGKELEL EPWDRPVVAE FSPSETQQLG LYAVVDNCDW LKLCLENGIK TVQLRIKNSD TPNLAEQIQT AVALGQQFQA RVYINDHWQL AIEHGAYGVH LGQEDLDTAD LVAIKAAGLK LGLSTHGFYE MLRAHNYQPS YLAFGAIYPT TTKDMTGQIQ GLEKLKHFVP LMKAYPTVAI GGIDLIRAPE VAATGVGSVA VVRAITEAAD PLQAISQLQQ AIKV // ID A4CW44_SYNPV Unreviewed; 353 AA. AC A4CW44; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=WH7805_05466; OS Synechococcus sp. (strain WH7805). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=59931; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 7805; RA Scanlan D., Ostrowski M., Mazard S., Wilkinson N., Partensky F., RA Dufresne A., Garczarek L., Hess W., Gierga G., Voss B., Axmann I., RA Post A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOK01000004; EAR18215.1; -; Genomic_DNA. DR ProteinModelPortal; A4CW44; -. DR EnsemblBacteria; EAR18215; EAR18215; WH7805_05466. DR PATRIC; 29901877; VBISynSp124776_1792. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 128 Unknown (By similarity). FT REGION 129 353 Thiamine-phosphate synthase (By FT similarity). FT REGION 185 189 HMP-PP binding (By similarity). FT REGION 282 284 THZ-P binding (By similarity). FT METAL 218 218 Magnesium (By similarity). FT METAL 237 237 Magnesium (By similarity). FT BINDING 217 217 HMP-PP (By similarity). FT BINDING 256 256 HMP-PP (By similarity). FT BINDING 285 285 HMP-PP (By similarity). FT BINDING 312 312 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 353 AA; 38527 MW; E5E9D0E7430FDF05 CRC64; MESMPVAPST DPRVARLIDA NLDRAREGLR VIEDWCRFGL DRHDLVVPLK DWRQQLGQLH DDAYRQARST ATDTAAGLGH PAQNSRTNSV AIVKANASRV QEALRVIEEF TRTADAVLAQ TAAEVRYSLY DHEVRILEAC GHNRRKQQLE EAKLCLITDP STDDDSGRLV RHVNAALDSG VTLVQYRRKH GSDGLRLQEA KQLAELCQSH HALFIVNDRI DLALLVNADG VHLGQEDLPH NEARRLLGSE KLIGRSTHAL GQLQEAQQAG ADYAGVGPVF ATATKADRQP AGLNWVKEAC AAAHIPWFAI GGITATTLPQ VREAGASRVA VVSAIMASDD PALASRQLLD LLL // ID A4E844_9ACTN Unreviewed; 231 AA. AC A4E844; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=COLAER_00584; OS Collinsella aerofaciens ATCC 25986. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Collinsella. OX NCBI_TaxID=411903; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25986; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Collinsella aerofaciens (ATCC 25986)."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25986; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVN02000002; EBA40060.1; -; Genomic_DNA. DR ProteinModelPortal; A4E844; -. DR EnsemblBacteria; EBA40060; EBA40060; COLAER_00584. DR PATRIC; 31034847; VBIColAer81217_0513. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 208 209 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 231 AA; 24058 MW; 2212A5E4EEBE5CD2 CRC64; MSIRDNLDIS AYLVLGPENT LGRPVGDVVA QALDAGFTCI QVRSKVASAR EIIALTGDAA QAIAQAGKTG QVALLIDDRL DCVLAAREQG IAVDGVHVGQ SDIPVEVCRK LLGPDAIVGL SARCEEMLEY VKTADMSLVD YLGIGPLHET ETKRDCGRAA DGSIITKSFE DLAALHAASP VPIVVGGGVK TADLPQLKAT GVDGFFVVSA VCSADDPYAA AKELVDTWQQ A // ID A4EMM7_9RHOB Unreviewed; 208 AA. AC A4EMM7; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 30. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=RCCS2_00087; OS Roseobacter sp. CCS2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391593; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCS2; RA Mary Ann M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYB01000007; EBA10833.1; -; Genomic_DNA. DR ProteinModelPortal; A4EMM7; -. DR EnsemblBacteria; EBA10833; EBA10833; RCCS2_00087. DR PATRIC; 28099119; VBIRosSp4847_3233. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 208 AA; 22420 MW; FB123302C9730DB2 CRC64; MSDAQDHPQI YLISPSEFDL STFPAQLAAC LDSTEVGCVR LALGSTDEGR IAKAADALRE VTHERDVALV IDSHIQLVER LGLDGVHLND GARSVRQTRK DLGDDAIVGS YCTNSRHDGM TAGELGADYV SFGPVGETPL GDGRRAELEL FEWWSMMIEV PVVAEGVLDA DLIRALTPHT DFFGIGDEIW SADNPAAALG DLRRAMLG // ID A4ERA6_9RHOB Unreviewed; 229 AA. AC A4ERA6; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 30. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=RSK20926_18777; OS Roseobacter sp. SK209-2-6. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=388739; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK209-2-6; RA Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYC01000002; EBA17812.1; -; Genomic_DNA. DR ProteinModelPortal; A4ERA6; -. DR EnsemblBacteria; EBA17812; EBA17812; RSK20926_18777. DR PATRIC; 28118169; VBIRosSp102653_0887. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 229 AA; 24639 MW; BD980AC9F5DE2751 CRC64; MRSISFALNK PVKDQEDLMM DSTADTPETP QIYLITPPSF ELGRYPEVLA RVLDKNEVAC VRLNMASRDE DTLSRAGDAL REVCHARDVA LVISDHQILA ERLGLDGVHL TDASKSVRAA RKALGADAIV GSFCGASRHD GMGAGEAGAD YVSFGPVGTS GLGDGAIADH ELFEWWSQMI EVPVVAEGGL NEELVRQFAP VTDFFGLSDE IWGVEDPATA LHKLIAAMK // ID A4EXV5_9RHOB Unreviewed; 201 AA. AC A4EXV5; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RSK20926_15246; OS Roseobacter sp. SK209-2-6. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=388739; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK209-2-6; RA Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYC01000010; EBA15585.1; -; Genomic_DNA. DR ProteinModelPortal; A4EXV5; -. DR EnsemblBacteria; EBA15585; EBA15585; RSK20926_15246. DR PATRIC; 28122788; VBIRosSp102653_3161. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22443 MW; C4715F84A34BCD99 CRC64; MERFYLIVGH VGRLELLVPQ GAKLVQLRIK DEPDAEVRRQ IARARDFCAV HDAQLVVNDY WQAALDLNCN FVHLGQEDME VADFPALRRR GIRFGLSTHD EAELERALSH DPAYVALGPV YPTLLKKMKW GAQGLERVTR WKEIAGKTPL VAIGGLTPER LQGVFDAGAD SAAVVTDIQL ADDPEAQTRM WAKACRELES A // ID A4G1V5_HERAR Unreviewed; 203 AA. AC A4G1V5; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 60. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HEAR0264; OS Herminiimonas arsenicoxydans. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Herminiimonas. OX NCBI_TaxID=204773; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ULPAs1; RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053; RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E., RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M., RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., RA Leize E., Lieutaud A., Lievremont D., Makita Y., Mangenot S., RA Nitschke W., Ortet P., Perdrial N., Schoepp B., Siguier P., RA Simeonova D.D., Rouy Z., Segurens B., Turlin E., Vallenet D., RA van Dorsselaer A., Weiss S., Weissenbach J., Lett M.-C., Danchin A., RA Bertin P.N.; RT "A tale of two oxidation states: bacterial colonization of arsenic- RT rich environments."; RL PLoS Genet. 3:518-530(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU207211; CAL60492.1; -; Genomic_DNA. DR RefSeq; YP_001098621.1; NC_009138.1. DR ProteinModelPortal; A4G1V5; -. DR STRING; 204773.HEAR0264; -. DR EnsemblBacteria; CAL60492; CAL60492; HEAR0264. DR GeneID; 4931278; -. DR KEGG; har:HEAR0264; -. DR PATRIC; 22110730; VBIHerArs17568_0258. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HARS204773:GJCA-257-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21801 MW; D20138B630348A13 CRC64; MQGLYLVTPD WDDTRKLLEI TELALKGGVT LLQYRHKTAD AALRREQAEC LQALAKSYQC PFIINDYIDL CMELDADGIH VGGTDMAVAD VRKAIGPQKI LGASCYGSLE MAHAAEAAGA SYVAFGGFYP SKVKKYPVTT DPMIVAHWKE QGKVPSCVIG GMTKENAAPL VRNGADMVAA ISSIYLAGDP QAAARAFVNL FAE // ID A4IKR3_GEOTN Unreviewed; 203 AA. AC A4IKR3; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 46. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=GTNG_0535; OS Geobacillus thermodenitrificans (strain NG80-2). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=420246; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NG80-2; RX PubMed=17372208; DOI=10.1073/pnas.0609650104; RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., RA Han W., Peng X., Liu R., Wang L.; RT "Genome and proteome of long-chain alkane degrading Geobacillus RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil RT reservoir."; RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000557; ABO65917.1; -; Genomic_DNA. DR RefSeq; YP_001124662.1; NC_009328.1. DR ProteinModelPortal; A4IKR3; -. DR STRING; 420246.GTNG_0535; -. DR EnsemblBacteria; ABO65917; ABO65917; GTNG_0535. DR GeneID; 4965479; -. DR KEGG; gtn:GTNG_0535; -. DR PATRIC; 21977347; VBIGeoThe136879_0558. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GTHE420246:GIXT-607-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 203 AA; 21573 MW; 7F5C0BD4F1F6C955 CRC64; MGTLHFVSTG RQTADEFAAI CQHIHPYADC IHIREKEKTA REVAAFVTAL LRVGVPPQKI IVNDRVDVAA VYGVHGVQLA YHSLPVRAVR RSFPSLTVGC SVHGLAEAKQ AEEDGAHFCL FGHIFPTASK PGVLPRGVDL LKEIAAAVHI PVIAIGGIHA GNARRVLEAG AAGVAVLSAI FFAADPVSEA KRLAEIVKGE RIK // ID A4J0M3_DESRM Unreviewed; 215 AA. AC A4J0M3; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 55. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dred_0076; OS Desulfotomaculum reducens (strain MI-1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=349161; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MI-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Tebo B.M., Richardson P.; RT "Complete sequence of Desulfotomaculum reducens MI-1."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000612; ABO48626.1; -; Genomic_DNA. DR RefSeq; YP_001111451.1; NC_009253.1. DR ProteinModelPortal; A4J0M3; -. DR STRING; 349161.Dred_0076; -. DR EnsemblBacteria; ABO48626; ABO48626; Dred_0076. DR GeneID; 4956693; -. DR KEGG; drm:Dred_0076; -. DR PATRIC; 21725912; VBIDesRed82656_0079. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GAKWIQY; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DRED349161:GHP6-89-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23696 MW; 52938B47CE05CB86 CRC64; MADKRQVQEL FNTGLYGITA EEYSLGRSNY AVIKAMINAG IKVIQYREKE KKLREKYQEC LDIRKLTQQA GVTFIVNDHI DLALMVGADG VHIGQDDLPP EKVRQLVGEK MIIGLSTHSP LQAQAALAAG VDYIGVGPIF ATRTKKDVCQ PVGLEYLEYV VKNIPLPFVA IGGIKEHNLS EVSKRGAQCA ALVTEIVGAK DIVEKVHSLR KRINI // ID A4J232_DESRM Unreviewed; 206 AA. AC A4J232; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 55. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dred_0593; OS Desulfotomaculum reducens (strain MI-1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=349161; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MI-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Tebo B.M., Richardson P.; RT "Complete sequence of Desulfotomaculum reducens MI-1."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000612; ABO49135.1; -; Genomic_DNA. DR RefSeq; YP_001111960.1; NC_009253.1. DR ProteinModelPortal; A4J232; -. DR STRING; 349161.Dred_0593; -. DR EnsemblBacteria; ABO49135; ABO49135; Dred_0593. DR GeneID; 4958204; -. DR KEGG; drm:Dred_0593; -. DR PATRIC; 21727133; VBIDesRed82656_0654. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DRED349161:GHP6-637-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22313 MW; 24535CC19BFFBADC CRC64; MKDIDYGLYL ITDDFYLNQR GILAVIEECL KAGVTMLQYR AKEKSSREML KEAEKLKELA LKYQVPFIIN DRLDIALAVQ ADGVHLGQSD LPFTVAKGLM ADRIIGVSAT SYEEGREAIQ QGADYVGVGP VFPTATKKDA KPPLGIEVIR QLKGDFPKAK LVAIGGISLD NASEVVNSGA DGLAIISAIL GASEPGERVK QFLKMN // ID A4JAV1_BURVG Unreviewed; 374 AA. AC A4JAV1; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 55. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Bcep1808_0392; OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia OS cepacia (strain R1808)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=269482; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G4 / LMG 22486; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000614; ABO53404.1; -; Genomic_DNA. DR RefSeq; YP_001118239.1; NC_009256.1. DR ProteinModelPortal; A4JAV1; -. DR STRING; 269482.Bcep1808_0392; -. DR EnsemblBacteria; ABO53404; ABO53404; Bcep1808_0392. DR GeneID; 4952079; -. DR KEGG; bvi:Bcep1808_0392; -. DR PATRIC; 19319181; VBIBurVie89221_4589. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BVIE269482:GJNA-406-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 374 AA; 39498 MW; E62D94902F2664A8 CRC64; MSARFADAFW PPADELAEAA ERIRARLGDW PAAATPWRIC VAAPDVPADG DVLIVSAGDR AAQVRASAAS RPASADAVAI EFDERGAVLH AAGARHALEG AHPLADDWIA ALAAFLDCGF APLDALVLAL AWRDGDETGD ADPWPVDPAR FPRVAGLPAA PEPAFPPCPA QLGLYPVVPD AEWVERLLDC GVRTVQLRVK GATPDALRRE IARAVAAGRR YPDARVFIND HWQIAVEEGA YGVHLGQEDL DTADLATIAR AGLRLGLSSH GYYEMLRALH ERPSYLALGP VFATATKAVA APPQGLARIA RYARFAAARA PLVAIGGVSL EALPDVLATG VGSVAVVSAI TGAADYRAAV IALQQWFARQ FDNR // ID A4JLQ3_BURVG Unreviewed; 194 AA. AC A4JLQ3; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bcep1808_4226; OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia OS cepacia (strain R1808)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=269482; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G4 / LMG 22486; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 2 of Burkholderia vietnamiensis G4."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000615; ABO57206.1; -; Genomic_DNA. DR RefSeq; YP_001116671.1; NC_009255.1. DR ProteinModelPortal; A4JLQ3; -. DR STRING; 269482.Bcep1808_4226; -. DR EnsemblBacteria; ABO57206; ABO57206; Bcep1808_4226. DR GeneID; 4950443; -. DR KEGG; bvi:Bcep1808_4226; -. DR PATRIC; 19315913; VBIBurVie89221_2970. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BVIE269482:GJNA-4307-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 19841 MW; 4701C588CB3F0595 CRC64; MSVALPRCCV ITPEPASASA AACRALLDRL SAVLARGETL VQLRVKSLDA AAFARLAADA LARCDAAGAQ LMLNGPIDAA GVMRLDGAGW HLDGAALHAV AQRPLPPARR VSAACHTAHD LALAARVGAD FVTLSPVLPT LSHPGAPTLG WNAFAALAAQ AAMPVYALGG MTRAHLDDAR RHGAHGVAGI RGFW // ID A4KEA2_MYCTX Unreviewed; 222 AA. AC A4KEA2; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TBHG_00410; OS Mycobacterium tuberculosis str. Haarlem. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=395095; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Haarlem; RG The Broad Institute Genome Sequencing Platform; RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L., RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., RA Mauceli E., Brockman W., Rounsley S., Young S., LaButti K., RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., RA Montgomery P., Pearson M., Howarth C., Zeng Q., Kodira C., Yandava C., RA O'Leary S., Alvarado L., Murray M., Kreiswirth B.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Haarlem; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Murray M., Kreisworth B., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis str. Haarlem."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001664; EBA40937.1; -; Genomic_DNA. DR RefSeq; YP_002160509.1; NC_022350.1. DR ProteinModelPortal; A4KEA2; -. DR SMR; A4KEA2; 1-221. DR EnsemblBacteria; EBA40937; EBA40937; TBHG_00410. DR GeneID; 6821145; -. DR KEGG; mtul:TBHG_00410; -. DR PATRIC; 30813066; VBIMycTub106824_0696. DR KO; K00788; -. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID A4LF97_BURPE Unreviewed; 209 AA. AC A4LF97; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 16-OCT-2013, entry version 27. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BURPS305_5978; OS Burkholderia pseudomallei 305. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=425067; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=305; RA Nelson W.C., Wagner D., Currie B., Tuanyok A., Mayo M., Schupp J., RA Lum G., Keim P., Brettin T.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYX01000002; EBA49985.1; -; Genomic_DNA. DR ProteinModelPortal; A4LF97; -. DR EnsemblBacteria; EBA49985; EBA49985; BURPS305_5978. DR PATRIC; 27853138; VBIBurPse67809_1310. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID A4LSX5_BURPE Unreviewed; 367 AA. AC A4LSX5; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BURPS305_1950; OS Burkholderia pseudomallei 305. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=425067; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=305; RA Nelson W.C., Wagner D., Currie B., Tuanyok A., Mayo M., Schupp J., RA Lum G., Keim P., Brettin T.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYX01000015; EBA45452.1; -; Genomic_DNA. DR ProteinModelPortal; A4LSX5; -. DR EnsemblBacteria; EBA45452; EBA45452; BURPS305_1950. DR PATRIC; 27862577; VBIBurPse67809_5988. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 367 AA; 38273 MW; 8C82851C6E850E63 CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGAQAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEVE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID A4LTW4_BURPE Unreviewed; 93 AA. AC A4LTW4; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Thiamine monophosphate synthase/teni subfamily; GN ORFNames=BURPS305_0446; OS Burkholderia pseudomallei 305. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=425067; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=305; RA Nelson W.C., Wagner D., Currie B., Tuanyok A., Mayo M., Schupp J., RA Lum G., Keim P., Brettin T.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYX01000018; EBA44989.1; -; Genomic_DNA. DR ProteinModelPortal; A4LTW4; -. DR EnsemblBacteria; EBA44989; EBA44989; BURPS305_0446. DR PATRIC; 27863432; VBIBurPse67809_6408. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 93 AA; 9855 MW; 9A1B1748F66C9334 CRC64; MLVSAACHDE DQVRHADSIG VDLITISPVM PTATHTTAEP LGWPRFRELA TLTSVPVYAL GGMSVDSLAE ARNAGAYGIA AIRAFWGSNV DRS // ID A4MY48_HAEIF Unreviewed; 228 AA. AC A4MY48; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSHi22121_07200; OS Haemophilus influenzae 22.1-21. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=374927; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=22.1-21; RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103; RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., RA Post J.C., Ehrlich G.D.; RT "Characterization and modeling of the Haemophilus influenzae core and RT supragenomes based on the complete genomic sequences of Rd and 12 RT clinical nontypeable strains."; RL Genome Biol. 8:R103.1-R103.18(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZD01000002; EDJ88940.1; -; Genomic_DNA. DR ProteinModelPortal; A4MY48; -. DR EnsemblBacteria; EDJ88940; EDJ88940; CGSHi22121_07200. DR PATRIC; 26729986; VBIHaeInf63515_1072. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT REGION 203 204 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 183 183 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 25003 MW; 71388E7CA0B08A44 CRC64; MKDENIQKIL PLYFVAGTQD CRHLGENLSE NLLFVLKQAL EGGITCFQFR DKGKFSLEHT PSAQKALAIN CRDLCREYGV PFIVDDNVDL ALEIEADGIH VGQSDMPVQE IRAKTDKPLI IGWSVNRLDE AKIGENLAEI DYFGIGPIFP TQSKENPKPT LGMAFIQTLR NVGITKPLVA IGGVKLAHVK TLREFGADGV AVITAITHAD NVQAATKALR EASDEYAK // ID A4N2Q5_HAEIF Unreviewed; 226 AA. AC A4N2Q5; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSHi22421_07422; OS Haemophilus influenzae R3021. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=375432; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R3021; RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103; RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., RA Post J.C., Ehrlich G.D.; RT "Characterization and modeling of the Haemophilus influenzae core and RT supragenomes based on the complete genomic sequences of Rd and 12 RT clinical nontypeable strains."; RL Genome Biol. 8:R103.1-R103.18(2007). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R3021; RA Ehrlich G.D.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZE01000002; EDJ91582.1; -; Genomic_DNA. DR ProteinModelPortal; A4N2Q5; -. DR EnsemblBacteria; EDJ91582; EDJ91582; CGSHi22421_07422. DR PATRIC; 26790417; VBIHaeInf50037_0481. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24719 MW; 4C299CCE114F00BB CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKVLAINCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA GITKPLVAIG GVKLAHVKTL REFGADGVAM ITAISHAENV KAATKALREA SDGYAK // ID A4N911_HAEI3 Unreviewed; 226 AA. AC A4N911; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSHi3655_02574; OS Haemophilus influenzae (strain NTHi 3655). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=375177; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3655; RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103; RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., RA Post J.C., Ehrlich G.D.; RT "Characterization and modeling of the Haemophilus influenzae core and RT supragenomes based on the complete genomic sequences of Rd and 12 RT clinical nontypeable strains."; RL Genome Biol. 8:R103.1-R103.18(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZF01000002; EDJ93410.1; -; Genomic_DNA. DR ProteinModelPortal; A4N911; -. DR EnsemblBacteria; EDJ93410; EDJ93410; CGSHi3655_02574. DR PATRIC; 28854042; VBIHaeInf56590_0592. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24736 MW; CC2434460079404F CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVAEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA EITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID A4NES4_HAEIF Unreviewed; 226 AA. AC A4NES4; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSHiAA_05161; OS Haemophilus influenzae PittAA. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=374928; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PittAA; RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103; RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., RA Post J.C., Ehrlich G.D.; RT "Characterization and modeling of the Haemophilus influenzae core and RT supragenomes based on the complete genomic sequences of Rd and 12 RT clinical nontypeable strains."; RL Genome Biol. 8:R103.1-R103.18(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZG01000003; EDK08127.1; -; Genomic_DNA. DR ProteinModelPortal; A4NES4; -. DR EnsemblBacteria; EDK08127; EDK08127; CGSHiAA_05161. DR PATRIC; 28869555; VBIHaeInf35192_0553. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24736 MW; CC2434460079404F CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVAEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA EITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID A4NJA7_HAEIF Unreviewed; 226 AA. AC A4NJA7; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSHiHH_07556; OS Haemophilus influenzae PittHH. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=374932; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PittHH; RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103; RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., RA Post J.C., Ehrlich G.D.; RT "Characterization and modeling of the Haemophilus influenzae core and RT supragenomes based on the complete genomic sequences of Rd and 12 RT clinical nontypeable strains."; RL Genome Biol. 8:R103.1-R103.18(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZH01000002; EDK10414.1; -; Genomic_DNA. DR ProteinModelPortal; A4NJA7; -. DR EnsemblBacteria; EDK10414; EDK10414; CGSHiHH_07556. DR PATRIC; 28873036; VBIHaeInf67192_0264. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24780 MW; E29327421765E786 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS TQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNV GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID A4NR39_HAEIF Unreviewed; 226 AA. AC A4NR39; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSHiII_08156; OS Haemophilus influenzae PittII. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=374933; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PittII; RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103; RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., RA Post J.C., Ehrlich G.D.; RT "Characterization and modeling of the Haemophilus influenzae core and RT supragenomes based on the complete genomic sequences of Rd and 12 RT clinical nontypeable strains."; RL Genome Biol. 8:R103.1-R103.18(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZI01000002; EDK12175.1; -; Genomic_DNA. DR ProteinModelPortal; A4NR39; -. DR EnsemblBacteria; EDK12175; EDK12175; CGSHiII_08156. DR PATRIC; 28877779; VBIHaeInf106412_0597. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24758 MW; D2FC00C9C781EEE7 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAINCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNV GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID A4NVP6_HAEIF Unreviewed; 226 AA. AC A4NVP6; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSHiR3021_09980; OS Haemophilus influenzae 22.4-21. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=375063; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=22.4-21; RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103; RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., RA Post J.C., Ehrlich G.D.; RT "Characterization and modeling of the Haemophilus influenzae core and RT supragenomes based on the complete genomic sequences of Rd and 12 RT clinical nontypeable strains."; RL Genome Biol. 8:R103.1-R103.18(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZJ01000001; EDK14827.1; -; Genomic_DNA. DR ProteinModelPortal; A4NVP6; -. DR EnsemblBacteria; EDK14827; EDK14827; CGSHiR3021_09980. DR PATRIC; 28848584; VBIHaeInf65193_0251. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24721 MW; 5E34364400694040 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID A4QE50_CORGB Unreviewed; 763 AA. AC A4QE50; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=cgR_1524; OS Corynebacterium glutamicum (strain R). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=340322; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R; RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0; RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., RA Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.; RT "Comparative analysis of the Corynebacterium glutamicum group and RT complete genome sequence of strain R."; RL Microbiology 153:1042-1058(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009044; BAF54516.1; -; Genomic_DNA. DR RefSeq; YP_001138418.1; NC_009342.1. DR ProteinModelPortal; A4QE50; -. DR STRING; 340322.cgR_1524; -. DR EnsemblBacteria; BAF54516; BAF54516; cgR_1524. DR GeneID; 4993926; -. DR KEGG; cgt:cgR_1524; -. DR PATRIC; 21507636; VBICorGlu58097_1571. DR eggNOG; COG0351; -. DR HOGENOM; HOG000225275; -. DR KO; K14153; -. DR OMA; GFWEMFP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CGLU340322:GJBE-1596-MONOMER; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.910.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF03070; TENA_THI-4; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; SSF48613; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 763 AA; 80472 MW; C7D243D8D3DD305D CRC64; MTDFSLYLVT DPVLGGGPEK VAGIVDSAIS GGVSVVQLRD KNSGVEDVRA AAKELKELCD ARGVALVVND YLDIAVELGL HLHIGQGDTP YTQARELLPA HLELGLSIEN LDQLHAVIAQ CAETGVALPD VIGIGPVAST ATKPDAAPAL GVEGIAEIAA VAQDHGIASV AIGGVGLRNA AELAATPIDG LCVVSEIMTA ANPAAAATRL RTAFQPTFSP ETQTELSQTE LQGAFVNSPS APRVLSIAGT DPTGGAGIQA DLKSIAAGGG YGMCIVTSLV AQNTHGVNTI HTPPLTFLEE QLEAVFSDVT VDAIKLGMLG SADTVDLVAS WLGSHEHGPV VLDPVMIATS GDRLLDASAE ESLRRLAVHV DVVTPNIPEL AVLCDSAPAI TMDEAIAQAQ GFARTHDTIV IVKGGHLTGT LADNAVVRPD GSVFQVENLR VNTTNSHGTG CSLSASLATR IAAGESVEKA LEWSTRWLNE ALRHADHLAV GTGNGPVDHG HLARRMTHAA ETTPWAHLRA PRLDGATAAS FTTPSTVKSP APRIEPAGPF TRALWEASGE IIAGINSSDF ITMLGDGTLR RPEFDFYIDQ DAQYLAQYSR ALARLSSIAP DSHAQIEWAQ SAAECLVVEA ELHRSYMTGK EVSAPSHITM AYTDFLIART YTEDYVCGVA AVLPCYWLYA EIGLMLAEQN HDEHPYKDWL NTYSGEEFIA GTRAAIARLE KALENAGAEQ RVDAARAFLS ASVHEREFFD QATRHGWTMV GSS // ID A4QFA5_CORGB Unreviewed; 221 AA. AC A4QFA5; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=cgR_1926; OS Corynebacterium glutamicum (strain R). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=340322; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R; RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0; RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., RA Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.; RT "Comparative analysis of the Corynebacterium glutamicum group and RT complete genome sequence of strain R."; RL Microbiology 153:1042-1058(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009044; BAF54921.1; -; Genomic_DNA. DR RefSeq; YP_001138823.1; NC_009342.1. DR ProteinModelPortal; A4QFA5; -. DR STRING; 340322.cgR_1926; -. DR EnsemblBacteria; BAF54921; BAF54921; cgR_1926. DR GeneID; 4992850; -. DR KEGG; cgt:cgR_1926; -. DR PATRIC; 21508474; VBICorGlu58097_1983. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6PZXB0; -. DR BioCyc; CGLU340322:GJBE-2008-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). SQ SEQUENCE 221 AA; 23098 MW; 4CEE5D0936EE0FFC CRC64; MFENRFDLRC YVVTGAGSVD EVVHTASAAA RGGAGVVQVR SKPISPEAMR ELASKVALEV ARCSPTTRVL IDDHLHVASS LMREGLPIHG VHLGQDDVSV LEARELLGPE AIIGLTTGTL ELVAAANELS DVLDYIGAGP FRKTPTKDSG RPPIGLAGYP PLVELSKVPI VAIGDVTPAD VRALSATGVA GVAMVRAFSE SDDPQQVAEN VVANFELGRL S // ID A4S495_OSTLU Unreviewed; 632 AA. AC A4S495; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 39. DE SubName: Full=Predicted protein; DE Flags: Fragment; GN ORFNames=OSTLU_44250; OS Ostreococcus lucimarinus (strain CCE9901). OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales; OC Ostreococcus. OX NCBI_TaxID=436017; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCE9901; RX PubMed=17460045; DOI=10.1073/pnas.0611046104; RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N., RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R., RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K., RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M., RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I., RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D., RA Van de Peer Y., Moreau H., Grigoriev I.V.; RT "The tiny eukaryote Ostreococcus provides genomic insights into the RT paradox of plankton speciation."; RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000591; ABO98685.1; -; Genomic_DNA. DR RefSeq; XP_001420392.1; XM_001420355.1. DR ProteinModelPortal; A4S495; -. DR STRING; 436017.A4S495; -. DR GeneID; 5004537; -. DR KEGG; olu:OSTLU_44250; -. DR eggNOG; COG0699; -. DR HOGENOM; HOG000241410; -. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. PE 4: Predicted; KW Complete proteome; GTP-binding; Nucleotide-binding. FT NON_TER 632 632 SQ SEQUENCE 632 AA; 68067 MW; 2E57A04653C6C117 CRC64; MTRAVPSIDA RARAHATQTR RRPRRAHLYH PSTRARSSTA PRAFLDRLSG NATATGDKQQ RDLFAQTKRA EVRIPGFLAY VDVDEATSTR GAEVVDAVLH AGATCVALRE YGVDGTGGGN SGKKLYEAAT TLKTLVRGRA CVLIVDRTDI AASAELDGVV LTDDGVPTVV ARKALPETAV VAHESESAEE AEKASKEGAD LLLVRDVAML EAIRQSVSVP IFVDAADGLG ALASENSSTL QDLAAKGANG VTIRNLTKDP ASGDEALLQS AVRAVANALE QSYEALGDSK GANGSAPQVT PKKFSLVSAD GEEMIERERQ LVEEILKFLR ENCTDLDEIK LLAEARKGLE DLFLVVICGE FNAGKSSVIN AMLGDKFVAE GILPTTNEIA VLRYSSKKSR EQTEDGFFNV GIPAELLQQM RIVDTPGTNV ILQRQQRLTE EFVPRADLVL FVLSADRPMT ESEVKFLTYI RKWGKKVVFV VNKTDLLSDL GDVDEVVAFV KENATRLLSV SDPAVLPVSS RNALKAKKAD SSNYANSRAF VESGFGKFED YVMSFLGGSG ERAGEALRLK LSTPLNVSEL LLNAAEQILE GEDEEAKSEV AMATGVTSQM ESYRQEMITD AAAQRAAARE VV // ID A4S5F9_OSTLU Unreviewed; 478 AA. AC A4S5F9; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 44. DE SubName: Full=Predicted protein; GN ORFNames=OSTLU_17535; OS Ostreococcus lucimarinus (strain CCE9901). OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales; OC Ostreococcus. OX NCBI_TaxID=436017; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCE9901; RX PubMed=17460045; DOI=10.1073/pnas.0611046104; RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N., RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R., RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K., RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M., RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I., RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D., RA Van de Peer Y., Moreau H., Grigoriev I.V.; RT "The tiny eukaryote Ostreococcus provides genomic insights into the RT paradox of plankton speciation."; RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000592; ABO98893.1; -; Genomic_DNA. DR RefSeq; XP_001420600.1; XM_001420563.1. DR ProteinModelPortal; A4S5F9; -. DR STRING; 436017.A4S5F9; -. DR GeneID; 5004685; -. DR KEGG; olu:OSTLU_17535; -. DR eggNOG; COG0351; -. DR KO; K14153; -. DR OMA; NTKANNP; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 478 AA; 49874 MW; AE3E9444A95C7106 CRC64; MVRGKVLVVA GSDSGGGAGV QADVKAILAH GAFATTAITA LTAQNTTGVH GVHAAPLEFI EAQIEAVVTD LPPDACKTGM LANAATTRAV ADAIERHRLT NVVVDTVMLA KGGASLLEAE ALEVMRDRLA PLATVITPNV PEAAALLNLS EEEFVMETMA TRAKELGKLG CQWVLLKGGH VKDDAEMSVD YLYEANTGRT TTFSSARIDT RHTHGTGCTL ASSIAASLAQ RYDVPTAVHR AKRYISEAIR TSPGYGAGHG PLNHLPFHAG AAARGKRFDP RCLKLYLVSS EALTMDKLRQ ALEAGVTIVQ MRDKDPSTRA LIERAKAMKA ACDEYGVPFI VNDRVDVAIA CDADGVHLGQ SDMTCAEARQ ILGPNKWIGV SCREVSLARQ ASADDADYIG CGACFGTNSK GDAKVIGLDG VGKVIAVARE LSLPVVAIGG VSLENAASVR ATGADGIAVI SAVANAADVK KAVHKLLH // ID A4SEP7_PROVI Unreviewed; 214 AA. AC A4SEP7; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 39. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Cvib_0942; OS Prosthecochloris vibrioformis (strain DSM 265) (Chlorobium vibrioforme OS subsp. thiosulfatophilum (strain DSM 265)) (Chlorobium phaeovibrioides OS (strain DSM 265)). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290318; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 265; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., RA Schuster S.C., Bryant D.A., Richardson P.; RT "Complete sequence of Prosthecochloris vibrioformis DSM 265."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000607; ABP36956.1; -; Genomic_DNA. DR RefSeq; YP_001130458.1; NC_009337.1. DR ProteinModelPortal; A4SEP7; -. DR STRING; 290318.Cvib_0942; -. DR EnsemblBacteria; ABP36956; ABP36956; Cvib_0942. DR GeneID; 4970595; -. DR KEGG; pvi:Cvib_0942; -. DR PATRIC; 21396300; VBIChlPha132153_0995. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FGPPQGL; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPHA290318:GHNQ-960-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 214 AA; 22939 MW; 26E56764220CF007 CRC64; MSSANSQPLP LPRICWITSG RETDGSGQQI SRLLQELPLN RPAMVLIREK QLNGRQLLAL ASRIAKETLP NGSRLMLSER MDIALAAGLH GVHLPEHSCP ADRLSSASPG MLIGKSVHSP ESALAAEKEG VDYLFFSPVF ASLSKPGYGP LQGTALLREV CRATSVPVFA LGGIRPENTI PCIECGAWGV ASLGLFTETA NFRKTAETID RLLP // ID A4SSI5_AERS4 Unreviewed; 524 AA. AC A4SSI5; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 46. DE SubName: Full=Thiamine monophosphate synthase; GN Name=thiE; OrderedLocusNames=ASA_3904; OS Aeromonas salmonicida (strain A449). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=382245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A449; RX PubMed=18801193; DOI=10.1186/1471-2164-9-427; RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., RA Kimball J., Munholland J., Murphy C., Sarty D., Williams J., RA Nash J.H., Johnson S.C., Brown L.L.; RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights RT into the evolution of a fish pathogen."; RL BMC Genomics 9:427-427(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000644; ABO91857.1; -; Genomic_DNA. DR RefSeq; YP_001143605.1; NC_009348.1. DR ProteinModelPortal; A4SSI5; -. DR STRING; 382245.ASA_3904; -. DR EnsemblBacteria; ABO91857; ABO91857; ASA_3904. DR GeneID; 4998632; -. DR KEGG; asa:ASA_3904; -. DR PATRIC; 20794236; VBIAerSal2987_3868. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ASAL382245:GJJN-3891-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 524 AA; 55357 MW; A9C8600758E271C7 CRC64; MNSRPIVWTI AGSDSGGGAG IQADLHTLHD LGVHGCSVIT AITAQNSVAV KMVDPVLMQT FTAQIDALGV DLPPAAIKIG LLPTRLHVEV LARRLDTLTA PFVVYDPVAI ASTGTPMAEA NMLAAVREHL LPRLSLITPN GPELEALTGI PASSPELVRA GAARLRELGA RAVLVKGGHL GWSDELCLDY YQDEQREFWL GAPRIDTRHG HGTGCCYASA IAAVVAQDHP VDDAITLARA YLQQGLAGAQ GVGAGPGPIA HLGWPADLAH FPRAVLAGSS LDRRFGLYPA CEARLPEGPF AATEHRLGLY PVVDSVKWLK RLLGAGVKTL QLRIKNLPAA QVAPAIAEAV ALGHRFGARL FINDYWQQAI AAGAYGVHLG QEDMETADLA AIQAADLRLG LSTHGYFELM RARELAPSYI ALGHIFPTNT KQMPSRPQGL VRLQRYRALM CDWPTVAIGG IGEERIAAVQ ASGVGSIALV SAITASDDWQ GATARLLAAV GAGDEPCSAL IHQAITQQEA DHAL // ID A4SX94_POLSQ Unreviewed; 308 AA. AC A4SX94; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Pnuc_0892; OS Polynucleobacter necessarius subsp. asymbioticus (strain DSM 18221 / OS CIP 109841 / QLW-P1DMWA-1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Polynucleobacter. OX NCBI_TaxID=312153; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1; RX PubMed=22675600; DOI=10.4056/sigs.2395367; RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., RA Bruce D., Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., RA Brettin T., Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., RA Goker M., Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.; RT "Complete genome sequence of Polynucleobacter necessarius subsp. RT asymbioticus type strain (QLW-P1DMWA-1(T))."; RL Stand. Genomic Sci. 6:74-83(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000655; ABP34108.1; -; Genomic_DNA. DR RefSeq; YP_001155672.1; NC_009379.1. DR ProteinModelPortal; A4SX94; -. DR STRING; 312153.Pnuc_0892; -. DR EnsemblBacteria; ABP34108; ABP34108; Pnuc_0892. DR GeneID; 5052420; -. DR KEGG; pnu:Pnuc_0892; -. DR PATRIC; 22966201; VBIPolNec12025_0923. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RFKSEDR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PNEC312153:GH50-915-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 137 141 HMP-PP binding (By similarity). FT METAL 170 170 Magnesium (By similarity). FT METAL 189 189 Magnesium (By similarity). FT BINDING 169 169 HMP-PP (By similarity). FT BINDING 208 208 HMP-PP (By similarity). FT BINDING 237 237 HMP-PP (By similarity). FT BINDING 266 266 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 308 AA; 34467 MW; 20D9C93967AFC2E3 CRC64; MSLIRDLADQ IVSAHRKDDI CLPIPDYTLN TPPPRIDNES AADLNELAAT LAAIEMGFIE KDAKTIGKAW SRMVLQDGGF DPFKWPSRPE HFDLLPWTRN MNPKAFKECP KRLGLYGVMP DADWVKRMVE AEIPTVQLRF KSEDRYKIRK QIRESVKATE GSKTLLFIND YWEEAIDAEA YGVHLGQEDM ETADLEAIRS AGLRLGLSTH GYAEMVYADR FCPSYIAMGA VFPTNLKKMP TAPQGLGRLY KYAQLMNHYP LVAIGGIDES SIHAVVKSGV GSVAVVRAIT QTKDPKAAVK HLQELMRA // ID A4TWG2_9PROT Unreviewed; 210 AA. AC A4TWG2; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MGR_3756; OS Magnetospirillum gryphiswaldense. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Magnetospirillum. OX NCBI_TaxID=55518; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MSR-1; RX PubMed=17449609; DOI=10.1128/JB.00119-07; RA Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O., RA Reinhardt R., Schueler D.; RT "Comparative genome analysis of four magnetotactic bacteria reveals a RT complex set of group-specific genes with putative functions in RT magnetosome biomineralization and magnetotaxis."; RL J. Bacteriol. 189:4899-4910(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU459003; CAM74969.1; -; Genomic_DNA. DR ProteinModelPortal; A4TWG2; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22733 MW; 3306D3845A4825DF CRC64; MSSNSCRLYL ITPPVIENPF QWQTVWEQAL DGGDIACVQI RLKGLDDDAL CRAVDVLRPP AQRRGIAVLL NDRPDLAFET GCDGVHIGQT DGSYEAARKA LGDGIVGMTC HNSRHLAMEA GEKGADYVAF GAFYPTDTKE TEFKAEPEIL EWWSPLFTVP SVAIGGITVD NCQPIIRAGA DFLAVSGGVW NHPEGPAAAV KAFEKRMNEG // ID A4U2Y8_9PROT Unreviewed; 212 AA. AC A4U2Y8; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=MGR_3653; OS Magnetospirillum gryphiswaldense. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Magnetospirillum. OX NCBI_TaxID=55518; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MSR-1; RX PubMed=17449609; DOI=10.1128/JB.00119-07; RA Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O., RA Reinhardt R., Schueler D.; RT "Comparative genome analysis of four magnetotactic bacteria reveals a RT complex set of group-specific genes with putative functions in RT magnetosome biomineralization and magnetotaxis."; RL J. Bacteriol. 189:4899-4910(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU459003; CAM77245.1; -; Genomic_DNA. DR ProteinModelPortal; A4U2Y8; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 212 AA; 23012 MW; 8B468C5071E9324A CRC64; MAANSCTLGA MTLAEPRPHH NSAARRIPRL VLLTDDQRLP DPLPAIARLP AGSAVILRHH DWPERRQLAH SVARLCRLKR LILLVANDWR LAAEIGADGV HLAEGLARHG LTASCRLWRR RHGALLSVAA HSALALGRAA HLGADFCLLS QAFPSRSHPG KPALGPVRFA ILAQSSRLPV IALGGVNRQS WRRLPKFCTH GWAAIDGLCP PK // ID A4VPA0_PSEU5 Unreviewed; 313 AA. AC A4VPA0; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE SubName: Full=MutT/nudix family protein; GN OrderedLocusNames=PST_3163; OS Pseudomonas stutzeri (strain A1501). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=379731; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A1501; RA Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., RA Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., RA Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.; RT "Complete genome sequence of the metabolically versatile and root- RT associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000304; ABP80801.1; -; Genomic_DNA. DR RefSeq; YP_001173643.1; NC_009434.1. DR ProteinModelPortal; A4VPA0; -. DR STRING; 379731.PST_3163; -. DR EnsemblBacteria; ABP80801; ABP80801; PST_3163. DR GeneID; 5096124; -. DR KEGG; psa:PST_3163; -. DR PATRIC; 19966864; VBIPseStu31643_3176. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PSTU379731:GJER-3157-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 313 AA; 33629 MW; 1824C18CD9D39A38 CRC64; MKRIHVAAAV IRGADARVLI AKRPLDKHQG GLWEFPGGKV EADERVEAAL ARELLEELGI VVTAAQPLIQ VRHDYPDKQV LLDVWEVHAF TGEPHGAEGQ PLMWVTADQL TNYSFPAANQ PIVAAARLPH CYLITPDGIA PQRLLEGLAR ALDDGIRLIQ LRVPSLPPAA YRALAERALA LCEGQAQLML KGPLQWACDY PGAGWHLTAG QLREQAGRER PIAASRWLAA SCHDAEELAL AAVLGVDFVT LSPVLATASH PDASPLGWPQ VADLLLGFDR PAYLLGGLQA SDLSAARQAG AQGVAAIRAF WPD // ID A4VUB2_STRSY Unreviewed; 245 AA. AC A4VUB2; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SSU05_0735; OS Streptococcus suis (strain 05ZYH33). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=391295; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=05ZYH33; RX PubMed=17375201; DOI=10.1371/journal.pone.0000315; RG BGI; RA Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., RA Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., RA Ju A., Ge J., Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., RA Wang X., Gao G.F., Yang R., Wang J., Yu J.; RT "A glimpse of streptococcal toxic shock syndrome from comparative RT genomics of S. suis 2 Chinese isolates."; RL PLoS ONE 2:E315-E315(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000407; ABP89701.1; -; Genomic_DNA. DR RefSeq; YP_001198101.1; NC_009442.1. DR ProteinModelPortal; A4VUB2; -. DR STRING; 391295.SSU05_0735; -. DR EnsemblBacteria; ABP89701; ABP89701; SSU05_0735. DR GeneID; 5099562; -. DR KEGG; ssu:SSU05_0735; -. DR PATRIC; 19773227; VBIStrSui128929_0716. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSUI391295:GHI8-795-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 153 155 THZ-P binding (By similarity). FT REGION 205 206 THZ-P binding (By similarity). FT METAL 90 90 Magnesium (By similarity). FT METAL 109 109 Magnesium (By similarity). FT BINDING 89 89 HMP-PP (By similarity). FT BINDING 127 127 HMP-PP (By similarity). FT BINDING 156 156 HMP-PP (By similarity). FT BINDING 185 185 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 245 AA; 26871 MW; 96823B742012E353 CRC64; MQSNQKRLKK IKRSFIMNRK MLQVYFMCGT SDCPKGKFLD VLEKALQAGI TCFQFREKGE QGLTGADKLL LAKQVQHLCH RYQVPLIIND DVELARAIDA DGIHLGQEDL SVVEARQLFP GKIIGLSVGT KEEYLNSPID LVDYIGSGPV FPTLSKDDAS PAIGMDGLKQ LRKLNSDIPM VAIGGLSAKD CKEVLQAGAD GIAVISAISH AEDPYKATKI LVDGMQAMIL KFNQVESNKQ ILKNP // ID A4WQ26_RHOS5 Unreviewed; 203 AA. AC A4WQ26; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rsph17025_0584; OS Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=349102; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17025 / ATH 2.4.3; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P., RA Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.; RT "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC RT 17025."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000661; ABP69490.1; -; Genomic_DNA. DR RefSeq; YP_001166795.1; NC_009428.1. DR ProteinModelPortal; A4WQ26; -. DR STRING; 349102.Rsph17025_0584; -. DR EnsemblBacteria; ABP69490; ABP69490; Rsph17025_0584. DR GeneID; 5082889; -. DR KEGG; rsq:Rsph17025_0584; -. DR PATRIC; 23159301; VBIRhoSph94549_0591. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RSPH349102:GHE1-1913-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 20422 MW; 496983356B8BA756 CRC64; MNLTLYFVTP DGAADPEALA VAAVRGGATL VQLRDKRRSD AELVPLARRL IAALDPFGVP LIVNDRVEVV LAAGAAGLHV GLGDLGIEEA RRRIGPDRLL GLSVEAPGHL QALPLGIVDY VGVGPVRATA SKPDHAPPIG FDGLARLVAA APVPAVAIGG LGAGDARAVK AAGADGLAVV SAIGSAADPE AAARALAEEW RQA // ID A4WZ52_RHOS5 Unreviewed; 206 AA. AC A4WZ52; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 38. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=Rsph17025_3809; OS Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3). OG Plasmid pRSPA01. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=349102; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17025 / ATH 2.4.3; PLASMID=pRSPA01; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P., RA Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.; RT "Complete sequence of plasmid pRSPA01 of Rhodobacter sphaeroides ATCC RT 17025."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000662; ABP72666.1; -; Genomic_DNA. DR RefSeq; YP_001169971.1; NC_009429.1. DR ProteinModelPortal; A4WZ52; -. DR STRING; 349102.Rsph17025_3809; -. DR EnsemblBacteria; ABP72666; ABP72666; Rsph17025_3809. DR GeneID; 5085350; -. DR KEGG; rsq:Rsph17025_3809; -. DR PATRIC; 23166109; VBIRhoSph94549_3945. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RSPH349102:GHE1-1123-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Plasmid. SQ SEQUENCE 206 AA; 22164 MW; AA1AB871EE5B4C1D CRC64; MAEAERPQIY LITPPEIDLG IFPDRLARVL DATGIACLRL ALAGKDEDRI ARAADALREV AHARDVAIVI ENHVLMVERL GLDGVHLTDG ARLVRKLRKD LGPDAIVGAF CGRSRHEGIN AAEAGTDYVS FGPVGATALG DGSLAETDLF AWWSEMIEVP VVAEGALTRE KVAELAPVTD FYAVGEEIWR EEDAAEALRS LLSPLG // ID A4XBK8_SALTO Unreviewed; 202 AA. AC A4XBK8; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Strop_3885; OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Salinispora. OX NCBI_TaxID=369723; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., RA Udwary D.W., Richardson P.; RT "Complete sequence of Salinispora tropica CNB-440."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000667; ABP56315.1; -; Genomic_DNA. DR RefSeq; YP_001160693.1; NC_009380.1. DR ProteinModelPortal; A4XBK8; -. DR STRING; 369723.Strop_3885; -. DR EnsemblBacteria; ABP56315; ABP56315; Strop_3885. DR GeneID; 5060363; -. DR KEGG; stp:Strop_3885; -. DR PATRIC; 23446964; VBISalTro43511_4010. DR eggNOG; NOG131844; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VMRAEDP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; STRO369723:GI49-3934-MONOMER; -. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 20537 MW; B3AF1BBF9A324C4F CRC64; MTGPTGLVVL TDRRAARRPL VEVVADAVAG GVRWVVLRER DLPRAERAAL AGDLRRVLTP VGGTLLVAGP DPLGGSAVHL SAAGPYPPPR PGLVGRSCHD EAELGRLTTE DYATLSPIFP TRTKPGYGPP LLPAGLATLI EASPVPVVAL GGIGTAGQVR DCVTAGAVGV AVLGAIMRAE DPRAVATALQ GVFNTVPSGG KR // ID A4XQT6_PSEMY Unreviewed; 313 AA. AC A4XQT6; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 55. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=Pmen_0934; OS Pseudomonas mendocina (strain ymp). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=399739; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ymp; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., RA Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Hersman L., Dubois J., Maurice P., RA Richardson P.; RT "Complete sequence of Pseudomonas mendocina ymp."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000680; ABP83702.1; -; Genomic_DNA. DR RefSeq; YP_001186434.1; NC_009439.1. DR ProteinModelPortal; A4XQT6; -. DR STRING; 399739.Pmen_0934; -. DR EnsemblBacteria; ABP83702; ABP83702; Pmen_0934. DR GeneID; 5108792; -. DR KEGG; pmy:Pmen_0934; -. DR PATRIC; 19908300; VBIPseMen131592_0943. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMEN399739:GHR6-939-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 313 AA; 34240 MW; ACFB0D4B3D14EEA7 CRC64; MRRVHVAAAV IRGVDGRILI ARRPQDKHQG GLWEFPGGKV EEGEAVRVAL DRELEEELGI RPQAARPLIQ IRHDYPDKQV LLDVWEVSAF SGEPHGAEGQ PLAWVSERQL LEYEFPAANK PIVAAARLPE RYLITPDGLE PSELLAGIRS ALAQGVRLIQ LRAPNMFDAQ YRDLAVDVQG LCAGKAQLML KGPLEWLGDF PAAGWHLTAE QLRRYAAGGR PFPEDRWLAA SCHSAEELAL ASQMGVDFAT LSPLQATATH PEAPPLGWEA ASEMLTHFNL PAYLLGGVGP GDIERAWQTG AQGVAGIRAF WPQ // ID A4Y6R3_SHEPC Unreviewed; 637 AA. AC A4Y6R3; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 54. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Sputcn32_1923; OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=319224; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CN-32 / ATCC BAA-453; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Romine M.F., Fredrickson J., Tiedje J., Richardson P.; RT "Complete sequence of Shewanella putrefaciens CN-32."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000681; ABP75646.1; -; Genomic_DNA. DR RefSeq; YP_001183445.1; NC_009438.1. DR ProteinModelPortal; A4Y6R3; -. DR STRING; 319224.Sputcn32_1923; -. DR EnsemblBacteria; ABP75646; ABP75646; Sputcn32_1923. DR GeneID; 5078543; -. DR KEGG; spc:Sputcn32_1923; -. DR PATRIC; 23552660; VBIShePut135485_2010. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SPUT319224:GHAP-1981-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 637 AA; 67381 MW; A4290064A0CE87B1 CRC64; MSTARPAIVW TIAGSDSGGG AGIQADLATI QDLGCHGCSV ITTVTAQSSV AVTLVEPVSA AMLMAQLTTL LSDLPPKAIK IGLLADQSQV ALLADWIASF KIHYPSVPVI VDPVMVASCG DALAVDNCQD IKSTAKSALD FNPFKGLIEL ITPNVLELGR LTHSDVPTKA QFAAAAQALS QSLDCSVLAK GGDVSFGCTD ILDDTHAKTH DNTHAQTQAN VHVSTLDSNG WDHGLAEDYL VCHQVRASSE LHQNGCFWLA SQRVNTRHNH GSGCTLSSAI AAVLAQGFVL QDAVVVAKAY VSQGLSAAIG LGQGPGPLAR TGWPNDLSRY AKIRLCDGNF ISHKLNQHLD IVNDLVETVL SATDQATAQV VRIASTPAQC ISSHGFKILD ADLGVYPVVS DLTMLESLLA AGVKTLQLRI KTDISELSSA APAESDLGKC ESGKSELVGS ELEAQIQTAI ALGKHFNAQL FINDHWQLAI KYHAFGVHLG QEDLAVTDLE AIQSAGLALG ISSHSYFELL LAHQYSPSYI ALGHIFPTTT KQMPSAPQGL AKLKHYVALL QDHYPLVAIG GIDLDNLAKV KATGVGNIAV VRAITEAQDP VAAFAQLSQA WEQCSLSEEL AAKHEFDVKH KLDAKYE // ID A4YLD7_BRASO Unreviewed; 121 AA. AC A4YLD7; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 16-APR-2014, entry version 35. DE SubName: Full=Putative Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=BRADO0790; OS Bradyrhizobium sp. (strain ORS278). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=114615; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ORS278; RX PubMed=17540897; DOI=10.1126/science.1139548; RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C., RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., RA Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., RA Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B., RA Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C., RA Sadowsky M.; RT "Legumes symbioses: absence of nod genes in photosynthetic RT bradyrhizobia."; RL Science 316:1307-1312(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU234118; CAL74713.1; -; Genomic_DNA. DR RefSeq; YP_001202950.1; NC_009445.1. DR ProteinModelPortal; A4YLD7; -. DR STRING; 114615.BRADO0790; -. DR EnsemblBacteria; CAL74713; CAL74713; BRADO0790. DR GeneID; 5115240; -. DR KEGG; bra:BRADO0790; -. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BSP114615:GJN5-750-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 121 AA; 13098 MW; 40CAD9A00DB0B789 CRC64; MPFDLRLYAI VDPEQARGRD LADLARRCVE GGATLVQLRD KRSSKGAFVE QARAIKSALA PHGAQLIIND RIDVVLDSGA DGVHIGPDDI TAEDTAACSV PVQSSACRSN RRPKPRQPLW P // ID A4YLD8_BRASO Unreviewed; 90 AA. AC A4YLD8; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 16-APR-2014, entry version 33. DE SubName: Full=Thiamine-phosphate pyrophosphorylase (EC 2.5.1. 3) (TMP pyrophosphorylase) (TMP-PPase) (Thiamine-phosphate synthase); DE EC=2.5.1.3; GN OrderedLocusNames=BRADO0791; OS Bradyrhizobium sp. (strain ORS278). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=114615; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ORS278; RX PubMed=17540897; DOI=10.1126/science.1139548; RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C., RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., RA Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., RA Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B., RA Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C., RA Sadowsky M.; RT "Legumes symbioses: absence of nod genes in photosynthetic RT bradyrhizobia."; RL Science 316:1307-1312(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU234118; CAL74714.1; -; Genomic_DNA. DR RefSeq; YP_001202951.1; NC_009445.1. DR STRING; 114615.BRADO0791; -. DR EnsemblBacteria; CAL74714; CAL74714; BRADO0791. DR GeneID; 5115241; -. DR KEGG; bra:BRADO0791; -. DR PATRIC; 21217837; VBIBraSp122330_0747. DR KO; K00788; -. DR BioCyc; BSP114615:GJN5-751-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 90 AA; 9352 MW; 382E4CABAB1945FD CRC64; MRRCLASSSK EQQQAPIGLD GLARILAVLR RRAPKLPVCA NAGIHAANAA SVIAAGADGV AVISALSRSP DPRAAAQLRH VVDHELAARR // ID A4YMA5_BRASO Unreviewed; 224 AA. AC A4YMA5; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 40. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase (Thiamin phosphate synthase/diphosphorylase); DE EC=2.5.1.3; GN OrderedLocusNames=BRADO1119; OS Bradyrhizobium sp. (strain ORS278). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=114615; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ORS278; RX PubMed=17540897; DOI=10.1126/science.1139548; RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C., RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., RA Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., RA Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B., RA Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C., RA Sadowsky M.; RT "Legumes symbioses: absence of nod genes in photosynthetic RT bradyrhizobia."; RL Science 316:1307-1312(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU234118; CAL75031.1; -; Genomic_DNA. DR RefSeq; YP_001203268.1; NC_009445.1. DR ProteinModelPortal; A4YMA5; -. DR STRING; 114615.BRADO1119; -. DR EnsemblBacteria; CAL75031; CAL75031; BRADO1119. DR GeneID; 5114944; -. DR KEGG; bra:BRADO1119; -. DR PATRIC; 21218473; VBIBraSp122330_1065. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BSP114615:GJN5-1069-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 224 AA; 22983 MW; C17A2F204A69A7A8 CRC64; MSGKSTPARP EPRIYLATPV VTDAAALAAS LPVILASADV AAVLVRLKES DPRSMITTVK TLAPVIQGTG AALLIDGHPD IVARAGADGA HLTGIAALEE ALPGLKPDRI AGGGGLSTRH DSMRAGELGA DYVLFGERDA QGRRPSPDAV NERLAWWAEL FEPPCVGYAI SLKEAADFVA AGADFVLVDD LVWNDERGPA AALADIGATI RQAHAAAPIA IAGS // ID A4YQE2_BRASO Unreviewed; 289 AA. AC A4YQE2; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=BRADO2283; OS Bradyrhizobium sp. (strain ORS278). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=114615; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ORS278; RX PubMed=17540897; DOI=10.1126/science.1139548; RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C., RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., RA Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., RA Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B., RA Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C., RA Sadowsky M.; RT "Legumes symbioses: absence of nod genes in photosynthetic RT bradyrhizobia."; RL Science 316:1307-1312(2007). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU234118; CAL76118.1; -; Genomic_DNA. DR RefSeq; YP_001204355.1; NC_009445.1. DR ProteinModelPortal; A4YQE2; -. DR STRING; 114615.BRADO2283; -. DR EnsemblBacteria; CAL76118; CAL76118; BRADO2283. DR GeneID; 5119621; -. DR KEGG; bra:BRADO2283; -. DR PATRIC; 21220755; VBIBraSp122330_2200. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BSP114615:GJN5-2163-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 289 AA; 30489 MW; 6A3D37EA14A57E6A CRC64; MSPPLIDVAV AVVQEPSGRV LLAERTARQV AAGFWELPGG KIEPGEAAAE AAARELSEEI GIHATGLRPW LCYVHAFPTK RVRLHIHRVE SWRGTPHGRE GQRLAWVDPA APSVAPVLPS NGRAMSALGL PRLLACIDVN DVSGAVAAAR AARDRGAGLI IVRAPQCAPG QRVALARRII AAAADLRVLL EGPALEAQRA GAHGAFVGPA NLRRSTVRPN LPLWGAACSD SNDLVLAAHL GADFAIATPA HPASSRTPHF TMFRTDDTAA PLPLFKTADK TIRDTSRPS // ID A4YZQ5_BRASO Unreviewed; 202 AA. AC A4YZQ5; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BRADO5712; OS Bradyrhizobium sp. (strain ORS278). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=114615; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ORS278; RX PubMed=17540897; DOI=10.1126/science.1139548; RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C., RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., RA Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., RA Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B., RA Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C., RA Sadowsky M.; RT "Legumes symbioses: absence of nod genes in photosynthetic RT bradyrhizobia."; RL Science 316:1307-1312(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU234118; CAL79381.1; -; Genomic_DNA. DR RefSeq; YP_001207598.1; NC_009445.1. DR ProteinModelPortal; A4YZQ5; -. DR STRING; 114615.BRADO5712; -. DR EnsemblBacteria; CAL79381; CAL79381; BRADO5712. DR GeneID; 5117848; -. DR KEGG; bra:BRADO5712; -. DR PATRIC; 21227379; VBIBraSp122330_5486. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BSP114615:GJN5-5458-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 29 33 HMP-PP binding (By similarity). FT REGION 178 179 THZ-P binding (By similarity). FT METAL 62 62 Magnesium (By similarity). FT METAL 81 81 Magnesium (By similarity). FT BINDING 61 61 HMP-PP (By similarity). FT BINDING 100 100 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 202 AA; 21447 MW; 651F097CC8C64911 CRC64; MPYPDRFYPV VDSLAWVERL TRLGVGTVQL RAKNLDDAAA LQIVTDALAI TRGTATKLIV NDYWRAAIAA GAAHVHLGQE DLAEADVKAI KDAGLTLGLS THDDAELETA LAAKPDYVAL GPIFPTTLKA MRFAPQGIPK ISVWKQRVGS IPLVAIGGIK LEQAAEIFAA GADSIAVVSD VTQNADPDAR VRAWLDATKE PA // ID A5CSW1_CLAM3 Unreviewed; 743 AA. AC A5CSW1; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE SubName: Full=Thiamine-phosphate synthase/phosphomethylpyrimidine kinase; DE EC=2.5.1.3; GN Name=thiED; OrderedLocusNames=CMM_2116; OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Microbacteriaceae; Clavibacter. OX NCBI_TaxID=443906; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 382; RX PubMed=18192381; DOI=10.1128/JB.01595-07; RA Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., RA Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., RA Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., RA Rueckert C., Schneiker S., Zellermann E.-M., Puehler A., RA Eichenlaub R., Kaiser O., Bartels D.; RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter RT michiganensis subsp. michiganensis NCPPB382 reveals a large island RT involved in pathogenicity."; RL J. Bacteriol. 190:2138-2149(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM711867; CAN02185.1; -; Genomic_DNA. DR RefSeq; YP_001222861.1; NC_009480.1. DR ProteinModelPortal; A5CSW1; -. DR STRING; 443906.CMM_2116; -. DR EnsemblBacteria; CAN02185; CAN02185; CMM_2116. DR GeneID; 5175026; -. DR KEGG; cmi:CMM_2116; -. DR PATRIC; 21455069; VBIClaMic82482_2241. DR eggNOG; COG0351; -. DR HOGENOM; HOG000225275; -. DR KO; K14153; -. DR OMA; RHELEFF; -. DR OrthoDB; EOG6WHP06; -. DR BioCyc; CMIC443906:GCI2-2183-MONOMER; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.910.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF03070; TENA_THI-4; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; SSF48613; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 743 AA; 76065 MW; A94EC4C96811D72D CRC64; MSALDLSVYL VTDPALCGAR GVPAVVAAAV AGGAMAVQIR DKHASAAELL ATVVAAAEAI DAHAAAHPSA RRPLLLVDDR VDVVLAALAR GVRVDGVHVG QSDVPADLVR RMLDAASPDR RLVVGLTANT PAHVEAVRAL PAGTVDYLGV GVIRPTSTKP DHPAPLGHDG FGIIAGLSPV PCVAIGGVDV RDVAAIAAAG GAGTAVVSAI CAGEDPGAAA RELAEAWARV RAAAGDATAA EDDASARALR PVPRVLSIAG TDPTGGAGIQ ADLKSIAANG GYGMAVVTAL VAQNTTGVRE IHVPPVAFLR AQLDAVSDDV AIDAVKIGML GSAAVVDEVA DWLRAVRPPV VVLDPVMVAQ SGDALLDADA TEALRRLLPL ADVVTPNLPE LAALLGEREA DGWDEALAQG RTLAVRHGVR VVVKGGHLRV DDCPDALVTP GAAGAEAAVH VVDGPRITTT STHGTGCSLS SALATLHPRR GDWLSALTEA KAWLTGSLAH AEDLEVGSGA GPLDHLRALW DAAGTHAGPI SAEMWAGSAD LRREIDDLAF VRRLGDGTLP EAWFSHYLAQ DAIYLRAYSR VLARASQLAP TPDAQVVWAR SAADAIAAES TLHEEWLSRH PAPAVAGPVT RAYVDHLLAH AATSDYAVLV AALLPCFTIY ADVGTRLRAA GSAAASAGEA HPYAAWLATY ADPGFAAATR RACELVDEAA VIAGPSRRTA MLEASLLSSA YERDFFRAPE ALG // ID A5CVJ5_VESOH Unreviewed; 204 AA. AC A5CVJ5; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 13-NOV-2013, entry version 37. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=COSY_0918; OS Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA). OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=412965; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HA; RX PubMed=17493812; DOI=10.1016/j.cub.2007.04.039; RA Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M., RA Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., RA Sato T., Kato C., Kitagawa M., Kato I., Maruyama T.; RT "Reduced genome of the thioautotrophic intracellular symbiont in a RT deep-sea clam, Calyptogena okutanii."; RL Curr. Biol. 17:881-886(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009247; BAF62017.1; -; Genomic_DNA. DR RefSeq; YP_001219741.1; NC_009465.1. DR ProteinModelPortal; A5CVJ5; -. DR STRING; 412965.COSY_0918; -. DR EnsemblBacteria; BAF62017; BAF62017; COSY_0918. DR GeneID; 5171857; -. DR KEGG; vok:COSY_0918; -. DR PATRIC; 32021715; VBICanVes128383_0918. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K03574; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CVES412965:GHZZ-918-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 204 AA; 23304 MW; C4148F8D2B0E07AD CRC64; MILNKQLDDY KLLPVMKTFI NSIALPDKYW ITPSNNHQSN KWMEKFNQKL TQNIKLIQLR SKTKINNNFI QQLHNKCKQH NIQLLLNTVN KTFNEAYCDG WNLTTAEMLK FKKRPCTNNK LLGVSTHNLT EALKAQIIGA DFVIISPVQA TKTHPKLLPL GWDNAKEVVN TLNIPVYFLG GMRLQDLKKT QQLGAQGIAG VSTF // ID A5CXW4_VESOH Unreviewed; 193 AA. AC A5CXW4; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=COSY_0087; OS Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA). OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=412965; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HA; RX PubMed=17493812; DOI=10.1016/j.cub.2007.04.039; RA Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M., RA Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., RA Sato T., Kato C., Kitagawa M., Kato I., Maruyama T.; RT "Reduced genome of the thioautotrophic intracellular symbiont in a RT deep-sea clam, Calyptogena okutanii."; RL Curr. Biol. 17:881-886(2007). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009247; BAF61223.1; -; Genomic_DNA. DR RefSeq; YP_001218947.1; NC_009465.1. DR ProteinModelPortal; A5CXW4; -. DR STRING; 412965.COSY_0087; -. DR EnsemblBacteria; BAF61223; BAF61223; COSY_0087. DR GeneID; 5172287; -. DR KEGG; vok:COSY_0087; -. DR PATRIC; 32019985; VBICanVes128383_0086. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CIGGINE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CVES412965:GHZZ-88-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 193 AA; 21623 MW; A94AE9D9D79CDA0C CRC64; MVFNKKISHI YAITPDVSLN SILIRWVINK HHISILQYRH KTNNNNMKLK EAYVLRQLCL VHNTLFIIND DINLTEKVHA DGVHLGKDDG SIQQARQQLG IDSIIGISCY NDINLAFQAQ KQGANYVTFG ALFDSKTKPN APHCPLNVIT KAKQILHIPI VGIGGIDLYN QQQAFDAGCD AVAMINALFK NYN // ID A5DMZ3_PICGU Unreviewed; 417 AA. AC A5DMZ3; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 2. DT 16-APR-2014, entry version 41. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=PGUG_04644; OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM OS 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Meyerozyma. OX NCBI_TaxID=294746; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL RC Y-324; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., RA Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., RA Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D., RA Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., RA Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., RA Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., RA Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., RA Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., RA Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., RA Kellis M., Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH408160; EDK40546.2; -; Genomic_DNA. DR RefSeq; XP_001482689.1; XM_001482639.1. DR ProteinModelPortal; A5DMZ3; -. DR STRING; 4929.A5DMZ3; -. DR GeneID; 5124802; -. DR KEGG; pgu:PGUG_04644; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 417 AA; 45551 MW; 5A95E37EC00B94D7 CRC64; MRSAHRWNIF REKSIPTVQF AMVDYSVYLV TDSSMIPESS TFLKQVENAI DNGATMVQLR EKTMATRDFI DRALAIKRMT EKKGIPLIIN DRVDVALAVD ADGVHVGQDD MEAVTVRRLI GPNKILGVTC SYPHEVEKVC EDGIADYVGL GTVYKTATKK DVKTPEGTGP IGIRKMLHVL EKHKANIKAV AIGGINHSNA AKVLFQCRIP GRALDGLAVV SCIMADPDAS AATQSLAKIV REKEFGKDKK NSGREEGKET EVIRAVRASN PLVHHITNNV VKNFCANVTL AVGASPIMSE FAEEYDELAQ NIEKLALVIN LGTPNSSTMD IFKHALQVYN KHGKPVVFDP VAAGASAARF ECCRQILNAG QVSVIKGNVG RDHVSLQTYS RVYTRRGRQS AHEGSRLGGG LECRKDN // ID A5DXB6_LODEL Unreviewed; 553 AA. AC A5DXB6; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 16-APR-2014, entry version 40. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=LELG_02003; OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / OS NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Lodderomyces. OX NCBI_TaxID=379508; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., RA Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., RA Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D., RA Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., RA Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., RA Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., RA Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., RA Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., RA Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., RA Kellis M., Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH981525; EDK43824.1; -; Genomic_DNA. DR RefSeq; XP_001527174.1; XM_001527124.1. DR ProteinModelPortal; A5DXB6; -. DR STRING; 36914.A5DXB6; -. DR GeneID; 5234202; -. DR KEGG; lel:LELG_02003; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 2. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 553 AA; 59840 MW; C0C7D82D8DE0E8E4 CRC64; MSELNDDLFK LYLVTDSTMI PESKTFLGQI EEAVNNGVTI VQLREKKLST REFIKRAQQV HALTKPRGIP LIINDRVDVA LAIDAEGVHV GQDDMPATSV RELIGPNKIL GVTCSTPEEA QEVVDQDVAD YVGLGTVYAT NTKKDVTNPD GVGPIGIKSM LLVLAKHKRD IKSVAIGGIN HSNAKFVQSA CRVPGRSISG PAVVSCIMAS QDAGNATKKL KEILESCAKE RGVDTIGTEQ HQRNQDSFSD FRVTGAYKQK NKLKTLVQSH PLVHHITNNV VKNFSANVTL AIGASPIMSE LPTEFEEFTS KIPNLALVLN LGTPNEELMK VFAKAISAYN MYNKPIVFDP VACGASQARL SCCRKLLNTG HMTVIKGNLG EIVSIWKLTQ CYNLLNLGDD LMHGVDSVAD VSEDILFKIA SDILYDFNAT LVITGQVNYV FATDGKRYEK IAGGSLLMSL VTGTGCSLGS VIAAFLAARA DGLNDGEIDN VEKNEKNTIS QSNSCDNYSC VVAAVSLYNE AGRNAASKTS APSSFMTAFI DELYKLTHER LET // ID A5EPQ4_BRASB Unreviewed; 202 AA. AC A5EPQ4; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BBta_6225; OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=288000; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BTAi1 / ATCC BAA-1182; RX PubMed=17540897; DOI=10.1126/science.1139548; RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C., RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., RA Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., RA Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B., RA Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C., RA Sadowsky M.; RT "Legumes symbioses: absence of nod genes in photosynthetic RT bradyrhizobia."; RL Science 316:1307-1312(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000494; ABQ38148.1; -; Genomic_DNA. DR RefSeq; YP_001242054.1; NC_009485.1. DR ProteinModelPortal; A5EPQ4; -. DR STRING; 288000.BBta_6225; -. DR EnsemblBacteria; ABQ38148; ABQ38148; BBta_6225. DR GeneID; 5149211; -. DR KEGG; bbt:BBta_6225; -. DR PATRIC; 21213135; VBIBraSp29847_6222. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BSP288000:GJBR-5967-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 29 33 HMP-PP binding (By similarity). FT REGION 178 179 THZ-P binding (By similarity). FT METAL 62 62 Magnesium (By similarity). FT METAL 81 81 Magnesium (By similarity). FT BINDING 61 61 HMP-PP (By similarity). FT BINDING 100 100 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 202 AA; 21677 MW; DE1E0FFDD073C5C4 CRC64; MPYPDRFYPV VDSLAWVERL TKLGVGTVQL RAKDLNDGEA LQIVTDALEI TKGTATKLIV NDYWRAAIVA GAEHLHLGQE DLADADVRAI KQAGLTLGLS THDDAELENA LAAEPDYVAL GPIFPTTLKA MRFAPQGIPK ISVWKQRVGN IPLVAIGGIK LEQAAEIFAA GADSIAVVSD VTQNADPDAR VRAWLDATKE LA // ID A5ERM3_BRASB Unreviewed; 225 AA. AC A5ERM3; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 41. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase (Thiamin phosphate synthase/diphosphorylase); DE EC=2.5.1.3; GN OrderedLocusNames=BBta_6930; OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=288000; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BTAi1 / ATCC BAA-1182; RX PubMed=17540897; DOI=10.1126/science.1139548; RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C., RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., RA Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., RA Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B., RA Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C., RA Sadowsky M.; RT "Legumes symbioses: absence of nod genes in photosynthetic RT bradyrhizobia."; RL Science 316:1307-1312(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000494; ABQ38817.1; -; Genomic_DNA. DR RefSeq; YP_001242723.1; NC_009485.1. DR ProteinModelPortal; A5ERM3; -. DR STRING; 288000.BBta_6930; -. DR EnsemblBacteria; ABQ38817; ABQ38817; BBta_6930. DR GeneID; 5149819; -. DR KEGG; bbt:BBta_6930; -. DR PATRIC; 21214519; VBIBraSp29847_6909. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6F55F7; -. DR BioCyc; BSP288000:GJBR-6648-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 225 AA; 23127 MW; 50F4124C8AB9A4D7 CRC64; MSDKTAPARP APRLYLATQM VTDPAPLAAS LPAILGSADV AAVLVRLKET DPRSMITTVK ALAPAIQGTG AALLIDGHPD IVARAGADGA HLTGIKVLEE ALPGLKPDRI AGIGGLSTRH DSMRAGELGA DYVLFGERDA HGRRPSPDAI NERLAWWAEL FEPPCVGYAI SLKEAADFVA AGADFVLVDD LVWNDARGPA AALAEIGATI RAAHAAAPVA PAGQG // ID A5F4D1_VIBC3 Unreviewed; 440 AA. AC A5F4D1; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=VC0395_A2451, VC395_0118; OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / OS O395). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=345073; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395, and O395; RA Heidelberg J.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395, and O395; RX PubMed=19115014; DOI=10.1371/journal.pone.0004053; RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., RA Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.; RT "A recalibrated molecular clock and independent origins for the RT cholera pandemic clones."; RL PLoS ONE 3:E4053-E4053(2008). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000627; ABQ21206.1; -; Genomic_DNA. DR EMBL; CP001235; ACP08146.1; -; Genomic_DNA. DR RefSeq; YP_001218351.1; NC_009457.1. DR RefSeq; YP_002818382.1; NC_012582.1. DR STRING; 345073.VC0395_A2451; -. DR EnsemblBacteria; ABQ21206; ABQ21206; VC0395_A2451. DR EnsemblBacteria; ACP08146; ACP08146; VC395_0118. DR GeneID; 5136648; -. DR GeneID; 7774220; -. DR KEGG; vco:VC0395_A2451; -. DR KEGG; vcr:VC395_0118; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RIKDSTH; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48877 MW; 5602F84C24A2F3D8 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPHQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID A5FJJ3_FLAJ1 Unreviewed; 203 AA. AC A5FJJ3; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 39. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Fjoh_1602; OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) OS (Cytophaga johnsonae). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=376686; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17061 / DSM 2064 / UW101; RX PubMed=19717629; DOI=10.1128/AEM.01495-09; RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., RA Rhodes R.G., Goltsman E., Wang W., Xu J., Hunnicutt D.W., RA Staroscik A.M., Hoover T.R., Cheng Y.Q., Stein J.L.; RT "Novel features of the polysaccharide-digesting gliding bacterium RT Flavobacterium johnsoniae as revealed by genome sequence analysis."; RL Appl. Environ. Microbiol. 75:6864-6875(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000685; ABQ04634.1; -; Genomic_DNA. DR RefSeq; YP_001193953.1; NC_009441.1. DR ProteinModelPortal; A5FJJ3; -. DR STRING; 376686.Fjoh_1602; -. DR EnsemblBacteria; ABQ04634; ABQ04634; Fjoh_1602. DR GeneID; 5090953; -. DR KEGG; fjo:Fjoh_1602; -. DR PATRIC; 21897543; VBIFlaJoh53613_1647. DR eggNOG; NOG86118; -. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR OrthoDB; EOG6RC3V1; -. DR BioCyc; FJOH376686:GIXN-1633-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 203 AA; 23381 MW; CDAA802015BEB48B CRC64; MIVITNPFSI KNEIEILHSL LEEGLSLLHI RKPDFSEIEM AHFIHQIKLE FRGNLFLHSH HDLAEDFGIT RIHFSEKERK DLNDFPARFL KPCRSKSTST HSIEDFNSLE SDFDYAFLSP VFKSISKENY QPETDLFEAL KSRKNYKTKA IALGGICSDN ISKTLINGFD DVALLGTIWN NENPVKQFKI CQQTVLSYLQ SQA // ID A5FR88_DEHMB Unreviewed; 352 AA. AC A5FR88; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=DehaBAV1_0708; OS Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 OS / BAV1). OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales; OC Dehalococcoidaceae; Dehalococcoides. OX NCBI_TaxID=216389; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAV1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S., RA Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Ritalahti K.M., Loeffler F., Richardson P.; RT "Complete sequence of Dehalococcoides sp. BAV1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000688; ABQ17292.1; -; Genomic_DNA. DR RefSeq; YP_001214170.1; NC_009455.1. DR ProteinModelPortal; A5FR88; -. DR STRING; 216389.DehaBAV1_0708; -. DR EnsemblBacteria; ABQ17292; ABQ17292; DehaBAV1_0708. DR GeneID; 5131462; -. DR KEGG; deb:DehaBAV1_0708; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DSP216389:GH6D-726-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 179 183 HMP-PP binding (By similarity). FT REGION 276 278 THZ-P binding (By similarity). FT REGION 326 327 THZ-P binding (By similarity). FT METAL 212 212 Magnesium (By similarity). FT METAL 231 231 Magnesium (By similarity). FT BINDING 211 211 HMP-PP (By similarity). FT BINDING 250 250 HMP-PP (By similarity). FT BINDING 279 279 HMP-PP (By similarity). FT BINDING 306 306 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 352 AA; 38361 MW; 0017FC8988EF8675 CRC64; MDNLEKLWRI VDVNQNRLSE GLRILEEIAR LYLENETLTL RLKNLRHALT LQDTASNCHL LFSRQADTDI GAHLKTVDQS KPETLFSLIS ANAKRAEQSL RVLEEFAGLL ELGFDTSIYS RGRFELYTLE KDLAAILLRK NRRDMIKGLY VAIDVDYLAG RDIPRVTKEV LEGGCRLVQL RAKTASARQF LSLALSLKEL CIEYGAVFIV NDRLDIALAC GADGLHLGQT DLPLSQARCL MPAGSIIGIS ADSPEDAASA QAGDADYVAA GAVFPTQTKL DVLYGGLSGL KAIRQVVNIP LVAIGGINKS NYNEALQAGA DSLCLISAVL GAPDIKKATS EFMTLVEAEK ND // ID A5FVH4_ACICJ Unreviewed; 206 AA. AC A5FVH4; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Acry_0381; OS Acidiphilium cryptum (strain JF-5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=349163; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JF-5; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T., RA Richardson P.; RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000697; ABQ29606.1; -; Genomic_DNA. DR RefSeq; YP_001233525.1; NC_009484.1. DR ProteinModelPortal; A5FVH4; -. DR STRING; 349163.Acry_0381; -. DR EnsemblBacteria; ABQ29606; ABQ29606; Acry_0381. DR GeneID; 5160296; -. DR KEGG; acr:Acry_0381; -. DR PATRIC; 20645724; VBIAciCry6074_0864. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ACRY349163:GHET-388-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21645 MW; 3C40584C425FBD47 CRC64; MTELYLITPP RLGPDFADAL AAALDAGPVA CVQLRLKEAG ADEMRRAIDA LRPVAQSRGV AFLLNDDPRL AVETGCDGAH LGQDDLAAHG GLARVRRVLD GLSLGITCHD SRHLAMEAAE QGADYVAFGA FYPTGTKEPK ARADVEILRW WSELMEVPCV AIGGITPGNA APLVEAGADF LAVVGAVWQH PDGPAAGVRA FRAELA // ID A5G071_ACICJ Unreviewed; 169 AA. AC A5G071; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 40. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Acry_2053; OS Acidiphilium cryptum (strain JF-5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=349163; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JF-5; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T., RA Richardson P.; RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000697; ABQ31253.1; -; Genomic_DNA. DR RefSeq; YP_001235172.1; NC_009484.1. DR ProteinModelPortal; A5G071; -. DR STRING; 349163.Acry_2053; -. DR EnsemblBacteria; ABQ31253; ABQ31253; Acry_2053. DR GeneID; 5161449; -. DR KEGG; acr:Acry_2053; -. DR PATRIC; 20649176; VBIAciCry6074_2559. DR eggNOG; NOG121918; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NRRDSIM; -. DR OrthoDB; EOG679THR; -. DR BioCyc; ACRY349163:GHET-2090-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 169 AA; 17353 MW; CA2BE134B4720C38 CRC64; MPDPLGAIAR LPPGLSGVVL RDDAAPDRAA LAAAVAKLCR RRRIALVVAG DARLAARLHA GLHLRRGRVA PGRKPGLVTA SAHGRQELVR ARRAGAGLVF LSPAFPTASH PGAPALGPVR WAALARLAGG VQVVALGGIE GRRMRALGPA CRGVAAIGAL SNQCHTVWR // ID A5G7P5_GEOUR Unreviewed; 220 AA. AC A5G7P5; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Gura_3660; OS Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=351605; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rf4; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Shelobolina E., Aklujkar M., Lovley D., Richardson P.; RT "Complete sequence of Geobacter uraniireducens Rf4."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000698; ABQ27813.1; -; Genomic_DNA. DR RefSeq; YP_001232386.1; NC_009483.1. DR ProteinModelPortal; A5G7P5; -. DR STRING; 351605.Gura_3660; -. DR EnsemblBacteria; ABQ27813; ABQ27813; Gura_3660. DR GeneID; 5166602; -. DR KEGG; gur:Gura_3660; -. DR PATRIC; 22037730; VBIGeoUra13052_3915. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VTDRTLC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GURA351605:GI6A-3710-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24257 MW; 5C28953619DBDA72 CRC64; MKTATDSPWI DFNLYLITDR KQTEGRSLEF VVEEALRGGV RAVQLREKDL PSRELYETAY ELRKLTARHN AKLFINDRVD IALAVDADGV HLGYNSIPIY RARKILGEKK LIGVSCHNQV QAIIAQEQGA DFITFGPIYF TQSKAPYGEP VGIVKLAEIT HLLTIPIFAL GGIKPYNVPE VIAAGAHGIA LVSAILSADE PRTAAKTLIS LLPPMEQHEV // ID A5G883_GEOUR Unreviewed; 497 AA. AC A5G883; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE SubName: Full=Phosphomethylpyrimidine kinase; GN OrderedLocusNames=Gura_3851; OS Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=351605; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rf4; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Shelobolina E., Aklujkar M., Lovley D., Richardson P.; RT "Complete sequence of Geobacter uraniireducens Rf4."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000698; ABQ28001.1; -; Genomic_DNA. DR RefSeq; YP_001232574.1; NC_009483.1. DR ProteinModelPortal; A5G883; -. DR STRING; 351605.Gura_3851; -. DR EnsemblBacteria; ABQ28001; ABQ28001; Gura_3851. DR GeneID; 5166062; -. DR KEGG; gur:Gura_3851; -. DR PATRIC; 22038121; VBIGeoUra13052_4109. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OMA; YLAQGEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; GURA351605:GI6A-3903-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 497 AA; 52417 MW; E89E00B00EABC7E0 CRC64; MEHKKDFLRL VVDRETTDSP IKGVYLITDH ADHLTERVRG ALSGGVTVLQ YRNKMGDAED KFTVGMELKT ICAEAGITFI VNDDLELARE LDADGLHLGQ EDGDPIGARK LLGPRKIIGV STHNLEEALR AEAAGADYIG FGAMYPTGSK DIEHLPGPDM LVEVKAKVKI PVVAIGGINR DNGARVIDNG ADAVAVISGI LGSREPGLAA AELSLLFNRK GAFPRGNVLT IAGSDSGGGA GIQADLKTVT LLGSYGASVI TALTAQNTRG VSAIHGVPPE FVAEQLDAVL SDIRIDVVKT GMLFSAEIIS VIADKLGEYN RKIVVIDPVM LAKGGAELID HEALAIFKKR LMAAAYLLTP NIPEAEKLTG IAISNEDGME QAARAICSMG ARNVLIKGGH LPEGIAVDIL YDGSAFTRFP VPRILTKNTH GTGCTLASAI AAFLAQGEPL PVAIAKAKEF ITTAIKLAQP LGKGHGPVNH YRAACELRDL GPGTRDR // ID A5GUT1_SYNR3 Unreviewed; 346 AA. AC A5GUT1; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SynRCC307_1737; OS Synechococcus sp. (strain RCC307). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=316278; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCC307; RG Genoscope; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT978603; CAK28640.1; -; Genomic_DNA. DR RefSeq; YP_001227993.1; NC_009482.1. DR ProteinModelPortal; A5GUT1; -. DR STRING; 316278.SynRCC307_1737; -. DR EnsemblBacteria; CAK28640; CAK28640; SynRCC307_1737. DR GeneID; 5157622; -. DR KEGG; syr:SynRCC307_1737; -. DR PATRIC; 23824403; VBISynSp108374_1749. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 125 Unknown (By similarity). FT REGION 126 346 Thiamine-phosphate synthase (By FT similarity). FT REGION 174 178 HMP-PP binding (By similarity). FT REGION 271 273 THZ-P binding (By similarity). FT METAL 207 207 Magnesium (By similarity). FT METAL 226 226 Magnesium (By similarity). FT BINDING 206 206 HMP-PP (By similarity). FT BINDING 245 245 HMP-PP (By similarity). FT BINDING 274 274 HMP-PP (By similarity). FT BINDING 301 301 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 346 AA; 37641 MW; 6A1A4E89B1894102 CRC64; MTISSEGVDP AVLRLLDANL DRAREGLRVA EDWARFGLDR RDLVEGLKDL RQQLGRCHLP RYRQARHTAT DSAAGLAHPA QQQRSDATVV AANCARAQEA LRVLEEFGRS CDPELARVAE HCRYRLYDLE TRLLADQSRR QRLAAERLYL ITSPVPQLRS VVEQALQAGV KLVQHRSKLT DDLPRYQEAV ALRDLCAAHG ALFIVNDRVD LALAVEADGV HLGQGDLPPA QARRLLGPDR LIGRSTHAPA QLQQAMADGC DYAGVGPLQA TPTKPGREPV GLDYLRQAAQ IATIPHYAIG GVDVQLLPAL LEAGGPHCRV AVVRAVMEAA DPAAAARQLL ELLADG // ID A5IC65_LEGPC Unreviewed; 495 AA. AC A5IC65; DT 26-JUN-2007, integrated into UniProtKB/TrEMBL. DT 26-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE SubName: Full=Phosphomethylpyrimidine kinase ThiD/thiamin-phosphate pyrophosphorylase fused protein ThiE; GN Name=thiDE; OrderedLocusNames=LPC_0992; OS Legionella pneumophila (strain Corby). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=400673; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Corby; RA Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., RA Schunder E., Steinert M., Buchrieser C., Hacker J., Heuner K.; RT "Identification and characterization of a new conjugation/ type IVA RT secretion system (trb/tra) of L. pneumophila Corby localized on a RT mobile genomic island."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000675; ABQ54965.1; -; Genomic_DNA. DR RefSeq; YP_001250311.1; NC_009494.2. DR ProteinModelPortal; A5IC65; -. DR STRING; 400673.LPC_0992; -. DR EnsemblBacteria; ABQ54965; ABQ54965; LPC_0992. DR GeneID; 5180820; -. DR KEGG; lpc:LPC_0992; -. DR PATRIC; 22308395; VBILegPne45588_1032. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; LPNE400673:GCIT-1670-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 495 AA; 54981 MW; A39DAF82526F6F66 CRC64; MKKPIVWTIA GVDSSGLAGV HADMETFSRL NVRACSVITA VTAQNAHSIT AVEAISRDQV AAQCRALELN LKPDAIKIGM LCSTPICEEI AYFLKGYEGF VVLDPIITSS SGTNLFFPDL QQHKENLIQL FPYVTIITPN RIEAEIILNR SISSYQDIIN AASDLLSLGA KQVLLKGGHV KDNSFSQDYW TDGKELFWIA NRRFPETNYR GTGCVLSSAL TACLALGYSI KDAIVIAKMY VNRGIRQSIE LDKDASQLYH DGWPEDEADL PYLSPTPFIK PVPSFKKCSM GFYPIVDSSH WLEMLLPLGI KCIQLRIKEA SQERLEEEIK RSVHLANQYN AALFINDHWE LAIHYGAAGV HLGQEDLEKA DVDRINRAGL FLGISTHCYY EVARAHALNP SYVACGPIYE TTSKIMPFQA QGIARLERWR KTLRYPLVAI GGITLKNLSD VLKTKIDGVS VISAITKASV PLVAAKQFLT QMNESHNEQI KFGNE // ID A5J530_BURML Unreviewed; 367 AA. AC A5J530; DT 26-JUN-2007, integrated into UniProtKB/TrEMBL. DT 26-JUN-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=BMAFMH_B0162; OS Burkholderia mallei FMH. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=334802; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FMH; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS264096; EDK54291.1; -; Genomic_DNA. DR ProteinModelPortal; A5J530; -. DR EnsemblBacteria; EDK54291; EDK54291; BMAFMH_B0162. DR PATRIC; 26914715; VBIBurMal45758_3157. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Transferase. SQ SEQUENCE 367 AA; 38315 MW; 3E9B351CCB7F5C2B CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGARAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID A5J9Z2_BURML Unreviewed; 209 AA. AC A5J9Z2; DT 26-JUN-2007, integrated into UniProtKB/TrEMBL. DT 26-JUN-2007, sequence version 1. DT 16-OCT-2013, entry version 26. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BMAFMH_K0232; OS Burkholderia mallei FMH. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=334802; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FMH; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS264098; EDK53158.1; -; Genomic_DNA. DR ProteinModelPortal; A5J9Z2; -. DR EnsemblBacteria; EDK53158; EDK53158; BMAFMH_K0232. DR PATRIC; 26918446; VBIBurMal45758_4389. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID A5K1X9_PLAVS Unreviewed; 538 AA. AC A5K1X9; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Thiamin-phosphate pyrophosphorylase, putative; GN ORFNames=PVX_113835; OS Plasmodium vivax (strain Salvador I). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=126793; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Salvador I; RX PubMed=18843361; DOI=10.1038/nature07327; RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., RA Caler E., Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., RA Cheng Q., Coulson R.M.R., Crabb B.S., del Portillo H.A., Essien K., RA Feldblyum T.V., Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., RA Kang'a S., Kooij T.W.A., Korsinczky M., Meyer E.V.-S., Nene V., RA Paulsen I., White O., Ralph S.A., Ren Q., Sargeant T.J., RA Salzberg S.L., Stoeckert C.J., Sullivan S.A., Yamamoto M.M., RA Hoffman S.L., Wortman J.R., Gardner M.J., Galinski M.R., RA Barnwell J.W., Fraser-Liggett C.M.; RT "Comparative genomics of the neglected human malaria parasite RT Plasmodium vivax."; RL Nature 455:757-763(2008). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAKM01000003; EDL46429.1; -; Genomic_DNA. DR RefSeq; XP_001616156.1; XM_001616106.1. DR ProteinModelPortal; A5K1X9; -. DR STRING; 5855.PVX_113835; -. DR GeneID; 5475455; -. DR KEGG; pvx:PVX_113835; -. DR EuPathDB; PlasmoDB:PVX_113835; -. DR HOGENOM; HOG000281504; -. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 538 AA; 59145 MW; 704C290011D506BF CRC64; MRVDKSGDAS LCNSPGRLAD YSLYLVTDDK FLTDKQNVCR TLIGKVREGV LGGVGLVQLR LKQADDRYFY NAAVRMKHLL SRYKVPLVIN NRVDICVGVD ADGVHVGRRD LPIKVARDIL GGEKIIGATI NFSNDEDIEM ALNSHVDYLV HEHTLYESST KQIAASHHEG LKQQIGTLLR KIKHLQERGK IYKPPLDSEA PPIIIIGGIN TNNIDDAMTH FSDACAGVAV VSNLIGENCN SFFNALRLKF AIDKHKKGCN EAFVNLCVSC LRHFFWTNLE GDMRGVDGGH FRLATNVDVK KNVRHFFESN LNLKIVQLSP PAVCSSAGGG NFFLFCSRRT RVERAATEER EALEVTEANG ATASTAATGE GEGTPTSHNP CVSKWIQQNK NIAHGVFILI GADLLALFRK LLAPEFFHTN NFVVITKREQ SAWEAVRCDV RGASIQCCNN LINVALKNSH VDSEVVNRFA ILLAYFLMVQ ERLKQVRPQF LTQIVGEGEA AAGAGENGRL LKLAAAVNMS FEVLSNEHTG LGVAAFST // ID A5KFJ0_CAMJU Unreviewed; 210 AA. AC A5KFJ0; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-MAR-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Cj8486_0995; OS Campylobacter jejuni subsp. jejuni CG8486. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=398000; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CG8486; RX PubMed=17438034; DOI=10.1128/IAI.00050-07; RA Poly F., Read T., Tribble D.R., Baqar S., Lorenzo M., Guerry P.; RT "Genome sequence of a clinical isolate of Campylobacter jejuni from RT Thailand."; RL Infect. Immun. 75:3425-3433(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AASY01000003; EDK22587.1; -; Genomic_DNA. DR ProteinModelPortal; A5KFJ0; -. DR EnsemblBacteria; EDK22587; EDK22587; Cj8486_0995. DR PATRIC; 27756928; VBICamJej15397_0532. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 24AFFA335287D700 CRC64; MKNKLDLSLY LVAAKGNKSE ECFLNTLENA IKGGVSIIQL REKELNTREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID A5KFM5_CAMJU Unreviewed; 201 AA. AC A5KFM5; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-MAR-2014, entry version 29. DE SubName: Full=Possible transferase; GN ORFNames=Cj8486_1032; OS Campylobacter jejuni subsp. jejuni CG8486. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=398000; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CG8486; RX PubMed=17438034; DOI=10.1128/IAI.00050-07; RA Poly F., Read T., Tribble D.R., Baqar S., Lorenzo M., Guerry P.; RT "Genome sequence of a clinical isolate of Campylobacter jejuni from RT Thailand."; RL Infect. Immun. 75:3425-3433(2007). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AASY01000003; EDK22622.1; -; Genomic_DNA. DR ProteinModelPortal; A5KFM5; -. DR EnsemblBacteria; EDK22622; EDK22622; Cj8486_1032. DR PATRIC; 27757006; VBICamJej15397_0571. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID A5KV12_9GAMM Unreviewed; 205 AA. AC A5KV12; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VSWAT3_25424; OS Vibrionales bacterium SWAT-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC unclassified Vibrionales. OX NCBI_TaxID=391574; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SWAT-3; RA Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZW01000002; EDK30686.1; -; Genomic_DNA. DR ProteinModelPortal; A5KV12; -. DR EnsemblBacteria; EDK30686; EDK30686; VSWAT3_25424. DR PATRIC; 25660604; VBIVibBac109234_0491. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22120 MW; 8E78F4ED51454C31 CRC64; MNPYKLYLVT DDQQDLETLK FVVEQAVAGG VTMVQVREKH GDVRAFIERA EAVKSVLAGT GVPLIINDRV DVALAVDADG LHLGQSDMPA ALARKLIGAD KILGLSIETE QQLQEADDLP IDYIGLSALF ETQTKTNLKK HWGYEGIKLA LETTKLPIVG IGGINESNIP QLTETGIHGL ALVSAICHAE DPKKATQDLL NLMGE // ID A5L3R0_9GAMM Unreviewed; 430 AA. AC A5L3R0; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VSWAT3_00485; OS Vibrionales bacterium SWAT-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC unclassified Vibrionales. OX NCBI_TaxID=391574; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SWAT-3; RA Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZW01000033; EDK27669.1; -; Genomic_DNA. DR ProteinModelPortal; A5L3R0; -. DR EnsemblBacteria; EDK27669; EDK27669; VSWAT3_00485. DR PATRIC; 25666550; VBIVibBac109234_3415. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 430 AA; 47529 MW; 3C31F3D43E80D3A0 CRC64; MTVKILIPSQ YIELTGEVQH CLLVAKRQGL ATDAVELGVS PTQYFSIVDS QHSLTIGFAS DVVSVEAEQL GSFDHIVSYD EPLSLADVRD ALAQYSNTIY VGVTNDAAVL DIWSHLNANR AIKSINPDHQ AIDSRHHFAW LLMLLALDFP LEDALVLARA ASNVSRGTWP SHYQEFPTPV LEDKRLGISV GWAHQGTSLS FPDLTKKSLG LYPVVDDVEW IERLLKLGIN TVQLRIKNPQ QADLEQQVAR SIELGREHNA QVFINDYWQL ALKHGAFGVH LGQEDIEESN LSQLSKAGIK IGLSTHGYYE LLRIVQINPS YIALGHIFPT TTKQMPSKPQ GLVRLALYQQ LIDTIPYSEE LVGYPTVAIG GIDQSTAEQV WDCGVSSLAV VRAITLAEDP KAVIEFFEAL MNGNSSTVTE EVRQELSHAE // ID A5LDW8_STREE Unreviewed; 198 AA. AC A5LDW8; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp3BS71_08786; OS Streptococcus pneumoniae SP3-BS71. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406556; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP3-BS71; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZZ01000008; EDK73608.1; -; Genomic_DNA. DR ProteinModelPortal; A5LDW8; -. DR EnsemblBacteria; EDK73608; EDK73608; CGSSp3BS71_08786. DR PATRIC; 28674080; VBIStrPne30073_1642. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 198 AA; 21939 MW; CB6320AD71EBC2F5 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKI // ID A5LDX5_STREE Unreviewed; 210 AA. AC A5LDX5; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp3BS71_08821; OS Streptococcus pneumoniae SP3-BS71. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406556; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP3-BS71; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZZ01000008; EDK73615.1; -; Genomic_DNA. DR ProteinModelPortal; A5LDX5; -. DR EnsemblBacteria; EDK73615; EDK73615; CGSSp3BS71_08821. DR PATRIC; 28674094; VBIStrPne30073_1649. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID A5LP40_STREE Unreviewed; 209 AA. AC A5LP40; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp6BS73_01373; OS Streptococcus pneumoniae SP6-BS73. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406557; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP6-BS73; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAA01000012; EDK75821.1; -; Genomic_DNA. DR ProteinModelPortal; A5LP40; -. DR EnsemblBacteria; EDK75821; EDK75821; CGSSp6BS73_01373. DR PATRIC; 29707882; VBIStrPne92647_1832. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23244 MW; 69798D236EB6C679 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID A5LP47_STREE Unreviewed; 210 AA. AC A5LP47; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp6BS73_01408; OS Streptococcus pneumoniae SP6-BS73. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406557; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP6-BS73; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAA01000012; EDK75828.1; -; Genomic_DNA. DR ProteinModelPortal; A5LP47; -. DR EnsemblBacteria; EDK75828; EDK75828; CGSSp6BS73_01408. DR PATRIC; 29707896; VBIStrPne92647_1839. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID A5LRY1_STREE Unreviewed; 210 AA. AC A5LRY1; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp9BS68_08202; OS Streptococcus pneumoniae SP9-BS68. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406558; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP9-BS68; RA Ehrlich G.D.; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAB01000003; EDK79715.1; -; Genomic_DNA. DR ProteinModelPortal; A5LRY1; -. DR EnsemblBacteria; EDK79715; EDK79715; CGSSp9BS68_08202. DR PATRIC; 37161946; VBIStrPne106222_0367. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID A5LWC3_STREE Unreviewed; 209 AA. AC A5LWC3; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp9BS68_04735; OS Streptococcus pneumoniae SP9-BS68. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406558; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP9-BS68; RA Ehrlich G.D.; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAB01000024; EDK78269.1; -; Genomic_DNA. DR ProteinModelPortal; A5LWC3; -. DR EnsemblBacteria; EDK78269; EDK78269; CGSSp9BS68_04735. DR PATRIC; 37164982; VBIStrPne106222_1857. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23244 MW; 69798D236EB6C679 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID A5LZV7_STREE Unreviewed; 210 AA. AC A5LZV7; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp11BS70_10580; OS Streptococcus pneumoniae SP11-BS70. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406559; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP11-BS70; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAC01000002; EDK63942.1; -; Genomic_DNA. DR ProteinModelPortal; A5LZV7; -. DR EnsemblBacteria; EDK63942; EDK63942; CGSSp11BS70_10580. DR PATRIC; 28642615; VBIStrPne77631_0701. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; AEAC90751A95738D CRC64; MNREALRLYL VTNRYQDSVE SFLAKIETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID A5LZW4_STREE Unreviewed; 209 AA. AC A5LZW4; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp11BS70_10615; OS Streptococcus pneumoniae SP11-BS70. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406559; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP11-BS70; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAC01000002; EDK63949.1; -; Genomic_DNA. DR ProteinModelPortal; A5LZW4; -. DR EnsemblBacteria; EDK63949; EDK63949; CGSSp11BS70_10615. DR PATRIC; 28642629; VBIStrPne77631_0708. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID A5M9G4_STREE Unreviewed; 209 AA. AC A5M9G4; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp14BS69_04947; OS Streptococcus pneumoniae SP14-BS69. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406560; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP14-BS69; RA Ehrlich G.D.; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAD01000010; EDK65505.1; -; Genomic_DNA. DR ProteinModelPortal; A5M9G4; -. DR EnsemblBacteria; EDK65505; EDK65505; CGSSp14BS69_04947. DR PATRIC; 28649280; VBIStrPne72417_1681. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID A5M9H2_STREE Unreviewed; 210 AA. AC A5M9H2; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp14BS69_04987; OS Streptococcus pneumoniae SP14-BS69. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406560; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP14-BS69; RA Ehrlich G.D.; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAD01000010; EDK65513.1; -; Genomic_DNA. DR ProteinModelPortal; A5M9H2; -. DR EnsemblBacteria; EDK65513; EDK65513; CGSSp14BS69_04987. DR PATRIC; 28649296; VBIStrPne72417_1689. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22786 MW; 7BE4851AE6B66247 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GLEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID A5MDB6_STREE Unreviewed; 209 AA. AC A5MDB6; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp18BS74_09675; OS Streptococcus pneumoniae SP18-BS74. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406561; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP18-BS74; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAE01000001; EDK69726.1; -; Genomic_DNA. DR ProteinModelPortal; A5MDB6; -. DR EnsemblBacteria; EDK69726; EDK69726; CGSSp18BS74_09675. DR PATRIC; 28651931; VBIStrPne31255_0251. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID A5MDC3_STREE Unreviewed; 210 AA. AC A5MDC3; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp18BS74_09710; OS Streptococcus pneumoniae SP18-BS74. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406561; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP18-BS74; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAE01000001; EDK69733.1; -; Genomic_DNA. DR ProteinModelPortal; A5MDC3; -. DR EnsemblBacteria; EDK69733; EDK69733; CGSSp18BS74_09710. DR PATRIC; 28651945; VBIStrPne31255_0258. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID A5MKC5_STREE Unreviewed; 210 AA. AC A5MKC5; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp19BS75_04842; OS Streptococcus pneumoniae SP19-BS75. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406562; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP19-BS75; RA Ehrlich G.D.; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAF01000001; EDK72063.1; -; Genomic_DNA. DR ProteinModelPortal; A5MKC5; -. DR EnsemblBacteria; EDK72063; EDK72063; CGSSp19BS75_04842. DR PATRIC; 28656800; VBIStrPne59842_0297. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID A5MKD3_STREE Unreviewed; 209 AA. AC A5MKD3; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp19BS75_04882; OS Streptococcus pneumoniae SP19-BS75. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406562; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP19-BS75; RA Ehrlich G.D.; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAF01000001; EDK72071.1; -; Genomic_DNA. DR ProteinModelPortal; A5MKD3; -. DR EnsemblBacteria; EDK72071; EDK72071; CGSSp19BS75_04882. DR PATRIC; 28656816; VBIStrPne59842_0305. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID A5MUK0_STREE Unreviewed; 209 AA. AC A5MUK0; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp23BS72_06279; OS Streptococcus pneumoniae SP23-BS72. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406563; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP23-BS72; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAG01000005; EDK81641.1; -; Genomic_DNA. DR ProteinModelPortal; A5MUK0; -. DR EnsemblBacteria; EDK81641; EDK81641; CGSSp23BS72_06279. DR PATRIC; 28668061; VBIStrPne38563_1005. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23376 MW; 2FA03125014CC79F CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYL GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID A5MUK7_STREE Unreviewed; 210 AA. AC A5MUK7; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp23BS72_06314; OS Streptococcus pneumoniae SP23-BS72. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=406563; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP23-BS72; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAG01000005; EDK81648.1; -; Genomic_DNA. DR ProteinModelPortal; A5MUK7; -. DR EnsemblBacteria; EDK81648; EDK81648; CGSSp23BS72_06314. DR PATRIC; 28668075; VBIStrPne38563_1012. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22811 MW; E3B55C492B70B036 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVRLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID A5N1D2_CLOK5 Unreviewed; 203 AA. AC A5N1D2; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; OrderedLocusNames=CKL_2917; OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=431943; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680; RX PubMed=18218779; DOI=10.1073/pnas.0711093105; RA Seedorf H., Fricke W.F., Veith B., Bruggemann H., Liesegang H., RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F., RA Hagemeier C., Thauer R.K., Gottschalk G.; RT "The genome of Clostridium kluyveri, a strict anaerobe with unique RT metabolic features."; RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000673; EDK34928.1; -; Genomic_DNA. DR RefSeq; YP_001396299.1; NC_009706.1. DR ProteinModelPortal; A5N1D2; -. DR STRING; 431943.CKL_2917; -. DR EnsemblBacteria; EDK34928; EDK34928; CKL_2917. DR GeneID; 5391069; -. DR KEGG; ckl:CKL_2917; -. DR PATRIC; 19467383; VBICloKlu111549_3025. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CKLU431943:GJF1-2910-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21913 MW; FE9FC84429D18D0E CRC64; MELDYSLYLV TDRNVLRGKS LYEAVEQAIL GGVTLVQLRE KDASTREFYE QALELKKITE TYNIPLIIND RLDIAQAVDA EGVHLGQSDM PLVAARNILG KNKIIGISVG NVEEALEAEK NGADYVGIGT IFFTGTKKDI DIPIGIEGLK SVYNSINIPA VAIGGINENN FREVLSTGID GISVVSAILG KNDIKAAAKA LHK // ID A5N8P6_CLOK5 Unreviewed; 200 AA. AC A5N8P6; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 42. DE SubName: Full=ThiE1; DE EC=2.5.1.3; GN Name=thiE1; OrderedLocusNames=CKL_1635; OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=431943; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680; RX PubMed=18218779; DOI=10.1073/pnas.0711093105; RA Seedorf H., Fricke W.F., Veith B., Bruggemann H., Liesegang H., RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F., RA Hagemeier C., Thauer R.K., Gottschalk G.; RT "The genome of Clostridium kluyveri, a strict anaerobe with unique RT metabolic features."; RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000673; EDK33677.1; -; Genomic_DNA. DR RefSeq; YP_001395025.1; NC_009706.1. DR ProteinModelPortal; A5N8P6; -. DR STRING; 431943.CKL_1635; -. DR EnsemblBacteria; EDK33677; EDK33677; CKL_1635. DR GeneID; 5394467; -. DR KEGG; ckl:CKL_1635; -. DR PATRIC; 19464737; VBICloKlu111549_1703. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CKLU431943:GJF1-1635-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 200 AA; 22090 MW; 9E546823E8B13498 CRC64; MIYVVTNRNL IKEDSIYNVV ENVVKNGADG IILREKDLSY TSLLSMSKKI KSITDKYNVP LIINGNIDIA LNIKAFGFHT SYEIFKKIKF KNNIYEKLKI GVSVHSIEEA KKAESLGANY LLAGHIFETD CKKGLKGRGL EFIREMHKNI LIPIIAIGGI DCSNLKDVLS NGACGAAIMS SAMTNDGGKV VKNLKLLLVR // ID A5P8V1_9SPHN Unreviewed; 183 AA. AC A5P8V1; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=ED21_18142; OS Erythrobacter sp. SD-21. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=161528; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SD-21; RA Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCG01000002; EDL49545.1; -; Genomic_DNA. DR ProteinModelPortal; A5P8V1; -. DR EnsemblBacteria; EDL49545; EDL49545; ED21_18142. DR PATRIC; 30320760; VBIErySp11529_0821. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 183 AA; 19431 MW; 3855FABB242A9C6C CRC64; MAARYSASVT NRQTLPLLWL LSDDRNDAGL ESALRNLPQG SGFVFRHYHL SEAARRERFE ALAAIARACN QVVILSGAGD WGADGHYGPP ECWGAGLKLA TGHNGDEIDT ALAAGADGIF LSPVFPTRSH PGAPMLGVMG FRVLAQQSPV PVIALGGMNR ARADELDWPR WGAIDGLAST KVA // ID A5PDK1_9SPHN Unreviewed; 210 AA. AC A5PDK1; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ED21_29196; OS Erythrobacter sp. SD-21. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=161528; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SD-21; RA Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCG01000008; EDL48004.1; -; Genomic_DNA. DR ProteinModelPortal; A5PDK1; -. DR EnsemblBacteria; EDL48004; EDL48004; ED21_29196. DR PATRIC; 30324046; VBIErySp11529_2434. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22355 MW; CDD22905BA4B3CC0 CRC64; MDENISTQLY LISPLDVSGD FPQRLERALE AGKGLVTAFQ FRVKGIDQHE AAALAEPLQA ICAAHEVAFI VNDSIALAKR LKADGVHLGQ KDGDVREARE ELGREAQIGV TCHASRHLAL EAGEAGADYV AFGAFFPSET KDSEHRADTD ILAWWHGLVE IPSVAIGGIT PANSRPLIEA GADFLAVSGA VWSGDEVAAV KGFAEQIART // ID A5THR8_BURML Unreviewed; 367 AA. AC A5THR8; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=BMA721280_E0417; OS Burkholderia mallei 2002721280. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=370895; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2002721280; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia mallei 2002721280."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899693; EDK84437.1; -; Genomic_DNA. DR ProteinModelPortal; A5THR8; -. DR EnsemblBacteria; EDK84437; EDK84437; BMA721280_E0417. DR PATRIC; 26890546; VBIBurMal4978_1829. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Transferase. SQ SEQUENCE 367 AA; 38315 MW; 3E9B351CCB7F5C2B CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGARAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID A5TVP2_FUSNP Unreviewed; 206 AA. AC A5TVP2; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 22-JAN-2014, entry version 28. DE SubName: Full=Possible thiamine monophosphate synthase ThiE; GN Name=thiE1; ORFNames=FNP_1180; OS Fusobacterium nucleatum subsp. polymorphum ATCC 10953. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=393480; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10953; RA Qin X., Weinstock G.M.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10953; RA Karpathy S.E., Xiang Q., Gioia J., Jiang H., Liu Y., Petrosino J.F., RA Yerrapragada S., Fox G.E., Kinder Haake S., Weinstock G.M., RA Highlander S.K.; RT "Genome sequence of Fusobacterium nucleatum subspecies polymorphum - a RT genetically tractable Fusobacterium."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000440; EDK88967.1; -; Genomic_DNA. DR ProteinModelPortal; A5TVP2; -. DR EnsemblBacteria; EDK88967; EDK88967; FNP_1180. DR PATRIC; 30266055; VBIFusNuc113593_0814. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 24004 MW; B66DF4C78591D870 CRC64; MLENKIKLNI ITNRKLCENE NLERQIEKIF SAYEKKIILK NFEIVTLTLR EKDLGKNEYL NLVEKIYPIC KRYRIDLILH QNYDLNLDEK YKIEGIHLSY DNFKSLNKNI REELIKKYKK IGVSIHSIDE VKEVEMLGAT YIVAGHIFET DCKKNLEPRG LNFIKELSSI LTIPIFAIGG INQEKSHLAI NSGAFGVCMM SSLMKY // ID A5TVP8_FUSNP Unreviewed; 206 AA. AC A5TVP8; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; ORFNames=FNP_1186; OS Fusobacterium nucleatum subsp. polymorphum ATCC 10953. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=393480; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10953; RA Qin X., Weinstock G.M.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10953; RA Karpathy S.E., Xiang Q., Gioia J., Jiang H., Liu Y., Petrosino J.F., RA Yerrapragada S., Fox G.E., Kinder Haake S., Weinstock G.M., RA Highlander S.K.; RT "Genome sequence of Fusobacterium nucleatum subspecies polymorphum - a RT genetically tractable Fusobacterium."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000440; EDK88973.1; -; Genomic_DNA. DR ProteinModelPortal; A5TVP8; -. DR EnsemblBacteria; EDK88973; EDK88973; FNP_1186. DR PATRIC; 30266067; VBIFusNuc113593_0820. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22812 MW; 6F20E2DAD2A6E264 CRC64; MDLKDCKIYL VTDEKACNRK DLYKCIEESI KGGVKIVQLR EKNISTKDFY EKALKVKEIC KNYGVLFIIN DRLDIAQAVK ADGVHLGQSD IPIEKAREIL KDKFLIGATA RNIEEAKKVE LLGADYIGSG AIFGTSTKDN AKKLEMEELK KIVTSVKIPV FAIGGININN VSLLKNIGLQ GICSVSGILS EKDCKKAVDI MLKNFN // ID A5VA92_SPHWW Unreviewed; 178 AA. AC A5VA92; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 40. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Swit_2855; OS Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=392499; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RW1 / DSM 6014 / JCM 10273; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., RA Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Halden R.U., Miller T.R., RA Salzberg S.L., Eisen J.A., Richardson P.; RT "Complete sequence of chromosome of Sphingomonas wittichii RW1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000699; ABQ69208.1; -; Genomic_DNA. DR RefSeq; YP_001263346.1; NC_009511.1. DR ProteinModelPortal; A5VA92; -. DR STRING; 392499.Swit_2855; -. DR EnsemblBacteria; ABQ69208; ABQ69208; Swit_2855. DR GeneID; 5199319; -. DR KEGG; swi:Swit_2855; -. DR PATRIC; 23684885; VBISphWit55028_3386. DR eggNOG; NOG121918; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NRRDSIM; -. DR OrthoDB; EOG679THR; -. DR BioCyc; SWIT392499:GHZK-2889-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 178 AA; 19816 MW; 5948E859B2A9372D CRC64; MQPRQPELPS LWMMTDERQG EALWAALRRL PPGSGIVFRH KSLLDRERRR LFERVRRITR RRGLILLLAG DEAEARRWGA DGAHHRRPGP PRAGTAPAHN LREIRAAERS GAAALLLSPL HPTRSHPGAP TLGRMRFAAM ARATRLPVIA LGGIDRRRGR AAMAVGAHGW AAIDAWTQ // ID A5VB33_SPHWW Unreviewed; 255 AA. AC A5VB33; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Swit_3151; OS Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=392499; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RW1 / DSM 6014 / JCM 10273; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., RA Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Halden R.U., Miller T.R., RA Salzberg S.L., Eisen J.A., Richardson P.; RT "Complete sequence of chromosome of Sphingomonas wittichii RW1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000699; ABQ69499.1; -; Genomic_DNA. DR RefSeq; YP_001263637.1; NC_009511.1. DR ProteinModelPortal; A5VB33; -. DR STRING; 392499.Swit_3151; -. DR EnsemblBacteria; ABQ69499; ABQ69499; Swit_3151. DR GeneID; 5199745; -. DR KEGG; swi:Swit_3151; -. DR PATRIC; 23685515; VBISphWit55028_3700. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SWIT392499:GHZK-3186-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 83 87 HMP-PP binding (By similarity). FT REGION 181 183 THZ-P binding (By similarity). FT METAL 116 116 Magnesium (By similarity). FT METAL 135 135 Magnesium (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 184 184 HMP-PP (By similarity). FT BINDING 211 211 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 255 AA; 26620 MW; 8216868DC80404F4 CRC64; MMAATAARSA STSHDHALER GMNDIDDLDD ALSLDPGFAD RFERDEGRPP CKLYLISPPA IDAGFAETLA AAIDAAPVVA AFQLRLKGID EHRIAELARP LQAVCASREV AFIVNDSIGL AKRLDADGVH LGQEDGDPRE ARQALGPTAQ IGVTCHDSRH LAMEAGEAGA DYVAFGAFYE TGTKPTKHRP EPSILGWWST LFELPSVAIG GITPANAAPL IAAGADFLAV SGAVWNAPEG PAAGVRAFAA LKGMG // ID A5VNE3_BRUO2 Unreviewed; 203 AA. AC A5VNE3; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BOV_0205; OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=444178; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512; RA Paulsen I.; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000708; ABQ60151.1; -; Genomic_DNA. DR RefSeq; YP_001258240.1; NC_009505.1. DR ProteinModelPortal; A5VNE3; -. DR STRING; 444178.BOV_0205; -. DR EnsemblBacteria; ABQ60151; ABQ60151; BOV_0205. DR GeneID; 5201456; -. DR KEGG; bov:BOV_0205; -. DR PATRIC; 17860139; VBIBruOvi136990_1492. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BOVI444178:GH2V-204-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22305 MW; EA846C980EA5A994 CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIQLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID A5VS63_BRUO2 Unreviewed; 221 AA. AC A5VS63; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 41. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BOV_1650; OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=444178; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512; RA Paulsen I.; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000708; ABQ61636.1; -; Genomic_DNA. DR RefSeq; YP_001259560.1; NC_009505.1. DR ProteinModelPortal; A5VS63; -. DR STRING; 444178.BOV_1650; -. DR EnsemblBacteria; ABQ61636; ABQ61636; BOV_1650. DR GeneID; 5201603; -. DR KEGG; bov:BOV_1650; -. DR PATRIC; 17863350; VBIBruOvi136990_3058. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BOVI444178:GH2V-1648-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID A5W8N9_PSEP1 Unreviewed; 314 AA. AC A5W8N9; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 57. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=Pput_4376; OS Pseudomonas putida (strain F1 / ATCC 700007). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=351746; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F1 / ATCC 700007; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Parales R., RA Richardson P.; RT "Complete sequence of Pseudomonas putida F1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000712; ABQ80499.1; -; Genomic_DNA. DR RefSeq; YP_001269683.1; NC_009512.1. DR ProteinModelPortal; A5W8N9; -. DR STRING; 351746.Pput_4376; -. DR EnsemblBacteria; ABQ80499; ABQ80499; Pput_4376. DR GeneID; 5193400; -. DR KEGG; ppf:Pput_4376; -. DR PATRIC; 19924973; VBIPsePut56420_4436. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPUT351746:GI26-4460-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 34371 MW; B25BEC42D1F6442F CRC64; MKRIHVVAAV IRGADGRILI ARRADTQHQG GLWEFPGGKV EEGESVEAAL ARELREELGI EVSHSRALIK VSHDYPDKQV LLDVREVEAF TGEPHGAEGQ PLEWVAPRDL PQYEFPEANK PIVAAARLPD QYLITPDGLE VPQMLKGIQK AVANGIRLIQ LRAPDMYDPK YRDVAVDAVG LCAGKAQLML KGPLEWLGDF PAAGWHLTAA QLRKYAARGR PFPKERWLAA SCHSAEELAL AEQMGVDFVT LSPVQATQTH PEAVPLGWDE AQRLIAGFNK PVYLLGGVGP GEREQAWEAG AQGVAGIRAF WPEV // ID A5WFV4_PSYWF Unreviewed; 369 AA. AC A5WFV4; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=PsycPRwf_1604; OS Psychrobacter sp. (strain PRwf-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=349106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRwf-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., RA Richardson P.; RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000713; ABQ94545.1; -; Genomic_DNA. DR RefSeq; YP_001280495.1; NC_009524.1. DR ProteinModelPortal; A5WFV4; -. DR STRING; 349106.PsycPRwf_1604; -. DR EnsemblBacteria; ABQ94545; ABQ94545; PsycPRwf_1604. DR GeneID; 5206890; -. DR KEGG; prw:PsycPRwf_1604; -. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; VAVIHYQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPRW349106:GHZF-1633-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 369 AA; 41779 MW; 2AB2279270B11DF8 CRC64; MKYIDVAVAV IHYQDKYLLG YRSSHQHQGD RYEFVGGKIE ASEQPKQALI REVYEEIGLD ITSDGCINPL GVLRHEYLDI SDTDRSKTVC LHVFRVQLSP DQFAVFRDKT QGCEGQRLHW VSKQRLLDNQ YVLPEANQSI LQWLRLDDVI CITNQLSFND TQGLDAVTEQ SLVQWLEYHH QSLPQSATVY VRLASSSLKQ QARVVLKLCA RRTDLNVIIQ QPLAGYLSQT NKLPVQVIAQ HLTQAMLEHQ LQQLQHGKNT SISQLSLPIT VSCHSQYQIQ AVNTLAQYQL NHKLAPVIGA YLSPVQPTQT HPEQPCLGWE QFAILAEHCE VPVIALGGLA PQDLATVRRN NGDKVAGIRQ FLTQEHQKI // ID A5WJC3_MYCTF Unreviewed; 222 AA. AC A5WJC3; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TBFG_10419; OS Mycobacterium tuberculosis (strain F11). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=336982; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F11; RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L., RA Grabherr M., Mauceli E., Brockman W., Young S., LaButti K., RA Pushparaj V., Sykes S., Baldwin J., Fitzgerald M., Bloom T., RA Zimmer A., Settipalli S., Shea T., Arachchi H., Macdonald P., RA Abouelleil A., Lui A., Priest M., Berlin A., Gearin G., Brown A., RA Aftuck L., Bessette D., Allen N., Lubonja R., Lokyitsang T., RA Matthews C., Dunbar C., Benamara M., Nguyen T., Negash T., RA DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., RA Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., O'Leary S., RA Alvarado L., Victor T., Murray M.; RT "The complete genome sequence of Mycobacterium tuberculosis F11."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000717; ABR04762.1; -; Genomic_DNA. DR RefSeq; YP_001286364.1; NC_009565.1. DR ProteinModelPortal; A5WJC3; -. DR SMR; A5WJC3; 1-221. DR STRING; 336982.TBFG_10419; -. DR EnsemblBacteria; ABR04762; ABR04762; TBFG_10419. DR GeneID; 5221083; -. DR KEGG; mtf:TBFG_10419; -. DR PATRIC; 18131561; VBIMycTub9078_0454. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MTUB336982:GH7I-423-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID A5XR23_BURML Unreviewed; 367 AA. AC A5XR23; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=BMAJHU_B0161; OS Burkholderia mallei JHU. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=334803; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JHU; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS264108; EDK59271.1; -; Genomic_DNA. DR ProteinModelPortal; A5XR23; -. DR EnsemblBacteria; EDK59271; EDK59271; BMAJHU_B0161. DR PATRIC; 26938431; VBIBurMal67795_3198. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Transferase. SQ SEQUENCE 367 AA; 38315 MW; 3E9B351CCB7F5C2B CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGARAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID A5XVX5_BURML Unreviewed; 209 AA. AC A5XVX5; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 16-OCT-2013, entry version 25. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BMAJHU_E0251; OS Burkholderia mallei JHU. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=334803; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JHU; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS264110; EDK58122.1; -; Genomic_DNA. DR ProteinModelPortal; A5XVX5; -. DR EnsemblBacteria; EDK58122; EDK58122; BMAJHU_E0251. DR PATRIC; 26942160; VBIBurMal67795_4648. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID A5Z4Z5_9FIRM Unreviewed; 213 AA. AC A5Z4Z5; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUBVEN_00772; OS Eubacterium ventriosum ATCC 27560. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=411463; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27560; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27560; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Eubacterium ventriosum (ATCC 27560)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVL02000029; EDM52045.1; -; Genomic_DNA. DR ProteinModelPortal; A5Z4Z5; -. DR EnsemblBacteria; EDM52045; EDM52045; EUBVEN_00772. DR PATRIC; 31246069; VBIEubVen137708_1114. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22717 MW; 975B79CAE7ADFB6E CRC64; MNFDYTLYLV TDRQLMSCDS LTEAVEQAIL GGCTMIQLRE KELSSLEFYN QAVAVKQVTD KYHIPLIIND RIDIAMAVQA TGVHIGQHDL PAAAVRKVIG ENMLLGVSAS SIAEAIQAQQ DGADYLGVGA MFPTGTKTDA DSVSMEELQK IRAAVSLPIV VIGGINKGNA GRFKPMGIDG LAVVSAIIAQ SDIKAAAAEL KDLFCGKEKK NGF // ID A5Z6S5_9FIRM Unreviewed; 225 AA. AC A5Z6S5; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUBVEN_01408; OS Eubacterium ventriosum ATCC 27560. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=411463; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27560; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27560; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Eubacterium ventriosum (ATCC 27560)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVL02000033; EDM51500.1; -; Genomic_DNA. DR ProteinModelPortal; A5Z6S5; -. DR EnsemblBacteria; EDM51500; EDM51500; EUBVEN_01408. DR PATRIC; 31247830; VBIEubVen137708_1971. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 53 57 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 24470 MW; DD9C025D8DF4B6CF CRC64; MEKHWKKEQN MKSSNTTTDE LLLYAVTDRA WLGNETLYEQ VEKSLKGGVT FVQLREKKLD EESFLQEAIE IKELCKKYNV PFVINDNVDI AIKMDADGVH VGQSDMEAGD VRKKLGPDKI IGVSAQTVEQ AILAEKHGAD YLGVGAVFPT GSKDDAEDVP FETLKAICEA VSIPVIAIGG ITKDNVKELA GSGICGIAVI SAIFASKDIE TATKELKVNT IKAVK // ID A5ZDA4_9BACE Unreviewed; 184 AA. AC A5ZDA4; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACCAC_00860; OS Bacteroides caccae ATCC 43185. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=411901; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43185; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43185; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides caccae (ATCC 43185)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVM02000001; EDM22473.1; -; Genomic_DNA. DR ProteinModelPortal; A5ZDA4; -. DR EnsemblBacteria; EDM22473; EDM22473; BACCAC_00860. DR PATRIC; 28980382; VBIBacCac10171_0798. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 11 15 HMP-PP binding (By similarity). FT REGION 108 110 THZ-P binding (By similarity). FT METAL 44 44 Magnesium (By similarity). FT METAL 63 63 Magnesium (By similarity). FT BINDING 43 43 HMP-PP (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 144 144 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 184 AA; 20119 MW; 75A73E7734CBF297 CRC64; MALEGGCKWI QLRMKDAPLD EVEAVALQLK PLCKEHEAIL ILDDHVELAK KLEVDGVHLG KKDMPIDQAR QILGEAFIIG GTANTFEDVL LHYRAGADYL GIGPFRFTTT KQNLSPVLGL EGYVSILAQM QEAHIELPVV AIGGITYEDI PAILRTGVNG IALSGTILRA NDPVEETRRI LNNN // ID A5ZDA9_9BACE Unreviewed; 202 AA. AC A5ZDA9; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BACCAC_00865; OS Bacteroides caccae ATCC 43185. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=411901; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43185; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43185; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides caccae (ATCC 43185)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVM02000001; EDM22478.1; -; Genomic_DNA. DR ProteinModelPortal; A5ZDA9; -. DR SMR; A5ZDA9; 1-202. DR EnsemblBacteria; EDM22478; EDM22478; BACCAC_00865. DR PATRIC; 28980392; VBIBacCac10171_0803. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23437 MW; DAA28E58C0239B2D CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYAGH VSCSCHSVEE VKNKKHFYDY VFMSPIYDSI SKVNYYSTYT AEELRDAQRT KIIDSKVMAL GGINADNLLE IKDFGFGGAV ILGDLWNRFD ACSDQDYLAV IEHFKKLKKL AD // ID A5ZMH7_9FIRM Unreviewed; 205 AA. AC A5ZMH7; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 16-OCT-2013, entry version 26. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=RUMOBE_00194; OS Ruminococcus obeum ATCC 29174. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=411459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29174; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29174; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Ruminococcus obeum (ATCC 29174)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVO02000001; EDM89071.1; -; Genomic_DNA. DR ProteinModelPortal; A5ZMH7; -. DR EnsemblBacteria; EDM89071; EDM89071; RUMOBE_00194. DR PATRIC; 29801110; VBIRumObe16879_3174. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 205 AA; 22676 MW; C499193A32F816A6 CRC64; MSICKEKNGT GNENAGAAEY RNIIAVTNRK LCEKPFLEQV ERICQMHPKA LILREKDLSE SAYEVMAGQV LEICGRYDTP CMLHSFVEVA RRLHHPYIHL PLFLLEEYCG KLNDFRMVGS SIHSPEEAIR AQKAGAAYVT AGHVYVTDCK KGLPPRGLEF LKEVCTKVTI PVYAIGGIHA GTGQIQEVMD CGASGGCIMS EMMKI // ID A5ZMJ6_9FIRM Unreviewed; 211 AA. AC A5ZMJ6; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RUMOBE_00213; OS Ruminococcus obeum ATCC 29174. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=411459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29174; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29174; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Ruminococcus obeum (ATCC 29174)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVO02000001; EDM89090.1; -; Genomic_DNA. DR ProteinModelPortal; A5ZMJ6; -. DR EnsemblBacteria; EDM89090; EDM89090; RUMOBE_00213. DR PATRIC; 29801144; VBIRumObe16879_3191. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22452 MW; 247B0D0F0603193F CRC64; MKISPEQLKL YAVTDRSWLK PDETLASVTE ELLRAGVSCV QLREKNASDE EILQEAALLK EICERYNVPL IINDRPDLAQ KANASGVHVG LSDMGIQKAR QLLGPDFIIG GSAHNVEEAL AAQNAGADYI GCGAVFGSTT KTNVTQLPVE TLRAICQAVE IPVVAIGGVT ADNLYLLAGS GISGAAVVSG LFKPDNKAEA VRHFLTELQK L // ID A6A5I5_VIBCL Unreviewed; 440 AA. AC A6A5I5; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=A5A_0063; OS Vibrio cholerae MZO-2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=417398; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MZO-2; RA Heidelberg J., Sebastian Y.; RT "Annotation of Vibrio cholerae MZO-2."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWF01000038; EDM53807.1; -; Genomic_DNA. DR ProteinModelPortal; A6A5I5; -. DR EnsemblBacteria; EDM53807; EDM53807; A5A_0063. DR PATRIC; 28075092; VBIVibCho76110_2812. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48913 MW; 845B6A4C8C9E8ECF CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGFA IQHIRLDVGS DAQFILEKSE ESLRIGSSLC SQEETSEPCD YYLDYVSENR VSPEAIMCNA RCTVTVGFHD KYAFTLDKWQ YGNAAEQLII YPSENHRLNS KVNQHLAWVL ASLALGFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQC DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID RSNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSVFAD FVDAEYKLMP ASESCEPLSC LAREVADAHR // ID A6ACJ7_VIBCL Unreviewed; 440 AA. AC A6ACJ7; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=A59_0101; OS Vibrio cholerae 623-39. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=417397; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=623-39; RA Heidelberg J., Sebastian Y.; RT "Annotation of Vibrio cholerae 623-39."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWG01000021; EDL73554.1; -; Genomic_DNA. DR ProteinModelPortal; A6ACJ7; -. DR EnsemblBacteria; EDL73554; EDL73554; A59_0101. DR PATRIC; 28016858; VBIVibCho134658_0341. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48891 MW; 5998183EC9673EE0 CRC64; MVSLVFPRHL SALIGHVQYA LLQAKEQGFA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQEETSEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGNAAEQLII YSSETHRLNS MLNQHLAWVL ATLTLDFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPA MQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CSNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID A6AMY8_9VIBR Unreviewed; 204 AA. AC A6AMY8; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=A1Q_4127; OS Vibrio campbellii HY01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=410291; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HY01; RA Heidelberg J., Sebastian Y.; RT "Annotation of Vibrio harveyi HY01."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWP01000008; EDL69974.1; -; Genomic_DNA. DR ProteinModelPortal; A6AMY8; -. DR EnsemblBacteria; EDL69974; EDL69974; A1Q_4127. DR PATRIC; 31185086; VBIVibHar127108_1967. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22011 MW; F3CCE5DC64982E26 CRC64; MNAYRLYLVT DDQQDLATLK RVVRKAVEGG VTMVQVREKH GDVRAFIERA QAVKDILKDT DVPLIINDRV DVALAVDADG VHLGQSDMPA TVARELIGPY KILGLSIENE QQLAEADSLP IDYIGLSAIF ATPTKTNTKK HWGIDGLKMA LETTSLPIVA IGGINESNIP QLSATGVHGL ALVSAICHAE DPKAASEYLL ELMS // ID A6ATG7_9VIBR Unreviewed; 471 AA. AC A6ATG7; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 16-OCT-2013, entry version 36. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=A1Q_0620; OS Vibrio campbellii HY01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=410291; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HY01; RA Heidelberg J., Sebastian Y.; RT "Annotation of Vibrio harveyi HY01."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWP01000047; EDL67942.1; -; Genomic_DNA. DR ProteinModelPortal; A6ATG7; -. DR EnsemblBacteria; EDL67942; EDL67942; A1Q_0620. DR PATRIC; 31186945; VBIVibHar127108_2857. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 471 AA; 52573 MW; 9208EC056047E6E0 CRC64; MSKILIPSSL IELTGLVQQC LLLAKEQGFS IEDIELGVSP TQSIQLVRDQ QTTRITTDFI DGYDSEHESS FVLYYRSALS VEACAKQPSK AIYIGIADTQ VSDEKEKVLQ FDIWRHPINN EVRALSVKSK FNAMFDPEHH LAWIVTLAVL DFPIEDALTL ARGMLTQQAN VSRETLLNDN FDGGQTTQWA DQFDDFPAPV LEDNRLGIQV GWSAQGESVS FPTLTKQSLG LYPVVDDVAW IERLLPLGIN TIQLRIKNPQ QADLERQIIR AIELGRQYQA QVFINDYWQL AIKHGAYGVH LGQEDIEESN LAQLTKAGIR LGLSTHGYYE LLRIVQIHPS YIALGHIFPT TTKQMPSKPQ GLVRLALYQK LIDSIPYTNT EAAFRPAKDK AGSDYVLGFP TVAIGGIDQS NAAQVWQTGV SSLAVVRAIT LAESPQSVIE FFAKLMKERQ LTFTDQNSEL AHNKRGEHAH G // ID A6B4A3_VIBPH Unreviewed; 204 AA. AC A6B4A3; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=A79_0102, D030_2287; OS Vibrio parahaemolyticus AQ3810. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=419109; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AQ3810; RA Heidelberg J., Sebastian Y.; RT "Annotation of Vibrio parahaemolyticus AQ3810."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AQ3810; RA Eppinger M., Hasan N.A., Sengamalay N., Hine E., Su Q., RA Daugherty S.C., Choi S.Y., Sadzewicz L., Tallon L., Cebula T.A., RA Ravel J., Colwell R.R.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWQ01000043; EDM58994.1; -; Genomic_DNA. DR EMBL; AZJP01000470; EXF70223.1; -; Genomic_DNA. DR ProteinModelPortal; A6B4A3; -. DR EnsemblBacteria; EDM58994; EDM58994; A79_0102. DR PATRIC; 38615821; VBIVibPar22798_2423. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21800 MW; A0452C65C4F15CDD CRC64; MNAYRLYLVT DDQQDLSTLK HVVRKAVEGG VTMVQVREKH GDVRAFIERA QAVKTILEGT GVPLIINDRV DVALAVDADG VHLGQSDMPA EIARQLIGPN KILGLSIETE DQLAEADSLP IDYIGLSAIF ATPTKTNTKK HWGIEGLKMA LNTTSLPIVA IGGINETNIP ALSATGVHGL ALVSAICHAE NPTKAAEYLL SLMD // ID A6B799_VIBPH Unreviewed; 422 AA. AC A6B799; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 35. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=A79_2778; OS Vibrio parahaemolyticus AQ3810. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=419109; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AQ3810; RA Heidelberg J., Sebastian Y.; RT "Annotation of Vibrio parahaemolyticus AQ3810."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWQ01000101; EDM57958.1; -; Genomic_DNA. DR ProteinModelPortal; A6B799; -. DR EnsemblBacteria; EDM57958; EDM57958; A79_2778. DR PATRIC; 38620779; VBIVibPar22798_4804. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 422 AA; 46914 MW; 0EEF191D4B7D7B04 CRC64; MAKEQGFSID EIELGVSPTQ FIQLVLGQNT FRVGTDLIDV CEEAETADFV LYYQSGLSVS ECRQQPSSAI FIGIQDVESK LDDSVKTTSA DVLDIWRHPV NDEIRALSVA STSRTTTLQT DQHLAWTVTL LALDFPIEDA LTLARPMTNV SRETLINGET MVKQEWASQF ADFPTPVLED CRLGIKVGWS SHGQSVNFPH LSKQSLGLYP VVDDVSWIER LLPLGINTIQ LRIKDPYQPD LEQQIARAIE LGRQYDAQVF INDYWQLAIK HGAFGVHLGQ EDIEDSNLSQ LSTAGICLGL STHGYYELLR IVQINPSYIA LGHIFSTTTK QMPSKPQGLV RLALYQKLND SIPYGESVGY PTVAIGGIDQ SNAEQVWQCG VSSLAVVRAI TLSESPKQVI EFFDQLMNTT STSLVMEDYR AY // ID A6BFY3_9FIRM Unreviewed; 136 AA. AC A6BFY3; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=DORLON_01205; OS Dorea longicatena DSM 13814. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea. OX NCBI_TaxID=411462; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13814; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13814; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Dorea longicatena (DSM 13814)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXB02000004; EDM63539.1; -; Genomic_DNA. DR ProteinModelPortal; A6BFY3; -. DR EnsemblBacteria; EDM63539; EDM63539; DORLON_01205. DR PATRIC; 36985340; VBIDorLon81175_0367. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 136 AA; 15067 MW; A18632512BDD2AA0 CRC64; MNICSRYQVS CILHNFWKTA LELGCTSVHL PLPILQKITD EEKKKFTKIG ISIHSVEEAK EAEQLGASYL TAGHIYATDC KRGLPPRGLG FLKEVCREVS IPVYGIGGIK FDEEQWNDMK KCGAVGGCVM SGMMEI // ID A6BJR2_9FIRM Unreviewed; 233 AA. AC A6BJR2; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DORLON_02557; OS Dorea longicatena DSM 13814. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea. OX NCBI_TaxID=411462; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13814; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13814; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Dorea longicatena (DSM 13814)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXB02000017; EDM62145.1; -; Genomic_DNA. DR ProteinModelPortal; A6BJR2; -. DR EnsemblBacteria; EDM62145; EDM62145; DORLON_02557. DR PATRIC; 36987978; VBIDorLon81175_1647. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 157 159 THZ-P binding (By similarity). FT REGION 207 208 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 160 160 HMP-PP (By similarity). FT BINDING 187 187 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 25625 MW; B3BE4BDB06095269 CRC64; MRSDKELEKD QMKEKTEHMC KKMKKEDLLL YAVTDRHWLN GETLYSQVEK TLEGGTTFVQ LREKELDEAH FLKEAKEIKE LCARYRVPFV INDNVDIALE MDADGVHVGQ SDMEADDVRA KLGPDKIIGV SAQTVEQAVL AEKRGADYLG VGAVFHTNSK ADVAEVSRET LKAICDAVDI PVIAIGGISK ENVSELAGTG ICGIAVISAI FAEKDIKKAT EKLKSLTGEM VKA // ID A6BXC9_YERPE Unreviewed; 215 AA. AC A6BXC9; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YPE_3664; OS Yersinia pestis CA88-4125. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=412420; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CA88-4125; RA Plunkett G.III., Anderson B.D., Burland V., Cabot E.L., Glasner J.D., RA Mau B., Neeno-Eckwall E., Perna N.T., Bruce D., Gilna P., Green L.D., RA Keim P., Munk A.C., Probert W.S., Vogler A.J., Wagner D.M., RA Brettin T.S.; RT "Yersinia pestis CA88-4125 whole genome shotgun sequencing project."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCD01000006; EDM39413.1; -; Genomic_DNA. DR ProteinModelPortal; A6BXC9; -. DR EnsemblBacteria; EDM39413; EDM39413; YPE_3664. DR PATRIC; 29564456; VBIYerPes909_4384. DR OMA; GRSTHEP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23275 MW; EE560D5E7AB02574 CRC64; MATPGFPSTE QRLGLYPVVD SLLWIERLLA AGVTTLQLRI KNADDAQVEQ DIVAAIELGK RYQARLFIND YWQLAVKHGA YGVHLGQEDL EAADLAAIQQ AGLRLGISTH DEHELAVAKT LRPSYIALGH IFPTQTKQMP SSPQGLASLS RQVKNTPDYP TVAIGGISIE RVPHVLATGV GSVAVVSAIT LASDWQRATA QLLHLIEGKE LADEK // ID A6C401_9PLAN Unreviewed; 520 AA. AC A6C401; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=PM8797T_11084; OS Planctomyces maris DSM 8797. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Planctomyces. OX NCBI_TaxID=344747; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 8797; RA Amann R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCE01000008; EDL60591.1; -; Genomic_DNA. DR ProteinModelPortal; A6C401; -. DR EnsemblBacteria; EDL60591; EDL60591; PM8797T_11084. DR PATRIC; 30926777; VBIPlaMar116015_1880. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0019538; P:protein metabolic process; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.1780.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004176; Clp_N. DR InterPro; IPR023150; Dbl_Clp-N. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02861; Clp_N; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 520 AA; 57173 MW; DD4FF15D2AE908A1 CRC64; MHHILTAGAQ RALIQAERIA SGSAESEPTL APLLAALALE ESRAAEIMRT HQIDLAQILQ EFQLPLSQDP ATSLLDSPVQ PLEMSQALQQ YPAFREVLNH AMQQASRADV PTEIGSEHLL WGLLATAGKE SEWLQSTGSL SAEKLDDSIN VIFRQTVEPL DVDFALRTVA ATADDQTNTL RTIDAAANRL REGLRVIEDF LRFSLDDAHL MSLLKSTRHR LTDALRFIGN ETLISSRDTL NDVGTSISTT SEIDRSSLEH LLQANLKRVQ EAARTLEEFS KLISPEAAAI FKQMRYASYT LEKTILTCIA SQRRLENSRL YLLVSESLCH HGAGPAIRES LAAGVNLVQI REKSMTDRQL LAHGNRVRKW TRDAGAILIM NDRPDLAIAI DADGVHVGQD ELPVREVRQI VGPRRLIGVS THNIEQARQA VLDGADYIGV GPTFPTSTKN FAEHEYAGLD FVNQVAAEIT LPWFAIGGIQ ADNLQQVLEA GATRVAVSGV ICSHEHPGQI TRELLEQLSN // ID A6CIN6_9BACI Unreviewed; 222 AA. AC A6CIN6; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSG1_04100; OS Bacillus sp. SG-1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=161544; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SG-1; RA Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCF01000001; EDL66506.1; -; Genomic_DNA. DR ProteinModelPortal; A6CIN6; -. DR SMR; A6CIN6; 4-215. DR EnsemblBacteria; EDL66506; EDL66506; BSG1_04100. DR PATRIC; 25227633; VBIBacSp59792_0502. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23714 MW; 731C93A0360E0C4A CRC64; MTYSSQQIKE LLKVYFIMGS ANCLQHPEEV LRGAIKGDIT LFQFREKGNG CLQGEDKLQL AKRLQSICQE NQIPFIVNDD IELAVELDAD GVHIGQEDEP AEDVRRKIGN KKILGVSAHT LEEAEHAIAA GADYLGIGPI YPTLTKEDAK AVQGLTFIQE LRESGIVIPL VGIGGITAEN AAPIIGAGAD GVSVITAISQ GKSPEAAARM LAVAVGNEDQ RI // ID A6CKN1_9BACI Unreviewed; 208 AA. AC A6CKN1; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=Transcriptional regulator TenI; GN ORFNames=BSG1_00510; OS Bacillus sp. SG-1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=161544; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SG-1; RA Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCF01000004; EDL65534.1; -; Genomic_DNA. DR ProteinModelPortal; A6CKN1; -. DR EnsemblBacteria; EDL65534; EDL65534; BSG1_00510. DR PATRIC; 25228926; VBIBacSp59792_1147. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 208 AA; 22601 MW; 45E0DA67B9DB8D6A CRC64; MKKPVLHAVT TGKKSIEETA SICLDISPHV EAIHIREHTK TAREIYELGK KMIDFGIPAD QIIINNRVDV AAALGICPVQ LGYHSLPVNV VKESFSRLSI GKSVHSLLEA VEAEEEGADY ILFGHVYPTS SKKGLTPRGL DELTQLISNV TIPVIAIGGI LPSNAREVIQ KGCSGIAVMS GIFDAVDPVK AAIDYQNHLE LIFHEQFL // ID A6CXQ8_9VIBR Unreviewed; 209 AA. AC A6CXQ8; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VSAK1_18654; OS Vibrio shilonii AK1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=391591; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AK1; RA Rosenberg E., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCH01000005; EDL54775.1; -; Genomic_DNA. DR ProteinModelPortal; A6CXQ8; -. DR EnsemblBacteria; EDL54775; EDL54775; VSAK1_18654. DR PATRIC; 28380605; VBIVibShi100628_1104. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22611 MW; C97245DE4B0F01D9 CRC64; MTRNPYRLYL VTDENQDLDT LIEVVKQAVE GGVTMVQIRE KHHDIRTFIT KAAAVKKVLE GTNVPLIIND RVDVALAIDA DGVHLGQTDM PATLARTLIG EDKILGLSIE SETQLQQAKQ LPIDYIGLSA IFSTTTKTNI KTEWGLEGLT NALQQIELPI VAIGGINESN LLDVAKTGVH GVAIVSAISH AGSPKQAVQQ LLTLMEKAE // ID A6D6K9_9VIBR Unreviewed; 411 AA. AC A6D6K9; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 31. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=VSAK1_24304; OS Vibrio shilonii AK1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=391591; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AK1; RA Rosenberg E., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCH01000047; EDL51788.1; -; Genomic_DNA. DR ProteinModelPortal; A6D6K9; -. DR EnsemblBacteria; EDL51788; EDL51788; VSAK1_24304. DR PATRIC; 28386740; VBIVibShi100628_4132. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 411 AA; 46186 MW; 95088A5E761EA020 CRC64; MTLLIPSNHQ DLIERVRHVL SLAQSVGFDI EDIQISEVKE SDVIHIDDSE RRQIISSDLL SVQMNNEADY RLHYHHGFVE SDFPKVIQSM TLGDIYIDVH SEFERKDIWS CREEVIKASS GALSLTGAQE HFAWFIVSIV LDFPLEDAVM LARAGSVSRE TWPSTREQFF TPVIENSHLA IKVGWAVRAS TSVFQTLSKS SLGLYPVVDN VEWIERLLKQ GIKTIQLRIK DPDYPNLAQQ IQKAIQLGEQ YDAQVFINDY WQLAIEYGAF GVHLGQEDIE TADLTLLASN NIALGLSTHG YYELLRVVQI HPSYIALGHI FPTTTKVMPS RPQGLVRLAL YQQLIDSIQY GEKLGYPTVA IGGIDLQTAK PVWDCGVTSL AVVRALTLAA DTQYVIDEFS LIMAGERDGL R // ID A6DCX6_9PROT Unreviewed; 216 AA. AC A6DCX6; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=CMTB2_05247; OS Caminibacter mediatlanticus TB-2. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales; OC Nautiliaceae; Caminibacter. OX NCBI_TaxID=391592; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TB-2; RX PubMed=22180817; RA Giovannelli D., Ferriera S., Johnson J., Kravitz S., RA Perez-Rodriguez I., Ricci J., O'Brien C., Voordeckers J.W., Bini E., RA Vetriani C.; RT "Draft genome sequence of Caminibacter mediatlanticus strain TB-2, an RT epsilonproteobacterium isolated from a deep-sea hydrothermal vent."; RL Stand. Genomic Sci. 5:135-143(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCJ01000004; EDM23664.1; -; Genomic_DNA. DR ProteinModelPortal; A6DCX6; -. DR EnsemblBacteria; EDM23664; EDM23664; CMTB2_05247. DR PATRIC; 30459187; VBICamMed78467_1041. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 216 AA; 24947 MW; F89A1EF4AC11C967 CRC64; MAIYALLDFD TLKKNDISIE EFIKTAKGLK AKILQYRDKN SSFEEKLKRI KKVRKLWKKT LIINDEIELL PFADGIHIGQ EDLENLCKKY NLTKFEIIKN LKNGNLNPQF STLNSQFIVG LSTHNKEEIL EANKLPLDYI GLGAYRPTNT KNTNNILGKK VIDLIKYSYH PVAIIGGIKI YDKIPANFKV VGSDICKLMY SRLRKKEIFK KKLKNL // ID A6DDB6_9PROT Unreviewed; 211 AA. AC A6DDB6; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=CMTB2_08402; OS Caminibacter mediatlanticus TB-2. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales; OC Nautiliaceae; Caminibacter. OX NCBI_TaxID=391592; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TB-2; RX PubMed=22180817; RA Giovannelli D., Ferriera S., Johnson J., Kravitz S., RA Perez-Rodriguez I., Ricci J., O'Brien C., Voordeckers J.W., Bini E., RA Vetriani C.; RT "Draft genome sequence of Caminibacter mediatlanticus strain TB-2, an RT epsilonproteobacterium isolated from a deep-sea hydrothermal vent."; RL Stand. Genomic Sci. 5:135-143(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCJ01000005; EDM23542.1; -; Genomic_DNA. DR ProteinModelPortal; A6DDB6; -. DR EnsemblBacteria; EDM23542; EDM23542; CMTB2_08402. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 211 AA; 24236 MW; 3CCB8C4E1D0856B5 CRC64; MGIPSCWLCI TYILSILTSI YFYGINICLS IWCNHRSRGS IIITYFITDP SFPFPKILNA IKNKKPTFVC YRNKNYYDES EILEFINFAK KYSKIFINYE SLKNKDLLTY FDGIHLPSSK LHLIENFKEK IVIASTHNLT EVKNSKNADF ITFSPIFNSK GRIGVGVEKL NEICKIHKNT IALGGIISNK EVEKIKKSCA VGFASIRYFL T // ID A6DTH0_9BACT Unreviewed; 211 AA. AC A6DTH0; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 16-OCT-2013, entry version 26. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; GN ORFNames=LNTAR_10056; OS Lentisphaera araneosa HTCC2155. OC Bacteria; Lentisphaerae; Lentisphaeria; Lentisphaerales; OC Lentisphaeraceae; Lentisphaera. OX NCBI_TaxID=313628; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2155; RA Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2155; RX PubMed=20363947; DOI=10.1128/JB.00208-10; RA Thrash J.C., Cho J.C., Vergin K.L., Morris R.M., Giovannoni S.J.; RT "Genome sequence of Lentisphaera araneosa HTCC2155T, the type species RT of the order Lentisphaerales in the phylum Lentisphaerae."; RL J. Bacteriol. 192:2938-2939(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCK01000037; EDM25074.1; -; Genomic_DNA. DR ProteinModelPortal; A6DTH0; -. DR EnsemblBacteria; EDM25074; EDM25074; LNTAR_10056. DR PATRIC; 29248642; VBILenAra45852_4405. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 211 AA; 23476 MW; 16150CDCE5AA5014 CRC64; MNQALLEAVE PYWIYDYDVA QSLDPKASLL KSLAQDLKLI QIRVKSLVDL ELKKQVKKYY DLIKEANPAC HVIMNDYVDL CAEFAMEGVH LGQSDDSVIE ARKNLGEKAI IGLTVRSLEE AQEAQGLLAQ GIVDYVGVGT VFQTTTKQGL KAKGPEFIEE VFKLIPAEKV YPIGGINKEN LSELKKIDVK HVALCSELYK NPDVKVYCGV C // ID A6E0I3_9RHOB Unreviewed; 206 AA. AC A6E0I3; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 21. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=RTM1035_09234; OS Roseovarius sp. TM1035. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=391613; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TM1035; RA Belas R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCL01000004; EDM32106.1; -; Genomic_DNA. DR ProteinModelPortal; A6E0I3; -. DR EnsemblBacteria; EDM32106; EDM32106; RTM1035_09234. DR PATRIC; 28156779; VBIRosSp37286_2051. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22237 MW; 19A47D093F4823B2 CRC64; MAETEQPQIY LITPPEFELS VFPDTLARVL DSHPVACVRL ALASRDEDRI ARAADACREV THARDVALVI ESHLMLVERH GLDGVHLPDA GRSVRAARKE LGEDAIVGCF CGTSRHDGMN AGEAGADYIS FGPVGATPLD DGAQVDMDVF DWWSKVIELP VVAEGALDLA LVAQLTPMAD FLAFGEEIWR EEDPVAALGR FIAAMG // ID A6E0V9_9RHOB Unreviewed; 198 AA. AC A6E0V9; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 25. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=RTM1035_19281; OS Roseovarius sp. TM1035. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=391613; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TM1035; RA Belas R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCL01000005; EDM31499.1; -; Genomic_DNA. DR ProteinModelPortal; A6E0V9; -. DR EnsemblBacteria; EDM31499; EDM31499; RTM1035_19281. DR PATRIC; 28157042; VBIRosSp37286_2181. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 198 AA; 21876 MW; 7E4942D612055ECF CRC64; MSLPRFYPIF DHTDWLRRVL PLGVKLVQLR IKDLTGEALN AQITQAQSLC RTHGATLVVN DHWQAAIDAG ATWVHLGQED LDTADIPAMR RAGLKLGLST HDHAELDRAL SHDPDYVALG PVYPTILKKM KWHEQGLDKL TEWKRLIGDV PLVAIGGMSV ERAGGAYAAG ADIVSAVTDI TLNPDPEARV QHWIEVTR // ID A6EB48_9SPHI Unreviewed; 210 AA. AC A6EB48; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=PBAL39_10606; OS Pedobacter sp. BAL39. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=391596; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL39; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCM01000004; EDM37589.1; -; Genomic_DNA. DR ProteinModelPortal; A6EB48; -. DR EnsemblBacteria; EDM37589; EDM37589; PBAL39_10606. DR PATRIC; 31337623; VBIPedSp63332_1621. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 210 AA; 23047 MW; 3B7C78E3E5FE12BA CRC64; MKKFIERLHF ITHDIPQLSH IDQARIACEA GAKWVQYRCL TKNDEELLKD IHVIAEICDD WGATLIVTDH IHLNGKADIQ GFHIEDMDAD FVRIREQLGE AITIGGSSNT VEGLQRLATE GVDYAGFGPF SHTDTKPNSM PHLGIDGYRK AIVSLNDLNI GLPVLAVGGV TAADIAELLD TGIFGIAASS AINQAPDMRE AYLSFYDKIM // ID A6EC69_9SPHI Unreviewed; 209 AA. AC A6EC69; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase; GN ORFNames=PBAL39_17914; OS Pedobacter sp. BAL39. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=391596; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL39; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCM01000006; EDM36775.1; -; Genomic_DNA. DR ProteinModelPortal; A6EC69; -. DR EnsemblBacteria; EDM36775; EDM36775; PBAL39_17914. DR PATRIC; 31338367; VBIPedSp63332_1986. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 23557 MW; FA85DE7DFA756F01 CRC64; MKLKVISSPA FFEGEAKIIN QLFEAGMSCF HLRKSRPEKA AYLSLLRQIN PVYHDRIALH QFHEVAQDMG ISRLHFPEYL RPLAQDSIAV LHKDFTLSTS THKISQLTDL KYFNYTFYGP VFHSISKKGY LSTCQNDFRL PLNTPLQVIA LGGVSASRIE QLKAMNFEGA AILGCLWTRS DNALQTFQAI QEKCRAVAAV KTVNGYGND // ID A6EC71_9SPHI Unreviewed; 220 AA. AC A6EC71; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PBAL39_17924; OS Pedobacter sp. BAL39. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=391596; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL39; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCM01000006; EDM36777.1; -; Genomic_DNA. DR ProteinModelPortal; A6EC71; -. DR EnsemblBacteria; EDM36777; EDM36777; PBAL39_17924. DR PATRIC; 31338371; VBIPedSp63332_1988. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23960 MW; E38696B718888814 CRC64; MVDRLHYISQ ENEKTDHITG ILSALNAGVK WIQLRVKNKP QDEVLALAEA ANRHCKKFAA HLIINDFPDV ARAVSAYGLH LGLNDMSITN ARLIVGKEIK IGGTANTFSE VQKRLQAGAD YIGLGPFRFT TTKQQLSPIL GISGYTKVMN QVRSAGITTP IIAIGGIEIS DLPALLKTGI YGVAVSGTLT HSKDPEETVR LMYQQLEKAA FIFPKTTTLC // ID A6EM48_9BACT Unreviewed; 208 AA. AC A6EM48; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SCB49_07562; OS unidentified eubacterium SCB49. OC Bacteria; Bacteroidetes; environmental samples. OX NCBI_TaxID=50743; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SCB49; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCO01000001; EDM45648.1; -; Genomic_DNA. DR ProteinModelPortal; A6EM48; -. DR PATRIC; 30959736; VBIUniEub121565_0404. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22902 MW; 4337F55345B0EF1F CRC64; MKKQLQYITQ NHPTKSHETL CLEFCEAGGK WVQLRMKNVS DSVLLATAKA CRKITTDYGA TLIINDRLDI ALKVNADGVH LGQEDLSTAL ARENTPKDFI IGGTANTCVE VIHHYNNGVD YVGVGPFRYT KTKKQLSPVL GIHGYRSILV DLKKAKIEIP LVAIGGIVTT DFSDLHNINI HSIAVSGLIT LSENKQKSIT AFNNVFKK // ID A6EM50_9BACT Unreviewed; 194 AA. AC A6EM50; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 13-NOV-2013, entry version 23. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase; GN ORFNames=SCB49_07572; OS unidentified eubacterium SCB49. OC Bacteria; Bacteroidetes; environmental samples. OX NCBI_TaxID=50743; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SCB49; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCO01000001; EDM45650.1; -; Genomic_DNA. DR ProteinModelPortal; A6EM50; -. DR PATRIC; 30959740; VBIUniEub121565_0406. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 22112 MW; 47C698C5B5CAF8E1 CRC64; MQLIVISSED FIADEINIIE GLFECGLTHF HLRKPNATLN EVSTFLSQIN SVYHDKIIIH HHFELLKQFN LKGAHVNLLK FPLEEAKQLK VNHLSISCHT LSELNILKTE QFNYAFLSPI FNSISKKGYL SPFKKEELYE ALKKHKNIVA LGGITKKQLA TCKELGFSGA AILGSLWLSK NKIKTFKKMQ KTCQ // ID A6ENN7_9BACT Unreviewed; 213 AA. AC A6ENN7; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SCB49_12930; OS unidentified eubacterium SCB49. OC Bacteria; Bacteroidetes; environmental samples. OX NCBI_TaxID=50743; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SCB49; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCO01000003; EDM44476.1; -; Genomic_DNA. DR ProteinModelPortal; A6ENN7; -. DR PATRIC; 30960814; VBIUniEub121565_0930. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23174 MW; A2C17865D59B6A1D CRC64; MIPKLHYISQ GNSPKEHLEN IQKACTSGAE LVQLRLKNIS EKKFLKIATQ AREITAHYQT RLIINDAYKV AKAVKADGVH LGKSDSCPSI ARKHLYSWQI IGGTANTIQD CEILLDKQVD YISLGPFRTS KTKENTPAVL GIQGYTAITD VLKTGTPLLG VGGITTEDVA DLLNAGISGI AVSEAITKDF NSISIFHKLL NASSTAEQKY TFD // ID A6EZK8_9ALTE Unreviewed; 237 AA. AC A6EZK8; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MDG893_13993; OS Marinobacter algicola DG893. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=443152; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DG893; RA Green D., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCP01000010; EDM47977.1; -; Genomic_DNA. DR ProteinModelPortal; A6EZK8; -. DR EnsemblBacteria; EDM47977; EDM47977; MDG893_13993. DR PATRIC; 28808765; VBIMarAlg30321_1839. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 53 57 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 237 AA; 24958 MW; 4BBB2467F0DACCB0 CRC64; MAELTPSGTF SAQAIAKGLK PGLYAITDSQ LLSEDRLLVA VEAALRGGAV LVQYREKKAP EPERLKQAQD LAALCHNARV PLIINDDPEL ARRCGAAGVH LGQSDGSLAQ ARRQLGDYAI IGATCHADLA LASRADADGA DYLAFGRFFN STTKPDAPVA EPSVLAKSRQ FGKPVTAIGG ITTDNGEGLI RAGADLLAVV GGLFDGDVAA IEERARRFTR LFAQHHPLFS SSVPEES // ID A6F2S7_9ALTE Unreviewed; 311 AA. AC A6F2S7; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE SubName: Full=Uncharacterized protein; GN ORFNames=MDG893_12635; OS Marinobacter algicola DG893. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=443152; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DG893; RA Green D., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCP01000026; EDM46913.1; -; Genomic_DNA. DR ProteinModelPortal; A6F2S7; -. DR EnsemblBacteria; EDM46913; EDM46913; MDG893_12635. DR PATRIC; 28810980; VBIMarAlg30321_2921. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 311 AA; 33784 MW; 0CE9FD13C7F31553 CRC64; MGVVFRDGKV LIARRPDHVH QGGLLEFPGG KVEAGETVQQ ALVREIREET GLRIDPDLLE PVIEIRHDYG DKRVFLDVWE ASCAEGAPEG REGQAIQWLG VQDLADVDFP AANRPIIRAL KLPRRYAITG SIGNPSAFPD QLRQCLLAAR PQLCLFRAPE LSEEIYERLA GWSLEACRAS DSLLMLHGAP LLLELLPQAA GLHMPWREAR QYSVRPIPEG QLLAISCHDE EEIAHAEQLQ ADFITLGPVK PTSSHPGAPG IGWARFQALA AGAGIPVYAL GGLAPDDTHA ARQAGAQGIA GIGFWWSGNG Y // ID A6FGE5_9GAMM Unreviewed; 491 AA. AC A6FGE5; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=PE36_24108; OS Moritella sp. PE36. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Moritellaceae; Moritella. OX NCBI_TaxID=58051; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PE36; RA Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCQ01000041; EDM65806.1; -; Genomic_DNA. DR ProteinModelPortal; A6FGE5; -. DR EnsemblBacteria; EDM65806; EDM65806; PE36_24108. DR PATRIC; 25982997; VBIMorSp76677_3440. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 491 AA; 52780 MW; 078F51AB41DBA879 CRC64; MTQAIIWTIA SLDARDNAAT QADINTINAL GGRGYHVSTK LLSDGDFAAE LAVLTAAPVA SAIKIGVIAT TSHVEILADF LQAYKQQHPD LSVIYEPLSI SLSDMAKAES ADSVLINTIK IRLLPIVDVL ILLQEQGGTG AAVLFSATKQ AINTLLSFGV KGVCAKAITV NGHHDDKQQS IALDVYIDGQ REILLSSPSA TLTPRSKDEH RGAFSSALAT VIAQDYPIDD ALVVARAYLN QTADAWPTDR SDFPQVVLPN TVLGDQLDLA QQMQLAYDFA PCDTNRLGLY PVVDTVAWLE KVLQQGVKTL QLRIKDKTPA EVVDDIKAAV ALGRQYQARL FINDYWKLAI EHGAYGVHLG QEDMLIADFV AIKTAGLKLG LSTHGYYEIL RAHQIKPSYI ALGHIFPTVT KDMPSKPQGL QRLQRYAALM QDYPLVAIGG ISIARAPLVA ATGVGSVAVV TAITRADDYK QAIADLLAIA EPHSVLACAN D // ID A6FN99_9RHOB Unreviewed; 198 AA. AC A6FN99; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=RAZWK3B_10046; OS Roseobacter sp. AzwK-3b. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=351016; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AzwK-3b; RA Francis C., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCR01000002; EDM72585.1; -; Genomic_DNA. DR ProteinModelPortal; A6FN99; -. DR EnsemblBacteria; EDM72585; EDM72585; RAZWK3B_10046. DR PATRIC; 28086793; VBIRosSp9675_1174. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 198 AA; 22503 MW; 0D10BEA4BD595812 CRC64; MTLDRFYPIF DDIRWLERMA PLGIKLVQMR IKDQPEPELR DQIAKAKTIC QNSDITLIVN DYWKLAMDLD CDWVHLGQED LDVADMAAIR RAGLRIGIST HDRDELDRAL GHDPDYVALG PIYPTKLKKM KWHQQGLEKL SEWKGLIGDI PLVAIGGMSV ERAPGAFEAG ADIVSAVTDI TWHDSPEDRV RAWLDATR // ID A6FSQ6_9RHOB Unreviewed; 206 AA. AC A6FSQ6; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 21. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=RAZWK3B_15213; OS Roseobacter sp. AzwK-3b. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=351016; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AzwK-3b; RA Francis C., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCR01000007; EDM70758.1; -; Genomic_DNA. DR ProteinModelPortal; A6FSQ6; -. DR EnsemblBacteria; EDM70758; EDM70758; RAZWK3B_15213. DR PATRIC; 28089901; VBIRosSp9675_2703. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 21857 MW; DA300EE6971883F5 CRC64; MAETEQPQIY LITPPDFELS DFPDRLAAVL DAQDIACVRL AMATRDEDRL ARAADACREV THARDVALVI DSHIMLVERL GLDGVHLTDG ARSVRKARKE LGADAIIGAF CGTSRHEGIS AGEAGADYIS FGPVGASALG DGSMAEHELF DWWSHMIELP VVAEGALDAQ LIAALAPVTD FFGIGDEIWS TEDPAGALGK LIAAMG // ID A6G1A2_9DELT Unreviewed; 240 AA. AC A6G1A2; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 22. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=PPSIR1_11495; OS Plesiocystis pacifica SIR-1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Nannocystaceae; Plesiocystis. OX NCBI_TaxID=391625; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SIR-1; RA Shimkets L., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCS01000011; EDM80397.1; -; Genomic_DNA. DR ProteinModelPortal; A6G1A2; -. DR EnsemblBacteria; EDM80397; EDM80397; PPSIR1_11495. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 240 AA; 24878 MW; 5CE436A02112366F CRC64; MTAAVPFRIL AITPPRPDPD AFTPARVRAL VDAWRPMLPG AGGPGLALLL REPGASLERT LAISETLRGA AADANIPVLT SIHPSDLEGL SATPRVTLEG LRGVQLKADA EPRAVARARK LGLTASSWWV GRSCHGAPPE QLGAADYECF APVFTPRTKQ LGVDKQAAGL DALRPWVARG VPVFALGGLT PDNATRCLSA GAHGVAGISL FFGDAGLVAD NAAQLCAAFR RAPARHAAPP // ID A6GJ22_9DELT Unreviewed; 230 AA. AC A6GJ22; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PPSIR1_32769; OS Plesiocystis pacifica SIR-1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Nannocystaceae; Plesiocystis. OX NCBI_TaxID=391625; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SIR-1; RA Shimkets L., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCS01000147; EDM74136.1; -; Genomic_DNA. DR ProteinModelPortal; A6GJ22; -. DR EnsemblBacteria; EDM74136; EDM74136; PPSIR1_32769. DR PATRIC; 29504924; VBIPlePac99763_7903. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 186 186 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 24264 MW; BCEF0D764E4E2CD1 CRC64; MTKHPIRPSV SGLYAILDWP FAHALEPDVL AAALLDGGAR VLQLRAKHAS RDERTALARR IAPVCVAAEV PFVLNDDLEL ALELLDAGVA VAAVHLGQED LAAVAEPARA LERVRDAGLG LGLSTHSRAQ VEALAALPWL PDYIGLGPVF PTRTKAKADP AVGLERLATI RREVAPPQLP IVAIGGIDHE RAPLVAQTKV ESLAAIGALT ADDPDAIRDR TRAMVAAFSP // ID A6GQ02_9BURK Unreviewed; 229 AA. AC A6GQ02; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMED105_08760; OS Limnobacter sp. MED105. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Limnobacter. OX NCBI_TaxID=391597; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED105; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCT01000005; EDM83907.1; -; Genomic_DNA. DR ProteinModelPortal; A6GQ02; -. DR EnsemblBacteria; EDM83907; EDM83907; LMED105_08760. DR PATRIC; 27463320; VBILimSp111806_1448. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 49 53 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 24539 MW; 0945434A6EFFDB2A CRC64; MKNELDTRLS TRLIKGVYAI TPERSALWTP DAIVDCVAAA LDGGVRLFQC RQKNWQQAEL IELVGQLDAL CEKYDAALIL NDVPSEEFAK FEGGAVAGVH LGKTDEAILK ARSSLGSKWV VGASCYNQFE MAEQAVREGA SYVAFGAMYP SATKPNAVRA ELDLFGKARS LGVPVVAIGG ITIERVPELM KAGAHAVAVV NGLFGMEPNA EQVCSVAQQW VEAVNGCHQ // ID A6GR33_9BURK Unreviewed; 324 AA. AC A6GR33; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE SubName: Full=Uncharacterized protein; GN ORFNames=LMED105_06888; OS Limnobacter sp. MED105. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Limnobacter. OX NCBI_TaxID=391597; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED105; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCT01000008; EDM83306.1; -; Genomic_DNA. DR ProteinModelPortal; A6GR33; -. DR EnsemblBacteria; EDM83306; EDM83306; LMED105_06888. DR PATRIC; 27464097; VBILimSp111806_1823. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 324 AA; 35739 MW; D16B8D3B8512EC11 CRC64; MNQMASSHVK PRIDVAVAVV FNAAGQVLWG CRPEGKPYAG YWEFPGGKVE PDETVWQALV RELKEELDIT ALEGGPWFRI EHDYEHANVR LHLYRVWHFE GTPKSLEQQP FTWASLDSSD LSPILPATEP LLPKLAQPTV MALSNYEAGF EACAERLERG LNATKLPVYV QFREKTLSGD ALIQAFEHCY GLCQKTGQAM LLNSDTWVNL REHLDALPCP LHLTQAHLLS GQFQDLQCAG ASVHDAGSLR IAFDRGLSYA VLGAVKQTTS HPEQSGLGWE RFLEITQAAR LPVFAIGGLA GYDIPDARLH GAHGIAMLSQ FGVA // ID A6GWR7_FLAPJ Unreviewed; 199 AA. AC A6GWR7; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 40. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE1; OrderedLocusNames=FP0429; OS Flavobacterium psychrophilum (strain JIP02/86 / ATCC 49511). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=402612; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JIP02/86 / ATCC 49511; RX PubMed=17592475; DOI=10.1038/nbt1313; RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., RA Kerouault B., Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., RA Gibrat J.-F., Claverol S., Dumetz F., Le Henaff M., Benmansour A.; RT "Complete genome sequence of the fish pathogen Flavobacterium RT psychrophilum."; RL Nat. Biotechnol. 25:763-769(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM398681; CAL42540.1; -; Genomic_DNA. DR RefSeq; YP_001295358.1; NC_009613.3. DR ProteinModelPortal; A6GWR7; -. DR STRING; 402612.FP0429; -. DR EnsemblBacteria; CAL42540; CAL42540; FP0429. DR GeneID; 5299698; -. DR KEGG; fps:FP0429; -. DR PATRIC; 21905714; VBIFlaPsy4505_0443. DR eggNOG; NOG86118; -. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome; Transferase. SQ SEQUENCE 199 AA; 22600 MW; FAF6C49692299D04 CRC64; MIVITNPNTI SNEINTIHSL FESGLELLHV RKPDFSEVKM SAFLSEIKLE YHQKLVLHSH HQLASEFEIN RIHFTEKSRI ETAEEILKTN KQIGFTLSTS VHKIADFEAL SSLFHYALFG PVFKSISKPN YISNLDFKKE LEKRTNNKTA LIALGGISSE SITTALKYGF NDVALLGSIW NSNKPIEKFK LCQQIALSY // ID A6L654_BACV8 Unreviewed; 202 AA. AC A6L654; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 40. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN OrderedLocusNames=BVU_3550; OS Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=435590; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8482 / DSM 1447 / NCTC 11154; RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156; RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., RA Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., RA Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., RA Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.; RT "Evolution of symbiotic bacteria in the distal human intestine."; RL PLoS Biol. 5:1574-1586(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000139; ABR41168.1; -; Genomic_DNA. DR RefSeq; YP_001300790.1; NC_009614.1. DR ProteinModelPortal; A6L654; -. DR SMR; A6L654; 1-202. DR STRING; 435590.BVU_3550; -. DR EnsemblBacteria; ABR41168; ABR41168; BVU_3550. DR GeneID; 5304510; -. DR KEGG; bvu:BVU_3550; -. DR PATRIC; 21072156; VBIBacVul85104_3653. DR eggNOG; NOG86118; -. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR OrthoDB; EOG6RC3V1; -. DR BioCyc; BVUL435590:GH96-3541-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 22933 MW; 0AE478B2289391FD CRC64; MKLILITPPT YFVEEDKIIT ALFEEGLDTL HLRKPGTAPM FAERLLTLIP EQYHKRIVVH GHFYLKEEYK LKGIHLNGRN PNLPEGYKGH VSCSCHSLDE VKERKSSCDY VFLSPVFNSI SKLNYNSAYT AEELRTAAKA GIIDKKVIAL GGIDEENLLE VKDFGFGGAA ILGALWNKFD ACTDRDYRCV IEHFRKLRDL AD // ID A6LAW2_PARD8 Unreviewed; 242 AA. AC A6LAW2; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 19-FEB-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BDI_1060; OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / NCTC OS 11152). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=435591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8503 / DSM 20701 / NCTC 11152; RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156; RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., RA Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., RA Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., RA Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.; RT "Evolution of symbiotic bacteria in the distal human intestine."; RL PLoS Biol. 5:1574-1586(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000140; ABR42826.1; -; Genomic_DNA. DR RefSeq; YP_001302448.1; NC_009615.1. DR ProteinModelPortal; A6LAW2; -. DR STRING; 435591.BDI_1060; -. DR EnsemblBacteria; ABR42826; ABR42826; BDI_1060. DR GeneID; 5306213; -. DR KEGG; pdi:BDI_1060; -. DR PATRIC; 22845284; VBIParDis29947_1049. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RTCATIC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PDIS435591:GCNH-1058-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 163 165 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 HMP-PP (By similarity). FT BINDING 199 199 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 242 AA; 26792 MW; E42A20AAF69E0ECC CRC64; MALNYYFGYD ENGRVDRRTT GLRPPFGGNN RLMFITHRTP KYTECDEVSM AIQGGCSWIQ LRMKDGIYED TVRTCATICA EECERIVDFC VNDDLEAAVT CGATACHLGK NDMPLDIAWE VLRDKLDSNA IFYIGATANT FEDIRLAVER GASYIGLGPY RFTGTKKNLS PILGLDGYRK IIAQCKEADI DIPIFAIGGI TLEDVGPLME TGITGIAVSG AIINASDPVE ETRRFIEEIN KY // ID A6LAW3_PARD8 Unreviewed; 198 AA. AC A6LAW3; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 22-JAN-2014, entry version 40. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN OrderedLocusNames=BDI_1061; OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / NCTC OS 11152). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=435591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8503 / DSM 20701 / NCTC 11152; RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156; RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., RA Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., RA Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., RA Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.; RT "Evolution of symbiotic bacteria in the distal human intestine."; RL PLoS Biol. 5:1574-1586(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000140; ABR42827.1; -; Genomic_DNA. DR RefSeq; YP_001302449.1; NC_009615.1. DR ProteinModelPortal; A6LAW3; -. DR STRING; 435591.BDI_1061; -. DR EnsemblBacteria; ABR42827; ABR42827; BDI_1061. DR GeneID; 5306214; -. DR KEGG; pdi:BDI_1061; -. DR PATRIC; 22845286; VBIParDis29947_1050. DR eggNOG; NOG86118; -. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR OrthoDB; EOG6RC3V1; -. DR BioCyc; PDIS435591:GCNH-1059-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 198 AA; 22212 MW; 47E076FC66E61020 CRC64; MNKLVVITTP YFFADEASLI ELLFAEGMSR LHLRKPDCKR DELEGLLDKI SPAYYDRIVL HDWFTLAEER ALGGIHLNKR NPEAPPLYKG SISRSCHSLE EIIEYKPVCD YVFLSPIFQS ISKEGYGSGF SLDGLRNAKG IIDDKVIALG GICPRTITKL KDIPFGGVAV LGALWGNDPS LFVADQLIKQ FKRLQVWP // ID A6LR55_CLOB8 Unreviewed; 216 AA. AC A6LR55; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 43. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Cbei_0648; OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium OS acetobutylicum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=290402; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51743 / NCIMB 8052; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Tapia R., Brainard J., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Bennet G., Cann I., Chen J.-S., Contreras A.L., RA Jones D., Kashket E., Mitchell W., Stoddard S., Schwarz W., RA Qureshi N., Young M., Shi Z., Ezeji T., White B., Blaschek H., RA Richardson P.; RT "Complete sequence of Clostridium beijerinckii NCIMB 8052."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000721; ABR32835.1; -; Genomic_DNA. DR RefSeq; YP_001307791.1; NC_009617.1. DR ProteinModelPortal; A6LR55; -. DR STRING; 290402.Cbei_0648; -. DR EnsemblBacteria; ABR32835; ABR32835; Cbei_0648. DR GeneID; 5291879; -. DR KEGG; cbe:Cbei_0648; -. DR PATRIC; 19345228; VBICloBei69853_0665. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ASHIFAT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CBEI290402:GHL5-713-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 216 AA; 24254 MW; 6C39763D226B3C26 CRC64; MSVIGITNRK LCRDFFDQIK KISESNLDFL IIREKDLSSE ELMILVLKVK EELKNTNIRI ILNSNIDIAK KSNVDGIQLS FNDFINISNR LCTGRAINSK EMVDNFHFSR NKYKIYKMIG VSIHSCEEGI QAAKLGADYV IYGHVFETDC KKGLPPRGIK EIEALSKKIN IPIIGIGGIN QDNYKKVLDA GASGIAIMSS LMKDKNPEEL VKSLSK // ID A6Q3A7_NITSB Unreviewed; 188 AA. AC A6Q3A7; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 43. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=NIS_0854; OS Nitratiruptor sp. (strain SB155-2). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nitratiruptor. OX NCBI_TaxID=387092; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB155-2; RX PubMed=17615243; DOI=10.1073/pnas.0700687104; RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.L., Takai K., RA Horikoshi K.; RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into RT emergence of pathogens."; RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009178; BAF69966.1; -; Genomic_DNA. DR RefSeq; YP_001356323.1; NC_009662.1. DR ProteinModelPortal; A6Q3A7; -. DR STRING; 387092.NIS_0854; -. DR EnsemblBacteria; BAF69966; BAF69966; NIS_0854. DR GeneID; 5361396; -. DR KEGG; nis:NIS_0854; -. DR PATRIC; 22683780; VBINitSp82229_0894. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IASTHNT; -. DR OrthoDB; EOG6FJNJD; -. DR BioCyc; NSP387092:GHA5-893-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 188 AA; 21336 MW; AB3D49896A985B22 CRC64; MKKNLDGFFS YLITDPSQYG KSSIAFKVYL HSVFRKHTPI FLLYRDKTDF QKRKALALLQ IASIYGSIPI VHSDLKLAKR YPFLGIHIPS DSFEKILLTK RLGIFTIVST HSEEEIEKAV RLGADFVTYS PIFSTPGKGE PKGVRQLRKV CKKYPKKIIA LGGIVGHKEI RRVLRAKAAG FASIRYFS // ID A6Q497_NITSB Unreviewed; 199 AA. AC A6Q497; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=NIS_1197; OS Nitratiruptor sp. (strain SB155-2). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nitratiruptor. OX NCBI_TaxID=387092; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB155-2; RX PubMed=17615243; DOI=10.1073/pnas.0700687104; RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.L., Takai K., RA Horikoshi K.; RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into RT emergence of pathogens."; RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009178; BAF70306.1; -; Genomic_DNA. DR RefSeq; YP_001356663.1; NC_009662.1. DR ProteinModelPortal; A6Q497; -. DR STRING; 387092.NIS_1197; -. DR EnsemblBacteria; BAF70306; BAF70306; NIS_1197. DR GeneID; 5360506; -. DR KEGG; nis:NIS_1197; -. DR PATRIC; 22684496; VBINitSp82229_1252. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NADIAFI; -. DR OrthoDB; EOG6WX4T9; -. DR BioCyc; NSP387092:GHA5-1236-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 199 AA; 22434 MW; 0ECA588F8AC78169 CRC64; MYPNDLYALC DRSLLKRFDI DLDGFLSIAQ RFGAKIVQYR NKSDDIEEKK KDLQYLRKGW KGILIVNDEL ALASLCDGVH IGQEDLDRLM VSFGIQSKNE ALSIIKKLYG AKIVGLSTHT LQEIREANEL DLEYVGLGAY RSSTTKDVQY VLGERLSDIA LRSKHKVVAI GGIRLFEPIE NVWLRAIGSD LLIKGLTFA // ID A6Q7N1_SULNB Unreviewed; 210 AA. AC A6Q7N1; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=SUN_0530; OS Sulfurovum sp. (strain NBC37-1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Sulfurovum. OX NCBI_TaxID=387093; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBC37-1; RX PubMed=17615243; DOI=10.1073/pnas.0700687104; RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.L., Takai K., RA Horikoshi K.; RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into RT emergence of pathogens."; RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009179; BAF71490.1; -; Genomic_DNA. DR RefSeq; YP_001357847.1; NC_009663.1. DR ProteinModelPortal; A6Q7N1; -. DR STRING; 387093.SUN_0530; -. DR EnsemblBacteria; BAF71490; BAF71490; SUN_0530. DR GeneID; 5362987; -. DR KEGG; sun:SUN_0530; -. DR PATRIC; 23774011; VBISulSp49917_0538. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SSP387093:GH25-540-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 210 AA; 23073 MW; 39345356C914C770 CRC64; MKFPKCNESP LGIYPVVDRA DKLRPLYECG ITTAQLRVKD MDGKALEQEI IEAIRISEEF KARLFVNDHW QLAIKHGAYG IHLGQEDIRE ADVAAIFDAG IRLGISTHTP EEIDIALGFE PSYIAIGPVF VPISKELKYN TVGIGLLKSW AESVDYPVVA IGGITLDNIK EVVQTKAASG IAMISGVLEA DKVSKEKTKV LIEVFETYGV // ID A6RCE6_AJECN Unreviewed; 447 AA. AC A6RCE6; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 16-APR-2014, entry version 34. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HCAG_07304; OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus) OS (Histoplasma capsulatum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Ajellomyces. OX NCBI_TaxID=339724; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NAm1 / WU24; RX PubMed=19717792; DOI=10.1101/gr.087551.108; RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., RA Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., RA Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., RA Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J., RA Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.; RT "Comparative genomic analyses of the human fungal pathogens RT Coccidioides and their relatives."; RL Genome Res. 19:1722-1731(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH476662; EDN10843.1; -; Genomic_DNA. DR RefSeq; XP_001537882.1; XM_001537832.1. DR ProteinModelPortal; A6RCE6; -. DR GeneID; 5443968; -. DR KEGG; aje:HCAG_07304; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 447 AA; 47452 MW; E100B5117B915828 CRC64; MDLSVYLVTD SSPAILRGRD LCEVVQDAIQ GGVTVVQYRD KHSDSGVMIE TAKRLHEITK KHNVPLIIND RVDVALAVGA EGVHLGQDDM SILDAKKLLP PNAYIGASVS SNEEALKAVQ DGADYLGIGT VFATPTKTNT KSIIGPAGTR EILAFLSTMP RRVGTVAIGG INLSNVQRVI YQSQAPLKSL DGAAIVSAIM AAENPREAAA SFCKLVKQIP ALATIPLPPR ENEVTLLLDQ VPDIVNLVAT RRPLCHNMIN FVVANFAANV AIAIGASPIM SGYGPEAVDL AKNGGSLLIN MGTLNNESID NYLQALQAYN AEGNPVVFDP VGAGATDVRR EAVKKLMAGG YFDLIKGNES ELIQLYGKVR GHQVGVDSGP STLNCKEKAR LVMDLAKRER NIALLTGAVD YLSDGERTLA IGNGHSLLGH ITGLVYFCSK LLLSALP // ID A6TVU4_ALKMQ Unreviewed; 196 AA. AC A6TVU4; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Amet_4232; OS Alkaliphilus metalliredigens (strain QYMF). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Alkaliphilus. OX NCBI_TaxID=293826; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QYMF; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Ye Q., RA Zhou J., Fields M., Richardson P.; RT "Complete sequence of Alkaliphilus metalliredigens QYMF."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000724; ABR50312.1; -; Genomic_DNA. DR RefSeq; YP_001321971.1; NC_009633.1. DR ProteinModelPortal; A6TVU4; -. DR STRING; 293826.Amet_4232; -. DR EnsemblBacteria; ABR50312; ABR50312; Amet_4232. DR GeneID; 5314313; -. DR KEGG; amt:Amet_4232; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEEAVIA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AMET293826:GI5P-4286-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 196 AA; 21345 MW; 037CC1B29DEEA0B4 CRC64; MLYLVTNRRM IEDHNFLSVI KGATNGGVDA IILREKDLSY KELLGLAKDI QGVVHGTNTR LIINNSLEVA NAVGAHGYHT GFQQFIEKRL HFQGGVGVSV HSIEEGIEAE NQGASYLLVG HIFETNSKKN LPPKGITFIE GFKKNIKIPI VAIGGINAGN IQQLCRVKVD GVAVMSEIMM ATDPHATTAK LKNLMK // ID A6UCW7_SINMW Unreviewed; 217 AA. AC A6UCW7; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 43. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Smed_2667; OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=366394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM419; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Reeve W.G., Richardson P.; RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000738; ABR61497.1; -; Genomic_DNA. DR RefSeq; YP_001328332.1; NC_009636.1. DR ProteinModelPortal; A6UCW7; -. DR STRING; 366394.Smed_2667; -. DR EnsemblBacteria; ABR61497; ABR61497; Smed_2667. DR GeneID; 5323536; -. DR KEGG; smd:Smed_2667; -. DR PATRIC; 23624479; VBISinMed134228_5868. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; SMED366394:GJAL-2709-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 217 AA; 22728 MW; 8481CDA6B6EE38D3 CRC64; MSKIEDRCRL VLVAPDIPDG LERVKLVGDA LKGGDVASVI VPQYGLSDAD FQKHAEALVP VIQKAGAAAL IEGDTRVAGR AKADGIHIAG AAAALAEAIE RHAPKLIVGG GNATDRHHAL EIGELRPDYV FFGRTDGDIK SEAHPKNLAL AEWWASMIEI PCIVMGGMDP QSALAVAETG AEFVALRLAV FGEAEQAPSV VAAVNALLDE KAPRFEG // ID A6UH45_SINMW Unreviewed; 201 AA. AC A6UH45; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Smed_4170; OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae). OG Plasmid pSMED01. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=366394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM419; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Reeve W.G., Richardson P.; RT "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000739; ABR62975.1; -; Genomic_DNA. DR RefSeq; YP_001312908.1; NC_009620.1. DR ProteinModelPortal; A6UH45; -. DR STRING; 366394.Smed_4170; -. DR EnsemblBacteria; ABR62975; ABR62975; Smed_4170. DR GeneID; 5318579; -. DR KEGG; smd:Smed_4170; -. DR PATRIC; 23613909; VBISinMed134228_0627. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SMED366394:GJAL-4231-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Plasmid; KW Thiamine biosynthesis; Transferase. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 177 178 THZ-P binding (By similarity). FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 201 AA; 22217 MW; 7070B8B11960FECB CRC64; MKLDPFYLIV NSAAWIERLV PLGVKLVQLR VKDLGADDIR SQIRLAKAVC SAHACQLIVN DYWRLAIEEG CDFVHLGQED LADADLGAIR AAGLKLGLST HDEAELETAL AAGPDYIALG PIYPTILKKM KWAPQGLERL STWRDRMGRL PLVAIGGLNP ERIEGVFAHG ADSAAVVTDI TLNADPEART REWIQRTDRR R // ID A6VB72_PSEA7 Unreviewed; 315 AA. AC A6VB72; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 57. DE SubName: Full=Probable pyrophosphohydrolase; GN OrderedLocusNames=PSPA7_4971; OS Pseudomonas aeruginosa (strain PA7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=381754; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PA7; RA Dodson R.J., Harkins D., Paulsen I.T.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000744; ABR85181.1; -; Genomic_DNA. DR RefSeq; YP_001350307.1; NC_009656.1. DR ProteinModelPortal; A6VB72; -. DR STRING; 381754.PSPA7_4971; -. DR EnsemblBacteria; ABR85181; ABR85181; PSPA7_4971. DR GeneID; 5359536; -. DR KEGG; pap:PSPA7_4971; -. DR PATRIC; 19831504; VBIPseAer80442_4745. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PAER381754:GHMY-4970-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34081 MW; EE7F5850805E94D7 CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EEGEPVRVAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEPHGAEGQ PLAWAEPREL ADYEFPAANV PIVQAARLPA HYLITPDGLE PGELISGVRK ALESGIRLIQ LRAPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDAEELAL AASMGVEFVT LSPVQPTESH PGAPALGWDK AAELIAGFNQ PVYLLGGVGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID A6VXY4_MARMS Unreviewed; 513 AA. AC A6VXY4; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 19-FEB-2014, entry version 60. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Mmwyl1_2391; OS Marinomonas sp. (strain MWYL1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=400668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MWYL1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Johnston A.W.B., Todd J.D., Rogers R., Wexler M., RA Bond P.L., Li Y., Richardson P.; RT "Complete sequence of Marinomonas sp. MWYL1."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000749; ABR71313.1; -; Genomic_DNA. DR RefSeq; YP_001341248.1; NC_009654.1. DR ProteinModelPortal; A6VXY4; -. DR STRING; 400668.Mmwyl1_2391; -. DR EnsemblBacteria; ABR71313; ABR71313; Mmwyl1_2391. DR GeneID; 5369154; -. DR KEGG; mmw:Mmwyl1_2391; -. DR PATRIC; 22468201; VBIMarSp124341_2469. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; MSP400668:GHKD-2434-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 513 AA; 55415 MW; 875FF0778A4350CF CRC64; MSIKPPVVWC VGGSDSSAHA GLQADLRTGQ DLRCHVQTIV TCITAQNSKE VRSVEPVSLA MFDEQWQTLL DDVPPDAIKV SLLPSIEIAK ACSIWLRRIK ADFPNVLVVF DPVMAASSES GNRLQQDSVG ASLLGSLLPY IDVITPNSIE FKRLTGLSDQ QPAVDIQGQL AVYLSSSKCA WLLKAGHSDS EQATDWLLDQ DSIVGFAYKR LSVHNTRGTG CTLSTALASF IAHGYDLLDA MTMAKAYITG ALKTGVQIGE GAGPLGRPGW PLQIENLPAI VSPYKLSTVT QAPMHQSFAK MDLDKMGLYP VVDSIAWLKL VLKQGVKLAQ LRIKDPDDAD LASKIQQAIA LGKEYEAQVF INDYWQEAIR FGAYGVHLGQ EDLDVADLAQ IQAAGLRLGI STHGYYEIAR AQSIQPSYIA LGHIFPTQTK DMPSQPQGLK RLSYYASLLK GVYPTVAIGG INAERLPAVA QTGVDSVALV TAITKVAEPE AATRSLICLF EKHSNTQRNT GGK // ID A6WNS1_SHEB8 Unreviewed; 632 AA. AC A6WNS1; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 57. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=Shew185_2322; OS Shewanella baltica (strain OS185). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=402882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS185; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Brettar I., Rodrigues J., RA Konstantinidis K., Tiedje J., Richardson P.; RT "Complete sequence of chromosome of Shewanella baltica OS185."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000753; ABS08460.1; -; Genomic_DNA. DR RefSeq; YP_001366523.1; NC_009665.1. DR ProteinModelPortal; A6WNS1; -. DR STRING; 402882.Shew185_2322; -. DR EnsemblBacteria; ABS08460; ABS08460; Shew185_2322. DR GeneID; 5370106; -. DR KEGG; sbm:Shew185_2322; -. DR PATRIC; 23461455; VBISheBal127872_2531. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SBAL402882:GJ99-2385-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 632 AA; 66915 MW; 05DCA191EB5A53C6 CRC64; MSTERPAFVW TIAGSDSGGG AGIQADLATI QDLGCHGCSV VTTVTAQSSV AVTLVEPVSA AMLMAQLTTL LSDLPPKAIK IGLLADQTQV ALLADWIASF KIHYPSVPVI VDPVMVASCG DALAVDNCQD IKSAAKSALD FRPFKGLIEL ITPNVLELGR LTHSDVSTKA QFAAAALALS QSLDCSVLAK GGDVSFGSTD ILENTHAKTH DNTYAQTQAN AHNSNGWDLE LAEDYLVCHQ VRASSKLHQN GRFWLASQRV NTRHNHGSGC TLSSAIAAVL AQGFVLQDAV VVAKAYVSQG LSAAIGLGQG PGPLARTGWP NNLSRYAKIN LCDGNFIRHH LNRHLDVRSD LVATVLSATD QATAQVRIAS TPPQNILSHG FKVLDAELGV YPVVSDLTML ESLLAAGVKT VQLRIKTDIS ELTTTTAPAE SDLGKSALGR CESGEPELIG SELEAQIQTA IALGKHFNAQ LFINDHWKLA IKYHAFGVHL GQEDLAVTDL AAIQAAGLAL GISSHSYFEL LLAHQYSPSY IALGHIFPTT TKQMPSAPQG LAKLKHYVAL LQGHYPLVAI GGIDLTNLAK VKATGVGNIA VVRAITKAKE PVAAFAELSQ AWEQCSLCEE LAVKQELDAK HE // ID A6WVK8_OCHA4 Unreviewed; 209 AA. AC A6WVK8; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Precursor; GN OrderedLocusNames=Oant_0281; OS Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Ochrobactrum. OX NCBI_TaxID=439375; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49188 / DSM 6882 / NCTC 12168; RX PubMed=21685287; DOI=10.1128/JB.05335-11; RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., RA Shin M., Ugalde R.A., Garcia E., Tolmasky M.E.; RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile RT opportunistic pathogen and symbiont of several eukaryotic hosts."; RL J. Bacteriol. 193:4274-4275(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000758; ABS13012.1; -; Genomic_DNA. DR RefSeq; YP_001368841.1; NC_009667.1. DR ProteinModelPortal; A6WVK8; -. DR STRING; 439375.Oant_0281; -. DR EnsemblBacteria; ABS13012; ABS13012; Oant_0281. DR GeneID; 5379243; -. DR KEGG; oan:Oant_0281; -. DR PATRIC; 20465547; VBIOchAnt73124_0301. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; OANT439375:GJIT-284-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 209 AA; 23301 MW; F32F1B18C2F43C2D CRC64; MALDPFYPIF DSAKWLERMV PLGVKLVQLR VKDKSEPELR SEIRAAREIC LAHNCQLIVN DYWKLALEEG CDFIHLGQED LDDADLSAIR DGGLKLGVSS HDEAELDRAL SVKPDYIALG PIYPTILKKM KWHEQGLPRL GQWKARIGDI PLVGIGGMSV ERAPGVFEAG ADIVSVVTDI TLNADPESRL RQWIETTRAY AGHALEQTT // ID A6WY71_OCHA4 Unreviewed; 221 AA. AC A6WY71; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 44. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Oant_1208; OS Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Ochrobactrum. OX NCBI_TaxID=439375; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49188 / DSM 6882 / NCTC 12168; RX PubMed=21685287; DOI=10.1128/JB.05335-11; RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., RA Shin M., Ugalde R.A., Garcia E., Tolmasky M.E.; RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile RT opportunistic pathogen and symbiont of several eukaryotic hosts."; RL J. Bacteriol. 193:4274-4275(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000758; ABS13925.1; -; Genomic_DNA. DR RefSeq; YP_001369754.1; NC_009667.1. DR ProteinModelPortal; A6WY71; -. DR STRING; 439375.Oant_1208; -. DR EnsemblBacteria; ABS13925; ABS13925; Oant_1208. DR GeneID; 5380462; -. DR KEGG; oan:Oant_1208; -. DR PATRIC; 20467495; VBIOchAnt73124_1262. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; OANT439375:GJIT-1224-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23250 MW; 9A9EC44833A71EE4 CRC64; MNTPAHQTET ERCRIVLVAP PLADGAALAK LLTAALSGGD VASVILDTGD LDEATFQATA EKVIPVIQEK GAAALILNDT RIAGRVGADG VHIEGKAADL ADAIEKHTPK MIVGTGNLRD RHGAMEIGEL QPDYVFFGKI GADNKPDAHP RNLSLAEWWS QMVEIPSIAQ AGSTLESIIP AAETGADFVA LGRAVFDAED PAKAVAEANR LLDENAPRFE N // ID A6XZE5_VIBCL Unreviewed; 440 AA. AC A6XZE5; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 19-FEB-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=A33_0087; OS Vibrio cholerae AM-19226. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=404974; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AM-19226; RA Heidelberg J., Sebastian Y.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS265253; EDN14208.1; -; Genomic_DNA. DR ProteinModelPortal; A6XZE5; -. DR EnsemblBacteria; EDN14208; EDN14208; A33_0087. DR PATRIC; 28029927; VBIVibCho101866_3188. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48959 MW; 4CF50C0429B3FD41 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGFA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQEETSEPCD YYLDYVSENR VLPEAMMCNA RCSVTVGLHD EYGFTLDKWQ YGNAAEQLII YSSETHRLNS KLNQHLAWVL ATLTLDFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPA MQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QVDLTSANLT ELLDAGIRLG LSTHCYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CSNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID A6ZW41_YEAS7 Unreviewed; 540 AA. AC A6ZW41; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 19-FEB-2014, entry version 33. DE SubName: Full=Hydroxyethylthiazole kinase; GN Name=THI6; ORFNames=SCY_5518; OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=307796; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJM789; RX PubMed=17652520; DOI=10.1073/pnas.0701291104; RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z., RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., RA Wang X., Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., RA Li Y., Davis R.W., Steinmetz L.M.; RT "Genome sequencing and comparative analysis of Saccharomyces RT cerevisiae strain YJM789."; RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAFW02000135; EDN60933.1; -; Genomic_DNA. DR ProteinModelPortal; A6ZW41; -. DR SMR; A6ZW41; 3-536. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 540 AA; 58059 MW; F34FA1E0B76E3930 CRC64; MVFTKEEVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDIE TKNFVAEALE VQKICKKYNV PLIINDRIDV AMAIDADGVH VGQDDMPIPM VRKLLGPSKI LGWSVGKPSE VETLAKWGPD MVDYIGVGTL FPTSTKKNPK KSPMGPQGAI AILDALEEFK ATWCRTVGIG GLHPDNIQRV LCQCVASNGK RSLDGISLVS DIMAAPDACA ATKRLRGLLD ATRYQFVECE LNNTFPTTTS IQNVISQVSN NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL ARIPNASLLL NTGSVAPIEM LKAAINAYNE VNRPITFDPV GYSATETRLC LNNTLLTYGQ FACIKGNCSE ILSLAKLNNH KMKGVDSSSG KTNIDTLVRA TQIVAFQYRT VAVCTGEFDC VADGTFGGEY KLSSGTEGIT AEDLPCVIIE DGPIPIMGDI TASGCSLGST IASFIGGLDS TGKLFDAVVG AVLLYKSAGK LASTRCQGSG SFHVELIDAL YQLFHENKPE KWSASLKKFK // ID A7A8T5_BIFAD Unreviewed; 251 AA. AC A7A8T5; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BIFADO_02277; OS Bifidobacterium adolescentis L2-32. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=411481; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-32; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-32; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bifidobacterium adolescentis (L2-32)."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXD02000074; EDN82150.1; -; Genomic_DNA. DR ProteinModelPortal; A7A8T5; -. DR EnsemblBacteria; EDN82150; EDN82150; BIFADO_02277. DR PATRIC; 27190119; VBIBifAdo136061_1874. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 156 158 THZ-P binding (By similarity). FT REGION 215 216 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 108 108 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 127 127 HMP-PP (By similarity). FT BINDING 159 159 HMP-PP (By similarity). FT BINDING 195 195 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 251 AA; 26706 MW; EC3CD76CB03C6CB1 CRC64; MNNYPFASMR DCFDMSAYFV VGPQDCKGRP VTDVVDDALR GGATFIQLRA KNADAKDITE MARDIAQVIK NSGKSDSVAF VIDDRVDVVW QARDKGIKVD GVHIGQTDME PQEARALLGE DAIVGLSAET ESLVKLINEL PSGCIDYIGA GPLHVSTTKP EASVGGNDGS GHTLDEEQIN AICAASEFPV VVGGGVHADD TEMLARSKAA GWFVVSAIAG ADDPEAATRE MVTRWKAVRG DAKHGYAPRV K // ID A7ALP7_9PORP Unreviewed; 245 AA. AC A7ALP7; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PARMER_04381; OS Parabacteroides merdae ATCC 43184. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=411477; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43184; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43184; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Parabacteroides merdae (ATCC 43184)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXE02000118; EDN84293.1; -; Genomic_DNA. DR ProteinModelPortal; A7ALP7; -. DR EnsemblBacteria; EDN84293; EDN84293; PARMER_04381. DR PATRIC; 25877495; VBIParMer55919_3595. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 53 57 HMP-PP binding (By similarity). FT REGION 155 157 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 HMP-PP (By similarity). FT BINDING 191 191 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 245 AA; 27552 MW; D9C0589CA004789B CRC64; MELDDFLYTS AGRGRYACFT GTNRLMFITH RTNKYTELDE VKMVTKGGCT WVQLRMKENL NLEVAKAIAH FTLFDCDTDC ACCLDDDLEM AFKAGIHCVH LGKNDIPVSE AWHRIIEKGK EDLFLVGATA NTFEDILKAD REGASYIGLG PYRYTETKKN LSPVLGLEGY RKIMEQCREA GLEIPIFAIG GIEFEDIAPL METGIEGIAV SGAIINAEDP VEETRRFIRE INKHKPDPCR DDSEI // ID A7ALP8_9PORP Unreviewed; 199 AA. AC A7ALP8; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 16-OCT-2013, entry version 31. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=PARMER_04382; OS Parabacteroides merdae ATCC 43184. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=411477; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43184; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43184; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Parabacteroides merdae (ATCC 43184)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXE02000118; EDN84294.1; -; Genomic_DNA. DR ProteinModelPortal; A7ALP8; -. DR EnsemblBacteria; EDN84294; EDN84294; PARMER_04382. DR PATRIC; 25877497; VBIParMer55919_3596. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 22260 MW; A41BD7D6B72CCEF5 CRC64; MKKLIVITSP YFFKGEDCIL SHLFDEGMQH LHLRKPDSEA NELRKLLDRI PDIYYPKVVL HDCFNLAVEY GLGGIHLNRR NNQSPDGFTG TISCSCHSIE ELEQFGKLDY LFLSPIFQSI SKEGYGNGFK PETLRQASNA GIINDKVIAL GGIDLTTLPL LRPFRFGGAA VLGAVWGNSP SADKEDSIIT QYKKLQAWN // ID A7B0X1_RUMGN Unreviewed; 211 AA. AC A7B0X1; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 19-FEB-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RUMGNA_01197; OS Ruminococcus gnavus ATCC 29149. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=411470; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29149; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29149; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Ruminococcus gnavus (ATCC 29149)."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYG02000010; EDN78460.1; -; Genomic_DNA. DR ProteinModelPortal; A7B0X1; -. DR EnsemblBacteria; EDN78460; EDN78460; RUMGNA_01197. DR PATRIC; 29784450; VBIRumGna65643_1036. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22887 MW; E3DC0B31E1BE3103 CRC64; MRCDKESLLL YAVTDRSWTK NDTLYHQVEE ALKGGVTFLQ LREKDLNTEN FLQEAEEMKK LCAAYRVPFV INDNVEIART VGADGVHVGQ DDMPAWKVRE ILGEDKIIGV SAQTVEQAIK AEKDGADYLG VGAVFPTSSK ADAVEVEHAT LRDICVAVQI PVVAIGGISA ENVSQLAGTG IDGIAVISAI FAQDFPKLAA EELKKKVEAI Q // ID A7BQL5_9GAMM Unreviewed; 210 AA. AC A7BQL5; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 19-MAR-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BGP_4303; OS Beggiatoa sp. PS. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Thiotrichaceae; Beggiatoa. OX NCBI_TaxID=422289; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PS; RA Mussmann M., Hu F.Z., Richter M., de Beer D., Preisler A., RA Jorgensen B.B., Huntemann M., Glockner F.O., Amann R., Koopman W.J.H., RA Janto B., Hogg J., Boissy R., Lasken R.S., Stoodley P., Ehrlich G.D.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABBZ01000042; EDN71162.1; -; Genomic_DNA. DR ProteinModelPortal; A7BQL5; -. DR EnsemblBacteria; EDN71162; EDN71162; BGP_4303. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22766 MW; C3DB18F896B91858 CRC64; MSPRPHILTG LYAITDNNLI PKQRFIETVE LAIIGGAKII QYRDKSDDKK HRLQQAHALK QLCHHYQIPL LINDDIALAQ QVGAEGVHLG KEDVSLSTAR AVLGEKAIIG VSCYNQLPLA LKAIEAGATY VAYGRFFPSQ SKPNAIQANI ALLHQTRQQL DCPLVAIGGI TPDNGSELIK AGVNCLAVIQ GLFGQPDVKV AAQRYAQLFA // ID A7BWN4_9GAMM Unreviewed; 314 AA. AC A7BWN4; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 19-MAR-2014, entry version 43. DE SubName: Full=Mutator mutT protein; GN ORFNames=BGP_0120; OS Beggiatoa sp. PS. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Thiotrichaceae; Beggiatoa. OX NCBI_TaxID=422289; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PS; RA Mussmann M., Hu F.Z., Richter M., de Beer D., Preisler A., RA Jorgensen B.B., Huntemann M., Glockner F.O., Amann R., Koopman W.J.H., RA Janto B., Hogg J., Boissy R., Lasken R.S., Stoodley P., Ehrlich G.D.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABBZ01000587; EDN69051.1; -; Genomic_DNA. DR ProteinModelPortal; A7BWN4; -. DR EnsemblBacteria; EDN69051; EDN69051; BGP_0120. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 314 AA; 35808 MW; 8B174342A3C06C6F CRC64; MNEFLHVVAG VIYNAQKEIL LAYRPKHTHQ GGLWEFPGGK RQPQETVEQA LVRELQEEIG ITVQQTRPLI RIAHTYPERK VLLDVWEIEQ WQDKAYGREG QLIQWCPIDS LRNHSFPAAN YPIITAVQLP SHYLITPEPV SWHDKKFFYR LEQCLDGEIS LMQLRAKNLS ERDYCYCAEK TLTLCDRYDT KLLANATAEM ALSVGTHGVH LTSERLLTCT ERPLDKTLWV AASCHSIAEI EQANQIGIDF IVLSPVRPTE SHPEVQPLGW FEFFQRTEQA NCPVFALGGM KWEDTAIALA HGAQGIAAIS AFWQ // ID A7F7I3_SCLS1 Unreviewed; 521 AA. AC A7F7I3; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 16-APR-2014, entry version 38. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=SS1G_13563; OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White OS mold) (Whetzelinia sclerotiorum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Sclerotinia. OX NCBI_TaxID=665079; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 18683 / 1980 / Ss-1; RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230; RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., RA Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., RA Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., RA Pradier J.-M., Quevillon E., Sharon A., Simon A., ten Have A., RA Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., RA Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., RA Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., RA Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., RA Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., RA Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., RA Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., RA Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., RA Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.; RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia RT sclerotiorum and Botrytis cinerea."; RL PLoS Genet. 7:E1002230-E1002230(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH476646; EDN98704.1; -; Genomic_DNA. DR RefSeq; XP_001585324.1; XM_001585274.1. DR ProteinModelPortal; A7F7I3; -. DR STRING; 665079.A7F7I3; -. DR GeneID; 5481518; -. DR KEGG; ssl:SS1G_13563; -. DR eggNOG; COG0352; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 521 AA; 54746 MW; F7B5832C7078844F CRC64; MAFKNVDYSL YLVTDSTSAI LGNRDLVDVV EAAIRGGVTI VQYRDKFSDT AALVTTARKL HTVTQKYKVP LLINDRIDVA LAIGCEGVHI GQDDMDLKTA RILLGEDAII GVTVSSVEEA MIASEHGADY LGIGTMFATP TKTNTKDIIG TAGTKEILHS LQQSGSKVHT VAIGGINSLN LQRVLYQSAA EGKQLDGVAI VSAIITAQDV ETAASELAEL IRTPAPFASA HIPNDQTKKD PCDLLLQVPG VIGQVAKRTP LSHNMTNLVV QNFAANVALA IGASPIMANY GEEAPGLASL GGGLVINMGT VTPEGIENYS KALKAYNREG GPVVLDPVGC GATAVRRSAV KTLLGAGYFD VIKGNEGEIK TVSGSSIQQR GVDSGASTSS LTEKATIVRD LALRERNVVL MTGAVDILSD GLRTFAIKNG HEILGRITGS GCVLGTIISA MLAVNRGDKL LAVLSALLHY EIAAETAAVR DDVRGPGTFV PALIDELYIL QKANSGGDLR WLEKARVEAI L // ID A7GLF5_BACCN Unreviewed; 206 AA. AC A7GLF5; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bcer98_0616; OS Bacillus cereus subsp. cytotoxis (strain NVH 391-98). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315749; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NVH 391-98; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., RA Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.H., RA Sanchis V., Nguen-The C., Lereclus D., Richardson P., Wincker P., RA Weissenbach J., Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000764; ABS20963.1; -; Genomic_DNA. DR RefSeq; YP_001373958.1; NC_009674.1. DR ProteinModelPortal; A7GLF5; -. DR STRING; 315749.Bcer98_0616; -. DR EnsemblBacteria; ABS20963; ABS20963; Bcer98_0616. DR GeneID; 5345989; -. DR KEGG; bcy:Bcer98_0616; -. DR PATRIC; 18929627; VBIBacCyt128034_0659. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCYT315749:GH2A-727-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 23121 MW; 9CE531367D5BFEFB CRC64; MKNELHVISN GQMTFEELTN VAMQMESEID YLHIREREKS TKELYEGVEG LLKRGFPASK LVLNDRIDIA ILLNIPRVQL GYRSVDVKSV KEKFSYLHVG YSVHSLEEAI VAFKNGADSL VYGHVFPTSC KKGVPARGLE EISDMARRLT IPITAIGGIT PENTTEVLKS GVSGIAVMSG IVSDRNPYEK ARLYKEIIRK WAENHE // ID A7GXD2_CAMC5 Unreviewed; 203 AA. AC A7GXD2; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CCV52592_0497; OS Campylobacter curvus (strain 525.92). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360105; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=525.92; RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., RA Mandrell R.E., Lastovica A.J., Nelson K.E.; RT "Genome sequence of Campylobacter curvus 525.92 isolated from human RT feces."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000767; EAU00719.1; -; Genomic_DNA. DR RefSeq; YP_001407874.1; NC_009715.1. DR ProteinModelPortal; A7GXD2; -. DR STRING; 360105.CCV52592_0497; -. DR EnsemblBacteria; EAU00719; EAU00719; CCV52592_0497. DR GeneID; 5407387; -. DR KEGG; ccv:CCV52592_0497; -. DR PATRIC; 20031574; VBICamCur47627_0605. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CCUR360105:GJ9P-618-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 22159 MW; C3F8C446AFAFB985 CRC64; MSQIYAISDD TLTPDETIIS QATEILRNGV KFFQYRSKKP VKNEKIAREL LTLCDDFKAK FIVNDDVKFA ASIGAKCVHI GIDDMDISSA REILGDDAFI GVSCYNDLNL ALKAQQNGAS YVAFGSVFKS RTKPDAVICP LETIKQAKEI LNIPICAIGG INASNIAQIS ALRIDLIAVI NAVYRPKSIG ENLARLRLAM SCL // ID A7GYH4_CAMC5 Unreviewed; 224 AA. AC A7GYH4; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 41. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=CCV52592_1869; OS Campylobacter curvus (strain 525.92). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360105; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=525.92; RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., RA Mandrell R.E., Lastovica A.J., Nelson K.E.; RT "Genome sequence of Campylobacter curvus 525.92 isolated from human RT feces."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000767; EAU00105.1; -; Genomic_DNA. DR RefSeq; YP_001408266.1; NC_009715.1. DR ProteinModelPortal; A7GYH4; -. DR STRING; 360105.CCV52592_1869; -. DR EnsemblBacteria; EAU00105; EAU00105; CCV52592_1869. DR GeneID; 5406877; -. DR KEGG; ccv:CCV52592_1869; -. DR PATRIC; 20032418; VBICamCur47627_1017. DR eggNOG; COG0352; -. DR HOGENOM; HOG000002417; -. DR KO; K00788; -. DR OMA; ASHIFAT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CCUR360105:GJ9P-1054-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 224 AA; 24787 MW; 32CE5DB962A128FE CRC64; MFKILIIADP KLAGGDLLER IAGLCETGVD AVLLRAKFLS EEEFRALAIS VKQICDKFGR EFIINQFFNV ACELKSSFWL TSAQIDLLQN FSDTSDEFGL NFAKFKDFKD MATKFTTISP ALKIYAPAHD QAQAEISAKF ADILIASHIF ATSCKAGLKP KGPALIRKIK ARVDRQVYAL GGINKLNFRS VLDVGADGIC LMSEAMRCEN EREFINGFLA DTLV // ID A7H2Z8_CAMJD Unreviewed; 203 AA. AC A7H2Z8; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 43. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=JJD26997_0738; OS Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / OS 269.97). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1458 / RM4099 / 269.97; RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., RA Mandrell R.E., Lastovica A.J., Nelson K.E.; RT "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97 RT isolated from human blood."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000768; ABS43645.1; -; Genomic_DNA. DR RefSeq; YP_001397878.1; NC_009707.1. DR ProteinModelPortal; A7H2Z8; -. DR STRING; 360109.JJD26997_0738; -. DR EnsemblBacteria; ABS43645; ABS43645; JJD26997_0738. DR GeneID; 5390038; -. DR KEGG; cjd:JJD26997_0738; -. DR PATRIC; 20047127; VBICamJej122183_0737. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CJEJ360109:GJDG-711-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 203 AA; 23658 MW; F2BC30BD96AEE407 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINIAGVCMR EILMKEKDLK TYIQVCKERL FHE // ID A7H6E9_ANADF Unreviewed; 222 AA. AC A7H6E9; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Anae109_0075; OS Anaeromyxobacter sp. (strain Fw109-5). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=404589; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fw109-5; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Fields M., Richardson P.; RT "Complete sequence of Anaeromyxobacter sp. Fw109-5."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000769; ABS24295.1; -; Genomic_DNA. DR RefSeq; YP_001377279.1; NC_009675.1. DR ProteinModelPortal; A7H6E9; -. DR STRING; 404589.Anae109_0075; -. DR EnsemblBacteria; ABS24295; ABS24295; Anae109_0075. DR GeneID; 5374016; -. DR KEGG; afw:Anae109_0075; -. DR PATRIC; 20925189; VBIAnaSp113478_0082. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6ZPT20; -. DR BioCyc; ASP404589:GHMT-77-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 21996 MW; 9C7671706C818079 CRC64; MPTSDGSAGA ARRARLAGLY AIVGGAAAVE QARAAIAGGA RVVQVRIKDA PAGAVLAAAR EIVALARGRA LVIVNDRADL ALLSGADGVH LGDEDLPPAE ARRLLGPDLL VGRTTRTLEE AREALREGAD HVGFGPIFPT GSKALAVPAR GAGMLREVAA ALAAPVVAIG GIGPANAGEV ARAGAACAAV IGALFDAGDA RANAERLAAA FEAGRAAREA TR // ID A7HA10_ANADF Unreviewed; 206 AA. AC A7HA10; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Anae109_1348; OS Anaeromyxobacter sp. (strain Fw109-5). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=404589; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fw109-5; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Fields M., Richardson P.; RT "Complete sequence of Anaeromyxobacter sp. Fw109-5."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000769; ABS25556.1; -; Genomic_DNA. DR RefSeq; YP_001378540.1; NC_009675.1. DR ProteinModelPortal; A7HA10; -. DR STRING; 404589.Anae109_1348; -. DR EnsemblBacteria; ABS25556; ABS25556; Anae109_1348. DR GeneID; 5373960; -. DR KEGG; afw:Anae109_1348; -. DR PATRIC; 20927877; VBIAnaSp113478_1418. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ASP404589:GHMT-1357-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 20760 MW; AB0B57878FECD98C CRC64; MAVPVVHLIT DRRLARDLPA RLAAALAGLP PGRVLVQLRE KDLGGRDLLA LARAVAAACR AAGQRIVVND RVDVALAAGA DGVHLPAAGI PAADARRLLG PDALVGVSCH SAAEVRRARD AGASFATVSP IYDTPSKRGY GPPVGLAVLR EAAALGLPIV ALGGITPARV PEVIAAGAHG VAAIRAWLEG GDPAAAVRAL LPATRS // ID A7HSM1_PARL1 Unreviewed; 202 AA. AC A7HSM1; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 13-NOV-2013, entry version 41. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Plav_1284; OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhodobiaceae; Parvibaculum. OX NCBI_TaxID=402881; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Richardson P.; RT "Complete genome sequence and annotation of Parvibaculum RT lavamentivorans DS-1."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000774; ABS62904.1; -; Genomic_DNA. DR RefSeq; YP_001412561.1; NC_009719.1. DR ProteinModelPortal; A7HSM1; -. DR STRING; 402881.Plav_1284; -. DR EnsemblBacteria; ABS62904; ABS62904; Plav_1284. DR GeneID; 5454786; -. DR KEGG; pla:Plav_1284; -. DR PATRIC; 22864166; VBIParLav90819_1322. DR eggNOG; NOG323178; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ACHSERA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PLAV402881:GHQA-1298-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 21406 MW; D279150E8BFBFD96 CRC64; MRAARRLSPD ADAITLIGMT DPERLSDPLA ALAALPRGSA LIWRTYDEPP AAGMLRRLAA HARARKCLLL LAGHPRTARR LGTHGLHLPE RALSRRFENG YLLSRRDLPP SFVVTAACHS ERAIVAAARA GVDAVLISPV FATASHPGGQ PLGVMRFAHL ARLARSFGME PYALGGIATA DSIRRLSGST AAGVAGISLL MP // ID A7HUY5_PARL1 Unreviewed; 223 AA. AC A7HUY5; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Precursor; GN Name=thiE; OrderedLocusNames=Plav_2104; OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhodobiaceae; Parvibaculum. OX NCBI_TaxID=402881; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Richardson P.; RT "Complete genome sequence and annotation of Parvibaculum RT lavamentivorans DS-1."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000774; ABS63718.1; -; Genomic_DNA. DR RefSeq; YP_001413375.1; NC_009719.1. DR ProteinModelPortal; A7HUY5; -. DR STRING; 402881.Plav_2104; -. DR EnsemblBacteria; ABS63718; ABS63718; Plav_2104. DR GeneID; 5454203; -. DR KEGG; pla:Plav_2104; -. DR PATRIC; 22865889; VBIParLav90819_2170. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PLAV402881:GHQA-2130-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23915 MW; 2583D58885D8F084 CRC64; MSDPDQRPAC RLYLITPPRF EPRAFADTFK AALDAGDVAS LQLRLKGDNE APPAADDIRY ATEILMPLAR ERDVAFIIND RPDLAAELDA DGVHVGQDDM SCREARKLVG PDRAVGVTCH SSRHLAMEAG EAGADYVAFG AFYETDTKIP ISKAEPEILT WWANLFVLPC VAIGGITVAN AAPLVRAGAD FLAVSSGVWA HEDGPAAAVR KLNVIMAEES AAR // ID A7I0J1_CAMHC Unreviewed; 204 AA. AC A7I0J1; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CHAB381_0436; OS Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / OS CH001A). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360107; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A; RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., RA Mandrell R.E., Nelson K.E.; RT "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a RT commensal isolated from the human gastrointestinal tract."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000776; ABS50890.1; -; Genomic_DNA. DR RefSeq; YP_001406032.1; NC_009714.1. DR ProteinModelPortal; A7I0J1; -. DR STRING; 360107.CHAB381_0436; -. DR EnsemblBacteria; ABS50890; ABS50890; CHAB381_0436. DR GeneID; 5409611; -. DR KEGG; cha:CHAB381_0436; -. DR PATRIC; 20039032; VBICamHom81367_0427. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CHOM360107:GHCX-439-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22764 MW; 4F53AD9929305D71 CRC64; MSEIYALSDD FFTPEDVIVK SIHEILDNGI KFVQFRSKKK EKNEKIISEL IRLCDDYHAY LIINDDALLA RKLGAHGVHI GKDDGSIIKA REILGENKII GVSCYDDLTL ALNAQQNGAS YAAFGAVFKS PTKKDAKICN HDVLKKAAEI LKIPTCVIGG INAGNLRQIL KFHPNFVAIV SALYHPRSIT ENLKNLQRII NEYN // ID A7I2I9_CAMHC Unreviewed; 194 AA. AC A7I2I9; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 13-NOV-2013, entry version 42. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=CHAB381_1175; OS Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / OS CH001A). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360107; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A; RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., RA Mandrell R.E., Nelson K.E.; RT "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a RT commensal isolated from the human gastrointestinal tract."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000776; ABS52540.1; -; Genomic_DNA. DR RefSeq; YP_001406730.1; NC_009714.1. DR ProteinModelPortal; A7I2I9; -. DR STRING; 360107.CHAB381_1175; -. DR EnsemblBacteria; ABS52540; ABS52540; CHAB381_1175. DR GeneID; 5409287; -. DR KEGG; cha:CHAB381_1175; -. DR PATRIC; 20040468; VBICamHom81367_1129. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; ASHIFAT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CHOM360107:GHCX-1179-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21879 MW; 5CC69CFCBF7F32B1 CRC64; MCKIFAVTNS EICGGFENLK IKVLRLCEAE ISGIIYRDKA LNSADYEKNF IEILKICKNF GVKLFLHNFY EVALKLNYPY IWLPLPTLKM CSAKNFKEIT VSAHNVYEAK EALGFGATAL CLSHIFKTSC KAELTPKGVN LIKNVREFFD GEIYALGGIS PNNFNEILLA GTNNLCLMSS LMQIQNEKEL LNKF // ID A7IHH7_XANP2 Unreviewed; 213 AA. AC A7IHH7; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 42. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Xaut_2226; OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Xanthobacter. OX NCBI_TaxID=78245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1158 / Py2; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., RA Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Ensigns S.A., Richardson P.; RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000781; ABS67470.1; -; Genomic_DNA. DR RefSeq; YP_001417127.1; NC_009720.1. DR ProteinModelPortal; A7IHH7; -. DR STRING; 78245.Xaut_2226; -. DR EnsemblBacteria; ABS67470; ABS67470; Xaut_2226. DR GeneID; 5425317; -. DR KEGG; xau:Xaut_2226; -. DR PATRIC; 24046545; VBIXanAut29526_2562. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VMRAEDP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XAUT78245:GHS6-2249-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 213 AA; 21334 MW; C8B6F48B45577820 CRC64; MLPEPPLLLI TDRTLAQGDL AQVAMEACVG GCRWISFREK DLPAAEQIAL FAHLREATRA FRPRLTLHGP ADLAAAAGAD GVHLSGGGHA GAARALLGPD ALVGLSVHTL AEAQAADGAS LDYITVSPVF LTASKPGHGP ALGASGLAAF VAASPVPVIA LAGIAPDNAR VCRDAGAAGL AVMGSVMRAE DPAAEFSALL AAWDGKGPNS ARA // ID A7IJW5_XANP2 Unreviewed; 208 AA. AC A7IJW5; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 41. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN OrderedLocusNames=Xaut_3078; OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Xanthobacter. OX NCBI_TaxID=78245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1158 / Py2; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., RA Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Ensigns S.A., Richardson P.; RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000781; ABS68308.1; -; Genomic_DNA. DR RefSeq; YP_001417965.1; NC_009720.1. DR ProteinModelPortal; A7IJW5; -. DR STRING; 78245.Xaut_3078; -. DR EnsemblBacteria; ABS68308; ABS68308; Xaut_3078. DR GeneID; 5424081; -. DR KEGG; xau:Xaut_3078; -. DR PATRIC; 24048241; VBIXanAut29526_3403. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVSAHED; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; XAUT78245:GHS6-3108-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 21262 MW; A96A3043CC25AA6A CRC64; MSSPLPPPGA RLMLVFTLTP ELRPDAAAAA VRAGDVAAVV LRVPKDGAPD IRHLRAVAEA LQKHDAAVLV EGPDTLVTAA GLDGVHVSDL RGLQAALREL KPQAIVGAGG LASRHDAMEA GESGADYVFF GALEPRPGDA PEILDLVAWW AELFEVPCVG LAASLDEAEA LAQAGADFVA LAEALVADGG AATVTAAMDR LSRVDAQP // ID A7JV63_PASHA Unreviewed; 509 AA. AC A7JV63; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 19-FEB-2014, entry version 45. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN Name=thiDE; ORFNames=MHA_2051; OS Mannheimia haemolytica PHL213. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Mannheimia. OX NCBI_TaxID=272629; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PHL213; RX PubMed=17015664; DOI=10.1128/JB.00675-06; RA Gioia J., Qin X., Jiang H., Clinkenbeard K., Lo R., Liu Y., Fox G.E., RA Yerrapragada S., McLeod M.P., McNeill T.Z., Hemphill L., Sodergren E., RA Wang Q., Muzny D.M., Homsi F.J., Weinstock G.M., Highlander S.K.; RT "The genome sequence of Mannheimia haemolytica A1: insights into RT virulence, natural competence, and Pasteurellaceae phylogeny."; RL J. Bacteriol. 188:7257-7266(2006). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PHL213; RA Giola J., Qin X., Jiang H., Clinkenbeard K., Lo R., Liu Y., Fox G.E., RA Yerrapragada S., McLeod M.P., McNeill T.Z., Hemphill L., Sodergren E., RA Wang Q., Muzney D.M., Homsi F.J., Weinstock G.M., Highlander S.K.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS264648; EDN74949.1; -; Genomic_DNA. DR ProteinModelPortal; A7JV63; -. DR EnsemblBacteria; EDN74949; EDN74949; MHA_2051. DR PATRIC; 28799803; VBIManHae426_1807. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 509 AA; 55321 MW; 0174E0A5ACE3E9C8 CRC64; MSNYSNSPYQ PNVIWTVAGS DSCAGAGLQT DLHTFHDFNL VGCSVVTSVT AQHPHGVLCV TPVDDHTFRQ QFEALLVQGY PNAIKIGLLC SQAQVEILCE YIQKIRAESS HYCYVVYDPV AVASSGQALS DSILLQIVQQ KLYPLVDLIT PNGTELALLS DTEIQTFGDV KTASHKLFAQ GIKAVLAKGG HFEWLGETVR DYLLTANEIY AFSHARQQSV NTHGTGCTYA SAVGAMLATG FDLADAVTVA TAYLQKGLSE KQGRGQTALS SLCHTGYPDD IAFFPQTELI SAPLKLPKEP FAPTEYQLGL YPVVDSVKWL ERLILVGVKT LQIRIKNRPL AEIEQEIAHS VALAKQHNVR LFVNDYWQLA MKYQAYGVHL GQEDLATADL NAIQQSGLRL GVSTHCYFEI MRALAVKPSY IAFGHVFPTQ TKVMPSQPQG LTNLAKYVAL VAPLNIPTVA IGGINEQSIE NVMHTGVGSA AVVSAVTQAK DWQQAVKNLA KFANGGRNE // ID A7JY48_VIBSE Unreviewed; 204 AA. AC A7JY48; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=VEA_000869; ORFNames=VEx25_A1573; OS Vibrio sp. (strain Ex25). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=150340; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ex25; RA Heidelberg J., Sebastian Y.; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ex25; RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V., RA Bartels D.; RT "Sequence of the deep-sea isolate Vibrio sp. strain Ex25."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EX25; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V., RA Bartels D.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001806; ACY53555.1; -; Genomic_DNA. DR EMBL; DS267808; EDN59008.1; -; Genomic_DNA. DR RefSeq; YP_003288020.1; NC_013457.1. DR STRING; 150340.VEA_000869; -. DR EnsemblBacteria; ACY53555; ACY53555; VEA_000869. DR EnsemblBacteria; EDN59008; EDN59008; VEx25_A1573. DR GeneID; 8559182; -. DR KEGG; vex:VEA_000869; -. DR PATRIC; 28397671; VBIVibSp2903_0290. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; VSP150340:GJJG-3944-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21810 MW; 0D952EB417F08E0C CRC64; MNAYRLYLVT DDQQDLPTLK HVVRKAVEGG VTMVQVREKH GDVRAFIERA QAVKTILEGT GVPLIINDRV DVALAVDADG VHLGQSDMPA EIARQLIGPN KILGLSIETE DQLAEADSLP IDYIGLSAIF ATPTKTNTKK HWGIEGLKMA LNTTSLPIVA IGGINETNIP ALSATGVHGL ALVSAICHAE NPTKAAEYLL SLMD // ID A7K5H6_VIBSE Unreviewed; 471 AA. AC A7K5H6; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE SubName: Full=Thiamine monophosphate synthase/teni subfamily, putative; GN OrderedLocusNames=VEA_002073; ORFNames=VEx25_2185; OS Vibrio sp. (strain Ex25). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=150340; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ex25; RA Heidelberg J., Sebastian Y.; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ex25; RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V., RA Bartels D.; RT "Sequence of the deep-sea isolate Vibrio sp. strain Ex25."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EX25; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V., RA Bartels D.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001805; ACY50236.1; -; Genomic_DNA. DR EMBL; DS267847; EDN56137.1; -; Genomic_DNA. DR RefSeq; YP_003284701.1; NC_013456.1. DR STRING; 150340.VEA_002073; -. DR EnsemblBacteria; ACY50236; ACY50236; VEA_002073. DR EnsemblBacteria; EDN56137; EDN56137; VEx25_2185. DR GeneID; 8555722; -. DR KEGG; vex:VEA_002073; -. DR PATRIC; 28404838; VBIVibSp2903_3786. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; WSAQGES; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; VSP150340:GJJG-485-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 471 AA; 52608 MW; 12A9C48494B3D277 CRC64; MSKILIPSSL IELTGLVQQC LLLAKEQGFS IEDIELGVSP TQSIQLVRDQ QTTHITTDLI DGHNSEHESS FVLYYRSSLS VEACAKQPSK AIYIGIADTQ VSDENEKVLQ LDIWRHPLND EVRALSVKSK PNAMFDPEHH LAWIVTLTAL DFPIEDALTL ARGILTQQAN VSRETLLNDK LDEGRSTKWA DQFDDFPTPV LEDNRLGIQV GWSAQGESVN FPTLTKQSLG LYPVVDDVAW IERLLPLGIN TIQLRIKNPQ QADLEQQIIR AIELGRKYQA QVFINDYWQL AIKHGAYGVH LGQEDIEESH LAQLTKAGIR LGLSTHGYYE LLRIVQIHPS YIALGHIFPT TTKQMPSKPQ GLVRLALYQK LIDSIPYGNT ESVFLPAKYK TVSDYVLGFP TVAIGGIDQS NADQVWQTGV SSLAVVRAIT LAESPQSVIE FFAQLMKERQ LTFTDQNSEL AHSKRGEHAH G // ID A7LX00_BACO1 Unreviewed; 202 AA. AC A7LX00; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 19-MAR-2014, entry version 31. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BACOVA_02355; OS Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / NCTC OS 11153). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=411476; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8483; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8483; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides ovatus (ATCC 8483)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXF02000048; EDO11861.1; -; Genomic_DNA. DR ProteinModelPortal; A7LX00; -. DR SMR; A7LX00; 1-202. DR EnsemblBacteria; EDO11861; EDO11861; BACOVA_02355. DR PATRIC; 27037912; VBIBacOva42630_0110. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23599 MW; 772F8DFC6BF5D5DD CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNKFD ACQDQNYLAV IEHFKKLKKL SD // ID A7LX05_BACO1 Unreviewed; 205 AA. AC A7LX05; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 19-MAR-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACOVA_02360; OS Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / NCTC OS 11153). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=411476; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8483; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8483; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides ovatus (ATCC 8483)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXF02000048; EDO11866.1; -; Genomic_DNA. DR ProteinModelPortal; A7LX05; -. DR EnsemblBacteria; EDO11866; EDO11866; BACOVA_02360. DR PATRIC; 27037922; VBIBacOva42630_0115. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22527 MW; 5BB6D8FCC017710C CRC64; MVSLQFITHQ TERYSYLESA RMALEGGCKW IQLRMKEAPL EEVEAVALQL KPLCKEHEAI LVLDDHVELA RKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LKGYSSILSQ MKEANIEIPV VAIGGITYED IPAILHTGVN GIALSGTILG ADNPVEETHR ILNHA // ID A7N140_VIBCB Unreviewed; 471 AA. AC A7N140; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 14-MAY-2014, entry version 56. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE SubName: Full=Uncharacterized protein; GN Name=thiE; OrderedLocusNames=VIBHAR_00365; ORFNames=M892_10905; OS Vibrio campbellii (strain ATCC BAA-1116 / BB120). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=338187; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1116, and ATCC BAA-1116 / BB120; RG The Vibrio harveyi Genome Sequencing Project; RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C., RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., RA Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., RA Irgon J., Wilson R.K.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1116; RX PubMed=24376440; DOI=10.3389/fmicb.2013.00379; RA Wang Z., Lin B., Mostaghim A., Rubin R.A., Glaser E.R., RA Mittraparp-Arthorn P., Thompson J.R., Vuddhakul V., Vora G.J.; RT "Vibrio campbellii hmgA-mediated pyomelanization impairs quorum RT sensing, virulence, and cellular fitness."; RL Front. Microbiol. 4:379-379(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000789; ABU69386.1; -; Genomic_DNA. DR EMBL; CP006605; AGU94994.1; -; Genomic_DNA. DR RefSeq; YP_001443613.1; NC_009783.1. DR RefSeq; YP_008526916.1; NC_022269.1. DR STRING; 338187.VIBHAR_00365; -. DR EnsemblBacteria; ABU69386; ABU69386; VIBHAR_00365. DR GeneID; 16816346; -. DR GeneID; 5553899; -. DR KEGG; vca:M892_10905; -. DR KEGG; vha:VIBHAR_00365; -. DR PATRIC; 20127611; VBIVibHar24526_0395. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; VHAR338187:GJCH-358-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 471 AA; 52753 MW; 990E6E52E7FAC9A6 CRC64; MSKILIPSSL IELTGLVQQC LLLAKEQGFS IEDVELGVSP TQSIQLVRNQ QTTRITTDLI DGYDSEHESS LVLYYRSALS VEACAKQPSK AIYIGIADTQ VSDEKEKELQ LDIWRHPINN EVRALSVKSK FNAMFDPEHH LAWTVTLTVL DFPIEDTLTL ARGMLTQQAN VSRETLLNDS LDEGRSTQWA DQFDDFPTPV LEDNRLDIQV GWSAQGESVS FPTLTKQSLG LYPVVDDVAW IERLLPLGIN TIQLRIKNLQ QADLEQQIIR AIELGRQYQA QVFINDYWQL AIKHCAYGVH LGQEDIEESN LAQLTKAGIR LGLSTHGYYE LLRIVQIHPS YIALGHIFPT TTKQMPSKPQ GLVRLELYQK LIDSIPYTNT EAAFRPAKGK AGSDYVLGFP TVAIGGIDQS NADQVWQTGV SSLAVVRAIT LAESPQSVIE FFAQLMNERQ LTFTDQNCEL AHNKRGEHAY G // ID A7TE74_VANPO Unreviewed; 540 AA. AC A7TE74; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 16-APR-2014, entry version 38. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=Kpol_1002p43; OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) OS (Kluyveromyces polysporus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; OC Vanderwaltozyma. OX NCBI_TaxID=436907; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 22028 / DSM 70294; RX PubMed=17494770; DOI=10.1073/pnas.0608218104; RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., RA Wolfe K.H.; RT "Independent sorting-out of thousands of duplicated gene pairs in two RT yeast species descended from a whole-genome duplication."; RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS480379; EDO19396.1; -; Genomic_DNA. DR RefSeq; XP_001647254.1; XM_001647204.1. DR ProteinModelPortal; A7TE74; -. DR STRING; 436907.A7TE74; -. DR GeneID; 5547746; -. DR KEGG; vpo:Kpol_1002p43; -. DR eggNOG; COG0352; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 58324 MW; 07204ADF67350468 CRC64; MVFTKDQVDY SLYLVTDSTM LPPGATLSSQ VEEGLMNGVT LVQIREKDCD TKNFFHEGVL IKKLCTDYNV PLIVNDRVDV ALAIRADGVH VGQDDMPIPV VRELLGPDKI IGWSVSKVEE VEKLANWGPG MVDNIGIGMV FPTQTKKNPK KSPMGTAGVI KVLDALENCG ASWVKTVAIG GLHPDNIQRV LYQCSSTNGR RYLDGIAVVS DIMASEDAGL STRILRDLLD SNSYKFVDFG LSNEALQVSN INAALHQVHF ARPLVQHMTN KVHQNFGANV TLAVFGSPIM SEVVSEVKDL SNIPYASLLI NTGTIAPLDV LKAAVTAYNE SKRPVVLDPV GYSATPTRMS LNNDLLSYGQ FSCIKCNASE MLSLAELSDE RMKGVDSSGS NINNDTVIKA TKIVAYRYKT IAVCTGEYDF IANGTMGGHY SLGTQEIRGD SPSIPCFVVH GGNIPIMGDI TASGCSLGST ITSFLGSLSF PNEAQNAVIA AVTLYKAAGK LAASRCKGSG SFQVEFIDAL YQLSRENIPE KWDVKYELIL // ID A7UVT5_NEUCR Unreviewed; 523 AA. AC A7UVT5; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 16-APR-2014, entry version 40. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=NCU11173; OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM OS 1257 / FGSC 987). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; OC Neurospora. OX NCBI_TaxID=367110; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; RX PubMed=12712197; DOI=10.1038/nature01554; RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., RA Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., RA Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., RA Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., RA Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., RA Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., RA Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., RA Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., RA Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.; RT "The genome sequence of the filamentous fungus Neurospora crassa."; RL Nature 422:859-868(2003). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM002238; EDO65405.1; -; Genomic_DNA. DR RefSeq; XP_001728496.1; XM_001728444.1. DR UniGene; Ncr.17837; -. DR ProteinModelPortal; A7UVT5; -. DR EnsemblFungi; EFNCRT00000000294; EFNCRP00000000294; EFNCRG00000000294. DR GeneID; 5847880; -. DR KEGG; ncr:NCU11173; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 523 AA; 55945 MW; 2C606C4E2993D576 CRC64; MDRNNVNYAV YLVTDSTPAI LGDRDLCEVV EASVRGGTTI VQLREKTSDT GDMIAMGKKL HAITKKYNVP LLINDRVDVA LAVGCEGVHI GQDDMELSTA RRLLGPDAII GVTVSTIQEA MVACKGGADY LGIGTVYATP TKTNTKNIIG AAGVRDILQA MADAGYDHVK TVCIGGINAE NLQRIVYQSE APSKKLDGVA VVSALVAAPD PEAAAKNLLG LFNSQPPFVR AATSPRAETA DSILELVPEV VLEVARKKPL SHNMTNLVVQ NFAANVALAI GASPIMANNG EEAFDLCKLG GALVVNMGTV DPDGLQNYLK ALRAYNSVGQ PVVYDPVGAG ATTLRRSAVK TILSHGYLDI IKGNEGEIRT VYGIYERETF QQRGVDSSAE LEVSQKAELV RKLALREKNV VVMTGESDYL SDGQHTFRID NGHAYLEMVT GTGCVLGTTI SAFVAAYPND KLVATVVALL HFEIAAERAA ERRDVQGPGT FVPAFLDELF KIRRETGQGR MGWLKSAKLT RLS // ID A7UZH1_BACUN Unreviewed; 219 AA. AC A7UZH1; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACUNI_00699; OS Bacteroides uniformis ATCC 8492. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=411479; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8492; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8492; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides uniformis (ATCC 8492)."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYH02000036; EDO55666.1; -; Genomic_DNA. DR ProteinModelPortal; A7UZH1; -. DR EnsemblBacteria; EDO55666; EDO55666; BACUNI_00699. DR PATRIC; 27175082; VBIBacUni30129_0954. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24301 MW; AA8D0E954A20AFF5 CRC64; MRKMKDERLK NGGMQFITHY TERYSYLDAA RMALEGGCRW VQLRMKDTPV ETIEPVALEV QALCRQYGAT FIIDDHVELA RKLHADGVHL GKKDMPIADA RRILGAEYII GGTANTFEDV LQHYKAGADY IGCGPFRYTT TKKNLSPILG LEGYTAIIHR MQEKDIHLPI VAIGGITIAD IPAVMQTGVS GIALSGTVLH ADSPADEMKR IISLMENEK // ID A7UZH6_BACUN Unreviewed; 200 AA. AC A7UZH6; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 16-OCT-2013, entry version 30. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BACUNI_00704; OS Bacteroides uniformis ATCC 8492. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=411479; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8492; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8492; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides uniformis (ATCC 8492)."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYH02000036; EDO55671.1; -; Genomic_DNA. DR ProteinModelPortal; A7UZH6; -. DR SMR; A7UZH6; 1-195. DR EnsemblBacteria; EDO55671; EDO55671; BACUNI_00704. DR PATRIC; 27175094; VBIBacUni30129_0960. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 200 AA; 22200 MW; 0304A33FD3A3D020 CRC64; MKLIVITTPQ FFEGEAAAVT SLFQNGLEIL HLRKPGASAE EMEYFLRQLP MEYMPRIVTH EQFQLASVFG LKGIHLNGRN PQIPFGYKGH ISCSCHSLEE VLKHKSDCSY VFLSPIYDSI SKEGYSSAYS CDTLKKAQQA GIIDSNVMAL GGISLEHLPE IAALGFGGAV LLGDVWQQAK EAFIPHFLHL KQLSSHPFNF // ID A7V428_BACUN Unreviewed; 202 AA. AC A7V428; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 16-OCT-2013, entry version 30. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BACUNI_02327; OS Bacteroides uniformis ATCC 8492. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=411479; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8492; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8492; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides uniformis (ATCC 8492)."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYH02000043; EDO54319.1; -; Genomic_DNA. DR ProteinModelPortal; A7V428; -. DR SMR; A7V428; 1-202. DR EnsemblBacteria; EDO54319; EDO54319; BACUNI_02327. DR PATRIC; 27178020; VBIBacUni30129_2399. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23263 MW; 7B68250C0095840D CRC64; MKLIVVTAPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHKRIITH EHFYLQEEFS LMGIHLNTRN SKEPHDYSGH ISCTCHSLDE VQNKKHFYDY LFLSPIYNCI TKSGVTSGFT AEELRQAGKS KVIDSRVMAL GGITPDNILE IKDYGFGGAV VMGDLWNKFN ACTDRDYLEV IRHFKKLKKM AD // ID A7VBK3_9CLOT Unreviewed; 217 AA. AC A7VBK3; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLOL250_00265; OS Clostridium sp. L2-50. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411489; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-50; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium sp. L2-50."; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-50; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Hodges J., RA Shah N., Mardis E.R., Wilson R.K.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYW02000002; EDO59206.1; -; Genomic_DNA. DR ProteinModelPortal; A7VBK3; -. DR EnsemblBacteria; EDO59206; EDO59206; CLOL250_00265. DR PATRIC; 27241684; VBICloSp41567_0859. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23561 MW; EC92CBCC746F3592 CRC64; MSKQTHIKPE ELLLYAVTDR HWLNGATLIS QVEAALKGGA TFIQLREKNL DDKAFYQEAL EIQKLCKEYK VPFVINDNVE LAKKIGADGV HVGQSDMEAL DVRKVLGDDK IIGVSAQTVE QAELAEKHGA DYLGVGAVFP TGSKNDATEV SFEMLQEICE HVHIPVIAIG GITRDNVVEL SQSGICGIAV ISAIFGQTDI EAATADLKKQ TKKMLGE // ID A7VJ81_9CLOT Unreviewed; 193 AA. AC A7VJ81; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 16-OCT-2013, entry version 29. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=CLOL250_02990; OS Clostridium sp. L2-50. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411489; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-50; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium sp. L2-50."; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-50; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Hodges J., RA Shah N., Mardis E.R., Wilson R.K.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYW02000023; EDO56366.1; -; Genomic_DNA. DR ProteinModelPortal; A7VJ81; -. DR EnsemblBacteria; EDO56366; EDO56366; CLOL250_02990. DR PATRIC; 27239955; VBICloSp41567_0032. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 193 AA; 21393 MW; 0BFEAD9ACD6E5620 CRC64; MCKCYEHAIV ITNRALVNGD FLEQLQKVAQ VHPHALILRE KDLPDAEYEK LAAKVLEIYK TAGIPVFLHS RMEIAERLGC ENIHLSIPVL QDLSDVWRDA LTTNFKEISV SCHSMEDVEL AVKSGATQIV LGTIFETECK KGLKGRGLEF VREICANCPV PVYAIGGINE ERLLQVMEAG AAGGCMMSGF MRM // ID A7Z3F5_BACA2 Unreviewed; 205 AA. AC A7Z3F5; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE SubName: Full=TenI; GN Name=tenI; OrderedLocusNames=RBAM_011670; OS Bacillus amyloliquefaciens subsp. plantarum (strain DSM 23117 / BGSC OS 10A6 / FZB42). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=326423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23117 / BGSC 10A6 / FZB42; RX PubMed=17704766; DOI=10.1038/nbt1325; RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., RA Voigt B., Jungblut P.R., Vater J., Sussmuth R., Liesegang H., RA Strittmatter A., Gottschalk G., Borriss R.; RT "Comparative analysis of the complete genome sequence of the plant RT growth-promoting bacterium Bacillus amyloliquefaciens FZB42."; RL Nat. Biotechnol. 25:1007-1014(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000560; ABS73531.1; -; Genomic_DNA. DR RefSeq; YP_001420762.1; NC_009725.1. DR ProteinModelPortal; A7Z3F5; -. DR SMR; A7Z3F5; 1-198. DR STRING; 326423.RBAM_011670; -. DR EnsemblBacteria; ABS73531; ABS73531; RBAM_011670. DR GeneID; 5462515; -. DR KEGG; bay:RBAM_011670; -. DR PATRIC; 18747334; VBIBacAmy31356_1145. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BAMY326423:GCM4-1165-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 22834 MW; 8923402492F2370C CRC64; MELHAVTDNR KPVAELAEDI LSIQREVSFI HIRERDKTAG EIMQLLSLLK KGGADKDKLI INDRADIALF ANIHRVQLPS RSFSVKQVRS RFPHLHIGRS VHSLKEAIQA EKEDADYVVF GHVFETECKQ GLEARGISLL SEIKRTLSIP VIAIGGMTLQ TIGHTKQAKP DGIAVMSGIF SAENPEEAAK RYARAVREAD YEEAL // ID A7ZDK7_CAMC1 Unreviewed; 204 AA. AC A7ZDK7; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 14-MAY-2014, entry version 43. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase (TMPpyrophosphorylase) (TMP-PPase) (Thiamine-phosphate synthase); GN ORFNames=CCC13826_1279; OS Campylobacter concisus (strain 13826). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360104; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13826; RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., RA Mandrell R.E., On S., Nelson K.E.; RT "Genome sequence of Campylobacter concisus 13826 isolated from human RT feces."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000792; EAT98684.1; -; Genomic_DNA. DR RefSeq; YP_001466865.1; NC_009802.1. DR ProteinModelPortal; A7ZDK7; -. DR STRING; 360104.CCC13826_1279; -. DR EnsemblBacteria; EAT98684; EAT98684; CCC13826_1279. DR GeneID; 5596184; -. DR KEGG; cco:CCC13826_1279; -. DR PATRIC; 20028209; VBICamCon95352_1043. DR eggNOG; COG0352; -. DR HOGENOM; HOG000002417; -. DR KO; K00788; -. DR OMA; ASHIFAT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CCON360104:GHAC-1061-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 204 AA; 22965 MW; 66D4FFD4861CE492 CRC64; MFKILCVADF ESYEGDDFLK RIQLLCKAGV DEILLRAKGL DEANFYDLAR VVAQICENYR KKFIINQFFD VACKLKSDFW LTSAQLDFFK NHAVFLDYFR KTAKIYAPAH DLEQAKISAS IADVLVASHI FATSCKVGLE PKGLKFISEL KSFDKEIYAL GGLDSGNYKE AIKAGANGIC FMSLAMNGDI ELIKKIIESK NEQI // ID A7ZEN7_CAMC1 Unreviewed; 204 AA. AC A7ZEN7; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CCC13826_0400; OS Campylobacter concisus (strain 13826). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360104; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13826; RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., RA Mandrell R.E., On S., Nelson K.E.; RT "Genome sequence of Campylobacter concisus 13826 isolated from human RT feces."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000792; EAT99253.1; -; Genomic_DNA. DR RefSeq; YP_001467245.1; NC_009802.1. DR ProteinModelPortal; A7ZEN7; -. DR STRING; 360104.CCC13826_0400; -. DR EnsemblBacteria; EAT99253; EAT99253; CCC13826_0400. DR GeneID; 5596267; -. DR KEGG; cco:CCC13826_0400; -. DR PATRIC; 20029043; VBICamCon95352_1449. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CCON360104:GHAC-1478-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22315 MW; 5CE79085B8A3143C CRC64; MAEIYAISDD ILMPENLALE YAREILECGV KFFQFRSKKA VKNEKLASEI LNLCEKFGAK FIVNDDVKFA KKIGAKAVHL GKDDENIKEA FEILGKDAYV GVSCYNDINL AINAAKNGAS YVAFGSVFTS LTKPNAPKCG LEVVKEAKQI LNLPICVIGG INETNIGSLS HAKPDLIAII SAIYKDGNIK ENIKNLQKII KANF // ID A8EM94_BURPE Unreviewed; 367 AA. AC A8EM94; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 19-FEB-2014, entry version 37. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=BURPS406E_I0551; OS Burkholderia pseudomallei 406e. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=360118; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=406e; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia pseudomallei 406e."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899737; EDO87662.1; -; Genomic_DNA. DR ProteinModelPortal; A8EM94; -. DR EnsemblBacteria; EDO87662; EDO87662; BURPS406E_I0551. DR PATRIC; 27875732; VBIBurPse88967_5462. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Transferase. SQ SEQUENCE 367 AA; 38308 MW; E8F50A360B15395D CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAQIARL NAAGAQAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDTLRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID A8ENR7_BURPE Unreviewed; 209 AA. AC A8ENR7; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 16-OCT-2013, entry version 29. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BURPS406E_D0555; OS Burkholderia pseudomallei 406e. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=360118; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=406e; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia pseudomallei 406e."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899738; EDO88111.1; -; Genomic_DNA. DR ProteinModelPortal; A8ENR7; -. DR EnsemblBacteria; EDO88111; EDO88111; BURPS406E_D0555. DR PATRIC; 27876833; VBIBurPse88967_6348. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID A8EQ96_BURPE Unreviewed; 199 AA. AC A8EQ96; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 16-OCT-2013, entry version 29. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=BURPS406E_C1535; OS Burkholderia pseudomallei 406e. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=360118; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=406e; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia pseudomallei 406e."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899739; EDO88796.1; -; Genomic_DNA. DR ProteinModelPortal; A8EQ96; -. DR EnsemblBacteria; EDO88796; EDO88796; BURPS406E_C1535. DR PATRIC; 27878041; VBIBurPse88967_6718. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 21280 MW; 15C55A6C40187FA9 CRC64; MNKSANLPSE YLITPEPPGD EALSDYLATL ERTLKAGISL VQLRAKAVTA PYYARLTEYA LACCRRYNAQ LLVNAAPEVA LGLHTDGVHL TSTRLMTCST RPLPAGLLVS AACHDEDQVR HADSIGVDLI TISPVMPTAT HTTAEPLGWP RFRELATLTS VPVYALGGMS VDSLAEARNA GAYGIAAIRA FWGSNVDRS // ID A8ERZ8_ARCB4 Unreviewed; 203 AA. AC A8ERZ8; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=Abu_0447; OS Arcobacter butzleri (strain RM4018). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=367737; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM4018; RX PubMed=18159241; DOI=10.1371/journal.pone.0001358; RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Wosten M.M., RA Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., RA Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.; RT "The complete genome sequence and analysis of the RT Epsilonproteobacterium Arcobacter butzleri."; RL PLoS ONE 2:E1358-E1358(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000361; ABV66722.1; -; Genomic_DNA. DR RefSeq; YP_001489391.1; NC_009850.1. DR ProteinModelPortal; A8ERZ8; -. DR STRING; 367737.Abu_0447; -. DR EnsemblBacteria; ABV66722; ABV66722; Abu_0447. DR GeneID; 5624516; -. DR KEGG; abu:Abu_0447; -. DR PATRIC; 20962254; VBIArcBut20197_0440. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NADIAFI; -. DR OrthoDB; EOG6WX4T9; -. DR BioCyc; ABUT367737:GHWO-446-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 203 AA; 23132 MW; ED219AB360E6AAB8 CRC64; MISNLEKALG FKLEAFNYLY VLCDYETLLK KNISLETFVD LCRKKDVKII QYRDKISSFE EQKINLLYLK SQLNIPIIVN DKIELIDFAD GLHLGQEDLE KIHKDKKLAI KLVRTKIKDK LLGLSTHNEI EILEANELNL DMIGLGAYKQ TNTKDVSTIL GEKISYLAKI SKHPVCAIGG VKIEDKILNV KFNVVGSGFF DEN // ID A8EWC5_ARCB4 Unreviewed; 184 AA. AC A8EWC5; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Abu_2031; OS Arcobacter butzleri (strain RM4018). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=367737; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM4018; RX PubMed=18159241; DOI=10.1371/journal.pone.0001358; RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Wosten M.M., RA Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., RA Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.; RT "The complete genome sequence and analysis of the RT Epsilonproteobacterium Arcobacter butzleri."; RL PLoS ONE 2:E1358-E1358(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000361; ABV68248.1; -; Genomic_DNA. DR RefSeq; YP_001490918.1; NC_009850.1. DR ProteinModelPortal; A8EWC5; -. DR STRING; 367737.Abu_2031; -. DR EnsemblBacteria; ABV68248; ABV68248; Abu_2031. DR GeneID; 5625104; -. DR KEGG; abu:Abu_2031; -. DR PATRIC; 20965428; VBIArcBut20197_1978. DR eggNOG; NOG119803; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FATPNKG; -. DR OrthoDB; EOG6FJNJD; -. DR BioCyc; ABUT367737:GHWO-2029-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 184 AA; 21304 MW; 2C768CAE246B8432 CRC64; MKKYLITDPN YYTNNELIFK QTLSNAFEKH KVDFACFRDK QSNNFEALAK TFIETCHERN IKNTFLNSDF LLAQRLGFYG VHLTSTQFED IKRAKELNLK IIISCHNIED VETAKKYEAN YITYSPIFDT PNKGKAKGIK DLELILNSFK DTKIIALGGI IDETQVSKIE KTKAYGFASI RYFI // ID A8FC12_BACP2 Unreviewed; 210 AA. AC A8FC12; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE SubName: Full=Possible thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=tenI; OrderedLocusNames=BPUM_1095; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=315750; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., RA Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C., RA Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., RA Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., RA Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., RA Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., RA Venkateswaran K., Highlander S.K., Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000813; ABV61779.1; -; Genomic_DNA. DR RefSeq; YP_001486339.1; NC_009848.1. DR ProteinModelPortal; A8FC12; -. DR STRING; 315750.BPUM_1095; -. DR EnsemblBacteria; ABV61779; ABV61779; BPUM_1095. DR GeneID; 5620361; -. DR KEGG; bpu:BPUM_1095; -. DR PATRIC; 18966023; VBIBacPum16546_1109. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPUM315750:GH6N-1149-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 210 AA; 23202 MW; 6DB5FA7C7D6389C1 CRC64; MGLVQMELHA VTNDSLPAEE LIKQIIAIAS EVDFIHIRER SKTASELVDL VKSLLLEGVP KEKLIINDRV DVALLTNIHR VHLPGHSFSP KELREKFPHL HAGVSVHSIE EGKAAEKNGA EYVIFGHVYD TTCKPGLQAR GVQLVKELTS LLSIPVVAIG GVTPERVPEL RHVNVKGIAV MSGIFTHHQP RKMAQAFSKQ VKENPYEEAL // ID A8FM92_CAMJ8 Unreviewed; 201 AA. AC A8FM92; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE SubName: Full=Possible transferase; GN OrderedLocusNames=C8J_0980; OS Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC OS 11828). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=407148; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=81116 / NCTC 11828; RX PubMed=17873037; DOI=10.1128/JB.01404-07; RA Pearson B.M., Gaskin D.J., Segers R.P., Wells J.M., Nuijten P.J., RA van Vliet A.H.; RT "The complete genome sequence of Campylobacter jejuni strain 81116 RT (NCTC11828)."; RL J. Bacteriol. 189:8402-8403(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000814; ABV52579.1; -; Genomic_DNA. DR RefSeq; YP_001482556.1; NC_009839.1. DR ProteinModelPortal; A8FM92; -. DR STRING; 407148.C8J_0980; -. DR EnsemblBacteria; ABV52579; ABV52579; C8J_0980. DR GeneID; 5617489; -. DR KEGG; cju:C8J_0980; -. DR PATRIC; 20055592; VBICamJej119085_0990. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CJEJ407148:GHCS-1015-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 201 AA; 23486 MW; 61622900362A43FB CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICVKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG IDFLKSLLEF SQIPLYAIGG INTQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID A8FUV0_SHESH Unreviewed; 557 AA. AC A8FUV0; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Phosphomethylpyrimidine kinase, Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=Ssed_2014; OS Shewanella sediminis (strain HAW-EB3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=425104; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAW-EB3; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella sediminis HAW-EB3."; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000821; ABV36623.1; -; Genomic_DNA. DR RefSeq; YP_001473751.1; NC_009831.1. DR ProteinModelPortal; A8FUV0; -. DR STRING; 425104.Ssed_2014; -. DR EnsemblBacteria; ABV36623; ABV36623; Ssed_2014. DR GeneID; 5614093; -. DR KEGG; sse:Ssed_2014; -. DR PATRIC; 23561536; VBISheSed62411_2142. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SSED425104:GH7Q-2078-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 557 AA; 59077 MW; 69577BB7545885E4 CRC64; MTNLELTSSA LKPVVWTIAG SDSGGGAGIQ ADLATIQDLG CHACSAITCL TAQNSVSVTL VEPVSEAMLL AQLDVLLTDL PPMAIKIGLL ASQAQLNLLG KWLNTSLREF TQTNAMDVSV ILDPVMVASC GAHFTAQSRA ESNTKKLDND SGPGLDSDSA NGSGGSVRDG TISHLNFLPL KGLITLITPN TAELSVLSGR RLTDLSDCHR AAKALSKTFE CNVLAKGGDK GAAWEAKTAQ DIFVCVQAPG SAVIHQQRSF LLSSPRVDST NNHGSGCTLS SAIASVMAWG FVLQDAVVVA KAYVTEGIKQ SYRVGKGPGP LARTGWSDEL SGFAHITSLD GGAALPDELT FKVLDDRLGV YPVVTELSML QALLGAGAKT IQLRIKDADD PELEAKIITA IQLGRDYRAK VFINDYWQLA VKHQAFGVHL GQEDLYDADL TQIAQSGLAL GVSSHSYFEL LLASQFKPSY IALGHIFPTT TKVMPSLPQG LHKLKHYVDL LKGHFPLVAI GGIDLNRLPA VKKTNVDDIA VVRAVTEADE PAVAYQTLVA AWSIEDE // ID A8G681_PROM2 Unreviewed; 351 AA. AC A8G681; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=P9215_14991; OS Prochlorococcus marinus (strain MIT 9215). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=93060; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9215; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., RA Steglich C., Church G.M., Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000825; ABV51112.1; -; Genomic_DNA. DR RefSeq; YP_001484698.1; NC_009840.1. DR ProteinModelPortal; A8G681; -. DR STRING; 93060.P9215_14991; -. DR EnsemblBacteria; ABV51112; ABV51112; P9215_14991. DR GeneID; 5614640; -. DR KEGG; pmh:P9215_14991; -. DR PATRIC; 22992572; VBIProMar119824_1550. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR93060:GI08-1545-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 128 Unknown (By similarity). FT REGION 129 351 Thiamine-phosphate synthase (By FT similarity). FT REGION 180 184 HMP-PP binding (By similarity). FT REGION 277 279 THZ-P binding (By similarity). FT METAL 213 213 Magnesium (By similarity). FT METAL 232 232 Magnesium (By similarity). FT BINDING 212 212 HMP-PP (By similarity). FT BINDING 251 251 HMP-PP (By similarity). FT BINDING 280 280 HMP-PP (By similarity). FT BINDING 307 307 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 351 AA; 40284 MW; 0E9CC170528B2AAB CRC64; MLNSNPKDAE DLRIYQIIDA NLDRAREGLR VLEDWARFGL GKEKYVEKIK NFRQILGKNH LEVYKQSRNQ IEDKCKGLSH QEQFNRKTSE QIISSNSARV QEALRVIEEF SRLQNHELSK IASEIRYEIY TIEIDLLSYS KFKKSEEILK ENDLYVITDQ KDNLLEIIEE ILIAGVKIIQ HRFKTGTDQD NLQEAIQIKN LCKRYNSLFI VNDRIDIALA SNADGIHLGQ DDLDLKTARR LLGYSKIVGI SANNTIDISN ALKEGCDYLG IGPVFETTTK KNKIPLGIEN IKLLTKDLNI PWFAIGGIKS NNISYLKRNG FKKVALVSEL MNSEDPKEDA MMILKKLSHE N // ID A8H565_SHEPA Unreviewed; 530 AA. AC A8H565; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 14-MAY-2014, entry version 56. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Spea_2382; OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=398579; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700345 / ANG-SQ1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Zhao J.-S.Z., Manno D., Hawari J., Richardson P.; RT "Complete sequence of Shewanella pealeana ATCC 700345."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000851; ABV87702.1; -; Genomic_DNA. DR RefSeq; YP_001502237.1; NC_009901.1. DR ProteinModelPortal; A8H565; -. DR STRING; 398579.Spea_2382; -. DR EnsemblBacteria; ABV87702; ABV87702; Spea_2382. DR GeneID; 5662775; -. DR KEGG; spl:Spea_2382; -. DR PATRIC; 23534748; VBIShePea72822_2493. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SPEA398579:GHG5-2505-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 530 AA; 56600 MW; 2686F4E83C07C0E5 CRC64; MANAHTLPVR LPVVWTIAGS DSGGGAGIQA DLATMSDLDA HACSVITAVT AQSSVTVALV ESVSSQMLKS QLDTLVSDLP PAAIKIGLLA EQAQIDYLAK WLAKQQASWR QSGIVVPIIL DPVMVATCGD ALANGGRLDF TPFKGLLTLI TPNVSELAIL AATELESVDA CISAAKQLSE QLSTSVLAKG GDLGPAWCQH QANDLLVCTD VEGISDKHQW QSFWLSSHRV NSQNSHGTGC TLSSAIASVM AHGFVLNDAI VVAKAYVNAG LIASYQPGSG PGCLARTAWP KDLQQFPYIK VITASDTEPM SLAAWELMNN QRGDFKQIDG TLGLYPVVAD VELLQILLKA GAKTIQLRVK DASSPTLEAQ IIKAIALGRD YQSRVFINDH WQLAIKHQAY GVHLGQEDLL DSNLKQLREA DIALGLSSHS YFEILLAKQH QPSYIAFGHI FPTTTKQMPS LPQGLEKLSR YVSLMKGELP IVAIGGIDAA RLRSVKATGV DDIAVVRALT EADDPTAAFT ALNRAWADEK // ID A8HNR8_CHLRE Unreviewed; 759 AA. AC A8HNR8; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Predicted protein; GN ORFNames=CHLREDRAFT_190184; OS Chlamydomonas reinhardtii (Chlamydomonas smithii). OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; OC Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas. OX NCBI_TaxID=3055; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC-503; RX PubMed=17932292; DOI=10.1126/science.1143609; RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., RA Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R., RA Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P., RA Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J., RA Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T., RA Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D., RA Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W., RA Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D., RA Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M., RA Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M., RA Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J., Purton S., RA Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M., RA Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J., RA Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C., RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J., RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P., RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., RA Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., RA Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W., RA Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A., RA Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V., RA Rokhsar D.S., Grossman A.R.; RT "The Chlamydomonas genome reveals the evolution of key animal and RT plant functions."; RL Science 318:245-250(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS496108; EDP09549.1; -; Genomic_DNA. DR RefSeq; XP_001689811.1; XM_001689759.1. DR ProteinModelPortal; A8HNR8; -. DR STRING; 3055.JGI190184; -. DR PRIDE; A8HNR8; -. DR ProMEX; A8HNR8; -. DR EnsemblPlants; EDP09549; EDP09549; CHLREDRAFT_190184. DR GeneID; 5715815; -. DR KEGG; cre:CHLREDRAFT_190184; -. DR eggNOG; COG0699; -. DR GO; GO:0031969; C:chloroplast membrane; IEA:EnsemblPlants/Gramene. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR GO; GO:0010027; P:thylakoid membrane organization; IEA:EnsemblPlants/Gramene. DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants/Gramene. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. SQ SEQUENCE 759 AA; 80255 MW; 0E760B26DBE273D9 CRC64; MQTARVQLPA VVLQLEASKV LADGAALDTL SQALQGGCNM VVLWDSNANA AAMYDAALRV QEALRARAPL LLVDRTDIAL AIGAQGVLLT DQGVPTVVAK RMMPQALVGR VVGDEGAAAA AAADGASLVL VEGAGGAVPA ASMLTGAKTG QRSGNAIPVL MSNATAEDYA QAILTRLNRE SLLSEEKAKL TEVLAFLEEV LPGVNELGLL RDALKALDEP FLVAVVGEFN SGKSSVINAL LGRRYLAEGI LPTTNEISIL KYSDTAPATS NPSQVQLVQQ SDGLYVRYLP AKLLQDLNIV DTPGTNVILE RQQRLTEEYV PRADLVLFVM SADRPFSESE VRFLEYIRQW QKKVVFVVNK SDILESSDEV DAVKEFVAAN AQRILRLDRP SVIAVSSRSA LRAKLTASNL PITASFDSDL PSASPTAPLS NVDPEAMEAA LSNSRDWAVS NFSELERNVS NFLVGKGAGG GEGVRLKLQT PLFVADALLG AAGRQLETDL AAARAELEGV QLVGRQLGRF RAEMEKDAAA QRAALQPVLA EVLARAEKFV DSTVQLSNAP LLVSIAAGNK EYPFRAAFEK EVTELSGDRA ASGADASSST SASSPALRAV GDFNLRAIST LLDTELQQAM ATTAGTAVGA PVFGLFAMQI VGNTLEDLLL AALAGGVSYV SLLNLPLRRA DLKGKIGRVA GNFVSDVQAK MEQEVADEVK ATVAAVGELM APLEQTYGAE VARLEARKSD LVAFGEALQE LQRRTANLE // ID A8IEV7_AZOC5 Unreviewed; 203 AA. AC A8IEV7; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 14-MAY-2014, entry version 43. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=AZC_3541; OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / ORS 571). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Azorhizobium. OX NCBI_TaxID=438753; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43989 / DSM 5975 / ORS 571; RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., RA Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., RA Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., RA Oyaizu H.; RT "Complete genome sequence of the nitrogen-fixing bacterium RT Azorhizobium caulinodans ORS571."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009384; BAF89539.1; -; Genomic_DNA. DR RefSeq; YP_001526457.1; NC_009937.1. DR ProteinModelPortal; A8IEV7; -. DR STRING; 438753.AZC_3541; -. DR EnsemblBacteria; BAF89539; BAF89539; AZC_3541. DR GeneID; 5690353; -. DR KEGG; azc:AZC_3541; -. DR PATRIC; 21023913; VBIAzoCau17976_3702. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INERSDI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ACAU438753:GJF3-3580-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 203 AA; 20535 MW; 4B216CF31012DB5E CRC64; MLPHPPLLLI TDRHQARTDL SDVLEASFGA GLRWTSVREK DLAPAEQVDL VRRLLPVAHA HGACLTLHGT AALALEAGAD GVHLPSGADV NAARALLGPD ALIGLSVHSM AEVTAAPPSA SYLVAGPAFE TASKPGYGPA LGPEGLAQLA RATALPLLAL GGLDRHTLLL CQDSGLAGAA VMGGVMRAND PAAEVRALLA AIG // ID A8IM70_AZOC5 Unreviewed; 236 AA. AC A8IM70; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 13-NOV-2013, entry version 40. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=AZC_0500; OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / ORS 571). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Azorhizobium. OX NCBI_TaxID=438753; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43989 / DSM 5975 / ORS 571; RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., RA Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., RA Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., RA Oyaizu H.; RT "Complete genome sequence of the nitrogen-fixing bacterium RT Azorhizobium caulinodans ORS571."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009384; BAF86498.1; -; Genomic_DNA. DR RefSeq; YP_001523416.1; NC_009937.1. DR ProteinModelPortal; A8IM70; -. DR STRING; 438753.AZC_0500; -. DR EnsemblBacteria; BAF86498; BAF86498; AZC_0500. DR GeneID; 5688849; -. DR KEGG; azc:AZC_0500; -. DR PATRIC; 21017479; VBIAzoCau17976_0521. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6BW4TV; -. DR BioCyc; ACAU438753:GJF3-503-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 236 AA; 23611 MW; 4B86FD3DECFE7F62 CRC64; MPSGPASERA GCPSFACFLA EPVIMPTEPE IPRCRLMLVL PPTLSAAEAI ACMGAGDVAA VIVTTPAGDE TAAKAQLSEL CTATQAAGVA FLLADRVELA SDIGADGVHL GSYAALKRAL PAVKPGGIAG IGLEGRHEAM EAGEAGADYV LFGARDGSGP IEPVVELVSW WAEVFEVPCV GVATTVEDAR AIAVAGADFV ALAAVPAGPD GPALVADVER AVAAVDRTVA DATPKA // ID A8KCZ7_BURPE Unreviewed; 209 AA. AC A8KCZ7; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 16-OCT-2013, entry version 29. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BURPSPAST_AC0483; OS Burkholderia pseudomallei Pasteur 52237. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=331978; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pasteur 52237; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia pseudomallei Pasteur 52237."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899740; EDO89465.1; -; Genomic_DNA. DR ProteinModelPortal; A8KCZ7; -. DR EnsemblBacteria; EDO89465; EDO89465; BURPSPAST_AC0483. DR PATRIC; 30398403; VBIBurPse100884_0459. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID A8KST3_BURPE Unreviewed; 367 AA. AC A8KST3; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 19-FEB-2014, entry version 38. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=BURPSPAST_P0210; OS Burkholderia pseudomallei Pasteur 52237. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=331978; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pasteur 52237; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia pseudomallei Pasteur 52237."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899750; EDO93713.1; -; Genomic_DNA. DR ProteinModelPortal; A8KST3; -. DR EnsemblBacteria; EDO93713; EDO93713; BURPSPAST_P0210. DR PATRIC; 30407548; VBIBurPse100884_5024. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Transferase. SQ SEQUENCE 367 AA; 38308 MW; E8F50A360B15395D CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAQIARL NAAGAQAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDTLRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID A8KUP9_BURPE Unreviewed; 199 AA. AC A8KUP9; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 16-OCT-2013, entry version 29. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=BURPSPAST_V0006; OS Burkholderia pseudomallei Pasteur 52237. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=331978; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pasteur 52237; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia pseudomallei Pasteur 52237."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899753; EDO94379.1; -; Genomic_DNA. DR ProteinModelPortal; A8KUP9; -. DR EnsemblBacteria; EDO94379; EDO94379; BURPSPAST_V0006. DR PATRIC; 30408968; VBIBurPse100884_5722. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 21351 MW; F4C4456E8E187770 CRC64; MNKSANLPSE YLITPEPPGD EALSDYLATL ERTLKAGISL VQLRAKAVTA PYYARLTEYA LACCRRYNAR LLVNAAPEVA RGLHTDGVHL TSTRLMTCST RPLPAGLLVS AACHDEDQVR HADSIGVDLI TISPVMPTAT HTTAEPLGWP RFRELATLTS VPVYALGGMS VDSLAEARNA GAYGIAAIRA FWGSNVDRS // ID A8LFH7_FRASN Unreviewed; 229 AA. AC A8LFH7; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Franean1_1842; OS Frankia sp. (strain EAN1pec). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=298653; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EAN1pec; RX PubMed=17151343; DOI=10.1101/gr.5798407; RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., RA Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N., RA Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L., RA Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E., RA Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z., RA Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D., RA Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.; RT "Genome characteristics of facultatively symbiotic Frankia sp. strains RT reflect host range and host plant biogeography."; RL Genome Res. 17:7-15(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000820; ABW11280.1; -; Genomic_DNA. DR RefSeq; YP_001506186.1; NC_009921.1. DR ProteinModelPortal; A8LFH7; -. DR STRING; 298653.Franean1_1842; -. DR EnsemblBacteria; ABW11280; ABW11280; Franean1_1842. DR GeneID; 5670244; -. DR KEGG; fre:Franean1_1842; -. DR PATRIC; 21936572; VBIFraSp51419_1896. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CVGPVHA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; FSP298653:GHPI-1861-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 52 56 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 186 186 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 24118 MW; D5F2BF6C06F27373 CRC64; MPSPGAEPLR ARRLARLLDA RLYLCTARRG DEGSFLEDVL GLPGAPAVDL VQLREKGLEW REELAGLARM REAADRVGAL VSANDRADVA AFAGVDILHV GQDDIPPRLA RTIVGADALI GLSTHDPEQF LAALADPDVD YVCVGPVHAT PTKEGRPPVG MGLPRLAARH APPFEPGAKP WFVTGGVDAR TLDAILETGA RRVVVVRGIA EAADPGAAAT ALAERLRSA // ID A8LK57_DINSH Unreviewed; 207 AA. AC A8LK57; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 14-MAY-2014, entry version 41. DE SubName: Full=Putative thiamine monophosphate synthase; GN OrderedLocusNames=Dshi_1514; OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Dinoroseobacter. OX NCBI_TaxID=398580; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12; RX PubMed=19741735; DOI=10.1038/ismej.2009.94; RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I., RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., RA Han C., Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., RA Liebl W., Liesegang H., Meincke L., Pati A., Petersen J., RA Piekarski T., Pommerenke C., Pradella S., Pukall R., Rabus R., RA Stackebrandt E., Thole S., Thompson L., Tielen P., Tomasch J., RA von Jan M., Wanphrut N., Wichels A., Zech H., Simon M.; RT "The complete genome sequence of the algal symbiont Dinoroseobacter RT shibae: a hitchhiker's guide to life in the sea."; RL ISME J. 4:61-77(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000830; ABV93256.1; -; Genomic_DNA. DR RefSeq; YP_001532857.1; NC_009952.1. DR ProteinModelPortal; A8LK57; -. DR STRING; 398580.Dshi_1514; -. DR EnsemblBacteria; ABV93256; ABV93256; Dshi_1514. DR GeneID; 5713171; -. DR KEGG; dsh:Dshi_1514; -. DR PATRIC; 21815645; VBIDinShi9476_1573. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; DSHI398580:GKEL-1536-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 207 AA; 21873 MW; C349A77A0F067395 CRC64; MADTPEQPQL YLVTPPEIEL SSFPGTLARL LDGAEIACVR LALSTRDEDR IARAADACRE VAHARDVPLV IDTHFRMVER LGLDGVHLGD GARSVRKVRK EIGAEAVVGA HCGASQHDGM TAGEAGADYV AFGPVAASLT GAGEVAEADL FAWWSQMIEL PVVAEGNLTT AAVETLAPLT DFFALGEEIW GTDDPLEALR TLTAPLG // ID A8LRU9_DINSH Unreviewed; 199 AA. AC A8LRU9; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 14-MAY-2014, entry version 42. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=Dshi_0911; OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Dinoroseobacter. OX NCBI_TaxID=398580; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12; RX PubMed=19741735; DOI=10.1038/ismej.2009.94; RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I., RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., RA Han C., Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., RA Liebl W., Liesegang H., Meincke L., Pati A., Petersen J., RA Piekarski T., Pommerenke C., Pradella S., Pukall R., Rabus R., RA Stackebrandt E., Thole S., Thompson L., Tielen P., Tomasch J., RA von Jan M., Wanphrut N., Wichels A., Zech H., Simon M.; RT "The complete genome sequence of the algal symbiont Dinoroseobacter RT shibae: a hitchhiker's guide to life in the sea."; RL ISME J. 4:61-77(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000830; ABV92656.1; -; Genomic_DNA. DR RefSeq; YP_001532257.1; NC_009952.1. DR ProteinModelPortal; A8LRU9; -. DR STRING; 398580.Dshi_0911; -. DR EnsemblBacteria; ABV92656; ABV92656; Dshi_0911. DR GeneID; 5710601; -. DR KEGG; dsh:Dshi_0911; -. DR PATRIC; 21814365; VBIDinShi9476_0940. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; DSHI398580:GKEL-928-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 199 AA; 21782 MW; 834EDF43D1D051C0 CRC64; MSALHPFYPI FDRAEWLIRL LPLGIKLVQL RVKDQPPEVI RAEIRAAKGL CAEHGCTLVV NDHWQMAIAE GCDWVHLGQE DLDTADLGAL RAAGIKLGIS THDEAELDRA LACKPAYIAL GPIYPTILKK MKWEQQGIEK LTEWKSRIGD VPLIAIGGMT PDRAPGALAA GADVVSAVTD ITLNPDPEAQ VRRWLEVLG // ID A8M4E2_SALAI Unreviewed; 232 AA. AC A8M4E2; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Sare_4276; OS Salinispora arenicola (strain CNS-205). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Salinispora. OX NCBI_TaxID=391037; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNS-205; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., RA Penn K., Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.; RT "Complete sequence of Salinispora arenicola CNS-205."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000850; ABW00058.1; -; Genomic_DNA. DR RefSeq; YP_001539048.1; NC_009953.1. DR ProteinModelPortal; A8M4E2; -. DR STRING; 391037.Sare_4276; -. DR EnsemblBacteria; ABW00058; ABW00058; Sare_4276. DR GeneID; 5706988; -. DR KEGG; saq:Sare_4276; -. DR PATRIC; 23437137; VBISalAre38676_4317. DR eggNOG; NOG131844; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VITDWRL; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SARE391037:GH66-4326-MONOMER; -. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 232 AA; 23486 MW; 44A3C28BF245D9FA CRC64; MTGPTGLVVL TDRRAVRRPL VEVVADAVAG GARWVVLREK DLPRAERAAL ACDLRAVLEP VGGTLVVAGP DPLGGSAVHL PAAGPYPPPR RGLVGRSCHD EAELGRLTVE DYAVLSPVYP TSTKPGYGPP LRPARLAALI RISPVPVLAL GGIETAEQVR ECVTAGAAGV VVLGAIMRAE SPRAAAAALQ GAFDRAAVGL ACDGPAPTGG SPDLGPDACT RADPIALSGG RT // ID A8N7H4_COPC7 Unreviewed; 523 AA. AC A8N7H4; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 16-APR-2014, entry version 32. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme; GN ORFNames=CC1G_03317; OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC OS 9003) (Inky cap fungus) (Hormographiella aspergillata). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Agaricomycetidae; Agaricales; Psathyrellaceae; OC Coprinopsis. OX NCBI_TaxID=240176; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003; RX PubMed=20547848; DOI=10.1073/pnas.1003391107; RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., RA Borodovsky M., Burns C., Canbaeck B., Casselton L.A., Cheng C.K., RA Deng J., Dietrich F.S., Fargo D.C., Farman M.L., Gathman A.C., RA Goldberg J., Guigo R., Hoegger P.J., Hooker J.B., Huggins A., RA James T.Y., Kamada T., Kilaru S., Kodira C., Kuees U., Kupfer D., RA Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J., Mackey A.J., RA Manning G., Martin F., Muraguchi H., Natvig D.O., Palmerini H., RA Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M., RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q., RA Zolan M.E., Pukkila P.J.; RT "Insights into evolution of multicellular fungi from the assembled RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus)."; RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACS02000003; EAU91149.1; -; Genomic_DNA. DR RefSeq; XP_001830780.1; XM_001830728.2. DR ProteinModelPortal; A8N7H4; -. DR GeneID; 6007225; -. DR KEGG; cci:CC1G_03317; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 523 AA; 54978 MW; 1898DF3A6DAFAEDC CRC64; MVEIDYSVYL VTGRNFLPPG KDYLDSLEES LQGGVTVVQV REKDADTGEF IEIARKSKEV CDKYNVPLII NDRVDVALVV GAAGLHIGQD DMDIAQARKL LPPGTIIGVS CNKIEELEAA VKAGADYVGI GTVWPTQTKD VAHRIIGPRG IGERLKVLDG TGVKAVAIGG IKSTNLWRTL HGGVTTTGSA LDGVAVVSEI MGSPEPKSAA EKLSSIVKAF KKEHARVTEL RASQRLTKES IIGQVAELVK KIRDVNPLVH QITNHVVATQ SANVTLAIGA SPIMATEPAE MEDLSKIANA LLVNIGTMVS SGVEGARLAG VCANKYRKPI VFDPVGVGAS AFRRNNANGF LNQWQASIIK GNAGELAALA GTTEVLSKGV DSVGSGFKDP VSFVRNLARK ERCVIVLTGH TDYISDGNTV VSLSNGHPAL GQITGSGCIL GSCLASYCAT ALQGKEVDLQ GPIVDDTSFV AAIAGTLVLT VAAEIATKKD EFKGPGTFLS VLIDTLSTLK AEDIVENAKL TIH // ID A8PMT5_9COXI Unreviewed; 208 AA. AC A8PMT5; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RICGR_0824; OS Rickettsiella grylli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Rickettsiella. OX NCBI_TaxID=59196; RN [1] RP NUCLEOTIDE SEQUENCE. RA Seshadri R., Federici B.A.; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RA Myers G.S.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQJ02000001; EDP46230.1; -; Genomic_DNA. DR ProteinModelPortal; A8PMT5; -. DR EnsemblBacteria; EDP46230; EDP46230; RICGR_0824. DR PATRIC; 30022933; VBIRicGry46442_0780. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 23121 MW; 59DD9E1C93A7CD60 CRC64; MNIDYSYYLL ADEQASEPLS VIDAVQRVLN HTVRCVQLRM KNQRRKKIMD TGKQLVDLLQ AWNIPLIIND HADIACAIDA AGVHLGQTDR PYPEIRQHCG YKKIIGLTIE NSQQAQQCRH YDCDYFGVGP IFSTVTKKFS TPPLGLVQFN RIMRILNAPV VAIGGITLEN VQSVLETGCA GIAVASAVFQ TPDPVKQSQK FAHIISQS // ID A8PSG5_MALGO Unreviewed; 561 AA. AC A8PSG5; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 16-APR-2014, entry version 36. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=MGL_0253; OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) OS (Dandruff-associated fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina; OC Exobasidiomycetes; Malasseziales; Malasseziaceae; Malassezia. OX NCBI_TaxID=425265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4612 / CBS 7966; RX PubMed=18000048; DOI=10.1073/pnas.0706756104; RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E., RA Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M., RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T., RA Chu L., Sears R., Yuan B., Dawson T.L. Jr.; RT "Dandruff-associated Malassezia genomes reveal convergent and RT divergent virulence traits shared with plant and human fungal RT pathogens."; RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYY01000001; EDP45264.1; -; Genomic_DNA. DR RefSeq; XP_001732478.1; XM_001732426.1. DR ProteinModelPortal; A8PSG5; -. DR GeneID; 5856784; -. DR KEGG; mgl:MGL_0253; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 561 AA; 60257 MW; 990114C1A2AB3980 CRC64; MSFDLSVYLV TGRELLPPGK DYLQSLDESL RDGYVSIVQI REKHVSFEEF LAVAQASLAI CDKYHVRMMI NDNVDVAALL PERVGLHIGQ EDAKLEYARQ RLGPHRIIGL SVHSVDEARA ALDSDADYVG VGPCWPTKSK EGVSDDDALM LRGAADILAS LRRDPATTPP GKRTHVPSVL IGGINVRTAF RTLFGASSEH AEPDGIAVIS AIVSRRDPDV AAKELHSIVT AFRRVRQDTA PSSPTFPTES KVLIQSVQEL LRAYHTRYES VTRKDDASCV SLPRPLVHTI TSHVSSNFSA NMTLAFSASP IMSHEYEEVE PLSHVYGSLV LNIGTISPDS RKGMARAGPA ANNRGKPVVL DPVGVGATPF RHRTVQSILN ETQVTLIKGN AAEIATLCNS NDAQTQGVDS VGELTSAPVL ARRLARQEGA FVLLTGEVDY LTDGNVVLES RCGTPMLGRI TASGCSLGCV VAAGMAAAQS KYGIQLGNQV EQRQSPPRLH HELMIGALAG LLTYTIAAER AAALPSVRGP GSFIPALLDE VASFDPACLE LYKDRLTFAS P // ID A8RW76_9CLOT Unreviewed; 226 AA. AC A8RW76; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLOBOL_04493; OS Clostridium bolteae ATCC BAA-613. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411902; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-613; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-613; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium bolteae (ATCC BAA-613)."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCC02000036; EDP15156.1; -; Genomic_DNA. DR ProteinModelPortal; A8RW76; -. DR EnsemblBacteria; EDP15156; EDP15156; CLOBOL_04493. DR PATRIC; 36962626; VBICloBol101009_0174. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24395 MW; 3AC903F364CB0D0C CRC64; MRFDRRQLLI YAVTDKAWIG KLSLKEQVEE ALKGGATMVQ LREKELDKGN FEEVLRTAWD IRRITEDYNV PLMIDDNLEL ALACRADGLH VGQNDMEASE ARRLLGPDRI LGVTAKTVDQ ARKAQAAGAD YLGSGAIFGT STKADARPMT METLNAICDC VDIPVVAIGG ICLDNIGHLA GSHAAGAAIV SGIFGAPNIR ETTEKLVKAM EEITRLSGQD LRAGSV // ID A8S7P4_9FIRM Unreviewed; 212 AA. AC A8S7P4; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FAEPRAM212_00527; OS Faecalibacterium prausnitzii M21/2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=411485; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M21/2; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Faecalibacterium prausnitzii M21/2."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M21/2; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABED02000017; EDP22747.1; -; Genomic_DNA. DR ProteinModelPortal; A8S7P4; -. DR EnsemblBacteria; EDP22747; EDP22747; FAEPRAM212_00527. DR PATRIC; 30684106; VBIFaePra13114_0132. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22788 MW; CA8598C89546D27A CRC64; MKCDKHTMLL YAVTDRAWVG EQTLYQQVES ALKGGATCVQ LREKQLGDAD FLQEAIQIHA LCQQYGVPLF INDNVEVALQ CHAEGIHVGQ DDMAAAQVRQ RVGDGVMIGV SAHTVQEALD AVAHGADYLG VGAVFATHTK TDVSEMPRQT LLDICNAVDV PVVAIGGIHK ENILQLKGTG VDGVALVSAI FAAKDIEAEC RELRALSEQI IK // ID A8SP51_9FIRM Unreviewed; 217 AA. AC A8SP51; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=COPEUT_00172; OS Coprococcus eutactus ATCC 27759. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=411474; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27759; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Coprococcus_eutactus(ATCC 27759)."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27759; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABEY02000002; EDP27708.1; -; Genomic_DNA. DR ProteinModelPortal; A8SP51; -. DR EnsemblBacteria; EDP27708; EDP27708; COPEUT_00172. DR PATRIC; 29079266; VBICopEut84706_1073. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23419 MW; 633E9C75DF661238 CRC64; MYIMINCSKK ELMLYAVTDR HWLGDETLYD QVKKALDGGA TFVQLREKKL DREDFLAEAL EIQKLCKKYG VPFVINDEVS IAKDIDADGV HVGQSDMEAM DVRKVLGPDK ILGVSAQTVE QAIIAEKHGA DYLGVGAVFA TGSKDDADDV SHETLKAICE AVSIPVIAIG GITKDNVSEL AGSGICGVAV ISAIFGQNDI KKATEDLKAS VEKMLEQ // ID A8SUL1_9FIRM Unreviewed; 216 AA. AC A8SUL1; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=COPEUT_01799; OS Coprococcus eutactus ATCC 27759. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=411474; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27759; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Coprococcus_eutactus(ATCC 27759)."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27759; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABEY02000022; EDP26256.1; -; Genomic_DNA. DR ProteinModelPortal; A8SUL1; -. DR EnsemblBacteria; EDP26256; EDP26256; COPEUT_01799. DR PATRIC; 29077903; VBICopEut84706_0422. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23454 MW; 38F1C1655CE7D022 CRC64; MYTFNPTLYF ITDSTGLSEE EFLYRVECAL DGGATLIQLR EKDRTTREYI HLAYKVHSIA RRYNVPLIVD DRVDVALAVG TEGVHVGQTD MPVSIARKLM GPDRIVGATT KTVTQAVEAY EQGADYLGVG AIYPTTTKVK TVLTTTDTLR DICAAVPIPV NAIGGLNKTN LDVLTGIPIA GICVVSAIMK SDNPCKSAHD LLILSKQLQN KLQNGK // ID A8T9Y8_9VIBR Unreviewed; 471 AA. AC A8T9Y8; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 19-FEB-2014, entry version 41. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=AND4_16769; OS Vibrio sp. AND4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=314289; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AND4; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AND4; RX PubMed=20436956; DOI=10.1371/journal.pbio.1000358; RA Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R., RA Milton D.L., Gonzalez J.M., Pinhassi J.; RT "Proteorhodopsin phototrophy promotes survival of marine bacteria RT during starvation."; RL PLoS Biol. 8:E1000358-E1000358(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGR01000020; EDP57860.1; -; Genomic_DNA. DR ProteinModelPortal; A8T9Y8; -. DR EnsemblBacteria; EDP57860; EDP57860; AND4_16769. DR PATRIC; 28395327; VBIVibSp137788_3019. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 471 AA; 52666 MW; CCC3A9AE1F73785B CRC64; MSKILIPSSL CELTGLVQHC LLLAKEQGFS IEDIELGVSP TQYLQLVRDQ QITHITTDLI DGYDSEHECS FVLYYHSALS VEACAKQPSK AIYIGIADTQ VSDEKDKVLQ LDIWRHPIND ELRALSVKSK PNAMFDPVHH LAWIVALTVL DFPIEDALTL ARGMLTQQAN VSRETRLNDN PNEGRSIQWV DQFGDFPTPV LEDHRLGIQV GWSAQGESIV FPTLTKQSLG LYPVVDDVAW VERLIPLGIN TIQLRIKNPQ QADLEQQIIR AIELGRQYQA QVFINDYWQL AIKHGAYGVH LGQEDIEESN LAQLTKAGVR LGLSTHGYYE LLRIVQIHPS YIALGHIFPT TTKQMPSKPQ GLVRLALYQK LIDSIPYGNK NLAFRPSKDK AVSDYVLGFP TVAIGGIDQS NADQVWQAGV SSLAVVRAIT LAESPQSVID FFAQLMKERQ QTFTDQNCEL VDTKRGEHAH G // ID A8TXD1_9PROT Unreviewed; 230 AA. AC A8TXD1; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BAL199_19351; OS alpha proteobacterium BAL199. OC Bacteria; Proteobacteria; Alphaproteobacteria. OX NCBI_TaxID=331869; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL199; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHC01000017; EDP63041.1; -; Genomic_DNA. DR ProteinModelPortal; A8TXD1; -. DR EnsemblBacteria; EDP63041; EDP63041; BAL199_19351. DR PATRIC; 30880219; VBIAlpPro7182_4075. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 51 55 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 24378 MW; C4E781E4B6D8B153 CRC64; MSDRNNMGLG TPDERVPTQL YLITPPRIDD LDGFADRLAE ALDAGPVACL QIRLKDVVDD AVRRATERLL PVAHERGVPV LMNDSAKLAL ETGCDGVHVG QDDTPYAEAR RLLGGRAMIG VTCKASRHLA MAAAEAGADY VAFGAFFETA TKQSETRAPV EILDWWQDIA LIPCVAIGGI TPDNCGPLVE AGADFLAVVG AVWNHPQGPG AAVKAFEAAI AASMDFTRPT // ID A8USJ4_9AQUI Unreviewed; 215 AA. AC A8USJ4; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HG1285_18209; OS Hydrogenivirga sp. 128-5-R1-1. OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga. OX NCBI_TaxID=392423; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=128-5-R1-1; RA Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHJ01000002; EDP76130.1; -; Genomic_DNA. DR ProteinModelPortal; A8USJ4; -. DR EnsemblBacteria; EDP76130; EDP76130; HG1285_18209. DR PATRIC; 38512075; VBIHydSp35543_0522. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 24081 MW; B5FF0EAD891B4EE4 CRC64; MNLTIYLITD DKYFKGREFL PTVEEALKGG VTAVQYRFKN KNTKEMYEEL LKLRELTKKY GADLVVNDRA DLALAVEADG VHVGKEDLPP EAVRKVVGDK LYIGYTANSL EELRKAQNLP VDYIGFGSIY PTTTKESYEL VGVEALREAV RISEKPIVCI GGIMPYRVEE VVKAGCRNLA ISAGILGFED VKKAAEEIQR AYKNTLKQLM LLGRI // ID A8UY05_9AQUI Unreviewed; 196 AA. AC A8UY05; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HG1285_08506; OS Hydrogenivirga sp. 128-5-R1-1. OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga. OX NCBI_TaxID=392423; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=128-5-R1-1; RA Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHJ01000012; EDP74645.1; -; Genomic_DNA. DR ProteinModelPortal; A8UY05; -. DR EnsemblBacteria; EDP74645; EDP74645; HG1285_08506. DR PATRIC; 38515073; VBIHydSp35543_1993. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 196 AA; 21940 MW; BB00732A26B695E6 CRC64; MKELPRLYAI TDRAKYGEDF IKTLEGIFKK GVKMVQLREK DLNGRALYEL AEEVRALTRR YDALLLINER FDVARAVGAD GVHLPEKSFP PSVVKSLFPD MIVGFSAHSL ESVRYAEEEG ADFVTLGPVF RTTSHPEVKP IGTLKLKEVS GKVNIPIYAL GGVTWDRIKL CYKNGAYGIA GITIFLNGYE DERPDT // ID A8UZB5_9AQUI Unreviewed; 185 AA. AC A8UZB5; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 19-FEB-2014, entry version 28. DE SubName: Full=Thiamine phosphate synthase; GN ORFNames=HG1285_08206; OS Hydrogenivirga sp. 128-5-R1-1. OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga. OX NCBI_TaxID=392423; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=128-5-R1-1; RA Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHJ01000033; EDP74309.1; -; Genomic_DNA. DR ProteinModelPortal; A8UZB5; -. DR EnsemblBacteria; EDP74309; EDP74309; HG1285_08206. DR PATRIC; 38515632; VBIHydSp35543_2260. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 185 AA; 21054 MW; 3D8AE94BEB596B68 CRC64; MKNKLQKFYA ITDRKKYSSF EDTVKKLLDK GIRMFQIREK DLPTGELYRF TEKFLKLTEG YNVHIFINDR VDIALMFSLD GVHLPENSFD VEVVKSNFPQ LIVGKSCHSL ECAKKAEENG ADYVIFSPIF KVEGKGKPQG IEKLKEVVNL LNIPVYALGG INKNNIEKVL KTGVYGIAGI RTFLD // ID A8YGC5_MICAE Unreviewed; 338 AA. AC A8YGC5; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IPF_171; OS Microcystis aeruginosa PCC 7806. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Microcystis. OX NCBI_TaxID=267872; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7806; RA Frangeul L.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM778938; CAO87229.1; -; Genomic_DNA. DR ProteinModelPortal; A8YGC5; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 122 Unknown (By similarity). FT REGION 123 338 Thiamine-phosphate synthase (By FT similarity). FT REGION 170 174 HMP-PP binding (By similarity). FT REGION 267 269 THZ-P binding (By similarity). FT METAL 203 203 Magnesium (By similarity). FT METAL 222 222 Magnesium (By similarity). FT BINDING 202 202 HMP-PP (By similarity). FT BINDING 241 241 HMP-PP (By similarity). FT BINDING 270 270 HMP-PP (By similarity). FT BINDING 297 297 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 338 AA; 37891 MW; 347D4A6391AEBB37 CRC64; MKLETTAIKR ILDANLDRAR EGLRIIEEWC RFGLDNPNLA QECKEMRHQL ASWHSIDLKR HRDTAGDIGT NLSHPREEIR ETVEGLLQAN LARVQEAFRV LEEYGKLYDL ELGIACKQLR YRVYQLESKL LISPPLEKLK ASPLYLVTSP AENLLEIVEL ALKGGLKLVQ YRHKTAADTI RLEEAAKLCE LCHRYDALFI MNDRVDIAKA VHADGVHLGQ QDVPISLARQ FLGPTAIIGR STTNPQEMAK AIQEKADYVG VGPVYATPTK AGKTPAGLEY VRYARENCPL PWFAIGGIDS SNIKEVLEAG AQRVAVVRAI MEAQHPDVVT QELLTQLK // ID A9A0U4_DESOH Unreviewed; 539 AA. AC A9A0U4; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 14-MAY-2014, entry version 57. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Dole_1765; OS Desulfococcus oleovorans (strain DSM 6200 / Hxd3). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfococcus. OX NCBI_TaxID=96561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6200 / Hxd3; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Wawrik B., Richardson P.; RT "Complete sequence of Desulfococcus oleovorans Hxd3."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000859; ABW67569.1; -; Genomic_DNA. DR RefSeq; YP_001529646.1; NC_009943.1. DR ProteinModelPortal; A9A0U4; -. DR STRING; 96561.Dole_1765; -. DR EnsemblBacteria; ABW67569; ABW67569; Dole_1765. DR GeneID; 5694604; -. DR KEGG; dol:Dole_1765; -. DR PATRIC; 21693637; VBIDesOle35880_1824. DR eggNOG; COG0352; -. DR OrthoDB; EOG6RRKQ4; -. DR BioCyc; DOLE96561:GHF3-1790-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009030; F:thiamine-phosphate kinase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR000728; AIR_synth_N_dom. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016188; PurM_N-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR006283; ThiL. DR InterPro; IPR003733; TMP_synthase. DR PANTHER; PTHR30270; PTHR30270; 1. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55326; SSF55326; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR01379; thiL; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 539 AA; 57095 MW; 8B75D6C5E0B8F54F CRC64; MLPEDLRKHL RFYFITDDSG GPAPLEQAKA AILGGATMVQ YRNKAFDGRF FEEATAILRL CRVNQIPFIV NDDPVLARAL GADGVHVGQA DGSLKTARSI VGKNALVGVS VSTLDELART PVEFCDYIGT GPVFATSTKP DASPVIGVAG LKAVIDRSKK PVVAIGGINA ANAAACFSAG AAGVAVISCV SRADSPLEDA RFLAGACGIE VFSEKLNVPW NDEFGLIDRL LAGDKKANAA EEEILKVGPG DDAAVLHALK TPVITTDAQV ENVHFSFSWQ RPGEVGQRAV TVVLSDLAAA YARPVSLFVN LTLPHDRPES LAIDLYAGLK KGLAVYDCAL GGGNLSGGRE VSLNLFAVGE ARAPFYPARA NARPGDDLYC TGPLGRSRAG LLALAAGLEG YDSLVEAFKF PRARFDAAIV LADYNVRCVM DISDGLAGDA RHIARASGIT LCFDVDTAVC SDDLQRFCEK TGNRPEEMIF SGGEDYELLF ACPPETARRI GDVMPVYRLG RCLSFDGEYL RNLPEGVAPF QHGHAGSGD // ID A9ADY9_BURM1 Unreviewed; 371 AA. AC A9ADY9; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=Bmul_0316, BMULJ_02938; OS Burkholderia multivorans (strain ATCC 17616 / 249). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=395019; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17616, and ATCC 17616 / 249; RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., RA Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., RA Yuji N., Hattori M., Tsuda M.; RT "Complete genome sequence of Burkholderia multivorans ATCC 17616."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17616 / 249; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC RT 17616."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17616; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Tiedje J., Richardson P.; RT "Complete sequence of chromosome1 of Burkholderia multivorans ATCC RT 17616."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000868; ABX14011.1; -; Genomic_DNA. DR EMBL; AP009385; BAG44823.1; -; Genomic_DNA. DR RefSeq; YP_001578508.1; NC_010084.1. DR RefSeq; YP_001947359.1; NC_010804.1. DR STRING; 395019.Bmul_0316; -. DR EnsemblBacteria; ABX14011; ABX14011; Bmul_0316. DR EnsemblBacteria; BAG44823; BAG44823; BMULJ_02938. DR GeneID; 5765480; -. DR GeneID; 6358801; -. DR KEGG; bmj:BMULJ_02938; -. DR KEGG; bmu:Bmul_0316; -. DR PATRIC; 19167838; VBIBurMul203716_3968. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BMUL395019:GIYO-2936-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 371 AA; 38971 MW; F7C8CA86893B4BFE CRC64; MSARFADAFW PPADELAEAA ERIRARLGDW PRAAAPWRLC MTAPDAPADG DVLIVSRGDR AGQARASAVS RPASPNAVAI EFDERGAALH AADARYALDA AHALADDWIA ALAAFLDCGF APLDALVLAL AWRDGDETRA DDAWPVDAAQ FPRVAGLPAA AEPAFAPCPA RLGLYPVVPD AEWVERVLDC GVQTIQLRVK GAAPDVLRRE IARAVAAGRR YPDARVFIND HWQIAADEGA YGVHLGQEDL ETADLAALAR AGLRLGLSSH GYYEMLRALH ERPSYLALGP VFATATKAVA APPQGLARIA RYARFASPRV PLVAIGGVGL DALPAVLATG VGSVAVVSAV TGAGDYRAAI AALQRCFASP I // ID A9ANQ7_BURM1 Unreviewed; 194 AA. AC A9ANQ7; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE SubName: Full=Thiamine monophosphate synthase; DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=Bmul_4895, BMULJ_03620; OS Burkholderia multivorans (strain ATCC 17616 / 249). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=395019; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17616, and ATCC 17616 / 249; RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., RA Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., RA Yuji N., Hattori M., Tsuda M.; RT "Complete genome sequence of Burkholderia multivorans ATCC 17616."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17616 / 249; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 2 of Burkholderia multivorans ATCC RT 17616."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17616; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Tiedje J., Richardson P.; RT "Complete sequence of chromosome2 of Burkholderia multivorans ATCC RT 17616."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000869; ABX18566.1; -; Genomic_DNA. DR EMBL; AP009386; BAG45492.1; -; Genomic_DNA. DR RefSeq; YP_001584858.1; NC_010086.1. DR RefSeq; YP_001948028.1; NC_010805.1. DR STRING; 395019.Bmul_4895; -. DR EnsemblBacteria; ABX18566; ABX18566; Bmul_4895. DR EnsemblBacteria; BAG45492; BAG45492; BMULJ_03620. DR GeneID; 5768343; -. DR GeneID; 6362498; -. DR KEGG; bmj:BMULJ_03620; -. DR KEGG; bmu:Bmul_4895; -. DR PATRIC; 19169306; VBIBurMul203716_4690. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BMUL395019:GIYO-3618-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 194 AA; 20531 MW; C23591ADE30021A8 CRC64; MKPALPRRYV ITPEPASASA ADCDAFLDRL SAVLARGDTL VQLRVKSFDA AAFARLAADA LARCEAAGAQ LMLNGPIDAH GVLQLEHAGW HLDGATLRAT QQRPLPADRL LSAACHDADD LRLAARAGAD FVTLSPVLPT LSHPGAPTLG WAQFGAWAAQ AAMPVYALGG MTHAHLDEAR RRHAYGIAGI RGFW // ID A9BBN8_PROM4 Unreviewed; 343 AA. AC A9BBN8; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=P9211_13191; OS Prochlorococcus marinus (strain MIT 9211). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=93059; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9211; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., RA Steglich C., Church G.M., Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000878; ABX09250.1; -; Genomic_DNA. DR RefSeq; YP_001551204.1; NC_009976.1. DR ProteinModelPortal; A9BBN8; -. DR STRING; 93059.P9211_13191; -. DR EnsemblBacteria; ABX09250; ABX09250; P9211_13191. DR GeneID; 5731714; -. DR KEGG; pmj:P9211_13191; -. DR PATRIC; 22988242; VBIProMar136502_1393. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR93059:GHJV-1349-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 125 Unknown (By similarity). FT REGION 126 343 Thiamine-phosphate synthase (By FT similarity). FT REGION 177 181 HMP-PP binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 343 AA; 38031 MW; 764A65E7FF399592 CRC64; MAVIPTPEKH VAQLIDANLD RAREGLRVIE DWCRYGLQRK DLIIIIKDYR HQLGRLHQKT YKQARSAQTD QGSGLTHEAQ NDRISPLQIV SANCARVQEA LRVIEEFARN IDPELTKAAS KIRYEIYDLE INIQEATSGK KRQKELSACK LCLITTPHQE LIAKVSAGLK AGVGMVQYRC KKGKDIDKFS EAEKLAVICK DYGALFIVND RIDIALAVDA DGIHIGQEDL PLDIARKLIG PEKLIGVSCH SLEEAQKADK NGSDYIGFGP IFRTTSKPEV APLGLECLKQ ISNSINQPCF AIGGINHLNR SKLLSTGVSR IAVIDAIMKA EDPFQASKQL LEI // ID A9BZM0_DELAS Unreviewed; 307 AA. AC A9BZM0; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Daci_3290; OS Delftia acidovorans (strain DSM 14801 / SPH-1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Delftia. OX NCBI_TaxID=398578; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14801 / SPH-1; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Schleheck D., RA Richardson P.; RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000884; ABX35928.1; -; Genomic_DNA. DR RefSeq; YP_001564313.1; NC_010002.1. DR ProteinModelPortal; A9BZM0; -. DR STRING; 398578.Daci_3290; -. DR EnsemblBacteria; ABX35928; ABX35928; Daci_3290. DR GeneID; 5748875; -. DR KEGG; dac:Daci_3290; -. DR PATRIC; 21640541; VBIDelAci41351_3328. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RFKSEDR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; DACI398578:GHK3-3339-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 307 AA; 32438 MW; 32C896EAFC2EF535 CRC64; MSNDSIQSWA DAIVRLHGAT FAPEGSALPS QPVPQAQRQE PAYLAALQAC SALGFIAIDA QTLACAWQAQ TLRRGRFEAT LWPDDPRDFG LEGADPALAF PECPRSLGLY GVLPDAQWVG RMARAGVPTV QLRFKSEDRD AIAREVRSAV AAVEGTGALL FINDHWREAI DAGAYGVHVG QEDLDALAGA DLQAIHASGL RLGVSTHGYA EMVRAHAVQP SYIALGAVFP TTLKKMATAP QGLARLGAYV RLMQRYPLVA IGGISADQFP AVRATGVGSV AVVRALVNAE DPEAAAQQLL ARMHAAG // ID A9D1C7_9RHIZ Unreviewed; 228 AA. AC A9D1C7; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 27. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=HPDFL43_15502; OS Hoeflea phototrophica DFL-43. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Hoeflea. OX NCBI_TaxID=411684; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFL-43; RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIA02000003; EDQ34416.1; -; Genomic_DNA. DR ProteinModelPortal; A9D1C7; -. DR EnsemblBacteria; EDQ34416; EDQ34416; HPDFL43_15502. DR PATRIC; 27536433; VBIHoePho121037_0901. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 228 AA; 23902 MW; 73DB53BF1EC8030C CRC64; MTIRLFPTGY LMTSPANRCR LVLVTPDIAD AGELAEIMAN ALRGGDVASV IIPQHGIDEK SFQQRCEALI PVIQAAGAAA LVAGDTRVAG RVRADGLHIE AGPTAMAEAV ERHAPGLIVG GGNAKERHAA LSIGEAQPDY LIFGSIAGDI KPEPHPKNLA LAEWWADMIE IPCVLMGGTS TAFVEEMAAT DAEFIAFGQA VFSQPADAPR LVAEINAVLD EKAPRFGA // ID A9D303_9GAMM Unreviewed; 190 AA. AC A9D303; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=KT99_16064; OS Shewanella benthica KT99. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=314608; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KT99; RA Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIC01000008; EDQ01598.1; -; Genomic_DNA. DR ProteinModelPortal; A9D303; -. DR EnsemblBacteria; EDQ01598; EDQ01598; KT99_16064. DR PATRIC; 28557050; VBISheBen91426_1158. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 3 7 HMP-PP binding (By similarity). FT REGION 100 102 THZ-P binding (By similarity). FT REGION 151 152 THZ-P binding (By similarity). FT METAL 36 36 Magnesium (By similarity). FT METAL 55 55 Magnesium (By similarity). FT BINDING 35 35 HMP-PP (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 131 131 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 190 AA; 20267 MW; 071F6A6A82F1DB55 CRC64; MVQLREKHND VRTFIERALA VKEILQGSGV PLIINDRVDV ALEVDADGVH LGQSDMPVVL ARRLIGQEKL LGLSIENKQQ LIDAEYLPLD YLGLSAIFAT PTKTNINREW GIAGLAAAVR QSTLPIVAIG GINATNLDAI SATGVNRIAL VSAICHAESP RAAATKLLLQ RVNSAQYCAK GVIGSLSIGR // ID A9E499_9RHOB Unreviewed; 205 AA. AC A9E499; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 26. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=OIHEL45_12685; OS Oceanibulbus indolifex HEL-45. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Oceanibulbus. OX NCBI_TaxID=391624; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HEL-45; RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABID01000003; EDQ04556.1; -; Genomic_DNA. DR ProteinModelPortal; A9E499; -. DR EnsemblBacteria; EDQ04556; EDQ04556; OIHEL45_12685. DR PATRIC; 25528116; VBIOceInd27211_2108. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 205 AA; 22120 MW; 3ABB027E99C9D962 CRC64; MDAPEQPQIY LITPPEVELS RFPAQLAAVL DAHPVACVRM ALSTRDEDRL SRAGDALREV THSRDVALVI SDHLLMVERL GLDGVHLSDA ARTVRHARKE LGEDAIIGSY CGISRHEGMA AGEAGADYVS FGPVQSSALG DGSFAEAELF QWWSEVIEVP VVAEGALDID MIRALAPRTD FFGIGAEIWD KDDPVAELAT LIAAM // ID A9E7P4_9RHOB Unreviewed; 198 AA. AC A9E7P4; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=OIHEL45_15279; OS Oceanibulbus indolifex HEL-45. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Oceanibulbus. OX NCBI_TaxID=391624; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HEL-45; RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABID01000004; EDQ04303.1; -; Genomic_DNA. DR ProteinModelPortal; A9E7P4; -. DR EnsemblBacteria; EDQ04303; EDQ04303; OIHEL45_15279. DR PATRIC; 25529165; VBIOceInd27211_2625. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 198 AA; 21791 MW; 20BC6CE076DEF17B CRC64; MNLPHFYPVF DSAAWVARAM PLGVKLVQLR IKDAPEDVLR DEITIALDLC RQHGAQLVVN DHWQLAIELG VDWLHLGQED LDTADIPAIR RAGMKLGLST HDHAELERAL ALAPDYIALG PVYPTILKKM KWTEQGLDRL TEWKARIGDI PLCAIGGMSV ARAPGAFAAG ADMVAAVTDI TLNADPEARM REWLEVTA // ID A9EKJ4_9GAMM Unreviewed; 524 AA. AC A9EKJ4; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=KT99_11495; OS Shewanella benthica KT99. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=314608; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KT99; RA Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIC01000038; EDP99488.1; -; Genomic_DNA. DR ProteinModelPortal; A9EKJ4; -. DR EnsemblBacteria; EDP99488; EDP99488; KT99_11495. DR PATRIC; 28561541; VBISheBen91426_3347. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 524 AA; 56109 MW; CA726F8707BDADC4 CRC64; MENVEPTSSA LKPVVWSIAG SDSGGGAGIG ADLATMNDLA CHACTVITTL TAQSSVAVNL VEPVSDEMLL AQLDTLLQDL PPKAIKIGLL ANQRQIDILS RWLALELDDH NKRSGTEVAV ILDPVMIASC GDRLDEDDSR LDFSPFKGLI TLITPNALEL GELVGQSLAD MSQYHLAAQD LAQLLDTNVL AKGGGKGPAW RADAAQDIFV CTRATACSEM HQGRSFLLSS PRASNNNHGT GCTLSSAIAS VMASGFVLHD AIVVAKAYVC AGIKHSYRVD EGPGPLARTS WPRELSHFPT ISSLDEGPSL PVGIKFKTIG ERLGLYPVVS DLPLLASLLK AGAKTIQLRI KDENDPQLED KIAHAIALGR DYQAKVFIND YWELALKHNA YGVHLGQEDL YVADLKRIAE AQLALGISSH SYFELLLASQ ITPSYIALGH IFPTTTKVMP SAPQGLMKLQ HYVDLFKGHY PLVAIGGIDA SRIETVKRTG VDDVAIVRAV TESQQPGAAY LALSSAWEQA HVSQ // ID A9EXD7_SORC5 Unreviewed; 205 AA. AC A9EXD7; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 41. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE2; OrderedLocusNames=sce4238; OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain OS So ce56)). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Polyangiaceae; Sorangium. OX NCBI_TaxID=448385; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56; RX PubMed=17965706; DOI=10.1038/nbt1354; RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., RA Altmeyer M.O., Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., RA Bolten C.J., Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., RA Gaigalat L., Goesmann A., Groeger C., Gross F., Jelsbak L., RA Jelsbak L., Kalinowski J., Kegler C., Knauber T., Konietzny S., RA Kopp M., Krause L., Krug D., Linke B., Mahmud T., Martinez-Arias R., RA McHardy A.C., Merai M., Meyer F., Mormann S., Munoz-Dorado J., RA Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., Rueckert C., RA Sasse F., Scharfe M., Schuster S.C., Suen G., Treuner-Lange A., RA Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., Wenzel S.C., RA Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., Puehler A., RA Mueller R.; RT "Complete genome sequence of the myxobacterium Sorangium cellulosum."; RL Nat. Biotechnol. 25:1281-1289(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM746676; CAN94401.1; -; Genomic_DNA. DR RefSeq; YP_001614881.1; NC_010162.1. DR ProteinModelPortal; A9EXD7; -. DR STRING; 448385.sce4238; -. DR EnsemblBacteria; CAN94401; CAN94401; sce4238. DR GeneID; 5809143; -. DR KEGG; scl:sce4238; -. DR PATRIC; 23666863; VBISorCel80414_4633. DR eggNOG; NOG287972; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSCHTL; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SCEL448385:GJ75-4400-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 205 AA; 20347 MW; FF878C8F36295B98 CRC64; MLTPRLTLIT QAADVPEPVL LARLSAFGAL PPEARARVAV QLRDPELSGA ALHALGRRLR DATAALGASF VVNDRLDLAL LLGADGVHLG RRSVAVADAR ALLGAGAFVS VACHGVDDVL RAAEAGADAA VLSPIFATPG KGPPLGLAAL REARARLAAA SRDVALLALG GIDAASAPAC LAAGADGVAA IRADFGGALP AQRAG // ID A9FJE0_SORC5 Unreviewed; 250 AA. AC A9FJE0; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; Synonyms=thiE; OrderedLocusNames=sce1789; OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain OS So ce56)). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Polyangiaceae; Sorangium. OX NCBI_TaxID=448385; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56; RX PubMed=17965706; DOI=10.1038/nbt1354; RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., RA Altmeyer M.O., Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., RA Bolten C.J., Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., RA Gaigalat L., Goesmann A., Groeger C., Gross F., Jelsbak L., RA Jelsbak L., Kalinowski J., Kegler C., Knauber T., Konietzny S., RA Kopp M., Krause L., Krug D., Linke B., Mahmud T., Martinez-Arias R., RA McHardy A.C., Merai M., Meyer F., Mormann S., Munoz-Dorado J., RA Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., Rueckert C., RA Sasse F., Scharfe M., Schuster S.C., Suen G., Treuner-Lange A., RA Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., Wenzel S.C., RA Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., Puehler A., RA Mueller R.; RT "Complete genome sequence of the myxobacterium Sorangium cellulosum."; RL Nat. Biotechnol. 25:1281-1289(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM746676; CAN91947.1; -; Genomic_DNA. DR RefSeq; YP_001612427.1; NC_010162.1. DR ProteinModelPortal; A9FJE0; -. DR STRING; 448385.sce1789; -. DR EnsemblBacteria; CAN91947; CAN91947; sce1789. DR GeneID; 5807145; -. DR KEGG; scl:sce1789; -. DR PATRIC; 23661441; VBISorCel80414_1945. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AMISALW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SCEL448385:GJ75-1852-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 187 187 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 250 AA; 25802 MW; 937638D76BECAEA6 CRC64; MRGLYAIVDT DSLARRGLDP AAFAEAVLDA RPAAIQLRDK RGGAAQTLSL LRAIQPLAAR AGVPLFANDR ADLAILARCD GVHVGQDDLP VAAVRRLAQR ASVPLRVGLS THTSAQIEAA LRALSELRDA GDSGDSLERL DYVAIGPIFA TSSKERPDAV VGLEGLASLC ALVERVRPGL PVVAIGGISL ERAAEVGARC SVAAIIAALL PDQGTPAPRA LEEVSARARA LQQALALAGA RAAPADRGAR // ID A9H6F4_GLUDA Unreviewed; 212 AA. AC A9H6F4; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 62. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GDI0512, Gdia_1495; OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / OS PAl5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconacetobacter. OX NCBI_TaxID=272568; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PAl 5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Triplett E.W.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49037 / DSM 5601 / PAl5, and PAl 5; RX PubMed=19775431; DOI=10.1186/1471-2164-10-450; RA Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A., RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., RA Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M., RA Nogueira E., Cidade D., Oliveira D., Simao T., Macedo J., Valadao A., RA Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E., RA Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H., RA Junior J., de Souza Filho G., Martin Quintana Flores V., Ferreira B., RA Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J., RA Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., RA Amaral G., Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., RA Rossle S.C., Urmenyi T., Rael Pereira A., Silva R., Rondinelli E., RA von Kruger W., Martins O., Baldani J.I., Ferreira P.C.; RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte RT Gluconacetobacter diazotrophicus Pal5."; RL BMC Genomics 10:450-450(2009). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49037 / DSM 5601 / PAl5, and PAl 5; RX PubMed=21304715; DOI=10.4056/sigs.972221; RA Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.; RT "Two genome sequences of the same bacterial strain, Gluconacetobacter RT diazotrophicus PAl 5, suggest a new standard in genome sequence RT submission."; RL Stand. Genomic Sci. 2:309-317(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001189; ACI51274.1; -; Genomic_DNA. DR EMBL; AM889285; CAP54455.1; -; Genomic_DNA. DR RefSeq; YP_001600796.1; NC_010125.1. DR RefSeq; YP_002275889.1; NC_011365.1. DR STRING; 272568.GDI_0512; -. DR EnsemblBacteria; ACI51274; ACI51274; Gdia_1495. DR EnsemblBacteria; CAP54455; CAP54455; GDI0512. DR GeneID; 5791352; -. DR GeneID; 6974905; -. DR KEGG; gdi:GDI_0512; -. DR KEGG; gdj:Gdia_1495; -. DR PATRIC; 22051388; VBIGluDia203729_1494. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GDIA272568:GJPS-518-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 138 140 THZ-P binding (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22026 MW; D729A9C4EC8EBC4A CRC64; MNDCQLYLVT PPALDPAAFA PDLARALDAG AVAAVQLRLT DATDDAVLRA VDVLRPVAQE RDVAFILNGR PDLARRTGCD GVHIDAPDLQ DGTELARIRA ILGEDLQLGV SCRDSRDLAM RAGEAGADYV SFGAFFPSAS VETPVLADPA LLAWWTTMME LPVVAIGGIT PANCAPLVQA GADFLAVIGA VWSHPDGPAA GVRAMNAAID AA // ID A9HI58_GLUDA Unreviewed; 202 AA. AC A9HI58; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 62. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=GDI1782, Gdia_0012; OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / OS PAl5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconacetobacter. OX NCBI_TaxID=272568; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PAl 5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Triplett E.W.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49037 / DSM 5601 / PAl5, and PAl 5; RX PubMed=19775431; DOI=10.1186/1471-2164-10-450; RA Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A., RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., RA Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M., RA Nogueira E., Cidade D., Oliveira D., Simao T., Macedo J., Valadao A., RA Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E., RA Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H., RA Junior J., de Souza Filho G., Martin Quintana Flores V., Ferreira B., RA Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J., RA Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., RA Amaral G., Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., RA Rossle S.C., Urmenyi T., Rael Pereira A., Silva R., Rondinelli E., RA von Kruger W., Martins O., Baldani J.I., Ferreira P.C.; RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte RT Gluconacetobacter diazotrophicus Pal5."; RL BMC Genomics 10:450-450(2009). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49037 / DSM 5601 / PAl5, and PAl 5; RX PubMed=21304715; DOI=10.4056/sigs.972221; RA Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.; RT "Two genome sequences of the same bacterial strain, Gluconacetobacter RT diazotrophicus PAl 5, suggest a new standard in genome sequence RT submission."; RL Stand. Genomic Sci. 2:309-317(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001189; ACI49814.1; -; Genomic_DNA. DR EMBL; AM889285; CAP55725.1; -; Genomic_DNA. DR RefSeq; YP_001602027.1; NC_010125.1. DR RefSeq; YP_002274429.1; NC_011365.1. DR STRING; 272568.GDI_1782; -. DR EnsemblBacteria; ACI49814; ACI49814; Gdia_0012. DR EnsemblBacteria; CAP55725; CAP55725; GDI1782. DR GeneID; 5790035; -. DR GeneID; 6973400; -. DR KEGG; gdi:GDI_1782; -. DR KEGG; gdj:Gdia_0012; -. DR PATRIC; 22048380; VBIGluDia203729_0012. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; GDIA272568:GJPS-1815-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 202 AA; 21477 MW; 46EF7EC614AC1A15 CRC64; MSLASRIYPV VDRADWIDRL GGAGARLIQL RVKDLQGAAL LAEIRAAKAH AARHGVTLVL NDYWRLALDE GIDFIHLGQE DLDTADVAAI RAGGIRLGVS THSTDELDRA LSVAPDYVAL GPVWPTKLKK MPWAPQGVER LAEWKRLVGP VPLVAIGGIT LARAASCIAA GADCVSAVSD FTGQPDPEAQ VRAWLAATGD MT // ID A9I1K3_BORPD Unreviewed; 320 AA. AC A9I1K3; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE SubName: Full=Bifunctional DGTP-pyrophosphohydrolase/thiamine phosphate synthase; DE EC=2.5.1.3; GN Name=mutT; OrderedLocusNames=Bpet0539; OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=340100; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448; RX PubMed=18826580; DOI=10.1186/1471-2164-9-449; RA Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., RA Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., RA Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., RA Larisch C., Link S., Linke B., Meyer F., Mormann S., Nakunst D., RA Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., RA Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., RA Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.; RT "The missing link: Bordetella petrii is endowed with both the RT metabolic versatility of environmental bacteria and virulence traits RT of pathogenic Bordetellae."; RL BMC Genomics 9:449-449(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM902716; CAP40871.1; -; Genomic_DNA. DR RefSeq; YP_001629142.1; NC_010170.1. DR ProteinModelPortal; A9I1K3; -. DR STRING; 340100.Bpet0539; -. DR EnsemblBacteria; CAP40871; CAP40871; Bpet0539. DR GeneID; 5818502; -. DR KEGG; bpt:Bpet0539; -. DR PATRIC; 21162533; VBIBorPet31633_0546. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPET340100:GJBO-542-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Transferase. SQ SEQUENCE 320 AA; 34169 MW; 02A24887C4363058 CRC64; MSERIVDVAA GLILRPDGQL LLGQRPEGKP WAGWWELPGG KLEPGETVLQ ALARELGEEL GIEVTQAVPW VTYVHVYPHT TVRLAFCQVT GWQGEPRGLE NQQLQWVDPA RAGEVGDLLP ATLPPLRWLQ LPDTYGISAI GGRAGLPDFL ERLERALARG LKLVQLREPG WPDGPGATSL RDALQAVLKL CHAAGARVLV NSAHPASWWR QADGVHLRWA DAALLQARPE LPADALVGVS THDHAQVVHA RELGADFAVL GPVAETPSHP DTAGIGWQGF VAGTRDAGLP VLALGGQSAD TLAEARQHGA HGIAGIRALI // ID A9I1R7_BORPD Unreviewed; 227 AA. AC A9I1R7; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Bpet0558; OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=340100; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448; RX PubMed=18826580; DOI=10.1186/1471-2164-9-449; RA Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., RA Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., RA Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., RA Larisch C., Link S., Linke B., Meyer F., Mormann S., Nakunst D., RA Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., RA Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., RA Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.; RT "The missing link: Bordetella petrii is endowed with both the RT metabolic versatility of environmental bacteria and virulence traits RT of pathogenic Bordetellae."; RL BMC Genomics 9:449-449(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM902716; CAP40890.1; -; Genomic_DNA. DR RefSeq; YP_001629161.1; NC_010170.1. DR ProteinModelPortal; A9I1R7; -. DR STRING; 340100.Bpet0558; -. DR EnsemblBacteria; CAP40890; CAP40890; Bpet0558. DR GeneID; 5819313; -. DR KEGG; bpt:Bpet0558; -. DR PATRIC; 21162573; VBIBorPet31633_0566. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPET340100:GJBO-561-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 23247 MW; FA60835D086D0DD2 CRC64; MNASPSAAPL RFPAGLYGVT PEWDDTGRLL DAVRQAAAGG MTALQLRRKN ASPAQRAAQA RALAPLCREL GVVFLINDHW QLALDVGADG AHLGRDDGDL AQARAQAGPG LILGASCYND LTRARGLLEA GADYIAFGAV FPSSTKPQAV RAPLALLGQA RALTADRGAP RPAVVAIGGI TPANAPQVAQ AGADSIAVIT GLFEAPDIRQ AAQACAAPFT ASTHFQP // ID A9IRG7_BART1 Unreviewed; 201 AA. AC A9IRG7; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; OrderedLocusNames=BT_0762; OS Bartonella tribocorum (strain CIP 105476 / IBS 506). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=382640; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 105476 / IBS 506; RX PubMed=18037886; DOI=10.1038/ng.2007.38; RA Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., RA Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.; RT "Genomic analysis of Bartonella identifies type IV secretion systems RT as host adaptability factors."; RL Nat. Genet. 39:1469-1476(2007). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM260525; CAK01179.1; -; Genomic_DNA. DR RefSeq; YP_001609174.1; NC_010161.1. DR ProteinModelPortal; A9IRG7; -. DR STRING; 382640.Btr_0762; -. DR GeneID; 5830009; -. DR KEGG; btr:Btr_0762; -. DR PATRIC; 20549282; VBIBarTri113218_0799. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BTRI382640:GJEK-677-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 23367 MW; F889F52D09B42FF2 CRC64; MKLDPFYLIV DNADWVERLV PLGVKLIQLR MKDEDFQTIS QHIKRAKNIC DHWGAQLIIN DHWRMAIDEK CHFIHLGQED LRNADLHAIR KNNIRFGVST HDEHELDIAL SVHPDYIALG PIYPTILKKM KWQPQGLEKI KQWRKRIGAL PFVGIGGLNP ERAMDVLKAG TNSAAVVTDI ILHKKPEERV KQWLKVTQPW R // ID A9IYL5_BART1 Unreviewed; 220 AA. AC A9IYL5; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE2; OrderedLocusNames=BT_2387; OS Bartonella tribocorum (strain CIP 105476 / IBS 506). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=382640; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 105476 / IBS 506; RX PubMed=18037886; DOI=10.1038/ng.2007.38; RA Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., RA Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.; RT "Genomic analysis of Bartonella identifies type IV secretion systems RT as host adaptability factors."; RL Nat. Genet. 39:1469-1476(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM260525; CAK02385.1; -; Genomic_DNA. DR RefSeq; YP_001610380.1; NC_010161.1. DR ProteinModelPortal; A9IYL5; -. DR STRING; 382640.Btr_2387; -. DR GeneID; 5830211; -. DR KEGG; btr:Btr_2387; -. DR PATRIC; 20552610; VBIBarTri113218_2422. DR eggNOG; COG0352; -. DR HOGENOM; HOG000246417; -. DR KO; K00788; -. DR OMA; FACVILY; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BTRI382640:GJEK-1901-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 220 AA; 24661 MW; 718B9EE25A223142 CRC64; MTQQTNKPIE SPLFPQLVLT LDIRRNTPHS FLRPILQTKS FACVILYDSE KQKDNGSFLQ QQAQIYAEDI QNNDAALLIT DDSRIAGRIK ADGLHIEDDL NALESFKNQQ KEQKILGFGN LRNRHSAMLA AETGVDYLLF GKLGADKKPH AHPRNLQLAA WWAEIMETPA IIQAGSDFAT FDEALKTGCE FVAVEEVILG NDNPLILLKT MQEKCENTPL // ID A9K0P3_BURML Unreviewed; 367 AA. AC A9K0P3; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 39. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=BMA10399_D0419; OS Burkholderia mallei ATCC 10399. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=412021; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10399; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia mallei ATCC 10399."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899680; EDP86141.1; -; Genomic_DNA. DR ProteinModelPortal; A9K0P3; -. DR EnsemblBacteria; EDP86141; EDP86141; BMA10399_D0419. DR PATRIC; 26899761; VBIBurMal41276_0925. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Transferase. SQ SEQUENCE 367 AA; 38315 MW; 3E9B351CCB7F5C2B CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGARAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID A9K731_BURML Unreviewed; 209 AA. AC A9K731; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 16-OCT-2013, entry version 28. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BMA10399_K0151; OS Burkholderia mallei ATCC 10399. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=412021; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10399; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia mallei ATCC 10399."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899685; EDP88252.1; -; Genomic_DNA. DR ProteinModelPortal; A9K731; -. DR EnsemblBacteria; EDP88252; EDP88252; BMA10399_K0151. DR PATRIC; 26905372; VBIBurMal41276_3718. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID A9KGN3_COXBN Unreviewed; 479 AA. AC A9KGN3; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.5.1.3; DE EC=2.7.1.49; DE EC=2.7.4.7; GN Name=thiDE; OrderedLocusNames=CBUD_1745; OS Coxiella burnetii (strain Dugway 5J108-111). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Coxiella. OX NCBI_TaxID=434922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Dugway 5J108-111; RX PubMed=19047403; DOI=10.1128/IAI.01141-08; RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., RA Samuel J.E., Heinzen R.A.; RT "Comparative genomics reveal extensive transposon-mediated genomic RT plasticity and diversity among potential effector proteins within the RT genus Coxiella."; RL Infect. Immun. 77:642-656(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000733; ABS76856.1; -; Genomic_DNA. DR RefSeq; YP_001425078.1; NC_009727.1. DR ProteinModelPortal; A9KGN3; -. DR STRING; 434922.CBUD_1745; -. DR EnsemblBacteria; ABS76856; ABS76856; CBUD_1745. DR GeneID; 5457512; -. DR KEGG; cbd:CBUD_1745; -. DR PATRIC; 17923302; VBICoxBur32972_1739. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CBUR434922:GJTP-1841-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 479 AA; 52724 MW; 2EEF0D59BB1B53AE CRC64; MNQKSIVWSI GGSDCSGGAG CQADILTCRD FNVHAASIIT TITAQNAEQV LKINYCDSDL IQKQIQALKE TLPPTVIKLG LLGTKEIVTA VASYLKNYSG KVVCDPVLNS TSGVLLHASD YLDLLKKLLF PHVDLLTPNI PEAEILIQNK IHTFSDIISA AHQLLKCGVS AVLLKGGHLI GSKARDFFTD GKCEFWLAHT KIPKTRVRGT GCALSSAISS AIALGYSLKD AIVVAKMYVQ QGIRQNFKVN TQELMGRQGF PRRSIDLPWV TKNANFKRKS FPLCNSFGFY PIVDSVEWVE RLLSYGVRTI QLRIKNASPQ KIKKAVIESV ALARHYQAKL FINDYWKLAI EAGAYGVHLG QEDLETADLS AIRAANLRLG ISTHTLYELS RAHAIQPSYV AFGPIYETYS KPMPYSARGL EWLRYWCEIS PYPVVAIGGI NLNRLESVLN AGAVNVAVIS AVTKSKTPQK TVRAFLNRI // ID A9L3J6_SHEB9 Unreviewed; 632 AA. AC A9L3J6; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=Sbal195_2438; OS Shewanella baltica (strain OS195). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=399599; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS195; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Brettar I., Rodrigues J., Konstantinidis K., Klappenbach J., RA Hofle M., Tiedje J., Richardson P.; RT "Complete sequence of chromosome of Shewanella baltica OS195."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000891; ABX49606.1; -; Genomic_DNA. DR RefSeq; YP_001554866.1; NC_009997.1. DR ProteinModelPortal; A9L3J6; -. DR STRING; 399599.Sbal195_2438; -. DR EnsemblBacteria; ABX49606; ABX49606; Sbal195_2438. DR GeneID; 5754197; -. DR KEGG; sbn:Sbal195_2438; -. DR PATRIC; 23471052; VBISheBal33754_2516. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SBAL399599:GH6B-2506-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 632 AA; 66915 MW; 05DCA191EB5A53C6 CRC64; MSTERPAFVW TIAGSDSGGG AGIQADLATI QDLGCHGCSV VTTVTAQSSV AVTLVEPVSA AMLMAQLTTL LSDLPPKAIK IGLLADQTQV ALLADWIASF KIHYPSVPVI VDPVMVASCG DALAVDNCQD IKSAAKSALD FRPFKGLIEL ITPNVLELGR LTHSDVSTKA QFAAAALALS QSLDCSVLAK GGDVSFGSTD ILENTHAKTH DNTYAQTQAN AHNSNGWDLE LAEDYLVCHQ VRASSKLHQN GRFWLASQRV NTRHNHGSGC TLSSAIAAVL AQGFVLQDAV VVAKAYVSQG LSAAIGLGQG PGPLARTGWP NNLSRYAKIN LCDGNFIRHH LNRHLDVRSD LVATVLSATD QATAQVRIAS TPPQNILSHG FKVLDAELGV YPVVSDLTML ESLLAAGVKT VQLRIKTDIS ELTTTTAPAE SDLGKSALGR CESGEPELIG SELEAQIQTA IALGKHFNAQ LFINDHWKLA IKYHAFGVHL GQEDLAVTDL AAIQAAGLAL GISSHSYFEL LLAHQYSPSY IALGHIFPTT TKQMPSAPQG LAKLKHYVAL LQGHYPLVAI GGIDLTNLAK VKATGVGNIA VVRAITKAKE PVAAFAELSQ AWEQCSLCEE LAVKQELDAK HE // ID A9M074_NEIM0 Unreviewed; 205 AA. AC A9M074; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NMCC_0116; OS Neisseria meningitidis serogroup C (strain 053442). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=374833; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=053442; RX PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004; RA Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., RA Xiong Z., Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., RA Shao Z., Liang X., Xu J., Jin Q.; RT "Characterization of ST-4821 complex, a unique Neisseria meningitidis RT clone."; RL Genomics 91:78-87(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000381; ABX72335.1; -; Genomic_DNA. DR RefSeq; YP_001598288.1; NC_010120.1. DR ProteinModelPortal; A9M074; -. DR STRING; 374833.NMCC_0116; -. DR EnsemblBacteria; ABX72335; ABX72335; NMCC_0116. DR GeneID; 5795452; -. DR KEGG; nmn:NMCC_0116; -. DR PATRIC; 20344398; VBINeiMen117761_0133. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NMEN374833:GJ7Z-115-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21576 MW; CDB4500019CCA4E5 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGDELKREIA RCVAACQGSR TQLFINDHWH EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELNRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID A9M7F2_BRUC2 Unreviewed; 203 AA. AC A9M7F2; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BCAN_A0216; OS Brucella canis (strain ATCC 23365 / NCTC 10854). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=483179; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23365 / NCTC 10854; RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., RA Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., RA Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., RA Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., RA Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., RA Munk C., Brettin T.S.; RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000872; ABX61311.1; -; Genomic_DNA. DR RefSeq; YP_001592082.1; NC_010103.1. DR ProteinModelPortal; A9M7F2; -. DR STRING; 483179.BCAN_A0216; -. DR EnsemblBacteria; ABX61311; ABX61311; BCAN_A0216. DR GeneID; 5786022; -. DR KEGG; bcs:BCAN_A0216; -. DR PATRIC; 17829091; VBIBruCan25663_0222. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BCAN483179:GJ7I-215-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID A9M7K5_BRUC2 Unreviewed; 221 AA. AC A9M7K5; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BCAN_A1746; OS Brucella canis (strain ATCC 23365 / NCTC 10854). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=483179; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23365 / NCTC 10854; RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., RA Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., RA Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., RA Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., RA Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., RA Munk C., Brettin T.S.; RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000872; ABX62752.1; -; Genomic_DNA. DR RefSeq; YP_001593523.1; NC_010103.1. DR ProteinModelPortal; A9M7K5; -. DR STRING; 483179.BCAN_A1746; -. DR EnsemblBacteria; ABX62752; ABX62752; BCAN_A1746. DR GeneID; 5785529; -. DR KEGG; bcs:BCAN_A1746; -. DR PATRIC; 17832196; VBIBruCan25663_1736. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BCAN483179:GJ7I-1728-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID A9NB66_COXBR Unreviewed; 479 AA. AC A9NB66; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE SubName: Full=Thiamine-phosphate pyrophosphorylase/thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN Name=thiDE; OrderedLocusNames=COXBURSA331_A0441; OS Coxiella burnetii (strain RSA 331 / Henzerling II). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Coxiella. OX NCBI_TaxID=360115; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 331 / Henzerling II; RA Seshadri R., Samuel J.E.; RT "Genome sequencing of phylogenetically and phenotypically diverse RT Coxiella burnetii isolates."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000890; ABX77564.1; -; Genomic_DNA. DR RefSeq; YP_001596281.1; NC_010117.1. DR ProteinModelPortal; A9NB66; -. DR STRING; 360115.COXBURSA331_A0441; -. DR EnsemblBacteria; ABX77564; ABX77564; COXBURSA331_A0441. DR GeneID; 5793330; -. DR KEGG; cbs:COXBURSA331_A0441; -. DR PATRIC; 17925138; VBICoxBur33747_0463. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CBUR360115:GI0X-446-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 479 AA; 52685 MW; C81AD2BCA1772305 CRC64; MNQKSIVWSI GGSDCSGGAG CQADILTCRD FNVHAASIIT TITAQNAEQV LKINYCDSDL IQKQIQALKE TLPPTVIKLG LLGTKEIVTA VASYLKNYSG KVVCDPVLNS TSGVLLHASD YLDLLKKLLF PHVDLLTPNI PEAEILIQNK IHTFSDIISA AHQLLKCGVS AVLLKGGHLI GSKACDFFTD GKCEFWLAHT KIPKTRVRGT GCALSSAISS AIALGYSLKD AIVVAKMYVQ QGIRQNFKVN TQELMGRQGF PRRSIDLPWV TKNANFKRKS FPLCNSFGFY PIVDSVEWVE RLLSYGIRTI QLRIKNASPQ KIKKAVIESV ALARHYQAKL FINDYWKLAI EAGAYGVHLG QEDLETADLS AIRAANLRLG ISTHTLYELS RAHAIQPSYV AFGPIYETYS KPMPYSARGL EWLRYWCEIS PYPVVAIGGI NLNRLESVLN AGAVNVAVIS AVTKSKTPQK TVRAFLNRI // ID A9PGH5_POPTR Unreviewed; 531 AA. AC A9PGH5; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 16-APR-2014, entry version 37. DE SubName: Full=Putative uncharacterized protein; OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera OS subsp. trichocarpa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Malpighiales; Salicaceae; Saliceae; OC Populus. OX NCBI_TaxID=3694; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Young and mature leaves; RX PubMed=18230180; DOI=10.1186/1471-2164-9-57; RA Ralph S.G., Chun H.J., Cooper D., Kirkpatrick R., Kolosova N., RA Gunter L., Tuskan G.A., Douglas C.J., Holt R.A., Jones S.J., RA Marra M.A., Bohlmann J.; RT "Analysis of 4,664 high-quality sequence-finished poplar full-length RT cDNA clones and their utility for the discovery of genes responding to RT insect feeding."; RL BMC Genomics 9:57-57(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EF147465; ABK95478.1; -; mRNA. DR ProteinModelPortal; A9PGH5; -. DR STRING; 3694.fgenesh4_pm.C_LG_III000008; -. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 531 AA; 55664 MW; 658FE4FBC8EFB7A1 CRC64; MAYGGVILSN SFSFYQKRIV MSSRMQEKNG GASIPHVLSV AGSDSGAGAG IQADLKACAA RGVYCSTVIT SVTAQNTVGV QAVHAVPEDF VAQQLKSVLS DMQVDVVKTG MLPSVGVVKV LLQSLTELSV RALVVDPVMV STSGDVLAGP SILSTFREEL LPIANIVTPN IKEASALLGG IRLETVADMR NAAELLHALG PRNVLVKGGD LPDSLDAVDI FFNGEHFYEL RSSRIKTRNT HGTGCTLASC IAAELAKGSP MLTAVRVAKR YVETALEYSK DILIGNGIQG PFDHLLRLKS GSHSFRRKDA FNPSDLFLYA VTDSGMNKKW GRSVVDAVAA AIQGGATIVQ LRDKDAGTKD FLETAKSCLA VCRSHGVPLL INDRVDVALA SDADGVHVGQ SDMPATVART LLGPEKIIGV SCKTIEQAQQ AWIGGADYIG CGGVYSTNTK ANNPTIGLDG LKTVCSASKL PVVAIGGINA SNAGTVMEMG VPNLKGVAVV SALFDRENVL AETKKLHALL MEASSSSSKI Q // ID A9R8D0_YERPG Unreviewed; 224 AA. AC A9R8D0; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=YpAngola_A0454; OS Yersinia pestis bv. Antiqua (strain Angola). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=349746; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Angola; RX PubMed=20061468; DOI=10.1128/JB.01518-09; RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., RA Mou S., Achtman M., Lindler L.E., Ravel J.; RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola RT reveals new insights into the evolution and pangenome of the plague RT bacterium."; RL J. Bacteriol. 192:1685-1699(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000901; ABX87252.1; -; Genomic_DNA. DR RefSeq; YP_001605059.1; NC_010159.1. DR ProteinModelPortal; A9R8D0; -. DR STRING; 349746.YpAngola_A0454; -. DR EnsemblBacteria; ABX87252; ABX87252; YpAngola_A0454. DR GeneID; 5798918; -. DR KEGG; ypg:YpAngola_A0454; -. DR PATRIC; 18569868; VBIYerPes97331_0755. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; YPES349746:GHPB-454-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID A9T4D5_PHYPA Unreviewed; 510 AA. AC A9T4D5; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE SubName: Full=Predicted protein; GN ORFNames=PHYPADRAFT_140095; OS Physcomitrella patens subsp. patens (Moss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; OC Physcomitrella. OX NCBI_TaxID=3218; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004; RX PubMed=18079367; DOI=10.1126/science.1150646; RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., RA Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T., RA Kuroki Y., Toyoda A., Suzuki Y., Hashimoto S.-I., Yamaguchi K., RA Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N., RA Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H., RA Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K., RA Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A., RA Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T., RA Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.-H., RA Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J., RA Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., RA Boore J.L.; RT "The Physcomitrella genome reveals evolutionary insights into the RT conquest of land by plants."; RL Science 319:64-69(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS545052; EDQ61662.1; -; Genomic_DNA. DR RefSeq; XP_001773462.1; XM_001773410.1. DR UniGene; Ppa.4554; -. DR ProteinModelPortal; A9T4D5; -. DR STRING; 3218.JGI140095; -. DR GeneID; 5936729; -. DR KEGG; ppp:PHYPADRAFT_140095; -. DR KO; K14153; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 510 AA; 53569 MW; B4694B28240D6F7C CRC64; MGTEESRRIP RVLTVAGSDS GAGAGIQADM KACGALGVYC TTAITAVTAQ NTVGVQGIHE VPADFVASQV KSVLLDIGAD VVKTGMLPSV EIIRSLCDIL RTYPVKGLVV DPVLISTSGD ELAGPAILDA LRDDLFPLAD LVTPNLPEAS AIIGGDPVTT VAEMREAAEA IHQLGPRYVL VKGGHLPGTN TLIDVLYDGT TFWHELPGSR IETRNTHGTG CTLASSIAAE LAKGQSMLPA VLASKRYLKD VLEENATLKI GEGKQGPVNH LFKLSDWEKS STQSKFRPES LLLYAVTDSS MNKTWGRSTS EAVRAAIEGG ATIVQIRSKE ADTGEFLQEA ETSLKVARDY GIPLLINDRI DIAIACDADG VHLGQSDLPV ARARAILGPG KIIGVSCKTP EQAEKAWKDG ADYVGSGGVY PTNTKKDNKT IGIEGLREVC YGSPIPVVAI GGISGANAAE VMAYPRPENL KGVAVVSAFF NQPDVKKATA AVKSVVEECL KDVSVPNTSS // ID A9VFL1_BACWK Unreviewed; 208 AA. AC A9VFL1; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 45. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=BcerKBAB4_0645; OS Bacillus weihenstephanensis (strain KBAB4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KBAB4; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., RA Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.H., RA Sanchis V., Nguen-The C., Lereclus D., Richardson P., Wincker P., RA Weissenbach J., Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000903; ABY41907.1; -; Genomic_DNA. DR RefSeq; YP_001643535.1; NC_010184.1. DR ProteinModelPortal; A9VFL1; -. DR STRING; 315730.BcerKBAB4_0645; -. DR EnsemblBacteria; ABY41907; ABY41907; BcerKBAB4_0645. DR GeneID; 5840858; -. DR KEGG; bwe:BcerKBAB4_0645; -. DR PATRIC; 19005796; VBIBacWei55973_1219. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BWEI315730:GHRU-761-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 22882 MW; 8BA57905BDFCA89D CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLGKGFPA SKIVINDRID IAILLNIPRV QLGYRSADVR LVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEIAHMASC LSIPITAIGG ITPENTGDVL ANGVSGIAVM SGIISSSNPY SKAKSYKESI RKWAEKHV // ID A9VWE5_METEP Unreviewed; 241 AA. AC A9VWE5; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mext_4471; OS Methylobacterium extorquens (strain PA1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=419610; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PA1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Marx C., Richardson P.; RT "Complete sequence of Methylobacterium extorquens PA1."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000908; ABY32839.1; -; Genomic_DNA. DR RefSeq; YP_001641910.1; NC_010172.1. DR ProteinModelPortal; A9VWE5; -. DR STRING; 419610.Mext_4471; -. DR EnsemblBacteria; ABY32839; ABY32839; Mext_4471. DR GeneID; 5833636; -. DR KEGG; mex:Mext_4471; -. DR PATRIC; 22539629; VBIMetExt98426_4549. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MEXT419610:GI32-4531-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT METAL 87 87 Magnesium (By similarity). FT METAL 106 106 Magnesium (By similarity). FT BINDING 86 86 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 241 AA; 24484 MW; 66AE0BA761D0F7D0 CRC64; MGSGTGLGLS RPSAGVAVDL RLYGILDVGV LGGDATALAT LAAEAVAGGA TLLQYRDKDL TDARAALARI RAIHAALAGR APLLVNDRVD LALAAGVEGV HLGQSDLHPE DARRLLGPRA IIGLTVKTGA QADELYRLPI DYACIGGVFA TTSKDNPDPP VGLDGLQRIV FRARLARGQS LPLGAIAGID ASNTASVIRA GADGVALIGA LFKGGATEAK ARDLLARVDE ALGQRGSTGM R // ID A9W0B0_METEP Unreviewed; 205 AA. AC A9W0B0; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Mext_0602; OS Methylobacterium extorquens (strain PA1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=419610; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PA1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Marx C., Richardson P.; RT "Complete sequence of Methylobacterium extorquens PA1."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000908; ABY29016.1; -; Genomic_DNA. DR RefSeq; YP_001638087.1; NC_010172.1. DR ProteinModelPortal; A9W0B0; -. DR STRING; 419610.Mext_0602; -. DR EnsemblBacteria; ABY29016; ABY29016; Mext_0602. DR GeneID; 5834996; -. DR KEGG; mex:Mext_0602; -. DR PATRIC; 22531555; VBIMetExt98426_0568. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MEXT419610:GI32-613-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 20407 MW; 391F9617C7D2DD89 CRC64; MTLPPLLVVT DRHGAARPLT ETVRAAVAGG APFVWLRDRD LDRDARRDLA RDLIGLLQPV GGRLVVGGDA DMAAETGAQG VHLPGSAGID GIRAARMALG AAALIGFSAH SVAEIAAAAA AGAGYATLSP IFPTASKPGY GPALGLDSLR AAAAHGLPVF ALGGIDMGNA RACREAGAAG VAVMGGVMRG SDPRDATARF VAALT // ID A9W5A9_METEP Unreviewed; 222 AA. AC A9W5A9; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 41. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Mext_2370; OS Methylobacterium extorquens (strain PA1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=419610; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PA1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Marx C., Richardson P.; RT "Complete sequence of Methylobacterium extorquens PA1."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000908; ABY30765.1; -; Genomic_DNA. DR RefSeq; YP_001639836.1; NC_010172.1. DR ProteinModelPortal; A9W5A9; -. DR STRING; 419610.Mext_2370; -. DR EnsemblBacteria; ABY30765; ABY30765; Mext_2370. DR GeneID; 5831584; -. DR KEGG; mex:Mext_2370; -. DR PATRIC; 22535260; VBIMetExt98426_2386. DR eggNOG; NOG280778; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; MEXT419610:GI32-2413-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 222 AA; 22916 MW; B605FDD992AC601C CRC64; MAESESAALR PRLALLTPYG LGASEAEATA RALDAACAAG DVAAVILRLA ASDERSLVAL VKRLAPPAQE RGAAVLVSVP GFTGDIVSVA ARGGADGVHL DRADEEALRD LRGRLRDGRI LGTGGVLGSR NAAMVAGETG VDYLMVGGLF PDGVAPDAEE VRERAAWWAE IFETPCIAVA TSAEDVATLV LTGSEFVGLE SALWLDDPEG VRAAQAQLDR AR // ID A9WPJ9_RENSM Unreviewed; 55 AA. AC A9WPJ9; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 16-OCT-2013, entry version 33. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=RSal33209_1206; OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 OS / NBRC 15589 / NCIMB 2235). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Renibacterium. OX NCBI_TaxID=288705; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235; RX PubMed=18723615; DOI=10.1128/JB.00721-08; RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., RA Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., RA Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.; RT "Genome sequence of the fish pathogen Renibacterium salmoninarum RT suggests reductive evolution away from an environmental Arthrobacter RT ancestor."; RL J. Bacteriol. 190:6970-6982(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000910; ABY22944.1; -; Genomic_DNA. DR RefSeq; YP_001624358.1; NC_010168.1. DR ProteinModelPortal; A9WPJ9; -. DR STRING; 288705.RSal33209_1206; -. DR EnsemblBacteria; ABY22944; ABY22944; RSal33209_1206. DR GeneID; 5823418; -. DR KEGG; rsa:RSal33209_1206; -. DR PATRIC; 23075653; VBIRenSal21953_1247. DR eggNOG; COG0352; -. DR BioCyc; RSAL288705:GHX1-1206-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 55 AA; 5588 MW; 2EED644A2B7AFDA8 CRC64; MQASKPWFGI GGIDLSNIAE VVAAGAQRVV VVRAITEATD PAAAATALKA ELPQL // ID A9WPK0_RENSM Unreviewed; 159 AA. AC A9WPK0; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 13-NOV-2013, entry version 38. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=RSal33209_1207; OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 OS / NBRC 15589 / NCIMB 2235). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Renibacterium. OX NCBI_TaxID=288705; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235; RX PubMed=18723615; DOI=10.1128/JB.00721-08; RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., RA Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., RA Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.; RT "Genome sequence of the fish pathogen Renibacterium salmoninarum RT suggests reductive evolution away from an environmental Arthrobacter RT ancestor."; RL J. Bacteriol. 190:6970-6982(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000910; ABY22945.1; -; Genomic_DNA. DR RefSeq; YP_001624359.1; NC_010168.1. DR ProteinModelPortal; A9WPK0; -. DR STRING; 288705.RSal33209_1207; -. DR EnsemblBacteria; ABY22945; ABY22945; RSal33209_1207. DR GeneID; 5822462; -. DR KEGG; rsa:RSal33209_1207; -. DR PATRIC; 23075655; VBIRenSal21953_1248. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RSAL288705:GHX1-1207-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 159 AA; 17314 MW; E2109575DEA8D9E4 CRC64; MTNLQTAQLY LCTEAREREG YFEDFLDSAF SGGVDIIQLR DKRLEAAKEL ELLSVLRSVA EQHGKLWAVN DRADIAQLSQ APVFHIGKKD LPVPAMRALL PNVSAGLSSH SPAQASAAAA NPGVDYFCVG PLWANAHETR PSRGGPGPRN PAEPRWAWP // ID A9WWI4_BRUSI Unreviewed; 221 AA. AC A9WWI4; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=BSUIS_B1183; OS Brucella suis (strain ATCC 23445 / NCTC 10510). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=470137; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23445 / NCTC 10510; RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., RA Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., RA Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., RA Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., RA Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., RA Munk C., Brettin T.S.; RT "Brucella suis ATCC 23445 whole genome shotgun sequencing project."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000912; ABY40120.1; -; Genomic_DNA. DR RefSeq; YP_001622942.1; NC_010167.1. DR ProteinModelPortal; A9WWI4; -. DR STRING; 470137.BSUIS_B1183; -. DR EnsemblBacteria; ABY40120; ABY40120; BSUIS_B1183. DR GeneID; 5836579; -. DR KEGG; bmt:BSUIS_B1183; -. DR PATRIC; 17866890; VBIBruSui83806_1253. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BSUI470137:GJIC-3187-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23234 MW; 8D39BD4778442168 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGES QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID A9Z9J8_YERPE Unreviewed; 224 AA. AC A9Z9J8; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YPIP275_1493; OS Yersinia pestis biovar Orientalis str. IP275. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=373665; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IP275; RA Carniel E., Rasko D.A., Kokorina G., Rosovitz M.J., Lindler L., RA Ravel J.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IP275; RA Ravel J., Eppinger M., Fricke W.F., Rosovitz M., Lindler L.E., RA Bearden S., Shriefer M.; RT "Yersinia pestis Strain IP275 project at JCVI/TIGR."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IP275; RA Ravel J., Eppinger M., Fricke W.F., Rosovitz M., Lindler L.E., RA Bearden S., Shriefer M.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IP275; RA Payne S.H., Sutton G.G.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOS02000012; EDR32416.1; -; Genomic_DNA. DR ProteinModelPortal; A9Z9J8; -. DR EnsemblBacteria; EDR32416; EDR32416; YPIP275_1493. DR PATRIC; 31293072; VBIYerPes5378_3010. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID A9ZK38_COXBE Unreviewed; 479 AA. AC A9ZK38; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 39. DE SubName: Full=Thiamine-phosphate pyrophosphorylase/thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN Name=thiDE; ORFNames=COXBURSA334_1745; OS Coxiella burnetii Q321. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Coxiella. OX NCBI_TaxID=360117; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Q321; RA Seshadri R., Samuel J.E.; RT "Genome sequencing of phylogenetically and phenotypically diverse RT Coxiella burnetii isolates."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYJ01000032; EDR35376.1; -; Genomic_DNA. DR ProteinModelPortal; A9ZK38; -. DR EnsemblBacteria; EDR35376; EDR35376; COXBURSA334_1745. DR PATRIC; 27688939; VBICoxBur129292_1488. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 479 AA; 52750 MW; C79A0954C6698BD0 CRC64; MNQKSIVWSI GGSDCSGGAG CQADILTCRD FNVHAASIIT TITAQNAEQV LKINYCDSDL IQKQIQALKE TLPPTVIKLG LLGTKEIVTP VASYLKNYSG KVVCDPVLNS TSGVLLHASD YLDLLKKLLF PHVDLLTPNI PEAEILIQNK IHTFSDIISA AHQLLKCGVS AVLLKGGHLI GSKARDFFTD GKCEFWLAHT KIPKTRVRGT GCALSSAISS AIALGYSLKD AIVVAKMYVQ QGIRQNFKVN TQELMGRQGF PRRSIDLPWV TKNANFKRKS FPLCNSFGFY PIVDSVEWVE RLLSYGVRTI QLRIKNASPQ KIKKAVIESV ALARHYQAKL FINDYWKLAI EAGAYGVHLG QEDLETADLS AIRAANLRLG ISTHTLYELS RAHAIQPSYV AFGPIYETYS KPMPYSARGL EWLRYWCEIS PYPVVAIGGI NLNRLESVLN AGAVNVAVIS AVTKSKTPQK TVRAFLNRI // ID B0A5B5_YERPE Unreviewed; 224 AA. AC B0A5B5; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YpF1991016_0068; OS Yersinia pestis biovar Orientalis str. F1991016. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=404214; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F1991016; RX PubMed=19820101; DOI=10.1128/JB.01227-09; RA Eppinger M., Guo Z., Sebastian Y., Song Y., Lindler L.E., Yang R., RA Ravel J.; RT "Draft genome sequences of Yersinia pestis isolates from natural foci RT of endemic plague in China."; RL J. Bacteriol. 191:7628-7629(2009). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F1991016; RA Payne S.H., Sutton G.G.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAT01000034; EDR37001.1; -; Genomic_DNA. DR ProteinModelPortal; B0A5B5; -. DR EnsemblBacteria; EDR37001; EDR37001; YpF1991016_0068. DR PATRIC; 29646026; VBIYerPes113109_4750. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID B0A675_9FIRM Unreviewed; 218 AA. AC B0A675; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLOBAR_00058; OS Clostridium bartlettii DSM 16795. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=445973; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16795; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16795; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium bartlettii (DSM 16795)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABEZ02000001; EDQ97969.1; -; Genomic_DNA. DR ProteinModelPortal; B0A675; -. DR EnsemblBacteria; EDQ97969; EDQ97969; CLOBAR_00058. DR PATRIC; 25246822; VBICloBar105643_0058. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23506 MW; A30DA8C4D2ED9FA6 CRC64; MKLDNDAIKK SMLLYAITDR GWLKEGETLE SVVEDVLKSG ATFLQLREKI QGHEEIVKTA INLQTLCKKY NVPFVVNDDI MAAKEIDADG VHIGQSDMEY TKAREILGPD KIIGVSAGNL AEAKEAERVG ADYIGVGAVF HTDTKKDATS LTMAQLKEIS EEVSIPVVAI GGISIDNALE LKGTGIDGIC VISAIFGSEN PSEATKKLLD LSKQIISK // ID B0AA82_9FIRM Unreviewed; 208 AA. AC B0AA82; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLOBAR_02037; OS Clostridium bartlettii DSM 16795. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=445973; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16795; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16795; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium bartlettii (DSM 16795)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABEZ02000019; EDQ96270.1; -; Genomic_DNA. DR ProteinModelPortal; B0AA82; -. DR EnsemblBacteria; EDQ96270; EDQ96270; CLOBAR_02037. DR PATRIC; 25250632; VBICloBar105643_1915. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 23194 MW; 34312F087F826256 CRC64; MKENLREDLK MYLISDSDIL KGRDFYKCIE DGLKAGVTML QLREKNADGG EFLEKALKLR ELTKKYNAKF IIDDRIDIAL LCDADGVHVG QSDIDAKSAR KLIGEDKILG VSARTLQEAK RAKEDGADYL GIGAMFSTST KLDAKSVSFE TLKEIKDNVD IPFVLIGGIN LDNVGQLKQF NPDGYAIISA ILKEEDIYAE VKKWLDVI // ID B0AB52_9FIRM Unreviewed; 209 AA. AC B0AB52; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 16-OCT-2013, entry version 29. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=CLOBAR_01602; OS Clostridium bartlettii DSM 16795. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=445973; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16795; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16795; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium bartlettii (DSM 16795)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABEZ02000019; EDQ95835.1; -; Genomic_DNA. DR ProteinModelPortal; B0AB52; -. DR EnsemblBacteria; EDQ95835; EDQ95835; CLOBAR_01602. DR PATRIC; 25249784; VBICloBar105643_1491. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 24122 MW; CDA351C1913CD254 CRC64; MYLISNRHLC SKEKYIKTIV EAAKNNVEYL ILREKDLEYS ELEKLYNEIV LSLKENNTDI NIIVNSSVEL YENYPVYGIH LPYNLFKDLL SKGYEFDRTK KIGLSLHSTS EVIELNKIIE SKNINIDYIT LSHIFETKCK EGLKPRGVEL LKNSRGLTDI KIVALGGILP QNIGEILGYC DDFAVMSTLF KSSDVKETIE DYNKNWNKL // ID B0AR35_BACAN Unreviewed; 219 AA. AC B0AR35; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BAC_0354; OS Bacillus anthracis str. A0488. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=486624; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A0488; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Brettin T.S.; RT "Genome sequence of Bacillus anthracis A0488."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABJC01000008; EDR19019.1; -; Genomic_DNA. DR ProteinModelPortal; B0AR35; -. DR SMR; B0AR35; 1-215. DR EnsemblBacteria; EDR19019; EDR19019; BAC_0354. DR PATRIC; 24643366; VBIBacAnt7575_2651. DR OMA; QFREKGP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23600 MW; 6D85F0FE3EFD3046 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGFI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWVIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID B0AW77_BACAN Unreviewed; 206 AA. AC B0AW77; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 19-MAR-2014, entry version 32. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BAC_0771; OS Bacillus anthracis str. A0488. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=486624; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A0488; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Brettin T.S.; RT "Genome sequence of Bacillus anthracis A0488."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABJC01000027; EDR17348.1; -; Genomic_DNA. DR ProteinModelPortal; B0AW77; -. DR EnsemblBacteria; EDR17348; EDR17348; BAC_0771. DR PATRIC; 24647422; VBIBacAnt7575_4598. DR OMA; ELVNVAM; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID B0CEK8_ACAM1 Unreviewed; 345 AA. AC B0CEK8; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AM1_1957; OS Acaryochloris marina (strain MBIC 11017). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Acaryochloris. OX NCBI_TaxID=329726; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBIC 11017; RX PubMed=18252824; DOI=10.1073/pnas.0709772105; RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., RA Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., RA Mimuro M., Blankenship R.E., Touchman J.W.; RT "Niche adaptation and genome expansion in the chlorophyll d-producing RT cyanobacterium Acaryochloris marina."; RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000828; ABW26974.1; -; Genomic_DNA. DR RefSeq; YP_001516288.1; NC_009925.1. DR ProteinModelPortal; B0CEK8; -. DR STRING; 329726.AM1_1957; -. DR EnsemblBacteria; ABW26974; ABW26974; AM1_1957. DR GeneID; 5680772; -. DR KEGG; amr:AM1_1957; -. DR PATRIC; 20618262; VBIAcaMar40141_1767. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AMAR329726:GCZJ-1948-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 122 Unknown (By similarity). FT REGION 123 345 Thiamine-phosphate synthase (By FT similarity). FT REGION 170 174 HMP-PP binding (By similarity). FT REGION 267 269 THZ-P binding (By similarity). FT METAL 203 203 Magnesium (By similarity). FT METAL 222 222 Magnesium (By similarity). FT BINDING 202 202 HMP-PP (By similarity). FT BINDING 241 241 HMP-PP (By similarity). FT BINDING 270 270 HMP-PP (By similarity). FT BINDING 297 297 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 345 AA; 38523 MW; 0AAB76496A74F267 CRC64; MMNANSTLYR ILDANLDRAR EGLRVIEEWC RFGLEDSQMS AQCKQLRQEL AHWHHPPLRM ARDTPNDPGT QLTHPQEAIR TDLPTVVQAN LCRVQEALRV LEEYSKIYDT QMAAACKQMR YQVYTLDTQL QPRHRLQQLL DAPLYLVTSP SDQLTAVVEA ALKGGLKLVQ YREKQADDDQ RLAVAQTLCR LCHQYNALFI VNDRIDIAVA VDADGVHLGQ QDMTMAVARQ MLGPGKLVGR STTNPQEMER AIQEEADYIG VGPIYETPTK AGKAAVGHEY IRYANQHAPM PYYAIGGINE SNLGEVLAAG AQRVAVVRAI MHAPSPTQAV QQMLKQFPQT SAPAP // ID B0CJ69_BRUSI Unreviewed; 203 AA. AC B0CJ69; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BSUIS_A0213; OS Brucella suis (strain ATCC 23445 / NCTC 10510). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=470137; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23445 / NCTC 10510; RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., RA Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., RA Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., RA Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., RA Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., RA Munk C., Brettin T.S.; RT "Brucella suis ATCC 23445 whole genome shotgun sequencing project."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000911; ABY37313.1; -; Genomic_DNA. DR RefSeq; YP_001626883.1; NC_010169.1. DR ProteinModelPortal; B0CJ69; -. DR STRING; 470137.BSUIS_A0213; -. DR EnsemblBacteria; ABY37313; ABY37313; BSUIS_A0213. DR GeneID; 5839197; -. DR KEGG; bmt:BSUIS_A0213; -. DR PATRIC; 17867902; VBIBruSui83806_1753. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BSUI470137:GJIC-212-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID B0D1A0_LACBS Unreviewed; 534 AA. AC B0D1A0; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 16-APR-2014, entry version 34. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme Thi4; GN ORFNames=LACBIDRAFT_231927; OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured OS deceiver) (Laccaria laccata var. bicolor). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Agaricomycetidae; Agaricales; Tricholomataceae; OC Laccaria. OX NCBI_TaxID=486041; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 / ATCC MYA-4686; RX PubMed=18322534; DOI=10.1038/nature06556; RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F., RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., RA Shapiro H.J., Wuyts J., Blaudez D., Buee M., Brokstein P., RA Canbaeck B., Cohen D., Courty P.E., Coutinho P.M., Delaruelle C., RA Detter J.C., Deveau A., DiFazio S., Duplessis S., RA Fraissinet-Tachet L., Lucic E., Frey-Klett P., Fourrey C., RA Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P., Kilaru S., RA Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R., Melayah D., RA Montanini B., Muratet M., Nehls U., Niculita-Hirzel H., RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M., RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U., RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J., RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A., RA Tuskan G., Grigoriev I.V.; RT "The genome of Laccaria bicolor provides insights into mycorrhizal RT symbiosis."; RL Nature 452:88-92(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS547095; EDR11966.1; -; Genomic_DNA. DR RefSeq; XP_001877863.1; XM_001877828.1. DR ProteinModelPortal; B0D1A0; -. DR STRING; 29883.JGI231927; -. DR GeneID; 6073156; -. DR KEGG; lbc:LACBIDRAFT_231927; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 534 AA; 55951 MW; 3C26077D808D8C7B CRC64; MNDIDYSLYL VTGRELLPPG KDYFESLEES LQGGVTVVQI REKNTDTGEF IKIARASKVI CDIYNVPLLI NDRVDVALAI NAHGVHLGQD DMPIALARKM LPKDAVIGVS CNNVDHVKAA VKDGADYVGI GAVWGTKSKS LTSPIIGVRG VGVMLEVLDG TNVKALAIGG IKSTNLLRTL HGTVSSTGHA LDGIAVISEI VSSTEPRRAT ETLANILSAF RADFPHPPGL DTRLTSDLYV TGDLSPEAVL EGVVQLLETI RGLNPLVHQI TNTVVATQSA NITLALGASP IMATEPREME DLAKISGALL VNIGTLRGES FDGMKKGGFF ANQSRKPIVF DPVGVGASAF RQETVNELLN TWQASVIKGN AGELAALAGT KEVDSKGVDS VGSGFKDPVS FVKALAKRER CVVVLTGATD YISDGLSVVS LKNGDAMLGK ITGSGCVLGS CIAAFCATAA HLASDEEKKG DGKLAKGDMF LGAIAGVLVL TVAAELAVQR EDVKGPGSFL SGLIDTLWAL HSDDVQNLAK VSIE // ID B0G6S7_9FIRM Unreviewed; 214 AA. AC B0G6S7; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DORFOR_02061; OS Dorea formicigenerans ATCC 27755. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea. OX NCBI_TaxID=411461; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27755; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Dorea formicigenerans(ATCC 27755)."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27755; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Wang C., RA Mardis E.R., Wilson R.K.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXA02000014; EDR46838.1; -; Genomic_DNA. DR ProteinModelPortal; B0G6S7; -. DR EnsemblBacteria; EDR46838; EDR46838; DORFOR_02061. DR PATRIC; 26660898; VBIDorFor18168_1886. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22923 MW; 51B417FE69C58C59 CRC64; MKCDKKDLLL YAVTDRSWLN GETLYSQVEK ALEGGATFVQ LREKHLDHDA FLQEAKEIKE LCAKYQVPFV LDDDVELALE VGADGVHVGQ SDMEAGDVRA KLGEDKIVGV SAQTVGQALL AQERGADYLG VGAVFPTSSK DDAVEVDHEM VKAICEAVDI PVIAIGGITK DNVQELSGCG LCGIAVISAI FAKPDIKKAT EELKAATEKM VKAC // ID B0GA24_9FIRM Unreviewed; 218 AA. AC B0GA24; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 16-OCT-2013, entry version 26. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=DORFOR_03140; OS Dorea formicigenerans ATCC 27755. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea. OX NCBI_TaxID=411461; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27755; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Dorea formicigenerans(ATCC 27755)."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27755; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Wang C., RA Mardis E.R., Wilson R.K.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXA02000016; EDR45356.1; -; Genomic_DNA. DR ProteinModelPortal; B0GA24; -. DR EnsemblBacteria; EDR45356; EDR45356; DORFOR_03140. DR PATRIC; 26662848; VBIDorFor18168_2840. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 218 AA; 24454 MW; 53135D47A4A6E5B9 CRC64; MINNSILKKM NNPGRNFQIL AISNRHLCNQ PFEDQIKRVC EWHPDALVLR EKDLPEDEYK TLAKNILDIC KAYDVPCILH TYWKAALELG HDAIHLPLPL LRELSAESQK HLQSQNSTIS QSFHVTDFHK IGTSVHSVED AMEAERLGAT YVTAGHIFTT DCKKGLPPRG LDFLKNVCDA VTIPVYGIGG IKFDPQQWNS LKKQGACGGC IMSGMMQL // ID B0GM38_YERPE Unreviewed; 224 AA. AC B0GM38; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YpUG050454_4063; OS Yersinia pestis biovar Antiqua str. UG05-0454. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=404218; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UG05-0454; RA Ravel J., Eppinger M., Rosovitz M., Lindler L.E., Bearden S., RA Shriefer M.; RT "Yersinia pestis Strain UG05-0454 project at JCVI/TIGR."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UG05-0454; RA Payne S.H., Sutton G.G.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYR01000023; EDR59616.1; -; Genomic_DNA. DR ProteinModelPortal; B0GM38; -. DR EnsemblBacteria; EDR59616; EDR59616; YpUG050454_4063. DR PATRIC; 29625793; VBIYerPes27505_4821. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID B0GZS5_YERPE Unreviewed; 224 AA. AC B0GZS5; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YpMG051020_4811; OS Yersinia pestis biovar Orientalis str. MG05-1020. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=404217; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MG05-1020; RA Ravel J., Eppinger M., Rosovitz M., Lindler L.E., Bearden S., RA Shriefer M.; RT "Yersinia pestis Strain MG05-1020 project at JCVI/TIGR."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MG05-1020; RA Payne S.H., Sutton G.G.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYS01000020; EDR55159.1; -; Genomic_DNA. DR ProteinModelPortal; B0GZS5; -. DR EnsemblBacteria; EDR55159; EDR55159; YpMG051020_4811. DR PATRIC; 31308385; VBIYerPes109917_4966. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID B0HAV4_YERPE Unreviewed; 224 AA. AC B0HAV4; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YpK1973002_1915; OS Yersinia pestis biovar Mediaevalis str. K1973002. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=404216; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K1973002; RX PubMed=19820101; DOI=10.1128/JB.01227-09; RA Eppinger M., Guo Z., Sebastian Y., Song Y., Lindler L.E., Yang R., RA Ravel J.; RT "Draft genome sequences of Yersinia pestis isolates from natural foci RT of endemic plague in China."; RL J. Bacteriol. 191:7628-7629(2009). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K1973002; RA Payne S.H., Sutton G.G.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYT01000024; EDR64014.1; -; Genomic_DNA. DR ProteinModelPortal; B0HAV4; -. DR EnsemblBacteria; EDR64014; EDR64014; YpK1973002_1915. DR PATRIC; 29635252; VBIYerPes37895_4348. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID B0HNE5_YERPE Unreviewed; 224 AA. AC B0HNE5; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YpB42003004_0504; OS Yersinia pestis biovar Antiqua str. B42003004. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=404215; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B42003004; RX PubMed=19820101; DOI=10.1128/JB.01227-09; RA Eppinger M., Guo Z., Sebastian Y., Song Y., Lindler L.E., Yang R., RA Ravel J.; RT "Draft genome sequences of Yersinia pestis isolates from natural foci RT of endemic plague in China."; RL J. Bacteriol. 191:7628-7629(2009). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B42003004; RA Payne S.H., Sutton G.G.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYU01000020; EDR48902.1; -; Genomic_DNA. DR ProteinModelPortal; B0HNE5; -. DR EnsemblBacteria; EDR48902; EDR48902; YpB42003004_0504. DR PATRIC; 29605000; VBIYerPes16979_4617. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID B0I0L3_YERPE Unreviewed; 224 AA. AC B0I0L3; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YpE1979001_2398; OS Yersinia pestis biovar Antiqua str. E1979001. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=360099; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E1979001; RX PubMed=19820101; DOI=10.1128/JB.01227-09; RA Eppinger M., Guo Z., Sebastian Y., Song Y., Lindler L.E., Yang R., RA Ravel J.; RT "Draft genome sequences of Yersinia pestis isolates from natural foci RT of endemic plague in China."; RL J. Bacteriol. 191:7628-7629(2009). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E1979001; RA Payne S.H., Sutton G.G.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYV01000024; EDR41347.1; -; Genomic_DNA. DR ProteinModelPortal; B0I0L3; -. DR EnsemblBacteria; EDR41347; EDR41347; YpE1979001_2398. DR PATRIC; 29615293; VBIYerPes119772_4700. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID B0JSC4_MICAN Unreviewed; 338 AA. AC B0JSC4; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MAE_42600; OS Microcystis aeruginosa (strain NIES-843). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Microcystis. OX NCBI_TaxID=449447; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-843; RX PubMed=18192279; DOI=10.1093/dnares/dsm026; RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M., RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A., RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., RA Katoh M., Nakazaki N., Nakayama S., Yamada M., Tabata S., RA Watanabe M.M.; RT "Complete genomic structure of the bloom-forming toxic cyanobacterium RT Microcystis aeruginosa NIES-843."; RL DNA Res. 14:247-256(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009552; BAG04082.1; -; Genomic_DNA. DR RefSeq; YP_001659274.1; NC_010296.1. DR ProteinModelPortal; B0JSC4; -. DR STRING; 449447.MAE_42600; -. DR PaxDb; B0JSC4; -. DR PRIDE; B0JSC4; -. DR EnsemblBacteria; BAG04082; BAG04082; MAE_42600. DR GeneID; 5865090; -. DR KEGG; mar:MAE_42600; -. DR PATRIC; 22633113; VBIMicAer59304_3867. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MAER449447:GHO8-4294-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 122 Unknown (By similarity). FT REGION 123 338 Thiamine-phosphate synthase (By FT similarity). FT REGION 170 174 HMP-PP binding (By similarity). FT REGION 267 269 THZ-P binding (By similarity). FT METAL 203 203 Magnesium (By similarity). FT METAL 222 222 Magnesium (By similarity). FT BINDING 202 202 HMP-PP (By similarity). FT BINDING 241 241 HMP-PP (By similarity). FT BINDING 270 270 HMP-PP (By similarity). FT BINDING 297 297 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 338 AA; 37947 MW; 4D7D65B988D60965 CRC64; MKLETTAIKR ILDANLDRAR EGLRIIEEWC RFGLDNPDLA QECKEMRHQL ASWHSIDLKR HRDTAGDIGR DLSHPREEIR ETVEGLLQAN LARVQEAFRV LEEYGKLYDL ELGIACKQLR YRVYQLESKL LISPPLEKLQ ASPLYLVTSP AENLLEIVEL ALKGGLKLVQ YRHKTAADTI RLEEAAKLCE LCHRYDALFI MNDRVDIAQA IHADGVHLGQ QDVPISLARQ FLGPTAIIGR STTNPQEMAK AIQEKADYVG VGPVYATPTK AGKTPAGLEY VRYARENCPL PWFAIGGIDS SNIKEVLEAG AQQVAVVRAI MEAQHPDVVT QQLLDQLK // ID B0K3U9_THEPX Unreviewed; 211 AA. AC B0K3U9; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Teth514_0566; OS Thermoanaerobacter sp. (strain X514). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=399726; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X514; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., RA Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., RA Richardson P.; RT "Complete sequence of Thermoanaerobacter sp. X514."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000923; ABY91874.1; -; Genomic_DNA. DR RefSeq; YP_001662210.1; NC_010320.1. DR ProteinModelPortal; B0K3U9; -. DR STRING; 399726.Teth514_0566; -. DR EnsemblBacteria; ABY91874; ABY91874; Teth514_0566. DR GeneID; 5877755; -. DR KEGG; tex:Teth514_0566; -. DR PATRIC; 23890675; VBITheSp86957_0592. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TSP399726:GHCK-584-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23018 MW; 437BD72098B68280 CRC64; MDLTLYAITD RSYIKNMDIA EAVELAIKGG ATVIQLREKD ISSREFYEIA LKVKEVTKRN RIPLIINDRV DIALAVDADG VHVGQEDLPA DIVRKIIGRD KIVGVSARTV EEALKAQRDG ADYLGVGAVF KTPTKPEAEA IGIEGLKKIK EAVTIPVVAI GGITKDNAYE VMLKSGVDGI SSVSAVFYGD IENNTRKLLE VIKKAINDRR I // ID B0KBA8_THEP3 Unreviewed; 211 AA. AC B0KBA8; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Teth39_1655; OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OS (Clostridium thermohydrosulfuricum). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=340099; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33223 / 39E; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., RA Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., RA Zhou J., Richardson P.; RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000924; ABY95296.1; -; Genomic_DNA. DR RefSeq; YP_001665632.1; NC_010321.1. DR ProteinModelPortal; B0KBA8; -. DR STRING; 340099.Teth39_1655; -. DR EnsemblBacteria; ABY95296; ABY95296; Teth39_1655. DR GeneID; 5874685; -. DR KEGG; tpd:Teth39_1655; -. DR PATRIC; 23888055; VBIThePse6203_1729. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TPSE340099:GH4W-1697-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22990 MW; 437BC9C076A68280 CRC64; MDLTLYAITD RSYIKNMDIA EAVELAIKGG ATVIQLREKD ISSREFYEIA LKVKEVTKRN RIPLIINDRV DIALAVDADG VHVGQEDLPA DIVRKIIGRD KIVGVSARTV EEALKAQRDG ADYLGVGAVF KTPTKPEAEA IGIEGLKKIK EAVTIPVVAI GGITKDNAYE VMLKSGADGI SSVSAVFYGD IENNTRKLLE VIKKAINDRR I // ID B0KFR5_PSEPG Unreviewed; 314 AA. AC B0KFR5; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 14-MAY-2014, entry version 52. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=PputGB1_4501; OS Pseudomonas putida (strain GB-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=76869; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.; RT "Complete sequence of Pseudomonas putida GB-1."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000926; ABZ00388.1; -; Genomic_DNA. DR RefSeq; YP_001670723.1; NC_010322.1. DR ProteinModelPortal; B0KFR5; -. DR STRING; 76869.PputGB1_4501; -. DR EnsemblBacteria; ABZ00388; ABZ00388; PputGB1_4501. DR GeneID; 5872308; -. DR KEGG; ppg:PputGB1_4501; -. DR PATRIC; 19936079; VBIPsePut76638_4504. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPUT76869:GIXB-4578-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 34408 MW; 1AA1FFE8E211B911 CRC64; MKRIHVVAAV IRGTDGRILI ARRADTQHQG GLWEFPGGKV EEGEGVEAAL ARELREELGI EVTRSRALIK VSHDYPDKQV LLDVREVEAF TGEPHGAEGQ PLEWVAPRDL PQYEFPEANK PIVAAARLPD QYLITPDGLE VPQMLKGIQR AVANGTRLIQ LRAPDMYDPK YRDVAVDAVG LCAGKAQLML KGPLEWLGDF PSAGWHLTAA QLRKYAAKGR PFPKERWLAA SCHSVEELAL AEQMGVDFVT LSPVQATQTH PEAVPLGWDE AQRLIAGFSK PVYLLGGVGP GEREQAWNAG AQGVAGIRAF WPEI // ID B0MCA8_9FIRM Unreviewed; 206 AA. AC B0MCA8; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ANACAC_01199; OS Anaerostipes caccae DSM 14662. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Anaerostipes. OX NCBI_TaxID=411490; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14662; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Anaerostipes caccae (DSM 14662)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14662; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAX03000012; EDR97578.1; -; Genomic_DNA. DR ProteinModelPortal; B0MCA8; -. DR EnsemblBacteria; EDR97578; EDR97578; ANACAC_01199. DR PATRIC; 24505190; VBIAnaCac18038_1211. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22448 MW; BA4C0476F0FA1397 CRC64; MTLYAVTDSA WTGGQTLMEQ VKDALDGGIT FLQLREKDLE YDAFLQEAIE MAKLSRKYGV PFVINDEVEI ALKCGADGVH VGQEDMACRN ARDILGPDKI IGVSVHNVKE ALKAQADGAD YLGLGAVKAT PTKTDARVVE FEEIKKVCDA VNIPVVAIGG IKKDNMMELK GSHVDGIAVV SAIFGAENIR KETEELRKKA EELRIR // ID B0MIZ3_9FIRM Unreviewed; 192 AA. AC B0MIZ3; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 16-OCT-2013, entry version 25. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=ANACAC_03598; OS Anaerostipes caccae DSM 14662. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Anaerostipes. OX NCBI_TaxID=411490; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14662; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Anaerostipes caccae (DSM 14662)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14662; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAX03000038; EDR95923.1; -; Genomic_DNA. DR ProteinModelPortal; B0MIZ3; -. DR EnsemblBacteria; EDR95923; EDR95923; ANACAC_03598. DR PATRIC; 24509422; VBIAnaCac18038_3302. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 192 AA; 20971 MW; D50C446C5CA6D8F4 CRC64; MNQEWIAVTD RKQCGGEFLK TVQTLAGQGL KTIILREKDL SEEEYGELAA RCMEICRKTG ASLTLHKYFH AARGLGADRI HLPYPVFREN AGKIDQHIHV STSIHAPGEA VEAERMGAEF VIAGHIFQTD CKKGVPPRGL EFLRETVQSV SIPVYAIGGI TPYNIGDVLD TGAAGGCMMS GFMKSPKIID KP // ID B0MSC1_9FIRM Unreviewed; 217 AA. AC B0MSC1; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUBSIR_02761; OS Eubacterium siraeum DSM 15702. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=428128; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15702; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15702; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Eubacterium siraeum (DSM 15702)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCA03000055; EDR99689.1; -; Genomic_DNA. DR ProteinModelPortal; B0MSC1; -. DR EnsemblBacteria; EDR99689; EDR99689; EUBSIR_02761. DR PATRIC; 30678044; VBIEubSir110241_2369. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23170 MW; 7AB826288F8D010D CRC64; MNITPKQMLL YAVSDRAWSN SDEEFLSQAK QAIKSGVTIF QLREKHTSYE HFREIALKLK PICKQYNVPL IINDNVKLAK EIDADGVHLG QDDLDIKAAR EYLGADKIIG VSAHNVKEAL EAENGGADYL GSGAAFVTST KTDAGAIDHK VLSDVAHSVK IPVVAIGGIN KDNISQLEGL GLDGVAVVSA IFAADDISSA VIDLKAKAEK AAESSVK // ID B0MYC4_9BACT Unreviewed; 196 AA. AC B0MYC4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 16-OCT-2013, entry version 27. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=ALIPUT_02029; OS Alistipes putredinis DSM 17216. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes. OX NCBI_TaxID=445970; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17216; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17216; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Alistipes putredinis (DSM 17216)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFK02000020; EDS02502.1; -; Genomic_DNA. DR ProteinModelPortal; B0MYC4; -. DR EnsemblBacteria; EDS02502; EDS02502; ALIPUT_02029. DR PATRIC; 24450890; VBIAliPut4767_0481. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 21753 MW; ABF383F62086D35B CRC64; MMRIIVITDT SFAASEAESI RILLSEGVDR VHLRKPQSAE ADMRRLIEAL PPELYPRLTL QDHLHLAGEY GIGGVHLNAR NPEIPAGFGG LISRSCHSFG EIASHPTEDY LFLSPIFDSI SKTGYRAGYA PDELRKAFAQ GIINPRVAAL GGIRPEHLPA LQEYGFGGAA FLGYIWQGAT PEELVRRMRE IRKFNR // ID B0MYC6_9BACT Unreviewed; 208 AA. AC B0MYC6; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ALIPUT_02031; OS Alistipes putredinis DSM 17216. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes. OX NCBI_TaxID=445970; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17216; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17216; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Alistipes putredinis (DSM 17216)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFK02000020; EDS02504.1; -; Genomic_DNA. DR ProteinModelPortal; B0MYC6; -. DR EnsemblBacteria; EDS02504; EDS02504; ALIPUT_02031. DR PATRIC; 24450894; VBIAliPut4767_0483. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 30 34 HMP-PP binding (By similarity). FT REGION 127 129 THZ-P binding (By similarity). FT METAL 63 63 Magnesium (By similarity). FT METAL 82 82 Magnesium (By similarity). FT BINDING 62 62 HMP-PP (By similarity). FT BINDING 101 101 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22859 MW; B8E9CE7527FF08DD CRC64; MLQFITHHTD RYDEIAGTRA VLEGGCRWVQ LRMKDTPAEE VLRIGREIEK LCREYGAKFI LDDHVELVRE LNADGVHLGK LDMPVAEARR LLGPEYLIGA TANTFEDIER GAGQGADYIG LGPFRFTQTK RNLSPVLGLE GYRTIMECCR NAGIALPVVA IGGITAADVE NILATGVTGI ALSGALLQAE NTLEETQRII NIINRTKQ // ID B0N2F4_9FIRM Unreviewed; 206 AA. AC B0N2F4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLORAM_00790; OS Clostridium ramosum DSM 1402. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=445974; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1402; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium ramosum(DSM 1402)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1402; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFX02000003; EDS19914.1; -; Genomic_DNA. DR ProteinModelPortal; B0N2F4; -. DR EnsemblBacteria; EDS19914; EDS19914; CLORAM_00790. DR PATRIC; 27220520; VBICloRam24443_0764. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22313 MW; C0B809C8F5673F8B CRC64; MLELYLVSDR SWLNDRPLEE DIEQAILGGV TMVQLREKNL TDEEFTIQAK KVKTICSKYH IPFIINDNVA VALAVDSDGI HIGQDDQPVK RVRKIIGPHK IIGVSAHNLK EALAAKEDGA DYLGVGAMFN TSTKDDATAV SFTQLHEITT KIGLPVVAIG GINQDNCLLL KGTKIDGIAV VSAIMSAPDI KEAAAKLKAH ARGIYD // ID B0NHJ9_CLOSV Unreviewed; 208 AA. AC B0NHJ9; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 11-DEC-2013, entry version 25. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=CLOSCI_02954; OS Clostridium scindens ATCC 35704. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411468; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35704; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium scindens(ATCC 35704)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35704; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFY02000043; EDS05931.1; -; Genomic_DNA. DR ProteinModelPortal; B0NHJ9; -. DR EnsemblBacteria; EDS05931; EDS05931; CLOSCI_02954. DR PATRIC; 27225726; VBICloSci136883_0232. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 208 AA; 22834 MW; A9AD7B382DCC795F CRC64; MCRPGVEEGQ KGMGILGNSE DFYSRVIAVT NRHLCAGPYL EQIERICRRQ PGAVIVREKD MGPEDYELLY RQVREICQTY GVPCIAHTYA KAALHVGSRA IHVPLHLLKE TPKIRGQFDI IGVSIHGKEE ALLAERLGAS YLTAGHIFAT DCKKGVAPRG VEFLENVCEA VCLPVYAIGG MKGEIGCVEE MMAHGARGIC VMSECMGW // ID B0NKE1_CLOSV Unreviewed; 213 AA. AC B0NKE1; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLOSCI_03983; OS Clostridium scindens ATCC 35704. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411468; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35704; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium scindens(ATCC 35704)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35704; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFY02000068; EDS04845.1; -; Genomic_DNA. DR ProteinModelPortal; B0NKE1; -. DR EnsemblBacteria; EDS04845; EDS04845; CLOSCI_03983. DR PATRIC; 27226874; VBICloSci136883_0757. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23026 MW; D2C65B4F08DF61DD CRC64; MKCDKKDLLL YAVTDRHWLN GRTLYSQVEE ALKGGATFIQ LREKELDEEH FLEEAKEIKE LCRRYQVPFV INDNVEIALA VDADGVHVGQ SDMEAGDVRA KLGPDKIIGV SAQTVEQAVM AEQNGADYLG VGAVFPTGSK ADALEVSHDT LKAICKAVKI PVIAIGGISK ENILELSGSG ICGIAVISAI FAKDDIEEAA RELRGLTEKM VTA // ID B0NPI5_BACSE Unreviewed; 197 AA. AC B0NPI5; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 16-OCT-2013, entry version 26. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BACSTE_01370; OS Bacteroides stercoris ATCC 43183. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=449673; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43183; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides stercoris(ATCC 43183)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43183; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFZ02000018; EDS15924.1; -; Genomic_DNA. DR ProteinModelPortal; B0NPI5; -. DR EnsemblBacteria; EDS15924; EDS15924; BACSTE_01370. DR PATRIC; 27168593; VBIBacSte95829_1187. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 197 AA; 21650 MW; 0F21FB4410E5EA0E CRC64; MKLITITQPA FFEGEAEAIT SLFDAGLEIL HLRKPSASYE DMEQLLNRLP PEYLKRIVTH EHFQLASFRN LKGIHLNGRN PTAPAGFTGH ISRSCHSLEE VAKYKATCDY VFLSPIYDSI SKEGYSSAYT TGSLQKARQA GIIDAKVMAL GGVTAAHFPE ISSLGFGGAV LLGDIWKRTG TDFIGHFKEL LRAASLF // ID B0NPJ0_BACSE Unreviewed; 217 AA. AC B0NPJ0; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACSTE_01375; OS Bacteroides stercoris ATCC 43183. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=449673; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43183; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides stercoris(ATCC 43183)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43183; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFZ02000018; EDS15929.1; -; Genomic_DNA. DR ProteinModelPortal; B0NPJ0; -. DR EnsemblBacteria; EDS15929; EDS15929; BACSTE_01375. DR PATRIC; 27168603; VBIBacSte95829_1192. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 24280 MW; 214E26562FD158E2 CRC64; MEKVQFITHY TERYSYLDSA RMALEGGCRW IQLRMKDAAE NEILPVAAEV RKLCNDYGAI FIIDDHVELV KEIRADGVHL GKNDMPVAEA RRILGEEYII GGTANTYEDV KKHWLDGVNY IGCGPFRYTT TKQKLSPILG LEGYKEIIRQ MRADNINLPI IAIGGITFAD IPSVMQTGVT GIALSGTVLR ADNPVEEMQR ILTETNQAGK INQTANY // ID B0NWV4_9CLOT Unreviewed; 185 AA. AC B0NWV4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 16-OCT-2013, entry version 26. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=CLOSS21_00147; OS Clostridium sp. SS2/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411484; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS2/1; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS2/1; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium sp. SS2/1."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGC03000008; EDS23213.1; -; Genomic_DNA. DR ProteinModelPortal; B0NWV4; -. DR EnsemblBacteria; EDS23213; EDS23213; CLOSS21_00147. DR PATRIC; 27254217; VBICloSp52530_0735. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 185 AA; 20647 MW; 1D5C6D2212CD670D CRC64; MNKPCFIAVT NRNLCKRPFF DVIEDLSKKD VKTIVLREKD LSEEEYYEIA EKCKEICDRN GASLTIHNFI DVARRLGIKK IHLPYPVFLK EAGNLSDFES VSTSIHKPEE AIKAQKLGVD FVFAGHVFVT DCKKGLPPRG LEFLTDVVNA VKIPVYGIGG INEENITKIM ECGAAGGCMM SGFMK // ID B0P1V8_9CLOT Unreviewed; 223 AA. AC B0P1V8; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLOSS21_01932; OS Clostridium sp. SS2/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411484; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS2/1; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS2/1; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium sp. SS2/1."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGC03000034; EDS21967.1; -; Genomic_DNA. DR ProteinModelPortal; B0P1V8; -. DR EnsemblBacteria; EDS21967; EDS21967; CLOSS21_01932. DR PATRIC; 27253911; VBICloSp52530_0588. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24481 MW; 2DFEAAB7FCF49305 CRC64; MQNGWKGAVK LRVNADAMTL YAVTDRTWVK DTTLMDQVKE ALEGGITFLQ LREKHLSKEE FIKEAREMKE LSKEYKVPFV INDNIEVALA VDADGVHIGQ DDMSVEEARK LLGEDKIIGV SAHNVEEAIK AQKGGADYLG VGAVCATSTK KDANVVSKEE IKKICHTVEI PVVAIGGIKK ENIKTLEGTD VDGVAVVSAI FAAKDIKKDT KQLRSLVEEM KQK // ID B0PAB3_9FIRM Unreviewed; 206 AA. AC B0PAB3; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ANACOL_01682; OS Anaerotruncus colihominis DSM 17241. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Anaerotruncus. OX NCBI_TaxID=445972; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17241; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Anaerotruncus colihominis(DSM 17241)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17241; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGD02000012; EDS11791.1; -; Genomic_DNA. DR ProteinModelPortal; B0PAB3; -. DR EnsemblBacteria; EDS11791; EDS11791; ANACOL_01682. DR PATRIC; 24513648; VBIAnaCol135235_1815. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21955 MW; 0ABCB12875D0EB2B CRC64; MLLYAVTDRA WLRGRALPAL VEDAVRGGAT FVQLREKEME FAAFLDEARR IKAVTDRYHV PFVINDDIEV ARACNADGVH IGQDDAAVSE ARRILGPDKI IGVSAHTVDE ARAAEQAGAD YLGVGAVFST STKLDADIVT LQTLRGIRAA VSIPIVAIGG INVENMLQLK GSGIDGAAVV SALFAQQDVY AAAKRLYATS KELVFG // ID B0Q849_BACAN Unreviewed; 219 AA. AC B0Q849; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BAQ_0413; OS Bacillus anthracis str. A0193. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=486619; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A0193; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Brettin T.S.; RT "Genome sequence of Bacillus anthracis A0193."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABKF01000028; EDR86189.1; -; Genomic_DNA. DR ProteinModelPortal; B0Q849; -. DR SMR; B0Q849; 1-215. DR EnsemblBacteria; EDR86189; EDR86189; BAQ_0413. DR PATRIC; 24598984; VBIBacAnt78565_4671. DR OMA; QFREKGP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23600 MW; 6D85F0FE3EFD3046 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGFI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWVIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID B0Q8A8_BACAN Unreviewed; 194 AA. AC B0Q8A8; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 19-MAR-2014, entry version 26. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BAQ_0798; OS Bacillus anthracis str. A0193. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=486619; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A0193; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Brettin T.S.; RT "Genome sequence of Bacillus anthracis A0193."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABKF01000029; EDR86107.1; -; Genomic_DNA. DR ProteinModelPortal; B0Q8A8; -. DR EnsemblBacteria; EDR86107; EDR86107; BAQ_0798. DR PATRIC; 24599222; VBIBacAnt78565_4789. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 21530 MW; 490CE1E379F83B38 CRC64; MSFEELVSVA MQIESEIDYL HIREREKSTK ELYEGVESLL KKGFPASKLV INDRIDIAIL LNIPRVQLGY RSTDVRSVKE KFSYLHVGYS VHSLEEAIEA FKNGADSLVY GHVFPTECKK GVPARGLEEI SDIARSLSIP IIAIGGITPE NTKDILASEV SGIAVMSGIV SSSNPYSKAK SYKESIRKWA EKHV // ID B0QK36_BACAN Unreviewed; 219 AA. AC B0QK36; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BAH_0405; OS Bacillus anthracis str. A0442. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=486621; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A0442; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Brettin T.S.; RT "Genome sequence of Bacillus anthracis A0442."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABKG01000009; EDR92539.1; -; Genomic_DNA. DR ProteinModelPortal; B0QK36; -. DR SMR; B0QK36; 1-215. DR EnsemblBacteria; EDR92539; EDR92539; BAH_0405. DR PATRIC; 24620968; VBIBacAnt67835_3549. DR OMA; QFREKGP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23600 MW; 6D85F0FE3EFD3046 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGFI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWVIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID B0QNH7_BACAN Unreviewed; 206 AA. AC B0QNH7; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 19-MAR-2014, entry version 31. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BAH_0799; OS Bacillus anthracis str. A0442. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=486621; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A0442; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Brettin T.S.; RT "Genome sequence of Bacillus anthracis A0442."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABKG01000021; EDR91423.1; -; Genomic_DNA. DR ProteinModelPortal; B0QNH7; -. DR EnsemblBacteria; EDR91423; EDR91423; BAH_0799. DR PATRIC; 24623510; VBIBacAnt67835_4777. DR OMA; ELVNVAM; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID B0RGG3_CLAMS Unreviewed; 752 AA. AC B0RGG3; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 45. DE SubName: Full=Multifunctional protein thied [includes: thiamine-phosphate pyrophosphorylase (Tmp pyrophosphorylase) (Tmp-ppase) (Thiamine-phosphate synthase) phosphomethylpyrimidine kinase (Hmp-phosphate kinase) (Hmp-p kinase)]; DE EC=2.7.4.7; GN Name=thiED; OrderedLocusNames=CMS1102; OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM OS 20744 / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Microbacteriaceae; Clavibacter. OX NCBI_TaxID=31964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1; RX PubMed=18192393; DOI=10.1128/JB.01598-07; RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J., RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D., RA Parkhill J., Ishimaru C.A.; RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis RT subsp. sepedonicus suggests recent niche adaptation."; RL J. Bacteriol. 190:2150-2160(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM849034; CAQ01220.1; -; Genomic_DNA. DR RefSeq; YP_001709846.1; NC_010407.1. DR ProteinModelPortal; B0RGG3; -. DR STRING; 31964.CMS_1102; -. DR EnsemblBacteria; CAQ01220; CAQ01220; CMS1102. DR GeneID; 6156997; -. DR KEGG; cms:CMS_1102; -. DR PATRIC; 21459210; VBIClaMic4666_1166. DR eggNOG; COG0351; -. DR KO; K14153; -. DR OMA; RHELEFF; -. DR BioCyc; CMIC31964:GJBN-1113-MONOMER; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.910.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF03070; TENA_THI-4; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; SSF48613; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 752 AA; 76778 MW; DFE15937E5528F4F CRC64; MIGLDLSVYL VTDPALCGAR GVPAVVAAAV AGGATAVQIR DKHASAAELL ATVVAAADAI DAHASAHPTA PRPLLLVDDR VDVVLAALAR GARVDGVHVG QSDVPADLVR RMLDAASPDR RLVVGLTANT PAHVEALRAL PAGTVDYLGV GVIRPTSTKP DHPAPLGHDG FGIIAGLSPV PCVAIGGVDV RDVDAIAAAG GAGTAVVSAI CAAEDPEAAA RELAEARARA RARPATTGDA TDDPAEVVAS SEDHAPPLRP VPRVLSIAGT DPTGGAGIQA DLKSIAANGG YGMAVVTALV AQNTTGVREI HVPPVAFLRA QLDAVSDDVA IDAVKIGMLG SAAVVDEVAA WLGAVRPPVV VLDPVMVAQS GDALLDADAT EALRRLLPLA DVVTPNLPEL AALLGEREAD GWEAALAQGR TLATRHGVRV VVKGGHLRVD DCPDALVTPG AGGAGPTAHV VDGPRIATTS THGTGCSLSS ALATLQPRRD DWRAALTEAK AWLTGSLAHA EDLGVGSGAG PLDHLRALWD AAGTHAGPIS AEMWAGSAGL RREIDDLPFV RRLGDGTLPE AWFSHYLAQD AIYLRAYSRV LARASQLAPA PDAQVVWARS AADAIAAESA LHEEWLSRHP APAVAGPVTR AYVDHLLAHA ATSDYAVLVA ALLPCFTIYA DVGTRLRAAG SEAAAAGVAH PYAAWLATYA DPAFAEATRR ASELVDEAAV LAGPTRRAAM LEASLLSSAY ERDFFHAPEA LG // ID B0RP77_XANCB Unreviewed; 235 AA. AC B0RP77; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=xcc-b100_0915; OS Xanthomonas campestris pv. campestris (strain B100). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=509169; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B100; RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013; RA Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., RA Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., RA Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., RA Niehaus K., Puehler A.; RT "The genome of Xanthomonas campestris pv. campestris B100 and its use RT for the reconstruction of metabolic pathways involved in xanthan RT biosynthesis."; RL J. Biotechnol. 134:33-45(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM920689; CAP50262.1; -; Genomic_DNA. DR RefSeq; YP_001902320.1; NC_010688.1. DR ProteinModelPortal; B0RP77; -. DR STRING; 509169.xccb100_0915; -. DR EnsemblBacteria; CAP50262; CAP50262; xcc-b100_0915. DR GeneID; 6321281; -. DR KEGG; xca:xccb100_0915; -. DR PATRIC; 24081677; VBIXanCam108527_0949. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XCAM509169:GHW4-937-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 66 70 HMP-PP binding (By similarity). FT REGION 164 166 THZ-P binding (By similarity). FT REGION 213 214 THZ-P binding (By similarity). FT METAL 99 99 Magnesium (By similarity). FT METAL 118 118 Magnesium (By similarity). FT BINDING 98 98 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 167 167 HMP-PP (By similarity). FT BINDING 193 193 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 235 AA; 24056 MW; BC6BF2BC713CA3B1 CRC64; MSRSSDNRGH ATVGLHCPIP PTAFGSAAMP TLQNARGVYL ITPDTRDTAQ LLACTLPLLP HITWLQYRNK QADAALRLAQ ATALRAACTA HGVPLIINDD AALAQQVGAD GVHLGEDDGE VAAARALLGA SAIIGVSCYD EIERARAAAA AGANYVAFGA FFPTATKVTT RRATPALLHE AAALGLPRVA IGGITPSQVP ELVTAGADLI AVVSGVYAAA DPVAAVQAYR AGFTQ // ID B0RV93_XANCB Unreviewed; 315 AA. AC B0RV93; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE SubName: Full=Putative NUDIX hydrolase family / thiamine monophosphate synthase fusionprotein; GN OrderedLocusNames=xcc-b100_3619; OS Xanthomonas campestris pv. campestris (strain B100). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=509169; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B100; RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013; RA Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., RA Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., RA Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., RA Niehaus K., Puehler A.; RT "The genome of Xanthomonas campestris pv. campestris B100 and its use RT for the reconstruction of metabolic pathways involved in xanthan RT biosynthesis."; RL J. Biotechnol. 134:33-45(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM920689; CAP52984.1; -; Genomic_DNA. DR RefSeq; YP_001905024.1; NC_010688.1. DR ProteinModelPortal; B0RV93; -. DR STRING; 509169.xccb100_3619; -. DR EnsemblBacteria; CAP52984; CAP52984; xcc-b100_3619. DR GeneID; 6323492; -. DR KEGG; xca:xccb100_3619; -. DR PATRIC; 24087180; VBIXanCam108527_3651. DR eggNOG; COG0494; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XCAM509169:GHW4-3702-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34564 MW; 0B822728BB7C050D CRC64; MPDSLRSIHV VAGVITDARG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIDAHVGA WVMDVPQLYP DKRLRLEVRE ITGWKGSPRG REGQAMTWVA ADKLARYSMP PADLPVVGVL RQPDRYLITP EPQNDAAWLD GVEQALQQEI ARIQLRAPAV DPARWRALVH QVMGLRGRQR AQWLLNRDIG LASELGIGVH LGSEQLATLT ERPLPADQPV AASCHGLEDL RHAQRLGCDF AVLGPVQATA SHPGATPLGW EGFETLREQV SLPIYALGGM QPGDVREARA HGAQGIAAIR GLWPA // ID B0S022_FINM2 Unreviewed; 212 AA. AC B0S022; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=FMG_0203; OS Finegoldia magna (strain ATCC 29328) (Peptostreptococcus magnus). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Finegoldia. OX NCBI_TaxID=334413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29328; RX PubMed=18263572; DOI=10.1093/dnares/dsm030; RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K., RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.; RT "Complete genome sequence of Finegoldia magna, an anaerobic RT opportunistic pathogen."; RL DNA Res. 15:39-47(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008971; BAG07621.1; -; Genomic_DNA. DR RefSeq; YP_001691511.1; NC_010376.1. DR ProteinModelPortal; B0S022; -. DR STRING; 334413.FMG_0203; -. DR EnsemblBacteria; BAG07621; BAG07621; FMG_0203. DR GeneID; 6019277; -. DR KEGG; fma:FMG_0203; -. DR PATRIC; 21886007; VBIFinMag33027_0404. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IGISCHT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; FMAG334413:GJ6M-220-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23450 MW; A058DC1CBB391E33 CRC64; MNKQFNLGLN LVTNKQTLKG RDLTETIEIA LKNGADSVRL REKNMDTRSI MQEAFKIKEI TQRMGKLLIV NDRVDIAKAC DVDGVHLGQK DMPIKYAREM LGDDKIIGIS CHTLEQALEA QEAGADYIGV GAIFPTFTGD DFLMVTIDTL KEISEKIHVP ITAIGGINKN NIRMIFDSNV DSVSLTSAVF STGDVAASTQ ELKQKFDMIL KK // ID B0S0L7_FINM2 Unreviewed; 214 AA. AC B0S0L7; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=FMG_0378; OS Finegoldia magna (strain ATCC 29328) (Peptostreptococcus magnus). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Finegoldia. OX NCBI_TaxID=334413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29328; RX PubMed=18263572; DOI=10.1093/dnares/dsm030; RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K., RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.; RT "Complete genome sequence of Finegoldia magna, an anaerobic RT opportunistic pathogen."; RL DNA Res. 15:39-47(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008971; BAG07796.1; -; Genomic_DNA. DR RefSeq; YP_001691686.1; NC_010376.1. DR ProteinModelPortal; B0S0L7; -. DR STRING; 334413.FMG_0378; -. DR EnsemblBacteria; BAG07796; BAG07796; FMG_0378. DR GeneID; 6019180; -. DR KEGG; fma:FMG_0378; -. DR PATRIC; 21886367; VBIFinMag33027_0583. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; FMAG334413:GJ6M-396-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23758 MW; BB3315CEAB2D90EB CRC64; MRKKLNLSLY LVTDRTNVAC EEKFLTKIEE SLKGGVTLVQ LREKNISTRE YIDLAKKVKI ICDKFDVPLL IDDRIDVCLA SECAGVHLGD EDMEIKDARK ILGDNYIIGA TAKSVERAVQ CEKEGADYLG VGAIYPTKTH VKTKITSVDT LRDINNSINI KTVAIGGLNE DNMDVLKNSG ASGIAVVRAL MNDDNPQEKA HRLLEKSKQI LELR // ID B0T6F0_CAUSK Unreviewed; 201 AA. AC B0T6F0; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 39. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Caul_5033; OS Caulobacter sp. (strain K31). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=366602; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K31; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., RA Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Stephens C., Richardson P.; RT "Complete sequence of chromosome of Caulobacter sp. K31."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000927; ABZ74153.1; -; Genomic_DNA. DR RefSeq; YP_001686651.1; NC_010338.1. DR ProteinModelPortal; B0T6F0; -. DR STRING; 366602.Caul_5033; -. DR EnsemblBacteria; ABZ74153; ABZ74153; Caul_5033. DR GeneID; 5902495; -. DR KEGG; cak:Caul_5033; -. DR PATRIC; 21323264; VBICauSp18104_5453. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ACHSERA; -. DR OrthoDB; EOG699751; -. DR BioCyc; CSP366602:GH0Y-5087-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 20888 MW; F195E277EDA754AE CRC64; MEALSRTAAR FRPWLVRGKP LPNLLFFTDP ERTLHPERVA ERLPAGAAVV FRAFGAPDAA ARGARLREIT RRRGLLLLVG ADENLARQVE ADGLHLPERM SAALPLLRAA HPDWLITLAA HGEAAGGIAA AAAGADALVV SPIFPSRSPS AGAPLGVEGL KRIVEAVKAP VYALGGVRAD TVESLAATGI VGIAAVEALN A // ID B0TD40_HELMI Unreviewed; 454 AA. AC B0TD40; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HM1_0113; OS Heliobacterium modesticaldum (strain ATCC 51547 / Ice1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Heliobacteriaceae; OC Heliobacterium. OX NCBI_TaxID=498761; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51547 / Ice1; RX PubMed=18441057; DOI=10.1128/JB.00299-08; RA Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M., RA Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E., RA Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., RA Wang Z.T., Raymond J., Chen M., Blankenship R.E., Touchman J.W.; RT "The genome of Heliobacterium modesticaldum, a phototrophic RT representative of the Firmicutes containing the simplest RT photosynthetic apparatus."; RL J. Bacteriol. 190:4687-4696(2008). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000930; ABZ82738.1; -; Genomic_DNA. DR RefSeq; YP_001678749.1; NC_010337.2. DR ProteinModelPortal; B0TD40; -. DR STRING; 498761.HM1_0113; -. DR EnsemblBacteria; ABZ82738; ABZ82738; HM1_0113. DR GeneID; 5909286; -. DR KEGG; hmo:HM1_0113; -. DR PATRIC; 22104549; VBIHelMod36755_0093. DR eggNOG; COG0352; -. DR OMA; ENITPAF; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HMOD498761:GI46-113-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 2. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 454 AA; 46221 MW; 4B8A5804395F61FD CRC64; MLVTHRRLCP SDKSLLDVIA GAIEGGIGAV ILREKDLTGR ELLDLAQSVL ALTRPAGVPL IVNGNPAVAI AAGADGVHLG AEDLPPSKVR SIIGPGMLLG RSIHSSEEAQ ALAESGDGAV LDYFLFGNVF ETACKPGKAA VGLDVLSQIV RRSPVPVIAI GGITADKVPL IGRSGAAGVA IMSAIMTAAD PVAAARAITV PAAKAVAGVT EAGEDAGILY GIIGREQASD AATLAAMADG AYAGGCDIIQ LREKNMPTGE FLRRAQILRE KASRWGKLFI VNDRIDIAIA AGADGVHLGA EDLPPEIARQ MWPKGIIGVT VRNLAQAQAA VAAGADYVGA GPVFPTTSKR LDAPPLGFAG LQAICDAIDI PVVAIGGLNA GTMNGIRKTG CSGVSVISAL FQLRDAKGHP DRGAAAPCRL TALQEEGTSD GPGAPADFVR AAVEEAARRL KAQL // ID B0TRP8_SHEHH Unreviewed; 537 AA. AC B0TRP8; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Shal_1901; OS Shewanella halifaxensis (strain HAW-EB4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=458817; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAW-EB4; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella halifaxensis HAW-EB4."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000931; ABZ76466.1; -; Genomic_DNA. DR RefSeq; YP_001674125.1; NC_010334.1. DR ProteinModelPortal; B0TRP8; -. DR STRING; 458817.Shal_1901; -. DR EnsemblBacteria; ABZ76466; ABZ76466; Shal_1901. DR GeneID; 5904655; -. DR KEGG; shl:Shal_1901; -. DR PATRIC; 23506495; VBISheHal24697_1995. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SHAL458817:GH1X-1963-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 537 AA; 57052 MW; 08F76A2157CE22D2 CRC64; MTSARQVLPA VRPIVWTIAG SDSGGGAGIQ ADLATMSDLD THACSVISAV TAQSSVTVSL VEAVSAQMLS SQLNTLVTDL PPDAIKIGLL ADQRQIALLA LWLRDQQDIW LKAGVKVPVI LDPVMVATCG DALANGGALD FTPFKGLLTL ITPNVSELEV LAGHCLDDVG ACITAAKKLA DVLATSVLAK GGDRGPSWCQ HQANDLLVCR DVNGISAKHQ WQSFWLSSIR EASGNNHGTG CTLSSAIAAV MAHGFVLNDA VVVAKAYVSA GLRGSYQPGK GAGCLARTAW PRELSLFPYI KQVTQQDPLP AALINNALSR TGKLKGFKKI DEALGLYPVV ADVALLEMLL KAGAKTLQLR IKDTKEQALK EQSLEQQIIQ AIALGRDYQA RVFINDHWQL AIKHQAYGVH LGQEDLIESN LKQLDDADIA LGLSSHSYFE ILLAKQHNPS YIAFGHIFPT TTKVMPSKPQ GLAKLARYVS LMKGELPIVA IGGIDASRLA SVKATGVDDI AVVRAVTESD DPAAAFKALA QAWLEES // ID B0TY65_FRAP2 Unreviewed; 485 AA. AC B0TY65; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 13-NOV-2013, entry version 40. DE SubName: Full=Thiamine-phosphate pyrophosphorylase/thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Fphi_0087; OS Francisella philomiragia subsp. philomiragia (strain ATCC 25017). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=484022; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25017; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Richardson P.; RT "Complete sequence of chromosome of Francisella philomiragia subsp. RT philomiragia ATCC 25017."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000937; ABZ86307.1; -; Genomic_DNA. DR RefSeq; YP_001676808.1; NC_010336.1. DR ProteinModelPortal; B0TY65; -. DR STRING; 484022.Fphi_0087; -. DR EnsemblBacteria; ABZ86307; ABZ86307; Fphi_0087. DR GeneID; 5908691; -. DR KEGG; fph:Fphi_0087; -. DR PATRIC; 17936955; VBIFraPhi43880_0090. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; FPHI484022:GHVB-83-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 485 AA; 53930 MW; B7FF4A15990970DB CRC64; MRDIFLTIGG SDSSSGAGIQ ADIKTANNIG VHACTIISCV TAQNSTNILN IEKVSKGIFK EQIQAISKEF KIKVIKTSVL SSTEQIDIVV DLLNDLKDVF YICDPVMVST TGYSLVDYRL VEYSKQKLYP LANILVPNLD EAKMLLDEHD SPNVEIAEIA KAIQEKYNCK SVLLKGGHDS DKNISLDCYY TPEVNYTLTS KRYKLDEKVR GTGCTFASAI ASFLTLGFDV NNSIILAKSY ISNAIKSSQK IASHGFFIVD SKYINKQGLF PKVSVHGKDL SIKFRSINKT GFYPIVDSAD KIPSLANLGV KTIQLRIKSN DSEYIQKHIV EAVEYQNKYG LQLFINDYYE LAIKHKAFGV HLGHEDLLSI DRQTLLKIKN TDIALGLSTH DYYELAIALG VNPSYIALGP IYTTNTKKMK FAPQGINKIH EWLNITNTRL VTIGGIKKRH IQSIANIGVD GIAVVTLIDE ISNYEIQNII KLLEK // ID B0U4F7_XYLFM Unreviewed; 204 AA. AC B0U4F7; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Xfasm12_1852; OS Xylella fastidiosa (strain M12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=405440; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M12; RX PubMed=20601474; DOI=10.1128/JB.00651-10; RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.; RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and RT M23) causing almond leaf scorch disease in California."; RL J. Bacteriol. 192:4534-4534(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000941; ACA12736.1; -; Genomic_DNA. DR RefSeq; YP_001776366.1; NC_010513.1. DR ProteinModelPortal; B0U4F7; -. DR STRING; 405440.Xfasm12_1852; -. DR EnsemblBacteria; ACA12736; ACA12736; Xfasm12_1852. DR GeneID; 6121573; -. DR KEGG; xfm:Xfasm12_1852; -. DR PATRIC; 24140470; VBIXylFas124301_2178. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XFAS405440:GH0D-1891-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21961 MW; 3D83B679BAFD11BD CRC64; MSQPRGIYLI TPDETDTARL IARTAPLLNG IVWLQYRNKL ANTALRTEQA QALLALCRPT GIPLLINDDL ELAQTIGADG VHLGMHDSNP SIARAQLGPH AIIGVSCYNQ IERAKQAIKA GASYVGFGAF YPSHTKTTPY RATPELLHQT THLGVPRVAI GGLTPKNIAP IIEAGAELLA VISGIYSAKN PITALKAYQY QFNI // ID B0U579_XYLFM Unreviewed; 320 AA. AC B0U579; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE SubName: Full=DGTP-pyrophosphohydrolase / thiamine phosphate synthase; GN OrderedLocusNames=Xfasm12_0465; OS Xylella fastidiosa (strain M12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=405440; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M12; RX PubMed=20601474; DOI=10.1128/JB.00651-10; RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.; RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and RT M23) causing almond leaf scorch disease in California."; RL J. Bacteriol. 192:4534-4534(2010). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000941; ACA11475.1; -; Genomic_DNA. DR RefSeq; YP_001775105.1; NC_010513.1. DR ProteinModelPortal; B0U579; -. DR STRING; 405440.Xfasm12_0465; -. DR EnsemblBacteria; ACA11475; ACA11475; Xfasm12_0465. DR GeneID; 6119529; -. DR KEGG; xfm:Xfasm12_0465; -. DR PATRIC; 24137204; VBIXylFas124301_0563. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XFAS405440:GH0D-488-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 320 AA; 35354 MW; 7EF8B4725E0542A9 CRC64; MTDSLRSIHV VAAVIVDVRG RLLLSRRTEN SDMPGLWEFP GGKRESGETS EQALARELYE ELGISADVGE WLMEVPQLYP GKRLRLEVRR VRAWKGGLRG REGQALTWVE PDKLLRYSMP PADQPVVGML RQPAHYLVTP EPGEKDAEWL DAVEHAYRLG IERIQLRMRQ HDPARWSGLV REAVQRRGRA HVEVLLNRDI ALAEALGIGV HLGAKQLAVL YARPLPVGLP VGASCHCLAD LCHAQRIGCD FAVLGPVLPT ESHPGAVTLG WEGFEQLREQ VALPIYAIGG MCADQVKEAR RHGAQGIAAM RGLWPGGAKQ // ID B0UEZ9_METS4 Unreviewed; 233 AA. AC B0UEZ9; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=M446_4940; OS Methylobacterium sp. (strain 4-46). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=426117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4-46; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Ivanova N., Marx C.J., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium sp. 4-46."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000943; ACA19269.1; -; Genomic_DNA. DR RefSeq; YP_001771703.1; NC_010511.1. DR ProteinModelPortal; B0UEZ9; -. DR STRING; 426117.M446_4940; -. DR EnsemblBacteria; ACA19269; ACA19269; M446_4940. DR GeneID; 6135280; -. DR KEGG; met:M446_4940; -. DR PATRIC; 22591076; VBIMetSp32184_4860. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTLLQYR; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MSP426117:GI2I-4993-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 202 203 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 23591 MW; AB2D6FDF46D77C45 CRC64; MRPVGMDGTV PVDLRLYGIL DVGVSGGDPA LLARMAGAAA AGGCTLLQYR EKAIPNARES LARLRAIRAA LSGSGVPLLV NDRVDLALAA GAEGVHLGQE DLHPAEARRL LGPGAIIGLT VKTGTQADEL YRLPVDYACI GGVFATASKR NPDPPVGLEG LARIAFRARL ARGGLPIGAI AGIDSGNAAS VIGAGADGIA LISALFGAPD EVEARARALR QLVDRALAAR GAA // ID B0UHP3_METS4 Unreviewed; 214 AA. AC B0UHP3; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=M446_6768; OS Methylobacterium sp. (strain 4-46). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=426117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4-46; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Ivanova N., Marx C.J., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium sp. 4-46."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000943; ACA21013.1; -; Genomic_DNA. DR RefSeq; YP_001773447.1; NC_010511.1. DR ProteinModelPortal; B0UHP3; -. DR STRING; 426117.M446_6768; -. DR EnsemblBacteria; ACA21013; ACA21013; M446_6768. DR GeneID; 6130041; -. DR KEGG; met:M446_6768; -. DR PATRIC; 22594828; VBIMetSp32184_6709. DR eggNOG; NOG270906; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6DNT5D; -. DR BioCyc; MSP426117:GI2I-6850-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 133 135 THZ-P binding (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 20887 MW; 5DA5E7FFD5377962 CRC64; MRPLPARLLV VSDRHGSDRP LVARVAAALA AGARWIWLRD RDLPEAERAA LAGELARLVG EAGGTLTIGR DAGLAARVGA GGVQAGDAAA AAAARARLGP GALVGVSAHS LAEVRAAREA GADYVTLSPI FATASKPGYG PALGPAALAP AAELGLPVVA LGGITPETAS SCLEAGAAGI AVMGGVMRAR DPGAAVGALL GALAIGRGPA PTRR // ID B0UKE9_METS4 Unreviewed; 230 AA. AC B0UKE9; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 37. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN OrderedLocusNames=M446_6005; OS Methylobacterium sp. (strain 4-46). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=426117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4-46; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Ivanova N., Marx C.J., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium sp. 4-46."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000943; ACA20282.1; -; Genomic_DNA. DR RefSeq; YP_001772716.1; NC_010511.1. DR ProteinModelPortal; B0UKE9; -. DR STRING; 426117.M446_6005; -. DR EnsemblBacteria; ACA20282; ACA20282; M446_6005. DR GeneID; 6132247; -. DR KEGG; met:M446_6005; -. DR PATRIC; 22593276; VBIMetSp32184_5946. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; MSP426117:GI2I-6073-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 230 AA; 23217 MW; 4FEF316824626F4D CRC64; MPTPHPPKTR LVLIAGPESG PDLAARLSAA CRAGDVAAVI LRLAAADERA LIRRVKDVAP AVQEAGAALV VACDAPGIDP VALAARAGAD GVHAGAGEEP GEALRDLRER LRDGRILGVG SLTSRHAAME AGEAGADYVL FGEEPRATPA GTRALAAWWA EIFETPCVAL ARSLDAVADL AATGAEFVAL DPALWEGPAL REGPALREGA GTQGPDAVAQ AQARLAGGAA // ID B0V8V4_ACIBY Unreviewed; 303 AA. AC B0V8V4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Putative bifunctional protein; GN OrderedLocusNames=ABAYE1196; OS Acinetobacter baumannii (strain AYE). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509173; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AYE; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., RA Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., RA Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., RA Raoult D., Medigue C., Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU459141; CAM86120.1; -; Genomic_DNA. DR RefSeq; YP_001713121.1; NC_010410.1. DR ProteinModelPortal; B0V8V4; -. DR STRING; 509173.ABAYE1196; -. DR EnsemblBacteria; CAM86120; CAM86120; ABAYE1196. DR GeneID; 6001039; -. DR KEGG; aby:ABAYE1196; -. DR PATRIC; 20725813; VBIAciBau69881_1229. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ABAU509173:GJXF-1174-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 303 AA; 34706 MW; 50DE5B4003174DFE CRC64; MSRKMPKPIV DVAIAILIHR GKILVGWRGE QQHQGGKHEF PGGKVEQGET PEEACRREIY EEVGIGLKDW HQFDYIHHEY DDIIVNLHLF HSYVPDELLN LIHQPWTWYT REQLLHLNFP KANKDIIKRL YWPHFIKISH TLTSVENSDA LLYWRIEDEF GPREVEQLTA LDEGQRSNLI INVDIWQQLN PELKKKIKTV HLKQSQLMSL HKGDLEVGVR FIAACHDAVS LQHAQQIGCD AVFVSPVKVT ATHPDVSALG WDRFADLIEK CQIPVFALGG MSPDDLATAQ QHGAYGLAGI RNF // ID B0VCN5_ACIBY Unreviewed; 203 AA. AC B0VCN5; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ABAYE1010; OS Acinetobacter baumannii (strain AYE). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509173; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AYE; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., RA Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., RA Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., RA Raoult D., Medigue C., Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU459141; CAM85945.1; -; Genomic_DNA. DR RefSeq; YP_001712948.1; NC_010410.1. DR ProteinModelPortal; B0VCN5; -. DR STRING; 509173.ABAYE1010; -. DR EnsemblBacteria; CAM85945; CAM85945; ABAYE1010. DR GeneID; 6000918; -. DR KEGG; aby:ABAYE1010; -. DR PATRIC; 20725453; VBIAciBau69881_1053. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ABAU509173:GJXF-995-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21750 MW; C30389C3887A22BE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKVD KADQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAK LFS // ID B0VU91_ACIBS Unreviewed; 203 AA. AC B0VU91; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ABSDF1078; OS Acinetobacter baumannii (strain SDF). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509170; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDF; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., RA Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., RA Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., RA Raoult D., Medigue C., Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU468230; CAP00429.1; -; Genomic_DNA. DR RefSeq; YP_001706588.1; NC_010400.1. DR ProteinModelPortal; B0VU91; -. DR STRING; 509170.ABSDF1078; -. DR EnsemblBacteria; CAP00429; CAP00429; ABSDF1078. DR GeneID; 5984611; -. DR KEGG; abm:ABSDF1078; -. DR PATRIC; 20733046; VBIAciBau88365_1045. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21792 MW; 4956A220DADFC570 CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKID KAEQPAEVEQ IKQLCEKYQI PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID B0VUZ4_ACIBS Unreviewed; 303 AA. AC B0VUZ4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE SubName: Full=Putative bifunctional protein; GN OrderedLocusNames=ABSDF1240; OS Acinetobacter baumannii (strain SDF). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509170; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDF; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., RA Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., RA Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., RA Raoult D., Medigue C., Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU468230; CAP00586.1; -; Genomic_DNA. DR RefSeq; YP_001706713.1; NC_010400.1. DR ProteinModelPortal; B0VUZ4; -. DR STRING; 509170.ABSDF1240; -. DR EnsemblBacteria; CAP00586; CAP00586; ABSDF1240. DR GeneID; 5984730; -. DR KEGG; abm:ABSDF1240; -. DR PATRIC; 20733374; VBIAciBau88365_1205. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 303 AA; 34655 MW; BB5294F2BD6458C5 CRC64; MSRKMPKPIV DVAIAILIHR GKILVGWRGE QQHQGGKHEF PGGKVEQGET PEEACRREIY EEVGIGLKDW HQFDYIHHEY DDIIVNLHLF HSYVPDELLN LIHQPWTWYT REQLLHLNFP KANKDIIKRL YWPHFIKISH TLTSVANSDA LLYWRIEDEF GPREVEQLTA LVEGQRSNLI INVDIWQQLN SELKKQIKTV HLKQSQLMSL HKGDLEVGIR FIAACHDAVS LQHAQQIGCD AVFVSPVKVT ATHPDVSALG WDRFADLIEK CQIPVFALGG MSPDDLATAQ QRGAYGLAGI RNF // ID B0XRU4_ASPFC Unreviewed; 519 AA. AC B0XRU4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 16-APR-2014, entry version 28. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative; GN ORFNames=AFUB_024860; OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OS (Aspergillus fumigatus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=451804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163; RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046; RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., RA Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., RA Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., RA Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R., RA Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., RA Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., RA Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., RA Jiang B., Denning D.W., Nierman W.C.; RT "Genomic islands in the pathogenic filamentous fungus Aspergillus RT fumigatus."; RL PLoS Genet. 4:E1000046-E1000046(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS499595; EDP54430.1; -; Genomic_DNA. DR ProteinModelPortal; B0XRU4; -. DR EnsemblFungi; CADAFUBT00002480; CADAFUBP00002429; CADAFUBG00002480. DR HOGENOM; HOG000214306; -. DR OrthoDB; EOG7KDFMZ; -. DR PhylomeDB; B0XRU4; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 519 AA; 55142 MW; A37EF25288B07BBB CRC64; MALDLSVYLV TDSTPAILKG RDLCTVVEEA LKGGVTIVQY RDKTSDTGAL IQTAKELHKI TKAYGVPLLI NDRVDVALAV GAEGVHLGQD DMYIEEAKKL LPKDAIIGIS ASSVEEAQRA IEAGADYLGI GTMFATPTKT NTKHILGTAG TQAILDAISD SSRNVGTVAI GGIKLSNVQR VIYQSKAPRK GLDGVAIVSA IMAADDPRAA AEEFVKRINN PPSFAWEPKA PRANEAAALA EEVAQIVQKM VKAHPLVHNM INYVVANFVA NVALAIGASP IMSPYGEEAV DLAKFDGALV INMGTLSRES IPNYLQAIKS YNERGNPVVY DPVGAAATHI RRGAVKELMS GGYFDLIKGN EGEIKQVSGS RNAVQRGVDS GPSTLDGQEK ARLARDLARR ERNVVLLTGA VDYLSDGERV IAVENGHEFL GQVTGTGCAV GMVSGCFLAV HPSDKLLAVL SGLLMYEIAA ENAASKDYVR GPGSFVPAFL DELYAIRQAA LKGDDSWFSG RAKIQEIKL // ID B1B757_CLOBO Unreviewed; 153 AA. AC B1B757; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 16-OCT-2013, entry version 26. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=CBC_A1197; OS Clostridium botulinum C str. Eklund. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=445337; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Eklund; RA Paulsen I.; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Eklund; RX PubMed=23516187; RA Hassan K.A., Tetu S.G., Elbourne L.D., Johnson E.A., Paulsen I.T.; RT "Genome Sequence of the Group III Clostridium botulinum Strain Eklund- RT C."; RL Genome Announc. 1:E0004413-E0004413(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDQ01000001; EDS78400.1; -; Genomic_DNA. DR ProteinModelPortal; B1B757; -. DR EnsemblBacteria; EDS78400; EDS78400; CBC_A1197. DR PATRIC; 26419473; VBICloBot5690_0052. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 153 AA; 16767 MW; BE765E23714B5BB7 CRC64; MAYNVKTITD KYNVPLIING NLEVAEHVNA YGCQLSYNML MKCKLWKKLK LKIGVSVHSI EEAVNAEKVG VNYILAGHVF ETDCKKGLKG RGLKFISDIS NNICIPLIAI GGINESNVQS VIKSGASGVA IMSTAMEKGN VHKIQEILYK IRT // ID B1BEE3_CLOBO Unreviewed; 71 AA. AC B1BEE3; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 16-OCT-2013, entry version 25. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE Flags: Fragment; GN ORFNames=CBC_A0015; OS Clostridium botulinum C str. Eklund. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=445337; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Eklund; RA Paulsen I.; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Eklund; RX PubMed=23516187; RA Hassan K.A., Tetu S.G., Elbourne L.D., Johnson E.A., Paulsen I.T.; RT "Genome Sequence of the Group III Clostridium botulinum Strain Eklund- RT C."; RL Genome Announc. 1:E0004413-E0004413(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDQ01000054; EDS76149.1; -; Genomic_DNA. DR ProteinModelPortal; B1BEE3; -. DR EnsemblBacteria; EDS76149; EDS76149; CBC_A0015. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. FT NON_TER 71 71 SQ SEQUENCE 71 AA; 8139 MW; 3EB25431289DA301 CRC64; MAIDYKLYLI TDRSFLNGRS LAECVEDAIK GGVTLVQVRE KNVSTRDFYN IAKEVQEVTT KYNVPLLIND R // ID B1BEH9_CLOPF Unreviewed; 207 AA. AC B1BEH9; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CPC_1570; OS Clostridium perfringens C str. JGS1495. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=445334; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JGS1495; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium perfringens C str. JGS1495."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDU01000004; EDS81793.1; -; Genomic_DNA. DR ProteinModelPortal; B1BEH9; -. DR EnsemblBacteria; EDS81793; EDS81793; CPC_1570. DR PATRIC; 30617118; VBICloPer103972_0026. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22872 MW; BCA7E3714061AF98 CRC64; MSNKDTKKLY LVTDYRIPFN ELLEKTKEAL IGGVSIVQYR AKNKKTKEMC KEAKELKKLC DEFGALFLVN DRIDVALAVK ANGVHIGQDD MEVSIAREIM PKDAVVGVTV HNKEEALKAI KEGADNLGVG ALFSTNSKDD ATLMTLETLR EIKSVSNIPL YGIGGITPYN LNKDILENLE GVAVISSLLN SDNIREKSKE FLNILSK // ID B1BGG8_CLOPF Unreviewed; 193 AA. AC B1BGG8; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 26. DE SubName: Full=Thiamine monophosphate synthase family protein; GN ORFNames=CPC_1841; OS Clostridium perfringens C str. JGS1495. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=445334; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JGS1495; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium perfringens C str. JGS1495."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDU01000023; EDS81194.1; -; Genomic_DNA. DR ProteinModelPortal; B1BGG8; -. DR EnsemblBacteria; EDS81194; EDS81194; CPC_1841. DR PATRIC; 30618605; VBICloPer103972_0729. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 193 AA; 22018 MW; 8CCF204D1FDB2DAE CRC64; MFLITNRKLV NRERYFNTIE EAGKYGVKNI ILREKDLSTE ELIEVYIKIK ELVPEETNII INSNIEATRI LKEKFIHLSF KDFKKNLEEV KSLQVGVSVH SILEAIEADR LGASYILVSP IFETQCKKGV TPKGINFIKE IKEKVNCKVI ALGGINELNF KEVLVAGADD FACMSLLFMS NNIKKCLDTF KEL // ID B1BXK9_CLOPF Unreviewed; 193 AA. AC B1BXK9; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 26. DE SubName: Full=Thiamine monophosphate synthase family protein; GN ORFNames=AC3_2060; OS Clostridium perfringens E str. JGS1987. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=451755; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JGS1987; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium perfringens E str. JGS1987."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDW01000046; EDT13562.1; -; Genomic_DNA. DR ProteinModelPortal; B1BXK9; -. DR EnsemblBacteria; EDT13562; EDT13562; AC3_2060. DR PATRIC; 30645432; VBICloPer82820_3380. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 193 AA; 21879 MW; 9753DEEE59A9A035 CRC64; MFLITNRKLV NRKRYFNTIE EAGKYGVKNI ILREKDLSTE ELIEVYIKIK ELVPKETNII INSNIEAARI LKEKFIHLSF KDFKKNLEGV KSLQVGVSVH SILEALEADR LGASYILVSP IFETQCKKGV IPKGINFIKE IKEKVNCKVI ALGGINELNF KEVLGAGADD FACMSLLFMR NNIKKSLDTF KAL // ID B1BY13_CLOPF Unreviewed; 207 AA. AC B1BY13; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AC3_1741; OS Clostridium perfringens E str. JGS1987. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=451755; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JGS1987; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium perfringens E str. JGS1987."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDW01000055; EDT13407.1; -; Genomic_DNA. DR ProteinModelPortal; B1BY13; -. DR EnsemblBacteria; EDT13407; EDT13407; AC3_1741. DR PATRIC; 30645797; VBICloPer82820_3552. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22921 MW; EC7F886E04482E53 CRC64; MSNKDYKKLY LVTDYRIPFN ELLEKTKEAL IGGVSIVQYR AKNKKTKEMC KEAKELKKLC DDFGALFLVN DRIDVALAVK ANGVHIGQDD MEVSIAREIM PKDAVIGVTV HNKEEALKAI KEGADNLGVG ALFSTNSKDD ATLMTLETLR EIKSVSNIPL YGIGGITPYN LNKDILENLD GVAVISSLLN SDNIREKSKE FLNILSK // ID B1C041_9FIRM Unreviewed; 212 AA. AC B1C041; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLOSPI_00568; OS Clostridium spiroforme DSM 1552. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=428126; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1552; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium spiroforme (DSM 1552)."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1552; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIK02000005; EDS75531.1; -; Genomic_DNA. DR ProteinModelPortal; B1C041; -. DR EnsemblBacteria; EDS75531; EDS75531; CLOSPI_00568. DR PATRIC; 27259599; VBICloSpi85079_0373. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23407 MW; 06EDC49C8E1537C0 CRC64; MKLNNKSLLL YAVTDRRWSY NDTFYKHIEE SLEGGVTFLQ LREKNLDIDS FFKEAIKIKE LCKKYNVPFI INDNVEIALK SNADGIHVGQ DDMGVEEVRK LIGKEKILGV SVQTVEQALL AQSQGANYLG VGSIFTTTSK DDAKSVSINT LKEICNVVNI PVVAIGGIDE NNAKQLSKTG ISGIAVISAI YANKNIKNAA MKLKELIEEI VK // ID B1C7E9_9FIRM Unreviewed; 215 AA. AC B1C7E9; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ANASTE_00651; OS Anaerofustis stercorihominis DSM 17244. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Anaerofustis. OX NCBI_TaxID=445971; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17244; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Anaerofustis stercorihominis (DSM 17244)."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17244; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIL02000005; EDS72936.1; -; Genomic_DNA. DR ProteinModelPortal; B1C7E9; -. DR EnsemblBacteria; EDS72936; EDS72936; ANASTE_00651. DR PATRIC; 24498633; VBIAnaSte97905_0297. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23348 MW; FDBA23D7A6ECA6F6 CRC64; MKVNSEDMLL YAVTDRAWTE SEDLYSQVKK ALKGGITFLQ LREKELDEET FLKEALKIKE LAKEYDVPFV INDNVDIAVK SDADGVHVGQ SDMEAGDVRK KIGKDKILGV SASNLKEAKL AEEKGADYLG VGAVFSTSTK LDADEVSFDT LKEICDNVSI PVVAIGGISK DNILKLKGTN VDGVAVVSAI FASSDIVNDT KELLKLSKEM VKGDK // ID B1CBK4_9FIRM Unreviewed; 189 AA. AC B1CBK4; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=ANASTE_01353; OS Anaerofustis stercorihominis DSM 17244. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Anaerofustis. OX NCBI_TaxID=445971; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17244; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Anaerofustis stercorihominis (DSM 17244)."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17244; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIL02000006; EDS71651.1; -; Genomic_DNA. DR ProteinModelPortal; B1CBK4; -. DR EnsemblBacteria; EDS71651; EDS71651; ANASTE_01353. DR PATRIC; 24500593; VBIAnaSte97905_1265. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 189 AA; 21274 MW; BCFEAAF82103D986 CRC64; MCTYSNIICI TNRHLSDIPF LERIEKIAKK HPKYIVLREK DLSENEYSKL AEEVMKICDR ENVDLILHSF IDTAISLGVK NIHLPLYIAK EQKSKLKYFD VIGISTHSME EAVEAENLGA SYITAGHIFE TDCKKGMKGR GLDFIKDITI NISIPVYGIG GININNMDKV LKCGAEGVCI MSEFMKGNI // ID B1ES79_9ESCH Unreviewed; 211 AA. AC B1ES79; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ESCAB7627_3792; OS Escherichia albertii TW07627. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=502347; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TW07627; RA Sutton G., Whittam T.S., Sebastian Y.; RT "Annotation of Escherichia albertii TW07627."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABKX01000019; EDS89945.1; -; Genomic_DNA. DR ProteinModelPortal; B1ES79; -. DR EnsemblBacteria; EDS89945; EDS89945; ESCAB7627_3792. DR PATRIC; 30328546; VBIEscAlb18499_4622. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23132 MW; 5AF53821A99E781B CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIERLADYP TVAIGGISLA RAPAVMATGV GSIAVVSAIT QAADWRLVTK QLLEIAGVGD E // ID B1F0H1_BACAN Unreviewed; 219 AA. AC B1F0H1; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BAK_0431; OS Bacillus anthracis str. A0389. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=486623; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A0389; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Brettin T.S.; RT "Genome sequence of Bacillus anthracis A0389."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABLB01000011; EDS96739.1; -; Genomic_DNA. DR ProteinModelPortal; B1F0H1; -. DR SMR; B1F0H1; 1-215. DR EnsemblBacteria; EDS96739; EDS96739; BAK_0431. DR PATRIC; 24607955; VBIBacAnt25810_3171. DR OMA; QFREKGP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23600 MW; 6D85F0FE3EFD3046 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGFI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWVIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID B1F4E5_BACAN Unreviewed; 206 AA. AC B1F4E5; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-MAR-2014, entry version 29. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BAK_0827; OS Bacillus anthracis str. A0389. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=486623; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A0389; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Brettin T.S.; RT "Genome sequence of Bacillus anthracis A0389."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABLB01000027; EDS95370.1; -; Genomic_DNA. DR ProteinModelPortal; B1F4E5; -. DR EnsemblBacteria; EDS95370; EDS95370; BAK_0827. DR PATRIC; 24611173; VBIBacAnt25810_4714. DR OMA; ELVNVAM; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID B1FLK1_9BURK Unreviewed; 84 AA. AC B1FLK1; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 25. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=BamIOP4010DRAFT_4912; OS Burkholderia ambifaria IOP40-10. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=396596; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IOP40-10; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Tiedje J., Richardson P.; RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria RT IOP40-10."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABLC01000171; EDT01586.1; -; Genomic_DNA. DR ProteinModelPortal; B1FLK1; -. DR EnsemblBacteria; EDT01586; EDT01586; BamIOP4010DRAFT_4912. DR PATRIC; 38374827; VBIBurAmb78662_4987. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 84 AA; 8745 MW; 3CB6F36C4EBA1786 CRC64; MSAACHAADD LVLAARAGVD FVTLSPVLPT LSHPGAPTLG WTRFAALAAQ AVMPVYALGG MTRAHLDDAR RHGAYGVAGI RSFW // ID B1FQF6_9BURK Unreviewed; 349 AA. AC B1FQF6; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 25. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=BamIOP4010DRAFT_6267; OS Burkholderia ambifaria IOP40-10. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=396596; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IOP40-10; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Tiedje J., Richardson P.; RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria RT IOP40-10."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABLC01000324; EDT00216.1; -; Genomic_DNA. DR ProteinModelPortal; B1FQF6; -. DR EnsemblBacteria; EDT00216; EDT00216; BamIOP4010DRAFT_6267. DR PATRIC; 38377829; VBIBurAmb78662_6408. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 349 AA; 37589 MW; 723836B226650B9C CRC64; MSARFADAFW PPADELAEAA ERIRARLGDW PAGTTPWRLC VAAPDVPVDG DVLIVSAGDR AAQARASAAS RPAAPDAVAI EFDEHGATLH AAGVRHALEA AHPPADDWIA ALAAFLDCGF APIDALVLAL AWRDGDETRG VDAWPVDAAR FPRVAGLAAA AEPAFPPCPA QLGLYPVVPD AEWVERVLDC GARTVQLRVK DADPAALRRE IARAVAAGRG YPDARVFIND HWQIAVEEGR TAYIWVRKTW GRPIWPRSRA PACGSGCRAT AITKCCGRCT SVRAISRSAP CTRPRPRRLR RRRRDSRGSP AMRVSQGRGR RSSQSAAWAS TRCLTCSRRA SAASRSSVR // ID B1G8P6_9BURK Unreviewed; 370 AA. AC B1G8P6; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BgramDRAFT_5704; OS Burkholderia graminis C4D1M. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=396598; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C4D1M; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Tiedje J., Richardson P.; RT "Sequencing of the draft genome and assembly of Burkholderia graminis RT C4D1M."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABLD01000026; EDT07543.1; -; Genomic_DNA. DR ProteinModelPortal; B1G8P6; -. DR EnsemblBacteria; EDT07543; EDT07543; BgramDRAFT_5704. DR PATRIC; 26884250; VBIBurGra66597_5829. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 370 AA; 39822 MW; 82B7CE3979DF976E CRC64; MTQTLALKDR DLFWPPADEL TEATERIRAR LGDWPPTHAP WRICLTAPDQ PNGGDLIVLA DAARHGEQMA RWLVQGAAVV EAAENKATLH LGGEKYRLEG HLAEDWIPAL AAFLDCGFDP HDALVLALAW RDGDETRTNA AGDSFPCDLA VFPRLAGLPQ APAQPFPRCP ERLGLYPVLP SAEWVERVVG YGVKTVQLRR KSAHPADELQ REIARCVAAG KRHDAQVFIN DHWQAALDAG AYGVHLGQED VHTADLAALA AAGIRLGLST HGFYEILKAL HFRPSYIALG AVFPTTTKVM PTAPQGVKRL ARYVRLLDGV VPLVAIGGID LQVLPEVLAT GVGCAAVVRA VTEASDPAAA VAALQQAFTQ // ID B1GNP9_BACAN Unreviewed; 219 AA. AC B1GNP9; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BAM_0385; OS Bacillus anthracis str. A0465. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=486620; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A0465; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Brettin T.S.; RT "Genome sequence of Bacillus anthracis A0465."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABLH01000025; EDT17832.1; -; Genomic_DNA. DR ProteinModelPortal; B1GNP9; -. DR SMR; B1GNP9; 1-215. DR EnsemblBacteria; EDT17832; EDT17832; BAM_0385. DR PATRIC; 24635580; VBIBacAnt29655_4789. DR OMA; QFREKGP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23600 MW; 6D85F0FE3EFD3046 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGFI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWVIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID B1GP30_BACAN Unreviewed; 206 AA. AC B1GP30; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-MAR-2014, entry version 29. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BAM_0778; OS Bacillus anthracis str. A0465. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=486620; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A0465; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Brettin T.S.; RT "Genome sequence of Bacillus anthracis A0465."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABLH01000028; EDT17677.1; -; Genomic_DNA. DR ProteinModelPortal; B1GP30; -. DR EnsemblBacteria; EDT17677; EDT17677; BAM_0778. DR PATRIC; 24635922; VBIBacAnt29655_4938. DR OMA; ELVNVAM; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID B1H024_UNCTG Unreviewed; 211 AA. AC B1H024; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TGRD_373; OS Uncultured termite group 1 bacterium phylotype Rs-D17. OC Bacteria; Elusimicrobia; environmental samples. OX NCBI_TaxID=471821; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18391199; DOI=10.1073/pnas.0801389105; RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T., RA Sakaki Y., Toyoda A., Hattori M., Ohkuma M.; RT "Complete genome of the uncultured termite group 1 bacteria in a RT single host protist cell."; RL Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009510; BAG13856.1; -; Genomic_DNA. DR RefSeq; YP_001956317.1; NC_020419.1. DR ProteinModelPortal; B1H024; -. DR STRING; 471821.TGRD_373; -. DR GeneID; 6373048; -. DR KEGG; rsd:TGRD_373; -. DR PATRIC; 38570826; VBIUncTer52152_0607. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; UTER471821:GJAD-400-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23593 MW; B532A6841F083574 CRC64; MKKQIPKGLY AITAENFSNG KDNISVVKEM LDAGIKILQY RDKYKTKLEK FKQCEIIRRL TLDYNVFFII NDDIDIALSI QSEGIHLGQD DLPLAKARGI AGPDITIGIS THLPKQALLA AEHGADYIGV GPIYKTFTKD NVVDPVGLGY LDFCVKNINI PKVAIGGIKF SNLLEIYRYN PENICMVTEI TASENIEFTV KKVKEAMNDY C // ID B1H7F7_BURPE Unreviewed; 209 AA. AC B1H7F7; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 16-OCT-2013, entry version 25. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BURPSS13_X0581; OS Burkholderia pseudomallei S13. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320374; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S13; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia pseudomallei S13."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899763; EDS83115.1; -; Genomic_DNA. DR ProteinModelPortal; B1H7F7; -. DR EnsemblBacteria; EDS83115; EDS83115; BURPSS13_X0581. DR PATRIC; 30415140; VBIBurPse99458_1734. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID B1HL79_BURPE Unreviewed; 367 AA. AC B1HL79; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=BURPSS13_S0088; OS Burkholderia pseudomallei S13. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320374; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S13; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia pseudomallei S13."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899774; EDS87948.1; -; Genomic_DNA. DR ProteinModelPortal; B1HL79; -. DR EnsemblBacteria; EDS87948; EDS87948; BURPSS13_S0088. DR PATRIC; 30423922; VBIBurPse99458_6085. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Transferase. SQ SEQUENCE 367 AA; 38308 MW; E8F50A360B15395D CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAQIARL NAAGAQAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDTLRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID B1I673_DESAP Unreviewed; 352 AA. AC B1I673; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Daud_2019; OS Desulforudis audaxviator (strain MP104C). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Candidatus Desulforudis. OX NCBI_TaxID=477974; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP104C; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., RA Land M.L., Hauser L., Kyrpides N., Ivanova N.N., Richardson P.; RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000860; ACA60510.1; -; Genomic_DNA. DR RefSeq; YP_001718142.1; NC_010424.1. DR ProteinModelPortal; B1I673; -. DR STRING; 477974.Daud_2019; -. DR EnsemblBacteria; ACA60510; ACA60510; Daud_2019. DR GeneID; 6025895; -. DR KEGG; dau:Daud_2019; -. DR PATRIC; 31970944; VBICanDes92303_2085. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; NFNRARE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DAUD477974:GH0B-2073-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 178 182 HMP-PP binding (By similarity). FT REGION 275 277 THZ-P binding (By similarity). FT METAL 211 211 Magnesium (By similarity). FT METAL 230 230 Magnesium (By similarity). FT BINDING 210 210 HMP-PP (By similarity). FT BINDING 249 249 HMP-PP (By similarity). FT BINDING 278 278 HMP-PP (By similarity). FT BINDING 305 305 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 352 AA; 37540 MW; C4000246BB76DA2D CRC64; MREICRIADV NFNRAREGLR VVEEACRFVL ADPGLTARIK ELRHRLSVLE EAFPGGRLAL LAARDISGDV GAPAPENRPR DNIFAAAGAG WKRAQEAARV LEELSREADP APARHFKEFR FALYAAEREW TLTSAAWGRK AAFDRVRLYL VAGRADTGGR PLVEVVRAAV AGGAGAFQLR EKNMETRELT ALAAELCAVV RSAGALFLVN DRVDVAAAVD ADGVHLGQDD LPVEAARRLL GLGKLIGVSV HSPAQAREAW EQGADYVGLG AVFPTATKPE ARAVSLSRLS ELAAGVDLPS VAIGGIDLSN IKEVLRAGFR RVAVVRAVAG APDPNLAAAA LCEAINEVWG DH // ID B1IAP0_STRPI Unreviewed; 209 AA. AC B1IAP0; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; OrderedLocusNames=SPH_0805; OS Streptococcus pneumoniae (strain Hungary19A-6). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=487214; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hungary19A-6; RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.; RT "Complete sequence of Streptococcus pneumoniae strain Hungary 19A-6."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000936; ACA36466.1; -; Genomic_DNA. DR RefSeq; YP_001694175.1; NC_010380.1. DR ProteinModelPortal; B1IAP0; -. DR STRING; 487214.SPH_0805; -. DR EnsemblBacteria; ACA36466; ACA36466; SPH_0805. DR GeneID; 6029586; -. DR KEGG; spv:SPH_0805; -. DR PATRIC; 19691716; VBIStrPne34925_0814. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE487214:GHY0-786-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID B1IAP7_STRPI Unreviewed; 210 AA. AC B1IAP7; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; OrderedLocusNames=SPH_0812; OS Streptococcus pneumoniae (strain Hungary19A-6). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=487214; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hungary19A-6; RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.; RT "Complete sequence of Streptococcus pneumoniae strain Hungary 19A-6."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000936; ACA36655.1; -; Genomic_DNA. DR RefSeq; YP_001694182.1; NC_010380.1. DR ProteinModelPortal; B1IAP7; -. DR STRING; 487214.SPH_0812; -. DR EnsemblBacteria; ACA36655; ACA36655; SPH_0812. DR GeneID; 6028259; -. DR KEGG; spv:SPH_0812; -. DR PATRIC; 19691730; VBIStrPne34925_0821. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE487214:GHY0-793-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID B1J3J2_PSEPW Unreviewed; 314 AA. AC B1J3J2; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=PputW619_0955; OS Pseudomonas putida (strain W619). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=390235; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W619; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Taghavi S., Vangronsveld D., RA van der Lelie D., Richardson P.; RT "Complete sequence of Pseudomonas putida W619."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000949; ACA71460.1; -; Genomic_DNA. DR RefSeq; YP_001747829.1; NC_010501.1. DR ProteinModelPortal; B1J3J2; -. DR STRING; 390235.PputW619_0955; -. DR EnsemblBacteria; ACA71460; ACA71460; PputW619_0955. DR GeneID; 6109873; -. DR KEGG; ppw:PputW619_0955; -. DR PATRIC; 19951641; VBIPsePut93764_0954. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPUT390235:GHHJ-966-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 34278 MW; EC085C3842F29B4A CRC64; MKRIHVAAAV IRGTDGRILI ARRADSQHQG GLWEFPGGKV EEGESVEAAL ARELREELGI EVTRSRALIK VSHDYPDKQV LLDVREVEAF AGEPHGAEGQ PLAWVSPRDL PQYEFPEANK PIVAAARLPD QYLITPEGLD VPEMLKGIQR AVAGGIRLIQ LRAPDMYDPK YRDVAVDAVG LCAGKAQLML KGPLEWLGDF PAAGWHLTAA QLRKYAAKGR PFPKDRWLAA SCHSAEELAL AEQMGVDFVT LSPVQLTQTH PEASPLGWDE AQRLIAGFGK PVFLLGGIGP DERERAWKAG AQGVAGIRAF WPEA // ID B1JJK5_YERPY Unreviewed; 224 AA. AC B1JJK5; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=YPK_0346; OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=502800; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YPIII; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., RA Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., RA Hauser L., Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., RA Richardson P.; RT "Complete sequence of Yersinia pseudotuberculosis YPIII."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000950; ACA66656.1; -; Genomic_DNA. DR RefSeq; YP_001719109.1; NC_010465.1. DR ProteinModelPortal; B1JJK5; -. DR STRING; 502800.YPK_0346; -. DR EnsemblBacteria; ACA66656; ACA66656; YPK_0346. DR GeneID; 6087142; -. DR KEGG; ypy:YPK_0346; -. DR PATRIC; 18657702; VBIYerPse127545_0362. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; YPSE502800:GH0W-353-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24216 MW; E13A24EDCD5E0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE TADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID B1JU87_BURCC Unreviewed; 375 AA. AC B1JU87; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Bcenmc03_0392; OS Burkholderia cenocepacia (strain MC0-3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=406425; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC0-3; RA Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0- RT 3."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000958; ACA89572.1; -; Genomic_DNA. DR RefSeq; YP_001763694.1; NC_010508.1. DR ProteinModelPortal; B1JU87; -. DR STRING; 406425.Bcenmc03_0392; -. DR EnsemblBacteria; ACA89572; ACA89572; Bcenmc03_0392. DR GeneID; 6122075; -. DR KEGG; bcm:Bcenmc03_0392; -. DR PATRIC; 19087721; VBIBurCen61509_0405. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BCEN406425:GHD9-407-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 375 AA; 39309 MW; B51F10E30A099A1B CRC64; MSAARFADAF WPPADELAEA AERIRARLGD WPEGAAPWRL CVAAPDVPAD GDVLIVSAGD RAAQARASAV SRPASPDAVA IEFDEQGAVL HAVGVRYALA AAHPLADDWI AALAAFLDCG FAPVDALVLA LAWRDGDETR AADAWPVDAA RFPQVAGLPP APEPAFAPCP ARLGLYPVVP SAEWVERVLD GGARTVQLRV KDATPDALRR EIARAVAAGR RYPDARVFIN DHWQIAAEEG AYGVHLGQED LETADLAAIA RAGLRLGLSS HGYYEMLRAL HERPSYLALG PVYATATKAV AAPPQGLARI ARYARFAGAR APLVAIGGVG LDTLPAVLAT GVGSVAVVSA VTGAADYRTA LIALQQCFTG QFDNH // ID B1K4B1_BURCC Unreviewed; 194 AA. AC B1K4B1; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 37. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bcenmc03_3677; OS Burkholderia cenocepacia (strain MC0-3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=406425; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC0-3; RA Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0- RT 3."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000959; ACA92829.1; -; Genomic_DNA. DR RefSeq; YP_001777319.1; NC_010515.1. DR ProteinModelPortal; B1K4B1; -. DR STRING; 406425.Bcenmc03_3677; -. DR EnsemblBacteria; ACA92829; ACA92829; Bcenmc03_3677. DR GeneID; 6126511; -. DR KEGG; bcm:Bcenmc03_3677; -. DR PATRIC; 19096988; VBIBurCen61509_4963. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCEN406425:GHD9-3754-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 19918 MW; C6EB413E18D31159 CRC64; MNAPLPRCCV ITPEPASASA ADRAAFLDRL SAVLARGETL VQLRVKSLDA AAFASLAAAA LARCAAAGAH LMLNGPIDAA GVMRLDGAGW HLDGTALRAA AQRPLPAARW VSAACHTQDD LLLAARAGAD FVTLSPVLPT LSHPGAPALG WARFDALAAQ AAMPVFALGG MTRAHLDDAR RHGAYGIAGI RGFW // ID B1KHI3_SHEWM Unreviewed; 535 AA. AC B1KHI3; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Swoo_2591; OS Shewanella woodyi (strain ATCC 51908 / MS32). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=392500; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51908 / MS32; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella woodyi ATCC 51908."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000961; ACA86868.1; -; Genomic_DNA. DR RefSeq; YP_001760963.1; NC_010506.1. DR ProteinModelPortal; B1KHI3; -. DR STRING; 392500.Swoo_2591; -. DR EnsemblBacteria; ACA86868; ACA86868; Swoo_2591. DR GeneID; 6116888; -. DR KEGG; swd:Swoo_2591; -. DR PATRIC; 23607677; VBISheWoo126588_2672. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SWOO392500:GI2C-2671-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 535 AA; 57065 MW; 8192DB7BC4CF70F5 CRC64; MANSTLSSSV NRPVVWTIAG SDSGGGAGIQ ADLLTMNDLG CHSCSVISCV TAQSSVAVNL VEAVSPQMFQ SQLDTLLHDL PPVAIKIGLL ANQSQVLMLA SWLRETLAEY CKQAGVEVSV ILDPVMFATC GDNLNSSLDF SPFKNLLTLI TPNITELAAL VEIKAKPDPA MSEAESFLVD QADCVLAAEQ LSEQLNCHVL AKGGDLGPTW LRDCAQDIFV CREAKGSSIF HQGRTFLLSG PRINSDNTHG SGCTLSSAIA SVMGQGYVLH DAIVVAKAYV TAGIAASFQP GSGAGTLART SWPSDLTLYP SISALDSGPS LPDRIKFKPI VERLGLYPVV ADLRLLHSLL ETGAKTIQLR IKEGLADDIE QQICSAIQLG RDYKAKLFIN DHWQLALKHG AYGVHLGQED LYTADLTKIA SAGIALGVSS HSYFELLLAH QIAPSYIALG HIFPTTTKVM PSKPQGLNKL SRYVELLGSH YPLVAIGGID ESKLEAVKHT RVHDIAVVRA ITQAGDPAGA FRMLAQKWEV CNATV // ID B1LNU5_ECOSM Unreviewed; 211 AA. AC B1LNU5; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EcSMS35_4441; OS Escherichia coli (strain SMS-3-5 / SECEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=439855; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SMS-3-5 / SECEC; RX PubMed=18708504; DOI=10.1128/JB.00661-08; RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., RA Ravel J., Stepanauskas R.; RT "Insights into the environmental resistance gene pool from the genome RT sequence of the multidrug-resistant environmental isolate Escherichia RT coli SMS-3-5."; RL J. Bacteriol. 190:6779-6794(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000970; ACB16611.1; -; Genomic_DNA. DR RefSeq; YP_001746377.1; NC_010498.1. DR ProteinModelPortal; B1LNU5; -. DR STRING; 439855.EcSMS35_4441; -. DR EnsemblBacteria; ACB16611; ACB16611; EcSMS35_4441. DR GeneID; 6144216; -. DR KEGG; ecm:EcSMS35_4441; -. DR PATRIC; 18437800; VBIEscCol6161_4559. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL439855:GHHB-4434-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23140 MW; 344C04FF588E42A3 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLVDYP TVAIGGISLP RAPEVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B1LTK8_METRJ Unreviewed; 248 AA. AC B1LTK8; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mrad2831_1959; OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM OS 2831). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=426355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Marx C.J., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM RT 2831."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001001; ACB23954.1; -; Genomic_DNA. DR RefSeq; YP_001754637.1; NC_010505.1. DR ProteinModelPortal; B1LTK8; -. DR STRING; 426355.Mrad2831_1959; -. DR EnsemblBacteria; ACB23954; ACB23954; Mrad2831_1959. DR GeneID; 6137988; -. DR KEGG; mrd:Mrad2831_1959; -. DR PATRIC; 22572246; VBIMetRad70578_2021. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTLLQYR; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MRAD426355:GJB5-1978-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 63 67 HMP-PP binding (By similarity). FT REGION 160 162 THZ-P binding (By similarity). FT REGION 217 218 THZ-P binding (By similarity). FT METAL 96 96 Magnesium (By similarity). FT METAL 115 115 Magnesium (By similarity). FT BINDING 95 95 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 HMP-PP (By similarity). FT BINDING 197 197 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 248 AA; 24822 MW; E8A50EB280B75227 CRC64; MPASATSPAN SPANSPAPSS AAGSRAVDLR LYGLLDVGVC GADGARLAEL GAEAVAGGCT LLQYREKDIA DARAALARIR AILAAVGGRV PVLVNDRVDL ALAAGADGVH LGQSDLHPAD ARRLLGEGAI IGLTLKKPAQ ADELYRLPVD YACIGGVFAT TSKDNPDPPV GLDGFASIAF RARLARGAGL PLGAIAGIGL DNAAAVVAAG ADGVAVITAL FGADSVRQRA HDLRARIDGA LAERAGAR // ID B1LVE6_METRJ Unreviewed; 218 AA. AC B1LVE6; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mrad2831_0580; OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM OS 2831). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=426355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Marx C.J., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM RT 2831."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001001; ACB22591.1; -; Genomic_DNA. DR RefSeq; YP_001753274.1; NC_010505.1. DR ProteinModelPortal; B1LVE6; -. DR STRING; 426355.Mrad2831_0580; -. DR EnsemblBacteria; ACB22591; ACB22591; Mrad2831_0580. DR GeneID; 6136593; -. DR KEGG; mrd:Mrad2831_0580; -. DR PATRIC; 22569390; VBIMetRad70578_0608. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MRAD426355:GJB5-583-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 136 138 THZ-P binding (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 21604 MW; 1D0A2E8950C46288 CRC64; MRALPSPLLT VTDRHGHPRP LAETVQAVLD GGGRWIWFRD KDLEPEARRR LGADVAARVR ALGGFLTVGG DVALARALEA DGAHLGGGAG PEAIAAARSA LGPSALIGVS VHAPREAAAA AQAGADYVTL SPIYATASKP GYGPALGLEG LTDSVGAGLP VVALGGLGPG AVGPCRAAGA AGFAIMGGLM RAADPIEATR ALLKVWGAAE TSAARTAT // ID B1M784_METRJ Unreviewed; 218 AA. AC B1M784; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN OrderedLocusNames=Mrad2831_0155; OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM OS 2831). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=426355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Marx C.J., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM RT 2831."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001001; ACB22182.1; -; Genomic_DNA. DR RefSeq; YP_001752865.1; NC_010505.1. DR ProteinModelPortal; B1M784; -. DR STRING; 426355.Mrad2831_0155; -. DR EnsemblBacteria; ACB22182; ACB22182; Mrad2831_0155. DR GeneID; 6136455; -. DR KEGG; mrd:Mrad2831_0155; -. DR PATRIC; 22568534; VBIMetRad70578_0181. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; MRAD426355:GJB5-157-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 218 AA; 22387 MW; B93010F9F6695348 CRC64; MPVSMSNSAR LALLGPHGLE AEGIAAFVTA LKVACEAGDV AAVILRLAAT DERGLTARVK SVAPLVQERG AALVVACPGF AGDLAAVAIR GGADGIHVDK PRDLKDLRGR LREGRILGAG GLETKHGAME AGEAGIDYLM FGGLYPDGVA PEAETVRARA AWWAEIFETP CIAVAAAADE IAPLAATGAE FVGLESGLWL PDPGAVERAQ RAVRESEA // ID B1MIS1_MYCA9 Unreviewed; 223 AA. AC B1MIS1; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MAB_4219; OS Mycobacterium abscessus (strain ATCC 19977 / DSM 44196). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium abscessus. OX NCBI_TaxID=561007; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19977 / DSM 44196; RG Genoscope; RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., RA Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., RA Gaillard J.L.; RT "Acquisition of foreign virulence genes by the cystic fibrosis RT pathogen Mycobacterium abscessus."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU458896; CAM64292.1; -; Genomic_DNA. DR RefSeq; YP_001704946.1; NC_010397.1. DR ProteinModelPortal; B1MIS1; -. DR STRING; 561007.MAB_4219; -. DR EnsemblBacteria; CAM64292; CAM64292; MAB_4219. DR GeneID; 5966681; -. DR KEGG; mab:MAB_4219; -. DR PATRIC; 17980266; VBIMycAbs55940_4298. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MABS561007:GJTG-4238-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23550 MW; 4D250B3D6D90B106 CRC64; MHSRSARLQS AHLYLCTDAR RERGDFAEFV DAALAGGVDI VQLRDKGSAG ERQFGRLEPA EELEYLAILS EAAARHGALF AVNDRADIAR AAGADVLHLG QDDLPLAVAR EIVGPDVLIG RSTHDAEQAA AAARDDEIDY FCCGPCWPTP TKPGRTASGL GLVRTAAELD TSKPWFAIGG IDEARVPQVV EAGASRIVVV RAITAAADPR AAAASLRGST RRA // ID B1Q5P8_CLOBO Unreviewed; 205 AA. AC B1Q5P8; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CBN_0480; OS Clostridium botulinum NCTC 2916. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=445335; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 2916; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium botulinum NCTC 2916."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDO02000001; EDT82358.1; -; Genomic_DNA. DR ProteinModelPortal; B1Q5P8; -. DR EnsemblBacteria; EDT82358; EDT82358; CBN_0480. DR PATRIC; 26438535; VBICloBot30358_0398. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22421 MW; C1251A32D1585842 CRC64; MEINYELYLI TDRRFLKGRQ LKKIVEDAIL GGVTIVQVRE KDVSTREFYN VAKEVKEVTD YYKVPIIIND RLDIAQAIDA SGVHLGQKDM HLNIAREILG KDKIIGISVG NVKEALEAQN NGADYLGIGT IFPTGSKKDV DAIIGIDGLS KIKDSISIPS VAIGGINKTN FKDVLKTGIE GISVISAILD EDDIKLAANN LLINK // ID B1QG40_CLOBO Unreviewed; 205 AA. AC B1QG40; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CBB_0482; OS Clostridium botulinum Bf. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=445336; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Bf; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium botulinum Bf."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Bf; RA Harkins D.M., Shrivastava S., Brinkac L.M., Durkin A.S., Sutton G.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDP01000001; EDT87282.1; -; Genomic_DNA. DR ProteinModelPortal; B1QG40; -. DR EnsemblBacteria; EDT87282; EDT87282; CBB_0482. DR PATRIC; 26411164; VBICloBot44891_0098. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22434 MW; 3841EBA6E001F1C7 CRC64; MEINYELYLI TDRRFLKGRQ LKKVVEDAIL GGVTIVQVRE KDVSTKEFYN VAKEVKEVTD YYRVPIIIND RLDIAQAIDA NGVHLGQKDM HLNIAREILG KDKIIGISVG NVKEALEAQN NGADYLGIGT IFPTGSKKDV DAIIGIDGLS KIKDSISIPS VAIGGINKTN FKDVLKTGIE GISVISAILD EDDIKLAANN LLINK // ID B1QZC6_CLOBU Unreviewed; 210 AA. AC B1QZC6; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CBY_1703; OS Clostridium butyricum 5521. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=447214; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5521; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium butyricum 5521."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDT01000092; EDT74704.1; -; Genomic_DNA. DR ProteinModelPortal; B1QZC6; -. DR EnsemblBacteria; EDT74704; EDT74704; CBY_1703. DR PATRIC; 26451175; VBICloBut117397_2725. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; D18E32489B35C17B CRC64; MKPKIDYSIY LVTDRDLMST ETLEEAVEEA IKGGCTLVQL REKDCSSLDF YNTAINLKRI TDKYNVPLLI NDRLDIALAV DAAGVHIGQS DLPCSVVRKV IGEDKIIGVS AGTLENAIKA ENDGADYIGV GAMYETGTKK DAKHTSMDEL KKIRENISIP IVVIGGINKE RITNFNGTDI DGLAIVSAII SQKDIYKATS ELKDLFFKLK // ID B1R0H1_CLOBU Unreviewed; 213 AA. AC B1R0H1; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 23. DE SubName: Full=Regulatory protein teni; GN ORFNames=CBY_3722; OS Clostridium butyricum 5521. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=447214; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5521; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium butyricum 5521."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDT01000097; EDT74169.1; -; Genomic_DNA. DR ProteinModelPortal; B1R0H1; -. DR EnsemblBacteria; EDT74169; EDT74169; CBY_3722. DR PATRIC; 26452016; VBICloBut117397_3132. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 213 AA; 23885 MW; B1E5AB0AD50C8BA7 CRC64; MYNILAITNR HLCKGDFLEQ IKKICLYNNK IQHMNSSKNY NKKSVNNISS ISIVLREKDL NERDYELLAS KVIRICEEYN TECILHTYYN VARKLGCSKI HLPLHILKSK PYIAEIFDVV GVSIHSVGDA LDAKNMNVTY VTAGHIFNTD CKKDIPARGL AFLNNIVNSV DIPVFAIGGI ASSNIGSVIN YGAFGVCIMS GFMNIENPED FFL // ID B1R4X9_CLOPF Unreviewed; 193 AA. AC B1R4X9; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=Thiamine monophosphate synthase family protein; GN ORFNames=AC1_1999; OS Clostridium perfringens B str. ATCC 3626. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=451754; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 3626; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium perfringens B str. ATCC 3626."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDV01000004; EDT24719.1; -; Genomic_DNA. DR ProteinModelPortal; B1R4X9; -. DR EnsemblBacteria; EDT24719; EDT24719; AC1_1999. DR PATRIC; 30611237; VBICloPer46771_0723. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 193 AA; 22057 MW; 2DD19491AE73B987 CRC64; MFLITNRKLV NREKYFNTIE EAGKYGVKNI ILREKDLSTE ELIEVYIKIR DLVPEETNII INSNIEATRI LKEKFIHLSF KDFKRNLEEV KSLEVGVSVH SILEAIEADR LGASYILVSP IFETQCKKDV TPKGINFIKE IKEKVNCKVI ALGGINELNF KEVLGAGADD FACMSLLFMS NNIKKSLYTF KAF // ID B1RBY2_CLOPF Unreviewed; 207 AA. AC B1RBY2; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AC1_1730; OS Clostridium perfringens B str. ATCC 3626. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=451754; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 3626; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium perfringens B str. ATCC 3626."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDV01000049; EDT22262.1; -; Genomic_DNA. DR ProteinModelPortal; B1RBY2; -. DR EnsemblBacteria; EDT22262; EDT22262; AC1_1730. DR PATRIC; 30616597; VBICloPer46771_3282. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 23005 MW; 8C1138BEB1EF9AD6 CRC64; MINKDYKKLY LVTDYRIPFN ELLEKTKEAL IGGVSIVQYR AKNKKTKEMC KEAKELKKLC DEFGALFLVN DRIDVALAVK ANGVHIGQDD MEVFIAREIM PKDAVIGVTV HNKEEALKAI KEGADNLGVG ALFSTNSKDD ATLMTLETLR EIKSVSNIPL YGIGGITPYN LNKDILENLD GVAVISALLN SDNIREKSKE FLNILSK // ID B1RG13_CLOPF Unreviewed; 193 AA. AC B1RG13; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=Thiamine monophosphate synthase family protein; GN ORFNames=AC5_1970; OS Clostridium perfringens CPE str. F4969. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=451756; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F4969; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium perfringens CPE str. F4969."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDX01000008; EDT27076.1; -; Genomic_DNA. DR ProteinModelPortal; B1RG13; -. DR EnsemblBacteria; EDT27076; EDT27076; AC5_1970. DR PATRIC; 30626740; VBICloPer69736_1375. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 193 AA; 21963 MW; 53D8897C1AD16152 CRC64; MFLITNRKLV NREKYFNTIE EAGKYGVKNI ILREKDLSTK ELIKIYIKIK ELVPEETNII INSNIEATMI LKEKFIHLSF KDFKRNLEEV KSLQVGVSVH SILEAIEADR LGASYILVSP IFETQCKKGV TPKGINFIKE IKEKVNCNVI ALGGINEHNF KEVLGAGADD FACMSLLFMS NNIKKSLYTF KSL // ID B1RKH0_CLOPF Unreviewed; 207 AA. AC B1RKH0; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AC5_1645; OS Clostridium perfringens CPE str. F4969. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=451756; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F4969; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium perfringens CPE str. F4969."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDX01000046; EDT25535.1; -; Genomic_DNA. DR ProteinModelPortal; B1RKH0; -. DR EnsemblBacteria; EDT25535; EDT25535; AC5_1645. DR PATRIC; 30630242; VBICloPer69736_2996. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22794 MW; ADE9A2301814122F CRC64; MSNKDTKKLY LVTDYRIPFN ELLEKTKEAL IGGVSIVQYR AKNKKTKEMC KEAKELKKLC DDFGALFLVN DRIDVALAVK ANGVHIGQDD MEVSIAREIM PKDAVIGVTV HNKEEALKAI KEGADNLGVG ALFSTNSKDD ATLMTLETLR EIKSVSNIPL YGIGGIAPEK LNKDILENLD GVAVISSLLN SDNIREKSNE FLNILSK // ID B1RSX9_CLOPF Unreviewed; 193 AA. AC B1RSX9; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=Thiamine monophosphate synthase family protein; GN ORFNames=AC7_1851; OS Clostridium perfringens NCTC 8239. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=451757; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 8239; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium perfringens NCTC 8239."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDY01000022; EDT77449.1; -; Genomic_DNA. DR ProteinModelPortal; B1RSX9; -. DR EnsemblBacteria; EDT77449; EDT77449; AC7_1851. DR PATRIC; 27218227; VBICloPer21751_2462. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 193 AA; 22034 MW; E4DD6736D92BE12F CRC64; MFLITNRKLV NREKYFNTIE EAGKYGVKNI ILREKDLSTE ELIEVYIKIK ELVPEETNII INSNIEAARI LKEKFIHLSF KDFKRNLEEV KSLQVGVSVH SILEALEADR LGASYILVSP IFETQCKKDV TPKEINFIKE IKEKVNCKVI ALGGINELNF KEVLGAGADD FACMSLLFMS NNIKKCLDTF KSL // ID B1RTM6_CLOPF Unreviewed; 207 AA. AC B1RTM6; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AC7_1595; OS Clostridium perfringens NCTC 8239. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=451757; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 8239; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium perfringens NCTC 8239."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDY01000033; EDT77193.1; -; Genomic_DNA. DR ProteinModelPortal; B1RTM6; -. DR EnsemblBacteria; EDT77193; EDT77193; AC7_1595. DR PATRIC; 27218774; VBICloPer21751_2710. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 23005 MW; 8C1138BEB1EF9AD6 CRC64; MINKDYKKLY LVTDYRIPFN ELLEKTKEAL IGGVSIVQYR AKNKKTKEMC KEAKELKKLC DEFGALFLVN DRIDVALAVK ANGVHIGQDD MEVFIAREIM PKDAVIGVTV HNKEEALKAI KEGADNLGVG ALFSTNSKDD ATLMTLETLR EIKSVSNIPL YGIGGITPYN LNKDILENLD GVAVISALLN SDNIREKSKE FLNILSK // ID B1RZH8_STREE Unreviewed; 209 AA. AC B1RZH8; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; ORFNames=SP187300_0795; OS Streptococcus pneumoniae CDC1873-00. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=453362; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC1873-00; RA Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., RA Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H.; RT "Genome Sequence of Streptococcus pneumoniae CDC1873-00."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFS01000001; EDT51791.1; -; Genomic_DNA. DR ProteinModelPortal; B1RZH8; -. DR EnsemblBacteria; EDT51791; EDT51791; SP187300_0795. DR PATRIC; 28626849; VBIStrPne101151_0368. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID B1RZI4_STREE Unreviewed; 210 AA. AC B1RZI4; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; ORFNames=SP187300_0802; OS Streptococcus pneumoniae CDC1873-00. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=453362; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC1873-00; RA Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., RA Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H.; RT "Genome Sequence of Streptococcus pneumoniae CDC1873-00."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFS01000001; EDT51812.1; -; Genomic_DNA. DR ProteinModelPortal; B1RZI4; -. DR EnsemblBacteria; EDT51812; EDT51812; SP187300_0802. DR PATRIC; 28626863; VBIStrPne101151_0375. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID B1S733_9BIFI Unreviewed; 855 AA. AC B1S733; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE SubName: Full=Thiamine biosynthesis family protein; GN ORFNames=BIFDEN_01574; OS Bifidobacterium dentium ATCC 27678. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=473819; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27678; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bifidobacterium dentium (ATCC 27678)."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27678; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIX02000002; EDT45737.1; -; Genomic_DNA. DR ProteinModelPortal; B1S733; -. DR EnsemblBacteria; EDT45737; EDT45737; BIFDEN_01574. DR PATRIC; 27211441; VBIBifDen119025_1347. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 855 AA; 94608 MW; F5D0FE02605A01E4 CRC64; MNDYPYASMR DCFDMSAYFV VGPQDCKGRP ITDVVDDALR GGATFIQLRA KNTDAKDLTL MAQDIAQIIE DNGKSDAVAF VIDDRVDVVW QARNKGIKVD GVHIGQTDME PREARALLGE EAIVGLSAET ESLVRLINEL PNGCIDYIGA GPLHVSTTKP EASVGGNDGS GNTLDEDQIN TICTASDFPV VVGGGVTADD MEMLARSKAA GWFVVSAIAG ADDPEAATRE MVTRWKAVRG ETKHGFAPRV QSADTATTTD TQMTESNNGK FTNAKEAKAS SKLAKQQRVD IAARGSKQRD KAHVRKTTPV HFENRFGSYD LEVPYTEIKL SDTPGVGPNA PFKDYNTEGP KCDPKEGLAP LRLDWIRDRG DVEEYEGRRR NLEDDGKRAI KRGKASKEWR GRQHKPLKAK DHPITQMWYA RHDIITPEMR YVAEREHCDV ELVRSELAAG RAVMPCNINH PEAEPMIIGS RFLTKLNANM GNSAVTSSID EEVEKLTWAT KWGADTVMDL STGNDIHTTR EWILRNSPVP IGTVPMYQAL EKVEDDASKL SWELFRDTVI EQCEQGVDYM TIHAGVLLRF VPLTANRMTG IVSRGGSIMA EWCLQHHQES FLYTHFDELC EIFAKYDVAF SLGDGLRPGS LADANDAAQF AELMTLGELT QRAWEHDVQV MIEGPGHIPF DTVRMNIEME KAICKDAPFY TLGPLTTDTA PGYDHITSAI GGVEIARYGT AMLCYVTPKE HLGLPNKDDV KQGVIAYKIA CHAADIAKHH PHAIDRDNAM SKARFEFRWL DQFNLSYDPD TAIAFHDDTL PAEPAKMAHF CSMCGPKFCS MAISQNIRRK FGNAEAQEKL VADAQ // ID B1SEV2_9STRE Unreviewed; 210 AA. AC B1SEV2; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=STRINF_01366; OS Streptococcus infantarius subsp. infantarius ATCC BAA-102. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=471872; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-102; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Streptococcus infantarius subsp. infantarius RT ATCC BAA-102."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-102; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABJK02000020; EDT47569.1; -; Genomic_DNA. DR ProteinModelPortal; B1SEV2; -. DR EnsemblBacteria; EDT47569; EDT47569; STRINF_01366. DR PATRIC; 25726978; VBIStrInf64650_1129. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22848 MW; EA93C96F0241340F CRC64; MNKEQLQVYF ICGTPNCPKG KFLDILEAAF KSGVTCFQFR EKGQGALSGQ EKKELALNVK SLCRKYHVLF FINDDIDLAL EIGVDGVHLG QDDMPVREAR KLFPDKLIGL SVGNAKEYHL SAIDVVDYIG VGPIFPTSSK SDAGQVIGLN GLREMRELDK DIPIVAIGGI TFGDVAAIRQ SGADGVAIIS AIAQSKEVEL DTQRFARAFD // ID B1TDJ2_9BURK Unreviewed; 194 AA. AC B1TDJ2; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 23. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=BamMEX5DRAFT_5858; OS Burkholderia ambifaria MEX-5. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=396597; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MEX-5; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Tiedje J., Richardson P.; RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria RT MEX-5."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABLK01000294; EDT38365.1; -; Genomic_DNA. DR ProteinModelPortal; B1TDJ2; -. DR EnsemblBacteria; EDT38365; EDT38365; BamMEX5DRAFT_5858. DR PATRIC; 38391613; VBIBurAmb126694_5919. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 20026 MW; C63CA21E2C79A7DF CRC64; MSATLPRCCV ITPEPASASA ADCRAFLDRL SAVLARGDTL VQLRVKSFDA AAFARLAADA LARCTAAGAQ LMLNGPIDAA GVMQLDGAGW HLDSAALRAV AQRPLPAARR VSAACHAADD LVLAARAGVD FVTLSPVLPT LSHPGAPTLG WTRFAALAAQ AAMPVYALGG MTRAHLDDAR RHGAYGVAGI RSFW // ID B1TF02_9BURK Unreviewed; 100 AA. AC B1TF02; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 22. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Precursor; GN ORFNames=BamMEX5DRAFT_6368; OS Burkholderia ambifaria MEX-5. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=396597; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MEX-5; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Tiedje J., Richardson P.; RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria RT MEX-5."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABLK01000370; EDT37854.1; -; Genomic_DNA. DR ProteinModelPortal; B1TF02; -. DR EnsemblBacteria; EDT37854; EDT37854; BamMEX5DRAFT_6368. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Signal. FT SIGNAL 1 27 Potential. FT CHAIN 28 100 Potential. FT /FTId=PRO_5000328761. SQ SEQUENCE 100 AA; 10286 MW; CD8DB4DEE1C556B6 CRC64; MLRALHERPS YLALGPVYAT ATKAVAAPPQ GLARIARYAR FAGARAPLVA IGGVGLDALP DVLATGVGSV AVVSAITGAI DYRAAVVALQ QCFARQFDNH // ID B1UW08_BACAN Unreviewed; 219 AA. AC B1UW08; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BAO_0371; OS Bacillus anthracis str. A0174. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=486622; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A0174; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Brettin T.S.; RT "Genome sequence of Bacillus anthracis A0174."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABLT01000026; EDT65712.1; -; Genomic_DNA. DR ProteinModelPortal; B1UW08; -. DR SMR; B1UW08; 1-215. DR EnsemblBacteria; EDT65712; EDT65712; BAO_0371. DR PATRIC; 24587222; VBIBacAnt86373_4727. DR OMA; QFREKGP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23600 MW; 6D85F0FE3EFD3046 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGFI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWVIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID B1UW79_BACAN Unreviewed; 206 AA. AC B1UW79; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-MAR-2014, entry version 27. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BAO_0757; OS Bacillus anthracis str. A0174. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=486622; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A0174; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Brettin T.S.; RT "Genome sequence of Bacillus anthracis A0174."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABLT01000028; EDT65617.1; -; Genomic_DNA. DR ProteinModelPortal; B1UW79; -. DR EnsemblBacteria; EDT65617; EDT65617; BAO_0757. DR PATRIC; 24587436; VBIBacAnt86373_4811. DR OMA; ELVNVAM; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID B1V4T8_CLOPF Unreviewed; 193 AA. AC B1V4T8; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=Thiamine monophosphate synthase family protein; GN ORFNames=CJD_2170; OS Clostridium perfringens D str. JGS1721. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=488537; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JGS1721; RA Paulsen I., Sebastian Y.; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABOO01000027; EDT71182.1; -; Genomic_DNA. DR ProteinModelPortal; B1V4T8; -. DR EnsemblBacteria; EDT71182; EDT71182; CJD_2170. DR PATRIC; 30635242; VBICloPer13534_2238. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 193 AA; 22032 MW; 735151A4F6F2C02A CRC64; MFLITNRKLV NREKYFNTIK EAGKYGVKNI ILREKDLSTE ELIEVYIKIR DLVPEETNII INSNIEAARI LKEKFIHLSF NDFKRNLEEI KFLKVGVSVH SILEALEADR LGASYILVSP IFETQCKKDV TPKGIDFIKE IKEKVNCRVI ALGGINELNF KEVLGAGADD FACMSLLFMS NNIKKSLDTF KAL // ID B1V7L2_CLOPF Unreviewed; 207 AA. AC B1V7L2; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CJD_1786; OS Clostridium perfringens D str. JGS1721. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=488537; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JGS1721; RA Paulsen I., Sebastian Y.; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABOO01000067; EDT70202.1; -; Genomic_DNA. DR ProteinModelPortal; B1V7L2; -. DR EnsemblBacteria; EDT70202; EDT70202; CJD_1786. DR PATRIC; 30637484; VBICloPer13534_3287. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22945 MW; 2C0F931EA1FF4067 CRC64; MINKDYKKLY LVTDYRIPFN ELLEKTKEAL IGGVSIVQYR AKNKKTKEMC KEAKELKKLC DEFGALFLVN DRIDVALAVK ANGVHIGQDD MEVSIAREIM PKDAVIGVTV HNKEEALKAI KDGADNLGVG ALFSTNSKDD ATLMTLETLR EIKSVSNIPL YGIGGITPYN LNKDILENLE GVAVISALLN SDNIREKSKE FLNILSK // ID B1VH23_CORU7 Unreviewed; 286 AA. AC B1VH23; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=cu1104; OS Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=504474; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43042 / DSM 7109; RX PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009; RA Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A., RA Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., RA Kalinowski J., Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., RA Soriano F., Droege M., Puehler A.; RT "The lifestyle of Corynebacterium urealyticum derived from its RT complete genome sequence established by pyrosequencing."; RL J. Biotechnol. 136:11-21(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM942444; CAQ05064.1; -; Genomic_DNA. DR RefSeq; YP_001800498.1; NC_010545.1. DR ProteinModelPortal; B1VH23; -. DR STRING; 504474.cur_1104; -. DR EnsemblBacteria; CAQ05064; CAQ05064; cu1104. DR GeneID; 6186164; -. DR KEGG; cur:cur_1104; -. DR PATRIC; 21521960; VBICorUre58120_1104. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; RPTPTKN; -. DR OrthoDB; EOG6PZXB0; -. DR BioCyc; CURE504474:GJ8Y-1132-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 104 108 HMP-PP binding (By similarity). FT REGION 209 211 THZ-P binding (By similarity). FT METAL 139 139 Magnesium (By similarity). FT METAL 162 162 Magnesium (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 181 181 HMP-PP (By similarity). FT BINDING 212 212 HMP-PP (By similarity). SQ SEQUENCE 286 AA; 30133 MW; BD0EFE98D1CA02AE CRC64; MPTRTSSRQS RLAWTKSPLS SWNVAGRSTW RMMRVCNTVD NGGDQPGAGP AQGAQAVTPR ALDPRSLTCY LVTGRIPDLD WDEECEEITR IAAEAAAGGA GVIQVRSKPI TVRQLTELSI RIAAAVAETN PRTLVLIDDR VDVAAALMTE HNIHGVHIGQ DDLDPRLARA VLGDDAIIGL TTGTLELVED ANAYADVIDY VGAGPYRPTP TKNSGRDPLG LEGYPALVTA SEVPVVAIGD VRAEDAADLA ATGVAGLAIV RGIMQAEDPK AYAASVISQF SGANER // ID B1VZV2_STRGG Unreviewed; 227 AA. AC B1VZV2; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SGR_5398; OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=455632; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 4626 / NBRC 13350; RX PubMed=18375553; DOI=10.1128/JB.00204-08; RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H., RA Yamashita A., Hattori M., Horinouchi S.; RT "Genome sequence of the streptomycin-producing microorganism RT Streptomyces griseus IFO 13350."; RL J. Bacteriol. 190:4050-4060(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009493; BAG22227.1; -; Genomic_DNA. DR RefSeq; YP_001826910.1; NC_010572.1. DR ProteinModelPortal; B1VZV2; -. DR STRING; 455632.SGR_5398; -. DR EnsemblBacteria; BAG22227; BAG22227; SGR_5398. DR GeneID; 6210706; -. DR KEGG; sgr:SGR_5398; -. DR PATRIC; 23757569; VBIStrGri32265_5528. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SGRI455632:GD3A-5469-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 53 57 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 24065 MW; AA29150CAE092CF7 CRC64; MHRHDHGGVP PMSTPREQLS DARLYLCTDA RTRQGDLPAF LDAVLAAGVD IVQLRDKGME AAEELEHLAV FADACRRHGK LLAVNDRADV AHAVGADVLH LGQGDLPVPA ARAIIGSDRL IGRSTHAEAE VDAALAQDGV DYFCTGPCWP TPTKPGRHAP GLDLVRYTAS LGGARPWFAI GGIDTGNLDQ VLDAGARRVV VVRAVTEADD PAAATAELAR RVRARAL // ID B1WWA6_CYAA5 Unreviewed; 360 AA. AC B1WWA6; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=cce_4686; OS Cyanothece sp. (strain ATCC 51142). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=43989; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51142; RX PubMed=18812508; DOI=10.1073/pnas.0805418105; RA Welsh E.A., Liberton M., Stockel J., Loh T., Elvitigala T., Wang C., RA Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., RA Ghosh B.K., Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.; RT "The genome of Cyanothece 51142, a unicellular diazotrophic RT cyanobacterium important in the marine nitrogen cycle."; RL Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000806; ACB54034.1; -; Genomic_DNA. DR RefSeq; YP_001806100.1; NC_010546.1. DR ProteinModelPortal; B1WWA6; -. DR STRING; 43989.cce_4686; -. DR EnsemblBacteria; ACB54034; ACB54034; cce_4686. DR GeneID; 6171764; -. DR KEGG; cyt:cce_4686; -. DR PATRIC; 21547698; VBICyaSp130209_4653. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CSP43989:GKC8-4741-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 142 Unknown (By similarity). FT REGION 143 360 Thiamine-phosphate synthase (By FT similarity). FT REGION 190 194 HMP-PP binding (By similarity). FT REGION 287 289 THZ-P binding (By similarity). FT METAL 223 223 Magnesium (By similarity). FT METAL 242 242 Magnesium (By similarity). FT BINDING 222 222 HMP-PP (By similarity). FT BINDING 261 261 HMP-PP (By similarity). FT BINDING 290 290 HMP-PP (By similarity). FT BINDING 317 317 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 360 AA; 41079 MW; 8F8D14E56773E2ED CRC64; MRYLVTHLRP MKIISRYCQE NMDKNLAIFR ILDANLDRAR EGLRVVEEWC RLGLENSDWA EKCKQMRQEI AYWHTSELRM ARDTPNDPGI QISHPQEEKR ETINQLLQAN LCRVQEALRV LEEYGKLYDG NMGTACKKIR YQVYTLESEL LQNYRYQKLK QSPLYLVTSS RENFLKIVES ALQGGLTLLQ YREKKIDDIV RLEMAQKLCE LCHQYDALFI VNDRVDIALA VNADGVHLGQ QDIPIALARR ILGPNKIIGR STTNPQEMEK AIAEKADYIG VGPVYATPTK PDKKAAGLDY VKYAAETSSI PWFAIGGIDE TNMTEVIASG ATQVALVRAI MEADDPQKTT QKLLKILTVK // ID B1XBZ6_ECODH Unreviewed; 211 AA. AC B1XBZ6; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECDH10B_4182; OS Escherichia coli (strain K12 / DH10B). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=316385; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / DH10B; RX PubMed=18245285; DOI=10.1128/JB.01695-07; RA Durfee T., Nelson R., Baldwin S., Plunkett G.III., Burland V., Mau B., RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., RA Posfai G., Weinstock G.M., Blattner F.R.; RT "The complete genome sequence of Escherichia coli DH10B: insights into RT the biology of a laboratory workhorse."; RL J. Bacteriol. 190:2597-2606(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000948; ACB04996.1; -; Genomic_DNA. DR RefSeq; YP_001732774.1; NC_010473.1. DR ProteinModelPortal; B1XBZ6; -. DR SMR; B1XBZ6; 20-202. DR STRING; 316385.ECDH10B_4182; -. DR EnsemblBacteria; ACB04996; ACB04996; ECDH10B_4182. DR GeneID; 6062414; -. DR KEGG; ecd:ECDH10B_4182; -. DR PATRIC; 18468363; VBIEscCol59506_4210. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL316385:GJ8B-4003-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B1XMV2_SYNP2 Unreviewed; 355 AA. AC B1XMV2; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SYNPCC7002_A0279; OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum OS quadruplicatum). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=32049; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27264 / PCC 7002 / PR-6; RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., RA Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.; RT "Complete sequence of Synechococcus sp. PCC 7002."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000951; ACA98289.1; -; Genomic_DNA. DR RefSeq; YP_001733545.1; NC_010475.1. DR ProteinModelPortal; B1XMV2; -. DR STRING; 32049.SYNPCC7002_A0279; -. DR EnsemblBacteria; ACA98289; ACA98289; SYNPCC7002_A0279. DR GeneID; 6055891; -. DR KEGG; syp:SYNPCC7002_A0279; -. DR PATRIC; 23814994; VBISynSp37135_0460. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSP32049:GKF7-279-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 126 Unknown (By similarity). FT REGION 127 355 Thiamine-phosphate synthase (By FT similarity). FT REGION 174 178 HMP-PP binding (By similarity). FT REGION 271 273 THZ-P binding (By similarity). FT METAL 207 207 Magnesium (By similarity). FT METAL 226 226 Magnesium (By similarity). FT BINDING 206 206 HMP-PP (By similarity). FT BINDING 245 245 HMP-PP (By similarity). FT BINDING 274 274 HMP-PP (By similarity). SQ SEQUENCE 355 AA; 39730 MW; F2E7008F36667DDE CRC64; MVKPASTDTT AIFRILDANL DRAREGLRIV EEWFRFGLNH AELAARCKEM RQTLAQWHHD ELRAARDTPN DVGTSLSHPQ EETRTDLNHL LRANLCRVEE ALRVLEEYAK LYKTEMAIAC KQMRYQVYTL ESQLFSPQLK QRLEKARLYL VTSPHEELLA VTEAALQGGV EIVQYRDKET PDEQRFANAI ALKKLCDRYH ALFLVNDRVD LALAVDADGV HLGQTDLPIA TARQLIGPDK IIGRSTTNPQ ELEKALREGA DYVGVGPVYE TPTKPGKAAA GHSYVSYARE TCPVPWFAIG SIDTENLGEV LAAGAERVAV VRALMQSAEP TLTAQFFAAQ LHRQQTLQNL EEATA // ID B1XUW4_POLNS Unreviewed; 88 AA. AC B1XUW4; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 16-APR-2014, entry version 31. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=Pnec_0949; OS Polynucleobacter necessarius subsp. necessarius (strain STIR1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Polynucleobacter. OX NCBI_TaxID=452638; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=STIR1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Hahn M., RA Richardson P.; RT "Complete sequence of Polynucleobacter necessarius STIR1."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001010; ACB44141.1; -; Genomic_DNA. DR RefSeq; YP_001797755.1; NC_010531.1. DR STRING; 452638.Pnec_0949; -. DR EnsemblBacteria; ACB44141; ACB44141; Pnec_0949. DR GeneID; 6184358; -. DR KEGG; pne:Pnec_0949; -. DR PATRIC; 22970982; VBIPolNec8289_1099. DR KO; K00788; -. DR BioCyc; PNEC452638:GI4T-962-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 88 AA; 9258 MW; 977B00AFE26FEFB2 CRC64; MSLIRDLADQ IVAAHRNADL CIPIPTFSLN TPPPQIDNEA AVDQLVAIGG INQDSIHAVA RSGVGSVAGV RAITQAKNPR DAVKHLKN // ID B1Y3E3_LEPCP Unreviewed; 220 AA. AC B1Y3E3; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Lcho_2205; OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix OS discophora (strain SP-6)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Leptothrix. OX NCBI_TaxID=395495; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51168 / LMG 8142 / SP-6; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Emerson D., Richardson P.; RT "Complete sequence of Leptothrix cholodnii SP-6."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001013; ACB34471.1; -; Genomic_DNA. DR RefSeq; YP_001791236.1; NC_010524.1. DR ProteinModelPortal; B1Y3E3; -. DR STRING; 395495.Lcho_2205; -. DR EnsemblBacteria; ACB34471; ACB34471; Lcho_2205. DR GeneID; 6163307; -. DR KEGG; lch:Lcho_2205; -. DR PATRIC; 22394787; VBILepCho83238_2229. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LCHO395495:GHYL-2240-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22405 MW; 7F1D5DB72F8D9E4A CRC64; MADRLPTRWQ PRHALCLVTD GSLCAPRTLV EVVSAALQGG VGMVQLREKK LDSRAFVERA RAIQALTASA GVPLVINDRL DIALVVGADG LHVGQSDLSV ADVRLWLPDA LVGLSIESMA DLLAAPAGVD YLGVSPVFAT ATKADAAAAL GLEGLAAIRA ATRLPLVAIG GIGAHNARAV LRHGADSLAV VSAICAAADP RAAAAELAGC IESESNSRPS // ID B1Y5I7_LEPCP Unreviewed; 613 AA. AC B1Y5I7; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 39. DE SubName: Full=Phosphomethylpyrimidine kinase type-1; GN OrderedLocusNames=Lcho_2434; OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix OS discophora (strain SP-6)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Leptothrix. OX NCBI_TaxID=395495; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51168 / LMG 8142 / SP-6; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Emerson D., Richardson P.; RT "Complete sequence of Leptothrix cholodnii SP-6."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001013; ACB34699.1; -; Genomic_DNA. DR RefSeq; YP_001791464.1; NC_010524.1. DR ProteinModelPortal; B1Y5I7; -. DR STRING; 395495.Lcho_2434; -. DR EnsemblBacteria; ACB34699; ACB34699; Lcho_2434. DR GeneID; 6163640; -. DR KEGG; lch:Lcho_2434; -. DR PATRIC; 22395237; VBILepCho83238_2452. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; RYQDTHD; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; LCHO395495:GHYL-2471-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 613 AA; 62955 MW; 1EB1277EE2BFCCE9 CRC64; MQAANPNTNT STDLDTPPGA TRRPIVWSIS SNDASGAAGL SADARVAAAF GVHLCPIVAC VTSQNSLSIE HITPISATLL DAQLDTLAAD MPPDAIKTGM LGSAELVAVV ARWVDRLRRR NPHLPLVVDP MLRAGTGTGS AFADALLLAA YQDDLLPRAT VITPNRREAR ALLDHDDSGN LPIQPDAVAP RGTDHAAVAA RLGPAPELAA VPAMARALRA AGAKAVCITG GHGDDNGSDS TAHNPAGLVL DWLDSELAQG WIALPKVETR NYRGSGNTHA TALAAALARG FVDADAAVLA KMASTAALRH GYAAGAGVGP VGTAEGFITD ASLLPRMSWG NDAQALAIAA AGTATAGQPL RSGYYALVDD ATRIPAILAA ASSDLCALQL RIKREAHSDL DDAAFQDHVQ TQIAGAAAQL RGSAIALIVN DHWPTAAAAL ARRGDALAGV ELGVHLGQAD LEILGPDGRA ALRQAVTGQQ PGAAPLALGI SSHSLWELAR AASLAPSYIA CGPVWPTLTK AMPWRAQGLD NLRWWSAMAP APVVAIGGVL QPDQARDCVA AGASAVCLVR ALDGDALAGW PAWREAWQRG REATATQPAV AWPHPSLDAA TAH // ID B1YER9_EXIS2 Unreviewed; 198 AA. AC B1YER9; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 37. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Exig_1198; OS Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15). OC Bacteria; Firmicutes; Bacilli; Bacillales; OC Bacillales Family XII. Incertae Sedis; Exiguobacterium. OX NCBI_TaxID=262543; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17290 / JCM 13490 / 255-15; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., RA Monk C., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Vishnivetskaya T., Rodrigues D.F., Gilichinsky D., Tiedje J., RA Richardson P.; RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255- RT 15."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001022; ACB60677.1; -; Genomic_DNA. DR RefSeq; YP_001813694.1; NC_010556.1. DR ProteinModelPortal; B1YER9; -. DR STRING; 262543.Exig_1198; -. DR EnsemblBacteria; ACB60677; ACB60677; Exig_1198. DR GeneID; 6174721; -. DR KEGG; esi:Exig_1198; -. DR PATRIC; 32135983; VBIExiSib53410_1217. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ESIB262543:GHBP-1274-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 198 AA; 21598 MW; E122E236383418BC CRC64; MTQLHLLTTG QQGWETLEHT LPELAMRVDR IHLREPLWSA RELVTCIEFL MKCGVPAERL IVHDRLDVAL VTGIGIQLTT RSIPVDRVRS RFPELRIGQS VHSLTEAAAA EQAGADYVMY GHIFETGSKP GVPPRGLHAL KQIVEQVSIP VIAIGGIKPG NVQEVIATGC SGVAVLSGIL GQANSLKAAD RFREVMQR // ID B1YJJ3_EXIS2 Unreviewed; 212 AA. AC B1YJJ3; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Exig_0542; OS Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15). OC Bacteria; Firmicutes; Bacilli; Bacillales; OC Bacillales Family XII. Incertae Sedis; Exiguobacterium. OX NCBI_TaxID=262543; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17290 / JCM 13490 / 255-15; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., RA Monk C., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Vishnivetskaya T., Rodrigues D.F., Gilichinsky D., Tiedje J., RA Richardson P.; RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255- RT 15."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001022; ACB60023.1; -; Genomic_DNA. DR RefSeq; YP_001813040.1; NC_010556.1. DR ProteinModelPortal; B1YJJ3; -. DR STRING; 262543.Exig_0542; -. DR EnsemblBacteria; ACB60023; ACB60023; Exig_0542. DR GeneID; 6173287; -. DR KEGG; esi:Exig_0542; -. DR PATRIC; 32134621; VBIExiSib53410_0557. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ESIB262543:GHBP-597-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23045 MW; 2EE1CDFC0DBC1E92 CRC64; MDSEYLIYAV TDRRLHPHLP LEDAVEATIK GGATIVQLRE KEMSGKNFLE SAVVLKDLTA SYNIPLIIND RIDIALLVEA GLHIGQDDIP LTEARRLLPT ATIGVSVSTV EQAVAAEQDG ADYLGVGSLF PTATKQDATF MSRVTLEQIR KAVRIPLVGI GGISETNVSL LDSLVDGYAV VSALFANPEI ERTTKKFKQT VEQVRQSVSD RV // ID B1YRU3_BURA4 Unreviewed; 374 AA. AC B1YRU3; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=BamMC406_0340; OS Burkholderia ambifaria (strain MC40-6). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=398577; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC40-6; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Ramette A., Konstantinidis K., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001025; ACB62841.1; -; Genomic_DNA. DR RefSeq; YP_001807057.1; NC_010551.1. DR ProteinModelPortal; B1YRU3; -. DR STRING; 398577.BamMC406_0340; -. DR EnsemblBacteria; ACB62841; ACB62841; BamMC406_0340. DR GeneID; 6178071; -. DR KEGG; bac:BamMC406_0340; -. DR PATRIC; 19029975; VBIBurAmb82852_0345. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BAMB398577:GH38-355-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 374 AA; 39270 MW; 28765AA18748DB52 CRC64; MSARFADAFW PPADELAEAA ERIRARLGDW PASTTPWRLC VAAPDVPVDG DVLIVSAGDR AAQARASAAS RPAAPDAVAI EFDEHGATLH AADVRHALEG AHPLADDWIA ALAAFLDCGF APIDALVLAL AWRDGDETRG ADAWPGDAAR FPRVAGLAAA PEPAFPPCPA QLGLYPVVPD AEWVERVLDC GARTVQLRVK GADPAALRGE IARAVAAGRR YPDARVFIND HWQIAVEEGA YGVHLGQEDL ETADLAAIAR ASLRLGLSSH GYYEMLRALH ERPSYLALGP VYATATKAVA APPQGLARIA RYARFAGARA PLVAIGGVGL DALPDVLATG VGSVAVVSAI TGAIDYRAAV VALQQCFARQ FDNH // ID B1Z134_BURA4 Unreviewed; 194 AA. AC B1Z134; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=BamMC406_3747; OS Burkholderia ambifaria (strain MC40-6). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=398577; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC40-6; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Ramette A., Konstantinidis K., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 2 of Burkholderia ambifaria MC40-6."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001026; ACB66214.1; -; Genomic_DNA. DR RefSeq; YP_001810430.1; NC_010552.1. DR ProteinModelPortal; B1Z134; -. DR STRING; 398577.BamMC406_3747; -. DR EnsemblBacteria; ACB66214; ACB66214; BamMC406_3747. DR GeneID; 6180683; -. DR KEGG; bac:BamMC406_3747; -. DR PATRIC; 19037147; VBIBurAmb82852_3866. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BAMB398577:GH38-3822-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 20112 MW; BF0F14BAAA3177AF CRC64; MSATLPRCCV ITPEPASASA ADCQAFLERL SAVLARGETL VQLRVKSFDA AAFARLAADA LARCTAAGAQ LMLNGPIDAA GVMQLDGAGW HLDSAALRAV AQRPLPAARR VSAACHAADD LVLAARAGVD FVTLSPVLPT LSHPGAPTLG WTRFAALAEQ AVMPVYALGG MTRAHLDDAR RHGAYGVAGI RSFW // ID B1Z982_METPB Unreviewed; 222 AA. AC B1Z982; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Mpop_2326; OS Methylobacterium populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=441620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-705 / NCIMB 13946 / BJ001; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Marx C., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium populi BJ001."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001029; ACB80488.1; -; Genomic_DNA. DR RefSeq; YP_001925023.1; NC_010725.1. DR ProteinModelPortal; B1Z982; -. DR STRING; 441620.Mpop_2326; -. DR EnsemblBacteria; ACB80488; ACB80488; Mpop_2326. DR GeneID; 6313771; -. DR KEGG; mpo:Mpop_2326; -. DR PATRIC; 22561938; VBIMetPop124700_2383. DR eggNOG; NOG280778; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR BioCyc; MPOP441620:GHMI-2373-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 222 AA; 22940 MW; C34B47240CB3FE4D CRC64; MPASDAAAPR PRLALLTPYG LGPSEAEAIA AALDAACAAG DVAAVILRLA VADERSLVTL VKRLAPSAQE RGAAVLVSVP GFTGDVVSVA ARGGADGVHF DRADEETLRD LRGRLRDGRI LGTGGVLASR DAAMVAGETG VDYLMFGGLF PDGVAPDAEE VRERATWWAE IFETPCIAVA TTAEDVAALA ATGAEFVGLE SVLWRDDPEG VRTAQAQLDM AR // ID B1ZKA3_METPB Unreviewed; 205 AA. AC B1ZKA3; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Mpop_0577; OS Methylobacterium populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=441620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-705 / NCIMB 13946 / BJ001; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Marx C., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium populi BJ001."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001029; ACB78755.1; -; Genomic_DNA. DR RefSeq; YP_001923290.1; NC_010725.1. DR ProteinModelPortal; B1ZKA3; -. DR STRING; 441620.Mpop_0577; -. DR EnsemblBacteria; ACB78755; ACB78755; Mpop_0577. DR GeneID; 6310835; -. DR KEGG; mpo:Mpop_0577; -. DR PATRIC; 22558308; VBIMetPop124700_0603. DR eggNOG; NOG131844; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MPOP441620:GHMI-589-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 205 AA; 20481 MW; 8483EEC26CBD5315 CRC64; MLPPLLLVTD RHGADRPLAE TVGAAVAGGA RFVWLRDREL DAEARRALAR DLIAILAPVG GRLVVGGDPD LASEAGAQGV HLPGSAGIDG VRALREKLGA AALIGFSAHS VAEIAAAEAA GADYATLSPV FPTASKPGYG PALGLEALRA ACSTSRLPVF ALGGIDGGNA RACREAGAAG VAVMGGVMRS LDPQSETARF VAAVS // ID B1ZM14_METPB Unreviewed; 242 AA. AC B1ZM14; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mpop_4985; OS Methylobacterium populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=441620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-705 / NCIMB 13946 / BJ001; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Marx C., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium populi BJ001."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001029; ACB83081.1; -; Genomic_DNA. DR RefSeq; YP_001927616.1; NC_010725.1. DR ProteinModelPortal; B1ZM14; -. DR STRING; 441620.Mpop_4985; -. DR EnsemblBacteria; ACB83081; ACB83081; Mpop_4985. DR GeneID; 6312066; -. DR KEGG; mpo:Mpop_4985; -. DR PATRIC; 22567248; VBIMetPop124700_5017. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MPOP441620:GHMI-5053-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 55 59 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT METAL 88 88 Magnesium (By similarity). FT METAL 107 107 Magnesium (By similarity). FT BINDING 87 87 HMP-PP (By similarity). FT BINDING 126 126 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 189 189 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 242 AA; 24503 MW; DEB0112089EF5346 CRC64; MSIGTGLGLS RPSSAGIAVD LRLYGILDVG VLGGDGAALA ALAAEAVAGG TTLLQYRDKD LTNARAALAR IRAIHAAVGG RAPLLVNDRI DLALAAGVEG VHLGQSDLHP EEARRLLGPR AIIGLTVKTG AQADELYRLP IDYACIGGVF ATTSKDNPDP PVGLDGLQRI VFRGRLARGQ ALPLGAIAGI DASNAASVIR AGADGVALIG ALFKGGATEA KARDLRARVD EALAQRGGAG TR // ID B2A6F6_NATTJ Unreviewed; 212 AA. AC B2A6F6; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Nther_1918; OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / OS JW/NM-WN-LF). OC Bacteria; Firmicutes; Clostridia; Natranaerobiales; Natranaerobiaceae; OC Natranaerobius. OX NCBI_TaxID=457570; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.; RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM- RT WN-LF."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001034; ACB85489.1; -; Genomic_DNA. DR RefSeq; YP_001918077.1; NC_010718.1. DR ProteinModelPortal; B2A6F6; -. DR STRING; 457570.Nther_1918; -. DR EnsemblBacteria; ACB85489; ACB85489; Nther_1918. DR GeneID; 6315298; -. DR KEGG; nth:Nther_1918; -. DR PATRIC; 22672558; VBINatThe92436_1968. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NTHE457570:GHRL-1967-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23322 MW; EA54723D099B752D CRC64; MTTGNKGLNT DIYAITAEPF SRGRDNIAVV SKMLKAGIKT IQYREKDKTP REKLTQCKKI REMTREANCK LIINDDIDIA LLVGADGVHV GQDDLPVNQV RKLVGDDMII GLSTHSPDQA KEAISLGADY IGVGPVFETN TKEDVQKPVG LEYVDYVSTN LNIPFTAIGG IKRNNIHLVK EKGASCFAIV TEIVEAPNIP ERIHEIRSII HS // ID B2AGF7_CUPTR Unreviewed; 377 AA. AC B2AGF7; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE SubName: Full=THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=RALTA_A0183; OS Cupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis OS (strain LMG 19424)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=164546; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R1 / LMG 19424; RX PubMed=18490699; DOI=10.1101/gr.076448.108; RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., RA Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., RA Batut J., Medigue C., Masson-Boivin C.; RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and RT comparative genomics of rhizobia."; RL Genome Res. 18:1472-1483(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU633749; CAP62856.1; -; Genomic_DNA. DR RefSeq; YP_001795578.1; NC_010528.1. DR ProteinModelPortal; B2AGF7; -. DR STRING; 164546.RALTA_A0183; -. DR EnsemblBacteria; CAP62856; CAP62856; RALTA_A0183. DR GeneID; 6301698; -. DR KEGG; cti:RALTA_A0183; -. DR PATRIC; 21526998; VBICupTai42494_0185. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CTAI164546:GJNE-184-MONOMER; -. DR BioCyc; CTAI977880:GLC7-184-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 377 AA; 40076 MW; 2D8EFBCA91AFFDFF CRC64; MTRRPVHVPS DGPLRQAVLE HYGDTFGVDD KPWQAWRLED APAQPGAHDV LLSDGEADAD TIARVAAAGA TLIETEREGG QWVDTVRSPM GTWVFSVAAD TDQPHSPAFV AVLLACLSLH FPAHDALCLA RAWAPGSADW PSDFARFPHV RHAALVAPEH TVAPFAPCPA LGLYVVVPSA EWIERLAPLN VPTLQLRFKS GDAAAVRAEI ARAARAMQGS SSRLFINDHW QAAIEHHAAH GAHSGIYGIH LGQEDLDDAD LDAIRASGLR LGVSTHGYAE MLRVAAIRPS YLALGAIFPT TTKTMPTQPQ GMGRFRAYVK LMQPVIPSLV GIGGVNATNM REVLAVGVGS AAVVRAVTEA DDVPAAVARL VSLFPAG // ID B2AVR9_PODAN Unreviewed; 520 AA. AC B2AVR9; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 16-APR-2014, entry version 37. DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 7, supercontig 1; GN ORFNames=PODANS_7_2010; OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) OS (Pleurage anserina). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Sordariales; Lasiosphaeriaceae; OC Podospora. OX NCBI_TaxID=515849; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383; RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77; RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., RA Porcel B.M., Couloux A., Aury J.-M., Segurens B., Poulain J., RA Anthouard V., Grossetete S., Khalili H., Coppin E., RA Dequard-Chablat M., Picard M., Contamine V., Arnaise S., Bourdais A., RA Berteaux-Lecellier V., Gautheret D., de Vries R.P., Battaglia E., RA Coutinho P.M., Danchin E.G.J., Henrissat B., El Khoury R., RA Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H., RA Debuchy R., Wincker P., Weissenbach J., Silar P.; RT "The genome sequence of the model ascomycete fungus Podospora RT anserina."; RL Genome Biol. 9:R77.1-R77.22(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU633900; CAP68493.1; -; Genomic_DNA. DR RefSeq; XP_001907820.1; XM_001907785.1. DR ProteinModelPortal; B2AVR9; -. DR GeneID; 6192045; -. DR KEGG; pan:PODANSg4855; -. DR KO; K14154; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 520 AA; 55596 MW; 9413DFDF349B14A9 CRC64; MPKPHVDYHL YLVTDSTPAV LKDPSRFFDA VEQALRGGVS LVQLREKTAD TGELVSIAKR LHELTKKYNV PLLINDRVDV ALAVGCEGVH IGQDDMDLET ARKLLGDDKI IGVTVSNVEE ALIACKNGAD YLGIGTAIIG AAGVREILAA METAGCYDKV RTVCIGGLNK YNIARIMYQS RHVDGKPGWL TLNGVAVVSA IMSADDPEEA SKELLTLVKS YDKFRGSSLM GARASKGVLE VAGDIIKKVH EAKPLTHNMT NLVVQNFAAN VALAVGGSPI MANYGEEAAD LSKLGGSLVV NMGTVTPEGL LNYYKALQAY NVAVQPVVFD PVGAGATSVR REAVRSILAN GYLDVIKGNE GEIKTVWGAV DGEQQKGVDS VDSLTPENKL DLVVKLARRE QSVVVMTGKT DYVSDGYSAV TVANGHEYLG LVTGTGCTLG TAISVALAVH HKEDKLWAVV TAMLHFEIAA EIAAEREDVK GPGTFISAFL DELYNIRTAT VSGDMKWLER AKGLNITLTR // ID B2DJ13_STREE Unreviewed; 210 AA. AC B2DJ13; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; ORFNames=SP108700_0719; OS Streptococcus pneumoniae CDC1087-00. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=453361; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC1087-00; RA Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., RA Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H.; RT "Genome Sequence of Streptococcus pneumoniae CDC1087-00."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFT01000011; EDT90802.1; -; Genomic_DNA. DR ProteinModelPortal; B2DJ13; -. DR EnsemblBacteria; EDT90802; EDT90802; SP108700_0719. DR PATRIC; 25744473; VBIStrPne99426_1336. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID B2DJ20_STREE Unreviewed; 209 AA. AC B2DJ20; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; Synonyms=thiE; ORFNames=SP108700_0712; OS Streptococcus pneumoniae CDC1087-00. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=453361; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC1087-00; RA Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., RA Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H.; RT "Genome Sequence of Streptococcus pneumoniae CDC1087-00."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFT01000011; EDT90784.1; -; Genomic_DNA. DR ProteinModelPortal; B2DJ20; -. DR EnsemblBacteria; EDT90784; EDT90784; SP108700_0712. DR PATRIC; 25744487; VBIStrPne99426_1343. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23244 MW; 69798D236EB6C679 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID B2DLI6_STREE Unreviewed; 209 AA. AC B2DLI6; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; ORFNames=SP195_0736; OS Streptococcus pneumoniae SP195. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=453363; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP195; RA Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., RA Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H.; RT "Genome Sequence of Streptococcus pneumoniae SP195."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGE01000001; EDT93432.1; -; Genomic_DNA. DR ProteinModelPortal; B2DLI6; -. DR EnsemblBacteria; EDT93432; EDT93432; SP195_0736. DR PATRIC; 28661764; VBIStrPne53256_0342. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23247 MW; 9D63833774B28637 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID B2DLJ3_STREE Unreviewed; 210 AA. AC B2DLJ3; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; ORFNames=SP195_0743; OS Streptococcus pneumoniae SP195. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=453363; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP195; RA Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., RA Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H.; RT "Genome Sequence of Streptococcus pneumoniae SP195."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGE01000001; EDT93459.1; -; Genomic_DNA. DR ProteinModelPortal; B2DLJ3; -. DR EnsemblBacteria; EDT93459; EDT93459; SP195_0743. DR PATRIC; 28661778; VBIStrPne53256_0349. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID B2DSG1_STREE Unreviewed; 209 AA. AC B2DSG1; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 19-FEB-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; ORFNames=SP28804_0622; OS Streptococcus pneumoniae CDC0288-04. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=453364; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC0288-04; RA Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., RA Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H.; RT "Genome Sequence of Streptococcus pneumoniae CDC0288-04."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGF01000002; EDT95095.1; -; Genomic_DNA. DR ProteinModelPortal; B2DSG1; -. DR EnsemblBacteria; EDT95095; EDT95095; SP28804_0622. DR PATRIC; 25737850; VBIStrPne58888_0332. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID B2DSG8_STREE Unreviewed; 210 AA. AC B2DSG8; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; ORFNames=SP28804_0629; OS Streptococcus pneumoniae CDC0288-04. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=453364; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC0288-04; RA Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., RA Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H.; RT "Genome Sequence of Streptococcus pneumoniae CDC0288-04."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGF01000002; EDT95258.1; -; Genomic_DNA. DR ProteinModelPortal; B2DSG8; -. DR EnsemblBacteria; EDT95258; EDT95258; SP28804_0629. DR PATRIC; 25737864; VBIStrPne58888_0339. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22744 MW; E8E490415C77D48E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID B2DXF0_STREE Unreviewed; 209 AA. AC B2DXF0; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; ORFNames=SP305906_0701; OS Streptococcus pneumoniae CDC3059-06. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=453365; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC3059-06; RA Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., RA Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H.; RT "Genome Sequence of Streptococcus pneumoniae CDC3059-06."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGG01000001; EDT97667.1; -; Genomic_DNA. DR ProteinModelPortal; B2DXF0; -. DR EnsemblBacteria; EDT97667; EDT97667; SP305906_0701. DR PATRIC; 28631661; VBIStrPne114647_0246. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID B2DXF7_STREE Unreviewed; 210 AA. AC B2DXF7; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; ORFNames=SP305906_0708; OS Streptococcus pneumoniae CDC3059-06. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=453365; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC3059-06; RA Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., RA Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H.; RT "Genome Sequence of Streptococcus pneumoniae CDC3059-06."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGG01000001; EDT97637.1; -; Genomic_DNA. DR ProteinModelPortal; B2DXF7; -. DR EnsemblBacteria; EDT97637; EDT97637; SP305906_0708. DR PATRIC; 28631675; VBIStrPne114647_0253. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID B2E3X3_STREE Unreviewed; 209 AA. AC B2E3X3; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; ORFNames=SPMLV016_0638; OS Streptococcus pneumoniae MLV-016. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=453366; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MLV-016; RA Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., RA Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H.; RT "Genome Sequence of Streptococcus pneumoniae MLV-016."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGH01000002; EDT99149.1; -; Genomic_DNA. DR ProteinModelPortal; B2E3X3; -. DR EnsemblBacteria; EDT99149; EDT99149; SPMLV016_0638. DR PATRIC; 28637221; VBIStrPne30809_0447. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID B2E3Y0_STREE Unreviewed; 210 AA. AC B2E3Y0; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; ORFNames=SPMLV016_0645; OS Streptococcus pneumoniae MLV-016. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=453366; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MLV-016; RA Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., RA Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H.; RT "Genome Sequence of Streptococcus pneumoniae MLV-016."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGH01000002; EDT98929.1; -; Genomic_DNA. DR ProteinModelPortal; B2E3Y0; -. DR EnsemblBacteria; EDT98929; EDT98929; SPMLV016_0645. DR PATRIC; 28637235; VBIStrPne30809_0454. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; AEAC90751A95738D CRC64; MNREALRLYL VTNRYQDSVE SFLAKIETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID B2EB40_BIFAN Unreviewed; 516 AA. AC B2EB40; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 19-MAR-2014, entry version 35. DE SubName: Full=Phosphomethylpyrimidine kinase; GN ORFNames=BIFLAC_05050; OS Bifidobacterium animalis subsp. lactis HN019. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=486409; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HN019; RA Collett M.A., Depree K.M., Rand C.J., Mason C., Stanton J.-A.L.; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABOT01000005; EDT88949.1; -; Genomic_DNA. DR ProteinModelPortal; B2EB40; -. DR EnsemblBacteria; EDT88949; EDT88949; BIFLAC_05050. DR PATRIC; 27195985; VBIBifAni43833_1050. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 516 AA; 54334 MW; BA2BECA74309264A CRC64; MNSFPYPSMR DRFDLRFYFV VGPDDCGNRP ILDVVAKALD GGASFIQLRA KTQDVAEIVS LANDIAEEIA GHHVEHSVAF VVDDRVDAAL EARAKGIKVD GVHIGQDDLD PVVARKLLGP DAIIGLSAKT VDEVREANHL PEGTIDYIGA GPLHMTATKP ESMIVDENGD ITTLNVSSID EMRTMSKYPL IVGGGVKADD IPMLAKTKAD GWFVVSAIAG ATDPEQATRR LVDDWTAIRG DEKPRYTGRK PAATKLPAVL TIATTDSSGG AGIPADLKTM LANDVFGECV VAGITAQNTT GVQAIAAVDP SIVGAQIDSV FDDIRPTAVK IGVIVGVESV KTVARKLRDH QATNIVVDPV MVATSGSSLA ADDTIAEEIS SLFPIATVIT PNIPEAQVLA QMPIGNQADM ETAAVQLAKD YGTCVLVKGG HGVKDADDVL AFPTGAVTWF EGERIANDNT HGTGCTLSSA IASYLAQGED LEDAVRDAKA YLSGALRANL NLGKGHGPMD HAWAMH // ID B2FPB3_STRMK Unreviewed; 318 AA. AC B2FPB3; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=Smlt0765; OS Stenotrophomonas maltophilia (strain K279a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=522373; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K279a; RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74; RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., RA Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., RA Rutter S., Quail M.A., Rajandream M.A., Harris D., Churcher C., RA Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.; RT "The complete genome, comparative and functional analysis of RT Stenotrophomonas maltophilia reveals an organism heavily shielded by RT drug resistance determinants."; RL Genome Biol. 9:R74.1-R74.13(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM743169; CAQ44342.1; -; Genomic_DNA. DR RefSeq; YP_001970656.1; NC_010943.1. DR ProteinModelPortal; B2FPB3; -. DR STRING; 522373.Smlt0765; -. DR EnsemblBacteria; CAQ44342; CAQ44342; Smlt0765. DR GeneID; 6394644; -. DR KEGG; sml:Smlt0765; -. DR PATRIC; 23697243; VBISteMal45202_0730. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SMAL522373:GJE8-736-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 318 AA; 34995 MW; 6D2462FCDCF49113 CRC64; MPSPTRSIHV VAAVITDARG RVLLNRRTEN RDMAGLWEFP GGKRESGETS EQALVRELRE ELGIEADVGE WLMDVPQRYP DKHLTLEVRH VRSWKGTPRG REGQAITWVA PDKLGRYSMP PADLPVVAAL RQPDSYLITP APADDEGGVQ HWHEQLQRVV AAGQQRIQLR LPTAHPQRQA MVEQAVRAHR RSGVQWLLNR DIELARALGV GVHLGSEQLQ ELSQRPLPQG QLVAASCHDL QQLQAAQQLG CDFAVLGPVQ ATASHPDAVP LGWDAFAELR AQVSLPIYAL GGVGRGHIAE ARRHGGQGIA AIRGLWPE // ID B2FT34_STRMK Unreviewed; 208 AA. AC B2FT34; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Smlt3872; OS Stenotrophomonas maltophilia (strain K279a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=522373; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K279a; RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74; RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., RA Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., RA Rutter S., Quail M.A., Rajandream M.A., Harris D., Churcher C., RA Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.; RT "The complete genome, comparative and functional analysis of RT Stenotrophomonas maltophilia reveals an organism heavily shielded by RT drug resistance determinants."; RL Genome Biol. 9:R74.1-R74.13(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM743169; CAQ47276.1; -; Genomic_DNA. DR RefSeq; YP_001973564.1; NC_010943.1. DR ProteinModelPortal; B2FT34; -. DR STRING; 522373.Smlt3872; -. DR EnsemblBacteria; CAQ47276; CAQ47276; Smlt3872. DR GeneID; 6392117; -. DR KEGG; sml:Smlt3872; -. DR PATRIC; 23703195; VBISteMal45202_3647. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SMAL522373:GJE8-3745-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 20982 MW; 94347D2A96BCF06F CRC64; MTSASPAPRG VYLITPDEPD TARLLARTAP LLAAGATWLQ YRHKTASDAL RQEQATALQG LCAAHGVPLI VNDDPVLAKA VGAAGVHLGG TDGDIPSARA LLGAEAIIGA SCYDQLANAE KAVAAGASYV AFGAFFPTAT KVTSSRAHAD LLRQSAALGV PRVAIGGLTP DNVGPIIDAG ADLVAVVSGI YAASDPVATQ RAYLAQFA // ID B2GH38_KOCRD Unreviewed; 220 AA. AC B2GH38; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=KRH_04430; OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / OS DC2201). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Kocuria. OX NCBI_TaxID=378753; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201; RX PubMed=18408034; DOI=10.1128/JB.01853-07; RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S., RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., RA Harayama S.; RT "Complete genome sequence of the soil actinomycete Kocuria RT rhizophila."; RL J. Bacteriol. 190:4139-4146(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009152; BAG28790.1; -; Genomic_DNA. DR RefSeq; YP_001854296.1; NC_010617.1. DR ProteinModelPortal; B2GH38; -. DR STRING; 378753.KRH_04430; -. DR EnsemblBacteria; BAG28790; BAG28790; KRH_04430. DR GeneID; 6239939; -. DR KEGG; krh:KRH_04430; -. DR PATRIC; 22181110; VBIKocRhi5258_0431. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; KRHI378753:GJ8F-452-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 49 53 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23717 MW; D3FDC48084691F2D CRC64; MERSEDQGRR RRRQLRDARL YVCVTARRER GDLRDFLHTA YEGGVDIIQL RDKTLEAAAE IEAIQVLAEV AREHGKLFAV NDRADVALLT GADVFHVGQG DLTTRQARTV LGPDVVLGRS CHSPAQVDAA LADPGLDYFC TGPVWETPTK PGRAAVGLEL PRYAAEHAGT TPFFAIGGVD AARLPAVLGT GATRIVVVRA VTEARDVTAA ARELRSALPA // ID B2GZR7_BURPE Unreviewed; 367 AA. AC B2GZR7; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BURPS1655_E0103; OS Burkholderia pseudomallei 1655. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=331109; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1655; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia pseudomallei 1655."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899712; EDU07986.1; -; Genomic_DNA. DR ProteinModelPortal; B2GZR7; -. DR EnsemblBacteria; EDU07986; EDU07986; BURPS1655_E0103. DR PATRIC; 27825509; VBIBurPse91116_1663. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 367 AA; 38230 MW; FA513D7B891D1ED7 CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIALL NAAGAQAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEVE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID B2H7X3_BURPE Unreviewed; 199 AA. AC B2H7X3; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=BURPS1655_I0759; OS Burkholderia pseudomallei 1655. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=331109; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1655; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia pseudomallei 1655."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899718; EDU11141.1; -; Genomic_DNA. DR ProteinModelPortal; B2H7X3; -. DR EnsemblBacteria; EDU11141; EDU11141; BURPS1655_I0759. DR PATRIC; 27832264; VBIBurPse91116_4114. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 21308 MW; BAC4456E90187FAB CRC64; MNKSANLPSE YLITPEPPGD EALSDYLATL ERTLKAGISL VQLRAKAVTA PYYARLTEYA LACCRRYNAR LLVNAAPEVA LGLHTDGVHL TSTRLMTCST RPLPAGLLVS AACHDEDQVR HADSIGVDLI TISPVMPTAT HTTAEPLGWP RFRELATLTS VPVYALGGMS VDSLAEARNA GAYGIAAIRA FWGSNVDRS // ID B2HBN0_BURPE Unreviewed; 209 AA. AC B2HBN0; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BURPS1655_D1353; OS Burkholderia pseudomallei 1655. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=331109; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1655; RA DeShazer D., Woods D.E., Nierman W.C.; RT "Annotation of Burkholderia pseudomallei 1655."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH899721; EDU12457.1; -; Genomic_DNA. DR ProteinModelPortal; B2HBN0; -. DR EnsemblBacteria; EDU12457; EDU12457; BURPS1655_D1353. DR PATRIC; 27835001; VBIBurPse91116_6152. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID B2HUW6_ACIBC Unreviewed; 299 AA. AC B2HUW6; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 44. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=ACICU_02484; OS Acinetobacter baumannii (strain ACICU). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=405416; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACICU; RX PubMed=18411315; DOI=10.1128/AAC.01643-07; RA Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J., RA Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.; RT "Whole-genome pyrosequencing of an epidemic multidrug-resistant RT Acinetobacter baumannii strain belonging to the European clone II RT group."; RL Antimicrob. Agents Chemother. 52:2616-2625(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000863; ACC57796.1; -; Genomic_DNA. DR RefSeq; YP_001847143.1; NC_010611.1. DR ProteinModelPortal; B2HUW6; -. DR STRING; 405416.ACICU_02484; -. DR EnsemblBacteria; ACC57796; ACC57796; ACICU_02484. DR GeneID; 6234314; -. DR KEGG; abc:ACICU_02484; -. DR PATRIC; 20713700; VBIAciBau103538_2535. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ABAU405416:GI27-2526-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 299 AA; 34203 MW; 49BD9DC168F2FC57 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLNPELK KQIKTVHLKQ SQLMSLHKGD LEVGVRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID B2HW20_ACIBC Unreviewed; 203 AA. AC B2HW20; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ACICU_02673; OS Acinetobacter baumannii (strain ACICU). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=405416; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACICU; RX PubMed=18411315; DOI=10.1128/AAC.01643-07; RA Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J., RA Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.; RT "Whole-genome pyrosequencing of an epidemic multidrug-resistant RT Acinetobacter baumannii strain belonging to the European clone II RT group."; RL Antimicrob. Agents Chemother. 52:2616-2625(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000863; ACC57985.1; -; Genomic_DNA. DR RefSeq; YP_001847332.1; NC_010611.1. DR ProteinModelPortal; B2HW20; -. DR STRING; 405416.ACICU_02673; -. DR EnsemblBacteria; ACC57985; ACC57985; ACICU_02673. DR GeneID; 6235320; -. DR KEGG; abc:ACICU_02673; -. DR PATRIC; 20714078; VBIAciBau103538_2718. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ABAU405416:GI27-2720-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21778 MW; F47FCEF0DAC9A9AE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKID KAEQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID B2I855_XYLF2 Unreviewed; 320 AA. AC B2I855; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 47. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=XfasM23_0405; OS Xylella fastidiosa (strain M23). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=405441; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M23; RX PubMed=20601474; DOI=10.1128/JB.00651-10; RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.; RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and RT M23) causing almond leaf scorch disease in California."; RL J. Bacteriol. 192:4534-4534(2010). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001011; ACB91853.1; -; Genomic_DNA. DR RefSeq; YP_001829127.1; NC_010577.1. DR ProteinModelPortal; B2I855; -. DR STRING; 405441.XfasM23_0405; -. DR EnsemblBacteria; ACB91853; ACB91853; XfasM23_0405. DR GeneID; 6204030; -. DR KEGG; xfn:XfasM23_0405; -. DR PATRIC; 24142709; VBIXylFas85937_0538. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XFAS405441:GJJI-428-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 320 AA; 35468 MW; E7754B57E973CFA1 CRC64; MTDSLRSIHV VAAVIADVRG RLLLSRRTEN SDMPGLWEFP GGKRESGETS EQALARELYE ELGISADVGE WLMEVPQLYP GKRLRLEVRR VRAWKGGLRG REGQALTWVE PDKLLRYSMP PADQPVVGML RQPDRYLVTP EPGEQDAEWL DAVEHAYRLG IERIQLRMRQ HDPVRWSGLV RQAVQRRGRA HVEVLLNRDI ALAEALGIGV HLGAEQLAVL DARPLPVGLP VGASCHCLAD LCHAQRIGCD FAVLGPVLPT ESHPGAVTLG WERFEQLREQ VALPIYAIGG MCADQVKEAR RHGAQGIAAM RGLWPGGAKQ // ID B2I8A8_XYLF2 Unreviewed; 204 AA. AC B2I8A8; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=XfasM23_1781; OS Xylella fastidiosa (strain M23). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=405441; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M23; RX PubMed=20601474; DOI=10.1128/JB.00651-10; RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.; RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and RT M23) causing almond leaf scorch disease in California."; RL J. Bacteriol. 192:4534-4534(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001011; ACB93184.1; -; Genomic_DNA. DR RefSeq; YP_001830458.1; NC_010577.1. DR ProteinModelPortal; B2I8A8; -. DR STRING; 405441.XfasM23_1781; -. DR EnsemblBacteria; ACB93184; ACB93184; XfasM23_1781. DR GeneID; 6203033; -. DR KEGG; xfn:XfasM23_1781; -. DR PATRIC; 24146088; VBIXylFas85937_2208. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XFAS405441:GJJI-1821-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21869 MW; 1DE42CE42C6D56EA CRC64; MPQPRGIYLI TPDETDTARL IAHTAPLLNG IVWLQYRNKL ANTALRTEQA QALLALCRPT GIPLLINDDL ELAQTIGADG VHLGMHDSNA SIARAQLGPH AIIGVSCYNQ IERAKQAIKA GASYVGFGAF YPSHTKTTPY RATPELLRQT THLGVPRVAI GGLTPKNIAP IIEAGAELLA VISGIYSAKN PITALKAYQS QFNI // ID B2IFI3_BEII9 Unreviewed; 214 AA. AC B2IFI3; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 34. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bind_3522; OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB OS 8712). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Beijerinckiaceae; Beijerinckia. OX NCBI_TaxID=395963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9039 / DSM 1715 / NCIB 8712; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Dunfield P.F., Dedysh S.N., Liesack W., Saw J.H., Alam M., Chen Y., RA Murrell J.C., Richardson P.; RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica RT ATCC 9039."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001016; ACB97079.1; -; Genomic_DNA. DR RefSeq; YP_001834568.1; NC_010581.1. DR ProteinModelPortal; B2IFI3; -. DR STRING; 395963.Bind_3522; -. DR EnsemblBacteria; ACB97079; ACB97079; Bind_3522. DR GeneID; 6199360; -. DR KEGG; bid:Bind_3522; -. DR PATRIC; 21090173; VBIBeiInd21058_3986. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BIND395963:GJA7-3586-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 214 AA; 22975 MW; B2223AC68DB2B99C CRC64; MSDAAPRLYL ITPLLDEAEA FAPRLKAALD AGDVACLLLR IADQARGDAK TIIRALTPLA QQRGVACLIE DDTQLAARAD TDGVHIEADP ETHKDVLDAA IAAMQPRRIV GVGGLMNRDA AMIAGESGAD YLMFGLPDVE EKQEDLLERI AWWAEIFQVP CVGQAHRLED VPALVQAGAD FIALGRIVWE DPRGPAAVIA EAMEKCTSSP MPAR // ID B2IGM2_BEII9 Unreviewed; 201 AA. AC B2IGM2; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Bind_2163; OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB OS 8712). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Beijerinckiaceae; Beijerinckia. OX NCBI_TaxID=395963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9039 / DSM 1715 / NCIB 8712; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Dunfield P.F., Dedysh S.N., Liesack W., Saw J.H., Alam M., Chen Y., RA Murrell J.C., Richardson P.; RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica RT ATCC 9039."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001016; ACB95783.1; -; Genomic_DNA. DR RefSeq; YP_001833272.1; NC_010581.1. DR ProteinModelPortal; B2IGM2; -. DR STRING; 395963.Bind_2163; -. DR EnsemblBacteria; ACB95783; ACB95783; Bind_2163. DR GeneID; 6198589; -. DR KEGG; bid:Bind_2163; -. DR PATRIC; 21087223; VBIBeiInd21058_2539. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HIANIQK; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BIND395963:GJA7-2196-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 21861 MW; 2E97CC70A3F1DFCA CRC64; MLDPFYLIVD NAAWLARLLP CGVKLVQLRV KDLTGEPLRA EIAKARTLCD THGAQLIVND YWVEAIDLGC DYVHLGQGDL DTADLPAIRR AGLRLGLSTH DEKELERALA CAPDYIALGP IYPTILKAMP FAPQGLARLG EWKRKIGSIP LVGIGGINLD RVAGVLEAGA DSASVVTDIS LNPDPEQRTR DWLAATRRFV A // ID B2INA0_STRPS Unreviewed; 209 AA. AC B2INA0; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPCG_0667; OS Streptococcus pneumoniae (strain CGSP14). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=516950; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CGSP14; RX PubMed=19361343; DOI=10.1186/1471-2164-10-158; RA Ding F., Tang P., Hsu M.H., Cui P., Hu S., Yu J., Chiu C.H.; RT "Genome evolution driven by host adaptations results in a more RT virulent and antimicrobial-resistant Streptococcus pneumoniae serotype RT 14."; RL BMC Genomics 10:158-158(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001033; ACB89919.1; -; Genomic_DNA. DR RefSeq; YP_001835384.1; NC_010582.1. DR ProteinModelPortal; B2INA0; -. DR STRING; 516950.SPCG_0667; -. DR EnsemblBacteria; ACB89919; ACB89919; SPCG_0667. DR GeneID; 6216545; -. DR KEGG; spw:SPCG_0667; -. DR PATRIC; 19677534; VBIStrPne123335_0727. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE516950:GI38-673-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23275 MW; 54691E8B38ED4ED4 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LRGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID B2INA7_STRPS Unreviewed; 210 AA. AC B2INA7; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPCG_0674; OS Streptococcus pneumoniae (strain CGSP14). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=516950; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CGSP14; RX PubMed=19361343; DOI=10.1186/1471-2164-10-158; RA Ding F., Tang P., Hsu M.H., Cui P., Hu S., Yu J., Chiu C.H.; RT "Genome evolution driven by host adaptations results in a more RT virulent and antimicrobial-resistant Streptococcus pneumoniae serotype RT 14."; RL BMC Genomics 10:158-158(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001033; ACB89926.1; -; Genomic_DNA. DR RefSeq; YP_001835391.1; NC_010582.1. DR ProteinModelPortal; B2INA7; -. DR STRING; 516950.SPCG_0674; -. DR EnsemblBacteria; ACB89926; ACB89926; SPCG_0674. DR GeneID; 6217775; -. DR KEGG; spw:SPCG_0674; -. DR PATRIC; 19677548; VBIStrPne123335_0734. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE516950:GI38-680-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID B2JAU6_NOSP7 Unreviewed; 200 AA. AC B2JAU6; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 13-NOV-2013, entry version 31. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN OrderedLocusNames=Npun_AF191; OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102). OG Plasmid pNPUN01. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=63737; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29133 / PCC 73102; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Meeks J.C., Elhai J., Campbell E.L., Thiel T., Longmire J., Potts M., RA Atlas R.; RT "Complete sequence of plasmid 1 of Nostoc punctiforme ATCC 29133."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001038; ACC85050.1; -; Genomic_DNA. DR RefSeq; YP_001870091.1; NC_010631.1. DR ProteinModelPortal; B2JAU6; -. DR STRING; 63737.Npun_AF191; -. DR EnsemblBacteria; ACC85050; ACC85050; Npun_AF191. DR GeneID; 6256264; -. DR KEGG; npu:Npun_AF191; -. DR PATRIC; 22768043; VBINosPun48114_8136. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NPUN63737:GJNP-6680-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Transferase. SQ SEQUENCE 200 AA; 22315 MW; CE11DB7371CD280B CRC64; MADQKETIKP FKKIAIFDIF SGENSEIICS DKSKIAAQVN KWVNRAISNG ADSCYVRLYE ANKENIDTII ENLSYKILQI ILPFSLNYKS SLVSAFHFRE KDQIKMPEAK SNNVLFGKSC HSLKSIEEAE YEGLDYVFFS PIFATPTHPE AKGIGLDMLT QACKSTQMKV FALGGINENN YQKCLDAGAS GIAAISMFKK // ID B2JHZ7_BURP8 Unreviewed; 375 AA. AC B2JHZ7; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Bphy_2771; OS Burkholderia phymatum (strain DSM 17167 / STM815). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=391038; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17167 / STM815; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D., RA Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Bacher J., Blanchard J., Cohan F., RA James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P., RA Riley M., Souza V., Wertz J., Young P.; RT "Complete sequence of chromosome 1 of Burkholderia phymatum STM815."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001043; ACC71943.1; -; Genomic_DNA. DR RefSeq; YP_001858989.1; NC_010622.1. DR ProteinModelPortal; B2JHZ7; -. DR STRING; 391038.Bphy_2771; -. DR EnsemblBacteria; ACC71943; ACC71943; Bphy_2771. DR GeneID; 6244254; -. DR KEGG; bph:Bphy_2771; -. DR PATRIC; 19192067; VBIBurPhy25146_2937. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VEWRICL; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BPHY391038:GI4Z-2830-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 375 AA; 40285 MW; 7DF04E0D0482F26A CRC64; MTQALKLSGR DLFWPPADEL TEAAERIRAR LGDWPPTHVE WRICLTAPDD ANGGDLIVFT DLKQNDAQHL EQIARWVAHG AGVIEAAEGR AVLHLGGVRY QLEGHLAEDW IPALAAFLDC GFDPHDALTL ALAWRDGDEM KSEDAWPCDL SRFPRVAGLP DAPAQPFAAC PDALGLYAVL PTAEWVERVA GFGVKTVQLR HKAADAGLQR EIARSVAAGR EHDAHVFIND HWQAAIDAGA YGVHLGQEDV HTADLHALSA AGVRLGLSTH GYYEMLTALH FRPSYIALGA VFPTTTKVMP TAPQGLVRLT RYVRLLDGVV PLVAIGGISG DVLARVLATG VKSAAVVRAI TEAADPASAT AALQNVFLQE KVLKS // ID B2K119_YERPB Unreviewed; 224 AA. AC B2K119; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=YPTS_0310; OS Yersinia pseudotuberculosis serotype IB (strain PB1/+). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=502801; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PB1/+; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., RA Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., RA Hauser L., Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., RA Richardson P.; RT "Complete sequence of Yersinia pseudotuberculosis PB1/+."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001048; ACC87301.1; -; Genomic_DNA. DR RefSeq; YP_001870758.1; NC_010634.1. DR ProteinModelPortal; B2K119; -. DR STRING; 502801.YPTS_0310; -. DR EnsemblBacteria; ACC87301; ACC87301; YPTS_0310. DR GeneID; 6260825; -. DR KEGG; ypb:YPTS_0310; -. DR PATRIC; 18648141; VBIYerPse20639_0322. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; YPSE502801:GHIH-407-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24216 MW; E13A24EDCD5E0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE TADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID B2N335_ECOLX Unreviewed; 211 AA. AC B2N335; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Ec53638_1781; OS Escherichia coli 53638. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=344610; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=53638; RA Rasko D.A., Rosovitz M.J., Brinkley C., Myers G.S.A., Seshadri R., RA Cer R.Z., Jiang L., Sebastian Y., Ravel J.; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAKB02000001; EDU62610.1; -; Genomic_DNA. DR ProteinModelPortal; B2N335; -. DR EnsemblBacteria; EDU62610; EDU62610; Ec53638_1781. DR PATRIC; 31210165; VBIEscCol26876_2154. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23074 MW; B486E1DDF16258DE CRC64; MYQPDFRPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B2NXZ2_ECO57 Unreviewed; 211 AA. AC B2NXZ2; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECH7EC4196_4103; OS Escherichia coli O157:H7 str. EC4196. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=444451; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4196; RA Rosovitz M.J., Ravel J.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4196; RA Eppinger M., Ravel J., Mammel M.K., LeClerc J.E., Cebula T.A., RA Sebastian Y.; RT "Annotation of Escherichia coli O157:H7 str. EC4196."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHO01000044; EDU31200.1; -; Genomic_DNA. DR ProteinModelPortal; B2NXZ2; -. DR SMR; B2NXZ2; 10-209. DR EnsemblBacteria; EDU31200; EDU31200; ECH7EC4196_4103. DR PATRIC; 26615474; VBIEscCol79648_4841. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B2PCG2_ECO57 Unreviewed; 211 AA. AC B2PCG2; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECH7EC4113_3596; OS Escherichia coli O157:H7 str. EC4113. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=444452; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4113; RA Rosovitz M.J., Ravel J.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4113; RA Eppinger M., Ravel J., Mammel M.K., LeClerc J.E., Cebula T.A., RA Sebastian Y.; RT "Annotation of Escherichia coli O157:H7 str. EC4113."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHP01000056; EDU52145.1; -; Genomic_DNA. DR ProteinModelPortal; B2PCG2; -. DR SMR; B2PCG2; 10-209. DR EnsemblBacteria; EDU52145; EDU52145; ECH7EC4113_3596. DR PATRIC; 26603508; VBIEscCol134660_4921. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B2PJ29_ECO57 Unreviewed; 211 AA. AC B2PJ29; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECH7EC4076_3606; OS Escherichia coli O157:H7 str. EC4076. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=444453; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4076; RA Rosovitz M.J., Ravel J.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4076; RA Eppinger M., Ravel J., Mammel M.K., LeClerc J.E., Cebula T.A., RA Sebastian Y.; RT "Annotation of Escherichia coli O157:H7 str. EC4076."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHQ01000005; EDU70836.1; -; Genomic_DNA. DR ProteinModelPortal; B2PJ29; -. DR SMR; B2PJ29; 10-209. DR EnsemblBacteria; EDU70836; EDU70836; ECH7EC4076_3606. DR PATRIC; 26585282; VBIEscCol87564_1873. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B2PW06_PROST Unreviewed; 212 AA. AC B2PW06; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PROSTU_00739; OS Providencia stuartii ATCC 25827. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Providencia. OX NCBI_TaxID=471874; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25827; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Providencia stuartii (ATCC 25827)."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25827; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Providencia stuartii(ATCC 25827)."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25827; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABJD02000074; EDU61254.1; -; Genomic_DNA. DR ProteinModelPortal; B2PW06; -. DR EnsemblBacteria; EDU61254; EDU61254; PROSTU_00739. DR PATRIC; 25545258; VBIProStu71739_3394. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23340 MW; 377D1FF142665E6C CRC64; MKKLPSTPFA PTEQRLGLYP VVDSVEWIER LLNAGVTTIQ LRIKDKHDDE VRDDIQQAIA LGEKHHARLF INDYWRLAIE LGAYGVHLGQ EDLETTDLLA IHQAGLRLGI STHDQHELAI AKSVRPSYIA MGHIFPTETK KMPSAPQGLE TLKTMVEATP DYPTVAIGGI SIDRVPAVLA TGVGSVALVS AITKADDWLE ATKTLLRLVE NH // ID B2RH33_PORG3 Unreviewed; 647 AA. AC B2RH33; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=PGN_0159; OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / JCM 12257). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=431947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33277 / DSM 20709 / JCM 12257; RX PubMed=18524787; DOI=10.1093/dnares/dsn013; RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H., RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T., RA Nakayama K.; RT "Determination of the genome sequence of Porphyromonas gingivalis RT strain ATCC 33277 and genomic comparison with strain W83 revealed RT extensive genome rearrangements in P. gingivalis."; RL DNA Res. 15:215-225(2008). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009380; BAG32678.1; -; Genomic_DNA. DR RefSeq; YP_001928275.1; NC_010729.1. DR ProteinModelPortal; B2RH33; -. DR STRING; 431947.PGN_0159; -. DR EnsemblBacteria; BAG32678; BAG32678; PGN_0159. DR GeneID; 6330138; -. DR KEGG; pgn:PGN_0159; -. DR PATRIC; 22973231; VBIPorGin26334_0153. DR eggNOG; COG0351; -. DR HOGENOM; HOG000059711; -. DR KO; K00788; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PGIN431947:GC9J-166-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 647 AA; 71256 MW; 2B0013A788906C17 CRC64; MKPWLITPER LTSEQIGLLD HFFDRGLERL HLRLPDAGEE EYSLVIEAVA ACYRRRIVVH DHPRLVGRYG LCGLHLPERV WKGMTDRPQL PDGCTVSASC HTIEDIESFP FRIDYCFLSP IFDSLCKVGH AGRFSPDSLG DRLQRLHLPV VALGGITPDR LPQLRRAGFA SAAALGYVWL AEGRELMRWQ ELCTPAVICV GGVDPSAGAG ITADVRTAEN MGVRAYTVAT AITFQGSGSY RGERWLDPAD IIRQIETLSA EMEPAVAKIG LIRDSDTLSF VVDCLKKVFP SIRIVWDPVL RASADSSSGQ ADRFNLEDIT ALSRIDFITP NLPEARHLLG CEPDDETLLD FYRRSGVGLV LKGGHAGESV VTDRIVYDGR CEALRLLRGG TEKHGTGCAH STAFAAALAL EQEPFTAAGM AQLYVSRLRE RTSGLLAMHK DLPVDPVVRL MSEIDLQFIT HRQPDLSELE EAEAVCRMGV RWVQLRMKEA SHEEMLRTAC AVKAVCRHYG SLFVVNDRVE IARQVDADGV HLGKEDMAIV EARRILGSNK IIGRTCNTME DVRRAYAEGA DYVGIGPYRY TETKQRLAPV LGLEGYKAIA ACMQAEGIRL PAFAIGGIED ADIPLIRDCG IGGIAVSGSL IRKIKKN // ID B2S7E4_BRUA1 Unreviewed; 221 AA. AC B2S7E4; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 37. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=BAbS19_I16070; OS Brucella abortus (strain S19). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=430066; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S19; RX PubMed=18478107; DOI=10.1371/journal.pone.0002193; RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., RA Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.; RT "Genome sequence of Brucella abortus vaccine strain S19 compared to RT virulent strains yields candidate virulence genes."; RL PLoS ONE 3:E2193-E2193(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000887; ACD73091.1; -; Genomic_DNA. DR RefSeq; YP_001935565.1; NC_010742.1. DR ProteinModelPortal; B2S7E4; -. DR STRING; 430066.BAbS19_I16070; -. DR EnsemblBacteria; ACD73091; ACD73091; BAbS19_I16070. DR GeneID; 6327555; -. DR KEGG; bmc:BAbS19_I16070; -. DR PATRIC; 17820493; VBIBruAbo38055_2987. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BABO430066:GHI6-1606-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID B2S8J8_BRUA1 Unreviewed; 203 AA. AC B2S8J8; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BAbS19_I02020; OS Brucella abortus (strain S19). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=430066; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S19; RX PubMed=18478107; DOI=10.1371/journal.pone.0002193; RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., RA Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.; RT "Genome sequence of Brucella abortus vaccine strain S19 compared to RT virulent strains yields candidate virulence genes."; RL PLoS ONE 3:E2193-E2193(2008). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000887; ACD71751.1; -; Genomic_DNA. DR RefSeq; YP_001934225.1; NC_010742.1. DR ProteinModelPortal; B2S8J8; -. DR STRING; 430066.BAbS19_I02020; -. DR EnsemblBacteria; ACD71751; ACD71751; BAbS19_I02020. DR GeneID; 6328145; -. DR KEGG; bmc:BAbS19_I02020; -. DR PATRIC; 17817297; VBIBruAbo38055_1429. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BABO430066:GHI6-198-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID B2SLN0_XANOP Unreviewed; 207 AA. AC B2SLN0; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PXO_02388; OS Xanthomonas oryzae pv. oryzae (strain PXO99A). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=360094; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PXO99A; RX PubMed=18452608; DOI=10.1186/1471-2164-9-204; RA Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., RA Rabinowicz P.D., Tsuge S., Furutani A., Ochiai H., Delcher A.L., RA Kelley D., Madupu R., Puiu D., Radune D., Shumway M., Trapnell C., RA Aparna G., Jha G., Pandey A., Patil P.B., Ishihara H., Meyer D.F., RA Szurek B., Verdier V., Koebnik R., Dow J.M., Ryan R.P., Hirata H., RA Tsuyumu S., Won Lee S., Seo Y.S., Sriariyanum M., Ronald P.C., RA Sonti R.V., Van Sluys M.A., Leach J.E., White F.F., Bogdanove A.J.; RT "Genome sequence and rapid evolution of the rice pathogen Xanthomonas RT oryzae pv. oryzae PXO99A."; RL BMC Genomics 9:204-204(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000967; ACD60679.1; -; Genomic_DNA. DR RefSeq; YP_001915211.1; NC_010717.1. DR ProteinModelPortal; B2SLN0; -. DR STRING; 360094.PXO_02388; -. DR EnsemblBacteria; ACD60679; ACD60679; PXO_02388. DR GeneID; 6307625; -. DR KEGG; xop:PXO_02388; -. DR PATRIC; 24127786; VBIXanOry73153_4243. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XORY360094:GI45-4106-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21466 MW; 20335AC5E094C2DA CRC64; MPNRLNVRGV YLITPDEPNT QRLLLRTTPL LASIAWLQYR NKQADAALRL RQASALREAC VAHGVPLIIN DDAQLAAQVG AQGVHLGEDD GEVTAARALL GEHAIIGVSC YDAIGRARAA AAAGASYVAF GAFFPTITKQ TTRRATPALL EQAAELHLAR VAIGGIAPAQ VPALVTAGAD LIAVVSGVYA APDPVAAVQA YRAGFAA // ID B2SPL8_XANOP Unreviewed; 302 AA. AC B2SPL8; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 53. DE SubName: Full=Dgtp-pyrophosphohydrolase thiamine phosphate synthase; GN OrderedLocusNames=PXO_04356; OS Xanthomonas oryzae pv. oryzae (strain PXO99A). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=360094; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PXO99A; RX PubMed=18452608; DOI=10.1186/1471-2164-9-204; RA Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., RA Rabinowicz P.D., Tsuge S., Furutani A., Ochiai H., Delcher A.L., RA Kelley D., Madupu R., Puiu D., Radune D., Shumway M., Trapnell C., RA Aparna G., Jha G., Pandey A., Patil P.B., Ishihara H., Meyer D.F., RA Szurek B., Verdier V., Koebnik R., Dow J.M., Ryan R.P., Hirata H., RA Tsuyumu S., Won Lee S., Seo Y.S., Sriariyanum M., Ronald P.C., RA Sonti R.V., Van Sluys M.A., Leach J.E., White F.F., Bogdanove A.J.; RT "Genome sequence and rapid evolution of the rice pathogen Xanthomonas RT oryzae pv. oryzae PXO99A."; RL BMC Genomics 9:204-204(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000967; ACD57705.1; -; Genomic_DNA. DR RefSeq; YP_001912237.1; NC_010717.1. DR ProteinModelPortal; B2SPL8; -. DR STRING; 360094.PXO_04356; -. DR PRIDE; B2SPL8; -. DR EnsemblBacteria; ACD57705; ACD57705; PXO_04356. DR GeneID; 6304580; -. DR KEGG; xop:PXO_04356; -. DR PATRIC; 24121443; VBIXanOry73153_1102. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XORY360094:GI45-1061-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 302 AA; 33540 MW; 08BAFFA882B93C63 CRC64; MITDPRGRIL LTRRTETRDM PGLWEFPGGK REPGETSEQA LVRELNEELG IEAQVGDWLM DVPQLYPDKR LRLEVRHITA WKGSPRGREG QAMTWVAADK LARYSMPPAD VPVVGALRQP DHYLITPEPE DDARWLEGLE RALQNGITRI QLRARQTAPA QWQALLQQVM RLRGRTRAQL LLNRDIALAA ELGVGVHLGS EQLAGLQERP LPAEQLVAAS CHGLDDLRHA QRICCDFAVL GPVQATASHP GATPLGWGGF ETLREQVSLP IYALGGMQIE DVREARSHGA QGIAAIRSLW PQ // ID B2T6X9_BURPP Unreviewed; 367 AA. AC B2T6X9; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Bphyt_3572; OS Burkholderia phytofirmans (strain DSM 17436 / PsJN). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=398527; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17436 / PsJN; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Nowak J., Sessitsch A., Lazarovits G., Compant S., RA Barka E., Tiedje J.; RT "Complete sequence of chromosome 1 of Burkholderia phytofirmans RT PsJN."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001052; ACD17962.1; -; Genomic_DNA. DR RefSeq; YP_001897186.1; NC_010681.1. DR ProteinModelPortal; B2T6X9; -. DR STRING; 398527.Bphyt_3572; -. DR EnsemblBacteria; ACD17962; ACD17962; Bphyt_3572. DR GeneID; 6281078; -. DR KEGG; bpy:Bphyt_3572; -. DR PATRIC; 19217727; VBIBurPhy117947_7603. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BPHY398527:GJEX-3625-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 367 AA; 39653 MW; E6EAD79F4E1AC7B6 CRC64; MTQTLTLKDR DLFWPPADEL TEAAERIRAR LGDWPPTHAP WRICLTAPDE PNGGDLIVIA DAQQHGEQVA RWLVRGAGVI EAAEDKATLH LGGEKYRLEG HLAEDWVAAL AAFLDCGFDP HDALVLALAW RDGDETRADD AFPADLSHFP RLAGLPDALA QAFPRCPDRL GLYPVLPTAE WVERVVGFGV KTVQLRRKSS EPAEELKREI ARCVAVGRQH DAQVFINDHW QAALEAGAYG VHLGQEDVHT ADLAALAAGG VRLGLSTHGF YEILRALHFR PSYIALGAVF PTTTKVMPTA PQGLRRLARY VRLLDGVVPL VAIGGIDLQV LPDVLATGVG CAAVVRAVTE AADPAAAVSA LQQGFTR // ID B2U765_RALPJ Unreviewed; 384 AA. AC B2U765; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Rpic_3646; OS Ralstonia pickettii (strain 12J). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=402626; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12J; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.; RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001068; ACD28765.1; -; Genomic_DNA. DR RefSeq; YP_001901197.1; NC_010682.1. DR ProteinModelPortal; B2U765; -. DR STRING; 402626.Rpic_3646; -. DR EnsemblBacteria; ACD28765; ACD28765; Rpic_3646. DR GeneID; 6289510; -. DR KEGG; rpi:Rpic_3646; -. DR PATRIC; 20258135; VBIRalPic63053_4782. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; RPIC402626:GH94-3703-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 384 AA; 40444 MW; CCCDDE38DF436550 CRC64; MSASALRFSA AWPEAAALAA QIVDRHVEAF GRAPHAWSVT DHADEATSTA TVLLTTDTAQ AERARSAGAA VVLTAVEGDQ RIDTVYDRLG TYRFTSAAQG DAFDVRFVAI FGAALALAFE PRDALCVARA WIAEGNADAL AWPTQFDALP RVLEPALPCP TAADLAFAPC PTQLGIYAVV PDADWVARLV ALKVPTLQLR FKSDDAQAVV DQVRRAEAAA RGSATRLFIN DHWQVALDVH TQAPDSGIYG IHLGQEDIDE ADLVAIRSAG LRLGISTHGF AEMLRVAPLN PSYLALGAVF ATPTKTMPTV PQGLGRLFAY AAAMRTREPA PPLVAIGGID LPAMPRVLES GVGCVAVVRA ITQAADVPAA VDALQATFAA HVRA // ID B2UNA3_AKKM8 Unreviewed; 214 AA. AC B2UNA3; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Amuc_0376; OS Akkermansia muciniphila (strain ATCC BAA-835). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Verrucomicrobiaceae; Akkermansia. OX NCBI_TaxID=349741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., RA de Vos W.M., Richardson P.; RT "Complete sequence of Akkermansia muciniphila ATCC BAA-835."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001071; ACD04215.1; -; Genomic_DNA. DR RefSeq; YP_001876996.1; NC_010655.1. DR ProteinModelPortal; B2UNA3; -. DR STRING; 349741.Amuc_0376; -. DR EnsemblBacteria; ACD04215; ACD04215; Amuc_0376. DR GeneID; 6274864; -. DR KEGG; amu:Amuc_0376; -. DR PATRIC; 20833346; VBIAkkMuc16855_0429. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AMUC349741:GHZ7-396-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23007 MW; 0D74BC3D9B4BA4F4 CRC64; MNRKECLSSC RLYGIVDMGY TAEHQLLPVT EKLLAGGLRI LQLRAKNHNP EHIENMGLQL APLCRKYGCL FIINDYPEIA LNIGADGVHL GQDDGDLASV RGLLGKDAVI GRSTHSPEQA LGACGEQADY IGFGPLFPTG TKPGRQAIGL EDIASVQQQL PENFPVFCIG GINGNTLPSV LEAGANRVVI VSWLLTHPDI TGTVRTLRKE LGEA // ID B2UP54_AKKM8 Unreviewed; 204 AA. AC B2UP54; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Amuc_2015; OS Akkermansia muciniphila (strain ATCC BAA-835). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Verrucomicrobiaceae; Akkermansia. OX NCBI_TaxID=349741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., RA de Vos W.M., Richardson P.; RT "Complete sequence of Akkermansia muciniphila ATCC BAA-835."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001071; ACD05825.1; -; Genomic_DNA. DR RefSeq; YP_001878606.1; NC_010655.1. DR ProteinModelPortal; B2UP54; -. DR STRING; 349741.Amuc_2015; -. DR EnsemblBacteria; ACD05825; ACD05825; Amuc_2015. DR GeneID; 6274511; -. DR KEGG; amu:Amuc_2015; -. DR PATRIC; 20837154; VBIAkkMuc16855_2298. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AMUC349741:GHZ7-2072-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21444 MW; 59B23D9E39CBA72B CRC64; MKKFNLHLYL VTDEASKCRL SLLETVRKAA DGGVTIVQYR STNPDAGTCY REALPIRDFL ASRGIPFIVN NRIDLALALE ADGVHIGQRD LPVPSVRAMI GPDKILGLSV SNKEQLRAVD ASLVDYLGMG PVFPTISKLN APPVLGVEGF AALASQSPLP VVAIGGLDAE RARQVRATGT ASGIAVVSAI CGAENPETAA RALA // ID B2V631_SULSY Unreviewed; 206 AA. AC B2V631; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SYO3AOP1_0005; OS Sulfurihydrogenibium sp. (strain YO3AOP1). OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; OC Sulfurihydrogenibium. OX NCBI_TaxID=436114; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YO3AOP1; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the RT Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001080; ACD65656.1; -; Genomic_DNA. DR RefSeq; YP_001930210.1; NC_010730.1. DR ProteinModelPortal; B2V631; -. DR STRING; 436114.SYO3AOP1_0005; -. DR EnsemblBacteria; ACD65656; ACD65656; SYO3AOP1_0005. DR GeneID; 6332574; -. DR KEGG; sul:SYO3AOP1_0005; -. DR PATRIC; 23764667; VBISulSp94719_0004. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSP436114:GI6I-5-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 23099 MW; 23C86288E3C72520 CRC64; MLKGLYVITD EKLTPYDKIF DMVEQSLKGG AKLVQLRDKN NTDDFLLPIA KDLKNLCHKY DALFIVNDRL ELTLKSDADG IHVGEEDVDI SEIRKALKDK IVGVSCYGDV ERAILMERLS ATYAAFGSFY PSPTKPKSKV VDKSAITEAK RFLKIPVCVI GGITVERAKE LVELGADLVA VISDIWTAEN IEERAREYAE LFRGKR // ID B2V7U1_SULSY Unreviewed; 183 AA. AC B2V7U1; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=SYO3AOP1_0370; OS Sulfurihydrogenibium sp. (strain YO3AOP1). OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; OC Sulfurihydrogenibium. OX NCBI_TaxID=436114; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YO3AOP1; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the RT Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001080; ACD66014.1; -; Genomic_DNA. DR RefSeq; YP_001930568.1; NC_010730.1. DR ProteinModelPortal; B2V7U1; -. DR STRING; 436114.SYO3AOP1_0370; -. DR EnsemblBacteria; ACD66014; ACD66014; SYO3AOP1_0370. DR GeneID; 6332120; -. DR KEGG; sul:SYO3AOP1_0370; -. DR PATRIC; 23765459; VBISulSp94719_0383. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HRFYFIT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSP436114:GI6I-391-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 183 AA; 20817 MW; BFF92D656476E5D4 CRC64; MLHRFYFITD RKKFKKPFLD TIKEVLDKGI RLFQIREKDL PDNELFKLTE DVLKIAEGYD VKIIINSRLD VALLLNLDGV HLPENGLPIE PIKKKFPNLI VGKSCHSLEC GLQAYQDGVD YVFISPIFQV EGKAPPIGVE KLREIVNKLP LPVYALGGIN KYNVQSVLDT GVYGIASIRY FLD // ID B2VG83_ERWT9 Unreviewed; 214 AA. AC B2VG83; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ETA_01700; OS Erwinia tasmaniensis (strain DSM 17950 / Et1/99). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=338565; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17950 / Et1/99; RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x; RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R., RA Geider K.; RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic RT bacterium in the genus Erwinia."; RL Environ. Microbiol. 10:2211-2222(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU468135; CAO95216.1; -; Genomic_DNA. DR RefSeq; YP_001906124.1; NC_010694.1. DR ProteinModelPortal; B2VG83; -. DR STRING; 465817.ETA_01700; -. DR EnsemblBacteria; CAO95216; CAO95216; ETA_01700. DR GeneID; 6300908; -. DR KEGG; eta:ETA_01700; -. DR PATRIC; 20426000; VBIErwTas9546_0217. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ETAS465817:GI36-183-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23058 MW; 0DF4C857BFA469B9 CRC64; MSRGAFPTTA ARLGLYPVVD SVEWIARLLD AGVRTIQLRI KDRTEQEVDA QVAEAITLGK RYQARLFIND YWRLAVKYQA YGVHLGQGDL NSADLDAIHA AGLRLGLSTH DDAELDRALA ERPSYVALGH VFPTQTKDMP SAPQGVAALT RYVKRLPGIS TVAIGGISLE RAPAVMASGV GSIAVVSAIT QARDWQAATR QLLALAEASR PSRV // ID B2WH62_PYRTR Unreviewed; 337 AA. AC B2WH62; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=PTRG_09321; OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot OS fungus) (Drechslera tritici-repentis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae; OC Pleosporaceae; Pyrenophora. OX NCBI_TaxID=426418; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pt-1C-BFP; RX PubMed=23316438; DOI=10.1534/g3.112.004044; RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B., RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., RA Holman W.H., Kodira C.D., Martin J., Oliver R.P., Robbertse B., RA Schackwitz W., Schwartz D.C., Spatafora J.W., Turgeon B.G., RA Yandava C., Young S., Zhou S., Zeng Q., Grigoriev I.V., Ma L.-J., RA Ciuffetti L.M.; RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora RT tritici-repentis, reveals transduplication and the impact of repeat RT elements on pathogenicity and population divergence."; RL G3 (Bethesda) 3:41-63(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS231625; EDU42372.1; -; Genomic_DNA. DR RefSeq; XP_001939653.1; XM_001939618.1. DR ProteinModelPortal; B2WH62; -. DR EnsemblFungi; EDU42372; EDU42372; PTRG_09321. DR GeneID; 6347611; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 337 AA; 36039 MW; F840D9061E30CAD8 CRC64; MEKQKVDYSL YLVTDSTKAI LGSRDLVDVV EQALSGGVTI VQYRDKTSDT GVLISIAKKL HEKCKAHGIP LVINDRMDVA LAVGCEGVHL GQDDMNVVEA RRILGDSKII GATVSSIEEA RIAVERGADY LGIGTLYATN TKKNTKDIIG ITGIRKILRY LDNGTKAEKN VGTVCIGGVN ASNVQRITHQ LLAPTPLNRN PKTIDGVAVV SAIIGSPSPK SASQHLSQLL HSPPPFTLHS TAPHFWHENP EDELSSIFHK ALQCKKAVKS KTPLSHNMTN LVVQNFAANV ALAIGASPIM ANYGLEAPDL ARLQGGLVVN MGTRHTTQPA DPSSSIP // ID B3AEJ1_ECO57 Unreviewed; 211 AA. AC B3AEJ1; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECH7EC4401_5927; OS Escherichia coli O157:H7 str. EC4401. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=478004; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4401; RA Rosovitz M.J., Ravel J.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4401; RA Eppinger M., Ravel J., Mammel M.K., LeClerc J.E., Cebula T.A., RA Sebastian Y.; RT "Annotation of Escherichia coli O157:H7 str. EC4401."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHR01000048; EDU73012.1; -; Genomic_DNA. DR ProteinModelPortal; B3AEJ1; -. DR SMR; B3AEJ1; 10-209. DR EnsemblBacteria; EDU73012; EDU73012; ECH7EC4401_5927. DR PATRIC; 29336931; VBIEscCol43159_5174. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B3AV41_ECO57 Unreviewed; 211 AA. AC B3AV41; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECH7EC4486_5468; OS Escherichia coli O157:H7 str. EC4486. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=478005; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4486; RA Rosovitz M.J., Ravel J.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4486; RA Eppinger M., Ravel J., Mammel M.K., LeClerc J.E., Cebula T.A., RA Sebastian Y.; RT "Annotation of Escherichia coli O157:H7 str. EC4486."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHS01000037; EDU78196.1; -; Genomic_DNA. DR ProteinModelPortal; B3AV41; -. DR SMR; B3AV41; 10-209. DR EnsemblBacteria; EDU78196; EDU78196; ECH7EC4486_5468. DR PATRIC; 31129996; VBIEscCol73827_5059. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B3B8Z8_ECO57 Unreviewed; 211 AA. AC B3B8Z8; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECH7EC4501_5631; OS Escherichia coli O157:H7 str. EC4501. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=478006; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4501; RA Rosovitz M.J., Ravel J.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4501; RA Eppinger M., Ravel J., Mammel M.K., LeClerc J.E., Cebula T.A., RA Sebastian Y.; RT "Annotation of Escherichia coli O157:H7 str. EC4501."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHT01000050; EDU83878.1; -; Genomic_DNA. DR ProteinModelPortal; B3B8Z8; -. DR SMR; B3B8Z8; 10-209. DR EnsemblBacteria; EDU83878; EDU83878; ECH7EC4501_5631. DR PATRIC; 29348381; VBIEscCol99915_4862. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B3BQ34_ECO57 Unreviewed; 211 AA. AC B3BQ34; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECH7EC869_3858; OS Escherichia coli O157:H7 str. EC869. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=478008; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC869; RA Rosovitz M.J., Ravel J.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC869; RX PubMed=21421787; DOI=10.1128/AEM.02554-10; RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.; RT "Genome signatures of Escherichia coli O157:H7 isolates from the RT bovine host reservoir."; RL Appl. Environ. Microbiol. 77:2916-2925(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHU01000037; EDU88578.1; -; Genomic_DNA. DR ProteinModelPortal; B3BQ34; -. DR SMR; B3BQ34; 10-209. DR EnsemblBacteria; EDU88578; EDU88578; ECH7EC869_3858. DR PATRIC; 29373773; VBIEscCol71386_5370. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B3BTY0_ECO57 Unreviewed; 211 AA. AC B3BTY0; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECH7EC508_3365; OS Escherichia coli O157:H7 str. EC508. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=478007; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC508; RA Eppinger M., Ravel J., Mammel M.K., LeClerc J.E., Cebula T.A., RA Sebastian Y.; RT "Annotation of Escherichia coli O157:H7 str. EC508."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC508; RA Rosovitz M.J., Ravel J.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHW01000005; EDU97632.1; -; Genomic_DNA. DR ProteinModelPortal; B3BTY0; -. DR SMR; B3BTY0; 10-209. DR EnsemblBacteria; EDU97632; EDU97632; ECH7EC508_3365. DR PATRIC; 29353103; VBIEscCol61748_1201. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B3C583_9BACE Unreviewed; 200 AA. AC B3C583; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BACINT_00065; OS Bacteroides intestinalis DSM 17393. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=471870; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17393; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides intestinalis (DSM 17393)."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17393; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABJL02000001; EDV07667.1; -; Genomic_DNA. DR ProteinModelPortal; B3C583; -. DR EnsemblBacteria; EDV07667; EDV07667; BACINT_00065. DR PATRIC; 27028221; VBIBacInt56937_0061. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 200 AA; 22798 MW; CE3F3863710FEB29 CRC64; MKLIIITSPD FLPGEARILT ELFKAGLDLL HLRKPEAEIY EVESLLQEIP MEYRSRIVIH DFFLLKEKYS LGGIHLNSRH PEAPENYHGL LSRACHSLEE VETTTPRFDY VLMSPVYDSI SKQGYRSGYS TEALRQAQEK GIINEKVIAL GGISEANLAE IKSLGFGGAT LLGDIWNRYH AWEDTEQLLT HFRKLKHCAE // ID B3C587_9BACE Unreviewed; 206 AA. AC B3C587; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACINT_00069; OS Bacteroides intestinalis DSM 17393. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=471870; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17393; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides intestinalis (DSM 17393)."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17393; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABJL02000001; EDV07671.1; -; Genomic_DNA. DR ProteinModelPortal; B3C587; -. DR EnsemblBacteria; EDV07671; EDV07671; BACINT_00069. DR PATRIC; 27028229; VBIBacInt56937_0065. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22551 MW; 8475D6489177E7C0 CRC64; MFDVQFITHF TASISYPDSA RIALEGGCRW VQLRMKDVSE EELKNTAMHV QELCRQYGAT FIIDDRVDLV KEIGADGVHL GKLDMPIKEA RKMLGKGFII GGTANTFADI RQHVADGADY IGCGPFRFTT TKQKLSPILG LDGYRSILVQ MQEEGLTIPI VAIGGITRED IPSLKALGLS GIALSGGILK AENPVLEMET IIRLTQ // ID B3CEB8_9BACE Unreviewed; 202 AA. AC B3CEB8; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BACINT_02437; OS Bacteroides intestinalis DSM 17393. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=471870; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17393; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides intestinalis (DSM 17393)."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17393; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABJL02000008; EDV03316.1; -; Genomic_DNA. DR ProteinModelPortal; B3CEB8; -. DR EnsemblBacteria; EDV03316; EDV03316; BACINT_02437. DR PATRIC; 27032780; VBIBacInt56937_2299. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23301 MW; 56CAEBB8022DE2F4 CRC64; MKLIIVTAPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHRRIVTH EHFYLKEEFD LMGIHLNTRN PNEPHDYSGH VSCTCHSVEE VKSKKHFYDY VFMSPVYDCI TKTGTLSGYT PEELRTAGKE RIIDTKVMAL GGITPDNILE IKDFGFGGAV VLGDLWNKFN VCTDRDYLGV IRHFKKLKEM AD // ID B3DQ79_BIFLD Unreviewed; 917 AA. AC B3DQ79; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 47. DE SubName: Full=Thiamine monophosphate synthase; GN Name=thiE; OrderedLocusNames=BLD_0132; OS Bifidobacterium longum (strain DJO10A). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=205913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJO10A; RX PubMed=18505588; DOI=10.1186/1471-2164-9-247; RA Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., RA Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., RA Slesarev A.I., Weimer B., O'Sullivan D.J.; RT "Comparative genomic analysis of the gut bacterium Bifidobacterium RT longum reveals loci susceptible to deletion during pure culture RT growth."; RL BMC Genomics 9:247-247(2008). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000605; ACD97578.1; -; Genomic_DNA. DR RefSeq; YP_001954076.1; NC_010816.1. DR ProteinModelPortal; B3DQ79; -. DR STRING; 205913.BLD_0132; -. DR EnsemblBacteria; ACD97578; ACD97578; BLD_0132. DR GeneID; 6363499; -. DR KEGG; blj:BLD_0132; -. DR PATRIC; 21113169; VBIBifLon134794_0149. DR eggNOG; COG0352; -. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR OMA; INTICSA; -. DR OrthoDB; EOG6NWBM5; -. DR BioCyc; BLON205913:GJB4-133-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100355 MW; 00000DA28A98E1F6 CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLADTKA AGWFVVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID B3DYQ3_METI4 Unreviewed; 221 AA. AC B3DYQ3; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Minf_0367; OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum OS (strain V4)). OC Bacteria; Verrucomicrobia; unclassified Verrucomicrobia; OC Methylacidiphilales; Methylacidiphilaceae; Methylacidiphilum. OX NCBI_TaxID=481448; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate V4; RX PubMed=18593465; DOI=10.1186/1745-6150-3-26; RA Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y., RA Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., RA Koonin E.V., Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., RA Dunfield P.F., Feng L., Wang L., Alam M.; RT "Complete genome sequence of the extremely acidophilic methanotroph RT isolate V4, Methylacidiphilum infernorum, a representative of the RT bacterial phylum Verrucomicrobia."; RL Biol. Direct 3:26-26(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000975; ACD82425.1; -; Genomic_DNA. DR RefSeq; YP_001939023.1; NC_010794.1. DR ProteinModelPortal; B3DYQ3; -. DR STRING; 481448.Minf_0367; -. DR EnsemblBacteria; ACD82425; ACD82425; Minf_0367. DR GeneID; 6351284; -. DR KEGG; min:Minf_0367; -. DR PATRIC; 22489755; VBIMetInf111569_0384. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MINF481448:GJEI-374-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 24441 MW; 4679AADBC9EA1DA2 CRC64; MIQGYLRKKY LLSQARFYGI LDLGYVPPSQ AASFARKLVE GKVDILQLRA KKEDKKEILR ISLEIKPLLG GADILFIIND HPDVALESGA DGVHLGQEDM PISEARSYLG DNFLIGKSTH SLEQALRAAS EQTDYIGCGP IFKTPTKPDY LPLGLEAIPR VKQQIKKPVF FIGGINQENI HEVLDAGADR VVMVSALLKA ADIPLFCRQM KNLLSLKGLW A // ID B3E7F9_GEOLS Unreviewed; 492 AA. AC B3E7F9; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=Glov_2763; OS Geobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=398767; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1151 / DSM 17278 / SZ; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., RA Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y., RA Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.; RT "Complete sequence of chromosome of Geobacter lovleyi SZ."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001089; ACD96476.1; -; Genomic_DNA. DR RefSeq; YP_001952996.1; NC_010814.1. DR ProteinModelPortal; B3E7F9; -. DR STRING; 398767.Glov_2763; -. DR EnsemblBacteria; ACD96476; ACD96476; Glov_2763. DR GeneID; 6367490; -. DR KEGG; glo:Glov_2763; -. DR PATRIC; 21997201; VBIGeoLov31523_2700. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OMA; YLAQGEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; GLOV398767:GH32-2804-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 492 AA; 52292 MW; 471D52C6A677FE08 CRC64; MSEKSMPLRL VITTPKTIRN RSIAGVYLIT DQQDDLLKRV AQALRGGVTV LQYRAKDKPY EFCLEEGSQL KQLCSRFGSL FIVNDDLRLA HALDADGVHL GQEDSSPQQA RELLGPDKII GVSTHNLDEA LKAESDGADY LGFGAMYPTD SKSITHMPGT SGLAAIRDRV KLPIVAIGGI SPANACRVIE AGADAVAVIS SVLAAPRPEV AATELRLLFN RLAPYPRGGV LTIAGSDSGG GAGIQADLKT ITLLGSYGAS AITALTAQNT RGVKSIHGIP PSFVRDQIDT VLTDLPIDVI KTGMLHTPAI ISLLAEYLTE QPNYYPVVID PVMVAKGGAS LLELDAVSIF QQALLPQAYL LTPNIPEAER LLNCRINSEA AMEQAARQLH GMGAANVLLK GGHLSGGDAV DILFDGQTIQ RFSSERFFTS ATHGTGCSFA SAIAACLAQG EPLREAVRLA KNFITTAIRL ARPMGKGHGP INHYLAAKET DQ // ID B3E9A9_GEOLS Unreviewed; 206 AA. AC B3E9A9; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Glov_0037; OS Geobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=398767; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1151 / DSM 17278 / SZ; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., RA Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y., RA Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.; RT "Complete sequence of chromosome of Geobacter lovleyi SZ."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001089; ACD93775.1; -; Genomic_DNA. DR RefSeq; YP_001950295.1; NC_010814.1. DR ProteinModelPortal; B3E9A9; -. DR STRING; 398767.Glov_0037; -. DR EnsemblBacteria; ACD93775; ACD93775; Glov_0037. DR GeneID; 6366054; -. DR KEGG; glo:Glov_0037; -. DR PATRIC; 21991801; VBIGeoLov31523_0032. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GLOV398767:GH32-37-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21734 MW; 1E99AEC787CAADCC CRC64; MIDFSLYLIT DRNQTGGRPL LEVVEAALSG GVRAVQLREK DLTPAELYDL AWEMRALTSR YDARLLINER IDIALAVEAD GVHLGVNSLP VTAARRIAPD LLIGYSSHSV GEAVAALAKG ADFVTFGPVF PTPSKAAYGE PVGLGELERA CRQAVGDLVF GLGGIKRDNL AQVTAAGCYR VALISDILAA PDPAEAAGAF RRGLGC // ID B3ED40_CHLL2 Unreviewed; 213 AA. AC B3ED40; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Clim_1405; OS Chlorobium limicola (strain DSM 245 / NBRC 103803). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290315; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 245 / NBRC 103803; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., RA Liu Z., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobium limicola DSM 245."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001097; ACD90465.1; -; Genomic_DNA. DR RefSeq; YP_001943444.1; NC_010803.1. DR ProteinModelPortal; B3ED40; -. DR STRING; 290315.Clim_1405; -. DR EnsemblBacteria; ACD90465; ACD90465; Clim_1405. DR GeneID; 6356176; -. DR KEGG; cli:Clim_1405; -. DR PATRIC; 21374927; VBIChlLim118737_1499. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FGPPQGL; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CLIM290315:GHUH-1438-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 213 AA; 22709 MW; A78DFF8D7F7837D5 CRC64; MSKDALAVLP RLCIISSGND PDGSGLLIRR QIELLLPSLP CLIQIREKHL DASTLFRLSR TMKAAAAGKN VLIFLNERAD IAASAALDGV HLRESSSPPD KLRSFTGSML IGKSSHSVES AVKSAQSGAD YLIFGPVFDT PSKRQYGNPQ GLLKLGEVCR SVSIPVFAIG GITPENTPLC LSKGAYGIAA LSLFCDTDRL PGLLKTFEQI LDS // ID B3EJ13_CHLPB Unreviewed; 206 AA. AC B3EJ13; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cphamn1_1282; OS Chlorobium phaeobacteroides (strain BS1). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=331678; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BS1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., RA Zhao F., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobium phaeobacteroides BS1."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001101; ACE04213.1; -; Genomic_DNA. DR RefSeq; YP_001959694.1; NC_010831.1. DR ProteinModelPortal; B3EJ13; -. DR STRING; 331678.Cphamn1_1282; -. DR EnsemblBacteria; ACE04213; ACE04213; Cphamn1_1282. DR GeneID; 6374959; -. DR KEGG; cpb:Cphamn1_1282; -. DR PATRIC; 21384772; VBIChlPha121022_1384. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPHA331678:GHME-1318-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21303 MW; AFF34160AC5DC5C2 CRC64; MKQQDILCCI TADSLCPVLQ AEKALGGGAS MIQLRNKSAS GADLYSWAKR IKKLCQAHDA TCIINDRLDI ALAVEADGVH LGQGDLPADA ARKLLGSKRI LGVSVASVDE AKKAVASGAD YLGLGHIFPT VSKHKSSEPI GLERIAEVTK TISIPVIAIG GITENSVCAV LRAGASGIAV ISSVAHAPDP ENAAASLTKK IQACRQ // ID B3EJ14_CHLPB Unreviewed; 212 AA. AC B3EJ14; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cphamn1_1283; OS Chlorobium phaeobacteroides (strain BS1). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=331678; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BS1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., RA Zhao F., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobium phaeobacteroides BS1."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001101; ACE04214.1; -; Genomic_DNA. DR RefSeq; YP_001959695.1; NC_010831.1. DR ProteinModelPortal; B3EJ14; -. DR STRING; 331678.Cphamn1_1283; -. DR EnsemblBacteria; ACE04214; ACE04214; Cphamn1_1283. DR GeneID; 6374960; -. DR KEGG; cpb:Cphamn1_1283; -. DR PATRIC; 21384774; VBIChlPha121022_1385. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INERSDI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPHA331678:GHME-1319-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23109 MW; B9B51C930F6B5380 CRC64; MKPVKKTLPR LYVVSNCREL PSPEIQLPEL VSRISSHLPV IIQLREKHLS AKALYELTLK VTARKPDSAF LLSINERFDI SLATNSDGVH LPENSCPLAK VRSAAPDLLI GKSTHSLKEA VTAESDGADY LFFGPVFETP LKKRYGPPMG LDKLATVCSS VSIPVYAIGG ITPQNAAHCL EHGAYGVAAM SIFTSTQNLV RTLDNFHSSL DR // ID B3HI14_ECOLX Unreviewed; 211 AA. AC B3HI14; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EcB7A_3764; OS Escherichia coli B7A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=340184; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B7A; RA Rasko D.A., Rosovitz M.J., Brinkley C., Myers G.S.A., Seshadri R., RA Cer R.Z., Jiang L., Ravel J.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B7A; RA Rasko D., Rosovitz M., Myers G., Seshadri R., Cer R., Jiang L., RA Ravel J., Fricke W.F., Sebastian Y.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJT02000064; EDV61057.1; -; Genomic_DNA. DR ProteinModelPortal; B3HI14; -. DR SMR; B3HI14; 10-208. DR EnsemblBacteria; EDV61057; EDV61057; EcB7A_3764. DR PATRIC; 30353373; VBIEscCol49857_3932. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B3HYB8_ECOLX Unreviewed; 211 AA. AC B3HYB8; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EcF11_1592; OS Escherichia coli F11. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=340197; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F11; RA Rasko D.A., Rosovitz M.J., Mobley H.L.T., Myers G.S.A., Seshadri R., RA Cer R.Z., Jiang L., Ravel J.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F11; RA Rasko D., Rosovitz M., Myers G., Seshadri R., Cer R., Jiang L., RA Ravel J., Fricke W.F., Sebastian Y.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJU02000047; EDV65048.1; -; Genomic_DNA. DR ProteinModelPortal; B3HYB8; -. DR SMR; B3HYB8; 10-208. DR EnsemblBacteria; EDV65048; EDV65048; EcF11_1592. DR PATRIC; 26556997; VBIEscCol13398_4614. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23086 MW; 1A8F52AF19C8B3F0 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ERPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B3ICV5_ECOLX Unreviewed; 211 AA. AC B3ICV5; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EcE22_0250; OS Escherichia coli E22. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=340185; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E22; RA Rasko D.A., Rosovitz M.J., Kaper J.B., Boedecker E.C., Myers G.S.A., RA Seshadri R., Cer R.Z., Jiang L., Ravel J.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E22; RA Rasko D., Rosovitz M., Myers G., Seshadri R., Cer R., Jiang L., RA Ravel J., Fricke W.F., Sebastian Y.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJV02000051; EDV80577.1; -; Genomic_DNA. DR ProteinModelPortal; B3ICV5; -. DR SMR; B3ICV5; 10-208. DR EnsemblBacteria; EDV80577; EDV80577; EcE22_0250. DR PATRIC; 26546311; VBIEscCol79205_5048. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B3IGI5_ECOLX Unreviewed; 211 AA. AC B3IGI5; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EcE110019_3437; OS Escherichia coli E110019. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=340186; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E110019; RA Rasko D.A., Rosovitz M.J., Kaper J.B., Myers G.S.A., Seshadri R., RA Cer R.Z., Jiang L., Ravel J.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E110019; RA Rasko D., Rosovitz M., Myers G., Seshadri R., Cer R., Jiang L., RA Ravel J., Fricke W.F., Sebastian Y.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJW02000004; EDV89208.1; -; Genomic_DNA. DR ProteinModelPortal; B3IGI5; -. DR SMR; B3IGI5; 10-208. DR EnsemblBacteria; EDV89208; EDV89208; EcE110019_3437. DR PATRIC; 26526570; VBIEscCol59696_0951. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B3J7G5_BACAN Unreviewed; 219 AA. AC B3J7G5; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BATI_0416; OS Bacillus anthracis str. Tsiankovskii-I. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405536; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tsiankovskii-I; RA Rosovitz M.J., Rasko D.A., Friedlander A., Ravel J.; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tsiankovskii-I; RA Dodson R.J., Durkin A.S., Sutton G.; RT "Genome sequence of Bacillus anthracis Tsiankovskii-I."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDN02000009; EDV15311.1; -; Genomic_DNA. DR ProteinModelPortal; B3J7G5; -. DR SMR; B3J7G5; 1-215. DR EnsemblBacteria; EDV15311; EDV15311; BATI_0416. DR PATRIC; 24572508; VBIBacAnt18208_3574. DR OMA; QFREKGP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23600 MW; 6D85F0FE3EFD3046 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGFI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWVIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID B3JB99_BACAN Unreviewed; 206 AA. AC B3JB99; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 16-OCT-2013, entry version 28. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BATI_0805; OS Bacillus anthracis str. Tsiankovskii-I. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405536; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tsiankovskii-I; RA Rosovitz M.J., Rasko D.A., Friedlander A., Ravel J.; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tsiankovskii-I; RA Dodson R.J., Durkin A.S., Sutton G.; RT "Genome sequence of Bacillus anthracis Tsiankovskii-I."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDN02000019; EDV14025.1; -; Genomic_DNA. DR ProteinModelPortal; B3JB99; -. DR EnsemblBacteria; EDV14025; EDV14025; BATI_0805. DR PATRIC; 24575348; VBIBacAnt18208_4945. DR OMA; ELVNVAM; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID B3JF71_9BACE Unreviewed; 202 AA. AC B3JF71; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BACCOP_00519; OS Bacteroides coprocola DSM 17136. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=470145; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17136; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides coprocola (DSM 17136)."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17136; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIY02000051; EDV02388.1; -; Genomic_DNA. DR ProteinModelPortal; B3JF71; -. DR EnsemblBacteria; EDV02388; EDV02388; BACCOP_00519. DR PATRIC; 26982664; VBIBacCop77500_1730. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23433 MW; 93F4B14CF77C612D CRC64; MKLILITRPT YFVEEDKIIT TLFDEGLDYL HLRKPDTAPV YAERLLTLIP EKYRKRIVVH GHFYLKEEYN LKGIHLNHRN PIAPDNYTGQ ISTSCHSLEE VKEKKNNFDY VFLSPVFDSI SKQGYAAEYT PEQIRQAAKD GIIDKRVIAL GGIDEDNILQ VKDYGFGGAA ILGGLWNKFD LDHDYNYQNL IEHFRKLKRL AD // ID B3JF76_9BACE Unreviewed; 210 AA. AC B3JF76; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACCOP_00524; OS Bacteroides coprocola DSM 17136. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=470145; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17136; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides coprocola (DSM 17136)."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17136; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIY02000051; EDV02393.1; -; Genomic_DNA. DR ProteinModelPortal; B3JF76; -. DR EnsemblBacteria; EDV02393; EDV02393; BACCOP_00524. DR PATRIC; 26982674; VBIBacCop77500_1735. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 31 35 HMP-PP binding (By similarity). FT REGION 128 130 THZ-P binding (By similarity). FT METAL 64 64 Magnesium (By similarity). FT METAL 83 83 Magnesium (By similarity). FT BINDING 63 63 HMP-PP (By similarity). FT BINDING 102 102 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23260 MW; D664251D83D05A7F CRC64; MELQFITHFT DQYSYYDSAR MALEGGCRWI QLRMKDATPD EIRPEAVRIQ ALCREYGATF IIDDHVELVK ELHADGVHLG KKDMPIAEAR QILGKDFIIG GTANTFEDVQ MHYQAGADYI GCGPFRFTTT KKNLSPILGL EGYKAIVSQM KTAGINLPIV AIGGITYDDI PSIMQTGVTG IALSGTILRA ENPVVETHRI LEAIQNSKQL // ID B3L7R4_PLAKH Unreviewed; 573 AA. AC B3L7R4; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Thiamin-phosphate pyrophosphorylase, putative; GN ORFNames=PKH_113500; OS Plasmodium knowlesi (strain H). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=5851; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H; RX PubMed=18843368; DOI=10.1038/nature07306; RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R.D., Jackson A.P., RA Mourier T., Mistry J., Pasini E.M., Aslett M.A., Balasubrammaniam S., RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I., RA Chillingworth T., Clark T.G., Galinski M.R., Hall N., Harper D., RA Harris D., Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., RA Lapp S., Marti M., Moule S., Meyer I.M., Ormond D., Peters N., RA Sanders M., Sanders S., Sargeant T.J., Simmonds M., Smith F., RA Squares R., Thurston S., Tivey A.R., Walker D., White B., RA Zuiderwijk E., Churcher C., Quail M.A., Cowman A.F., Turner C.M.R., RA Rajandream M.A., Kocken C.H.M., Thomas A.W., Newbold C.I., RA Barrell B.G., Berriman M.; RT "The genome of the simian and human malaria parasite Plasmodium RT knowlesi."; RL Nature 455:799-803(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM910993; CAQ40937.1; -; Genomic_DNA. DR RefSeq; XP_002261532.1; XM_002261496.1. DR STRING; 5850.PKH_113500; -. DR EnsemblProtists; PKH_113500; PKH_113500; PKH_113500. DR GeneID; 7321571; -. DR KEGG; pkn:PKH_113500; -. DR EuPathDB; PlasmoDB:PKH_113500; -. DR HOGENOM; HOG000281504; -. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 573 AA; 64532 MW; 7174055C2A7936F3 CRC64; MQKMKKNFSS PGLLGLSEWP RLRELSPFRW ASTRCSSSGK PVDYSLYLVT DDKFFMDKEN VCNTLIGKVR EGVLGGVGLV QLRLKKADDR YFYNTAVRMK HMLAKYKVPL VINNRIDICL GVDADGVHVG RTDLPINVAR DMLGEDKIVG ATINFSNDED IEMALNNNVD YIAHEHTLYE STTKPIAASH HDGIKEQIRM LLCRIKHLQE KGKIYKPNLN SEAPPIILIG GINTNNIQQT MITFWDSSAG VAVVSNIIGE KCNSFFNSLR LRYVIDKHKK GYNDAFMNLC MSCLRYVFWT NVESDMKGVY TNWMVREPHM HIPRSEAKGC NFRLATNMNV KKNVLHFFQN NLDLKFVQLN QPAVCTSVGG GNFFLFGSKR TDGRAPATGA TKSTEAGEGC YLHGEDKRMP FSHDQCVSKW IKENKKIRGG VFILIGEDFL ALFQKLLTPE FFHRNNFVVI TKKKQSGWKT VRCSVRGASI QFNNNLINVA LENIHVDSEV MNQFAILLAY FLMVQEKMKE VSPQFLTQIV GEGEATAEAG EEGKLLKLAA AVNMSFEVFS NEHTGLGLAT FSS // ID B3LKL6_YEAS1 Unreviewed; 540 AA. AC B3LKL6; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 16-APR-2014, entry version 29. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=SCRG_02285; OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=285006; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM11-1a; RG The Broad Institute Genome Sequencing Platform; RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., RA Cuomo C., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., RA Kleber M., Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., RA Young S.K., LaButti K., Pushparaj V., DeCaprio D., Crawford M., RA Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., RA Larson L., Luoma S., White J., O'Leary S., Kodira C.D., Zeng Q., RA Yandava C., Alvarado L., Pratt S., Kruglyak L.; RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH408046; EDV11014.1; -; Genomic_DNA. DR ProteinModelPortal; B3LKL6; -. DR SMR; B3LKL6; 3-536. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 58059 MW; F34FA1E0B76E3930 CRC64; MVFTKEEVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDIE TKNFVAEALE VQKICKKYNV PLIINDRIDV AMAIDADGVH VGQDDMPIPM VRKLLGPSKI LGWSVGKPSE VETLAKWGPD MVDYIGVGTL FPTSTKKNPK KSPMGPQGAI AILDALEEFK ATWCRTVGIG GLHPDNIQRV LCQCVASNGK RSLDGISLVS DIMAAPDACA ATKRLRGLLD ATRYQFVECE LNNTFPTTTS IQNVISQVSN NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL ARIPNASLLL NTGSVAPIEM LKAAINAYNE VNRPITFDPV GYSATETRLC LNNTLLTYGQ FACIKGNCSE ILSLAKLNNH KMKGVDSSSG KTNIDTLVRA TQIVAFQYRT VAVCTGEFDC VADGTFGGEY KLSSGTEGIT AEDLPCVIIE DGPIPIMGDI TASGCSLGST IASFIGGLDS TGKLFDAVVG AVLLYKSAGK LASTRCQGSG SFHVELIDAL YQLFHENKPE KWSASLKKFK // ID B3PCK8_CELJU Unreviewed; 316 AA. AC B3PCK8; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 16-APR-2014, entry version 52. DE SubName: Full=Putative mutT protein; GN OrderedLocusNames=CJA_2917; OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. OS cellulosa). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Cellvibrio. OX NCBI_TaxID=498211; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ueda107; RX PubMed=18556790; DOI=10.1128/JB.01701-07; RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., RA Nelson K.E.; RT "Insights into plant cell wall degradation from the genome sequence of RT the soil bacterium Cellvibrio japonicus."; RL J. Bacteriol. 190:5455-5463(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000934; ACE83416.1; -; Genomic_DNA. DR RefSeq; YP_001983373.1; NC_010995.1. DR ProteinModelPortal; B3PCK8; -. DR STRING; 498211.CJA_2917; -. DR EnsemblBacteria; ACE83416; ACE83416; CJA_2917. DR GeneID; 6414101; -. DR KEGG; cja:CJA_2917; -. DR PATRIC; 21329217; VBICelJap122165_2874. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CJAP498211:GHIT-2908-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 316 AA; 34368 MW; 5B4131967F9391EA CRC64; MSKQIHVAVG VIQNACGEIF IAQRAADAHQ GGLWEFPGGK LEPGETTPQA LTRELREELA IDVEACEPLI QIRHQYPDKA VLLDVYRVTA FSGEPRGNEG QPVRWVSPGH LGHYAFPAAN RPIIKALGLP SLCAISGAYR DAADLVKKLQ HTIQSGAGMF VLRDRQLAAN THLPLIAQVG ESLASTSVQF QINTSVVEFE QIQLHYPMAG LHLNRHELRH CRQRPVADEV CLGASCHNPE ELEMAERVGV DYVFLSPVLP TLSHSGATPL GWPAFADWVK QINVPVYALG GVTPAQLDQA KLAGAQGIAA IRAFWP // ID B3PL69_CELJU Unreviewed; 214 AA. AC B3PL69; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CJA_0881; OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. OS cellulosa). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Cellvibrio. OX NCBI_TaxID=498211; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ueda107; RX PubMed=18556790; DOI=10.1128/JB.01701-07; RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., RA Nelson K.E.; RT "Insights into plant cell wall degradation from the genome sequence of RT the soil bacterium Cellvibrio japonicus."; RL J. Bacteriol. 190:5455-5463(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000934; ACE86073.1; -; Genomic_DNA. DR RefSeq; YP_001981389.1; NC_010995.1. DR ProteinModelPortal; B3PL69; -. DR STRING; 498211.CJA_0881; -. DR EnsemblBacteria; ACE86073; ACE86073; CJA_0881. DR GeneID; 6414435; -. DR KEGG; cja:CJA_0881; -. DR PATRIC; 21325139; VBICelJap122165_0874. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CIGGINE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CJAP498211:GHIT-881-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23256 MW; F0182AAE6C6D6485 CRC64; MSSWSWSNPF KMNSTLYAIT DSGLLPGERL ALGVEAALQG GCRWIQYRDK STDNHRRELE ARQLVSLCNQ YQAKLIINDD MQLAQRVNAH GVHLGQDDGN PAEARRSLGE SAIIGVTCHD SLALAEKAIQ DGASYIAFGR FFPSKTKPHA RPAKFTLISE AKAKFPQVTL VVIGGITLDN AAVLLDAGAD KLAVCHDLFA AADIAAQAQR FNHL // ID B3PZ50_RHIE6 Unreviewed; 217 AA. AC B3PZ50; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Thiamine-phosphate pyrophosphorylase protein; DE EC=2.5.1.3; GN Name=thiEch; OrderedLocusNames=RHECIAT_CH0003776; OS Rhizobium etli (strain CIAT 652). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=491916; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIAT 652; RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P., RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J., RA Palacios R., Davila G.; RT "Genome diversity and DNA divergence of Rhizobium etli."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001074; ACE92714.1; -; Genomic_DNA. DR RefSeq; YP_001979892.1; NC_010994.1. DR ProteinModelPortal; B3PZ50; -. DR STRING; 491916.RHECIAT_CH0003776; -. DR EnsemblBacteria; ACE92714; ACE92714; RHECIAT_CH0003776. DR GeneID; 6401863; -. DR KEGG; rec:RHECIAT_CH0003776; -. DR PATRIC; 23100998; VBIRhiEtl120572_3721. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RETL491916:GH4T-3775-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 217 AA; 22862 MW; FB2A9AB6964AEF36 CRC64; MTEPENRCRL VLIVPDIADA DEQARIVADA LKGGDVASVI VPQYGLDDGT FQKHAEKLVP VIQDAGAAAL IAGDSRVAGR AKADGLHLSG NAEALSEAID KHAPKLIVGG GNAADRHTAL EIGEVRPDYI FFGKLDGDIK PEAHPKNLAL GEWWASMIEI PCIVMGGTDP TSALAVAETG AEFVALRLAV FDDPARAPSI IAEINALLDE KAPRFED // ID B3Q1Q4_RHIE6 Unreviewed; 211 AA. AC B3Q1Q4; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiEa; Synonyms=thiE; OrderedLocusNames=RHECIAT_PA0000266; OS Rhizobium etli (strain CIAT 652). OG Plasmid pA. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=491916; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIAT 652; PLASMID=pA; RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P., RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J., RA Palacios R., Davila G.; RT "Genome diversity and DNA divergence of Rhizobium etli."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001075; ACE93610.1; -; Genomic_DNA. DR RefSeq; YP_001985873.1; NC_010998.1. DR ProteinModelPortal; B3Q1Q4; -. DR STRING; 491916.RHECIAT_PA0000266; -. DR EnsemblBacteria; ACE93610; ACE93610; RHECIAT_PA0000266. DR GeneID; 6404142; -. DR KEGG; rec:RHECIAT_PA0000266; -. DR PATRIC; 23105578; VBIRhiEtl120572_5998. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RETL491916:GH4T-6054-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Plasmid; KW Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21876 MW; FCA91FB52B9F0DE0 CRC64; MKAFDLSLYL VLDPDLCARI GMVETARLAV AGGATMVQLR DKQAGTARMI ETGRALKQAL RGTGARLIVN DDVKAAIAIS ADGLHIGQED MDARTARGMI GPDMILGLSV ETEALAAAVD RDLVDYTGVG PVFATPTKAD HKQPIGFDGL ARLVQLSPVP SVAIGGLKAE HVPDVFAAGA KGLAVVSAVC GTPDPETATR RIAAEIRKVP A // ID B3Q548_RHIE6 Unreviewed; 204 AA. AC B3Q548; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiEc; Synonyms=thiE; OrderedLocusNames=RHECIAT_PC0000248; OS Rhizobium etli (strain CIAT 652). OG Plasmid pC. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=491916; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIAT 652; PLASMID=pC; RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P., RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J., RA Palacios R., Davila G.; RT "Genome diversity and DNA divergence of Rhizobium etli."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001077; ACE94329.1; -; Genomic_DNA. DR RefSeq; YP_001984879.1; NC_010997.1. DR ProteinModelPortal; B3Q548; -. DR STRING; 491916.RHECIAT_PC0000248; -. DR EnsemblBacteria; ACE94329; ACE94329; RHECIAT_PC0000248. DR GeneID; 6403135; -. DR KEGG; rec:RHECIAT_PC0000248; -. DR PATRIC; 23103564; VBIRhiEtl120572_4992. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; RETL491916:GH4T-4666-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Plasmid; KW Thiamine biosynthesis; Transferase. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 177 178 THZ-P binding (By similarity). FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22444 MW; 78D7AF5D37D33783 CRC64; MKLDPFYLIV DSAEWIERLV PLGVKLVQLR IKDRPGPVLR EEIRRSKAAC AAAACQLIIN DYWKLAIDEG CDFIHLGQED LAAADLNAIR RAGLKLGLST HDPSELETAL AAAPDYVALG PVWPTILKEM KWAPQGVERL ADWRRRVGPM PLVAIGGISA ERAPLVLENG ADSAAVVTDI TRNPDPEART RQWLAATAPW RSVK // ID B3QFS8_RHOPT Unreviewed; 202 AA. AC B3QFS8; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Rpal_4095; OS Rhodopseudomonas palustris (strain TIE-1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=395960; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TIE-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Emerson D., Newman D.K., Roden E., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris TIE-1."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001096; ACF02591.1; -; Genomic_DNA. DR RefSeq; YP_001993066.1; NC_011004.1. DR ProteinModelPortal; B3QFS8; -. DR STRING; 395960.Rpal_4095; -. DR EnsemblBacteria; ACF02591; ACF02591; Rpal_4095. DR GeneID; 6411779; -. DR KEGG; rpt:Rpal_4095; -. DR PATRIC; 23312687; VBIRhoPal88240_4134. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; RPAL395960:GHPC-4138-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 202 AA; 21801 MW; 34981A51167126E9 CRC64; MPYPDRFYPV VDSIAWVKRL AALGVGTVQL RAKDLDDGAA LQLVTDALAA VKDTPTKLII NDYWRAAIVA GAQHLHLGQE DLAEADLYEI KNAGLTLGLS THDDAELETA LAAEPDYIAL GPIFPTTLKS MRFAPQGIPK ITEWKKRVGN MPLVAIGGIK LEQAEEIFAA GADSIAVVSD VTQNPDPDAR VRAWLDFVAE KA // ID B3QFX4_RHOPT Unreviewed; 219 AA. AC B3QFX4; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Rpal_1009; OS Rhodopseudomonas palustris (strain TIE-1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=395960; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TIE-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Emerson D., Newman D.K., Roden E., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris TIE-1."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001096; ACE99565.1; -; Genomic_DNA. DR RefSeq; YP_001990041.1; NC_011004.1. DR ProteinModelPortal; B3QFX4; -. DR STRING; 395960.Rpal_1009; -. DR EnsemblBacteria; ACE99565; ACE99565; Rpal_1009. DR GeneID; 6408664; -. DR KEGG; rpt:Rpal_1009; -. DR PATRIC; 23306438; VBIRhoPal88240_1040. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RPAL395960:GHPC-1022-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 219 AA; 22590 MW; F3CA9717E89E9BE0 CRC64; MNAKPAPSRP APRLYLATPV TADPAAVAAA LPKLLAAADI AAVLLRLESS DPRTLTSRIK AVAPVVQAGG AALLVDGHAD LVARGGADGA HLSGIKAMQE WLPQLQPSRI AGVGGLETRH DSMIAGEAGA DYVLFGEPGA DGTRPSPEAI AERLDWWAEL FEPPCVGYAT SREEVHQFAT AGADFVLVGD FIWGADDPTA ALADAGEALR QGFAAAPRQ // ID B3QNM1_CHLP8 Unreviewed; 212 AA. AC B3QNM1; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Cpar_1117; OS Chlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. OS thiosulfatophilum (strain DSM 263 / NCIB 8327)). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=517417; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIB 8327; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., RA Liu Z., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobaculum parvum NCIB 8327."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001099; ACF11524.1; -; Genomic_DNA. DR RefSeq; YP_001998724.1; NC_011027.1. DR ProteinModelPortal; B3QNM1; -. DR STRING; 517417.Cpar_1117; -. DR EnsemblBacteria; ACF11524; ACF11524; Cpar_1117. DR GeneID; 6420048; -. DR KEGG; cpc:Cpar_1117; -. DR PATRIC; 21365485; VBIChlPar72705_1108. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INERSDI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPAR517417:GH95-1149-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 212 AA; 22596 MW; B62707DDD67AB1DD CRC64; MVRKQTPLPR LMIVSSGEEH RSLQGLALRQ AEALGCSAPV VYQLREKGLD AGELEALCRQ IVPAIKATGS LFTVNERFDI ALTSKASGVH LPEASCPPDA VRKAAPSLIV GQSVHSAKAA RAATAAGLDY LLFGPVFQTP SKEPFGAPQG LERLREVCRA TPLPVFAVGG ITPERSPSCI ECGAWGVAAM RPFFDPETMP ETINLFLSYL PS // ID B3QUZ3_CHLT3 Unreviewed; 212 AA. AC B3QUZ3; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ctha_2042; OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chloroherpeton. OX NCBI_TaxID=517418; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35110 / GB-78; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., RA Zhao F., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chloroherpeton thalassium ATCC 35110."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001100; ACF14494.1; -; Genomic_DNA. DR RefSeq; YP_001996941.1; NC_011026.1. DR ProteinModelPortal; B3QUZ3; -. DR STRING; 517418.Ctha_2042; -. DR EnsemblBacteria; ACF14494; ACF14494; Ctha_2042. DR GeneID; 6423122; -. DR KEGG; cts:Ctha_2042; -. DR PATRIC; 21433185; VBIChlTha99257_2385. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTLLQYR; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CTHA517418:GHTO-2082-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22557 MW; 270A07E1757D61DE CRC64; MRKKHIGQLC AITDTHIQSR FSHVELARLA LQGGADIIQL RDKTLPTSEL FCIAKEILTL CQALGGKLII NDRADIALAA DADGVHLGQD DLPIAEARKL LGENKIIGAT ASTLALAKQA EFDGADYIGF GHIFPTSTKH KPEPPKGVLA ISEIKKSLRI PVMAIGGIDY ENIGEVMRAG ADSAAVVSAI CCAENPEAAT QEIKKQIAEA IK // ID B3QUZ4_CHLT3 Unreviewed; 207 AA. AC B3QUZ4; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Precursor; GN Name=thiE; OrderedLocusNames=Ctha_2043; OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chloroherpeton. OX NCBI_TaxID=517418; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35110 / GB-78; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., RA Zhao F., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chloroherpeton thalassium ATCC 35110."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001100; ACF14495.1; -; Genomic_DNA. DR RefSeq; YP_001996942.1; NC_011026.1. DR ProteinModelPortal; B3QUZ4; -. DR STRING; 517418.Ctha_2043; -. DR EnsemblBacteria; ACF14495; ACF14495; Ctha_2043. DR GeneID; 6423123; -. DR KEGG; cts:Ctha_2043; -. DR PATRIC; 21433187; VBIChlTha99257_2386. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INERSDI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CTHA517418:GHTO-2083-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Signal; Thiamine biosynthesis; Transferase. FT SIGNAL 1 19 Potential. FT CHAIN 20 207 Potential. FT /FTId=PRO_5000378658. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22291 MW; C32B40309FC85EEF CRC64; MKKKSLPRLM LITNQARANA PLQEIVEKAA TAGGCMVQLR EKALSGKNLF ELAKELRKIT EPHDTPLLIN ERLDIALAAH ADGLHLPETG LSIETTRKFM PNGLIGKSVH SLQGAWDAEI AGADYVLFGH IFPTASKPND AKPRGLAELE SLCQAVQIPV FAVGGITPER TKACLNAGAY GVAAIGALMQ IEHLESTLQS FHQVLEL // ID B3SFJ5_TRIAD Unreviewed; 214 AA. AC B3SFJ5; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 34. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=TRIADDRAFT_62984; OS Trichoplax adhaerens (Trichoplax reptans). OC Eukaryota; Metazoa; Placozoa; Trichoplax. OX NCBI_TaxID=10228; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Grell-BS-1999; RX PubMed=18719581; DOI=10.1038/nature07191; RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U., RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L., RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J., RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., RA Dellaporta S.L., Rokhsar D.S.; RT "The Trichoplax genome and the nature of placozoans."; RL Nature 454:955-960(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS986364; EDV18500.1; -; Genomic_DNA. DR RefSeq; XP_002119014.1; XM_002118978.1. DR ProteinModelPortal; B3SFJ5; -. DR STRING; 10228.JGI62984; -. DR EnsemblMetazoa; TriadT62984; TriadP62984; TriadG62984. DR GeneID; 6760228; -. DR KEGG; tad:TRIADDRAFT_62984; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG76X63G; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 214 AA; 23959 MW; 7A3B7F5B987A4B0B CRC64; MLRDALKLYL VTNRNKQISD IEFLDIIEKS IIGGVTSVQL REKNLEDDEF LKIAYQCKEI TSTYSIPLFI NDNLAIAKKA LADGVHLGQS DILLNNAREF LGNDFIIGIS VNNLSQLNNN QNIFADYISL GPIFYTNTKL DIEKPIGIEE ISLLTKNKIK PTILIGGIKL DNIHQLMNSN VDGFAISSAI FNDQNPKIQA SKFKFKINEL QKGA // ID B3TA32_9ZZZZ Unreviewed; 110 AA. AC B3TA32; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=ALOHA_HF4000APKG8C21ctg1g29; OS uncultured marine microorganism HF4000_APKG8C21. OC unclassified sequences; environmental samples. OX NCBI_TaxID=455553; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=18580971; DOI=10.1038/ismej.2008.62; RA Konstantinidis K.T., Delong E.F.; RT "Genomic patterns of recombination, clonal divergence and environment RT in marine microbial populations."; RL ISME J. 2:1052-1065(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EU016651; ABZ09441.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 110 AA; 10731 MW; A1308DB0F2E7BD3F CRC64; MGRPSSRPGL GGVLRSLTVF ARPGPEAVKV VVTIAGSDSS GGLKLEEGTS QAVSPLPVLA MGGTDEANAG AVTASGAAGV AVRGAILQAA DPRETALPIR KTLSTKGNPG // ID B3WSV1_ECOLX Unreviewed; 211 AA. AC B3WSV1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EcB171_0594; OS Escherichia coli B171. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=344601; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B171; RA Rasko D.A., Rosovitz M.J., Kaper J.B., Myers G.S.A., Sheshadri R., RA Cer R.Z., Jiang L., Ravel J.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B171; RA Rasko D., Rosovitz M., Myers G., Seshadri R., Cer R., Jiang L., RA Ravel J., Fricke W.F., Sebastian Y.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJX02000048; EDX28302.1; -; Genomic_DNA. DR ProteinModelPortal; B3WSV1; -. DR SMR; B3WSV1; 10-208. DR EnsemblBacteria; EDX28302; EDX28302; EcB171_0594. DR PATRIC; 31236506; VBIEscCol100091_4527. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B3X5V1_SHIDY Unreviewed; 194 AA. AC B3X5V1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Sd1012_1230; OS Shigella dysenteriae 1012. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=358708; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1012; RA Rasko D.A., Rosovitz M.J., Brinkley C., Myers G.S.A., Sheshadri R., RA Cer R.Z., Jiang L., Ravel J.; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1012; RA Rasko D., Rosovitz M., Myers G., Seshadri R., Cer R., Jiang L., RA Ravel J., Fricke W.F., Sebastian Y.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMJ02000043; EDX33120.1; -; Genomic_DNA. DR ProteinModelPortal; B3X5V1; -. DR EnsemblBacteria; EDX33120; EDX33120; Sd1012_1230. DR PATRIC; 28582148; VBIShiDys19375_4661. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 117 119 THZ-P binding (By similarity). FT REGION 169 170 THZ-P binding (By similarity). FT METAL 53 53 Magnesium (By similarity). FT METAL 72 72 Magnesium (By similarity). FT BINDING 52 52 HMP-PP (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 194 AA; 21054 MW; 03EC7BA0FF854F6F CRC64; MVDSVQWIER LLDAGVRTLQ LRIKDRRDEE VEADVVAAIA LGRRYNARLF INDYWRLAIK HQAYGVHLGQ EDLQATDLNA IRAAGLRLGV STHDDMEIDV ALAARPSYIA LGHVFPTQTK QMPSAPQGLE QLARHVERLA DYPTVAIGGI SLARAPAVIA TGVGSIAVVS AITQAADWRL ATAQLLEIAG VGDE // ID B3XJN1_ECOLX Unreviewed; 211 AA. AC B3XJN1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EC1011_3724; OS Escherichia coli 101-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=358709; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=101-1; RA Rasko D.A., Rosovitz M.J., Nataro J.P., Myers G.S.A., Sheshadri R., RA Cer R.Z., Jiang L., Ravel J.; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=101-1; RA Rasko D., Rosovitz M., Myers G., Seshadri R., Cer R., Jiang L., RA Ravel J., Fricke W.F., Sebastian Y.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMK02000037; EDX37292.1; -; Genomic_DNA. DR ProteinModelPortal; B3XJN1; -. DR SMR; B3XJN1; 20-202. DR EnsemblBacteria; EDX37292; EDX37292; EC1011_3724. DR PATRIC; 30344150; VBIEscCol127656_4540. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B3XLB5_LACRE Unreviewed; 215 AA. AC B3XLB5; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Lreu23DRAFT_3792; OS Lactobacillus reuteri 100-23. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=349123; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=100-23; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Bruce D., RA Pitluck S., Richardson P.; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=100-23; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., RA Walter J., Heng N.C.K., Tannock G.W., Richardson P.; RT "Permanent Draft sequence of Lactobacillus reuteri 100-23."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPZ02000001; EDX42276.1; -; Genomic_DNA. DR ProteinModelPortal; B3XLB5; -. DR EnsemblBacteria; EDX42276; EDX42276; Lreu23DRAFT_3792. DR PATRIC; 26514630; VBILacReu112121_0067. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23869 MW; 795038F3C46546DF CRC64; MMFDPKMLQV YLVGGTQDVH NDVVKFLEKV ELAMKSGITA FQYREKGNSK LRPNERVDLG LELRTLCTRY GIPLIVDDDY ELAQQINADG VHVGQNDTKI EQVSVAVGHQ MFIGYSCNTP EQVERANTMD FVDYIGCGPV FPTKSKPDAD TAIGINRLER LNMISERPVV AIGGIDEENM KVVHDTGVAG LAVISLVFDS KDLAATVKEM KKLYK // ID B3YH27_SALET Unreviewed; 211 AA. AC B3YH27; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SeKA_A3805; OS Salmonella enterica subsp. enterica serovar Kentucky str. CVM29188. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=439842; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CVM29188; RX PubMed=21602358; DOI=10.1128/JB.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAK02000001; EDX47660.1; -; Genomic_DNA. DR ProteinModelPortal; B3YH27; -. DR EnsemblBacteria; EDX47660; EDX47660; SeKA_A3805. DR PATRIC; 27976692; VBISalEnt954_3935. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22833 MW; F86B5A68649B3A94 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIEHLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHNA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSVAVVSAIT QAANWREATA QLLAIAGVGD E // ID B3YV12_BACCE Unreviewed; 219 AA. AC B3YV12; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BCW_0404; OS Bacillus cereus W. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405917; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=W; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Ravel J., RA Sutton G.; RT "Genome sequence of Bacillus cereus W."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCZ02000007; EDX56580.1; -; Genomic_DNA. DR ProteinModelPortal; B3YV12; -. DR EnsemblBacteria; EDX56580; EDX56580; BCW_0404. DR PATRIC; 25111043; VBIBacCer31393_2798. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23438 MW; D01B099F285CFAEC CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA AGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID B3Z0N4_BACCE Unreviewed; 206 AA. AC B3Z0N4; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 23. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BCW_0737; OS Bacillus cereus W. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405917; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=W; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Ravel J., RA Sutton G.; RT "Genome sequence of Bacillus cereus W."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCZ02000021; EDX54755.1; -; Genomic_DNA. DR ProteinModelPortal; B3Z0N4; -. DR EnsemblBacteria; EDX54755; EDX54755; BCW_0737. DR PATRIC; 25115167; VBIBacCer31393_4753. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID B3Z3H0_BACCE Unreviewed; 206 AA. AC B3Z3H0; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 22. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BC059799_0733; OS Bacillus cereus NVH0597-99. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=451707; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVH0597-99; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Ravel J., RA Sutton G.; RT "Genome sequence of Bacillus cereus NVH0597-99."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVH0597-99; RA Joardar V., Shrivastava S., Brinkac L.M., Harkins D.M., Durkin A.S., RA Sutton G.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDK02000001; EDX70120.1; -; Genomic_DNA. DR ProteinModelPortal; B3Z3H0; -. DR EnsemblBacteria; EDX70120; EDX70120; BC059799_0733. DR PATRIC; 24989650; VBIBacCer85191_0526. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22879 MW; BB47B746E523CE62 CRC64; MKNELHVISN GNMSFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPPSK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAV EAFKSGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID B3ZAM1_BACCE Unreviewed; 219 AA. AC B3ZAM1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BC059799_0357; OS Bacillus cereus NVH0597-99. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=451707; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVH0597-99; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Ravel J., RA Sutton G.; RT "Genome sequence of Bacillus cereus NVH0597-99."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVH0597-99; RA Joardar V., Shrivastava S., Brinkac L.M., Harkins D.M., Durkin A.S., RA Sutton G.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDK02000010; EDX67707.1; -; Genomic_DNA. DR ProteinModelPortal; B3ZAM1; -. DR EnsemblBacteria; EDX67707; EDX67707; BC059799_0357. DR PATRIC; 24994827; VBIBacCer85191_3104. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23481 MW; D48CA359285CF02A CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVKLALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID B3ZQ39_BACCE Unreviewed; 219 AA. AC B3ZQ39; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BC03BB108_0364; OS Bacillus cereus 03BB108. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=451709; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=03BB108; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus 03BB108."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDM02000008; EDX62520.1; -; Genomic_DNA. DR ProteinModelPortal; B3ZQ39; -. DR EnsemblBacteria; EDX62520; EDX62520; BC03BB108_0364. DR PATRIC; 24742069; VBIBacCer75314_2861. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23482 MW; D33A0EEF285CFD9C CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID B3ZU87_BACCE Unreviewed; 206 AA. AC B3ZU87; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 22. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BC03BB108_0711; OS Bacillus cereus 03BB108. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=451709; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=03BB108; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus 03BB108."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDM02000017; EDX61166.1; -; Genomic_DNA. DR ProteinModelPortal; B3ZU87; -. DR EnsemblBacteria; EDX61166; EDX61166; BC03BB108_0711. DR PATRIC; 24745082; VBIBacCer75314_4305. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22936 MW; 82BF311EA1599DF0 CRC64; MKNELHVISN GNMSFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPPSK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHAG YSVHSLEEAI EAFKNGADSL VYGHVFPTDC KKDVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID B4AC44_SALNE Unreviewed; 211 AA. AC B4AC44; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SNSL317_A2324; OS Salmonella enterica subsp. enterica serovar Newport str. SL317. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=454168; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SL317; RX PubMed=21602358; DOI=10.1128/JB.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABEW01000017; EDX48392.1; -; Genomic_DNA. DR ProteinModelPortal; B4AC44; -. DR EnsemblBacteria; EDX48392; EDX48392; SNSL317_A2324. DR PATRIC; 27988431; VBISalEnt75003_4710. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22852 MW; EA4D23D59BB9C5DA CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA GHITRLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID B4AF83_BACPU Unreviewed; 205 AA. AC B4AF83; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-MAR-2014, entry version 22. DE SubName: Full=Regulatory protein TenI; GN ORFNames=BAT_2970; OS Bacillus pumilus ATCC 7061. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=536229; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 7061; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Venkateswaran K., Fox G., Laduc M.T., RA Brettin T.S.; RT "Genome sequence of Bacillus pumilis ATCC 7061."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABRX01000001; EDW23088.1; -; Genomic_DNA. DR ProteinModelPortal; B4AF83; -. DR EnsemblBacteria; EDW23088; EDW23088; BAT_2970. DR PATRIC; 25203356; VBIBacPum54595_0735. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 205 AA; 22633 MW; 83E420A9ED27AA29 CRC64; MELHAVTNDS LPAGELIKQI KNIAPEVDFI HIRERSKTAS ELVDLVKGLL LEGVPKEKLI INDRVDVALL TNIHRVHLPG HSFSPKELRQ KFPHLHAGVS VHSIEEGKAA EKNGAEYVIF GHVYDTTCKP GLQARGVQLV KELTSLLSIP VVAIGGVTPD RIPELRHANV KGIAVMSGIF THHQPRKMAQ AFSKQVKEHP YEEAL // ID B4AJN3_BACPU Unreviewed; 222 AA. AC B4AJN3; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-MAR-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BAT_0926; OS Bacillus pumilus ATCC 7061. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=536229; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 7061; RA Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Sutton G., Venkateswaran K., Fox G., Laduc M.T., RA Brettin T.S.; RT "Genome sequence of Bacillus pumilis ATCC 7061."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABRX01000004; EDW21282.1; -; Genomic_DNA. DR ProteinModelPortal; B4AJN3; -. DR EnsemblBacteria; EDW21282; EDW21282; BAT_0926. DR PATRIC; 25206592; VBIBacPum54595_2317. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23888 MW; B2DB4BCB545DBA0C CRC64; MTKTDQQQIK QQLSVYFIMG TANTSRQPLD VLKEAIQGGI TMFQFREKGE GALQGEEKKQ LARQLQVLCQ EANVPFIVND DVQLAIDLDA DGVHVGQEDT NAEDVRQKIG NKILGVSTHN LDEVKQAMKD GADYVGMGPV YPTETKKDTR SVQGVSLITE VRHHGLHIPI VGIGGITYGN AAPVIQAGAD GISIISAISQ SADPKKAAEE LKALVASEKV SL // ID B4BKC2_9BACI Unreviewed; 221 AA. AC B4BKC2; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=G11MC16DRAFT_0858; OS Geobacillus sp. G11MC16. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=495036; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=G11MC16; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Mead D.; RT "Sequencing of the draft genome and assembly of Geobacillus sp. RT G11MC16."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVH01000002; EDY06886.1; -; Genomic_DNA. DR ProteinModelPortal; B4BKC2; -. DR EnsemblBacteria; EDY06886; EDY06886; G11MC16DRAFT_0858. DR PATRIC; 28768292; VBIGeoSp31856_0892. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23484 MW; E2314376009A8319 CRC64; MARITSEEMK KRLAVYFIMG SQNSERPAED VLKEALDGGV TLFQFREKGS AALEGEEKEA LARQLQRLCR TYGVPFIVND DVELAIAIDA DGVHVGQDDE DARRVREKIG DKILGVSAHN VEEARAAIEA GADYIGVGPI YPTRSKDDAN EAQGPGILRH LREQGITIPI VAIGGITADN TRAVIEAGAD GVSVISAIAS APEPKAAAAA LATAVREANL R // ID B4BRU7_9BACI Unreviewed; 203 AA. AC B4BRU7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 23. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=G11MC16DRAFT_3136; OS Geobacillus sp. G11MC16. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=495036; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=G11MC16; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Mead D.; RT "Sequencing of the draft genome and assembly of Geobacillus sp. RT G11MC16."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVH01000015; EDY04541.1; -; Genomic_DNA. DR ProteinModelPortal; B4BRU7; -. DR EnsemblBacteria; EDY04541; EDY04541; G11MC16DRAFT_3136. DR PATRIC; 28773115; VBIGeoSp31856_3260. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 203 AA; 21573 MW; 7F5C0BD4F1F6C955 CRC64; MGTLHFVSTG RQTADEFAAI CQHIHPYADC IHIREKEKTA REVAAFVTAL LRVGVPPQKI IVNDRVDVAA VYGVHGVQLA YHSLPVRAVR RSFPSLTVGC SVHGLAEAKQ AEEDGAHFCL FGHIFPTASK PGVLPRGVDL LKEIAAAVHI PVIAIGGIHA GNARRVLEAG AAGVAVLSAI FFAADPVSEA KRLAEIVKGE RIK // ID B4CYD8_9BACT Unreviewed; 218 AA. AC B4CYD8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CfE428DRAFT_1676; OS Chthoniobacter flavus Ellin428. OC Bacteria; Verrucomicrobia; Spartobacteria; Chthoniobacter. OX NCBI_TaxID=497964; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ellin428; RX PubMed=21460085; DOI=10.1128/JB.00295-11; RA Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A., RA Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., RA Pitluck S., Larimer F.W., Land M.L., Hauser L., Sangwan P., RA de Vos W.M., Janssen P.H., Smidt H.; RT "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic RT heterotrophic soil bacterium."; RL J. Bacteriol. 193:2902-2903(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVL01000004; EDY20479.1; -; Genomic_DNA. DR ProteinModelPortal; B4CYD8; -. DR EnsemblBacteria; EDY20479; EDY20479; CfE428DRAFT_1676. DR PATRIC; 27074146; VBIChtFla82190_1690. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23250 MW; FB4DBD383E0AB11C CRC64; MKNLADALLY GILDLGYTPA DDVERVTEQM LAGGVDILQL RAKDWDESAV ESLCNRLLPL TEGAGVPFII NDYPQLVPSV GAQGAHVGQD DFTVSDARWR AGRALAGEVP PVIIGKSTHS FEQAVAAAAD GADYIGFGPL FATPTKPGRP AIGLENIARI HETVQIPIFC IGGIKWENLD AIIEAGARRV VIVSGLLQAP DIAAYARRAK ERLLNNAI // ID B4E623_BURCJ Unreviewed; 374 AA. AC B4E623; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BCAL0300; OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 OS / NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=216591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / RC CF5610; RX PubMed=18931103; DOI=10.1128/JB.01230-08; RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., RA Bentley S.D., Cerdeno-Tarraga A.M., Thomson N.R., Bason N., RA Quail M.A., Sharp S., Cherevach I., Churcher C., Goodhead I., RA Hauser H., Holroyd N., Mungall K., Scott P., Walker D., White B., RA Rose H., Iversen P., Mil-Homens D., Rocha E.P., Fialho A.M., RA Baldwin A., Dowson C., Barrell B.G., Govan J.R., Vandamme P., RA Hart C.A., Mahenthiralingam E., Parkhill J.; RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of RT cystic fibrosis patients."; RL J. Bacteriol. 191:261-277(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM747720; CAR50610.1; -; Genomic_DNA. DR RefSeq; YP_002229466.1; NC_011000.1. DR ProteinModelPortal; B4E623; -. DR STRING; 216591.BCAL0300; -. DR GeneID; 6934182; -. DR KEGG; bcj:BCAL0300; -. DR PATRIC; 19072265; VBIBurCen118154_0317. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BCEN216591:GJI4-322-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 374 AA; 39299 MW; B51D61B0A1A7927E CRC64; MSARFADAFW PPADELAEAA ERIRARLGDW PDGVAPWRLC VAAPDVPADG DVLIVSAGDR AAQARASAVS RPASPDAVAI EFDERSAVLH AAGVRYALDA AHPLADDWIA ALAAFLDCGF APVDALVLAL AWRDGDETHA ADAWPVDAER FPCVAGLPPA PEPAFPPCPA QLGLYPVVPS AEWVERVLDG GARTVQLRVK DATPDTLRQE IARAVAAGRR YPDARVFIND HWQIAAEEGA YGVHLGQEDL ETADLAAIAR AGLRLGLSSH GYYEMLRALH ERPSYLALGP VYATATKAVA APPQGLARIA RYARFAGARA PLVAIGGVGL DALPAVLATG VGSVAVVSAV TGAADYRTAL IALQQCFAGQ FDNR // ID B4EN00_BURCJ Unreviewed; 198 AA. AC B4EN00; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 34. DE SubName: Full=Putative exported protein; DE Flags: Precursor; GN ORFNames=BCAM0882; OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 OS / NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=216591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / RC CF5610; RX PubMed=18931103; DOI=10.1128/JB.01230-08; RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., RA Bentley S.D., Cerdeno-Tarraga A.M., Thomson N.R., Bason N., RA Quail M.A., Sharp S., Cherevach I., Churcher C., Goodhead I., RA Hauser H., Holroyd N., Mungall K., Scott P., Walker D., White B., RA Rose H., Iversen P., Mil-Homens D., Rocha E.P., Fialho A.M., RA Baldwin A., Dowson C., Barrell B.G., Govan J.R., Vandamme P., RA Hart C.A., Mahenthiralingam E., Parkhill J.; RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of RT cystic fibrosis patients."; RL J. Bacteriol. 191:261-277(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM747721; CAR54739.1; -; Genomic_DNA. DR RefSeq; YP_002233500.1; NC_011001.1. DR ProteinModelPortal; B4EN00; -. DR STRING; 216591.BCAM0882; -. DR GeneID; 6928623; -. DR KEGG; bcj:BCAM0882; -. DR PATRIC; 19080957; VBIBurCen118154_4596. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCEN216591:GJI4-4503-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 198 Potential. FT /FTId=PRO_5000387844. SQ SEQUENCE 198 AA; 20567 MW; AC925331ED3EFD47 CRC64; MRRTMNAPLP RCCVITPEPA SASAADRAAF LDRLSAVLAR GETLVQLRVK SLDAAAFAAL AAAALARCDA AGAHLMLNGP IDAAGVMRLD GAGWHLDGAA LRGVTQRPLP ADRWVSAACH SQDDLLLAAQ AGADFVTLSP VLPTLSHPGA PTLGWARFDT LAAQAAMPVF ALGGMTRAHL DDARRHGAYG IAGIRGFW // ID B4FXC3_MAIZE Unreviewed; 390 AA. AC B4FXC3; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 2. DT 19-MAR-2014, entry version 33. DE SubName: Full=Uncharacterized protein; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B73; RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740; RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J., RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., RA Fernandes J., Walbot V., Yu Y.; RT "Sequencing, mapping, and analysis of 27,455 maize full-length RT cDNAs."; RL PLoS Genet. 5:E1000740-E1000740(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BT041761; ACF86766.2; -; mRNA. DR ProteinModelPortal; B4FXC3; -. DR PRIDE; B4FXC3; -. DR Gramene; B4FXC3; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 390 AA; 41488 MW; 43556106D704F95D CRC64; MVSTSGDTLS GPSTLATYRD ELFSMADIVT PNVKEASKLL GDVSLHTISD MCNAAESIYK LGPKYVLVKG GDMPDSSDAI DVLFDGKEFT ELRGLRIKTR NTHGTGCTLA SCIAAELAKG ATMLHAVQAA KKFVESALYH SKDLVIGNGP QGPFDHHFEL KSPSYKMGSL QKFNPDDLFL YAVTDSGMNK KWGRSIKDAV KAAIEGGATI VQLREKDAET REFLEAAKAC VEICKSSGVP LLINDRVDVA LACDADGVHV GQSDMPAWEV RRLLGPGKII GVSCKTPAQA EQAWKDGADY IGCGGVFPTT TKANNPTLGF EGLRTVCLAS KLPVVAIGGI NAGNAGSVME LGLPNLKGVA VVSALFDRER VAAETRNLRS ILMKNAYSRS // ID B4RAL1_PHEZH Unreviewed; 216 AA. AC B4RAL1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PHZ_c3200; OS Phenylobacterium zucineum (strain HLK1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Phenylobacterium. OX NCBI_TaxID=450851; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLK1; RX PubMed=18700039; DOI=10.1186/1471-2164-9-386; RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., RA Hu X.; RT "Complete genome of Phenylobacterium zucineum - a novel facultative RT intracellular bacterium isolated from human erythroleukemia cell line RT K562."; RL BMC Genomics 9:386-386(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000747; ACG79609.1; -; Genomic_DNA. DR RefSeq; YP_002132038.1; NC_011144.1. DR ProteinModelPortal; B4RAL1; -. DR STRING; 450851.PHZ_c3200; -. DR EnsemblBacteria; ACG79609; ACG79609; PHZ_c3200. DR GeneID; 6789150; -. DR KEGG; pzu:PHZ_c3200; -. DR PATRIC; 22929742; VBIPheZuc44517_3928. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PZUC450851:GHUG-3242-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22513 MW; 9722B7E9F0A5E4FB CRC64; MAEPLCRLYL ITPPRIDDLA AFGHVLAHAL DAGDVAALQI RLKDQPDEVV AAAVDALAPI AQARGVAVIL NDRPDLAARL GCDGVHVGQD DAPYAEARRI MGKDKIVGVT CHDSRHLAME AAEAGADYVA FGAFHPTATK EPKTRADPEI LTIWQETMET PCVAIGGITV ENARALAAAG ADFLAVSAGV WSHGEGPAAA VKALNDEIAK GLADRA // ID B4RCZ1_PHEZH Unreviewed; 200 AA. AC B4RCZ1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 34. DE SubName: Full=Thiamine monophosphate synthase; GN Name=thiE; OrderedLocusNames=PHZ_c3514; OS Phenylobacterium zucineum (strain HLK1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Phenylobacterium. OX NCBI_TaxID=450851; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLK1; RX PubMed=18700039; DOI=10.1186/1471-2164-9-386; RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., RA Hu X.; RT "Complete genome of Phenylobacterium zucineum - a novel facultative RT intracellular bacterium isolated from human erythroleukemia cell line RT K562."; RL BMC Genomics 9:386-386(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000747; ACG79923.1; -; Genomic_DNA. DR RefSeq; YP_002132352.1; NC_011144.1. DR ProteinModelPortal; B4RCZ1; -. DR STRING; 450851.PHZ_c3514; -. DR EnsemblBacteria; ACG79923; ACG79923; PHZ_c3514. DR GeneID; 6789467; -. DR KEGG; pzu:PHZ_c3514; -. DR PATRIC; 22930430; VBIPheZuc44517_4269. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NRRDSIM; -. DR OrthoDB; EOG699751; -. DR BioCyc; PZUC450851:GHUG-3559-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 200 AA; 20498 MW; 51D7CA42C962C7D4 CRC64; MERTARLLPA RRRLRKALPA LLFFTDPART PDPLAAARAL PPGSGIVYRA FGDPGALATA RALKQVARAR GLVLLVGQDA QLAAAAGADG VHLPERLARL AMPLKRARPG WIVTAAAHSL AAARTPGPDA VVISAAFPSN SPSAGPPLGP VRLAALARAA GRPAYALGGV NMKTARRLRD AGLIGLAAVE GLSPETSART // ID B4RQM5_NEIG2 Unreviewed; 205 AA. AC B4RQM5; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NGK_2231; OS Neisseria gonorrhoeae (strain NCCP11945). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=521006; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCCP11945; RX PubMed=18586945; DOI=10.1128/JB.00566-08; RA Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.; RT "Complete genome sequence of Neisseria gonorrhoeae NCCP11945."; RL J. Bacteriol. 190:6035-6036(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001050; ACF30835.1; -; Genomic_DNA. DR RefSeq; YP_002002856.1; NC_011035.1. DR ProteinModelPortal; B4RQM5; -. DR STRING; 521006.NGK_2231; -. DR EnsemblBacteria; ACF30835; ACF30835; NGK_2231. DR GeneID; 6447554; -. DR KEGG; ngk:NGK_2231; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NGON521006:GJ73-2280-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21779 MW; 1353772F6A7897A9 CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFQ TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID B4S7K7_PROA2 Unreviewed; 202 AA. AC B4S7K7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Paes_1005; OS Prosthecochloris aestuarii (strain DSM 271 / SK 413). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Prosthecochloris. OX NCBI_TaxID=290512; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 271 / SK 413; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., RA Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM RT 271."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001108; ACF46044.1; -; Genomic_DNA. DR RefSeq; YP_002015691.1; NC_011059.1. DR ProteinModelPortal; B4S7K7; -. DR STRING; 290512.Paes_1005; -. DR EnsemblBacteria; ACF46044; ACF46044; Paes_1005. DR GeneID; 6458901; -. DR KEGG; paa:Paes_1005; -. DR PATRIC; 23041756; VBIProAes37017_1056. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PAES290512:GHUT-1040-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 31 35 HMP-PP binding (By similarity). FT REGION 128 130 THZ-P binding (By similarity). FT REGION 179 180 THZ-P binding (By similarity). FT METAL 64 64 Magnesium (By similarity). FT METAL 83 83 Magnesium (By similarity). FT BINDING 63 63 HMP-PP (By similarity). FT BINDING 102 102 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 159 159 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 202 AA; 21332 MW; F5D8AE48882C7880 CRC64; MNKLLCFITT QQDNPEIVAE EALKGGTGMI QLRHKNASGH DLFTWALSIG KMCRRYGALF IVNDRLDIAL AAGADGVHLG QNDLPIDVAR KLLPSPAIIG CSVSSVHEAL DAQQKGADYI GLGHIFPTGS KQKENAPLGP EYIRTVKQSV DIPLIAIGGI GLDNAREVMS NGADGLAVIS AISSAVNPAE AARELAIIIE QT // ID B4S7K8_PROA2 Unreviewed; 216 AA. AC B4S7K8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Paes_1006; OS Prosthecochloris aestuarii (strain DSM 271 / SK 413). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Prosthecochloris. OX NCBI_TaxID=290512; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 271 / SK 413; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., RA Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM RT 271."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001108; ACF46045.1; -; Genomic_DNA. DR RefSeq; YP_002015692.1; NC_011059.1. DR ProteinModelPortal; B4S7K8; -. DR STRING; 290512.Paes_1006; -. DR EnsemblBacteria; ACF46045; ACF46045; Paes_1006. DR GeneID; 6458908; -. DR KEGG; paa:Paes_1006; -. DR PATRIC; 23041758; VBIProAes37017_1057. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INERSDI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PAES290512:GHUT-1041-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23465 MW; 287B1C603078C431 CRC64; MPSPGHELPR LYMVTYSRVF SFPEEKLPSL VSSAVSRSRI IVQLREKHLD TARLYTLAAR LQSAINKSDS LLFINERSDI ALAVGANGVH MPEQSCPLSA TRSICPGLYT GKSTHSVQSA ITAEQDGADY LLFGPVFDTP LKRKYGPPQG VKQLGEICKN VSVPVFAIGG ITPENAASCL DEGAYGLAAM SLFASPTNLH RTIESFQTIL NHVHHE // ID B4SA53_PELPB Unreviewed; 215 AA. AC B4SA53; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Ppha_1499; OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Pelodictyon. OX NCBI_TaxID=324925; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5477 / BU-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., RA Zhao F., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001110; ACF43749.1; -; Genomic_DNA. DR RefSeq; YP_002018366.1; NC_011060.1. DR ProteinModelPortal; B4SA53; -. DR STRING; 324925.Ppha_1499; -. DR EnsemblBacteria; ACF43749; ACF43749; Ppha_1499. DR GeneID; 6463492; -. DR KEGG; pph:Ppha_1499; -. DR PATRIC; 22903592; VBIPelPha134556_1573. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPHA324925:GHBF-1528-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 215 AA; 23341 MW; FD31405C677D8D63 CRC64; MKHNRKKETP LPRLHLISSG KESSDTSTPL LNQLSLLPGS FPCMVQIREK QLNAKELLNL ALKARAIKAP EGTLLLINER ADIALAAGLD GVHLPESGCS ASKLRPFTPG MIYGYSVHSA SALRMAEESG ADYLLFGPVF DTPSKRRYGA PQGLEKLGAL CRSTSLPVFA LGGISPMNAR FCMDKGAYGI AGISLFQERS RLAEIIEQLY LHLHP // ID B4SA54_PELPB Unreviewed; 207 AA. AC B4SA54; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ppha_1500; OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Pelodictyon. OX NCBI_TaxID=324925; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5477 / BU-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., RA Zhao F., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001110; ACF43750.1; -; Genomic_DNA. DR RefSeq; YP_002018367.1; NC_011060.1. DR ProteinModelPortal; B4SA54; -. DR STRING; 324925.Ppha_1500; -. DR EnsemblBacteria; ACF43750; ACF43750; Ppha_1500. DR GeneID; 6463490; -. DR KEGG; pph:Ppha_1500; -. DR PATRIC; 22903594; VBIPelPha134556_1574. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPHA324925:GHBF-1529-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21503 MW; FEA848A4860DA2C3 CRC64; MIPSPPFLCV ITDEALCPVT LAEQALKGGA AMIQLRHKTA SGSQLFSWAV EISKRCHQYH ALCIINDRVD IALASSADGV HLGQQDMPAS TARKLLGKMA IIGVSASSPD EARLAEQEGA DYIGFGHIYP TASKVKEFSP VGVEALRKTA AIVSLPIIAI GGITIENSAS LISCGASGVA VISAVSKAND PSKAAHELLC AIQGREA // ID B4SI22_STRM5 Unreviewed; 208 AA. AC B4SI22; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Smal_3287; OS Stenotrophomonas maltophilia (strain R551-3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=391008; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R551-3; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J., RA van der Lelie D., Richardson P.; RT "Complete sequence of Stenotrophomonas maltophilia R551-3."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001111; ACF52986.1; -; Genomic_DNA. DR RefSeq; YP_002029669.1; NC_011071.1. DR ProteinModelPortal; B4SI22; -. DR STRING; 391008.Smal_3287; -. DR EnsemblBacteria; ACF52986; ACF52986; Smal_3287. DR GeneID; 6476415; -. DR KEGG; smt:Smal_3287; -. DR PATRIC; 23711562; VBISteMal40512_3312. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SMAL391008:GH1H-3362-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21191 MW; B61C6DE9622C281A CRC64; MTSASPAPRG VYLITPDEPD TARLLDRTAP LLAAGATWLQ YRNKTASDAL RREQATALQA LCAEHGVPLI VNDDPALAKA VGAAGVHLGG TDGDIPSARA LLGADAIIGA SCYDQLANAE QAVAAGASYV AFGAFFPTTT KITTSRAHTD LLRQSAALGV PRVAIGGLTP DNVGPIIDAG ADLVAVVSSV FAAEDPVATQ RAYLAQFA // ID B4SJY5_STRM5 Unreviewed; 318 AA. AC B4SJY5; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=Smal_0612; OS Stenotrophomonas maltophilia (strain R551-3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=391008; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R551-3; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J., RA van der Lelie D., Richardson P.; RT "Complete sequence of Stenotrophomonas maltophilia R551-3."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001111; ACF50317.1; -; Genomic_DNA. DR RefSeq; YP_002027000.1; NC_011071.1. DR ProteinModelPortal; B4SJY5; -. DR STRING; 391008.Smal_0612; -. DR EnsemblBacteria; ACF50317; ACF50317; Smal_0612. DR GeneID; 6477558; -. DR KEGG; smt:Smal_0612; -. DR PATRIC; 23706056; VBISteMal40512_0620. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SMAL391008:GH1H-625-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 318 AA; 34988 MW; 187D127FDB28B5DE CRC64; MPSPTRSIHV VAAVITDARG RVLLNRRTEN RDMAGLWEFP GGKRESGETS EQALVRELRE ELGIEADVGE WLMDVPQRYP DKHLTLEVRH VRSWKGTPRG REGQAITWVA PDKLGRYSMP PADLPVVAAL RQPDSYLITP APADDDSGIQ HWHEQLQRAV GAGQQRIQLR LPPTHPQRQA MLEQALRTHR RSGVQWLLNR DIELARALGV GVHLGSEQLL ELEKRPLPEG QLVAASCHDL RQLQAAQRLG CDFAVLGPVQ ATASHPAATP MGWDAFAALR AQVSLPIYAL GGMGSGHIAE ARRHGGQGIA AIRALWPA // ID B4U9P8_HYDS0 Unreviewed; 185 AA. AC B4U9P8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 41. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=HY04AAS1_1173; OS Hydrogenobaculum sp. (strain Y04AAS1). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum. OX NCBI_TaxID=380749; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y04AAS1; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the RT Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001130; ACG57859.1; -; Genomic_DNA. DR RefSeq; YP_002121837.1; NC_011126.1. DR ProteinModelPortal; B4U9P8; -. DR STRING; 380749.HY04AAS1_1173; -. DR PRIDE; B4U9P8; -. DR EnsemblBacteria; ACG57859; ACG57859; HY04AAS1_1173. DR GeneID; 6743990; -. DR KEGG; hya:HY04AAS1_1173; -. DR PATRIC; 22137044; VBIHydSp64203_1180. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GLGPICH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HSP380749:GH30-1212-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 185 AA; 20691 MW; 183E9DECE6F8B0DC CRC64; MKLSKYLTIV DVDVFKDDIT EKTKKIVETY KPSIMLRAKN LKGKYFYEYA KAIRDITLNY GVLFFVNERF DIALAVGANG VHLPSNALDV SVVKNICKDM TIGYSAHSKE DALEAFQKGA DYVTLSPIFP TKSHENATPL GLEYLEDVVK SSKKPIFALG GITKENIDDV FKTGVYGIAS IRFFL // ID B4UIG4_ANASK Unreviewed; 203 AA. AC B4UIG4; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AnaeK_1337; OS Anaeromyxobacter sp. (strain K). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=447217; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikiva G., Beliaev A.; RT "Complete sequence of Anaeromyxobacter sp. K."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001131; ACG72569.1; -; Genomic_DNA. DR RefSeq; YP_002133698.1; NC_011145.1. DR ProteinModelPortal; B4UIG4; -. DR STRING; 447217.AnaeK_1337; -. DR EnsemblBacteria; ACG72569; ACG72569; AnaeK_1337. DR GeneID; 6787188; -. DR KEGG; ank:AnaeK_1337; -. DR PATRIC; 20937290; VBIAnaSp90767_1350. DR eggNOG; NOG287972; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ASP447217:GHB0-1354-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 134 136 THZ-P binding (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 20609 MW; FE6DDDBBBA018919 CRC64; MEVPVVHLIT DRRLASSLPA RAAAALRGLP PGIAAIHLRE KDLCGLDLLR LARALAAVCR DAGQRLLVND RLDVALAAGA DGVHLPSAGV SPVDARRLLG PAALLGVSCH SEADVVRARA GGASFATFGP VYDTPSKRPY GAPVGVGALR AAARLGLPLV ALGGVDPSRV AEVRAAGARG VATIRAWLTG DDPAGAVRAL LGR // ID B4UKN3_ANASK Unreviewed; 215 AA. AC B4UKN3; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AnaeK_0081; OS Anaeromyxobacter sp. (strain K). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=447217; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikiva G., Beliaev A.; RT "Complete sequence of Anaeromyxobacter sp. K."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001131; ACG71324.1; -; Genomic_DNA. DR RefSeq; YP_002132453.1; NC_011145.1. DR ProteinModelPortal; B4UKN3; -. DR STRING; 447217.AnaeK_0081; -. DR EnsemblBacteria; ACG71324; ACG71324; AnaeK_0081. DR GeneID; 6785091; -. DR KEGG; ank:AnaeK_0081; -. DR PATRIC; 20934726; VBIAnaSp90767_0083. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ASP447217:GHB0-83-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 21351 MW; A99AD508681F9C32 CRC64; MGAGRRARLG GLYVIVGGAD PVAQAHAAIG GGARAVQVRM KDAPAGAVLE ATRRILALAA GRALVLVNDR ADLALLAGAD GVHLGDDDLP VPEARRLLGP DLLVGRTTRT LEEARAALDE GADHVGYGPI FASRSKALPV PPRGLQALAE VARALPAPVV AIGGIGLDDV GAVARAGAAC AAVIEAVVGA ADPEAAAARM QAAFEAGRAA RGANP // ID B4V3E8_9ACTO Unreviewed; 212 AA. AC B4V3E8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSAG_02276; OS Streptomyces sp. Mg1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=465541; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Mg1; RG The Broad Institute Genome Sequencing Platform; RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., RA Heiman D., Hepburn T., Sykes S., Mehta T., Alvarado L., Kodira C.D., RA Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., RA Walsh C.T., Lander E., Galagan J., Nusbaum C., Birren B.; RT "Annotation of Streptomyces sp. Mg1."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS570392; EDX22485.1; -; Genomic_DNA. DR ProteinModelPortal; B4V3E8; -. DR EnsemblBacteria; EDX22485; EDX22485; SSAG_02276. DR PATRIC; 25454552; VBIStrSp106026_2113. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22440 MW; F82E57C06C5FE27F CRC64; MQQLSDARLY LCTDARKRQG DLPEFLDAVL AGGVDVVQLR DKGMEAGEEL EHLRVFADAA RRHGKLLAVN DRADVAHAIG SDVLHLGQGD IPVPAARAIL GEDLLIGRSC HAESEVDAAV AEPGVDYFCT GPCWPTPTKP GRHAPGLGLV RYAASLAQDR PWFAIGGIDG TNLDEVLDAG ATRIVVVRAL TEASDPGAAA ADLAKRVRAR LP // ID B4VZU3_9CYAN Unreviewed; 359 AA. AC B4VZU3; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MC7420_2510; OS Coleofasciculus chthonoplastes PCC 7420. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Coleofasciculus. OX NCBI_TaxID=118168; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7420; RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS989863; EDX72602.1; -; Genomic_DNA. DR ProteinModelPortal; B4VZU3; -. DR EnsemblBacteria; EDX72602; EDX72602; MC7420_2510. DR PATRIC; 26253989; VBIMicCht100541_5812. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 128 Unknown (By similarity). FT REGION 129 359 Thiamine-phosphate synthase (By FT similarity). FT REGION 176 180 HMP-PP binding (By similarity). FT REGION 273 275 THZ-P binding (By similarity). FT METAL 209 209 Magnesium (By similarity). FT METAL 228 228 Magnesium (By similarity). FT BINDING 208 208 HMP-PP (By similarity). FT BINDING 247 247 HMP-PP (By similarity). FT BINDING 276 276 HMP-PP (By similarity). FT BINDING 303 303 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 359 AA; 40246 MW; 44A06CB17C751498 CRC64; MSGYNGWIGQ EPAVCRILDA NLDRAREGLR IIEEWCRFGL NSVQMASECK QMRQELARWH SREIRAERDT PGDLGTELSH PQEEQRANIQ QVLQANLCRV QEALRVLEEY GKLHSPNMGT ACKQMRYRVY TLESQLLIYH RYQRLKRSQL YLVTSSSDQL LPTVEAALQG GLTLVQYREK GADDLVKLAQ AQKLRQMCHH YGALLIMNDR VDLALAIDAD GVHLGQQDLP IAVARKLLGP HRIIGRSTTN PEEMQQAISE GADYIGVGPV YETPTKVGKA AAGLDYVQYA AQQASVPWFA IGGIDPNNIH EVLGAGAKRV AIVRAIMQAE QPTLVTQYFL SQLTKEQHLR RIEAGIPQS // ID B4W552_9CYAN Unreviewed; 221 AA. AC B4W552; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Thiamine monophosphate synthase/TENI subfamily; GN ORFNames=MC7420_5294; OS Coleofasciculus chthonoplastes PCC 7420. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Coleofasciculus. OX NCBI_TaxID=118168; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7420; RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS989884; EDX70666.1; -; Genomic_DNA. DR ProteinModelPortal; B4W552; -. DR EnsemblBacteria; EDX70666; EDX70666; MC7420_5294. DR PATRIC; 26257436; VBIMicCht100541_7508. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23497 MW; DE27FB72FF1FC374 CRC64; MINNCSALSF ELLLITDKAA CHRAGRTVEQ TLTSILNDIN SRCVAILVRD KKATISEIAT LISNLKPLTD STGVLLLVHS YPQLALEYNL AGVHLSSTTA IAPVRQQLPP EMLIGVSRHG TDALDQDDIG LANYATISPV YSPLSKPDDQ RNTLGLQGLR DSVKRSYRPL VALGGIEPGR VSDAIAQGAK AVAVIGAVMG AENPASVVQL LLDKDTHRAA K // ID B4W5Q6_9CAUL Unreviewed; 215 AA. AC B4W5Q6; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Thiamine monophosphate synthase/TENI subfamily; GN ORFNames=BBAL3_956; OS Brevundimonas sp. BAL3. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=391600; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL3; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS989898; EDX79799.1; -; Genomic_DNA. DR ProteinModelPortal; B4W5Q6; -. DR EnsemblBacteria; EDX79799; EDX79799; BBAL3_956. DR PATRIC; 29024224; VBIBreSp110930_0479. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 215 AA; 22333 MW; 2CA67BF7B922C639 CRC64; MILPAGYSDD ARALWDAATA LNRAAAAVSP SVARLPPLLF FTDPDRTSRP WETVARLPAG SGVVYRAFGA ADAIQTGRRL REATRGAGVK LLVGRDADLA EILEADGLHL PEREARQARS VGRAHPDWLL TAAWHGGRPI TEGLDALVLS PVFPAGGASA VKPALGVAEF GRWIQDVDLP VYALGGIGPD NVASLTGSGA CGLAGVEAIQ SAFHS // ID B4W9Y8_9CAUL Unreviewed; 235 AA. AC B4W9Y8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BBAL3_2638; OS Brevundimonas sp. BAL3. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=391600; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL3; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS989898; EDX81481.1; -; Genomic_DNA. DR ProteinModelPortal; B4W9Y8; -. DR EnsemblBacteria; EDX81481; EDX81481; BBAL3_2638. DR PATRIC; 29028971; VBIBreSp110930_2006. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 64 68 HMP-PP binding (By similarity). FT REGION 162 164 THZ-P binding (By similarity). FT METAL 97 97 Magnesium (By similarity). FT METAL 116 116 Magnesium (By similarity). FT BINDING 96 96 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 165 165 HMP-PP (By similarity). FT BINDING 192 192 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 235 AA; 24697 MW; 91026B441D83B112 CRC64; MCDDGPVDEW SQEGEVSPMA RTPTVPDRPP CRLYLITPPA IPDLDAFAAT LDEALGAGDV AALQIRLKPA DDAAICAAVE RLAPIARRHG VAVLLNDRPD LAKAAGCDGV HIGQEDGSLA EARRILGPDA MIGVTCHDDR DLAWDAAEGG ADYVAFGAFY PTDTKTTVHR PGLEILTVWQ ETVETPCVAI GGITVETAAE VARAGADFIA VSAGVWSYDA GPASAVKDFN HRLNN // ID B4WH59_9SYNE Unreviewed; 357 AA. AC B4WH59; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=S7335_2493; OS Synechococcus sp. PCC 7335. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=91464; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7335; RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS989904; EDX84796.1; -; Genomic_DNA. DR ProteinModelPortal; B4WH59; -. DR EnsemblBacteria; EDX84796; EDX84796; S7335_2493. DR PATRIC; 29878953; VBISynSp82123_2008. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 126 Unknown (By similarity). FT REGION 127 357 Thiamine-phosphate synthase (By FT similarity). FT REGION 183 187 HMP-PP binding (By similarity). FT REGION 280 282 THZ-P binding (By similarity). FT METAL 216 216 Magnesium (By similarity). FT METAL 235 235 Magnesium (By similarity). FT BINDING 215 215 HMP-PP (By similarity). FT BINDING 254 254 HMP-PP (By similarity). FT BINDING 283 283 HMP-PP (By similarity). FT BINDING 310 310 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 357 AA; 39134 MW; CA003EC8485C5DBC CRC64; MPQQTVSKTN ALLRILDANL DRAREGMRII EEWCRFGLND EATTAQLKNL RQTIAQWHTP EIRAARDTPG DMGTALTHTQ ESLRDSLGDV LQVNLARTQE ALRVLEEYGK LYSQEMAAAC KQMRYQLYTL DSQLMAKFPD TTDQGTRRMQ QLARSRTYLV TSPVPDLLGV VESALKGGIA IVQYREKQAD DNTRLQTAHQ MKKLCHQYGA LFVVNDRVDI AAASDADGVH LGQQDLPMEA ARKVLGPSKI VGRSTTNPQE LQRALDEGAD YIGVGPVHET PTKPGKAASG NDYVRYAAAY ATMPWFTIGG LNADNLGPTL AAGATRVAVV RALMEASDPS AVARSLVEQT QQQPIGT // ID B4WWZ6_9GAMM Unreviewed; 313 AA. AC B4WWZ6; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 16-OCT-2013, entry version 32. DE SubName: Full=Thiamine monophosphate synthase/TENI subfamily, putative; GN ORFNames=ADG881_1287; OS Alcanivorax sp. DG881. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=236097; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DG881; RA Bolch C., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS989915; EDX89185.1; -; Genomic_DNA. DR ProteinModelPortal; B4WWZ6; -. DR EnsemblBacteria; EDX89185; EDX89185; ADG881_1287. DR PATRIC; 24421407; VBIAlcSp134196_2561. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 313 AA; 33718 MW; A72D06A44C40B0FB CRC64; MPTRSTPAIT VVAAIIRGED GRICLSKRPD NKHQGGRWEF PGGKVEQGEA LSEALARELE EELGMAGATS SPFMTIAHQY DDLHVTLHFR DVCVWQGEPE GREGQWVQWF LPGELADLRF PAANQPVVNA IQLPEQLVVA PEDITLHELL AGIDRLNGEQ QGLYLRQWSD HAEVAAVVAQ CQQRGVKVWL RAVDTQSVAT AKTLGVFAVH FPGRTLAQLD ERPAFDGITS AAVHDQAARD KAGNLGLDMA LVSPVLPTPT HPGKPALGWP QAELLMKGAP LACYALGGVA PGDLINARDH GAVGVAGIRA FWP // ID B4X541_9GAMM Unreviewed; 226 AA. AC B4X541; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ADG881_2238; OS Alcanivorax sp. DG881. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=236097; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DG881; RA Bolch C., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS989915; EDX90136.1; -; Genomic_DNA. DR ProteinModelPortal; B4X541; -. DR EnsemblBacteria; EDX90136; EDX90136; ADG881_2238. DR PATRIC; 24420833; VBIAlcSp134196_2286. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23819 MW; 69117CA214E2183D CRC64; MSPHRHHRPL RLHGLYAITD PALTPDERLL PAAEAALRGG ARLLQYRDKT ASPAQREYRA AQLRALCHQY GTLFIVNDDP ALAARVDADG VHIGQSDGGI KAARDQLGDS RIIGVTCHGD LALAGQAAEA GADYLAMGRF FTSQTKPQAP PASLAVLRQA CQQFHQPVVA IGGVNPDNAP QLIDAGAVSV AVIHALFGHT DTASIEAAAR RFSACFPATA GQAIPE // ID B5BVR9_SALET Unreviewed; 211 AA. AC B5BVR9; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SeSPA_A0016; OS Salmonella enterica subsp. enterica serovar Saintpaul str. SARA23. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=439846; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SARA23; RA Rosovitz M.J., McDermott P., White D., LeClerc J.E., Mammel M.K., RA Cebula T.A., Ravel J.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SARA23; RA Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., RA Leclerc J., Cebula T., Sebastian Y.; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SARA23; RX PubMed=21602358; DOI=10.1128/JB.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAM02000001; EDY23235.1; -; Genomic_DNA. DR ProteinModelPortal; B5BVR9; -. DR EnsemblBacteria; EDY23235; EDY23235; SeSPA_A0016. DR PATRIC; 27989000; VBISalEnt100029_0015. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22910 MW; F79C32D59EBCC5CE CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID B5CK50_SALET Unreviewed; 211 AA. AC B5CK50; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SeSB_A4482; OS Salmonella enterica subsp. enterica serovar Schwarzengrund str. SL480. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=454165; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SL480; RX PubMed=21602358; DOI=10.1128/JB.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABEJ01000035; EDY27108.1; -; Genomic_DNA. DR ProteinModelPortal; B5CK50; -. DR EnsemblBacteria; EDY27108; EDY27108; SeSB_A4482. DR PATRIC; 28007644; VBISalEnt97326_4532. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22997 MW; 53EBA33604968A81 CRC64; MYQPDFPTVP FRLGLYPVVD SVQWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPSVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID B5CLH5_9FIRM Unreviewed; 769 AA. AC B5CLH5; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 19-FEB-2014, entry version 32. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.7.4.7; GN Name=thiD; ORFNames=RUMLAC_00296; OS Ruminococcus lactaris ATCC 29176. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=471875; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29176; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Ruminococcus lactaris ATCC 29176."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29176; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABOU02000014; EDY33827.1; -; Genomic_DNA. DR ProteinModelPortal; B5CLH5; -. DR EnsemblBacteria; EDY33827; EDY33827; RUMLAC_00296. DR PATRIC; 29791062; VBIRumLac66300_0815. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 2. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 769 AA; 82708 MW; BB5136085F19D857 CRC64; MEKNVKVHCL TNPVTMQSVA NVLLAAGGSA VMAQDEQEVE EITAICQATL LNTGVPDERK IRSCILAGKC ANRLGHPVVL DPVGAGASKF RRKKIGQLLQ SVVPSIIRCN QEEASALLRA EDEKEFLVLG TERQKIEGTA ESCQQDGDAV FSGIQSGGVE SSLELELEKA RRLAVRLAKK YRCTVCMTGE QDVISDGERV KVISGGDGRI CRITGSGCML SALCALKCGD GTDSFEAAAE AAETWRHCAE RAGETVDEKE EGIGSFQIRL LDALSLKMEM ERGRRMEVQS RMKQNKKRYI SPEQLRLYAV TDRKWLAEGE TLETVVETLV RSGVTCVQLR EKHASDEEII SEGKKLNEIC RKHHVPLIVN DRPDLAKKIG AAGVHVGLSD MGIEKARELL GEDFIIGGSA HNVKEALQAQ KAGADYIGCG AVFGSQTKSD VTTLAKEELC AICEAVEIPV VAIGGITAEN IKELTGTGID GVAVVSGLFA AKDKPEMVRR FLKAFEMKKV LTIAGSDCSG GAGIQADLKT MAANGVYGMS AVMALTAQNT TGVQGIMEVT PEFAGQQIDS IFTDIRPDAV KIGMLSSGEI IHVVAEKLKE YQAEHIVLDP VMVSTSGHRL IQKDAEQSLK KELFPLAELI TPNIPEAEVL SGRKIKNAQD MESAAEKIVE EYGCAVLLKG GHRINDANDF LCTGEKKVWI CGERVENPNT HGTGCTLSSA IASNLAKGVG MEEAVQKAKE YLTEALKEQL DLGAGSGPMD HTLGKIIFE // ID B5CTD3_9FIRM Unreviewed; 211 AA. AC B5CTD3; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 13-NOV-2013, entry version 22. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=RUMLAC_02756; OS Ruminococcus lactaris ATCC 29176. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=471875; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29176; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Ruminococcus lactaris ATCC 29176."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29176; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABOU02000055; EDY31555.1; -; Genomic_DNA. DR ProteinModelPortal; B5CTD3; -. DR EnsemblBacteria; EDY31555; EDY31555; RUMLAC_02756. DR PATRIC; 29790217; VBIRumLac66300_0415. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 211 AA; 23788 MW; 6898C032A0E9A847 CRC64; MYKENQEYCE NVIAVSNRHL CKRPFLEQIK IVCEWHPKAL ILREKDLTEA EYEQLAGQVM KICETYKVPC ILHNFWQIAV KLNCNQIHLP LPVLRQLVNQ AVIQEKNQGS GTFYQIGTSV HSVEEAVEAE KLGASYLVAG HIYVTDCKKG VPPRGIRFLK EVCDAVRLPV YGIGGIHFEP EQWKELAKAG AKGGCIMSGM MTLSEEEGKA E // ID B5D344_BACPM Unreviewed; 202 AA. AC B5D344; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 19-FEB-2014, entry version 22. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BACPLE_03438; OS Bacteroides plebeius (strain DSM 17135 / JCM 12973 / M2). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=484018; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17135; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides plebeius (DSM 17135)."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17135; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABQC02000024; EDY93994.1; -; Genomic_DNA. DR ProteinModelPortal; B5D344; -. DR EnsemblBacteria; EDY93994; EDY93994; BACPLE_03438. DR PATRIC; 30483985; VBIBacPle58056_3080. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23050 MW; DF5ACC0E918FCCAA CRC64; MKLILITTPT YFVEEDKIIT TLFDEGLDIL HLRKPDTAPV YAERLLTLIP EKYHKRIVVH DHFYLKEEYK LKGIHLSHRN PLIPDNYTGH VSASCHTFDE VMADKKMCDY VFLSPIFDSI SKEGYASAFT SESIREAAEK GIIDKRVIAL GGVDENNLLQ VKDFGFGGAA ILGGLWNKFD PASDYNYQEL IAHFRKLKRL AD // ID B5D393_BACPM Unreviewed; 218 AA. AC B5D393; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACPLE_03487; OS Bacteroides plebeius (strain DSM 17135 / JCM 12973 / M2). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=484018; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17135; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides plebeius (DSM 17135)."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17135; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABQC02000024; EDY94043.1; -; Genomic_DNA. DR ProteinModelPortal; B5D393; -. DR EnsemblBacteria; EDY94043; EDY94043; BACPLE_03487. DR PATRIC; 30484073; VBIBacPle58056_3124. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 24122 MW; 259B566382C4FC9B CRC64; MEDKAMDMNH FKLQFITHFT DTYSYLDSAR MALEGGCRWV QLRMKHASDE ETEAVAVEVQ KLCRTYGATF LIDDRVELVR KLKADGVHLG KNDMPIAEAR KILGKDFLIG GTANTFDDVR AHYEAGADYI GCGPFRFTTT KEKLSPILGL EGYRSIVQQM KAEGIHLPIV AIGGITLEDI PAIMQTGVTG IALSGTILRA ANPVEETKKI IEELKSKS // ID B5E321_STRP4 Unreviewed; 209 AA. AC B5E321; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPG_0651; OS Streptococcus pneumoniae serotype 19F (strain G54). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=512566; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G54; RX PubMed=11442348; DOI=10.1089/10766290152044995; RA Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L., RA Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A., RA Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.; RT "Annotated draft genomic sequence from a Streptococcus pneumoniae type RT 19F clinical isolate."; RL Microb. Drug Resist. 7:99-125(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G54; RA Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., RA Davidsen T.M., Tettelin H., Oggioni M.; RT "Pneumococcal beta glucoside metabolism investigated by whole genome RT comparison."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001015; ACF56399.1; -; Genomic_DNA. DR RefSeq; YP_002037366.1; NC_011072.1. DR ProteinModelPortal; B5E321; -. DR STRING; 512566.SPG_0651; -. DR EnsemblBacteria; ACF56399; ACF56399; SPG_0651. DR GeneID; 6479686; -. DR KEGG; spx:SPG_0651; -. DR PATRIC; 19686863; VBIStrPne77426_0691. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE512566:GCA3-651-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID B5E328_STRP4 Unreviewed; 210 AA. AC B5E328; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; OrderedLocusNames=SPG_0658; OS Streptococcus pneumoniae serotype 19F (strain G54). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=512566; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G54; RX PubMed=11442348; DOI=10.1089/10766290152044995; RA Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L., RA Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A., RA Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.; RT "Annotated draft genomic sequence from a Streptococcus pneumoniae type RT 19F clinical isolate."; RL Microb. Drug Resist. 7:99-125(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G54; RA Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., RA Davidsen T.M., Tettelin H., Oggioni M.; RT "Pneumococcal beta glucoside metabolism investigated by whole genome RT comparison."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001015; ACF56367.1; -; Genomic_DNA. DR RefSeq; YP_002037373.1; NC_011072.1. DR ProteinModelPortal; B5E328; -. DR STRING; 512566.SPG_0658; -. DR EnsemblBacteria; ACF56367; ACF56367; SPG_0658. DR GeneID; 6479461; -. DR KEGG; spx:SPG_0658; -. DR PATRIC; 19686877; VBIStrPne77426_0698. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE512566:GCA3-658-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22744 MW; A3239DF7871A7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID B5EBG3_GEOBB Unreviewed; 484 AA. AC B5EBG3; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 14-MAY-2014, entry version 44. DE SubName: Full=4-amino-5-hydroxymethyl-2-methylpyrimidine-phosphate kinase and thiamin monophosphate synthase; GN Name=thiD; Synonyms=thiE; OrderedLocusNames=Gbem_3462; OS Geobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=404380; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bem / ATCC BAA-1014 / DSM 16622; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Lovley D., Richardson P.; RT "Complete sequence of Geobacter bemidjiensis BEM."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001124; ACH40455.1; -; Genomic_DNA. DR RefSeq; YP_002140251.1; NC_011146.1. DR ProteinModelPortal; B5EBG3; -. DR STRING; 404380.Gbem_3462; -. DR EnsemblBacteria; ACH40455; ACH40455; Gbem_3462. DR GeneID; 6780324; -. DR KEGG; gbm:Gbem_3462; -. DR PATRIC; 21990564; VBIGeoBem56306_3385. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OMA; YLAQGEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; GBEM404380:GHFR-3525-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 484 AA; 50909 MW; C1C1B3360F9673F2 CRC64; MLRLVVDHSG KERRIGGLYL ITDQAERLVH RVREALSSGG VAVLQYRDKV RSYEERLELG QELKHLCTEF QVEFIVNDDV ELAFALDADG VHLGQDDGDP AAAREALGPK KMIGISTHSL TEALEAQEAG ADYVGFGAIY PTDSKEVEHI QGPEKLVLLK EKLRIPVVAI GGITRDNACA VIDAGADAIA VISAVLSARS PALAATELAL LFNRKAMQPR GGVLTVAGSD SGGGAGIQAD LKTVTLLGSY GASAVTALTA QNTRGVTAIH PVPAAFLAEQ IDAVLTDIPI DVVKVGMLSS AENAATLADR LTDHGVRMVV LDPVMSAKGG VALMEDEALG VLKQRLIPLC YLLTPNIPEA EALTGLTITD TAGMELAARA LHLMGAKHVL VKGGHLTEGV VTDILFDGAG FTRFTAPRVL TRNTHGTGCT LASAIASYLA QGEPLPGAVL RAKLFVTRAI KYAQPLGKGH GPVNHFMAAR DQAE // ID B5ED94_GEOBB Unreviewed; 218 AA. AC B5ED94; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=tenI; Synonyms=thiE; OrderedLocusNames=Gbem_0652; OS Geobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=404380; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bem / ATCC BAA-1014 / DSM 16622; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Lovley D., Richardson P.; RT "Complete sequence of Geobacter bemidjiensis BEM."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001124; ACH37680.1; -; Genomic_DNA. DR RefSeq; YP_002137476.1; NC_011146.1. DR ProteinModelPortal; B5ED94; -. DR STRING; 404380.Gbem_0652; -. DR EnsemblBacteria; ACH37680; ACH37680; Gbem_0652. DR GeneID; 6783485; -. DR KEGG; gbm:Gbem_0652; -. DR PATRIC; 21984969; VBIGeoBem56306_0643. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HRFYFIT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GBEM404380:GHFR-660-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23461 MW; B7C53E132B0A0C37 CRC64; MKELESPWID FNLYLITGRE ETQGRPLGYV VEEALKGGVR AVQYRDKDAT SKELYETAHE LRRLTSRYGA KLIINDRADI ALAVDADGVH IGSASMPIYK VRRILGERKL IGVSCHNKAQ AIAAQEMGAD FITFGPVYYT PSKAPYGDPV GTAKLQTVAG LLQVPVFALG GIKKENCAEA AGCGVRGVAL ISAVLSAADP REAAKKLIAL LPPLEHAD // ID B5ELE1_ACIF5 Unreviewed; 329 AA. AC B5ELE1; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 14-MAY-2014, entry version 46. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=Lferr_0403; OS Acidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum OS ferrooxidans (ATCC 53993)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=380394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 53993; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Borole A.P.; RT "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001132; ACH82657.1; -; Genomic_DNA. DR RefSeq; YP_002218864.1; NC_011206.1. DR ProteinModelPortal; B5ELE1; -. DR STRING; 380394.Lferr_0403; -. DR EnsemblBacteria; ACH82657; ACH82657; Lferr_0403. DR GeneID; 6876355; -. DR KEGG; afe:Lferr_0403; -. DR PATRIC; 20658324; VBIAciFer6930_0387. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AFER380394:GHE0-406-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 329 AA; 35387 MW; 71B5BFB1BD17D76D CRC64; MPTVPVATGI IEDAFGRLLV ALRPEGKPWP GFWEFPGGKV DPGETPEQAL VRELWEELGV TVTAPEPFRE LEYTYPERTV RVHFYRVRHW TGTAHGREGQ EVRWLFPWEI PALECLPANL RLTADVLAEA LPQPPLCLIA DPGRLPLPDF RRALEAALDA GLRWLVLRCK AVPDGSSADV LAALCAGALA GGVQVYLNHP DPLPGWPRTG RHLTQAQSDA GVKPDEAFGV SCHDAAGLQQ AARLGARYAF LSPIFPTSSH PDTEALGPEV FAAMAAESSL PLIALGGMTA ARVPEALAAG ARGVAVLSGI LEAQDPAAAT RALLRHWER // ID B5ET97_VIBFM Unreviewed; 212 AA. AC B5ET97; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_1; Synonyms=thiE; OrderedLocusNames=VFMJ11_A0360; OS Vibrio fischeri (strain MJ11). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=388396; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MJ11; RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., RA Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., RA Frazier M., Venter J.C.; RT "Complete sequence of Vibrio fischeri strain MJ11."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001133; ACH63618.1; -; Genomic_DNA. DR RefSeq; YP_002157915.1; NC_011186.1. DR ProteinModelPortal; B5ET97; -. DR STRING; 388396.VFMJ11_A0360; -. DR EnsemblBacteria; ACH63618; ACH63618; VFMJ11_A0360. DR GeneID; 6808773; -. DR KEGG; vfm:VFMJ11_A0360; -. DR PATRIC; 20124973; VBIVibFis37164_3119. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22764 MW; 1C4D12484EEC01AC CRC64; MNNPYTLYLV TDEKQDIDTL CHVVAEAVKG GVTMVQVREK HGDVRAFIQR SLAIKEILKD SGVPLIINDR VDVALAVQAD GVHLGQSDMP AQIARQLIGP DMILGLSVEN ETQLRKAQEL PVDYLGISAI FSTPTKTNII KEWGIQGLAF AVKESQLPLV AIGGINDSNI REVGDTGVDG IALVSAICHA SSPKQASQAL LGLMNDDVEL KT // ID B5FF67_VIBFM Unreviewed; 219 AA. AC B5FF67; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_2; Synonyms=thiE; OrderedLocusNames=VFMJ11_0034; OS Vibrio fischeri (strain MJ11). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=388396; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MJ11; RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., RA Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., RA Frazier M., Venter J.C.; RT "Complete sequence of Vibrio fischeri strain MJ11."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001139; ACH64873.1; -; Genomic_DNA. DR RefSeq; YP_002154805.1; NC_011184.1. DR ProteinModelPortal; B5FF67; -. DR STRING; 388396.VFMJ11_0034; -. DR EnsemblBacteria; ACH64873; ACH64873; VFMJ11_0034. DR GeneID; 6806813; -. DR KEGG; vfm:VFMJ11_0034; -. DR PATRIC; 20118521; VBIVibFis37164_0034. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24221 MW; 3C17CFCCF65A7C7F CRC64; MFAFPNIDKS KFGLYPVVDD VSWIEKLLKL DVKTIQLRIK NPEQADLEQQ VIKAIRLGRE YDAQVFINDY WQLAIKHNAF GIHLGQEDIE VADLQAIAEA NICLGLSTHD DSELLKVKAL NPSYLALGHI FPTPTKEMPS QPQGLTNLAK NQQLAGETPT VAIGGIDLSV ANDVWQTGVD SIAVVRAITE AEDTEQAVAK FNAIISEPRR GNLQEVAYE // ID B5GGR0_9ACTO Unreviewed; 199 AA. AC B5GGR0; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 2. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN ORFNames=SSBG_03425; OS Streptomyces sp. SPB74. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=465543; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SPB74; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Streptomyces sp. strain SPB74."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770539; EDY45506.3; -; Genomic_DNA. DR ProteinModelPortal; B5GGR0; -. DR EnsemblBacteria; EDY45506; EDY45506; SSBG_03425. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT NON_TER 199 199 SQ SEQUENCE 199 AA; 19345 MW; EBD1EBE5E62E7C6E CRC64; MSPDMSVYLV TDSAQCAARG RTVAETVAAA VAGGVTAVQV REKEAGGRAF LAQVLAVAAV LPARVTLLVN DRVDVYLAAR AAGARVHGVH VGQSDLPVAA VRELTGPDAL LGLSAATPAE LAEAATAGVD HVGVGALRAT ATKTDAPPAL GVSGFARLLA APGLPPAVAI GGVLPADLPA LRRAGAAGAA IVSGICAAA // ID B5IED8_ACIB4 Unreviewed; 205 AA. AC B5IED8; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ABOONEI_2775; OS Aciduliprofundum boonei (strain DSM 19572 / T469). OC Archaea; Euryarchaeota; Aciduliprofundum. OX NCBI_TaxID=439481; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T469; RX PubMed=18445019; DOI=10.1111/j.1472-4669.2008.00152.x; RA Reysenbach A.L., Flores G.E.; RT "Electron microscopy encounters with unusual thermophiles helps direct RT genomic analysis of Aciduliprofundum boonei."; RL Geobiology 6:331-336(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990523; EDY35327.1; -; Genomic_DNA. DR ProteinModelPortal; B5IED8; -. DR EnsemblBacteria; EDY35327; EDY35327; ABOONEI_2775. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22543 MW; 98C10D5679F3E8B6 CRC64; MNLREKLKLY VITDGRLRDE IESVKLVLEG GAKAIQLRMK NSTTRQMVEK GIKIRKIVED YGALLFVDDR VDVALAIEAH GVHLGPEDMP LKMARRIAPQ LLIGATVHSV EEAIKAQEDG ADYIGAGSVY PTRSKENAVV IGLENLRRIV ESVRIPVVAI GGVNIENVRN VLSTGVDGIA VISFILAAEN PKEATRRMLR EIEGR // ID B5IEQ3_ACIB4 Unreviewed; 205 AA. AC B5IEQ3; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Aboo_0116; ORFNames=ABOONEI_308; OS Aciduliprofundum boonei (strain DSM 19572 / T469). OC Archaea; Euryarchaeota; Aciduliprofundum. OX NCBI_TaxID=439481; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T469; RX PubMed=18445019; DOI=10.1111/j.1472-4669.2008.00152.x; RA Reysenbach A.L., Flores G.E.; RT "Electron microscopy encounters with unusual thermophiles helps direct RT genomic analysis of Aciduliprofundum boonei."; RL Geobiology 6:331-336(2008). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T469; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., RA Woyke T.; RT "Complete sequence of Aciduliprofundum boonei T469."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19572 / T469; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., RA Woyke T.; RT "Complete sequence of Aciduliprofundum boonei T469."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001941; ADD07928.1; -; Genomic_DNA. DR EMBL; DS990524; EDY35237.1; -; Genomic_DNA. DR RefSeq; YP_003482490.1; NC_013926.1. DR EnsemblBacteria; ADD07928; ADD07928; Aboo_0116. DR EnsemblBacteria; EDY35237; EDY35237; ABOONEI_308. DR GeneID; 8827052; -. DR KEGG; abi:Aboo_0116; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; ABOO439481:GJNL-119-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22510 MW; 1222F9780277804C CRC64; MNLREKLKLY VITDGRLRDE IESVKLVLEG GAKAIQLRMK NSTTRQMVEK GIRIRKIVED YGALLFVDDR VDVALAIEAH GVHLGPEDMP LKMARIIAPQ LLIGATVHSV EEAIKAQEDG ADYIGAGSVY PTRSKENAVV IGLENLRRIV ESVRIPVVAI GGINIENVRN VLSTGVDGIA VISSILVAEN PKEATRRMLR EIEGR // ID B5IN65_9CHRO Unreviewed; 364 AA. AC B5IN65; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CPCC7001_2528; OS Cyanobium sp. PCC 7001. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanobium. OX NCBI_TaxID=180281; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7001; RA Lily E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990556; EDY39647.1; -; Genomic_DNA. DR ProteinModelPortal; B5IN65; -. DR EnsemblBacteria; EDY39647; EDY39647; CPCC7001_2528. DR PATRIC; 27721974; VBICyaSp52852_1670. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 131 Unknown (By similarity). FT REGION 132 364 Thiamine-phosphate synthase (By FT similarity). FT REGION 184 188 HMP-PP binding (By similarity). FT REGION 290 292 THZ-P binding (By similarity). FT METAL 226 226 Magnesium (By similarity). FT METAL 245 245 Magnesium (By similarity). FT BINDING 225 225 HMP-PP (By similarity). FT BINDING 264 264 HMP-PP (By similarity). FT BINDING 293 293 HMP-PP (By similarity). FT BINDING 320 320 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 364 AA; 38496 MW; 57E525B28D90BD01 CRC64; MVLPPLSPQA AADTPALRRL LDANLDRARE GLRVLEDWAR FGLERADLVS RCKDLRQRLG RLHGEAYKLA RHTATDAGAG LTHPAQAERQ RPQQVVAANA SRVQEALRVL EEFGRGIDPV LASEAAAIRY TLYDLDADLL RAGQGAAARR RRLEACHLYL VTSPVPDLDA VVAGALAGGV RLVQYRAKPE STGPGGAPLT DRERLQQAGA LRELCAQAGA LFIVNDRIDL ALAVDADGVH LGQGDLPPAL ARRLLGPDRL IGRSTHALPQ LQQAIQDGCD YVGVGPVQAT PTKPGRQPVG LAYVSQAAQA CPIPFFAIGG LTAEGIAAVR QAGGERVAVV RAITEADDPA AASRQLLSAL GRSS // ID B5JTI5_9GAMM Unreviewed; 216 AA. AC B5JTI5; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GP5015_2375; OS gamma proteobacterium HTCC5015. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=391615; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC5015; RA Lily E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990599; EDY87197.1; -; Genomic_DNA. DR ProteinModelPortal; B5JTI5; -. DR EnsemblBacteria; EDY87197; EDY87197; GP5015_2375. DR PATRIC; 25909084; VBIGamPro11258_0668. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23655 MW; 6F0A109642AF7D98 CRC64; MRGLYAITPD GVDEPELLSR SRDILAAGAV MLQYRDKSDD TQKRQRQAQS LLTLCRDHNA LCIINDDIEL AAAVGADGVH LGRDDDTYSH ARQRLGEHAI VGISCYNDIQ RAQHAQQIGA SYAAFGAFFP SQTKPHAPRA QLEQLDRQRS QLAIPQCAIG GITTQRAPEL IRAGADLLAV ITALYEAQDS AEATRQFVAH FEHDHSRLGR DNTGAT // ID B5JXG4_9GAMM Unreviewed; 319 AA. AC B5JXG4; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 16-OCT-2013, entry version 31. DE SubName: Full=Mutator MutT; GN ORFNames=GP5015_1299; OS gamma proteobacterium HTCC5015. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=391615; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC5015; RA Lily E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990611; EDY85672.1; -; Genomic_DNA. DR ProteinModelPortal; B5JXG4; -. DR EnsemblBacteria; EDY85672; EDY85672; GP5015_1299. DR PATRIC; 25911856; VBIGamPro11258_2033. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; SQ SEQUENCE 319 AA; 35120 MW; A07B37FEF5D96B4C CRC64; MVERIEVVAA AILDGSGRVL ISRRPQHVHL GGKLEFPGGK RELPESTEQT LARELEEELG IRPTASQPLI RLDYDYPDKS IRLIVYRVHG FVGEPQGREG QEVAWLDILS LNSGDFPAAN GPIINALKLP ESLLVTPDIP WTGDGASVPL EALSELIEKR QPQIALLRQP RWPEAIYRRI ATVLSERQAI NWQWKSSALM GGALPQNVGL HLSARELWDY AERPAELSDQ QWFSASVHNL SELARAEEVG VDFVVLGSVL ETPTHPSEPG LGWERAQTLI EKAHVPVYLI GGLGLEDMAR AHRAGAQGIA GIRCFSQAS // ID B5MTE4_SALET Unreviewed; 211 AA. AC B5MTE4; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SeSPB_A4367; OS Salmonella enterica subsp. enterica serovar Saintpaul str. SARA29. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=439847; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SARA29; RX PubMed=21602358; DOI=10.1128/JB.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAN01000046; EDZ09663.1; -; Genomic_DNA. DR ProteinModelPortal; B5MTE4; -. DR EnsemblBacteria; EDZ09663; EDZ09663; SeSPB_A4367. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22950 MW; E595042ED80F3420 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIDRLADYP TVAIGGISVE RAPAVLATGV GSVAVVSAIT QAADWREATA QLLAIAGVGD E // ID B5N6V3_SALET Unreviewed; 211 AA. AC B5N6V3; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SeI_A3658; OS Salmonella enterica subsp. enterica serovar 4,[5],12:i:- str. OS CVM23701. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=440534; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CVM23701; RX PubMed=21602358; DOI=10.1128/JB.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABAO01000054; EDZ14026.1; -; Genomic_DNA. DR ProteinModelPortal; B5N6V3; -. DR EnsemblBacteria; EDZ14026; EDZ14026; SeI_A3658. DR PATRIC; 27929872; VBISalEnt101080_4595. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22983 MW; 803CF861FC550D88 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE SGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID B5NJL7_SALET Unreviewed; 211 AA. AC B5NJL7; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SeJ_A4623; OS Salmonella enterica subsp. enterica serovar Javiana str. OS GA_MM04042433. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=454167; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA_MM04042433; RA Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., RA Leclerc J., Cebula T., Sebastian Y.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABEH02000013; EDZ05091.1; -; Genomic_DNA. DR ProteinModelPortal; B5NJL7; -. DR EnsemblBacteria; EDZ05091; EDZ05091; SeJ_A4623. DR PATRIC; 27959082; VBISalEnt72631_4420. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22990 MW; 057A16E68A2D3E3E CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEINIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID B5NX37_SALET Unreviewed; 211 AA. AC B5NX37; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SeKB_A4348; OS Salmonella enterica subsp. enterica serovar Kentucky str. CDC 191. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=454231; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC 191; RX PubMed=21602358; DOI=10.1128/JB.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABEI01000033; EDZ18420.1; -; Genomic_DNA. DR ProteinModelPortal; B5NX37; -. DR EnsemblBacteria; EDZ18420; EDZ18420; SeKB_A4348. DR PATRIC; 27968431; VBISalEnt51064_4540. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22833 MW; F86B5A68649B3A94 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIEHLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHNA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSVAVVSAIT QAANWREATA QLLAIAGVGD E // ID B5P9N0_SALET Unreviewed; 211 AA. AC B5P9N0; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SeHB_A4296; OS Salmonella enterica subsp. enterica serovar Heidelberg str. SL486. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=454164; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SL486; RX PubMed=21602358; DOI=10.1128/JB.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABEL01000027; EDZ22876.1; -; Genomic_DNA. DR ProteinModelPortal; B5P9N0; -. DR EnsemblBacteria; EDZ22876; EDZ22876; SeHB_A4296. DR PATRIC; 27949658; VBISalEnt60298_4519. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22950 MW; A495042EC6FEDE33 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIDRLADYP TVAIGGISVE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID B5PN64_SALET Unreviewed; 211 AA. AC B5PN64; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SeW_A4601; OS Salmonella enterica subsp. enterica serovar Weltevreden str. OS HI_N05-537. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=465518; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HI_N05-537; RX PubMed=21602358; DOI=10.1128/JB.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFF01000034; EDZ27350.1; -; Genomic_DNA. DR ProteinModelPortal; B5PN64; -. DR EnsemblBacteria; EDZ27350; EDZ27350; SeW_A4601. DR PATRIC; 25798391; VBISalEnt31937_4675. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22859 MW; DF93565F60864431 CRC64; MYQPDFPTVP FCLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVES DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSVAVVSAIT QAADWRAATA QLLDIAGVGD E // ID B5Q0W9_SALHA Unreviewed; 211 AA. AC B5Q0W9; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SeH_A4639; OS Salmonella enterica subsp. enterica serovar Hadar str. RI_05P066. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=465516; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RI_05P066; RX PubMed=21602358; DOI=10.1128/JB.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFG01000019; EDZ33608.1; -; Genomic_DNA. DR ProteinModelPortal; B5Q0W9; -. DR EnsemblBacteria; EDZ33608; EDZ33608; SeH_A4639. DR PATRIC; 27940016; VBISalEnt125778_4538. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22895 MW; B69C23919EBCC0DD CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID B5Q4U2_SALVI Unreviewed; 211 AA. AC B5Q4U2; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SeV_B0767; OS Salmonella enterica subsp. enterica serovar Virchow str. SL491. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=465517; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SL491; RX PubMed=21602358; DOI=10.1128/JB.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFH02000001; EDZ04354.1; -; Genomic_DNA. DR ProteinModelPortal; B5Q4U2; -. DR EnsemblBacteria; EDZ04354; EDZ04354; SeV_B0767. DR PATRIC; 25780608; VBISalEnt69786_0751. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22907 MW; F61109A42DBDBE56 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE VGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH NDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSVAVVSAIT QAADWRAATA QLLDIAGVGD E // ID B5QG69_CAMJU Unreviewed; 201 AA. AC B5QG69; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 16-OCT-2013, entry version 26. DE SubName: Full=Possible transferase; GN ORFNames=Cj8421_1066; OS Campylobacter jejuni subsp. jejuni CG8421. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=478547; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CG8421; RX PubMed=18809665; DOI=10.1128/IAI.00780-08; RA Poly F., Read T.D., Chen Y.H., Monteiro M.A., Serichantalergs O., RA Pootong P., Bodhidatta L., Mason C.J., Rockabrand D., Baqar S., RA Porter C.K., Tribble D., Darsley M., Guerry P.; RT "Characterization of two Campylobacter jejuni strains for use in RT volunteer experimental-infection studies."; RL Infect. Immun. 76:5655-5667(2008). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGQ01000003; EDZ32868.1; -; Genomic_DNA. DR ProteinModelPortal; B5QG69; -. DR EnsemblBacteria; EDZ32868; EDZ32868; Cj8421_1066. DR PATRIC; 27753295; VBICamJej65419_0561. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID B5QGA0_CAMJU Unreviewed; 210 AA. AC B5QGA0; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Cj8421_1107; OS Campylobacter jejuni subsp. jejuni CG8421. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=478547; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CG8421; RX PubMed=18809665; DOI=10.1128/IAI.00780-08; RA Poly F., Read T.D., Chen Y.H., Monteiro M.A., Serichantalergs O., RA Pootong P., Bodhidatta L., Mason C.J., Rockabrand D., Baqar S., RA Porter C.K., Tribble D., Darsley M., Guerry P.; RT "Characterization of two Campylobacter jejuni strains for use in RT volunteer experimental-infection studies."; RL Infect. Immun. 76:5655-5667(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGQ01000003; EDZ32899.1; -; Genomic_DNA. DR ProteinModelPortal; B5QGA0; -. DR EnsemblBacteria; EDZ32899; EDZ32899; Cj8421_1107. DR PATRIC; 27753381; VBICamJej65419_0604. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23055 MW; 783B9EF6EECA9963 CRC64; MKNKLDLNLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID B5QLP8_LACRH Unreviewed; 209 AA. AC B5QLP8; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 19-MAR-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LRH_00972; OS Lactobacillus rhamnosus HN001. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=486408; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HN001; RA Collett M.A., Rand C.J., Mason C., Stanton J.-A.L.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWJ01000007; EDY99463.1; -; Genomic_DNA. DR ProteinModelPortal; B5QLP8; -. DR EnsemblBacteria; EDY99463; EDY99463; LRH_00972. DR PATRIC; 26520820; VBILacRha3627_0898. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21836 MW; FDF458E872FD9638 CRC64; MNAEALQLYL VTNRYADSPE VFLAKIAAAC ENGVTMVQLR EKSLTTRDYY ALAKQVKLIT DRYRIPLIID DRVDVCLAVD AAGVHIGDDE LPVAVTRQLL GPDKILGVST KTVATATAAV AAGADYLGVG AIFPTQTKAA APLTSLATLK AITAAVSVPV VAIGGIKADN LDTFKATGIA GVAIVSEIMQ APDTAQKVQT LSAKLKEVL // ID B5RV10_DEBHA Unreviewed; 542 AA. AC B5RV10; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 16-APR-2014, entry version 34. DE SubName: Full=DEHA2G01166p; GN OrderedLocusNames=DEHA2G01166g; OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC OS 0083 / IGC 2968) (Yeast) (Torulaspora hansenii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces. OX NCBI_TaxID=284592; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968; RX PubMed=15229592; DOI=10.1038/nature02579; RG Genolevures; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR382139; CAR65889.1; -; Genomic_DNA. DR RefSeq; XP_002770554.1; XM_002770508.1. DR ProteinModelPortal; B5RV10; -. DR STRING; 4959.B5RV10; -. DR GeneID; 8999098; -. DR KEGG; dha:DEHA2G01166g; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 542 AA; 58038 MW; 23208C3DA94AA3A1 CRC64; MTSHVDYTLY LVTDSTMIPE GSTFLKQVEH SINNGATMVQ LREKTLSTLD FIERASQVHE LTLKRGIPLI INDRVDVALA IDAEGVHVGQ DDMPASIVRK LVGPNKIVGV SCSFPSEVEA VCKEGLADYV GLGTVYKTNT KTNVSVPQGT GTIGVRKMLQ VLKAHNAAQV NNYISSVAIG GINESNASKV LYQSAIPGQS LDGVAVVSCI MASKNAAEST IKLENVIKSS VPWVKDLTNE SLCQTTDVKI KAVVRSKPLI HHITNNVVKN FSANVTLSIG ASPIMSELPD EFEEFTSSIP NLALVLNLGT PSTSQMDVFK HAISVYNKHG KHIIFDPVAA GASSPRLECC KELLNAGQFS VIKGNVGEIS AIWKLTSKYQ VSETGKNDLL MRGVDSVAEF NESDILRIGK EVAQDFRAIV VITGAKNFVF DGICVSKDSQ NIHDASSPNN VDDIKHTQIK GGHEVMSSIT GTGCSLGSTI AAFVAANADG NSGTTFNIFE AVVGAVEFYN KCGSEVGQDV TGPGSFMIRF LDRLNYEAHA IK // ID B5SB79_RALSL Unreviewed; 198 AA. AC B5SB79; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 14-MAY-2014, entry version 11. DE SubName: Full=Thiamine-phosphate pyrophosphorylase protein; DE EC=2.5.1.3; GN Name=thiE2; ORFNames=RSIPO_03409; OS Ralstonia solanacearum (Pseudomonas solanacearum). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=305; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1609; RA Boucher C., Carrere S., Dossat C., Elbaz M., Genin S., Gouzy J., RA Prior P., Segurens B., Wincker P.; RT "Genomic draft of R. solanacearum strain IPO1609, a phylotype RT IIB1/biovar 2/race 3 strain isolated from potato in Europe."; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1609; RA Genoscope - CEA; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU914166; CAQ58993.1; -; Genomic_DNA. DR RefSeq; YP_002257112.1; NW_002196568.1. DR ProteinModelPortal; B5SB79; -. DR GeneID; 6957140; -. DR OMA; SCHSEAD; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 198 AA; 21562 MW; 4B5720A83B29EF5F CRC64; MKDISLPDFY QITPEPVGSP HFETFFAELT DTLRSGIRLL QLRAKQLGPR EHLDVARRTL DLCRQSGAIL ILNGPIDMAL EVGCDGVHLS SDALMSLRSR PVPDTVLLSA ACHSAEQLEQ AASMAVDFVT LSPVLRTRTH PDADPLGWER FTELAQRARV PVFALGGMHP DMLAQAKRAG AWGVAAISAT WCHRSVGA // ID B5SEK8_RALSL Unreviewed; 383 AA. AC B5SEK8; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine-phosphate pyrophosphorylase protein; DE EC=2.5.1.3; GN Name=thiE1; ORFNames=RSIPO_00160; OS Ralstonia solanacearum IPO1609. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=564066; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1609; RA Boucher C., Carrere S., Dossat C., Elbaz M., Genin S., Gouzy J., RA Prior P., Segurens B., Wincker P.; RT "Genomic draft of R. solanacearum strain IPO1609, a phylotype RT IIB1/biovar 2/race 3 strain isolated from potato in Europe."; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1609; RA Genoscope - CEA; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU914168; CAQ60293.1; -; Genomic_DNA. DR RefSeq; YP_002258372.1; NW_002196569.1. DR GeneID; 6958412; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 383 AA; 40128 MW; 9E91AC79684C0F1D CRC64; MYVSTAWPGA VALAAQIVDR HADAFGRAPH AWRVTDRADE ATTAATVLLT ADAAQADRAR AAGAAVVLTE TRDGERIDTV HDRLGTYRFA GAATDEALGE RFVAMFGAAL ALAFEPRDAL CVARAWIAEA PADALAWPAR FDTLPRVLEP ALPCAASPEL AFAPCPTRLG IYAVVPDADW VERLVALGVP TVQLRVKSDD MQAVAGQVRR AAAAARGCTT RLFINDHWRV ALDVHAGRPE GAPDSGLYGI HLGQEDIDDA DLPAIRASGL RLGISTHGYA EMLRVAPLNP SYLALGAVFA TPTKTMPTVP QGLGRLFAHA AAMRTRVPAP PLVAIGGIDL AAMPSVLQSG VGCVAVVRAL TQAEDVPAAV QALQATFAAH VRA // ID B5UIL9_BACCE Unreviewed; 219 AA. AC B5UIL9; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BCAH1134_0432; OS Bacillus cereus AH1134. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405533; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1134; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Callegan M.C., RA Kolsto A.B., Okstad O.A., Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus AH1134."; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDA02000001; EDZ54460.1; -; Genomic_DNA. DR ProteinModelPortal; B5UIL9; -. DR EnsemblBacteria; EDZ54460; EDZ54460; BCAH1134_0432. DR PATRIC; 24772906; VBIBacCer51833_0098. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23629 MW; 7B98F2B475E84188 CRC64; MARIEIDKMS KLLQVYFIMG SNNCTRDPLA VLKEALDGGV TLFQFREKGE GSLIGEDRVR FAKELQTLCK EYSVPFIVND DVELAIELDA DGVHVGQDDE GITSVREKMG DKIIGVSAHT IEEARFAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAY FREQGITVPI VGIGGITIEN TAAVIEAGAD GVSVISAISL AESAYESTRK LVEEVKRSL // ID B5UJF7_BACCE Unreviewed; 208 AA. AC B5UJF7; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 22. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BCAH1134_0768; OS Bacillus cereus AH1134. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405533; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1134; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Callegan M.C., RA Kolsto A.B., Okstad O.A., Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus AH1134."; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDA02000001; EDZ54497.1; -; Genomic_DNA. DR ProteinModelPortal; B5UJF7; -. DR EnsemblBacteria; EDZ54497; EDZ54497; BCAH1134_0768. DR PATRIC; 24773567; VBIBacCer51833_0386. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 208 AA; 23050 MW; 2F93FBA22E470F4E CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLMEGFPA SKIVINDRID IAILLNIPRV QLGYRSTDVK SVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEISDIARC LSIPITAIGG ITPENTVDVL TNGVSGIAVM SGIISSSNPY SKAKSYKESI RKWAEKHV // ID B5V1E4_BACCE Unreviewed; 219 AA. AC B5V1E4; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BCH308197_0426; OS Bacillus cereus H3081.97. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=451708; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H3081.97; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus H3081.97."; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDL02000002; EDZ58857.1; -; Genomic_DNA. DR ProteinModelPortal; B5V1E4; -. DR EnsemblBacteria; EDZ58857; EDZ58857; BCH308197_0426. DR PATRIC; 24967379; VBIBacCer133158_1188. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23583 MW; 9EF4BB9B5967DB91 CRC64; MSRISKSEMS RLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTEEKRIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKR LVEEVSNSL // ID B5V9Y8_BACCE Unreviewed; 206 AA. AC B5V9Y8; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 23. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BCH308197_0760; OS Bacillus cereus H3081.97. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=451708; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H3081.97; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus H3081.97."; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDL02000021; EDZ55993.1; -; Genomic_DNA. DR ProteinModelPortal; B5V9Y8; -. DR EnsemblBacteria; EDZ55993; EDZ55993; BCH308197_0760. DR PATRIC; 24973927; VBIBacCer133158_4384. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22777 MW; 767D7D7B15B3A27E CRC64; MKNELHVISN GHMSFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK IVINDRIDIA ILLNIPRVQL GYRSADVRSV KEKFSYLHVG YSVHSLEEAI DAFKNGADSL VYGHVFPTDC KKGVPARGLE EISDIARCLS IPITAIGGIT PENTGDVLTN GVSGIAVMSG IISSSNPYSK AKSYKESIRK WAEKHV // ID B5VVZ0_ARTMA Unreviewed; 365 AA. AC B5VVZ0; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AmaxDRAFT_0682; OS Arthrospira maxima CS-328. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Arthrospira. OX NCBI_TaxID=513049; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CS-328; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Bryant D.A.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CS-328; RX PubMed=21890670; DOI=10.1128/AEM.00612-11; RA Carrieri D., Ananyev G., Lenz O., Bryant D.A., Dismukes G.C.; RT "Contribution of a Sodium Ion Gradient to Energy Conservation during RT Fermentation in the Cyanobacterium Arthrospira (Spirulina) maxima CS- RT 328."; RL Appl. Environ. Microbiol. 77:7185-7194(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYK01000003; EDZ96758.1; -; Genomic_DNA. DR ProteinModelPortal; B5VVZ0; -. DR EnsemblBacteria; EDZ96758; EDZ96758; AmaxDRAFT_0682. DR PATRIC; 24527281; VBIArtMax3094_0747. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 129 Unknown (By similarity). FT REGION 130 365 Thiamine-phosphate synthase (By FT similarity). FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 365 AA; 41306 MW; CCD1F42E5FDAB206 CRC64; MGDLNHKTKL GQPALYRILD ANLDRAREGI RTIEEWFRFG LDNSEMAAEC KNLRQQLAQW HSNELRMSRD TTTDVGTQLS HPSEENRESL EQVIQVNFCR VEEALRVLEE YGKVYHPNMG AAVKQMRYRV YTLESNLLAY GRHQKLQRAN LYLVTSPSER LMSVVEAALQ GGLKVVQYRD KDTDDHQRWK NARQLCQLCH RYNALFLVND RVDIAIAVNA DGVHLGQQDL PIAVAKQLLG PQKIVGKSTT NPEEMKLAIA EGADYIGVGP VYATPTKPDK QAAGLEYVRH ATRHASVPWF AIGGINMNNF DDVLMAGATR VAVVRSLMQA EQPTLVTQYF LSQFTRVQTL RDRQIVPENT PADFS // ID B5WF84_9BURK Unreviewed; 367 AA. AC B5WF84; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 13-NOV-2013, entry version 26. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=BH160DRAFT_1735; OS Burkholderia sp. H160. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=516466; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H160; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Tiedje J.; RT "Permanent draft sequence of Burkholderia sp. H160."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H160; RX PubMed=23209196; DOI=10.1128/JB.01756-12; RA Ormeno-Orrillo E., Rogel M.A., Chueire L.M., Tiedje J.M., RA Martinez-Romero E., Hungria M.; RT "Genome Sequences of Burkholderia sp. Strains CCGE1002 and H160, RT Isolated from Legume Nodules in Mexico and Brazil."; RL J. Bacteriol. 194:6927-6927(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYL01000016; EEA03047.1; -; Genomic_DNA. DR ProteinModelPortal; B5WF84; -. DR EnsemblBacteria; EEA03047; EEA03047; BH160DRAFT_1735. DR PATRIC; 30428663; VBIBurSp89998_1655. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 367 AA; 39481 MW; 1D189A2C47B41A5B CRC64; MTQSLTLRDR DLFWPPADEL IEAAERIRAC LGDWPPTHAP WRICLTAPDE PNGGDLIVIA DAQPHGEQMA HWLTRGAGVI VAAENRATLH LGGEKYGLEG HLAEDWIPAL AAFLDCGFDP HDALVLALAW RDGDETRADD AFPADLARFP RLTGLPAAPA QAFPRCPEKL GLYPVLPTAD WVERVVGFGV KTVQLRRKSA EPADVLKREI ARCVAAGRAH DAQVFINDHW QAALEAGAYG VHLGQEDVHT ADLSALADAG IRLGLSTHGF YEMLKALHFR PSYIALGAVF PTTTKVMPTA PQGLRRLARY VRLLDGVVPL VAIGGIDLQV LPDVLATGVG CAAVVRAVTE AADPAAAVSA LQHMFTQ // ID B5XYE5_KLEP3 Unreviewed; 211 AA. AC B5XYE5; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=KPK_5299; OS Klebsiella pneumoniae (strain 342). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=507522; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=342; RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141; RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H., RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., RA Mohamoud Y., Khouri H., Roesch L.F., Krogfelt K.A., Struve C., RA Triplett E.W., Methe B.A.; RT "Complete genome sequence of the N2-fixing broad host range endophyte RT Klebsiella pneumoniae 342 and virulence predictions verified in RT mice."; RL PLoS Genet. 4:E1000141-E1000141(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000964; ACI11279.1; -; Genomic_DNA. DR RefSeq; YP_002241066.1; NC_011283.1. DR ProteinModelPortal; B5XYE5; -. DR STRING; 507522.KPK_5299; -. DR EnsemblBacteria; ACI11279; ACI11279; KPK_5299. DR GeneID; 6939875; -. DR KEGG; kpe:KPK_5299; -. DR PATRIC; 20443696; VBIKlePne121904_5172. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; KPNE507522:GI0B-5300-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22958 MW; B6B4DFBEFBAA9D3E CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIERLLE AGVRTLQLRI KDQRDSDVEN DVIAAIALGR RYHARLFIND YWQLAIKHQA YGVHLGQEDL ETTDLSAIRK AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLDQLA RHIQRLADYP TVAIGGISLE KAPGVLATGV GSIAVVSAIT QAADWRAATD QLLALAGAGD E // ID B5YJ29_THEYD Unreviewed; 200 AA. AC B5YJ29; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; OrderedLocusNames=THEYE_A0397; OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / OS YP87). OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; OC Thermodesulfovibrio. OX NCBI_TaxID=289376; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51303 / DSM 11347 / YP87; RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.; RT "The complete genome sequence of Thermodesulfovibrio yellowstonii RT strain ATCC 51303 / DSM 11347 / YP87."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001147; ACI20306.1; -; Genomic_DNA. DR RefSeq; YP_002248244.1; NC_011296.1. DR ProteinModelPortal; B5YJ29; -. DR STRING; 289376.THEYE_A0397; -. DR EnsemblBacteria; ACI20306; ACI20306; THEYE_A0397. DR GeneID; 6942452; -. DR KEGG; tye:THEYE_A0397; -. DR PATRIC; 23907815; VBITheYel104483_0392. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TYEL289376:GH9L-397-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 200 AA; 22415 MW; A5B6C21FA5B7E76E CRC64; MINPELPSIC LIVSSKEIPE KLEIALKAGI KWIQYREKEL PRKEILKYAF WVKEITKHYN ALLTINDYLD IAITIKADGI HLGQNDLPIE VAKKFFSGII GISTHNLEEA LDAQKKGAHY IGYGPIFYTT TKKDALEPKG YDMLSLICKK IKVPVVAIGG IKKQHLKDLK AMGCKYVAIA SGILVGDVKS NVKDFLELFQ // ID B5YJ74_THEYD Unreviewed; 206 AA. AC B5YJ74; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; OrderedLocusNames=THEYE_A0444; OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / OS YP87). OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; OC Thermodesulfovibrio. OX NCBI_TaxID=289376; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51303 / DSM 11347 / YP87; RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.; RT "The complete genome sequence of Thermodesulfovibrio yellowstonii RT strain ATCC 51303 / DSM 11347 / YP87."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001147; ACI20874.1; -; Genomic_DNA. DR RefSeq; YP_002248289.1; NC_011296.1. DR ProteinModelPortal; B5YJ74; -. DR STRING; 289376.THEYE_A0444; -. DR EnsemblBacteria; ACI20874; ACI20874; THEYE_A0444. DR GeneID; 6941681; -. DR KEGG; tye:THEYE_A0444; -. DR PATRIC; 23907911; VBITheYel104483_0439. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GLGPICH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TYEL289376:GH9L-443-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 23365 MW; 063642F49679C473 CRC64; MNFKLYLISD RKIFPNKETF FRAVEIALKA GIKALQLREK DLTAKELYNL AKKLREITKR NDAMLFINDR IDIALAVEAD GVHLPQSGFP PRIVREVWKD RFLIGVSTHS IDEAKEASEW ADFITFSPIF HTPSKAHYGE PQGVEKLKEV KESVKCKVFA LGGIKLENVH ELIPYCDGIA LISGILAQRN IEGTVKKFKE ILGENI // ID B5Z7K7_HELPG Unreviewed; 211 AA. AC B5Z7K7; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPG27_801; OS Helicobacter pylori (strain G27). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=563041; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G27; RX PubMed=18952803; DOI=10.1128/JB.01416-08; RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S., RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.; RT "The complete genome sequence of Helicobacter pylori strain G27."; RL J. Bacteriol. 191:447-448(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001173; ACI27556.1; -; Genomic_DNA. DR RefSeq; YP_002266422.1; NC_011333.1. DR ProteinModelPortal; B5Z7K7; -. DR STRING; 563041.HPG27_801; -. DR EnsemblBacteria; ACI27556; ACI27556; HPG27_801. DR GeneID; 6963692; -. DR KEGG; hpg:HPG27_801; -. DR PATRIC; 20599610; VBIHelPyl113476_0859. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HPYL563041:GC38-815-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23135 MW; 5F037D4056B07510 CRC64; MFVAGSQDFY HIKSGKNDRI NVLLETLELA LQSQITAFQF RQKGDLALQD PIEIKQLALE CQKLCQKYGT PFIVNDEVQL ALELKADGVH VGQEDMAIEE VITLCKKRQF IGLSVNTLEQ ALKARHLDAV AYLGVGPIFP TPSKKDAKEV VGVNLLKKIR DSGVKKPLIA IGGITMHNAS KLREYGGIAV ISAITQAKDK ALAIEKLLNN A // ID B5ZPC8_RHILW Unreviewed; 217 AA. AC B5ZPC8; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Rleg2_3269; OS Rhizobium leguminosarum bv. trifolii (strain WSM2304). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=395492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM2304; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Yates R., Ardley J., Tiwari R.P., O'Hara G., Howieson J., Brau L., RA Reeve W.; RT "Complete sequence of chromosome of Rhizobium leguminosarum bv. RT trifolii WSM2304."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001191; ACI56536.1; -; Genomic_DNA. DR RefSeq; YP_002282762.1; NC_011369.1. DR ProteinModelPortal; B5ZPC8; -. DR STRING; 395492.Rleg2_3269; -. DR EnsemblBacteria; ACI56536; ACI56536; Rleg2_3269. DR GeneID; 6982022; -. DR KEGG; rlt:Rleg2_3269; -. DR PATRIC; 23130740; VBIRhiLeg95088_5180. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RLEG395492:GJB3-3314-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 217 AA; 22844 MW; 8980F1A6E42D4B00 CRC64; MTEPENRCRL VLIVPDIADA DEQARIVADA LKGGDVASVI VPQYGLDDGT FQKHAEKLVP LIQDAGAAAL IAGDSRVAGR AKADGLHLSG NAEALSEAIE KHAPKLIVGG GNAADRHNAL EIGEARPDYI FFGKLDGDIK PEVHPKNLAL GEWWASMIEI PCIVMGGTDP ASALAVAETG AEFVALRLAV FGEPNRAPSI VAEVNALLDE KAPRFED // ID B6A3G6_RHILW Unreviewed; 211 AA. AC B6A3G6; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rleg2_5776; OS Rhizobium leguminosarum bv. trifolii (strain WSM2304). OG Plasmid pRLG202. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=395492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM2304; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Yates R., Ardley J., Tiwari R.P., O'Hara G., Howieson J., Brau L., RA Reeve W.; RT "Complete sequence of plasmid 2 of Rhizobium leguminosarum bv. RT trifolii WSM2304."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001193; ACI58949.1; -; Genomic_DNA. DR RefSeq; YP_002278049.1; NC_011366.1. DR ProteinModelPortal; B6A3G6; -. DR STRING; 395492.Rleg2_5776; -. DR EnsemblBacteria; ACI58949; ACI58949; Rleg2_5776. DR GeneID; 6977165; -. DR KEGG; rlt:Rleg2_5776; -. DR PATRIC; 23120630; VBIRhiLeg95088_0167. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RLEG395492:GJB3-5843-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Plasmid; KW Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21499 MW; 5D055CC31FA894DF CRC64; MKTFDLSLYL VLDPDLCAGI GMVETARRAV AGGATMVQLR DKHAGTTAMI ETGRALKQAL DGTGARLIVN DDVEAAIAIG ADGLHIGQED MDAVRARAMI GPDMILGLSV ETAALAASVD PSLVDYTGIG PVFATPTKAD HKQPIGFHGL ARLVAASPVP SVAIGGLKAE HVAKVFAAGA SGLAVVSAIS GTPDPEAATR RIAAEIRKAR A // ID B6AMP2_9BACT Unreviewed; 215 AA. AC B6AMP2; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGL2_11181014; OS Leptospirillum sp. Group II '5-way CG'. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=419541; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=14961025; DOI=10.1038/nature02340; RA Tyson G.W., Chapman J., Hugenholtz P., Allen E.E., Ram R.J., RA Richardson P.M., Solovyev V.V., Rubin E.M., Rokhsar D.S., RA Banfield J.F.; RT "Community structure and metabolism through reconstruction of RT microbial genomes from the environment."; RL Nature 428:37-43(2004). RN [2] RP NUCLEOTIDE SEQUENCE. RX PubMed=18651792; DOI=10.1371/journal.pbio.0060177; RA Simmons S.L., Dibartolo G., Denef V.J., Goltsman D.S., Thelen M.P., RA Banfield J.F.; RT "Population genomic analysis of strain variation in Leptospirillum RT group II bacteria involved in acid mine drainage formation."; RL PLoS Biol. 6:E177-E177(2008). RN [3] RP NUCLEOTIDE SEQUENCE. RG US DOE Joint Genome Institute (JGI-PGF); RA DiBartolo G., Denef V.J., Aliaga Goltsman D.S., Simmons S.L., RA Banfield J.F., Lucas S.L., Copeland A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995259; EDZ39749.1; -; Genomic_DNA. DR ProteinModelPortal; B6AMP2; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23204 MW; D2EBA2996F1CE972 CRC64; MIKSLVSPLF PLMYVTPEDI PVKPLVQRAL EAVAGGVTSI QVRRKEGSAK ELFDLAILLA ESLPSGFPLI VNSRLDVALE AGAWGLHLPE EHIPLPFFRD RAPNLRLGVS CHSLESARKA FSEGADYLVA GPVFDTPSKR SYGPPPGPSF LGKVTKSVPL PVLAIGGVTE EGIPEVWRSG ASGFAVMGAL AYEEDTRSRA FSLRKCWSRQ GDLRP // ID B6APP1_9BACT Unreviewed; 212 AA. AC B6APP1; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGL2_11212078; OS Leptospirillum sp. Group II '5-way CG'. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=419541; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=14961025; DOI=10.1038/nature02340; RA Tyson G.W., Chapman J., Hugenholtz P., Allen E.E., Ram R.J., RA Richardson P.M., Solovyev V.V., Rubin E.M., Rokhsar D.S., RA Banfield J.F.; RT "Community structure and metabolism through reconstruction of RT microbial genomes from the environment."; RL Nature 428:37-43(2004). RN [2] RP NUCLEOTIDE SEQUENCE. RX PubMed=18651792; DOI=10.1371/journal.pbio.0060177; RA Simmons S.L., Dibartolo G., Denef V.J., Goltsman D.S., Thelen M.P., RA Banfield J.F.; RT "Population genomic analysis of strain variation in Leptospirillum RT group II bacteria involved in acid mine drainage formation."; RL PLoS Biol. 6:E177-E177(2008). RN [3] RP NUCLEOTIDE SEQUENCE. RG US DOE Joint Genome Institute (JGI-PGF); RA DiBartolo G., Denef V.J., Aliaga Goltsman D.S., Simmons S.L., RA Banfield J.F., Lucas S.L., Copeland A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995260; EDZ39227.1; -; Genomic_DNA. DR ProteinModelPortal; B6APP1; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23741 MW; BBFEECE1883A8364 CRC64; MTEMKRSFPS LLYLAGTQDF PSPDHFFSHV EKACQGGLKW FQYREKRLPD RLLYETAFRL REITREYGTL LTINDRTDIA LLVGADGVHL GQEDLPSVRE FQKLFPSETL HLGISTHSPY EVRRALLLKP DYLGVGPIFH TSTKNTGVEP RGVTAIEETR TLTSLPLVAI GGITPEHAGV LYRAGSHALA LSGAITNSLD PFPVLEMFFR SR // ID B6AW25_9RHOB Unreviewed; 207 AA. AC B6AW25; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=RB2083_2101; OS Rhodobacteraceae bacterium HTCC2083. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=314270; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2083; RA Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995276; EDZ42586.1; -; Genomic_DNA. DR ProteinModelPortal; B6AW25; -. DR EnsemblBacteria; EDZ42586; EDZ42586; RB2083_2101. DR PATRIC; 28459119; VBIRhoBac88862_0605. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 207 AA; 21975 MW; A6C30312152CDE23 CRC64; MSDIEQPQLY LITPPAFDLD VFPTLLAKVL DSVDMACVRL ALANQDEDDI CRAADALSGV TQARDVALVI DEHILLVEKL GLDGVHLGDG ARRVAKTRKM LGGDAIIGAF CGTSRHDGMN AGEAGADYVS FGPIGENTLG DGARAEHDLF QWWSEVIEVP IVAEGAIDDA ALQAFAPVTD FFAIGDEIWR ADAPAEEAKA ILAKVTG // ID B6BAJ4_9RHOB Unreviewed; 197 AA. AC B6BAJ4; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 16-OCT-2013, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RBY4I_2330; OS Rhodobacterales bacterium Y4I. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales. OX NCBI_TaxID=439496; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y4I; RA Moran M.A., Buchan A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995281; EDZ47112.1; -; Genomic_DNA. DR ProteinModelPortal; B6BAJ4; -. DR EnsemblBacteria; EDZ47112; EDZ47112; RBY4I_2330. DR PATRIC; 28483026; VBIRhoBac125813_0109. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 197 AA; 21912 MW; 1CDB46EE7A2357EE CRC64; MERFYLIVGH VGRLELLVPQ GVKLVQLRIK DQPDAEVRRQ IARARDFCAV HGAQLVVNDY WQAALELNCN FVHLGQEDMD AADFAALRRR GVRFGLSTHD EAELERALSL GPAYVALGPV YPTLLKRMKW EPQGLERVTR WKQMAGKTPL VAIGGLTPER LPGVFAAGAD SAAVVTDIQL AEDPEARTRE WAEACRA // ID B6BE07_9RHOB Unreviewed; 268 AA. AC B6BE07; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=RBY4I_236; OS Rhodobacterales bacterium Y4I. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales. OX NCBI_TaxID=439496; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y4I; RA Moran M.A., Buchan A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995281; EDZ45029.1; -; Genomic_DNA. DR ProteinModelPortal; B6BE07; -. DR EnsemblBacteria; EDZ45029; EDZ45029; RBY4I_236. DR PATRIC; 28484197; VBIRhoBac125813_0857. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 268 AA; 28638 MW; 125F4E1DBDFC31AC CRC64; MGIVFSGKIG TAVLPARRRG KVQRGFGAQY AGRHRRKSLR PAANRLNTLQ SPEQWSTMMG SPADAPEQPQ IYLISPPSFE LGKFPALLAR VLDEVDVACV RLDLASRDQD TLSRAGDALR EVTMARDVAL VISDHQILAE RLGLDGVHLT DASKSVRAAR KALGPDAIVG CFCGASQHDG MVAGEAGADY VSFGPVGTSG LGDGARAEAD LFEWWSKMIE VPVVAEGGLT EDLVRSIAPN TDFFGIGDEI WHAEDPLAAL KTLMRAMG // ID B6BK14_9HELI Unreviewed; 187 AA. AC B6BK14; H1FS24; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 19-MAR-2014, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN Name=thiE3; ORFNames=CBGD1_2311, SMGD1_2582; OS Sulfurimonas gotlandica GD1. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Sulfurimonas. OX NCBI_TaxID=929558; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GD 1; RA Labrenz M., Jurgens K., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GD1; RX PubMed=22203982; DOI=10.1073/pnas.1111262109; RA Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., RA Teeling H., Labrenz M., Jurgens K.; RT "Genome and physiology of a model Epsilonproteobacterium responsible RT for sulfide detoxification in marine oxygen depletion zones."; RL Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995287; EDZ62744.1; -; Genomic_DNA. DR EMBL; AFRZ01000001; EHP31104.1; -; Genomic_DNA. DR EnsemblBacteria; EDZ62744; EDZ62744; CBGD1_2311. DR EnsemblBacteria; EHP31104; EHP31104; SMGD1_2582. DR PATRIC; 27780630; VBICamBac111121_1154. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 187 AA; 21007 MW; 00B2F0AB45B20F6E CRC64; MRLYALCDQE LLDKRGLSLE EFIQIAKDHN AEIIQYRNKN ADVAFIKQQL IFIRKNYDGF LIVNDAYELI EFCDGVHVGQ EDLKAIDEDV FKAVKILRSV IKKEKLLGIS THNEQEVLQA NDMDLNYIGL GAYRETSTKK DISGVLGSSL DEIALKSKHL VAAIGGVKLD DNFSNVTYKV IGSGLIK // ID B6BNB5_9HELI Unreviewed; 183 AA. AC B6BNB5; H1FZH8; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 19-MAR-2014, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE2; ORFNames=CBGD1_2462, SMGD1_2462; OS Sulfurimonas gotlandica GD1. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Sulfurimonas. OX NCBI_TaxID=929558; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GD 1; RA Labrenz M., Jurgens K., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GD1; RX PubMed=22203982; DOI=10.1073/pnas.1111262109; RA Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., RA Teeling H., Labrenz M., Jurgens K.; RT "Genome and physiology of a model Epsilonproteobacterium responsible RT for sulfide detoxification in marine oxygen depletion zones."; RL Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995292; EDZ61396.1; -; Genomic_DNA. DR EMBL; AFRZ01000001; EHP30985.1; -; Genomic_DNA. DR EnsemblBacteria; EDZ61396; EDZ61396; CBGD1_2462. DR EnsemblBacteria; EHP30985; EHP30985; SMGD1_2462. DR PATRIC; 27783485; VBICamBac111121_2558. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 183 AA; 20779 MW; 1CF4B515537E2803 CRC64; MQKYLITSRE FYTDTPAIFR NILHEQFARH RPTYALYRDK SNPNYDIQAA HFVEVCNQFE TIKSFIHRDA ELAKKLEATG VHLTSTQFDE ITIAKELGLE VIISTHTHDE VIKAKKLGAD AVTYSPVFAS PGKGEPKGIK DLKDILNKCE IKVFALGGIV DSEQVKAIEE TEAYGFASIR YFY // ID B6BQW6_9PROT Unreviewed; 204 AA. AC B6BQW6; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PB7211_1109; OS Candidatus Pelagibacter sp. HTCC7211. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=439493; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC7211; RA Giovannoni S.J., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995298; EDZ60786.1; -; Genomic_DNA. DR ProteinModelPortal; B6BQW6; -. DR EnsemblBacteria; EDZ60786; EDZ60786; PB7211_1109. DR PATRIC; 30359477; VBICanPel29514_1497. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 23407 MW; 460451BF63BB71AE CRC64; MRINKKKFIY LISPNKIYPK FYHDLNKVFE TGKISLFQLR FKRYSLKQKI AIGKKIHPIC KKNKVKFLVN DDPTLSKKIN ADGCHIGQQD MSIVEARKII GNKIIGVTCH NSINLAKAAI KRKADYIAFG SFFSTKTKKV KYKATTKIVD KVKKLTKIPI VAIGGINISN YKKLLLNNVN LLAISGYVWN NKKYKPYKTI EKIK // ID B6BRL3_9PROT Unreviewed; 188 AA. AC B6BRL3; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=PB7211_843; OS Candidatus Pelagibacter sp. HTCC7211. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=439493; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC7211; RA Giovannoni S.J., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995298; EDZ60520.1; -; Genomic_DNA. DR ProteinModelPortal; B6BRL3; -. DR EnsemblBacteria; EDZ60520; EDZ60520; PB7211_843. DR PATRIC; 30356875; VBICanPel29514_0219. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 188 AA; 22119 MW; 3C34D84911D8400F CRC64; MQKNSFKIYS FVNEFNLSDL HQLSKDICII YRNYDDINHL ENILKLKDYC KNIRTKFYLS NDIKLSIKLR LDGVYIPSFN NKANYVQNYS LPKNFDIIGS AHNIPEINTK LKQKCSEIFL SPLFKVNKSR KFLGINRFNL MSLNKKAYFI ALGGINERNY KMIKLLRTNG FASISWAKKN GLRKLRPF // ID B6BUY1_9PROT Unreviewed; 310 AA. AC B6BUY1; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=KB13_1125; OS beta proteobacterium KB13. OC Bacteria; Proteobacteria; Betaproteobacteria. OX NCBI_TaxID=314607; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KB13; RA Rappe M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995299; EDZ64993.1; -; Genomic_DNA. DR ProteinModelPortal; B6BUY1; -. DR EnsemblBacteria; EDZ64993; EDZ64993; KB13_1125. DR PATRIC; 30886230; VBIBetPro60814_1036. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01401; MUTATORMUTT. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. PE 4: Predicted; SQ SEQUENCE 310 AA; 35979 MW; 2BC930DD6A2D6F5F CRC64; MQNIEPKITK VVAGILINSK NEVLISQRLT SQPWPGYWEF PGGKVEVNES LDQCLSRELF EEISINPISY TEWITREFFQ DNRVIKITFF KITRWTGEIQ KKEVNDYRWI DVENINSWPK KILPRNIYIL KALALPSYYL ITNFFEDEKS IKKTINSKDI WIQYREPLLS IEKLHYFYEF LMKKSASKIL INSRHKDLIK NNGIHYTSKD LNKIKKLDKS IVNGASVHSL DELKLANKLG FDFVVLSQIK KTLSHPQREG MGWNKFKELA NHSDVPVFAL GGLSLSDLAE AQKNGAVGIS SQREGWKLLN // ID B6C394_9GAMM Unreviewed; 321 AA. AC B6C394; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 16-OCT-2013, entry version 35. DE SubName: Full=Thiamine monophosphate synthase/TENI subfamily, putative; GN ORFNames=NOC27_2724; OS Nitrosococcus oceani AFC27. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=473788; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AFC27; RA Klotz M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995301; EDZ66044.1; -; Genomic_DNA. DR ProteinModelPortal; B6C394; -. DR EnsemblBacteria; EDZ66044; EDZ66044; NOC27_2724. DR PATRIC; 25493909; VBINitOce87996_3181. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 321 AA; 35262 MW; F731BA7BB7EC631E CRC64; MVLQVAAGAI FNRQGQVLLS KRPLHVHQGN LWEFPGGKLK PGEEVRQALS RELWEELGIQ VLQARPLLQV HHDYPDRSVL LHVWRVDRFS GTPKGQEGQP VVWVSPENLN AYPLPAANHA VVTAVCLPPT YLITKEPAGN QMAFLSSLRQ SLQAGVQLVQ LRAKKLSPEH YQNLTWKVQR LCFEYKAILL VNTVPAQAAE WGADGVHLTG NHLMHLSHRP LPANKWVAAS CHNAAQLAHA ANIGVDFAVL GPVFHTSTHP QALPLGWERF QTLIAQIPFP VYALGGVGPE HLKEAWSRGA QGIAAIRALW GDRAGSFGVS P // ID B6C477_9GAMM Unreviewed; 217 AA. AC B6C477; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NOC27_2766; OS Nitrosococcus oceani AFC27. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=473788; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AFC27; RA Klotz M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995301; EDZ66086.1; -; Genomic_DNA. DR ProteinModelPortal; B6C477; -. DR EnsemblBacteria; EDZ66086; EDZ66086; NOC27_2766. DR PATRIC; 25494605; VBINitOce87996_2187. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23327 MW; F171BA2D2D007049 CRC64; MSSSIRGLYA IADTHLLPRQ DLGNAVALAL QGGASLIQYR DKSQEITRRY KEAESLQRIC HQYQAPLIIN DDALLAAEIG AEGVHLGQDD SSITSARKIL GAKAIIGISC YNDLARAIAA EQAGADYVAF GRLFPSITKP EPIWASLALL REARKNLNLP IVAIGGITPE NALQVIEAGA SAVAVIGGLF KSRDIRAAAA AYRQHFPSWN LPKPRLF // ID B6EGV2_ALISL Unreviewed; 226 AA. AC B6EGV2; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=VSAL_I2984; OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain OS LFI1238)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=316275; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LFI1238; RX PubMed=19099551; DOI=10.1186/1471-2164-9-616; RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., RA Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., RA Sanders S., Thurston S., Parkhill J., Willassen N.P., Thomson N.R.; RT "The genome sequence of the fish pathogen Aliivibrio salmonicida RT strain LFI1238 shows extensive evidence of gene decay."; RL BMC Genomics 9:616-616(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM178379; CAQ80668.1; -; Genomic_DNA. DR RefSeq; YP_002264309.1; NC_011312.1. DR ProteinModelPortal; B6EGV2; -. DR STRING; 316275.VSAL_I2984; -. DR EnsemblBacteria; CAQ80668; CAQ80668; VSAL_I2984. DR GeneID; 6989281; -. DR KEGG; vsa:VSAL_I2984; -. DR PATRIC; 20856516; VBIAliSal95923_3228. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24985 MW; 3A03DF2995C0EB1B CRC64; MYSFPAIDRE KFGLYPVVDD VSWIETLLKL NVQTIQLRIK NSEHPDLEKQ IIEAIRLGRE YDAQVFINDY WQLAIKHGAF GIHLGQEDIE VADLLAISDA GICLGLSTHD DSELMTVKAL NPSYLALGHV FPTPTKDMPS EPQGLVNLAN NRKLAGETPT VAIGGIDLTV AEQVWQTGVD SIAVVRAITQ ADNIEKAVNQ FSAILAQPRT SDYLLKSQNT LEVMDE // ID B6ERB5_ALISL Unreviewed; 206 AA. AC B6ERB5; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=VSAL_II0492; OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain OS LFI1238)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=316275; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LFI1238; RX PubMed=19099551; DOI=10.1186/1471-2164-9-616; RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., RA Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., RA Sanders S., Thurston S., Parkhill J., Willassen N.P., Thomson N.R.; RT "The genome sequence of the fish pathogen Aliivibrio salmonicida RT strain LFI1238 shows extensive evidence of gene decay."; RL BMC Genomics 9:616-616(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM178380; CAQ81246.1; -; Genomic_DNA. DR RefSeq; YP_002264823.1; NC_011313.1. DR ProteinModelPortal; B6ERB5; -. DR STRING; 316275.VSAL_II0492; -. DR EnsemblBacteria; CAQ81246; CAQ81246; VSAL_II0492. DR GeneID; 6962604; -. DR KEGG; vsa:VSAL_II0492; -. DR PATRIC; 20857760; VBIAliSal95923_3841. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IGRTCHG; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22252 MW; A4CE717D6C443CDA CRC64; MNNPYKLYLV TDDKQDIDTL CNVVKEAVKG GVTMVQIREK HGDIRAFIER SIAVKNVLKD SGVPLIINDR VDVALAVRAD GVHLGQSDMP ANLARQLIGP DMILGLSVEN ETQLREAQDL PVDYLGISAI FSTPTKTNII KEWGIDGLTK AVKESKLPLV AIGGINETNI KKVADTQVDG IALVSAICHA TSPKQASEGL LELMGR // ID B6FKI1_9CLOT Unreviewed; 213 AA. AC B6FKI1; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLONEX_00627; OS Clostridium nexile DSM 1787. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=500632; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1787; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1787; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium nexile (DSM 1787)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWO01000041; EEA83479.1; -; Genomic_DNA. DR ProteinModelPortal; B6FKI1; -. DR EnsemblBacteria; EEA83479; EEA83479; CLONEX_00627. DR PATRIC; 30593995; VBICloNex32710_0943. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22717 MW; 975B79CAE7ADFB6E CRC64; MNFDYTLYLV TDRQLMSCDS LTEAVEQAIL GGCTMIQLRE KELSSLEFYN QAVAVKQVTD KYHIPLIIND RIDIAMAVQA TGVHIGQHDL PAAAVRKVIG ENMLLGVSAS SIAEAIQAQQ DGADYLGVGA MFPTGTKTDA DSVSMEELQK IRAAVSLPIV VIGGINKGNA GRFKPMGIDG LAVVSAIIAQ SDIKAAAAEL KDLFCGKEKK NGF // ID B6FL22_9CLOT Unreviewed; 218 AA. AC B6FL22; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLONEX_00818; OS Clostridium nexile DSM 1787. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=500632; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1787; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1787; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium nexile (DSM 1787)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWO01000048; EEA83277.1; -; Genomic_DNA. DR ProteinModelPortal; B6FL22; -. DR EnsemblBacteria; EEA83277; EEA83277; CLONEX_00818. DR PATRIC; 30594329; VBICloNex32710_0513. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23842 MW; 2F66D9363BB8320F CRC64; MKMERKVMRC RPEMMRLYAV TDRTWTKKKS LIEQVEAAIC GGATCIQLRE KNLDEEAFLR EAMEMQKLCE TYQVPLIIND HVEIAKQCKA AGVHLGQKDM EAGRAREILG PKMILGVSAR TVEQAVQAER AGADYLGVGA VFQTSTKTDA KEISHAILKE ICESVNIPVV AIGGIGKQNI EALAGSGIAG VALVSAVFAA EDIEQECRGL LKQIERIV // ID B6FX31_9FIRM Unreviewed; 210 AA. AC B6FX31; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=CLOHIR_00430; OS Clostridium hiranonis DSM 13275. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=500633; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13275; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13275; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium hiranonis (DSM 13275)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWP01000012; EEA85951.1; -; Genomic_DNA. DR ProteinModelPortal; B6FX31; -. DR EnsemblBacteria; EEA85951; EEA85951; CLOHIR_00430. DR PATRIC; 31116019; VBICloHir23630_0610. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 210 AA; 24063 MW; 7E1F8C459BFD2252 CRC64; MINLYLITNR TLCSEQEYFD RIKEACINGV DNIIIREKDL TDEEVICIYE KISQSLPVDV RKKTSIIINS KFKAYEDTDC DGIHLPFWLF KEKLEERYNF KIEKQIGLSL HSADEVAEME ELCSKYGVKV SYITLSHIYE TKCKEGLKPR GLELLKMGGE LTKVKVVALG GIDSSNVAET LKYCDDIAVM SLIMKSNDVK RTVEELINCK // ID B6FXN5_9FIRM Unreviewed; 223 AA. AC B6FXN5; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLOHIR_00635; OS Clostridium hiranonis DSM 13275. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=500633; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13275; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13275; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium hiranonis (DSM 13275)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWP01000024; EEA85736.1; -; Genomic_DNA. DR ProteinModelPortal; B6FXN5; -. DR EnsemblBacteria; EEA85736; EEA85736; CLOHIR_00635. DR PATRIC; 31116411; VBICloHir23630_0336. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 53 57 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24247 MW; 9ABBDEE8EBA67A01 CRC64; MEINWKKVLN LKSSNINGKD LQLYAITDRH WLNERTLAEQ VRECLEGGAT ILQIREKNLP ENEFLEEAKE IQALCKEFKI PFIVNDNINI AAEIKADGVH VGQEDMDAKK VRDMLGENAI LGVSASTVEE ALKAERDGAD YLGVGAVFPT STKGDADSVT FETLKEICET VSIPVVAIGG ISADNLLKLK GSGIDGVSVI SAIFASDDIT AATKKLKELT EEL // ID B6GC63_9ACTN Unreviewed; 497 AA. AC B6GC63; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 19-FEB-2014, entry version 32. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.7.4.7; GN Name=thiD; ORFNames=COLSTE_01682; OS Collinsella stercoris DSM 13279. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Collinsella. OX NCBI_TaxID=445975; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13279; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Collinsella stercoris (DSM 13279)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13279; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXJ01000091; EEA90129.1; -; Genomic_DNA. DR ProteinModelPortal; B6GC63; -. DR EnsemblBacteria; EEA90129; EEA90129; COLSTE_01682. DR PATRIC; 29050195; VBIColSte7090_1140. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 497 AA; 51114 MW; 8BDD9FE95B7FC231 CRC64; MRLYAVTDRA WLNGRTLPEL VADAIAGGAT FIQLREKHAT HDEIVALARE LMPICHAAGV PFVIDDEVEI AREVGADGVH VGQSDTACAD ARRLLGDGAI IGVSVQTVEE ARAAQAAGAD YLGVGALIPT PTKPDAVDVT SEELARICRA VDIPVVGIGG LRVETLDVLA NSGVDGAAVV SALFAADDAQ AAARSLRARL DEMLGGGESA FPALPPACAA LPAVLAIAGS DSSGGAGIQA DIKTVAAHGL FAETAVTALT AQNTMGVRNV LEATPTFIAE QIDAIFEDIP PAAIKIGMCP SAPVIEAVAD ALTRWSATNI VLDPVMVATS GARLIAEDAV HALEDRLIPL ARLITPNMPE AEVLAGFEVR DEKDQERAAV ALADRFGCAV LVKGGHGVHD ANDVLALPPT ETADVGAGVR TTWLRSPRVD TENTHGTGCT LSSAIACGLA RGLGLEESVA AAKSYLMGAL EAGLNLGAGS GPIDHMWAYR PHQKVPV // ID B6H1X4_PENCW Unreviewed; 508 AA. AC B6H1X4; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 16-APR-2014, entry version 37. DE SubName: Full=Pc13g03600 protein; GN ORFNames=Pc13g03600, PCH_Pc13g03600; OS Penicillium chrysogenum (strain ATCC 28089 / DSM 1075 / Wisconsin OS 54-1255) (Penicillium notatum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium; OC Penicillium chrysogenum complex. OX NCBI_TaxID=500485; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 28089 / DSM 1075 / Wisconsin 54-1255; RX PubMed=18820685; DOI=10.1038/nbt.1498; RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M., RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M., RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F., RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., RA van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H., RA Wagner C., Wortman J.R., Bovenberg R.A.L.; RT "Genome sequencing and analysis of the filamentous fungus Penicillium RT chrysogenum."; RL Nat. Biotechnol. 26:1161-1168(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM920428; CAP91429.1; -; Genomic_DNA. DR RefSeq; XP_002558797.1; XM_002558751.1. DR ProteinModelPortal; B6H1X4; -. DR STRING; 500485.B6H1X4; -. DR GeneID; 8313460; -. DR KEGG; pcs:Pc13g03600; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR BioCyc; PCHR:PC13G03600-MONOMER; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 508 AA; 53985 MW; B65B69BD42C9FC9D CRC64; MTVDLSLYLV TDSTPAILKG RDLCTVVESA LQGGVTVVQY RDKTNDTGVQ VETARKLHRV TKKYNVPLLI NDRVDVALAI GAEGFTEAKK LLPENAIIGI STSSVEEAKK ATADGADYIG IGTMFATPTK TNTKSVIGTA GTQVILDAIK DSPIGTVSIG GINHSNVQRV LYQSQSPKKA LDGVAIVSAI VGADDPKASA EHFVELIRNP PRFAQIANPP RANEAEALLN EVPQIIRKMV EVHPLVHNMI NFVVSNFVAN VALSIGASPI MSPYGDEATD LCKFDGALLI NMGTLTSESV SNYVKAIKAY NDRGNPVVYD PVGAAATHIR RNAVAQLMAG GYFDLIKGNE GEIRQVWGSS AVQQRGVDSG PSTLDGNQKA TLARDLARRE RNVVLLTGAT DYLSDGERVI AVENGHPYLG QVTGTGCAIG TISGCFLAAH RSDRLLAVLS GILMYEIAAE NAAAKEYVRG PGSFVPAFVD ELYAIRTAAA NGDDSWFAGR AKVHEVKL // ID B6J1X4_COXB2 Unreviewed; 479 AA. AC B6J1X4; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 14-MAY-2014, entry version 44. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.5.1.3; DE EC=2.7.1.49; DE EC=2.7.4.7; GN Name=thiDE; OrderedLocusNames=CbuG_1672; OS Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain OS Q212)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Coxiella. OX NCBI_TaxID=434923; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CbuG_Q212; RX PubMed=19047403; DOI=10.1128/IAI.01141-08; RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., RA Samuel J.E., Heinzen R.A.; RT "Comparative genomics reveal extensive transposon-mediated genomic RT plasticity and diversity among potential effector proteins within the RT genus Coxiella."; RL Infect. Immun. 77:642-656(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001019; ACJ18952.1; -; Genomic_DNA. DR RefSeq; YP_002304097.1; NC_011527.1. DR ProteinModelPortal; B6J1X4; -. DR STRING; 434923.CbuG_1672; -. DR EnsemblBacteria; ACJ18952; ACJ18952; CbuG_1672. DR GeneID; 7014088; -. DR KEGG; cbg:CbuG_1672; -. DR PATRIC; 17914427; VBICoxBur10955_1670. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CBUR434923:GC8S-1668-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 479 AA; 52724 MW; 2EEF0D59BB1B53AE CRC64; MNQKSIVWSI GGSDCSGGAG CQADILTCRD FNVHAASIIT TITAQNAEQV LKINYCDSDL IQKQIQALKE TLPPTVIKLG LLGTKEIVTA VASYLKNYSG KVVCDPVLNS TSGVLLHASD YLDLLKKLLF PHVDLLTPNI PEAEILIQNK IHTFSDIISA AHQLLKCGVS AVLLKGGHLI GSKARDFFTD GKCEFWLAHT KIPKTRVRGT GCALSSAISS AIALGYSLKD AIVVAKMYVQ QGIRQNFKVN TQELMGRQGF PRRSIDLPWV TKNANFKRKS FPLCNSFGFY PIVDSVEWVE RLLSYGVRTI QLRIKNASPQ KIKKAVIESV ALARHYQAKL FINDYWKLAI EAGAYGVHLG QEDLETADLS AIRAANLRLG ISTHTLYELS RAHAIQPSYV AFGPIYETYS KPMPYSARGL EWLRYWCEIS PYPVVAIGGI NLNRLESVLN AGAVNVAVIS AVTKSKTPQK TVRAFLNRI // ID B6J5W7_COXB1 Unreviewed; 479 AA. AC B6J5W7; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.5.1.3; DE EC=2.7.1.49; DE EC=2.7.4.7; GN Name=thiDE; OrderedLocusNames=CbuK_0530; OS Coxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain OS Q154)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Coxiella. OX NCBI_TaxID=434924; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CbuK_Q154; RX PubMed=19047403; DOI=10.1128/IAI.01141-08; RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., RA Samuel J.E., Heinzen R.A.; RT "Comparative genomics reveal extensive transposon-mediated genomic RT plasticity and diversity among potential effector proteins within the RT genus Coxiella."; RL Infect. Immun. 77:642-656(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001020; ACJ19809.1; -; Genomic_DNA. DR RefSeq; YP_002304954.1; NC_011528.1. DR ProteinModelPortal; B6J5W7; -. DR STRING; 434924.CbuK_0530; -. DR EnsemblBacteria; ACJ19809; ACJ19809; CbuK_0530. DR GeneID; 7015043; -. DR KEGG; cbc:CbuK_0530; -. DR PATRIC; 17916460; VBICoxBur77120_0545. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CBUR434924:GHWU-528-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 479 AA; 52750 MW; C79A0954C6698BD0 CRC64; MNQKSIVWSI GGSDCSGGAG CQADILTCRD FNVHAASIIT TITAQNAEQV LKINYCDSDL IQKQIQALKE TLPPTVIKLG LLGTKEIVTP VASYLKNYSG KVVCDPVLNS TSGVLLHASD YLDLLKKLLF PHVDLLTPNI PEAEILIQNK IHTFSDIISA AHQLLKCGVS AVLLKGGHLI GSKARDFFTD GKCEFWLAHT KIPKTRVRGT GCALSSAISS AIALGYSLKD AIVVAKMYVQ QGIRQNFKVN TQELMGRQGF PRRSIDLPWV TKNANFKRKS FPLCNSFGFY PIVDSVEWVE RLLSYGVRTI QLRIKNASPQ KIKKAVIESV ALARHYQAKL FINDYWKLAI EAGAYGVHLG QEDLETADLS AIRAANLRLG ISTHTLYELS RAHAIQPSYV AFGPIYETYS KPMPYSARGL EWLRYWCEIS PYPVVAIGGI NLNRLESVLN AGAVNVAVIS AVTKSKTPQK TVRAFLNRI // ID B6JI84_OLICO Unreviewed; 202 AA. AC B6JI84; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE SubName: Full=Thiamine-phosphate pyrophosphorylase ThiE; DE EC=2.5.1.3; GN Name=thiE2; OrderedLocusNames=OCA5_c10620, OCAR_7031; OS Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Oligotropha. OX NCBI_TaxID=504832; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49405 / DSM 1227 / OM5 [Mississippi], and OM5; RX PubMed=18539730; DOI=10.1128/JB.00614-08; RA Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.; RT "Genome sequence of the chemolithoautotrophic bacterium Oligotropha RT carboxidovorans OM5T."; RL J. Bacteriol. 190:5531-5532(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49405 / DSM 1227 / OM5, and OM5; RX PubMed=21742883; DOI=10.1128/JB.05619-11; RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., RA Meyer O.; RT "Complete genome sequences of the chemolithoautotrophic Oligotropha RT carboxidovorans strains OM4 and OM5."; RL J. Bacteriol. 193:5043-5043(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001196; ACI94139.1; -; Genomic_DNA. DR EMBL; CP002826; AEI05781.1; -; Genomic_DNA. DR RefSeq; YP_002290004.1; NC_011386.1. DR RefSeq; YP_004632022.1; NC_015684.1. DR STRING; 504832.OCAR_7031; -. DR EnsemblBacteria; ACI94139; ACI94139; OCAR_7031. DR EnsemblBacteria; AEI05781; AEI05781; OCA5_c10620. DR GeneID; 10846194; -. DR GeneID; 6992511; -. DR KEGG; oca:OCAR_7031; -. DR KEGG; ocg:OCA5_c10620; -. DR PATRIC; 22807861; VBIOliCar134280_2878. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; OCAR504832:GJPZ-1062-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 202 AA; 21831 MW; CBB85739686CB2EA CRC64; MPYPDRFYPV VDSVAWLARL AKLGVGTVQL RTKELDDPQA STLVRDALAA VAGTQTKLVV NDYWRAAIDH GAQHLHLGQE DLVDADLAAI RKAGLTLGIS THDEEELAIA LKARPDYIAL GPIFFTTLKA MRFKPQGIPR ITEWKRAIGT IPLVAIGGIK LEHAADVFAA GADSIAVVSD VTQNADPDAR VRAWLDATME TA // ID B6JJ24_OLICO Unreviewed; 229 AA. AC B6JJ24; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE SubName: Full=Thiamine monophosphate synthase; DE SubName: Full=Thiamine-phosphate pyrophosphorylase ThiE; DE EC=2.5.1.3; GN Name=thiE1; OrderedLocusNames=OCA5_c08030, OCAR_7314; OS Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Oligotropha. OX NCBI_TaxID=504832; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49405 / DSM 1227 / OM5 [Mississippi], and OM5; RX PubMed=18539730; DOI=10.1128/JB.00614-08; RA Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.; RT "Genome sequence of the chemolithoautotrophic bacterium Oligotropha RT carboxidovorans OM5T."; RL J. Bacteriol. 190:5531-5532(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49405 / DSM 1227 / OM5, and OM5; RX PubMed=21742883; DOI=10.1128/JB.05619-11; RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., RA Meyer O.; RT "Complete genome sequences of the chemolithoautotrophic Oligotropha RT carboxidovorans strains OM4 and OM5."; RL J. Bacteriol. 193:5043-5043(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001196; ACI94418.1; -; Genomic_DNA. DR EMBL; CP002826; AEI05525.1; -; Genomic_DNA. DR RefSeq; YP_002290283.1; NC_011386.1. DR RefSeq; YP_004631766.1; NC_015684.1. DR STRING; 504832.OCAR_7314; -. DR EnsemblBacteria; ACI94418; ACI94418; OCAR_7314. DR EnsemblBacteria; AEI05525; AEI05525; OCA5_c08030. DR GeneID; 10845935; -. DR GeneID; 6992791; -. DR KEGG; oca:OCAR_7314; -. DR KEGG; ocg:OCA5_c08030; -. DR PATRIC; 22808419; VBIOliCar134280_3154. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; OCAR504832:GJPZ-803-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 229 AA; 24231 MW; ED734198A12E5A38 CRC64; MAPSRSSAPA QPMPRLYLAT PALDDTAAFA ASLPPLLTAC DVAAVLLRLN EADERTLTSR IKTLAGPVQA AGTALLVEGR QSLAVRGGAD GVHVEGLEQM EDAASLKAQR IVGVGQLHTR HDAMLAGERG ADYLLFGEPS RNGERPSPEA IFERLQWWAE LFEPPCVGYA ATLEEATLFA GSGADFIMAA DFIWNDARGP KAALEEAQAA IRARFEATFS AAAGQVTRS // ID B6JVH0_SCHJY Unreviewed; 515 AA. AC B6JVH0; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 19-MAR-2014, entry version 24. DE SubName: Full=Thiamine-phosphate dipyrophosphorylase/hydroxyethylthiazole kinase; GN ORFNames=SJAG_00381; OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission OS yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=402676; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=yFS275 / FY16936; RX PubMed=21511999; DOI=10.1126/science.1203357; RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., RA Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., RA Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., RA FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., RA Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., RA Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., RA Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., RA Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., RA Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.; RT "Comparative functional genomics of the fission yeasts."; RL Science 332:930-936(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KE651166; EEB05371.1; -; Genomic_DNA. DR RefSeq; XP_002171664.1; XM_002171628.1. DR ProteinModelPortal; B6JVH0; -. DR EnsemblFungi; EEB05371; EEB05371; SJAG_00381. DR GeneID; 7049527; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 515 AA; 55160 MW; 3FB0DE4868D3A586 CRC64; MKPTVDYSLY LVTSSVIVPT GSTLEQQVEQ AILGGVTLVQ LREKNVSTKL FIERAEKVLQ VCRKHNVPLL INDRVDVALA VGAEGVHIGQ SDMDCATARR ILGSDAVIGV TANNIQEIDK AEADGADYVG LGSVYDTATK NVKDRIIGIH GLRDLLEHIS NMKRRLQTVA IAGLNASNVQ RVIYLSEVNG VRVDGIALVS AIMASTEPKK AAEKLIQLIK TTPKFALPVS KLPKSDSTAF VSSIERVFSR AKSKTPLVQQ LTNNVSKNFN ANVTLAVGGS PLMCEFDDEF PELARANGAL LCNYAAVDKL ESYIFAAQCN NAENKPVILD PVGAGATEVR KRALTTMLDS AYFDYIKGNE GEILTLAGVE VQMRGVDSTS EFPLTEKVRV TKLLAEKRRC VVIMTGAVDV ISDGNRTFVV KRGHPMLANI TASGCAMGAV LCVAAALCPE DRLVAALAAT LLFSIAGERA ASVSDCGPGS FIPHFVDELY SITNDCTART FKVADNDNGV EEIVA // ID B6Q988_PENMQ Unreviewed; 522 AA. AC B6Q988; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 16-APR-2014, entry version 25. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative; GN ORFNames=PMAA_071270; OS Penicillium marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces. OX NCBI_TaxID=441960; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333; RA Fedorova N.D., Joardar V.S., Maiti R., Schobel S., Amedeo P., RA Galens K., Inman J.M., White O.R., Whitty B.R., Wortman J.R., RA Nierman W.C.; RT "The genome sequence of Penicillium marneffei strain ATCC 18224."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995900; EEA26042.1; -; Genomic_DNA. DR RefSeq; XP_002146589.1; XM_002146553.1. DR ProteinModelPortal; B6Q988; -. DR GeneID; 7024260; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 522 AA; 54992 MW; E71C0FBFF1FCCA4C CRC64; MTLDLSLYLV TDSTPAILGS RDIFKVVEEA CKGGVTIVQY RDKTSDTGAL VETATRLHDI TKRYNVPLII NDRVDVAIAS GAEGVHLGQD DMSITAAKKI LSKDAIVGIS ASTVEEAVKA VEEGADYLGI GTLFATATKT NTKNIIGTEG VKTILDSISR LDRSVGTVGI GGINLSNVQR VLYQSAATNK ALGGVAVVSA IMAADDPKSV AEQFRNAIAT PPVFVTRSPD ESSAAVDVNA LAAAVPEVVQ KVVKFHPIVH SMINFVVANF VANVAISAGL SPIMSQYGDE AKDLAVHKGG LVINMGTLTS ASIGEYLKAV KAYNSNGNPV VLDPVGAGAT AIRRDAVKTL MAGGYFDLIK GNEREITQIY GNTHNLTQRG VDSGPSALND VEKATLARDL ARRERNIVLL TGKIDYLSDG NRVIAVKNGH ELLSKATGTG CAIGTVCSAY LAAYRENKFL AVLAGLLMYE IAAENAAAKD TVHGPGTFLP AFLDEIHSIW QKASDGDLAW AQGRAKIEEV QL // ID B6R116_9RHOB Unreviewed; 200 AA. AC B6R116; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 16-OCT-2013, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_1; ORFNames=PJE062_5088; OS Pseudovibrio sp. JE062. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudovibrio. OX NCBI_TaxID=439495; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JE062; RA Hill R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS996806; EEA96049.1; -; Genomic_DNA. DR ProteinModelPortal; B6R116; -. DR EnsemblBacteria; EEA96049; EEA96049; PJE062_5088. DR PATRIC; 25634857; VBIPseSp14949_1507. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 200 AA; 22535 MW; D599D6377822FD13 CRC64; MLDRFYLIID GTQWLPRVLP LGVKFCQLRI KDKSEDEIRS QVREAKQLCD KAGAVLVVND HWQAAYDANV GYVHLGQEDL KTADFRALRS AGIYYGISTH YEAELDTALA LDPEYVALGP IYNSTSKEMH WQPQGLETLK KWRERTNNHL VAIGGITLER ASDVFSAGAD SIATISDVTT ATNPEHRTAQ WLDASKSWQR // ID B6R262_9RHOB Unreviewed; 210 AA. AC B6R262; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_2; Synonyms=thiE; ORFNames=PJE062_2616; OS Pseudovibrio sp. JE062. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudovibrio. OX NCBI_TaxID=439495; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JE062; RA Hill R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS996807; EEA95048.1; -; Genomic_DNA. DR ProteinModelPortal; B6R262; -. DR EnsemblBacteria; EEA95048; EEA95048; PJE062_2616. DR PATRIC; 25635228; VBIPseSp14949_1691. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 21518 MW; 39BB77DD7BFF967C CRC64; MLDLSVYLVL GPQDCPGQDP VNIAVAAAQN GATVVQLRDK TGSTKEQIEL AERLMQALKP LNVPLIVNDR VDVALAVDAD GVHVGQDDMN ATKARELIGA DKLLGLSVST QDELDAADIA ACDYLGIGAC FPTNSKDDAA DVGMQNFAGL TAQSQLPVVG IGGISLANAD QVIKAGADGV AVISAICGAP SAAEATRKLQ EIVKSVKDLG // ID B6R2B5_9RHOB Unreviewed; 197 AA. AC B6R2B5; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_3; Synonyms=thiE; ORFNames=PJE062_2761; OS Pseudovibrio sp. JE062. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudovibrio. OX NCBI_TaxID=439495; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JE062; RA Hill R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS996807; EEA95192.1; -; Genomic_DNA. DR ProteinModelPortal; B6R2B5; -. DR EnsemblBacteria; EEA95192; EEA95192; PJE062_2761. DR PATRIC; 25635842; VBIPseSp14949_1988. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 26 30 HMP-PP binding (By similarity). FT REGION 175 176 THZ-P binding (By similarity). FT METAL 59 59 Magnesium (By similarity). FT METAL 78 78 Magnesium (By similarity). FT BINDING 58 58 HMP-PP (By similarity). FT BINDING 97 97 HMP-PP (By similarity). FT BINDING 126 126 HMP-PP (By similarity). FT BINDING 155 155 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 197 AA; 22099 MW; 399C65346FF2DE97 CRC64; MERFYLITGD VDWIEKLVPH GVKLVQLRIK DQPEAEVRRQ VIKAQDFCKA HGTQLIINDY WELALELGCD FIHLGQEDMD TADFAALRRA SVRFGLSTHD EAELDRALSH EPEYVALGPV YPTKLKKMKW APQGLDRVHR WKQMVGGTPL VAIGGLTPER LAGVFEAGAD SAAVVTDILQ APDPVSRAQE WVEACRL // ID B6R793_9RHOB Unreviewed; 213 AA. AC B6R793; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=PJE062_2332; OS Pseudovibrio sp. JE062. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudovibrio. OX NCBI_TaxID=439495; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JE062; RA Hill R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS996812; EEA93182.1; -; Genomic_DNA. DR ProteinModelPortal; B6R793; -. DR EnsemblBacteria; EEA93182; EEA93182; PJE062_2332. DR PATRIC; 25640027; VBIPseSp14949_4059. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 213 AA; 23122 MW; 5C4B4922AE49B3C4 CRC64; MHPRLYLVTP PTFDLHEFEG QLKQALEGGD IASLLISMPD ANEGELQAAA KRLVPQAQAN EVAVLIENNT QIMGRSGADG LHVSGTDKDL EDVMQSFPED RIIGHAGVKT RHDAMVIASM GVDYMFFGLL SLKQEEEPHR KSLDYGSWWS EVFETPCVVL AGTSVSSVDT VAQTGAEFVA VREAVWNHPE GPKAAVEQAN AILATHTLAE VED // ID B6TMJ4_MAIZE Unreviewed; 551 AA. AC B6TMJ4; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 19-MAR-2014, entry version 27. DE SubName: Full=Phosphomethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4; RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., RA Tatarinova T.V., Zhang H., Swaller T.J., Lu Y.-P., Bouck J., RA Flavell R.B., Feldmann K.A.; RT "Insights into corn genes derived from large-scale cDNA sequencing."; RL Plant Mol. Biol. 69:179-194(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EU966209; ACG38327.1; -; mRNA. DR ProteinModelPortal; B6TMJ4; -. DR PRIDE; B6TMJ4; -. DR Gramene; B6TMJ4; -. DR HOGENOM; HOG000155781; -. DR OMA; PIVWTIA; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 2: Evidence at transcript level; KW Kinase; Transferase. SQ SEQUENCE 551 AA; 58004 MW; 87934A95A5075B79 CRC64; MTSVPLPPLS AALAQYRPSA AATLRFRTPS SAPGVSASSS TRARRFSVIA SAREMPWPHV LTVAGSDSSA GAGIQADIKA CAALGAYCSS VITAVTAQNT VGVQGIHAVP EKFVGEQLRS VLSDMSVDVV KTGMLPSAGV VKVLCESLRK FPVKALVVDP VMVSTSGDTL SGPSTLATYR DELFSMADIV TPNVKEASKL LGDVSLHTIS DMCNAAESIY KLGPKYVLVK GGDMPDSSDA IDVLFDGKEF TELRGLRIKT RNTHGTGCTL ASCIAAELAK GATMLHAVQA AKKFVESALY HSKDLVIGNG PQGPFDHHFE LKSPSYKMGS LQKFNPDDLF LYAVTDSGMN KKWGRSIKDA VKAAIEGGAT IVQLREKDAE TREFLEAAKA CVEICKSSGV PLLINDRVDV ALACDADGVH VGQSDMPAWE VRRLLGPGKI IGVSCKTPAQ AEQAWKDGAD YIGCGGVFPT TTKANNPTLG FEGLRTVCLA SKLPVVAIGG INAGNAGSVM ELGLPNLKGV AVVSALFDRE RVAAETRNLR SILMKNAYSR S // ID B6VYW0_9BACE Unreviewed; 202 AA. AC B6VYW0; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=BACDOR_02474; OS Bacteroides dorei DSM 17855. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=483217; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17855; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides dorei (DSM 17855)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17855; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWZ01000050; EEB25014.1; -; Genomic_DNA. DR ProteinModelPortal; B6VYW0; -. DR EnsemblBacteria; EEB25014; EEB25014; BACDOR_02474. DR PATRIC; 26998199; VBIBacDor28639_2159. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 22884 MW; 8737ADB47025626C CRC64; MKLILITPPT YFVEEDKIIT ALFEEGLDTL HLRKPGTAPM FAERLLTLIP EQYHKRIVVH GHFYLKEEYK LKGIHLNGRN PNLPEGYKGH VSCSCHSLDE VKEHKSGCDY VFLSPVFNSI SKLNYNSAYT AEELRAAAKA SIIDKKVIAL GGIDEENLLE VKDFGFGGAA ILGALWNKFD ACTDRDYRCV IEHFRKLRDL AD // ID B6VYX0_9BACE Unreviewed; 208 AA. AC B6VYX0; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACDOR_02484; OS Bacteroides dorei DSM 17855. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=483217; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17855; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides dorei (DSM 17855)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17855; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWZ01000050; EEB25024.1; -; Genomic_DNA. DR ProteinModelPortal; B6VYX0; -. DR EnsemblBacteria; EEB25024; EEB25024; BACDOR_02484. DR PATRIC; 26998215; VBIBacDor28639_2167. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 23084 MW; 95FB29E0B14F5B32 CRC64; MEDKTVELQF ITHFTDTYSY YDSARMALEG GCRWIQLRMK DTSVDEVERE AIRLQGLCKD YGATFIIDDH VELVNKIHAD GVHLGKKDMP VAEARKILGK EFIIGGTANT FDDVKMHYEA GADYIGCGPF RFTTTKKALS PVLGLEGYRS IIQQMNEADI HLPIVAIGGI TLEDIPSIME TGITGIALSG TILRAKDPVA ETKRIMNL // ID B6W721_9FIRM Unreviewed; 203 AA. AC B6W721; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ANHYDRO_00377; OS Anaerococcus hydrogenalis DSM 7454. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Anaerococcus. OX NCBI_TaxID=561177; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 7454; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 7454; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Anaerococcus hydrogenalis (DSM 7454)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXA01000010; EEB36776.1; -; Genomic_DNA. DR ProteinModelPortal; B6W721; -. DR EnsemblBacteria; EEB36776; EEB36776; ANHYDRO_00377. DR PATRIC; 24474680; VBIAnaHyd88381_0344. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 22651 MW; 54336B7C9F90B48A CRC64; MKKLYLVTNS DKYTEEEFLK RIEDAIKGGV DILQLREKEK TDLEILNLGK KVKKICDEYN IPMLIDDKPH LAWALGCGLH VGADDMPISL CRKLLGKDTL IGATAKSVEA AKKAQEDGAN YLGVGAIFET KTHVKTKRTS VETFKKIKEA VDIYVYAIGG LNIENVDILK DSKADGICVV RAIMDAEDVY QTSFDLKEKI QKL // ID B6WXK7_9DELT Unreviewed; 213 AA. AC B6WXK7; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DESPIG_02834; OS Desulfovibrio piger ATCC 29098. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=411464; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29098; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Desulvovibrio piger (ATCC 29098)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29098; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXU01000083; EEB32215.1; -; Genomic_DNA. DR ProteinModelPortal; B6WXK7; -. DR EnsemblBacteria; EEB32215; EEB32215; DESPIG_02834. DR PATRIC; 27363211; VBIDesPig88804_2257. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22698 MW; 3FB8C2A31BB1C656 CRC64; MPVILPGQTD IYALTDARLS CGRTLETVVS ALLGAGVKII QYREKHMKSG EMLEECRLMR RLTREAGACF IVDDHVDLAI LAEADGVHIG QEDFPLPAVR QLVGPDMCIG LSTHSPEQAK AAVAVGADYI GVGPIFATKT KEDVVAPVGF DYLDWVAANI TIPFVAIGGI KEHNIADVAR HGARCCALVS ELVGALDIVA KVQAVRAAMH QGM // ID B6X9S4_9ENTR Unreviewed; 225 AA. AC B6X9S4; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PROVALCAL_00069; OS Providencia alcalifaciens DSM 30120. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Providencia. OX NCBI_TaxID=520999; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 30120; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Providencia alcalifaciens (DSM 30120)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 30120; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXW01000003; EEB47854.1; -; Genomic_DNA. DR ProteinModelPortal; B6X9S4; -. DR EnsemblBacteria; EEB47854; EEB47854; PROVALCAL_00069. DR PATRIC; 26403420; VBIProAlc107602_0071. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 24743 MW; 26A39D3DAB7A5CFD CRC64; MNKTLKLPKS PFPQTEHRLG LYPVVDSVEW IERLLNAGVS TLQLRIKDKQ DSEVHEQIQR AIALGKQHNA RLFINDYWRL AVELGAYGVH LGQEDLDTTD LIAIHQAGLR LGISTHDPDE VAIAKSIRPS YIALGHIFPT QTKQMPSTPQ GLEALKRMVI ATPEFPTVAI GGISIERVPA VLDTGVGSIA VVSAITQAED WQAATQTLLD LIEPASRLKD NDHAQ // ID B6XU84_9BIFI Unreviewed; 871 AA. AC B6XU84; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; ORFNames=BIFCAT_00839; OS Bifidobacterium catenulatum DSM 16992 = JCM 1194 = LMG 11043. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=566552; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16992; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bifidobacterium catenulatum (DSM 16992)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16992; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXY01000011; EEB21870.1; -; Genomic_DNA. DR ProteinModelPortal; B6XU84; -. DR EnsemblBacteria; EEB21870; EEB21870; BIFCAT_00839. DR PATRIC; 27206505; VBIBifCat131822_0722. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 871 AA; 96096 MW; 83214E07B94A89A2 CRC64; MRDSFDLSAY LVVGPQDCKG RPITDVVDDA LRGGASFIQL RAKDADAKDL TDMARDIAQI IEDNNKSDSV AFVIDDRVDV VWQARSKGIK VDGVHIGQTD MEPREARALL GEDAIVGLSA ETESLVKLIN ELPDGCIDYI GAAPLHVSVT KPEASVGGND GSGRTLDEEQ INTICSASGF PVVVGGGVTA DDMEMLAHSK AAGWFVVSAI AGADDPEAAT RNMVARWKAV RSDAKHGYAP RMKAQKTAEI NPDNTADGAS GEKKFTNAKE AKAASKLAKQ QRVDIAARDS KQRDKAHIRK TTPVHFENEF GSYDLQVPYT EIKLSDTPGV GPNAPFKDYN TEGPKCDPKE GLAPLRLDWI LDRGDVEEYE GRRRNLEDDG KRAIKRGKAS KEWRGRQHKP MKAKDHPVTQ MWYARHNIIT PEMRYVAERE HCSVELVRSE LAAGRAVMPC NINHPEAEPM IIGSKFLTKL NANMGNSAVT SSIDEEVEKL TWATKWGADT VMDLSTGNDI HTTREWILRN SPVPIGTVPM YQALEKVEDD ASKLSWELFR DTVIEQCEQG VDYMTIHAGV LLRFVPLTAN RMTGIVSRGG SIMAEWCLQH HQESFLYTHF DELCEIFAKY DVAFSLGDGL RPGSLADAND AAQFAELMTL GELTQRAWEH DVQVMIEGPG HIPFDTVRMN IEMEKAICKD APFYTLGPLT TDTAPGYDHI TSAIGGVEIA RYGTAMLCYV TPKEHLGLPN KDDVKQGVIA YKIACHAADI AKHHPHAIDR DNAMSKARFE FRWLDQFNLS YDPDTAIAFH DDTLPAEPAK MAHFCSMCGP KFCSMAISQN IRKKFGNAEA QEKLVADAQT IAAGMQAMSE RFREQGGHLY Q // ID B6XUK1_9BIFI Unreviewed; 242 AA. AC B6XUK1; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BIFCAT_00415; OS Bifidobacterium catenulatum DSM 16992 = JCM 1194 = LMG 11043. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=566552; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16992; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bifidobacterium catenulatum (DSM 16992)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16992; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXY01000011; EEB21459.1; -; Genomic_DNA. DR ProteinModelPortal; B6XUK1; -. DR EnsemblBacteria; EEB21459; EEB21459; BIFCAT_00415. DR PATRIC; 27205731; VBIBifCat131822_0346. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 207 208 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 187 187 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 242 AA; 25667 MW; 27B66D1CC3E82C8C CRC64; MRDTFDMSAY FVVGPQDCKG RPITSVVEDA LRGGATFIQL RAKDTDAKDI TSMARDIAQV IEHNSKSDSV AFVIDDRVDV VWQARHKGIK VDGVHIGQTD LEPQEARALL GEDAIVGLSA ETESLVKLIN ELPAGCIDYI GAGPLHVSIT KPEASVGGND GSGHTLDEAQ INAICDASDF PVVVGGGVSA DDMEMLAHSK AAGWFVVSAI AGASDPEEAT RNMVSRWKAV RGDAKHGHVP HK // ID B6YS05_AZOPC Unreviewed; 210 AA. AC B6YS05; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CFPG_714; OS Azobacteroides pseudotrichonymphae genomovar. CFP2. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Candidatus Azobacteroides. OX NCBI_TaxID=511995; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=19008447; DOI=10.1126/science.1165578; RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., RA Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.; RT "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT RT protist cells in termite gut."; RL Science 322:1108-1109(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010656; BAG83977.1; -; Genomic_DNA. DR RefSeq; YP_002309388.1; NC_011565.1. DR ProteinModelPortal; B6YS05; -. DR STRING; 511995.CFPG_714; -. DR EnsemblBacteria; BAG83977; BAG83977; CFPG_714. DR GeneID; 7039155; -. DR KEGG; aps:CFPG_714; -. DR PATRIC; 31963464; VBICanAzo57536_1085. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CAZO511995:GKF1-752-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23635 MW; DF3C8CE60DB04A36 CRC64; MKKKIPQGLY AITAENFSKK NNVEIVKELL DSGIRIIQYR EKKKTKFEKL KQCETIRQLT LSYNCFFIVN DDIDIAMSVH SDGIHLGQDD LPLLKARIIV GQDMAIGIST HNPEQANKAT INGADYIGVG PIFQTFTKEN MIDAVGLEYL EYCVIHIKIP KVAIGGIKLS NLSRVAKFKP ENICMVTEIV GSKNIVETIN KAKKIINDYY // ID B6ZNN9_ECO57 Unreviewed; 211 AA. AC B6ZNN9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ESCCO14588_0873; OS Escherichia coli O157:H7 str. TW14588. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=502346; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TW14588; RA Sebastian Y., Whittam T.S., Manning S.D., Sutton G.; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABKY02000001; EEC28995.1; -; Genomic_DNA. DR ProteinModelPortal; B6ZNN9; -. DR SMR; B6ZNN9; 10-209. DR EnsemblBacteria; EEC28995; EEC28995; ESCCO14588_0873. DR PATRIC; 29400585; VBIEscCol82497_1678. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B7AB38_THEAQ Unreviewed; 206 AA. AC B7AB38; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TaqDRAFT_3299; OS Thermus aquaticus Y51MC23. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=498848; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y51MC23; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Saunders E., Tapia R., Green L., Rogers Y., Detter J.C., RA Brettin T.S., Mead D.; RT "Sequencing of the draft genome and assembly of Thermus aquaticus RT Y51MC23."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVK02000012; EED09305.1; -; Genomic_DNA. DR ProteinModelPortal; B7AB38; -. DR EnsemblBacteria; EED09305; EED09305; TaqDRAFT_3299. DR PATRIC; 25943445; VBITheAqu66851_2094. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22536 MW; 16CDE7D65A51429F CRC64; MQGRLYLVVT PRPGWSFAET LDRTERALAG GVEVLQLRAK DWEARPILEL GERMRALAER YGVPFFLNDR PDLAALLGAD GVHLGQNDLT PPEARRFFGG MVGRSTHAPE QALRALEEGA DYLSVGPVWE TPTKPGRPAA GLGYVRWAAE NLGNRPWFAI GGIDLANLDQ VLEAGARRIV VVRAILDAPD PEGAARAFRE RLYGVA // ID B7AJM6_9BACE Unreviewed; 206 AA. AC B7AJM6; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=BACEGG_02624; OS Bacteroides eggerthii DSM 20697. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=483216; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20697; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides eggerthii (DSM 20697)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20697; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVO01000041; EEC53058.1; -; Genomic_DNA. DR ProteinModelPortal; B7AJM6; -. DR EnsemblBacteria; EEC53058; EEC53058; BACEGG_02624. DR PATRIC; 27007622; VBIBacEgg69811_2211. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22675 MW; DF8DF86EFB7F1CAF CRC64; MAEKIYPNCM KLIVITQPEF FEDEAAAITS LFDAGLEILH LRKPGASYED MDKLLRRLPA EYMERIVTHD HFGLASERNL KGVHLNGRNP AAPAGFTGHV SRSCHSLEEV AEYKAACNYV FLSPIYNSIS KEGYAAAYAF DDLQKAHQAG IIDSGVMALG GVTAEHLPEI NSLGFGGVGL LGDIWQRTGT DFINHFRELL RSASVF // ID B7AJN1_9BACE Unreviewed; 212 AA. AC B7AJN1; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACEGG_02629; OS Bacteroides eggerthii DSM 20697. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=483216; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20697; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides eggerthii (DSM 20697)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20697; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVO01000041; EEC53063.1; -; Genomic_DNA. DR ProteinModelPortal; B7AJN1; -. DR EnsemblBacteria; EEC53063; EEC53063; BACEGG_02629. DR PATRIC; 27007632; VBIBacEgg69811_2216. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23642 MW; 24B28164D4FFAFE7 CRC64; MKTVQFITHY TEKYSYLDSA RMALKGGCRW IQLRMKDAGK EEIVSVAMEL RNLCNDCGAI FIIDDHVELV REIGADGVHL GKNDMSVAEA RRILGDEYII GGTANTYEDV KKHWLDGVNY IGCGPFRYTT TKQKLSPILG LEGYKEIIRK MQEEKICHLP VVAIGGITFA DIPAIMQTGV TGIALSGTVL RADNPVEEMR KILAVINQTD NY // ID B7ANA9_9FIRM Unreviewed; 196 AA. AC B7ANA9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=BACPEC_00162; OS [Bacteroides] pectinophilus ATCC 43243. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=483218; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43243; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides pectinophilus (ATCC 43243)."; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43243; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVQ01000031; EEC58820.1; -; Genomic_DNA. DR ProteinModelPortal; B7ANA9; -. DR EnsemblBacteria; EEC58820; EEC58820; BACPEC_00162. DR PATRIC; 27053435; VBIBacPec49690_2927. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 21781 MW; F698B0BAD38A4158 CRC64; MEELIMSDVV AVTNRHLCVR DYFEQIEVVA SSGVNKIIVR EKDLAPQEYK ELFVRVRDIC SVHKVKAIPH YFWREAAQCG SGAIHLPLDV LGECYDKQEF RQCRFDTIGT SVHSAEQALE ACRFGASYVT AGHVFATDCK KGLTPRGLDF LKNICSICVP KGVQVYAIGG ISPDNYRSAL DAGASAVCMM SHMMRL // ID B7AR00_9FIRM Unreviewed; 206 AA. AC B7AR00; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACPEC_01110; OS [Bacteroides] pectinophilus ATCC 43243. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=483218; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43243; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides pectinophilus (ATCC 43243)."; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43243; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVQ01000035; EEC58122.1; -; Genomic_DNA. DR ProteinModelPortal; B7AR00; -. DR EnsemblBacteria; EEC58122; EEC58122; BACPEC_01110. DR PATRIC; 27052313; VBIBacPec49690_2370. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 31 35 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22163 MW; 6D6BFBD4FD003E34 CRC64; MHGRILYLIA DLYDGDERVR SALDAGVDYV QLREKNITSA KYLQDALHMR HLVDEYNAKN KTDTKLIIND RLDIAVLSKA DGVHLGADDV PVGMAREFLG RDFIIGATAK TVEQAVAAQN AGADYLGTGA FHLTATKPDA KAITPELYKQ ILDAVSIPDV AIGGITVDNC NLPLECGADG LAVSAGILKM GDAGENVRLF RKKLLT // ID B7B8U4_9PORP Unreviewed; 199 AA. AC B7B8U4; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=PRABACTJOHN_01446; OS Parabacteroides johnsonii DSM 18315. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=537006; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18315; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Parabacteroides johnsonii (DSM 18315)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18315; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYH01000133; EEC97148.1; -; Genomic_DNA. DR ProteinModelPortal; B7B8U4; -. DR EnsemblBacteria; EEC97148; EEC97148; PRABACTJOHN_01446. DR PATRIC; 25864551; VBIParJoh38674_1207. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 22221 MW; 67BDD970C6CFCA5C CRC64; MKKLIVITSP RFFQGEDTVL SHLFDEGMQR LHLRKPDSEA NELRKLLDRI PAIYYPKIVL HDCFGLAVEY GLGGVHLNRR NNQIPDGFTG TISRSCHSIG ELEQFGELDY LFLSPIFQSI SKEGYGNGFE PETLRQASDT GTINDKVIAL GGIDQTTLPL LSPFRFGGAA VLGALWGNHP SVDKEDSIIT QYKKLQAWN // ID B7B8U5_9PORP Unreviewed; 245 AA. AC B7B8U5; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PRABACTJOHN_01447; OS Parabacteroides johnsonii DSM 18315. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=537006; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18315; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Parabacteroides johnsonii (DSM 18315)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18315; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYH01000133; EEC97149.1; -; Genomic_DNA. DR ProteinModelPortal; B7B8U5; -. DR EnsemblBacteria; EEC97149; EEC97149; PRABACTJOHN_01447. DR PATRIC; 25864553; VBIParJoh38674_1208. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 53 57 HMP-PP binding (By similarity). FT REGION 155 157 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 HMP-PP (By similarity). FT BINDING 191 191 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 245 AA; 27595 MW; AC07594F19E09733 CRC64; MELDDFLYTS AGRGRYACFT GTNRLMFITH RTDKYTELDE VKMVTKGGCT WVQLRMKENL NLEVAKAVAH FTMFDCDTDC ACCLDDDLEM AFKAGIHCVH LGKNDMPVSE AWRRIIEKGK EDLFLVGATA NTFEDILKAD REGASYIGLG PYRYTETKKN LSPVLGLEGY RKIMEQCREA GLEIPIFAIG GIEFEDIAPL METGIEGIAV SGAIINAEDP VEETRRFIRE INKHKPDPCR DDSEI // ID B7CB04_9FIRM Unreviewed; 209 AA. AC B7CB04; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUBIFOR_01375; OS Eubacterium biforme DSM 3989. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=518637; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3989; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3989; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Eubacterium biforme (DSM 3989)."; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYT01000074; EEC90068.1; -; Genomic_DNA. DR ProteinModelPortal; B7CB04; -. DR EnsemblBacteria; EEC90068; EEC90068; EUBIFOR_01375. DR PATRIC; 30658570; VBIEubBif128737_1059. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22464 MW; 8A9FCC203BC2BC18 CRC64; MKKVDYTLYF ITNSDGMDEE TFLNKVKGAC LGGATIIQLR EKNKSTLDYY ELALKVKNIT DAYNIPLIID DRIDIAMAVG CGVHLGNEDM PISVARKIMG KDCIIGATAK TVEVAKNAEA DGADYLGCGA IYPTKTHVKT KITSVETLND ICSSVNIPVC AIGGLNKDNL SVLEKSPIQG VCVVSAIMDA DDTKKAAEEL KKSIQKIVA // ID B7CHB0_BURPE Unreviewed; 212 AA. AC B7CHB0; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-MAR-2014, entry version 23. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=BUC_5862; OS Burkholderia pseudomallei 576. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=557724; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=576; RA Brinkac L.M., Harkins D.M., Shrivastava S., Durkin A.S., Sutton G.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCE01000001; EEC38378.1; -; Genomic_DNA. DR EnsemblBacteria; EEC38378; EEC38378; BUC_5862. DR PATRIC; 27879305; VBIBurPse132396_0186. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 212 AA; 22833 MW; B699124FCBE673DC CRC64; MIESIIHRHL KIIVNKSANL PSEYLITPEP PGDEALSDYL ATLERTLKAG ISLVQLRAKA VTAPYYARLT EYALACCRRY NAQLLVNAAP EVALGLHTDG VHLTSTRLMT CSTRPLPAGL LVSAACHDED QVRHADSIGV DLITISPVMP TATHTTAEPL GWPRFRELAT LTSVPVYALG GMSVDSLAEA RNAGAYGIAA IRAFWGSNVD RS // ID B7CR99_BURPE Unreviewed; 209 AA. AC B7CR99; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-MAR-2014, entry version 25. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BUC_6709; OS Burkholderia pseudomallei 576. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=557724; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=576; RA Brinkac L.M., Harkins D.M., Shrivastava S., Durkin A.S., Sutton G.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCE01000005; EEC34621.1; -; Genomic_DNA. DR ProteinModelPortal; B7CR99; -. DR EnsemblBacteria; EEC34621; EEC34621; BUC_6709. DR PATRIC; 27886736; VBIBurPse132396_3873. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID B7CXU6_BURPE Unreviewed; 367 AA. AC B7CXU6; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-MAR-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BUC_3977; OS Burkholderia pseudomallei 576. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=557724; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=576; RA Brinkac L.M., Harkins D.M., Shrivastava S., Durkin A.S., Sutton G.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCE01000011; EEC32148.1; -; Genomic_DNA. DR ProteinModelPortal; B7CXU6; -. DR EnsemblBacteria; EEC32148; EEC32148; BUC_3977. DR PATRIC; 27890979; VBIBurPse132396_5973. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 367 AA; 38273 MW; 8C82851C6E850E63 CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGAQAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEVE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID B7DN59_9BACL Unreviewed; 209 AA. AC B7DN59; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AaLAA1DRAFT_0434; OS Alicyclobacillus acidocaldarius LAA1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=543302; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LAA1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Mead D.; RT "Sequencing of the draft genome and assembly of Alicyclobacillus RT acidocaldarius LAA1."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCS01000003; EED08403.1; -; Genomic_DNA. DR ProteinModelPortal; B7DN59; -. DR EnsemblBacteria; EED08403; EED08403; AaLAA1DRAFT_0434. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21936 MW; BBC9B1BCD131DCA2 CRC64; MARRDWIEKL RVYLVTDDRP DHEEVAAIVE QALAGGVTCV QLRRKHEDGG PMLRLALRLR ELASAHDALF IVNDRLDIAL LSGADGVHVG QTDLPASLVK SRFPELLVGV SARSVDEAVR AEVDGADYLG VGSVYPTATK GDAVLTGLET LAACRRAVRI PIVGIGGITV ERASEVMAAG ASGVAVVSAI MSAPDPKAAA TAFAERTSS // ID B7DVC7_9BACL Unreviewed; 230 AA. AC B7DVC7; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AaLAA1DRAFT_2952; OS Alicyclobacillus acidocaldarius LAA1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=543302; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LAA1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Mead D.; RT "Sequencing of the draft genome and assembly of Alicyclobacillus RT acidocaldarius LAA1."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCS01000047; EED05924.1; -; Genomic_DNA. DR ProteinModelPortal; B7DVC7; -. DR EnsemblBacteria; EED05924; EED05924; AaLAA1DRAFT_2952. DR PATRIC; 24437012; VBIAliAci16525_2952. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 23744 MW; FA601D4EDAFF3888 CRC64; MTHVLHVLSD RTRGATVPLE EALWLAALGG ADVIQIREKK APALAVFEFT RSLIARMREA GASSQVFVND RLDVAMAAGA DGVHLAAKSL PVAAAREVVH RAGVGLVVGC SVHSLDEALA AEAAGADYVT FGHIFPTASH PGLPPRGVRE LAQVVEALSI PVVAIGGIDA ANVGEVLATG ASGVAVISAV VEAADPRAAV ARLKEAMARS HVSPKVPFPI SERGMRRARL // ID B7ER32_ORYSJ Unreviewed; 388 AA. AC B7ER32; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 16-APR-2014, entry version 33. DE SubName: Full=Thiamin biosynthesis protein, putative, expressed; DE SubName: Full=cDNA clone:J023133M06, full insert sequence; DE SubName: Full=cDNA clone:J033123K02, full insert sequence; GN OrderedLocusNames=LOC_Os12g09000; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE. RA Kikuchi S., Satoh K., Nagata T., Kawagashira N., Doi K., Kishimoto N., RA Yazaki J., Ishikawa M., Yamada H., Ooka H., Hotta I., Kojima K., RA Namiki T., Ohneda E., Yahagi W., Suzuki K., Li C., Ohtsuki K., RA Shishiki T., Otomo Y., Murakami K., Iida Y., Sugano S., Fujimura T., RA Suzuki Y., Tsunoda Y., Kurosaki T., Kodama T., Masuda H., RA Kobayashi M., Xie Q., Lu M., Narikawa R., Sugiyama A., Mizuno K., RA Yokomizo S., Niikura J., Ikeda R., Ishibiki J., Kawamata M., RA Yoshimura A., Miura J., Kusumegi T., Oka M., Ryu R., Ueda M., RA Matsubara K., Kawai J., Carninci P., Adachi J., Aizawa K., Arakawa T., RA Fukuda S., Hara A., Hashidume W., Hayatsu N., Imotani K., Ishii Y., RA Itoh M., Kagawa I., Kondo S., Konno H., Miyazaki A., Osato N., Ota Y., RA Saito R., Sasaki D., Sato K., Shibata K., Shinagawa A., Shiraki T., RA Yoshino M., Hayashizaki Y.; RT "Collection, Mapping, and Annotation of Over 28,000 cDNA Clones from RT japonica Rice."; RL Science 301:376-379(2003). RN [2] RP NUCLEOTIDE SEQUENCE. RA Adachi J., Aizawa K., Akimura T., Arakawa T., Carninci P., Doi K., RA Fujimura T., Fukuda S., Hanagaki T., Hara A., Hashizume W., RA Hayashida K., Hayashizaki Y., Hayatsu N., Hiramoto K., Hiraoka T., RA Hori F., Hotta I., Iida J., Iida Y., Ikeda R., Imamura K., Imotani K., RA Ishibiki J., Ishii Y., Ishikawa M., Itoh M., Kagawa I., Kanagawa S., RA Katoh H., Kawagashira N., Kawai J., Kawamata M., Kikuchi S., RA Kishikawa-Hirozane T., Kishimoto N., Kobayashi M., Kodama T., RA Kojima K., Kojima Y., Kondo S., Konno H., Kouda M., Koya S., RA Kurihara C., Kurosaki T., Kusumegi T., Li C., Lu M., Masuda H., RA Matsubara K., Matsuyama T., Miura J., Miyazaki A., Mizuno K., RA Murakami K., Murata M., Nagata T., Nakahama Y., Nakamura M., RA Namiki T., Narikawa R., Niikura J., Nishi K., Nomura K., Numasaki R., RA Ohneda E., Ohno M., Ohtsuki K., Oka M., Ooka H., Osato N., Ota Y., RA Otomo Y., Ryu R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H., RA Sasaki D., Sato K., Satoh K., Shibata K., Shinagawa A., Shiraki T., RA Shishiki T., Sogabe Y., Sugano S., Sugiyama A., Suzuki K., Suzuki Y., RA Tagami M., Tagami-Takeda Y., Tagawa A., Takahashi F., RA Takaku-Akahira S., Tanaka T., Tomaru A., Toya T., Tsunoda Y., Ueda M., RA Waki K., Xie Q., Yahagi W., Yamada H., Yamamoto M., Yasunishi A., RA Yazaki J., Yokomizo S., Yoshimura A.; RT "Collection, mapping, and annotation of 28K full-length cDNA clones RT from japonica rice."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16188032; DOI=10.1186/1741-7007-3-20; RG The rice chromosomes 11 and 12 sequencing consortia; RT "The sequence of rice chromosomes 11 and 12, rich in disease RT resistance genes and recent gene duplications."; RL BMC Biol. 3:20-20(2005). RN [4] RP NUCLEOTIDE SEQUENCE. RA Buell C.R., Wing R.A., McCombie W.A., Ouyang S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE. RA Buell R.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DP000011; ABG21903.1; -; Genomic_DNA. DR EMBL; AK100920; BAG94829.1; -; mRNA. DR EMBL; AK122089; BAH00789.1; -; mRNA. DR STRING; 39946.BGIOSIBCE035997; -. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 388 AA; 41176 MW; 711ACFB617B0A2EB CRC64; MVSTSGDTLS ESSTLSVYRD ELFAMADIVT PNVKEASRLL GGVSLRTVSD MRNAAESIYK FGPKHVLVKG GDMLESSDAT DVFFDGKEFI ELHAHRIKTH NTHGTGCTLA SCIASELAKG ATMLHAVQVA KNFVESALHH SKDLVVGNGP QGPFDHLFKL KCPPYNVGSQ PSFKPDQLFL YAVTDSGMNK KWGRSIKEAV QAAIEGGATI VQLREKDSET REFLEAAKAC MEICKSSGVP LLINDRVDIA LACNADGVHV GQLDMSAHEV RELLGPGKII GVSCKTPAQA QQAWNDGADY IGCGGVFPTS TKANNPTLGF DGLKTVCLAS KLPVVAIGGI NASNAGSVME LGLPNLKGVA VVSALFDRPS VVAETRNMKS ILTNTSRT // ID B7FZ00_PHATC Unreviewed; 336 AA. AC B7FZ00; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 19. DE SubName: Full=Predicted protein; GN ORFNames=PHATRDRAFT_35691; OS Phaeodactylum tricornutum (strain CCAP 1055/1). OC Eukaryota; Stramenopiles; Bacillariophyta; Bacillariophyceae; OC Bacillariophycidae; Naviculales; Phaeodactylaceae; Phaeodactylum. OX NCBI_TaxID=556484; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCAP 1055/1; RX PubMed=18923393; DOI=10.1038/nature07410; RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A., RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., RA Salamov A., Vandepoele K., Beszteri B., Gruber A., Heijde M., RA Katinka M., Mock T., Valentin K., Verret F., Berges J.A., Brownlee C., RA Cadoret J.P., Chiovitti A., Choi C.J., Coesel S., De Martino A., RA Detter J.C., Durkin C., Falciatore A., Fournet J., Haruta M., RA Huysman M.J., Jenkins B.D., Jiroutova K., Jorgensen R.E., Joubert Y., RA Kaplan A., Kroger N., Kroth P.G., La Roche J., Lindquist E., RA Lommer M., Martin-Jezequel V., Lopez P.J., Lucas S., Mangogna M., RA McGinnis K., Medlin L.K., Montsant A., Oudot-Le Secq M.P., Napoli C., RA Obornik M., Parker M.S., Petit J.L., Porcel B.M., Poulsen N., RA Robison M., Rychlewski L., Rynearson T.A., Schmutz J., Shapiro H., RA Siaut M., Stanley M., Sussman M.R., Taylor A.R., Vardi A., RA von Dassow P., Vyverman W., Willis A., Wyrwicz L.S., Rokhsar D.S., RA Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y., RA Grigoriev I.V.; RT "The Phaeodactylum genome reveals the evolutionary history of diatom RT genomes."; RL Nature 456:239-244(2008). RN [2] RP GENOME REANNOTATION. RC STRAIN=CCAP 1055/1; RG Diatom Consortium; RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., RA Detter J.C., Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., RA Pitluck S., Rokhsar D., Bowler C.; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000611; EEC48448.1; -; Genomic_DNA. DR RefSeq; XP_002180257.1; XM_002180221.1. DR ProteinModelPortal; B7FZ00; -. DR STRING; 2850.JGI35691; -. DR EnsemblProtists; Phatr35691; Phatr35691; Phatr35691. DR GeneID; 7201110; -. DR KEGG; pti:PHATRDRAFT_35691; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 336 AA; 37243 MW; E4DEB4C6DA33C288 CRC64; MFIVTISSRL RRQQVKLCQI SILIVTQMRY HQNPLIPLQL YAFLLGCRDF CVLGFLEKNG PFSLLVGGVQ RADQRAHRAT PGHLSLVDSD APRHSPFLRQ QGPYLAVITD QYSCDSDDQL EQALTCLNQA VSTKMVDVVS VRIQKRDAFD RNQERRVLML AKQLVSWSID YTFSVVLSSD WKHLLATSGA HGVHAKELNR DCIVEVRSQY PSALIGTSCH SVESAMEAYH TYRADYIFVG TCYLSDSHPE KETADLEGPE LPGIIRQKLH DRAAMDLDSN IAVPKVLAIG GIDATNCHIP VQTHGADGVA AIKSVLQAAD PYGTVQAIKT SMSRPL // ID B7G3W4_PHATC Unreviewed; 580 AA. AC B7G3W4; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 16-APR-2014, entry version 23. DE SubName: Full=Predicted protein; GN ORFNames=PHATRDRAFT_47293; OS Phaeodactylum tricornutum (strain CCAP 1055/1). OC Eukaryota; Stramenopiles; Bacillariophyta; Bacillariophyceae; OC Bacillariophycidae; Naviculales; Phaeodactylaceae; Phaeodactylum. OX NCBI_TaxID=556484; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCAP 1055/1; RX PubMed=18923393; DOI=10.1038/nature07410; RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A., RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., RA Salamov A., Vandepoele K., Beszteri B., Gruber A., Heijde M., RA Katinka M., Mock T., Valentin K., Verret F., Berges J.A., Brownlee C., RA Cadoret J.P., Chiovitti A., Choi C.J., Coesel S., De Martino A., RA Detter J.C., Durkin C., Falciatore A., Fournet J., Haruta M., RA Huysman M.J., Jenkins B.D., Jiroutova K., Jorgensen R.E., Joubert Y., RA Kaplan A., Kroger N., Kroth P.G., La Roche J., Lindquist E., RA Lommer M., Martin-Jezequel V., Lopez P.J., Lucas S., Mangogna M., RA McGinnis K., Medlin L.K., Montsant A., Oudot-Le Secq M.P., Napoli C., RA Obornik M., Parker M.S., Petit J.L., Porcel B.M., Poulsen N., RA Robison M., Rychlewski L., Rynearson T.A., Schmutz J., Shapiro H., RA Siaut M., Stanley M., Sussman M.R., Taylor A.R., Vardi A., RA von Dassow P., Vyverman W., Willis A., Wyrwicz L.S., Rokhsar D.S., RA Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y., RA Grigoriev I.V.; RT "The Phaeodactylum genome reveals the evolutionary history of diatom RT genomes."; RL Nature 456:239-244(2008). RN [2] RP GENOME REANNOTATION. RC STRAIN=CCAP 1055/1; RG Diatom Consortium; RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., RA Detter J.C., Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., RA Pitluck S., Rokhsar D., Bowler C.; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000615; EEC46722.1; -; Genomic_DNA. DR RefSeq; XP_002181508.1; XM_002181472.1. DR ProteinModelPortal; B7G3W4; -. DR STRING; 2850.JGI47293; -. DR EnsemblProtists; Phatr47293; Phatr47293; Phatr47293. DR GeneID; 7202328; -. DR KEGG; pti:PHATRDRAFT_47293; -. DR HOGENOM; HOG000155781; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 580 AA; 62723 MW; 7C4200BAA0130B27 CRC64; MKDLVTFSLF ILLFCTCSDS LAVYGRSAAT TSRTAPPIVY TIAGSDSGGG AGIQADLHAI HSFGCHGCSA ITCLTAQNSV GVIGVHAPPP DFLRAQLETL LEDLPPQAIK IGMLGTKELA IEVGAFLKKL KALDRKVWVV LDPVMITTSG HRLIEEDAQE AMVKHVFPHI DVLTPNKFEA EALLNRTLET ISDVEEGAKD LIALGAPSVL IKGGHTLYEG GKASNHIAYA QDYFLSSVQR NTGEPRLCDG DLGVWLRSPR YETEHTHGTG CTLSASLAAS LALGEQERQK PDGKRRGATS AIDTVDACCL AKAYVTAGIF HGIQLGQGPG PVAQTGFPSS HQYFPMVVAD AAEDHQRFPR MKAYDDKTTY DDNRPTLGRI LPVVNDEVWV QRLCQDPGVH DIQLRVKGID DNKKILEIIK KCQKLCQASG KRLWVNDYWQ EAIESGCFGV HVGQEDLYTC IRAGGLQLLR EKRMAFGIST HSYGELATAL GVKPSYISLG PVFATSSKTV QFDPQGLSLV RKWRELIQKE VPLVVIGGFS DAERAKAVRG LGANCVAVIG AVTQANDTVE AVSQMNEAMR // ID B7GEY5_ANOFW Unreviewed; 204 AA. AC B7GEY5; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Thiamine monophosphate synthase; GN Name=tenI; OrderedLocusNames=Aflv_2316; OS Anoxybacillus flavithermus (strain DSM 21510 / WK1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus. OX NCBI_TaxID=491915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21510 / WK1; RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161; RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A., RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V., RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., RA Alam M.; RT "Encapsulated in silica: genome, proteome and physiology of the RT thermophilic bacterium Anoxybacillus flavithermus WK1."; RL Genome Biol. 9:R161.1-R161.16(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000922; ACJ34673.1; -; Genomic_DNA. DR RefSeq; YP_002316658.1; NC_011567.1. DR ProteinModelPortal; B7GEY5; -. DR STRING; 491915.Aflv_2316; -. DR EnsemblBacteria; ACJ34673; ACJ34673; Aflv_2316. DR GeneID; 7038568; -. DR KEGG; afl:Aflv_2316; -. DR PATRIC; 20956552; VBIAnoFla45531_2383. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AFLA491915:GHEO-2385-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 204 AA; 22832 MW; 1BC2D5927A62ABFE CRC64; MKEFHLISTG NQSMDTFVHK SSLVHSYVDY IHIREKHRSA KEISMMVEKL LEANVPAQKI IVNDRVDVAV VYGVGGVQLA HHSLAPKRIK EKFPFLRVGR SVHTLEEAKQ AEDEGADYVV YGHIYETNCK EGLKPRGVSS LQQLASYICI PVVAIGGIKP SHVRDLFMAG AKGIAVMSTV FDADDPLYMV QLYRKQMGAN TWTF // ID B7GQ19_BIFLS Unreviewed; 917 AA. AC B7GQ19; E8MQX7; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 43. DE SubName: Full=Thiamine biosynthesis protein; DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=BLIJ_0810, Blon_0796; OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 OS / JCM 1222 / NCTC 11817 / S12). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=391904; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15697, and RC ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12 [JGI]; RX PubMed=19033196; DOI=10.1073/pnas.0809584105; RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R., RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P., RA Richardson P.M., Mills D.A.; RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals RT adaptations for milk utilization within the infant microbiome."; RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12 [Tokyo], RC and JCM 1222; RX PubMed=21270894; DOI=10.1038/nature09646; RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., RA Tobe T., Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., RA Kikuchi J., Morita H., Hattori M., Ohno H.; RT "Bifidobacteria can protect from enteropathogenic infection through RT production of acetate."; RL Nature 469:543-547(2011). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001095; ACJ51899.1; -; Genomic_DNA. DR EMBL; AP010889; BAJ68402.1; -; Genomic_DNA. DR RefSeq; YP_002322277.1; NC_011593.1. DR RefSeq; YP_005584572.1; NC_017219.1. DR STRING; 391904.Blon_0796; -. DR EnsemblBacteria; ACJ51899; ACJ51899; Blon_0796. DR EnsemblBacteria; BAJ68402; BAJ68402; BLIJ_0810. DR GeneID; 12166384; -. DR GeneID; 7054827; -. DR KEGG; bln:Blon_0796; -. DR KEGG; blon:BLIJ_0810; -. DR PATRIC; 21122538; VBIBifLon71229_0794. DR eggNOG; COG0352; -. DR KO; K03147; -. DR OMA; INTICSA; -. DR OrthoDB; EOG6NWBM5; -. DR BioCyc; BLON391904:GCDR-818-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Transferase; Zinc. SQ SEQUENCE 917 AA; 100234 MW; 60BC3E172F0368B2 CRC64; MSNEYPYASM RDNFDLSAYF VVGPEDCKGR PLTDVVDQAL RGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVQLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICAASEFP VVVGGGVTAA DMAMLAGTKA AGWFAVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVAHTPAADT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKS VCKGAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LAKAKANVDN DVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID B7GYZ4_ACIB3 Unreviewed; 203 AA. AC B7GYZ4; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ABBFA_000991; OS Acinetobacter baumannii (strain AB307-0294). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=557600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB307-0294; RX PubMed=18931120; DOI=10.1128/JB.00834-08; RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., RA Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., RA Hujer A.M., Bonomo R.A., Gill S.R.; RT "Comparative genome sequence analysis of multidrug-resistant RT Acinetobacter baumannii."; RL J. Bacteriol. 190:8053-8064(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001172; ACJ58710.1; -; Genomic_DNA. DR RefSeq; YP_002324903.1; NC_011595.1. DR ProteinModelPortal; B7GYZ4; -. DR STRING; 557600.ABBFA_000991; -. DR EnsemblBacteria; ACJ58710; ACJ58710; ABBFA_000991. DR GeneID; 7057937; -. DR KEGG; abb:ABBFA_000991; -. DR PATRIC; 20703510; VBIAciBau42682_0950. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ABAU557600:GKC3-997-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21750 MW; C30389C3887A22BE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKVD KADQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAK LFS // ID B7GZT8_ACIB3 Unreviewed; 299 AA. AC B7GZT8; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 44. DE SubName: Full=Mutator mutT protein; GN OrderedLocusNames=ABBFA_001158; OS Acinetobacter baumannii (strain AB307-0294). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=557600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB307-0294; RX PubMed=18931120; DOI=10.1128/JB.00834-08; RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., RA Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., RA Hujer A.M., Bonomo R.A., Gill S.R.; RT "Comparative genome sequence analysis of multidrug-resistant RT Acinetobacter baumannii."; RL J. Bacteriol. 190:8053-8064(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001172; ACJ57869.1; -; Genomic_DNA. DR RefSeq; YP_002325065.1; NC_011595.1. DR ProteinModelPortal; B7GZT8; -. DR STRING; 557600.ABBFA_001158; -. DR EnsemblBacteria; ACJ57869; ACJ57869; ABBFA_001158. DR GeneID; 7059838; -. DR KEGG; abb:ABBFA_001158; -. DR PATRIC; 20703840; VBIAciBau42682_1110. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ABAU557600:GKC3-1163-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 299 AA; 34203 MW; F41A81BC493DC0A4 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLNPELK KKIKTVHLKQ SQLMSLHKGD LEVGVRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID B7HDE9_BACC4 Unreviewed; 206 AA. AC B7HDE9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=BCB4264_A0786; OS Bacillus cereus (strain B4264). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405532; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4264; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus B4264."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001176; ACK63867.1; -; Genomic_DNA. DR RefSeq; YP_002365523.1; NC_011725.1. DR STRING; 405532.BCB4264_A0786; -. DR EnsemblBacteria; ACK63867; ACK63867; BCB4264_A0786. DR GeneID; 7098356; -. DR KEGG; bcb:BCB4264_A0786; -. DR PATRIC; 18873539; VBIBacCer117876_0679. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER405532:GI1K-783-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22791 MW; F39BD4067A87BD08 CRC64; MKNELHVISN GHMPFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLMEGFPASK IVINDRIDIA ILLNIPRVQL GYRSTDVKSV KEKFSYLHVG YSVHSLDEAI VAFKNGADSL VYGHVFPTDC KKGVPARGLE EISDIARCLS IPITAIGGIT PENTVDVLTN GVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID B7HWF1_BACC7 Unreviewed; 206 AA. AC B7HWF1; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=BCAH187_A0883; OS Bacillus cereus (strain AH187). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405534; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AH187; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B., RA Okstad O.A., Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus AH187."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001177; ACJ82552.1; -; Genomic_DNA. DR RefSeq; YP_002336860.1; NC_011658.1. DR ProteinModelPortal; B7HWF1; -. DR STRING; 405534.BCAH187_A0883; -. DR EnsemblBacteria; ACJ82552; ACJ82552; BCAH187_A0883. DR GeneID; 7077792; -. DR KEGG; bcr:BCAH187_A0883; -. DR PATRIC; 18827191; VBIBacCer120511_1070. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER405534:GHXM-852-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22777 MW; 767D7D7B15B3A27E CRC64; MKNELHVISN GHMSFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK IVINDRIDIA ILLNIPRVQL GYRSADVRSV KEKFSYLHVG YSVHSLEEAI DAFKNGADSL VYGHVFPTDC KKGVPARGLE EISDIARCLS IPITAIGGIT PENTGDVLTN GVSGIAVMSG IISSSNPYSK AKSYKESIRK WAEKHV // ID B7I2P5_ACIB5 Unreviewed; 299 AA. AC B7I2P5; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 44. DE SubName: Full=MutT/NUDIX family protein; GN OrderedLocusNames=AB57_2641; OS Acinetobacter baumannii (strain AB0057). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=480119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB0057; RX PubMed=18931120; DOI=10.1128/JB.00834-08; RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., RA Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., RA Hujer A.M., Bonomo R.A., Gill S.R.; RT "Comparative genome sequence analysis of multidrug-resistant RT Acinetobacter baumannii."; RL J. Bacteriol. 190:8053-8064(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001182; ACJ42747.1; -; Genomic_DNA. DR RefSeq; YP_002319983.1; NC_011586.1. DR ProteinModelPortal; B7I2P5; -. DR STRING; 480119.AB57_2641; -. DR EnsemblBacteria; ACJ42747; ACJ42747; AB57_2641. DR GeneID; 7044255; -. DR KEGG; abn:AB57_2641; -. DR PATRIC; 20698993; VBIAciBau111166_2552. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ABAU480119:GHQY-2630-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 299 AA; 34203 MW; F41A81BC493DC0A4 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLNPELK KKIKTVHLKQ SQLMSLHKGD LEVGVRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID B7I4N5_ACIB5 Unreviewed; 203 AA. AC B7I4N5; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AB57_2896; OS Acinetobacter baumannii (strain AB0057). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=480119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB0057; RX PubMed=18931120; DOI=10.1128/JB.00834-08; RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., RA Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., RA Hujer A.M., Bonomo R.A., Gill S.R.; RT "Comparative genome sequence analysis of multidrug-resistant RT Acinetobacter baumannii."; RL J. Bacteriol. 190:8053-8064(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001182; ACJ42241.1; -; Genomic_DNA. DR RefSeq; YP_002320230.1; NC_011586.1. DR ProteinModelPortal; B7I4N5; -. DR STRING; 480119.AB57_2896; -. DR EnsemblBacteria; ACJ42241; ACJ42241; AB57_2896. DR GeneID; 7044808; -. DR KEGG; abn:AB57_2896; -. DR PATRIC; 20699489; VBIAciBau111166_2794. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ABAU480119:GHQY-2885-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21750 MW; C30389C3887A22BE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKVD KADQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAK LFS // ID B7IVS9_BACC2 Unreviewed; 218 AA. AC B7IVS9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BCG9842_B4884; OS Bacillus cereus (strain G9842). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405531; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G9842; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus G9842."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001186; ACK94225.1; -; Genomic_DNA. DR RefSeq; YP_002443904.1; NC_011772.1. DR ProteinModelPortal; B7IVS9; -. DR STRING; 405531.BCG9842_B4884; -. DR EnsemblBacteria; ACK94225; ACK94225; BCG9842_B4884. DR GeneID; 7184337; -. DR KEGG; bcg:BCG9842_B4884; -. DR PATRIC; 18896325; VBIBacCer50903_0362. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER405531:GI5L-414-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23458 MW; 85CAA54E54939D7C CRC64; MRIETKKMSK LLQVYFIMGS NNCTRDPLAV LKEALDGGVT LFQFREKGEG SLIGGDRVRF AKELQTLCKE YSVPFIVNDD VELAIELDAD GVHVGQNDEG ITSVREKMGD KIIGVSAHTI EEARFAIENG ADYLGVGPIF PTSTKKDTKA VQGTKGLAYF REQGITVPIV GIGGITIENT AAVIEAGADG VSVISAISLA ESAYESTRKL AEEVKRSL // ID B7IXZ9_BACC2 Unreviewed; 206 AA. AC B7IXZ9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=BCG9842_B4545; OS Bacillus cereus (strain G9842). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405531; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G9842; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus G9842."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001186; ACK96799.1; -; Genomic_DNA. DR RefSeq; YP_002444196.1; NC_011772.1. DR ProteinModelPortal; B7IXZ9; -. DR STRING; 405531.BCG9842_B4545; -. DR EnsemblBacteria; ACK96799; ACK96799; BCG9842_B4545. DR GeneID; 7186436; -. DR KEGG; bcg:BCG9842_B4545; -. DR PATRIC; 18896995; VBIBacCer50903_0655. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER405531:GI5L-747-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22920 MW; 49E45A30F159B99E CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFLTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG ILSSSNPYSK AKSYKESIRK WAEKHV // ID B7J3X1_ACIF2 Unreviewed; 329 AA. AC B7J3X1; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Mutator mutT protein/thiamine-phosphate pyrophosphorylase family protein; GN OrderedLocusNames=AFE_0227; OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / NCIB OS 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=243159; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23270 / DSM 14882 / NCIB 8455; RX PubMed=19077236; DOI=10.1186/1471-2164-9-597; RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., RA Blake R.II., Eisen J.A., Holmes D.S.; RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to RT industrial applications."; RL BMC Genomics 9:597-597(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001219; ACK80735.1; -; Genomic_DNA. DR RefSeq; YP_002424734.1; NC_011761.1. DR ProteinModelPortal; B7J3X1; -. DR STRING; 243159.AFE_0227; -. DR EnsemblBacteria; ACK80735; ACK80735; AFE_0227. DR GeneID; 7135657; -. DR KEGG; afr:AFE_0227; -. DR PATRIC; 20651783; VBIAciFer29821_0216. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AFER243159:GH3S-227-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 329 AA; 35387 MW; 71B5BFB1BD17D76D CRC64; MPTVPVATGI IEDAFGRLLV ALRPEGKPWP GFWEFPGGKV DPGETPEQAL VRELWEELGV TVTAPEPFRE LEYTYPERTV RVHFYRVRHW TGTAHGREGQ EVRWLFPWEI PALECLPANL RLTADVLAEA LPQPPLCLIA DPGRLPLPDF RRALEAALDA GLRWLVLRCK AVPDGSSADV LAALCAGALA GGVQVYLNHP DPLPGWPRTG RHLTQAQSDA GVKPDEAFGV SCHDAAGLQQ AARLGARYAF LSPIFPTSSH PDTEALGPEV FAAMAAESSL PLIALGGMTA ARVPEALAAG ARGVAVLSGI LEAQDPAAAT RALLRHWER // ID B7JRA8_BACC0 Unreviewed; 206 AA. AC B7JRA8; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=BCAH820_0806; OS Bacillus cereus (strain AH820). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405535; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AH820; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus AH820."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001283; ACK92265.1; -; Genomic_DNA. DR RefSeq; YP_002449758.1; NC_011773.1. DR ProteinModelPortal; B7JRA8; -. DR STRING; 405535.BCAH820_0806; -. DR EnsemblBacteria; ACK92265; ACK92265; BCAH820_0806. DR GeneID; 7191227; -. DR KEGG; bcu:BCAH820_0806; -. DR PATRIC; 18838452; VBIBacCer122868_0741. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER405535:GHSL-817-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID B7K0B6_CYAP8 Unreviewed; 343 AA. AC B7K0B6; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PCC8801_3432; OS Cyanothece sp. (strain PCC 8801) (Synechococcus sp. (strain PCC 8801 / OS RF-1)). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=41431; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 8801; RX PubMed=21972240; DOI=10.1128/mBio.00214-11; RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., RA Min H., Sherman L.A., Pakrasi H.B.; RT "Novel metabolic attributes of the genus Cyanothece, comprising a RT group of unicellular nitrogen-fixing Cyanobacteria."; RL MBio 2:E214-E214(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001287; ACK67400.1; -; Genomic_DNA. DR RefSeq; YP_002373556.1; NC_011726.1. DR ProteinModelPortal; B7K0B6; -. DR STRING; 41431.PCC8801_3432; -. DR EnsemblBacteria; ACK67400; ACK67400; PCC8801_3432. DR GeneID; 7103124; -. DR KEGG; cyp:PCC8801_3432; -. DR PATRIC; 21579221; VBICyaSp125535_3615. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CSP41431:GHLK-3473-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 125 Unknown (By similarity). FT REGION 126 343 Thiamine-phosphate synthase (By FT similarity). FT REGION 173 177 HMP-PP binding (By similarity). FT REGION 270 272 THZ-P binding (By similarity). FT METAL 206 206 Magnesium (By similarity). FT METAL 225 225 Magnesium (By similarity). FT BINDING 205 205 HMP-PP (By similarity). FT BINDING 244 244 HMP-PP (By similarity). FT BINDING 273 273 HMP-PP (By similarity). FT BINDING 300 300 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 343 AA; 38322 MW; 4238948B130E06E6 CRC64; MLKETHNSLS IPRILDANLN RAREGLRIIE EWCRFGLENS QLADNCKQMR QEIARWHTSE LRIARDTPND PGTALTHPQE ETRSSIDHLL QANLCRIQEA LRVLEEYGKL YQPQMGIAFK NMRYQVYSLE SNLVKQTRYE KYKKSPLYLV TSPDDNILSI VEAALQGGLT LVQYRDKNSE DTIQLEIAQK LCQLCHKYDA LFIMNDRADI ALSVNADGVH LGQQDISIAL ARQIVGPNRI IGRSTTNPQE MAKAIAEGAD YIGVGPVYAT PTKPDKPAVG LDYVNYAKEN SPIPWVAIGG IDLNNLNDVI SAGAQQVAVV RAIMKADNPT KATQELLAKL SLK // ID B7K9V6_CYAP7 Unreviewed; 368 AA. AC B7K9V6; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PCC7424_2908; OS Cyanothece sp. (strain PCC 7424) (Synechococcus sp. (strain ATCC OS 29155)). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=65393; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7424; RX PubMed=21972240; DOI=10.1128/mBio.00214-11; RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., RA Min H., Sherman L.A., Pakrasi H.B.; RT "Novel metabolic attributes of the genus Cyanothece, comprising a RT group of unicellular nitrogen-fixing Cyanobacteria."; RL MBio 2:E214-E214(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001291; ACK71312.1; -; Genomic_DNA. DR RefSeq; YP_002378180.1; NC_011729.1. DR ProteinModelPortal; B7K9V6; -. DR STRING; 65393.PCC7424_2908; -. DR EnsemblBacteria; ACK71312; ACK71312; PCC7424_2908. DR GeneID; 7108453; -. DR KEGG; cyc:PCC7424_2908; -. DR PATRIC; 21554768; VBICyaSp136448_2994. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CSP65393:GJP7-2943-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 129 Unknown (By similarity). FT REGION 130 368 Thiamine-phosphate synthase (By FT similarity). FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 368 AA; 41232 MW; 343AD73B7D7731AA CRC64; MDEHYSQIRG QQSAIERILD ANLDRAREGL RIIEEWCRFG LNNSQLAEDC KEMRQELASW HSTELRMARD TPGDPGTELT HPQEETRNSI EQLLQANLCR IEEALRVLEE YGKLYHPKMG VVFKQMRYRV YTLESNLLGF RRHHYLRESL LYLVTSPSEN LISVVESALS AGLTLVQYRD KQTDDLIRLS IAHKLCQLCH EYGALFIVND RVDIALAVNA DGVHLGQQDI PISLARGMLG SQKIIGRSTT NPQEMQQAIA QGADYIGVGP VYETPTKAGK AAAGLDYVRY AAKHSPIPWF AIGGIDTSNL KDVLMAGAQR VSIVRAIMQA EKPALVTGQL LSVLSRKRTF PPVDPKPNVL SLTESIEQ // ID B7KNP8_METC4 Unreviewed; 222 AA. AC B7KNP8; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Mchl_2647; OS Methylobacterium extorquens (strain CM4 / NCIMB 13688) OS (Methylobacterium chloromethanicum). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=440085; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CM4 / NCIMB 13688; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Marx C., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium chloromethanicum RT CM4."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001298; ACK83487.1; -; Genomic_DNA. DR RefSeq; YP_002421415.1; NC_011757.1. DR ProteinModelPortal; B7KNP8; -. DR STRING; 440085.Mchl_2647; -. DR EnsemblBacteria; ACK83487; ACK83487; Mchl_2647. DR GeneID; 7117397; -. DR KEGG; mch:Mchl_2647; -. DR PATRIC; 22499541; VBIMetChl132133_2603. DR eggNOG; NOG280778; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; MCHL440085:GCXT-2699-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 222 AA; 22884 MW; 7F9ADCC9C8146888 CRC64; MAESESAAPR PRLALLTPYG LGASEAEATA RALDAACAAG DVAAVILRLA ASDERSLVAL VKRLAPPAQE RGAAVLVSVP GFTGDIVSVA ARGGADGVHL DRADEEALRD LRGRLRDGRI LGTGGVLGSR NAAMVAGETG VDYLMVGGLF PDGVAPDAEE VRERAAWWAE IFETPCIAVA TSAEDVAALV LTGSEFIGLE SALWLDDPEG VRAAQAQLDR AR // ID B7KSN2_METC4 Unreviewed; 241 AA. AC B7KSN2; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mchl_4935; OS Methylobacterium extorquens (strain CM4 / NCIMB 13688) OS (Methylobacterium chloromethanicum). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=440085; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CM4 / NCIMB 13688; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Marx C., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium chloromethanicum RT CM4."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001298; ACK85700.1; -; Genomic_DNA. DR RefSeq; YP_002423628.1; NC_011757.1. DR ProteinModelPortal; B7KSN2; -. DR STRING; 440085.Mchl_4935; -. DR EnsemblBacteria; ACK85700; ACK85700; Mchl_4935. DR GeneID; 7114356; -. DR KEGG; mch:Mchl_4935; -. DR PATRIC; 22504166; VBIMetChl132133_4894. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MCHL440085:GCXT-5009-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT METAL 87 87 Magnesium (By similarity). FT METAL 106 106 Magnesium (By similarity). FT BINDING 86 86 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 241 AA; 24454 MW; 66B93BA761D0F7D0 CRC64; MGSGTGLGLS RPSAGVAVDL RLYGILDVGV LGGDATALAT LAAEAVAGGA TLLQYRDKDL TDARAALARI RAIHAALAGR APLLVNDRVD LALAAGVEGV HLGQSDLHPE DARRLLGPRA IIGLTVKTGA QADELYRLPI DYACIGGVFA TTSKDNPDPP VGLDGLQRIV FRARLARGQS LPLGAIAGID ASNTASVIRA GADGVALIGA LFKGGATEAK ARDLLARVDE ALGQRGSTGT R // ID B7KY37_METC4 Unreviewed; 205 AA. AC B7KY37; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mchl_0613; OS Methylobacterium extorquens (strain CM4 / NCIMB 13688) OS (Methylobacterium chloromethanicum). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=440085; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CM4 / NCIMB 13688; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Marx C., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium chloromethanicum RT CM4."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001298; ACK81535.1; -; Genomic_DNA. DR RefSeq; YP_002419463.1; NC_011757.1. DR ProteinModelPortal; B7KY37; -. DR STRING; 440085.Mchl_0613; -. DR EnsemblBacteria; ACK81535; ACK81535; Mchl_0613. DR GeneID; 7117861; -. DR KEGG; mch:Mchl_0613; -. DR PATRIC; 22495379; VBIMetChl132133_0560. DR eggNOG; NOG131844; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INERSDI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MCHL440085:GCXT-628-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 134 136 THZ-P binding (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 20467 MW; B044BD2ED092F4AB CRC64; MTLPPLLVVT DRHGAARPLT ETVRAAVAGG ARFVWLRDRD LDRDARRDLA RDLIALLQPV GGRLVVGGDA DLAAETGAQG VHLSGSAGID GIRAARTSLG AAALIGFSAH SVAEVAAAAA AGADYATLSP IFPTASKPGY GPALGLASLR AAAAHRLPVF ALGGIDGGNA RACREAGAAG VAMMGGVMRG SDPRDATAQF VAALT // ID B7LA87_ECO55 Unreviewed; 211 AA. AC B7LA87; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EC55989_4478; OS Escherichia coli (strain 55989 / EAEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585055; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=55989 / EAEC; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M., RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S., RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU928145; CAV01240.1; -; Genomic_DNA. DR RefSeq; YP_002405368.1; NC_011748.1. DR ProteinModelPortal; B7LA87; -. DR SMR; B7LA87; 20-202. DR STRING; 585055.EC55989_4478; -. DR EnsemblBacteria; CAV01240; CAV01240; EC55989_4478. DR GeneID; 7147785; -. DR KEGG; eck:EC55989_4478; -. DR PATRIC; 38482544; VBIEscCol113220_4507. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL585055:GJOM-4551-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B7LUK9_ESCF3 Unreviewed; 211 AA. AC B7LUK9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EFER_3761; OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585054; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35469 / DSM 13698 / CDC 0568-73; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M., RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S., RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU928158; CAQ91212.1; -; Genomic_DNA. DR RefSeq; YP_002384814.1; NC_011740.1. DR ProteinModelPortal; B7LUK9; -. DR STRING; 585054.EFER_3761; -. DR EnsemblBacteria; CAQ91212; CAQ91212; EFER_3761. DR GeneID; 7121990; -. DR KEGG; efe:EFER_3761; -. DR PATRIC; 32131849; VBIEscFer122920_3623. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; EFER585054:GJJM-3766-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23154 MW; 798DEE5042229F97 CRC64; MYQPDFPHVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIERLAAYP TVAIGGISLP RAPAVMATGV GSIAVVSAIT QAADWRLATE QLLEIAGVGD E // ID B7M741_ECO8A Unreviewed; 211 AA. AC B7M741; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECIAI1_4208; OS Escherichia coli O8 (strain IAI1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585034; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IAI1; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M., RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S., RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU928160; CAR00967.1; -; Genomic_DNA. DR RefSeq; YP_002389462.1; NC_011741.1. DR ProteinModelPortal; B7M741; -. DR SMR; B7M741; 11-208. DR STRING; 585034.ECIAI1_4208; -. DR EnsemblBacteria; CAR00967; CAR00967; ECIAI1_4208. DR GeneID; 7126243; -. DR KEGG; ecr:ECIAI1_4208; -. DR PATRIC; 18327643; VBIEscCol26572_4089. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL585034:GJ84-4223-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23027 MW; 0AE827392C8C3853 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGVSLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B7MIX9_ECO45 Unreviewed; 211 AA. AC B7MIX9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECS88_4454; OS Escherichia coli O45:K1 (strain S88 / ExPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585035; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S88 / ExPEC; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M., RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S., RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU928161; CAR05623.1; -; Genomic_DNA. DR RefSeq; YP_002393972.1; NC_011742.1. DR ProteinModelPortal; B7MIX9; -. DR SMR; B7MIX9; 9-208. DR STRING; 585035.ECS88_4454; -. DR EnsemblBacteria; CAR05623; CAR05623; ECS88_4454. DR GeneID; 7131294; -. DR KEGG; ecz:ECS88_4454; -. DR PATRIC; 18416591; VBIEscCol91599_4361. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL585035:GJWP-4430-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B7MRB9_ECO81 Unreviewed; 211 AA. AC B7MRB9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECED1_4700; OS Escherichia coli O81 (strain ED1a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ED1a; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M., RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S., RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU928162; CAR10807.2; -; Genomic_DNA. DR RefSeq; YP_002400486.1; NC_011745.1. DR ProteinModelPortal; B7MRB9; -. DR SMR; B7MRB9; 10-208. DR STRING; 585397.ECED1_4700; -. DR EnsemblBacteria; CAR10807; CAR10807; ECED1_4700. DR GeneID; 7141542; -. DR KEGG; ecq:ECED1_4700; -. DR PATRIC; 38493494; VBIEscCol8292_4685. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL585397:GJCU-4746-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23086 MW; 1A8F52AF19C8B3F0 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ERPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B7NFT4_ECOLU Unreviewed; 211 AA. AC B7NFT4; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECUMN_4517; OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMN026 / ExPEC; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M., RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S., RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU928163; CAR15641.1; -; Genomic_DNA. DR RefSeq; YP_002415131.1; NC_011751.1. DR ProteinModelPortal; B7NFT4; -. DR STRING; 585056.ECUMN_4517; -. DR EnsemblBacteria; CAR15641; CAR15641; ECUMN_4517. DR GeneID; 7158055; -. DR KEGG; eum:ECUMN_4517; -. DR PATRIC; 18448387; VBIEscCol32010_4687. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 4A5B4907CA38B2E8 CRC64; MYQPDFPPVP FHLGLYPVVD SAQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAITLGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVMATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID B7NRS6_ECO7I Unreviewed; 211 AA. AC B7NRS6; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECIAI39_4383; OS Escherichia coli O7:K1 (strain IAI39 / ExPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IAI39 / ExPEC; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M., RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S., RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU928164; CAR20489.1; -; Genomic_DNA. DR RefSeq; YP_002410257.1; NC_011750.1. DR ProteinModelPortal; B7NRS6; -. DR STRING; 585057.ECIAI39_4383; -. DR EnsemblBacteria; CAR20489; CAR20489; ECIAI39_4383. DR GeneID; 7152968; -. DR KEGG; ect:ECIAI39_4383; -. DR PATRIC; 18337729; VBIEscCol51957_4529. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL585057:GJ8I-4540-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23138 MW; C625E6545C9DF5D0 CRC64; MYQPDFPHVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLDAIRT AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLVDYP TVAIGGISLP RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGAGD E // ID B7QSU0_9RHOB Unreviewed; 211 AA. AC B7QSU0; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=RR11_1637; OS Ruegeria sp. R11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=439497; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R11; RA Kjelleberg S., Case R., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999054; EEB70877.1; -; Genomic_DNA. DR ProteinModelPortal; B7QSU0; -. DR EnsemblBacteria; EEB70877; EEB70877; RR11_1637. DR PATRIC; 29768597; VBIRueSp9964_2711. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 211 AA; 22684 MW; 7A71263D6AC19280 CRC64; MDSPADAPET PQIYLTTPAS FELGRFPDQL ARVLDEVEIA CVRLELASRD EDTLSRAGDA LRAVAHARDV AIVITDHQIL AERLGLDGVH LSDAARPVRT ARKALGPDAI VGSFCAASRH DGLTAAEAGA DYVSFGPVGT SGLGDGNQAQ KDLFEWWSQM IEVPVVAEGG LTVDIVRELA PYTDFFGIGD EIWREEDHIA SLRKLMAAME G // ID B7QWQ0_9RHOB Unreviewed; 197 AA. AC B7QWQ0; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 16-OCT-2013, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RR11_1533; OS Ruegeria sp. R11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=439497; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R11; RA Kjelleberg S., Case R., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999054; EEB70773.1; -; Genomic_DNA. DR ProteinModelPortal; B7QWQ0; -. DR EnsemblBacteria; EEB70773; EEB70773; RR11_1533. DR PATRIC; 29769817; VBIRueSp9964_3312. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 197 AA; 21881 MW; 1A0E63503B81A128 CRC64; MERFYLIVGH VSQLELLVPH GVRLVQLRIK DQPETEVRRQ IARARDFCAV HGAQLVVNDY WQAALDLNCG FVHLGQEDMD SADFAALRRK GVRFGLSTHD ETELERALSH GPDYVALGPV YETLLKQMKW APQGLDRVRR WKQMVADTPL VAIGGLTIDR LPGVFAAGAD SAAVVTDIQQ APDPEAQTRA WIKACAA // ID B7R8X6_9THEO Unreviewed; 221 AA. AC B7R8X6; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-FEB-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_1; Synonyms=thiE; ORFNames=CDSM653_972; OS Carboxydibrachium pacificum DSM 12653. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Caldanaerobacter. OX NCBI_TaxID=391606; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 12653; RA Gonzalez J., Sokolova T., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999099; EEB75651.1; -; Genomic_DNA. DR ProteinModelPortal; B7R8X6; -. DR EnsemblBacteria; EEB75651; EEB75651; CDSM653_972. DR PATRIC; 30385681; VBICarPac114674_1570. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23943 MW; 6C62D318E0698481 CRC64; MNKGVKVVKR IDFTLYAITD RSFIKGMDIA EAVEIAIKNG VTVVQLREKD ISSREFYEIA LKVKEVTRKY NVPLIINDRV DIALAVDAEG VHVGPDDLPV GVVRRILGPD KIVGGSAYSV EEALKAEKEG ADYIGAGSVF AQPVKPEAEV IGIEGVRKIK EAVNIPVVAI GGVNKTNAYE VILHSGVDGI SAIAGIFDGD IEANTKDMLR EIRRAFKERG K // ID B7R9L6_9THEO Unreviewed; 213 AA. AC B7R9L6; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_2; Synonyms=thiE; ORFNames=CDSM653_162; OS Carboxydibrachium pacificum DSM 12653. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Caldanaerobacter. OX NCBI_TaxID=391606; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 12653; RA Gonzalez J., Sokolova T., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999118; EEB75388.1; -; Genomic_DNA. DR ProteinModelPortal; B7R9L6; -. DR EnsemblBacteria; EEB75388; EEB75388; CDSM653_162. DR PATRIC; 30386336; VBICarPac114674_1887. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23199 MW; 13007F7F4384522D CRC64; MDLTLYAITD RSYIKDMDIA DAVELAIKGG ATIIQLREKD ISSREFYEIA LKVKEVTKRN KIPLIINDRV DIALAVDADG VHVGQEDLPA DVVRRMIGPH KIVGVSARTV EEALKAQRDG ADYLGVGAVF KTPTKPEAEA IGIEGLKRIK EAVTIPVVAI GGITKDNAYE VMLKSGVDGI SSVSAVFYGD IENNTRKLLE VIAKAINDRR NLK // ID B7RQ54_9RHOB Unreviewed; 206 AA. AC B7RQ54; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=RGAI101_143; OS Roseobacter sp. GAI101. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391589; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GAI101; RA Edwards R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999213; EEB82998.1; -; Genomic_DNA. DR ProteinModelPortal; B7RQ54; -. DR EnsemblBacteria; EEB82998; EEB82998; RGAI101_143. DR PATRIC; 28100739; VBIRosSp12209_0190. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22220 MW; C887CCCDC6DFE9B7 CRC64; METPDQPQLY LITPAEFDLE VFPDQLARVL DAQPIACLRL ALGTRDEDRL LRAADALRTI TDARDIAFVI SDHTLLAERI GLDGVHLTDA ARSVRHARKT LGDDAIVGSF CAGSRHDGMA AGEAGADYVS FGPVRPSALD DGSYAELDLF KWWSEVIEVP VVAEGGLDDA LVRALTPMTD FFGIGDEIWG TDDPVKALAE LVAATK // ID B7RRI4_9RHOB Unreviewed; 213 AA. AC B7RRI4; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RGAI101_4197; OS Roseobacter sp. GAI101. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391589; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GAI101; RA Edwards R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999214; EEB82892.1; -; Genomic_DNA. DR ProteinModelPortal; B7RRI4; -. DR EnsemblBacteria; EEB82892; EEB82892; RGAI101_4197. DR PATRIC; 28107848; VBIRosSp12209_3932. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 21966 MW; 7A9FF8527B75E710 CRC64; MRDLKAQLRL YLVTDADLCA RLGVVETVRR AVAGGVTMVQ LRDKTATTAE RRALAIRLRH ALEGSGVPLV INDDVAAAVA ADVDGAHIGQ GDMSPERARA LLGPDKILGL SCETPQTVRA ADPLIVDYLG LGPVFGTATK TDHAKPVGFE GLADLVALTR LPTVAIGGLK SAHLRDVQAS GADGMAVVSA ICGQPDPCAA ALAFGSTKTQ VPT // ID B7UPE8_ECO27 Unreviewed; 211 AA. AC B7UPE8; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=E2348C_4300; OS Escherichia coli O127:H6 (strain E2348/69 / EPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=574521; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E2348/69 / EPEC; RX PubMed=18952797; DOI=10.1128/JB.01238-08; RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., RA Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P., RA Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J., RA Frankel G.; RT "Complete genome sequence and comparative genome analysis of RT enteropathogenic Escherichia coli O127:H6 strain E2348/69."; RL J. Bacteriol. 191:347-354(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM180568; CAS11848.1; -; Genomic_DNA. DR RefSeq; YP_002331756.1; NC_011601.1. DR ProteinModelPortal; B7UPE8; -. DR STRING; 574521.E2348C_4300; -. DR EnsemblBacteria; CAS11848; CAS11848; E2348C_4300. DR GeneID; 7061783; -. DR KEGG; ecg:E2348C_4300; -. DR PATRIC; 18347874; VBIEscCol90278_4398. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL574521:GJAO-4472-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23016 MW; CC43679342AF9407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEISGVGD E // ID B7UZH8_PSEA8 Unreviewed; 315 AA. AC B7UZH8; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 48. DE SubName: Full=Probable pyrophosphohydrolase; GN OrderedLocusNames=PLES_47791; OS Pseudomonas aeruginosa (strain LESB58). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=557722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LESB58; RX PubMed=19047519; DOI=10.1101/gr.086082.108; RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I., RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., RA Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., RA Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L., RA Levesque R.C.; RT "Newly introduced genomic prophage islands are critical determinants RT of in vivo competitiveness in the Liverpool epidemic strain of RT Pseudomonas aeruginosa."; RL Genome Res. 19:12-23(2009). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM209186; CAW29533.1; -; Genomic_DNA. DR RefSeq; YP_002442360.1; NC_011770.1. DR ProteinModelPortal; B7UZH8; -. DR SMR; B7UZH8; 6-123, 127-313. DR STRING; 557722.PLES_47791; -. DR EnsemblBacteria; CAW29533; CAW29533; PLES_47791. DR GeneID; 7178732; -. DR KEGG; pag:PLES_47791; -. DR PATRIC; 19819387; VBIPseAer113719_4905. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PAER557722:GHJW-4844-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34055 MW; 9165F7469596B47A CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EDGEPVRAAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEAHGAEGQ PLAWVEPREL ADYEFPAANA PIVQAARLPA HYLITPDGLE PGELISGVRK AVEAGIRLIQ LRAPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDAEELAL AASMGVEFVT LSPVQPTESH PGEPALGWDK AAELIAGFNQ PVYLLGGLGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID B7VMV6_VIBSL Unreviewed; 430 AA. AC B7VMV6; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=VS_3097; OS Vibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=575788; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LGP32; RA Mazel D., Le Roux F.; RT "Vibrio splendidus str. LGP32 complete genome."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM954972; CAV20364.1; -; Genomic_DNA. DR RefSeq; YP_002418604.1; NC_011753.2. DR ProteinModelPortal; B7VMV6; -. DR STRING; 575788.VS_3097; -. DR EnsemblBacteria; CAV20364; CAV20364; VS_3097. DR GeneID; 7162550; -. DR KEGG; vsp:VS_3097; -. DR PATRIC; 20156690; VBIVibSpl48387_4273. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; WSAQGES; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; VSPL575788:GH64-3028-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 430 AA; 47797 MW; 3702031652695033 CRC64; MTVKILIPSQ NIELTGEVQN CLLVAKRQGL ATDAVELGVS PTKYFSIVDT QQALSIGFAY DVDSLAECQL AELNHVVDYS NSVALTDVCD AFTQTPNTIY IGVSDDSVVL DIWSHLYANR AIKSDTTAHQ ELDNHGHFAW LLTLLALEFP LEDALVLARA SSNVSRGTWP AHYQNFPIPI LEDERLDISV GWAHQGTSLS FPELSKSSLG LYPVVDDVEW IERLLKLGIN TVQLRIKNPL QADLEQQVAR SIELGREHNA QVFINDYWQL ALKHDAFGVH LGQEDIEESN LSQLSRAGIK IGLSTHGYYE LLRIVQINPS YIALGHIFPT TTKQMPSKPQ GLVRLSLYQQ LIDTIPYTDQ LTGYPTVAIG GIDQSKAEQV WECGVSSLAV VRAITLAEDP QKVIEFFEKL MAPKSPILKE EVMQEPSYAE // ID B7VS64_VIBSL Unreviewed; 228 AA. AC B7VS64; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=VS_II1083; OS Vibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=575788; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LGP32; RA Mazel D., Le Roux F.; RT "Vibrio splendidus str. LGP32 complete genome."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM954973; CAV26964.1; -; Genomic_DNA. DR RefSeq; YP_002395662.1; NC_011744.2. DR ProteinModelPortal; B7VS64; -. DR STRING; 575788.VS_II1083; -. DR EnsemblBacteria; CAV26964; CAV26964; VS_II1083. DR GeneID; 7138369; -. DR KEGG; vsp:VS_II1083; -. DR PATRIC; 20149947; VBIVibSpl48387_1023. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; VSPL575788:GH64-4161-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 58 62 HMP-PP binding (By similarity). FT REGION 155 157 THZ-P binding (By similarity). FT REGION 206 207 THZ-P binding (By similarity). FT METAL 91 91 Magnesium (By similarity). FT METAL 110 110 Magnesium (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 HMP-PP (By similarity). FT BINDING 186 186 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 24997 MW; C6A2083CC8B9FC10 CRC64; MHMMRIVGKI VETQFRLRLQ RHDMNPYKLY LVTDDQQDLE TLKFVVEQAI AGGVTMVQVR EKHGDVRAFI ERAQAVKSIL AGSGVPLIIN DRVDVALAVD ADGLHLGQSD MPAELARQLI GPDKILGLSI ETEQQLREAD SLPIDYIGLS ALFTTPTKTN LKKHWGYDGI KMALETTKLP IVGIGGINES NIPQLVESGI HGLALVSAIC HAEDPKQATQ DLLSLMGE // ID B7X3K1_COMTE Unreviewed; 313 AA. AC B7X3K1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CtesDRAFT_PD1628; OS Comamonas testosteroni KF-1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=399795; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KF-1; RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004; RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.; RT "Mineralization of individual congeners of linear RT alkylbenzenesulfonate by defined pairs of heterotrophic bacteria."; RL Appl. Environ. Microbiol. 70:4053-4063(2004). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KF-1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Lowry S., RA Sun H., Larimer F., Land M.L., Hauser L., Kjelleberg S., Cook A., RA Knepper T.P., Fischer K., Schleheck D., Richardson P.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAUJ02000001; EED66682.1; -; Genomic_DNA. DR ProteinModelPortal; B7X3K1; -. DR EnsemblBacteria; EED66682; EED66682; CtesDRAFT_PD1628. DR PATRIC; 29054787; VBIComTes39478_1647. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 137 141 HMP-PP binding (By similarity). FT METAL 170 170 Magnesium (By similarity). FT METAL 189 189 Magnesium (By similarity). FT BINDING 169 169 HMP-PP (By similarity). FT BINDING 211 211 HMP-PP (By similarity). FT BINDING 240 240 HMP-PP (By similarity). FT BINDING 269 269 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 313 AA; 33461 MW; B8BD2BA1DC2E48C8 CRC64; MDSAEIKALA QAIVHQHSAN FGAQLHHDAN SVELTPQPVP PALRQEPAYL AALEACSQLG FIAVDAQTLA QAWQCQSERN NHFDATHWPD DPRDFGLGKA DPAQAFAHCP RELGLYGVLP TAEWVGRMAR AGVPTVQLRF KSGDQAAVAR EVKAAVEAVK GTHARLFIND HWQAALDAAA YGIHVGQEDL DVIGQRDLES IRTSGTRLGV STHGYAEMVR AHAVQPSYIA LGAVFPTTLK KMATAPQGLA RLAAYVRLMQ QYPLVAIGGI SEDLFPAVRA TGVGSVAVVR ALVNAPDPEA AAQHLLQRMQ AAA // ID B8BNJ1_ORYSI Unreviewed; 548 AA. AC B8BNJ1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 16-APR-2014, entry version 31. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=OsI_37743; OS Oryza sativa subsp. indica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=39946; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., RA Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., RA Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J., RA Samudrala R., Wang J., Wong G.K., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). RN [2] RP NUCLEOTIDE SEQUENCE. RA Wang J., Li R., Fan W., Huang Q., Zhang J., Zhou Y., Hu Y., Zi S., RA Li J., Ni P., Zheng H., Zhang Y., Zhao M., Hao Q., McDermott J., RA Samudrala R., Kristiansen K., Wong G.K.-S.; RT "Improved gene annotation of the rice (Oryza sativa) genomes."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RA Wang J., Li R., Fan W., Huang Q., Zhang J., Zhou Y., Hu Y., Zi S., RA Li J., Ni P., Zheng H., Zhang Y., Zhao M., Hao Q., McDermott J., RA Samudrala R., Kristiansen K., Wong G.K.-S.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000137; EEC68982.1; -; Genomic_DNA. DR ProteinModelPortal; B8BNJ1; -. DR Gramene; B8BNJ1; -. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; SQ SEQUENCE 548 AA; 57804 MW; 6F783EDA8AFC1FAC CRC64; MAAAPQQSVH PSLPSSTSTL RLLISSSPRR PPPPPPRARR YNRLAASASA AREMPWPHVL TVAGSDSGGG AGIQADIKAC AALGAYCSSV VTAVTAQNTA GVQGIHVVPE EFIREQLNSV LSDMSVDVVK TGMLPSIGVV RVLCESLKKF PVKALVVDPV MVSTSGDILS ESSTLSVYRD ELFAMADIVT PNVKEASRLL GGVSLRTVSD MRNAAESIYK FGPKHVLVKG GDMLESSDAT DVFFDGKEFI ELHAHRIKTH NTHGTGCTLA SCIASELAKG ATMLHAVQVA KNFVESALHH SKDLVIGNGP QGPFDHLFKL KCPPYNVGSQ PSFKPDQLFL YAVTDSGMNK KWGRSIKEAV QAAIEGGATI VQLREKDSET REFLEAAKAC MEICKSSGVP LLINDRVDIA LACNADGVHV GQSDMSAHEV RELLGPGKII GVSCKTPAQA QQAWNDGADY IGCGGVFPTS TKANNPTLGF DGLKTVCLAS KLPVVAIGGI NASNAGSVME LGLPNLKGVA VVSALFDRPS VVAETRNMKS ILTNTSRT // ID B8C465_THAPS Unreviewed; 193 AA. AC B8C465; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 13-NOV-2013, entry version 21. DE SubName: Full=Thiaminephosphate pyrophosphorylase thiamine phosphate synthase; DE EC=2.5.1.3; DE Flags: Fragment; GN ORFNames=THAPSDRAFT_262963; OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana). OC Eukaryota; Stramenopiles; Bacillariophyta; Coscinodiscophyceae; OC Thalassiosirophycidae; Thalassiosirales; Thalassiosiraceae; OC Thalassiosira. OX NCBI_TaxID=35128; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1335; RX PubMed=15459382; DOI=10.1126/science.1101156; RA Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D., RA Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., RA Brzezinski M.A., Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., RA Detter J.C., Glavina T., Goodstein D., Hadi M.Z., Hellsten U., RA Hildebrand M., Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., RA Lau W.W., Lane T.W., Larimer F.W., Lippmeier J.C., Lucas S., RA Medina M., Montsant A., Obornik M., Parker M.S., Palenik B., RA Pazour G.J., Richardson P.M., Rynearson T.A., Saito M.A., RA Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A., Wilkerson F.P., RA Rokhsar D.S.; RT "The genome of the diatom Thalassiosira pseudonana: ecology, RT evolution, and metabolism."; RL Science 306:79-86(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=CCMP1335; RG Diatom Consortium; RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., RA Detter J.C., Schmutz J., Lindquist E., Shapiro H., Lucas S., RA Glavina del Rio T., Bruce D., Pitluck S., Rokhsar D., Armbrust V.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000643; EED91667.1; -; Genomic_DNA. DR RefSeq; XP_002291560.1; XM_002291524.1. DR ProteinModelPortal; B8C465; -. DR STRING; 35128.JGI262963; -. DR EnsemblProtists; Thaps262963; Thaps262963; Thaps262963. DR GeneID; 7442738; -. DR KEGG; tps:THAPSDRAFT_262963; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome; Transferase. FT NON_TER 1 1 FT NON_TER 193 193 SQ SEQUENCE 193 AA; 20890 MW; BE83426DC8C5FC39 CRC64; ILPIVDTVEW IEQLVATPGI TDIQLRFKDT SDYATILDRI KRSQQLCKSA GVHLWINDHW KEAIEAGDCF GIHLGQEDMA ACGLEKIRSA GLAFGVSTHS YSELSAALGV YPSYISLGPV FQTASKDVKF DPQGLETVRQ WRRLIPANIP LVAIGGISNA DIAKVVREAG AECAAVIGAV TKAKDVKQSV EDL // ID B8CNV7_SHEPW Unreviewed; 527 AA. AC B8CNV7; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE SubName: Full=Phosphomethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase, putative; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=swp_2331; OS Shewanella piezotolerans (strain WP3 / JCM 13877). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=225849; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WP3 / JCM 13877; RX PubMed=18398463; DOI=10.1371/journal.pone.0001937; RA Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L., RA Bartlett D.H., Yu J., Hu S., Xiao X.; RT "Environmental adaptation: genomic analysis of the piezotolerant and RT psychrotolerant deep-sea iron reducing bacterium Shewanella RT piezotolerans WP3."; RL PLoS ONE 3:E1937-E1937(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000472; ACJ29076.1; -; Genomic_DNA. DR RefSeq; YP_002311663.1; NC_011566.1. DR ProteinModelPortal; B8CNV7; -. DR STRING; 225849.swp_2331; -. DR EnsemblBacteria; ACJ29076; ACJ29076; swp_2331. DR GeneID; 7033361; -. DR KEGG; swp:swp_2331; -. DR PATRIC; 23543202; VBIShePie65056_2142. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SPIE225849:GH6V-2275-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 527 AA; 56130 MW; 71E2ACA0EE1F450F CRC64; MAKVNSNPMP TRNRPIVWTI AGSDSGGGAG IQADLATIND LDAHGCSVIT AVTAQSSVTV ASVEAVSPQI LIAQLDVLTA DLAPQAIKIG LLANQQQINL VANWLHKILL QWRERGLTVA VILDPVMVAT CGDALTGSEA LDFTPFKGLL TLITPNVTEL ATLAGRQLIT PEQSVQAAQT LAAQLQVSVI AKGGDIGPNW DEGLARDLLV CHQVTGISSL HSEHAFWLTS NRINTNNNHG TGCTLSSAIA AVMAHGFVLN DAVVVAKAYV SQGLVQSYQP GSGPGCLARC GWPNTLSVYP FIQPLCEATA KTSSNNLNAC GFMKLTTQLG VYPVVAELDM LQQLLKAGVK TIQLRVKDPA DQLLEQKIVQ AIAFGRDYRA QVFINDHWQL AIKHHAFGVH LGQEDLVASN LKQLSEANIA LGLSSHSYFE ILLAMQHKPS YIAFGHIFPT TTKQMPSAPQ GLDKLARYVD LMQGELPLVA IGGIDSSTLA KVKKTGVDDI AVVRAVTEAV NPAAAYQALV KQWTEGE // ID B8DJ67_DESVM Unreviewed; 213 AA. AC B8DJ67; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=DvMF_3007; OS Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=883; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Miyazaki F / DSM 19637; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Hazen T.C., Richardson P.; RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001197; ACL09944.1; -; Genomic_DNA. DR RefSeq; YP_002437412.1; NC_011769.1. DR ProteinModelPortal; B8DJ67; -. DR STRING; 883.DvMF_3007; -. DR EnsemblBacteria; ACL09944; ACL09944; DvMF_3007. DR GeneID; 7174951; -. DR KEGG; dvm:DvMF_3007; -. DR PATRIC; 21776533; VBIDesVul86729_3261. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VTDRTLC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DVUL883:GCJ5-3085-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22095 MW; BD620855EDC92D9F CRC64; MRRNADYGVY LVTDRTLCRG RALTDVVTAA VAGGVTVVQL REKHVDTREF VELARALKAL LAPRGVPLLI NDRVDVALAC QADGVHVGQG DMHPADVRAL LGHSALVGLS VETMDQVREA ETLDVDYLGV SPVFATATKT DTAPPWGLDG LARLRAATGR TLVAIGGIGP ANAASVLAAG ADGLAVVSAL CAADDPGRAA EELRGSVRAV RGW // ID B8DL50_DESVM Unreviewed; 217 AA. AC B8DL50; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=DvMF_0797; OS Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=883; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Miyazaki F / DSM 19637; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Hazen T.C., Richardson P.; RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001197; ACL07753.1; -; Genomic_DNA. DR RefSeq; YP_002435221.1; NC_011769.1. DR ProteinModelPortal; B8DL50; -. DR STRING; 883.DvMF_0797; -. DR EnsemblBacteria; ACL07753; ACL07753; DvMF_0797. DR GeneID; 7172686; -. DR KEGG; dvm:DvMF_0797; -. DR PATRIC; 21771577; VBIDesVul86729_0837. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HRFYFIT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DVUL883:GCJ5-820-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22875 MW; 2757BA78AA6DE934 CRC64; MPRILPGSTP EADIYCLTDD GLSRGRSAVD VVDAMLRGGA RIVQYREKDK HAGEMLRECL ELRRMTREAG ACFIVNDHVD IAMLCDADGV HVGQEDLPVQ AVRQLVGPGR IIGLSTHSPE QARAAVASGA DYIGVGPIFA TRTKKDVCAP VGFEYLDWVV ANGTLPFVAI GGIKLHNIGQ VAAHGARCCA LVSEIVGADD VAARFAEARA AMGAAPG // ID B8DSX8_BIFA0 Unreviewed; 516 AA. AC B8DSX8; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE SubName: Full=ThiE-ThiD fusion protein; DE EC=2.5.1.3; GN Name=thiD; OrderedLocusNames=BLA_0815; OS Bifidobacterium animalis subsp. lactis (strain AD011). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=442563; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AD011; RX PubMed=19011029; DOI=10.1128/JB.01515-08; RA Kim J.F., Jeong H., Yu D.S., Choi S.H., Hur C.G., Park M.S., RA Yoon S.H., Kim D.W., Ji G.E., Park H.S., Oh T.K.; RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis RT subsp. lactis AD011."; RL J. Bacteriol. 191:678-679(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001213; ACL29107.1; -; Genomic_DNA. DR RefSeq; YP_002469683.1; NC_011835.1. DR ProteinModelPortal; B8DSX8; -. DR STRING; 442563.BLA_0815; -. DR EnsemblBacteria; ACL29107; ACL29107; BLA_0815. DR GeneID; 7264222; -. DR KEGG; bla:BLA_0815; -. DR PATRIC; 21104535; VBIBifAni98964_0849. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BANI442563:GHG0-810-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 516 AA; 54334 MW; BA2BECA74309264A CRC64; MNSFPYPSMR DRFDLRFYFV VGPDDCGNRP ILDVVAKALD GGASFIQLRA KTQDVAEIVS LANDIAEEIA GHHVEHSVAF VVDDRVDAAL EARAKGIKVD GVHIGQDDLD PVVARKLLGP DAIIGLSAKT VDEVREANHL PEGTIDYIGA GPLHMTATKP ESMIVDENGD ITTLNVSSID EMRTMSKYPL IVGGGVKADD IPMLAKTKAD GWFVVSAIAG ATDPEQATRR LVDDWTAIRG DEKPRYTGRK PAATKLPAVL TIATTDSSGG AGIPADLKTM LANDVFGECV VAGITAQNTT GVQAIAAVDP SIVGAQIDSV FDDIRPTAVK IGVIVGVESV KTVARKLRDH QATNIVVDPV MVATSGSSLA ADDTIAEEIS SLFPIATVIT PNIPEAQVLA QMPIGNQADM ETAAVQLAKD YGTCVLVKGG HGVKDADDVL AFPTGAVTWF EGERIANDNT HGTGCTLSSA IASYLAQGED LEDAVRDAKA YLSGALRANL NLGKGHGPMD HAWAMH // ID B8EA56_SHEB2 Unreviewed; 650 AA. AC B8EA56; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 46. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=Sbal223_2025; OS Shewanella baltica (strain OS223). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=407976; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS223; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., RA Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., RA Hauser L., Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., RA Konstantinidis K., Tiedje J.; RT "Complete sequence of chromosome of Shewanella baltica OS223."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001252; ACK46529.1; -; Genomic_DNA. DR RefSeq; YP_002357952.1; NC_011663.1. DR ProteinModelPortal; B8EA56; -. DR STRING; 407976.Sbal223_2025; -. DR EnsemblBacteria; ACK46529; ACK46529; Sbal223_2025. DR GeneID; 7086859; -. DR KEGG; sbp:Sbal223_2025; -. DR PATRIC; 23480272; VBISheBal125792_2093. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SBAL407976:GJ6Y-2102-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 650 AA; 68511 MW; 5AD81F72D86266AF CRC64; MLGIHGDNVP MNTERPAFVW TIAGSDSGGG AGIQADLATI QDLGCHGCSV VTTVTAQSSV AVTLVEPVSA AMLMAQLTTL LSDLPPKAIK IGLLADQTQV ALLADWIASF KIHYPSVPVI VDPVMVASCG DALAVDNCQD IKSAAKSALD FKHFKGLIEL ITPNVLELGR LTHSDVSTKA QFAAAALALS QSLDCSVLAK GGDVSFGSTD ILDDTHAQTH DNTYAQTQAN VHVIALDSNG WDLELAEDYL VCRQVRASSK LHQNGRFWLA SQRVNTRHNH GSGCTLSSAI AAVLAQGFVL QDAVVVAKAY VSQGLSAAIG LGQGPGPLAR TGWPNNLSRY AKINLCDGNF ISHQLNQHLD VLNDLVATVL SATDQATAQV KIASTPPQNI LSHGFKVLDA DLGVYPVVSD LTMLESLLAA GVKTVQLRIK TDSSESTAAA LAESDLGKSA LSRCESGKSK SGEPELIGSE LEAQIQTAIA LGKHFNAQLF INDHWRLAIK YHAFGVHLGQ EDLAVTDLAA IQAAGLALGI SSHSYFELLL AHQYSPSYIA LGHIFPTTTK QMPSAPQGLA KLKHYVALLQ GHYPLVAIGG IDLTNLAKVK ATGVGNIAVV RAITNAKDPL AAFAELSQAW EQCSLSEELA VNHELGAKHE // ID B8EQM1_METSB Unreviewed; 210 AA. AC B8EQM1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Msil_0313; OS Methylocella silvestris (strain BL2 / DSM 15510 / NCIMB 13906). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Beijerinckiaceae; Methylocella. OX NCBI_TaxID=395965; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BL2 / DSM 15510 / NCIMB 13906; RX PubMed=20472789; DOI=10.1128/JB.00506-10; RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B., RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.; RT "Complete genome sequence of the aerobic facultative methanotroph RT Methylocella silvestris BL2."; RL J. Bacteriol. 192:3840-3841(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001280; ACK49292.1; -; Genomic_DNA. DR RefSeq; YP_002360654.1; NC_011666.1. DR ProteinModelPortal; B8EQM1; -. DR STRING; 395965.Msil_0313; -. DR EnsemblBacteria; ACK49292; ACK49292; Msil_0313. DR GeneID; 7091531; -. DR KEGG; msl:Msil_0313; -. DR PATRIC; 22595897; VBIMetSil55537_0345. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; MSIL395965:GCND-318-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 210 AA; 22014 MW; 905B903A22D2ED32 CRC64; MPDDAPRLFL ITPRISEADS FAPQLAAALS VCDVACVLLR TQTRDPGDAK KIIKILAPIA QQRDVAVLVE GDPQLAVRAG ADGCHVEAGA EALQGALSSL KPDRIVGAGA LQSRDEAMSA GETGVDYLMF GGPDHPQPHE FVLERVAWWA EIFNIPCVAY AQTLGEAADF AEAGADFIAL ADAVFADPRG PTAAVADVAA ILATIREKAR // ID B8ESP7_METSB Unreviewed; 208 AA. AC B8ESP7; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Msil_1417; OS Methylocella silvestris (strain BL2 / DSM 15510 / NCIMB 13906). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Beijerinckiaceae; Methylocella. OX NCBI_TaxID=395965; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BL2 / DSM 15510 / NCIMB 13906; RX PubMed=20472789; DOI=10.1128/JB.00506-10; RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B., RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.; RT "Complete genome sequence of the aerobic facultative methanotroph RT Methylocella silvestris BL2."; RL J. Bacteriol. 192:3840-3841(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001280; ACK50382.1; -; Genomic_DNA. DR RefSeq; YP_002361744.1; NC_011666.1. DR ProteinModelPortal; B8ESP7; -. DR STRING; 395965.Msil_1417; -. DR EnsemblBacteria; ACK50382; ACK50382; Msil_1417. DR GeneID; 7091757; -. DR KEGG; msl:Msil_1417; -. DR PATRIC; 22598339; VBIMetSil55537_1547. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; MSIL395965:GCND-1442-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 21 25 HMP-PP binding (By similarity). FT REGION 170 171 THZ-P binding (By similarity). FT METAL 54 54 Magnesium (By similarity). FT METAL 73 73 Magnesium (By similarity). FT BINDING 53 53 HMP-PP (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 150 150 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22207 MW; D0EF49A14678864D CRC64; MIVDSSDWIA RLLPYGVKLV QLRAKDLSDE VLRKEIIRAR SLCEAGGAQL VVNDYWRHAI DLGCDFIHLG QEDLETADLK AIRQAGLKLG VSTHDEAELA RALETGPDYI ALGPIYPTIL KKMPFAPQGL ARIGEWKKRI GTIPLVAIGG ITLERAPGVL EAGADSAAVV TDITLNADPE ARARAWAAMA GGALRATDDS AASAGFPD // ID B8F7P2_HAEPS Unreviewed; 220 AA. AC B8F7P2; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HAPS_1839; OS Haemophilus parasuis serovar 5 (strain SH0165). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=557723; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH0165; RX PubMed=19074396; DOI=10.1128/JB.01682-08; RA Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R., RA Jin M., Jin Q., Chen H.; RT "Complete genome sequence of Haemophilus parasuis SH0165."; RL J. Bacteriol. 191:1359-1360(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001321; ACL33344.1; -; Genomic_DNA. DR RefSeq; YP_002476292.1; NC_011852.1. DR ProteinModelPortal; B8F7P2; -. DR STRING; 557723.HAPS_1839; -. DR EnsemblBacteria; ACL33344; ACL33344; HAPS_1839. DR GeneID; 7278685; -. DR KEGG; hap:HAPS_1839; -. DR PATRIC; 20196001; VBIHaePar127548_1820. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HPAR557723:GH24-1839-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23959 MW; 9CE411A9AF75619B CRC64; MFQRELLSVY FVAGTQDCLH LPTGSPEQKL LSTLETALQA GITCYQFREK GESALQDKQA QWQLARDCQA LCRQYGVPFV LNNDVEMAVK LGADGVHIGQ KDMAAIQAIQ LTQGKLFLGI SNSSLNDLQN SFRLPEIDYW AVGAIFNTQS KLDAMQNVGI DLIRQAKQLN PNQPLVAIGG ISVDNVASIW AAGADGVAVI SAITQADNVM QTVQKLKTTY // ID B8FB00_DESAA Unreviewed; 208 AA. AC B8FB00; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dalk_2393; OS Desulfatibacillum alkenivorans (strain AK-01). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfatibacillum. OX NCBI_TaxID=439235; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK-01; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Wawrik B., Richardson P.; RT "Complete sequence of Desulfatibacillum alkenivorans AK-01."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001322; ACL04086.1; -; Genomic_DNA. DR RefSeq; YP_002431554.1; NC_011768.1. DR ProteinModelPortal; B8FB00; -. DR STRING; 439235.Dalk_2393; -. DR EnsemblBacteria; ACL04086; ACL04086; Dalk_2393. DR GeneID; 7166325; -. DR KEGG; dal:Dalk_2393; -. DR PATRIC; 21651424; VBIDesAlk8144_2567. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HRFYFIT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DALK439235:GHP2-2418-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22749 MW; B5ED56861E23E7FB CRC64; MDKPYGLYLI LTNPVAGYEA CAWAAVNQGL RYLQLRMKHA PREEILEKAL SLREITKGSK TLFIVNDHVD IAKEADADGV HLGQEDMSLE EARSMWTAPG KQFGLSTHGV EQELAARDLQ PDYIGVGPVF PTPTKDKPDP TVGLEAMGRI IKGSPLSCVA IGGINPENLP QVLEHGAGNF SVVRAVNQSH DPESAIANLM DVWRKHYP // ID B8FI90_DESAA Unreviewed; 212 AA. AC B8FI90; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dalk_0954; OS Desulfatibacillum alkenivorans (strain AK-01). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfatibacillum. OX NCBI_TaxID=439235; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK-01; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Wawrik B., Richardson P.; RT "Complete sequence of Desulfatibacillum alkenivorans AK-01."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001322; ACL02657.1; -; Genomic_DNA. DR RefSeq; YP_002430125.1; NC_011768.1. DR ProteinModelPortal; B8FI90; -. DR STRING; 439235.Dalk_0954; -. DR EnsemblBacteria; ACL02657; ACL02657; Dalk_0954. DR GeneID; 7164867; -. DR KEGG; dal:Dalk_0954; -. DR PATRIC; 21648270; VBIDesAlk8144_1009. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DALK439235:GHP2-960-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). SQ SEQUENCE 212 AA; 22350 MW; 73D9908B229BB350 CRC64; MKKSIDYSLY LVTDRPLSLG RSLMEVMEKA AAGGTTIVQL REKECDSRTF VELARAAKKL LDAKGVPLII NDRADIALAV GAAGLHIGQT DMPYQDARRI MGPEAIVGLS VENRDQVKEA ASLDADYLGV GPIFATQTKP DAAPAIGLEG LAEIRTITKT PLIAIGSVNL SNAAEVIRAG ADGLAVVSAI CSQPDIEQAS RNLAAAIQKA RQ // ID B8G7I9_CHLAD Unreviewed; 221 AA. AC B8G7I9; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cagg_3166; OS Chloroflexus aggregans (strain MD-66 / DSM 9485). OC Bacteria; Chloroflexi; Chloroflexales; Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=326427; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MD-66 / DSM 9485; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Foster B., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.; RT "Complete sequence of Chloroflexus aggregans DSM 9485."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001337; ACL26024.1; -; Genomic_DNA. DR RefSeq; YP_002464460.1; NC_011831.1. DR ProteinModelPortal; B8G7I9; -. DR STRING; 326427.Cagg_3166; -. DR EnsemblBacteria; ACL26024; ACL26024; Cagg_3166. DR GeneID; 7269915; -. DR KEGG; cag:Cagg_3166; -. DR PATRIC; 21409008; VBIChlAgg85409_3270. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CAGG326427:GHS8-3210-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 22955 MW; 0F531D598854B0AB CRC64; MALRQAVDWS LYVVTDAGLS RGRSHVAVIE AAITGGATVV QYREKHAPTR QMVAEAQVLR ELTRRTGVPL IVNDRLDVAL AVDADGVHLG QDDMPAALAR RLIGPDKILG ISASTLAEAL QAVQDGADYL GVGPIFATPT KPDAAPPIGI DGLRLIRQHV SLPIVAIGGI NATNAAEVMA AGPDGIAVVS AVVAAEDIAV AAQELRAMVN ASRQRREAAS N // ID B8GJF8_METPE Unreviewed; 209 AA. AC B8GJF8; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mpal_1691; OS Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c). OC Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales; OC Methanoregulaceae; Methanosphaerula. OX NCBI_TaxID=521011; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Lu M., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G.O., Zinder S.; RT "Complete sequence of Candidatus Methanosphaerula E1-9c."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001338; ACL16999.1; -; Genomic_DNA. DR RefSeq; YP_002466722.1; NC_011832.1. DR ProteinModelPortal; B8GJF8; -. DR STRING; 521011.Mpal_1691; -. DR EnsemblBacteria; ACL16999; ACL16999; Mpal_1691. DR GeneID; 7271254; -. DR KEGG; mpl:Mpal_1691; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; MPAL521011:GI2F-1736-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21142 MW; CCE8DC22A47D60BA CRC64; MPYSLYVVTD PDLSLGRSHA EVAALAVAGG ADVIQLRDKS ASGRDLFAAA ELIRTITTSA GALFIVNDRL DIALASGADG VHLGQDDLPV RAARKVAPDL IIGVSVGSVE EGRRAVVDGA DYVALSPLFS TPSKIDAGAG RGFDLLAALC DDLTVPVLAI GGINASNVSQ VIRAGAAGVA VISAVVSQPD ISKATSGLKS IILEAKKSV // ID B8GMP1_THISH Unreviewed; 317 AA. AC B8GMP1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 13-NOV-2013, entry version 43. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=Tgr7_0781; OS Thioalkalivibrio sp. (strain HL-EbGR7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thioalkalivibrio. OX NCBI_TaxID=396588; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HL-EbGR7; RX PubMed=21475584; RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., RA Ivanova N., Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.; RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL- RT EbGr7."; RL Stand. Genomic Sci. 4:23-35(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001339; ACL71873.1; -; Genomic_DNA. DR RefSeq; YP_002512860.1; NC_011901.1. DR ProteinModelPortal; B8GMP1; -. DR STRING; 396588.Tgr7_0781; -. DR EnsemblBacteria; ACL71873; ACL71873; Tgr7_0781. DR GeneID; 7315042; -. DR KEGG; tgr:Tgr7_0781; -. DR PATRIC; 23961044; VBIThiSp19295_0781. DR eggNOG; COG0494; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TSUL396588:GH5B-784-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 317 AA; 34388 MW; B0E3CF7B982DF58C CRC64; MSNHSLPVQV AVAAIINAHD EVLIARRPEG VHQGGLWEFP GGKMEPGETL DQALARELRE ELGIAPLRSR PLITIHHDYG DKRVCLRVCR VESFSGVPHG REGQPLRWVS VGALQAFEFP AANRPIISAL QLPDRYLITP DPGTQTAAFI KYLERRLSAG DVTLLQLRAP SLDEQAYSTL AAEVIALARD LGLRVLLNAE VSTARQLGAH GVHLNGLRLS RWSAQQTEGL LVSASVHDET QLTQARGADF IVVSPVMATA SHPDATPIGW TGFQDLAERA AMPVYALGGM SVDDIERARL HGGQGIAAIR GLWEMKP // ID B8GW24_CAUCN Unreviewed; 206 AA. AC B8GW24; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 2. DT 14-MAY-2014, entry version 38. DE SubName: Full=Thiamine monophosphate synthase TenI; GN OrderedLocusNames=CCNA_03862; OS Caulobacter crescentus (strain NA1000 / CB15N). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=565050; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NA1000 / CB15N; RX PubMed=20472802; DOI=10.1128/JB.00255-10; RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V., RA Walunas T.L., Crosson S.; RT "The genetic basis of laboratory adaptation in Caulobacter RT crescentus."; RL J. Bacteriol. 192:3678-3688(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001340; ACL97327.2; -; Genomic_DNA. DR RefSeq; YP_002519235.2; NC_011916.1. DR ProteinModelPortal; B8GW24; -. DR STRING; 190650.CC_3746; -. DR EnsemblBacteria; ACL97327; ACL97327; CCNA_03862. DR GeneID; 7332710; -. DR KEGG; ccs:CCNA_03862; -. DR PATRIC; 21312213; VBICauCre52860_3767. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INERSDI; -. DR OrthoDB; EOG699751; -. DR BioCyc; CAULONA1000:CCNA_03862-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 21498 MW; 44350F621125CBC6 CRC64; MDGENELEVL SRAASAFPPR TVRGMALPRL LFFTDPARIT DPEAVAERLP PGSAIVFRAF GATDAVEQGR RLRAIATARD LMLLVGAHAG LAEGVGADGV HLPERMAANL PRLRAEHPRY LVTVAAHDLA AVQTAERSGA DAVVVSPVFP SNSPSAGEPL GLEGLMRLVE ATALPVYALG GVRAHTVDQL FDSGVAGIAA VEALAR // ID B8H4L4_CAUCN Unreviewed; 214 AA. AC B8H4L4; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CCNA_03373; OS Caulobacter crescentus (strain NA1000 / CB15N). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=565050; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NA1000 / CB15N; RX PubMed=20472802; DOI=10.1128/JB.00255-10; RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V., RA Walunas T.L., Crosson S.; RT "The genetic basis of laboratory adaptation in Caulobacter RT crescentus."; RL J. Bacteriol. 192:3678-3688(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001340; ACL96838.1; -; Genomic_DNA. DR RefSeq; YP_002518746.1; NC_011916.1. DR ProteinModelPortal; B8H4L4; -. DR SMR; B8H4L4; 27-198. DR STRING; 190650.CC_3264; -. DR EnsemblBacteria; ACL96838; ACL96838; CCNA_03373. DR GeneID; 7332047; -. DR KEGG; ccs:CCNA_03373; -. DR PATRIC; 21311235; VBICauCre52860_3287. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CAULONA1000:CCNA_03373-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22241 MW; 9C085C0B9A8C19DE CRC64; MTLDCRLYLI TPPALTDLAD FGRQLARALE GGDVAALQIR LKDAPDDLVA AAVDVLGPIA QARDVAVILN DRPDLAARLP VDGVHVGQSD MACRDARKLM GDRMVGVTCH DSRHLAMEAA EAGADYVAFG AFFPTSTKDA PTRAEPDILT IWQETMETPC VAIGGITVEN ASGLATAGAD FLAVSAGVWS YAQGPDAAVA ALNAAIAEGL AARK // ID B8HBT0_ARTCA Unreviewed; 240 AA. AC B8HBT0; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Achl_2503; OS Arthrobacter chlorophenolicus (strain A6 / ATCC 700700 / DSM 12829 / OS JCM 12360). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=452863; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A6 / ATCC 700700 / DSM 12829 / JCM 12360; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Jansson J., RA Richardson P.; RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus RT A6."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001341; ACL40468.1; -; Genomic_DNA. DR RefSeq; YP_002488557.1; NC_011886.1. DR ProteinModelPortal; B8HBT0; -. DR STRING; 452863.Achl_2503; -. DR EnsemblBacteria; ACL40468; ACL40468; Achl_2503. DR GeneID; 7293978; -. DR KEGG; ach:Achl_2503; -. DR PATRIC; 20991643; VBIArtChl38304_3190. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ACHL452863:GH1A-2555-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 61 65 HMP-PP binding (By similarity). FT REGION 163 165 THZ-P binding (By similarity). FT METAL 94 94 Magnesium (By similarity). FT METAL 113 113 Magnesium (By similarity). FT BINDING 93 93 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 166 166 HMP-PP (By similarity). FT BINDING 195 195 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 240 AA; 24325 MW; 3539A1E28CC53846 CRC64; MNVSHSPAPA AAPGTDAFTT GAGNGALKSA RLYLCTDARS ARGDFAEFVD AAFEGGVDII QLRDKAIEAA EELDLLAALK EAAQRHGRLW AVNDRADIAV LSGAPVFHVG QKDLPVQAAR TLLNGNAAIG LSSHTPEQVD AALADAAGPA GLDYFCVGPL WATPTKPGRA AVGLDLVKYA AAKAPSDVPW FAIGGIDHSN VDQVVAAGAS RIVVVRAITD AADPAAAAAS LRSALGTAVS // ID B8HY75_CYAP4 Unreviewed; 346 AA. AC B8HY75; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cyan7425_2521; OS Cyanothece sp. (strain PCC 7425 / ATCC 29141). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=395961; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7425 / ATCC 29141; RX PubMed=21972240; DOI=10.1128/mBio.00214-11; RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., RA Min H., Sherman L.A., Pakrasi H.B.; RT "Novel metabolic attributes of the genus Cyanothece, comprising a RT group of unicellular nitrogen-fixing Cyanobacteria."; RL MBio 2:E214-E214(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001344; ACL44878.1; -; Genomic_DNA. DR RefSeq; YP_002483239.1; NC_011884.1. DR ProteinModelPortal; B8HY75; -. DR STRING; 395961.Cyan7425_2521; -. DR EnsemblBacteria; ACL44878; ACL44878; Cyan7425_2521. DR GeneID; 7288452; -. DR KEGG; cyn:Cyan7425_2521; -. DR PATRIC; 21566005; VBICyaSp30657_2516. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CSP395961:GJDE-2347-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 122 Unknown (By similarity). FT REGION 123 346 Thiamine-phosphate synthase (By FT similarity). FT REGION 170 174 HMP-PP binding (By similarity). FT REGION 267 269 THZ-P binding (By similarity). FT METAL 203 203 Magnesium (By similarity). FT METAL 222 222 Magnesium (By similarity). FT BINDING 202 202 HMP-PP (By similarity). FT BINDING 241 241 HMP-PP (By similarity). FT BINDING 270 270 HMP-PP (By similarity). FT BINDING 297 297 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 346 AA; 38180 MW; 9A9BA2AEEFEF7B48 CRC64; MISPNPALYR ILDANLDRAR EGLRVVEEWC RFGLENATLT ECCKNLRQQL ARWHHPELRS ARNTPTDPGT SLTHPQEEQR TDLTALLQAN FGRVQEALRV LEEYGKLYNP ALAEESKQMR YQVYSLESQL LPPARQQKLR QSPLYLVTSP SDHLFTVVEQ ALQGGLTLVQ YRDKTTDDGI RFERAAKLCH LCHQYNALFL VNDRVDLALA VNADGVHLGQ QDLPLAVARQ LLGPDRIIGQ STTNPTEMAQ AIAAGADYIG VGPVYATPTK AGKAPAGLEY VRYAASHAPL PWYAIGGIDL TNVADVLAAG ARGVAVVRAL MEAESPEQVT RSFLSQFNRS STAVPE // ID B8IHD4_METNO Unreviewed; 231 AA. AC B8IHD4; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mnod_4969; OS Methylobacterium nodulans (strain ORS2060 / LMG 21967). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=460265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ORS2060 / LMG 21967; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Marx C.J., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium nodulans ORS RT 2060."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001349; ACL59826.1; -; Genomic_DNA. DR RefSeq; YP_002500129.1; NC_011894.1. DR ProteinModelPortal; B8IHD4; -. DR STRING; 460265.Mnod_4969; -. DR EnsemblBacteria; ACL59826; ACL59826; Mnod_4969. DR GeneID; 7307529; -. DR KEGG; mno:Mnod_4969; -. DR PATRIC; 22551774; VBIMetNod76414_5585. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTLLQYR; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MNOD460265:GCZK-5021-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 231 AA; 23477 MW; 5FD015303EA18532 CRC64; MDTCPIVPVD LRLYGILDVG VSGGDGAQLA RMARDAAAGG CTLLQYREKA VSNARTSLER IRAIHAALAG TGVPLLVNDR VDLALAAGVE GVHLGQEDLH PADARRLLGP KAIIGLTLKT GAQADELYRL PVNYACIGGV FATTSKVNPD PPVGLEGLAR IVFRARLARG AALPVGAIAG IDRSNAAAVI GAGADGIALV SALFGAPEVV EARARDLRGI VDGALAARGA A // ID B8ILP6_METNO Unreviewed; 234 AA. AC B8ILP6; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN OrderedLocusNames=Mnod_7282; OS Methylobacterium nodulans (strain ORS2060 / LMG 21967). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=460265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ORS2060 / LMG 21967; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Marx C.J., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium nodulans ORS RT 2060."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001349; ACL62021.1; -; Genomic_DNA. DR RefSeq; YP_002502324.1; NC_011894.1. DR ProteinModelPortal; B8ILP6; -. DR STRING; 460265.Mnod_7282; -. DR EnsemblBacteria; ACL62021; ACL62021; Mnod_7282. DR GeneID; 7305255; -. DR KEGG; mno:Mnod_7282; -. DR PATRIC; 22556257; VBIMetNod76414_7794. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; MNOD460265:GCZK-7366-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 234 AA; 24133 MW; 489A54E39003CFF3 CRC64; MDSSRKRSTG NHLNIAPPTP RMTDPQTRLV LITGPEAGPD LAERLAAACR AGDVAAVILR LAPADERSLV KRVKDLAPSA QEAGAAVLVA CDAPGVDPVA IAARGGADGV HALADEEPGD ALRDLRERLR DGRILGAGTL RSRHAAMEAG EAGADYVLFG DAEPASRESV RAQAAWWAEI FETPCVAVAR SLDAVAELAA TGAEFVALDP ALWDGPDAAA TVAAAQERLA GARP // ID B8IPG0_METNO Unreviewed; 232 AA. AC B8IPG0; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mnod_7515; OS Methylobacterium nodulans (strain ORS2060 / LMG 21967). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=460265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ORS2060 / LMG 21967; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Marx C.J., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium nodulans ORS RT 2060."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001349; ACL62252.1; -; Genomic_DNA. DR RefSeq; YP_002502555.1; NC_011894.1. DR ProteinModelPortal; B8IPG0; -. DR STRING; 460265.Mnod_7515; -. DR EnsemblBacteria; ACL62252; ACL62252; Mnod_7515. DR GeneID; 7303560; -. DR KEGG; mno:Mnod_7515; -. DR PATRIC; 22556705; VBIMetNod76414_8015. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VITDWRL; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MNOD460265:GCZK-7602-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 133 135 THZ-P binding (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 232 AA; 23498 MW; 1AAA57FED365856E CRC64; MNGLPARLLL VTDRHGSDLP LLRRVGAALE AGARWIWLRD RDLPEAERAA LAADLARLVR GAGGRLTIGR DVDLAARIGA DGVQLASAAV VAEARARLGP GALIGLSAHR LAEIAAAREA GADYATLSPI FASASKPGYG PALGPAALAQ AARTGLPVIA LGGVEPGTAP ACLAAGAAGV AVMGGVMRAA DPGAAVQALL KAMAREPRDP LFRVGEGYGD RRSHVRVPDP SE // ID B8J2N7_DESDA Unreviewed; 211 AA. AC B8J2N7; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ddes_0209; OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=525146; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27774 / DSM 6949; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., RA Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., RA Kyrpides N., Ovchinnikova G., Hazen T.C.; RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans RT str. ATCC 27774."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001358; ACL48125.1; -; Genomic_DNA. DR RefSeq; YP_002478803.1; NC_011883.1. DR ProteinModelPortal; B8J2N7; -. DR STRING; 525146.Ddes_0209; -. DR EnsemblBacteria; ACL48125; ACL48125; Ddes_0209. DR GeneID; 7283863; -. DR KEGG; dds:Ddes_0209; -. DR PATRIC; 21733738; VBIDesDes50650_0255. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DDES525146:GIWF-212-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22652 MW; 98FEB3BC9D62B188 CRC64; MPRILPGETD IYAITDSRLS LGRSLEEVAS ALLGAGVRLL QYREKNFKGG EMLEECRLLR RLTREAGACF IVNDHVDIAM LVDADGVHVG QEDLPVPEVR RLVGPDMIIG LSTHEPDQAL AARALGADYL GVGPIFATQT KEDVVAPVGF GYLDWVAANI DMPFVAIGGI KAHNIAEVAR HGARCCSLVS ELVGAPDIAA RVDAVRRAMR G // ID B8J7W0_ANAD2 Unreviewed; 222 AA. AC B8J7W0; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=A2cp1_0093; OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=455488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-1 / ATCC BAA-258; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Beliaev A.S., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001359; ACL63452.1; -; Genomic_DNA. DR RefSeq; YP_002490518.1; NC_011891.1. DR ProteinModelPortal; B8J7W0; -. DR STRING; 455488.A2cp1_0093; -. DR EnsemblBacteria; ACL63452; ACL63452; A2cp1_0093. DR GeneID; 7299735; -. DR KEGG; acp:A2cp1_0093; -. DR PATRIC; 20906969; VBIAnaDeh28364_0088. DR eggNOG; NOG133055; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HRFYFIT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ADEH455488:GH35-95-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 21976 MW; 9BAEE2CE20AA6C14 CRC64; MPVSEASVGA GRRARLGGLY VIVGGADPVA QAHAAIGGGA RAVQVRMKDA PAGAVLEATR RILALAAGRA LVLVNDRADL ALLAGADGVH LGDDDLPVPE ARRLLGPDLL VGRTTRTLEE ARAALAEGAD HVGYGPIFAS RSKALPVPPR GLQALAEVAR ALPAPVVAIG GIGLDDVGAV ARAGAACAAV IEAVVGAADP EAAAARMQAA FEAGRAARGA NP // ID B8JH77_ANAD2 Unreviewed; 203 AA. AC B8JH77; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=A2cp1_1435; OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=455488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-1 / ATCC BAA-258; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Beliaev A.S., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001359; ACL64779.1; -; Genomic_DNA. DR RefSeq; YP_002491845.1; NC_011891.1. DR ProteinModelPortal; B8JH77; -. DR STRING; 455488.A2cp1_1435; -. DR EnsemblBacteria; ACL64779; ACL64779; A2cp1_1435. DR GeneID; 7299956; -. DR KEGG; acp:A2cp1_1435; -. DR PATRIC; 20909730; VBIAnaDeh28364_1458. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ADEH455488:GH35-1451-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 134 136 THZ-P binding (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 20651 MW; 0A65C1DD7D76E264 CRC64; MEVPVVHLIT DRRLASSLPA RAAAALRGLP PGIAAIHLRE KDLCGLDLLR LARALAAVCR DAGQRLLVND RLDVALAAGA DGVHLPSAGI SPVDARRLLG PAALLGVSCH SEADVVRARA GGASFATFGP VYDTPSKRPY GAPVGVGALR EAARLGLPLV ALGGVDPSRV AEVRAAGARG VAAIRAWLTG DDPAGAVRAL LGR // ID B8KBM8_9VIBR Unreviewed; 471 AA. AC B8KBM8; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 16-OCT-2013, entry version 33. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=VPMS16_2072; OS Vibrio sp. 16. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=391586; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=16; RA Edwards R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999349; EED25806.1; -; Genomic_DNA. DR ProteinModelPortal; B8KBM8; -. DR EnsemblBacteria; EED25806; EED25806; VPMS16_2072. DR PATRIC; 28337554; VBIVibPar22686_2993. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 471 AA; 52636 MW; 1B4437796BBB63D0 CRC64; MSKILIPSSL IELTGLVQEC LLLAKGQGFS IEDIELGISP TQSIQLVRDQ QTTHITTDLI DGYDSYRECS FTLYYCSALS VEACAKQPSK AIYIGIADTQ LSDKKENVLQ LDIWRHPINN EVRALSVKSK LNAMFNPEHH LAWIVTLTVL DFPIEDALTL ARGMLTQQAN VSRETLLNDN LDEGRPTQWA DQFDDFPTPV LEDNRLGIQV GWSAQGESVR FPSLTKQSLG LYPVVDDVAW IERLLPLGIN TIQLRIKNQQ QADLEQQIIR AIELGRQYQA QVFINDYWQL AIKHSAYGVH LGQEDIEESN LAQLTKAGIR LGLSTHGYYE LLRIVQIHPS YIALGHIFPT TTKQMPSKPQ GLVRLALYQK LIDSIPYTNT EAAFRPAKDK AVSDYVLGFP TVAIGGIDQS NAGQVWQTGV SSLAVVRAIT LAESPKSVIE FFAQLMKERQ LTFADQNSEL THTKRGEHAH G // ID B8L0R1_9GAMM Unreviewed; 308 AA. AC B8L0R1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 16-OCT-2013, entry version 34. DE SubName: Full=Dgtp-pyrophosphohydrolase; GN ORFNames=SSKA14_2781; OS Stenotrophomonas sp. SKA14. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=391601; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SKA14; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999412; EED39763.1; -; Genomic_DNA. DR ProteinModelPortal; B8L0R1; -. DR EnsemblBacteria; EED39763; EED39763; SSKA14_2781. DR PATRIC; 30950250; VBISteSp70125_3675. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 308 AA; 33920 MW; 6CD4138EBD73641D CRC64; MAAVITDARG RVLLNRRTEN RDMAGLWEFP GGKRESGETS EQALVRELRE ELGIEADVGE WLMDVPQRYP DKHLTLEVRH VRSWKGTPRG REGQAITWVA PDKLGRYSMP PADLPVVAAL RQPDSYLITP APEDDASSVQ QWHDQLQRAV AAGQQRIQLR LPPAHPQRQA MVEQVVRAHR RSGVQWLLNR DIELARALSV GVHLGSEQLQ QLSQRPLPEG QLVAASCHDL QQLQAAQQLG CDFAVLGPVQ ATASHPDATP LGWDAFAELR AQVSLPIYAL GGMGSGHITE ARRHGGQGIA AIRGLWPA // ID B8L3T6_9GAMM Unreviewed; 208 AA. AC B8L3T6; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSKA14_136; OS Stenotrophomonas sp. SKA14. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=391601; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SKA14; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999412; EED37130.1; -; Genomic_DNA. DR ProteinModelPortal; B8L3T6; -. DR EnsemblBacteria; EED37130; EED37130; SSKA14_136. DR PATRIC; 30944247; VBISteSp70125_0569. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21112 MW; C4829E0F2028CD05 CRC64; MTSASPAPRG VYLITPDEPD TARLLVRTAP LLAAGATWLQ YRNKTASDAL RLEQARALQG LCAAHGVPLI INDDPLLAKA VGAAGVHLGG TDGDIPSARA LLGAEAIIGA SCYDQLANAE KAVAAGASYV AFGAFFPTTT KITTSRAHPD LLRQSAALGV PRVAIGGLTP DNVGPIIDAG ADLVAVVSSV FAAEDPVATQ HALLAQFA // ID B8LCR1_THAPS Unreviewed; 323 AA. AC B8LCR1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 21. DE SubName: Full=Predicted protein; GN ORFNames=THAPSDRAFT_10468; OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana). OC Eukaryota; Stramenopiles; Bacillariophyta; Coscinodiscophyceae; OC Thalassiosirophycidae; Thalassiosirales; Thalassiosiraceae; OC Thalassiosira. OX NCBI_TaxID=35128; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1335; RX PubMed=15459382; DOI=10.1126/science.1101156; RA Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D., RA Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., RA Brzezinski M.A., Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., RA Detter J.C., Glavina T., Goodstein D., Hadi M.Z., Hellsten U., RA Hildebrand M., Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., RA Lau W.W., Lane T.W., Larimer F.W., Lippmeier J.C., Lucas S., RA Medina M., Montsant A., Obornik M., Parker M.S., Palenik B., RA Pazour G.J., Richardson P.M., Rynearson T.A., Saito M.A., RA Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A., Wilkerson F.P., RA Rokhsar D.S.; RT "The genome of the diatom Thalassiosira pseudonana: ecology, RT evolution, and metabolism."; RL Science 306:79-86(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=CCMP1335; RG Diatom Consortium; RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., RA Detter J.C., Schmutz J., Lindquist E., Shapiro H., Lucas S., RA Glavina del Rio T., Bruce D., Pitluck S., Rokhsar D., Armbrust V.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999417; EED86944.1; -; Genomic_DNA. DR RefSeq; XP_002296743.1; XM_002296707.1. DR ProteinModelPortal; B8LCR1; -. DR STRING; 35128.JGI10468; -. DR EnsemblProtists; Thaps10468; Thaps10468; Thaps10468. DR GeneID; 7450028; -. DR KEGG; tps:THAPSDRAFT_10468; -. DR eggNOG; COG0352; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 323 AA; 35363 MW; 3509A22647A6FAB0 CRC64; MLSSVIIALL SSYILTVYGF VPSPVSLSHP SSSSRSASHQ LMAHHYDDTS PPSHQSSSFP WAHPPYIALL TEPDACDSDK RVEKSIQAIT LATIDGGVDL VVVRVADVDC AETSTEATNT NRWTLLQSLA ELKQTRQQEN RNFLLIINND VDLAIQALSK NIAIDGVHVK ERNALLIPTI RQQLRDATTP SHTDHIIIGT SCHSVESASK SYQLSPRGPD YLFVGTCYLT QSHPEKSSAD QLEGPRLPGE VKRTLHRLQR DTNSDVPPPI IFALGGIDEH NCEDPVVKYG ADGVGVIRSV MQAEDPQRVV QSMKNAMQGT IKE // ID B8M2M4_TALSN Unreviewed; 521 AA. AC B8M2M4; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 16-APR-2014, entry version 25. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative; GN ORFNames=TSTA_091760; OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / OS NRRL 1006) (Penicillium stipitatum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces. OX NCBI_TaxID=441959; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006; RA Fedorova N.D., Joardar V.S., Maiti R., Schobel S., Amedeo P., RA Galens K., Inman J.M., Galinsky K.J., White O.R., Whitty B.R., RA Wortman J.R., Nierman W.C.; RT "Genome sequence of Talaromyces stipitatus strain ATCC 10500."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ962653; EED21935.1; -; Genomic_DNA. DR RefSeq; XP_002478898.1; XM_002478853.1. DR ProteinModelPortal; B8M2M4; -. DR GeneID; 8098562; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 521 AA; 54798 MW; 146C1708D38F951F CRC64; MTLDLSLYLV TDSTSAILGS RDIYKVVEEA CKGGVTIVQY RDKTSDTGLL VETATRLHEI TKRYNVPLII NDRVDVAMAS GAEGVHLGQD DMSITAAKKI LSKDAIVGIS ASSVEEAVKA VEEGADYLGI GTLFATPTKT NTKNIIGTAG VKTILDSISR LNRTVGTVAI GGINLSNVQR VLYQSAGQNK ALDGVAIVSA IIAADDPKSV AEQFKQAIAI PPPFITGSPE ISSSVDAGAL AAAVPEVVQK VVNCHPIVHS MINFVVANFV ANVAISAGLS PIMSQYGDEA KDLAVHRGGL VINMGTLTSA SIGEYLKAIK AYNTNGNPVV LDPVGAGATA IRRDAVKTLM AGGYFDLIKG NEREIRQVYG NTSNLTQRGV DSGPSSLNDV EKATLARDLA RRERNIVLLT GAVDYLSDGY RVIAVKNGHE LLSKATGTGC AIGTVCGAYM AAYRDDKFLA VLAGLLMYEI AAENAAAKNT VHGPGSFLPA FLDEVHSIWG KASQGNVTWA HGRAKIEEIQ L // ID B8NBM7_ASPFN Unreviewed; 519 AA. AC B8NBM7; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 16-APR-2014, entry version 33. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative; GN ORFNames=AFLA_046020; OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM OS 12722 / SRRC 167). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=332952; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167; RA Payne W.G.A., Dean R.A., Nierman W.C., Amedeo P., Caler E.G.A., RA Fedorova N.D., Maiti R., Joardar V., Inman J., Galinsky K.J., Yu J., RA Bhatnagar D., Cleveland T.E.; RT "Genome sequence of Aspergillus flavus strain NRRL 3357."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ963476; EED52900.1; -; Genomic_DNA. DR RefSeq; XP_002378064.1; XM_002378023.1. DR ProteinModelPortal; B8NBM7; -. DR STRING; 5059.CADAFLAP00005929; -. DR EnsemblFungi; CADAFLAT00005929; CADAFLAP00005929; CADAFLAG00005929. DR GeneID; 7914495; -. DR KEGG; afv:AFLA_046020; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 519 AA; 54957 MW; 3858C5DE999ABFDC CRC64; MPLNLSLYLV TDSTPAILKG RDLCTVVEEA LKGGVTIVQY RDKKSDTGEQ IQTAKKLHQI TQKYGVPLLI NDRVDVALAA GVEGVHLGQD DMAIEQAKQL LPKDAIIGIT AASIEEAQKA IDAGADYLGI GTMFATPTKT NTKHIIGTAG TQAILDAISD TGRSVGTVSI GGINLSNVQR VLYQSRAPRK ELDGVAIVSA IIAADDPKAA AAEFVKRIAT PPPFVRAPAA PQIREVAALQ EEVPKIVQKV VQAHPLVHNM INFVVANFVA NVALSMGASP IMAPHGDEAV DLAQFDGGLV VNMGTLTSES VPNYVKAIKA YNERGNPVVY DPVGAPATHI RRGAVKQLMA GGYFDLIKGN EGEIRQVFGS SGVIQRGVDS GPSRLDGQAK AILVRDLARR EHNLVLLTGA VDYLSDGERV IAVENGHELL GQVTGTGCAV GTVSGCFLTG HPSDRLLAVL SGILMYEIAA ENAASKEYVR GPGSFVPAFL DELYAIRQAA LKGDHSWFTG RAKIQMIDL // ID B8P3I8_POSPM Unreviewed; 525 AA. AC B8P3I8; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 16-APR-2014, entry version 28. DE SubName: Full=Predicted protein; GN ORFNames=POSPLDRAFT_88528; OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus) OS (Poria monticola). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Polyporales; Postia. OX NCBI_TaxID=561896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 44394 / Madison 698-R; RX PubMed=19193860; DOI=10.1073/pnas.0809575106; RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M., RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., RA Kersten P., Hammel K.E., Vanden Wymelenberg A., Gaskell J., RA Lindquist E., Sabat G., Splinter BonDurant S., Larrondo L.F., RA Canessa P., Vicuna R., Yadav J., Doddapaneni H., Subramanian V., RA Pisabarro A.G., Lavin J.L., Oguiza J.A., Master E., Henrissat B., RA Coutinho P.M., Harris P., Magnuson J.K., Baker S.E., Bruno K., RA Kenealy W., Hoegger P.J., Kuees U., Ramaiya P., Lucas S., Salamov A., RA Shapiro H., Tu H., Chee C.L., Misra M., Xie G., Teter S., Yaver D., RA James T., Mokrejs M., Pospisek M., Grigoriev I.V., Brettin T., RA Rokhsar D., Berka R., Cullen D.; RT "Genome, transcriptome, and secretome analysis of wood decay fungus RT Postia placenta supports unique mechanisms of lignocellulose RT conversion."; RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ966248; EED84533.1; -; Genomic_DNA. DR RefSeq; XP_002470230.1; XM_002470185.1. DR ProteinModelPortal; B8P3I8; -. DR STRING; 104341.JGI88528; -. DR GeneID; 8143071; -. DR KEGG; ppl:POSPLDRAFT_88528; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 525 AA; 54936 MW; 7A1E9DD3DB36196A CRC64; MAESKREIDY SVYLVTGRDL LPPGKDYLES LEESLRGGVT IVQIREKTTE TGEFLEVARR SQALCRKFNV PILINDRLDI ALAIGADGVH IGQTDMPIAV AKALLPPGAI IGMTCNTPAH VAQAVKDGAD YVGVGPVFAT QTKNVASPML GVRGLQDILA PLEGTNVKAV AIAGIKYTNA LQCLYGAVRP SGLGLDGLAI VSDIVASHEP EAAARKLATV VHAFKSTIPH IFSLSQHPYS SQYIKENAAQ LFPAIRRHGP LVQQITNTVV TTQSANATLA LGASPIMANA PQEMADISKA IGGLLINFGT IQSLDGMIEA GKHANINRKP VVFDPVGVGA SQYRRSSANS LLNTWQATVI KGNAGELAAI ANSQEVRAKG VDSVGQGFKN PALFVRDLAR RERCIVVLSG KTDYVSDGTT VVSLNNGHPL LGDITGSGCM LGTCIAIFCA AASMEATPED SKLVSGDMFV AAIGGVLALT LASEKAAARD DVKGSGTFLP ALIDELGKLS PEEVVALANV EVVSV // ID B8PL92_POSPM Unreviewed; 400 AA. AC B8PL92; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 25. DE SubName: Full=Predicted protein; DE Flags: Fragment; GN ORFNames=POSPLDRAFT_22001; OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus) OS (Poria monticola). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Polyporales; Postia. OX NCBI_TaxID=561896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 44394 / Madison 698-R; RX PubMed=19193860; DOI=10.1073/pnas.0809575106; RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M., RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., RA Kersten P., Hammel K.E., Vanden Wymelenberg A., Gaskell J., RA Lindquist E., Sabat G., Splinter BonDurant S., Larrondo L.F., RA Canessa P., Vicuna R., Yadav J., Doddapaneni H., Subramanian V., RA Pisabarro A.G., Lavin J.L., Oguiza J.A., Master E., Henrissat B., RA Coutinho P.M., Harris P., Magnuson J.K., Baker S.E., Bruno K., RA Kenealy W., Hoegger P.J., Kuees U., Ramaiya P., Lucas S., Salamov A., RA Shapiro H., Tu H., Chee C.L., Misra M., Xie G., Teter S., Yaver D., RA James T., Mokrejs M., Pospisek M., Grigoriev I.V., Brettin T., RA Rokhsar D., Berka R., Cullen D.; RT "Genome, transcriptome, and secretome analysis of wood decay fungus RT Postia placenta supports unique mechanisms of lignocellulose RT conversion."; RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ966448; EED78362.1; -; Genomic_DNA. DR RefSeq; XP_002476449.1; XM_002476404.1. DR ProteinModelPortal; B8PL92; -. DR STRING; 104341.JGI22001; -. DR GeneID; 8146596; -. DR KEGG; ppl:POSPLDRAFT_22001; -. DR OMA; ISIENTM; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome. FT NON_TER 1 1 FT NON_TER 400 400 SQ SEQUENCE 400 AA; 41395 MW; 579A297730CFB994 CRC64; AAVKDGADYV GVGPVFATQT KNVASPMLGV RGLQDILAPL EGTNVKAVAI AGIKYTNALQ CLYGAVRPSG LGLDGLAVVS DIVASHEPEA AARKLATVVH AFKSTIPHIF SLSQHPYTSQ YIKENAAQLF PAIRRHGPLV QQITNTVVTT QSANATLALG ASPIMANAPQ EMADISKAIG GLLINFGTIQ SLDGMIEAGK HANINRKPVV FDPVGVGASQ YRRSSANSLL NTWQATVIKG NAGELAAIAN SQEVRAKGVD SVGQGFKNPA LFVRDLARRE RCIVVLSGKT DYVSDGTTVV SLNNGHPLLG DITGSGCMLG TCIAIFCAAA SMEATPEDSK LVSGDMFVAA IGGVLALTLA SEKAAARDDV KGSGTFLPAL IDELGKLSPE EVVALANVEV // ID B8ZN15_STRPJ Unreviewed; 209 AA. AC B8ZN15; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPN23F06430; OS Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=561276; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700669 / Spain 23F-1; RX PubMed=19114491; DOI=10.1128/JB.01343-08; RA Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., RA Bason N.C., Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., RA Bentley S.D., Mitchell T.J.; RT "Role of conjugative elements in the evolution of the multidrug- RT resistant pandemic clone Streptococcus pneumoniae Spain23F ST81."; RL J. Bacteriol. 191:1480-1489(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM211187; CAR68490.1; -; Genomic_DNA. DR RefSeq; YP_002510672.1; NC_011900.1. DR ProteinModelPortal; B8ZN15; -. DR STRING; 561276.SPN23F_06430; -. DR GeneID; 7329171; -. DR KEGG; sne:SPN23F_06430; -. DR PATRIC; 19672573; VBIStrPne132160_0693. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE561276:GJFJ-638-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23275 MW; 54691E8B38ED4ED4 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LRGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID B8ZN22_STRPJ Unreviewed; 210 AA. AC B8ZN22; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPN23F06500; OS Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=561276; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700669 / Spain 23F-1; RX PubMed=19114491; DOI=10.1128/JB.01343-08; RA Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., RA Bason N.C., Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., RA Bentley S.D., Mitchell T.J.; RT "Role of conjugative elements in the evolution of the multidrug- RT resistant pandemic clone Streptococcus pneumoniae Spain23F ST81."; RL J. Bacteriol. 191:1480-1489(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM211187; CAR68497.1; -; Genomic_DNA. DR RefSeq; YP_002510679.1; NC_011900.1. DR ProteinModelPortal; B8ZN22; -. DR STRING; 561276.SPN23F_06500; -. DR GeneID; 7328271; -. DR KEGG; sne:SPN23F_06500; -. DR PATRIC; 19672587; VBIStrPne132160_0700. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE561276:GJFJ-646-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID B9AEQ4_METSM Unreviewed; 209 AA. AC B9AEQ4; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=METSMIALI_00842; OS Methanobrevibacter smithii DSM 2375. OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanobrevibacter. OX NCBI_TaxID=483214; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2375; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2375; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Methanobrevibacter smithii (DSM 2375)."; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYW01000007; EEE41944.1; -; Genomic_DNA. DR ProteinModelPortal; B9AEQ4; -. DR EnsemblBacteria; EEE41944; EEE41944; METSMIALI_00842. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22680 MW; 80B74152504F0F1D CRC64; MNNLDLSLYL VTNNSEDEEK FLNIIEESLK GGVSVVQLRE KKAETLDFYN LALKVKEIAQ KYNVPLIIND RIDIALAIDA DGVHVGQSDM PAKIARSMIG EDKILGVSAA NIKEAKKAQR DSADYIGVGA VYPTNTKDDA TSVPKKELKE IVKSVDIPVV AIGGITQENA HELNDCGIDG LSVVSAIMEA KNPKIASKNL LKEFKAKNS // ID B9B765_9BURK Unreviewed; 194 AA. AC B9B765; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=BURMUCGD1_5063; OS Burkholderia multivorans CGD1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=513051; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGD1; RX PubMed=23105085; DOI=10.1128/JB.01306-12; RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., RA Radune D., Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., RA Greenberg D.E., Holland S.M., Goldberg J.B.; RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic RT Granulomatous Disease Burkholderia multivorans Isolates."; RL J. Bacteriol. 194:6356-6357(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFB01000005; EED99882.1; -; Genomic_DNA. DR ProteinModelPortal; B9B765; -. DR EnsemblBacteria; EED99882; EED99882; BURMUCGD1_5063. DR PATRIC; 26962103; VBIBurMul43326_2854. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 20542 MW; 2C3421ADE4F39AA8 CRC64; MKPALPRRYV ITPEPASASA ADCDAFLDRL SAVLARGDTL VQLRVKSFDA ATFARLAADA LARCEAAGAQ LMLNGPIDAH GVLQLEHAGW HLDGATLRAT QQRPLPADRL LSAACHDADD LRLAARAGAD FVTLSPVLPT LSHPGAPTLG WAQFGAWAAQ AAMPVYALGG MTHAHLDEAR RHHAYGIAGI RGFW // ID B9B9Y9_9BURK Unreviewed; 371 AA. AC B9B9Y9; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=BURMUCGD1_3125; OS Burkholderia multivorans CGD1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=513051; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGD1; RX PubMed=23105085; DOI=10.1128/JB.01306-12; RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., RA Radune D., Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., RA Greenberg D.E., Holland S.M., Goldberg J.B.; RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic RT Granulomatous Disease Burkholderia multivorans Isolates."; RL J. Bacteriol. 194:6356-6357(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFB01000007; EED99352.1; -; Genomic_DNA. DR ProteinModelPortal; B9B9Y9; -. DR EnsemblBacteria; EED99352; EED99352; BURMUCGD1_3125. DR PATRIC; 26964217; VBIBurMul43326_3897. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; SQ SEQUENCE 371 AA; 38798 MW; C778E987CFDD654C CRC64; MSARFADAFW PPADELAEAA ERIRARLGDW PRAAAPWRLC MTAPDAPADG DVLIVSRGDR AGQARASAVS RPASPNAVAI EFDERGAALH AAGARYALDA AHALADDWIA ALAAFLDCGF APLDALVLAL AWRDGDETRA DDAWPVDAAQ FPRVSGLHAA AEPAFAPCPA RLGLYPVVPD AEWVERVLDC GVQTVQLRVK GAAPDALRRE IARAVAAGRR YPDARVFIND HWQIAADEGA YGVHLGQEDL ETADLAALAR AGLRLGLSSH GYYEMLRALH ERPSYLALGP VFATATKAVA APPQGLARIA RYARFAGPGV PLVAIGGVGL DALPAVLATG VGSVAVVSAV TGAGDYRAAI AALQRCFASP I // ID B9BK93_9BURK Unreviewed; 194 AA. AC B9BK93; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=BURMUCGD2_5501; OS Burkholderia multivorans CGD2. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=513052; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGD2; RX PubMed=23105085; DOI=10.1128/JB.01306-12; RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., RA Radune D., Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., RA Greenberg D.E., Holland S.M., Goldberg J.B.; RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic RT Granulomatous Disease Burkholderia multivorans Isolates."; RL J. Bacteriol. 194:6356-6357(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFC01000002; EEE08360.1; -; Genomic_DNA. DR ProteinModelPortal; B9BK93; -. DR EnsemblBacteria; EEE08360; EEE08360; BURMUCGD2_5501. DR PATRIC; 27786262; VBIBurMul91169_1092. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 20552 MW; BF7E86C88CC6321C CRC64; MKPALPRRYV ITPEPASASA ADCDAFLDRL SAVLARGDTL VQLRVKSFDA ATFARLAADA LARCEAAGAQ LMLNGPIDAQ GVLQFERAGW HLDGATLRAT QQRPLPAERL LSAACHDAGD LRLAARAGAD FVTLSPVLPT LSHPGAPTLG WAQFGAWAAH AAMPVYALGG MTHAHLDEAR RHHAYGIAGI RGFW // ID B9BVB1_9BURK Unreviewed; 371 AA. AC B9BVB1; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BURMUCGD2_0305; OS Burkholderia multivorans CGD2. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=513052; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGD2; RX PubMed=23105085; DOI=10.1128/JB.01306-12; RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., RA Radune D., Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., RA Greenberg D.E., Holland S.M., Goldberg J.B.; RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic RT Granulomatous Disease Burkholderia multivorans Isolates."; RL J. Bacteriol. 194:6356-6357(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFC01000010; EEE05316.1; -; Genomic_DNA. DR ProteinModelPortal; B9BVB1; -. DR EnsemblBacteria; EEE05316; EEE05316; BURMUCGD2_0305. DR PATRIC; 27792820; VBIBurMul91169_4333. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 371 AA; 38914 MW; C7D84642A12A0526 CRC64; MSARFADAFW PPADELAEAA ERIRARLGDW PRAAAPWRLC MTAPDAPTDG DVLIVSRGDR AGQARASAVS RPASPNAVAI EFDERGAALH AAGARYALDA AHALADDWIA ALAAFLDCGF APLDALVLAL AWRDGDETRA DDAWPVDAAQ FPRVAGLPAA AEPAFAPCPA RLGLYPIVPD AEWVERVLDC GVQTVQLRVK GAAPDALRRE IARAVAAGRR YPDARVFIND YWQIAADEGA YGVHLGQEDL ETADLAALAR AGLRLGLSSH GYYEMLRALH ERPSYLALGP VFATATKAVA APPQGLARIA RYARFAGSSV PLVAIGGVGL DALPAVLATG VGSVAVVSAV TGAADYRAAI TALQRCFVPP I // ID B9C499_9BURK Unreviewed; 194 AA. AC B9C499; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 22. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=BURMUCGD2M_5492; OS Burkholderia multivorans CGD2M. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=513053; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGD2M; RA Holland S.M., Harkins D.M., Brinkac L.M., Hostetler J., Nierman W.C.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFD01000001; EEE16047.1; -; Genomic_DNA. DR ProteinModelPortal; B9C499; -. DR EnsemblBacteria; EEE16047; EEE16047; BURMUCGD2M_5492. DR PATRIC; 27798796; VBIBurMul35808_1089. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 20552 MW; BF7E86C88CC6321C CRC64; MKPALPRRYV ITPEPASASA ADCDAFLDRL SAVLARGDTL VQLRVKSFDA ATFARLAADA LARCEAAGAQ LMLNGPIDAQ GVLQFERAGW HLDGATLRAT QQRPLPAERL LSAACHDAGD LRLAARAGAD FVTLSPVLPT LSHPGAPTLG WAQFGAWAAH AAMPVYALGG MTHAHLDEAR RHHAYGIAGI RGFW // ID B9CH92_9BURK Unreviewed; 371 AA. AC B9CH92; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BURMUCGD2M_0301; OS Burkholderia multivorans CGD2M. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=513053; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGD2M; RA Holland S.M., Harkins D.M., Brinkac L.M., Hostetler J., Nierman W.C.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFD01000010; EEE10859.1; -; Genomic_DNA. DR ProteinModelPortal; B9CH92; -. DR EnsemblBacteria; EEE10859; EEE10859; BURMUCGD2M_0301. DR PATRIC; 27807342; VBIBurMul35808_5292. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 371 AA; 38914 MW; C7D84642A12A0526 CRC64; MSARFADAFW PPADELAEAA ERIRARLGDW PRAAAPWRLC MTAPDAPTDG DVLIVSRGDR AGQARASAVS RPASPNAVAI EFDERGAALH AAGARYALDA AHALADDWIA ALAAFLDCGF APLDALVLAL AWRDGDETRA DDAWPVDAAQ FPRVAGLPAA AEPAFAPCPA RLGLYPIVPD AEWVERVLDC GVQTVQLRVK GAAPDALRRE IARAVAAGRR YPDARVFIND YWQIAADEGA YGVHLGQEDL ETADLAALAR AGLRLGLSSH GYYEMLRALH ERPSYLALGP VFATATKAVA APPQGLARIA RYARFAGSSV PLVAIGGVGL DALPAVLATG VGSVAVVSAV TGAADYRAAI TALQRCFVPP I // ID B9CPM8_STACP Unreviewed; 196 AA. AC B9CPM8; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=STACA0001_1001; OS Staphylococcus capitis SK14. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553212; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK14; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFR01000001; EEE50077.1; -; Genomic_DNA. DR ProteinModelPortal; B9CPM8; -. DR EnsemblBacteria; EEE50077; EEE50077; STACA0001_1001. DR PATRIC; 31384567; VBIStaCap19029_0129. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 22520 MW; A2ECCFDB921F4F37 CRC64; MHIFIAITYD KTLTTQDLEH FLNIEEGIDA LLFRTSMPKN ELKKILIQLI NQGFPKDKMI IHSDTALLEE LNLSRIHFKE NVKTAFAYKK SHPEIQVGMS THSIDTIYTC IDEGLDYVFY GHIFPTPSHP HDAPRSHDEI VEALNLPIPI YAIGGISEHT ILKLEYGFDG ICAISFFMNA SLKEIKELRR KWLQHA // ID B9CU01_STACP Unreviewed; 212 AA. AC B9CU01; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=STACA0001_0795; OS Staphylococcus capitis SK14. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553212; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK14; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFR01000009; EEE48743.1; -; Genomic_DNA. DR ProteinModelPortal; B9CU01; -. DR EnsemblBacteria; EEE48743; EEE48743; STACA0001_0795. DR PATRIC; 31387847; VBIStaCap19029_1721. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23706 MW; FFE3130988D42CA8 CRC64; MFSSEQLQVY FICGTQDIPE NRTIEQVLDE ALKAGITMYQ FREKGPSSLI GEEKKQLAIN LKRKCERYHV PFIVNDDIEL AKDIDADGVH VGQDDKEVKD FAMQFRNKII GLSVGNLDEY QQSDLSQVDY IGVGPMYTTS SKDDANAPVG PHMITKLRDY VGELPIVAIG GINETNIEPI AEACADGVSV ISAITRSKNI DKTVKHFRKY FN // ID B9D1C5_CAMRE Unreviewed; 200 AA. AC B9D1C5; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CAMRE0001_3212; OS Campylobacter rectus RM3267. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=553218; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RM3267; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFU01000008; EEF14231.1; -; Genomic_DNA. DR ProteinModelPortal; B9D1C5; -. DR EnsemblBacteria; EEF14231; EEF14231; CAMRE0001_3212. DR PATRIC; 27766023; VBICamRec32822_1311. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 200 AA; 21684 MW; 391BFCAFB30C5757 CRC64; MAKIYAITDD ILTPENSVVE QTRELLECGV KFLQYRTKLE PKNERVATAL KELCESYGAR FIVNDDVKFA AKIGANAVHI GKDDGGVKAA RKILGDDAFI GVSCYDNLNL ALKAQDEGAS YAAFGAVFAS PTKPNASLCK FETIMRAKEI LRIPICVIGG INVANIAQIA ALNPDYIAVI SALYQPASIK ENLRNLQAFL // ID B9D4Y0_CAMRE Unreviewed; 331 AA. AC B9D4Y0; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 13-NOV-2013, entry version 23. DE SubName: Full=Thiamine monophosphate synthase/TENI; DE EC=2.5.1.3; GN ORFNames=CAMRE0001_0844; OS Campylobacter rectus RM3267. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=553218; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RM3267; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFU01000031; EEF12952.1; -; Genomic_DNA. DR EnsemblBacteria; EEF12952; EEF12952; CAMRE0001_0844. DR PATRIC; 27768702; VBICamRec32822_2626. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. PE 4: Predicted; KW Transferase. SQ SEQUENCE 331 AA; 36505 MW; 35C1F9081B92993F CRC64; MKTDKFELVW VTNRRLSDDF FADVARVVQG GKADKILLRE SDLSEREYEI LARNTLEVIA KYSQNARLIV HTYADVAGRL GICELHLPFA KFIEACTSGG LKFENSNAAK CDEICVNTPH LLSDKFDKAC GSDKARMSGQ NGERGLSLTS KSRKFTANDK RTAGELNLTS PNLRKFDEPG INATEFERDI KPMSPDLSKS DEFCADVSAA SGERRLNLTD LFLAKFDDAC FRKGGVRAPN LTQKRKIGVS VHSLEEALSA QELGADYVVA GHVFDTPSHT LERGRGLKFL REICEKLSIK TYAIGGINFE NLSAIKDAGA AGAYMMRGFL S // ID B9DKF8_STACT Unreviewed; 156 AA. AC B9DKF8; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Putative uncharacterized protein; GN OrderedLocusNames=Sca_2076; ORFNames=SCA_2076; OS Staphylococcus carnosus (strain TM300). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=396513; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TM300; RX PubMed=19060169; DOI=10.1128/AEM.01982-08; RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., RA Schuster S.C., Goetz F.; RT "Genome analysis of the meat starter culture bacterium Staphylococcus RT carnosus TM300."; RL Appl. Environ. Microbiol. 75:811-822(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM295250; CAL28981.1; -; Genomic_DNA. DR RefSeq; YP_002635166.1; NC_012121.1. DR ProteinModelPortal; B9DKF8; -. DR STRING; 396513.Sca_2076; -. DR GeneID; 7551030; -. DR KEGG; sca:Sca_2076; -. DR PATRIC; 19605024; VBIStaCar105558_2074. DR eggNOG; COG0352; -. DR HOGENOM; HOG000090085; -. DR KO; K10810; -. DR OMA; FAGICAI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SCAR396513:GJ9G-2137-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 156 AA; 17456 MW; 10E962EE3CD68518 CRC64; MEQDELTKFI ENLIQAGFPK DKITIHTDTD LLQKLSLNAI HFREGDERAY NYKAEHPDVC VSMSSHNTQN AQTAKAHNLD YILFGHLFKT KSKPGKAPRT NSEIESVLNV NIPVIALGGI NADTLNLVPK EFSGIAAISY FREQDLETIR SAKEAE // ID B9E246_CLOK1 Unreviewed; 205 AA. AC B9E246; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 31. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=CKR_1520; OS Clostridium kluyveri (strain NBRC 12016). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=583346; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 12016; RA Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., RA Vertes A.A., Yukawa H.; RT "Complete genome sequence of Clostridium kluyveri and comparative RT genomics of Clostridia species."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009049; BAH06571.1; -; Genomic_DNA. DR RefSeq; YP_002471985.1; NC_011837.1. DR ProteinModelPortal; B9E246; -. DR STRING; 583346.CKR_1520; -. DR EnsemblBacteria; BAH06571; BAH06571; CKR_1520. DR GeneID; 7272966; -. DR KEGG; ckr:CKR_1520; -. DR PATRIC; 19472904; VBICloKlu118830_1699. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CKLU583346:GJNQ-1565-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 22622 MW; 1ABC3ED6DE0EA34A CRC64; MGTNKMIYVV TNRNLIKEDS IYNVVENVVK NGADGIILRE KDLSYTSLLS MSKKIKSITD KYNVPLIING NIDIALNIKA FGFHTSYEIF KKIKFKNNIY EKLKIGVSVH SIEEAKKAES LGANYLLAGH IFETDCKKGL KGRGLEFIRE MHKNILIPII AIGGIDCSNL KDVLSNGACG AAIMSSAMTN DGGKVVKNLK LLLVR // ID B9E563_CLOK1 Unreviewed; 203 AA. AC B9E563; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CKR_2587; OS Clostridium kluyveri (strain NBRC 12016). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=583346; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 12016; RA Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., RA Vertes A.A., Yukawa H.; RT "Complete genome sequence of Clostridium kluyveri and comparative RT genomics of Clostridia species."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009049; BAH07638.1; -; Genomic_DNA. DR RefSeq; YP_002473052.1; NC_011837.1. DR ProteinModelPortal; B9E563; -. DR STRING; 583346.CKR_2587; -. DR EnsemblBacteria; BAH07638; BAH07638; CKR_2587. DR GeneID; 7273004; -. DR KEGG; ckr:CKR_2587; -. DR PATRIC; 19475350; VBICloKlu118830_2921. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CKLU583346:GJNQ-2633-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21913 MW; FE9FC84429D18D0E CRC64; MELDYSLYLV TDRNVLRGKS LYEAVEQAIL GGVTLVQLRE KDASTREFYE QALELKKITE TYNIPLIIND RLDIAQAVDA EGVHLGQSDM PLVAARNILG KNKIIGISVG NVEEALEAEK NGADYVGIGT IFFTGTKKDI DIPIGIEGLK SVYNSINIPA VAIGGINENN FREVLSTGID GISVVSAILG KNDIKAAAKA LHK // ID B9E8D5_MACCJ Unreviewed; 211 AA. AC B9E8D5; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MCCL_1746; OS Macrococcus caseolyticus (strain JCSC5402). OC Bacteria; Firmicutes; Bacilli; Bacillales; Macrococcus. OX NCBI_TaxID=458233; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC5402; RX PubMed=19074389; DOI=10.1128/JB.01058-08; RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., RA Hiramatsu K.; RT "Complete genome sequence of Macrococcus caseolyticus strain RT JCSCS5402, reflecting the ancestral genome of the human-pathogenic RT staphylococci."; RL J. Bacteriol. 191:1180-1190(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009484; BAH18453.1; -; Genomic_DNA. DR RefSeq; YP_002561149.1; NC_011999.1. DR ProteinModelPortal; B9E8D5; -. DR STRING; 458233.MCCL_1746; -. DR EnsemblBacteria; BAH18453; BAH18453; MCCL_1746. DR GeneID; 7390374; -. DR KEGG; mcl:MCCL_1746; -. DR PATRIC; 22425975; VBIMacCas48391_1887. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MCAS458233:GI03-1796-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23460 MW; 8199CDBCB779FA39 CRC64; MFKREMLHVY FIAGTSDVPD GDLEDVLKEA LEAGITMFQF REKGPKAKTG QEKHLLAERL FNLCKDYKVP FIVNDDVALA KAIDADGIHL GQNDEKIKNI IDDFQGKIIG LSVGNFEEYD QSDLTHVDYI GVGPIYETSS KSDAKKPGGI ELIRKMRLYD EDIPIVAIGG ITSRNCEMII ASGADGISTI SSITRSSDIK QVVTDYLQYY K // ID B9E9B6_MACCJ Unreviewed; 193 AA. AC B9E9B6; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Thiamine monophosphate synthase ThiE; GN Name=thiE; OrderedLocusNames=MCCL_0120; OS Macrococcus caseolyticus (strain JCSC5402). OC Bacteria; Firmicutes; Bacilli; Bacillales; Macrococcus. OX NCBI_TaxID=458233; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC5402; RX PubMed=19074389; DOI=10.1128/JB.01058-08; RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., RA Hiramatsu K.; RT "Complete genome sequence of Macrococcus caseolyticus strain RT JCSCS5402, reflecting the ancestral genome of the human-pathogenic RT staphylococci."; RL J. Bacteriol. 191:1180-1190(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009484; BAH16827.1; -; Genomic_DNA. DR RefSeq; YP_002559523.1; NC_011999.1. DR ProteinModelPortal; B9E9B6; -. DR STRING; 458233.MCCL_0120; -. DR EnsemblBacteria; BAH16827; BAH16827; MCCL_0120. DR GeneID; 7390467; -. DR KEGG; mcl:MCCL_0120; -. DR PATRIC; 22422480; VBIMacCas48391_0194. DR eggNOG; NOG327032; -. DR HOGENOM; HOG000090085; -. DR KO; K10810; -. DR OMA; FAGICAI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MCAS458233:GI03-122-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 193 AA; 21933 MW; C090B80D9CE65669 CRC64; MFYMITPFVK PSDTVIQSIV DVEALVDGVI LRLDAYDDAL DVFIIQLKRH IDPSKIIVHD APYLMMKHGL TRIHFKERAS DAIAFKQQHP EFRVGMSVHS KESVHRIDGV LDYCIFGHVF PTPSKPGLTP QSAPVIDTVL SYDIPIVAIG GIDEHTIHQL DTRFSGFSGI RLFQHKAHLE YVQKEWLLRN SMS // ID B9GZ65_POPTR Unreviewed; 531 AA. AC B9GZ65; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 2. DT 14-MAY-2014, entry version 38. DE SubName: Full=THIAMINE REQUIRING 1 family protein; GN ORFNames=POPTR_0003s01150g; OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera OS subsp. trichocarpa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Malpighiales; Salicaceae; Saliceae; OC Populus. OX NCBI_TaxID=3694; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nisqually; RX PubMed=16973872; DOI=10.1126/science.1128691; RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I., RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., RA Boerjan W., Brun A., Brunner A., Busov V., Campbell M., Carlson J., RA Chalot M., Chapman J., Chen G.-L., Cooper D., Coutinho P.M., RA Couturier J., Covert S., Cronk Q., Cunningham R., Davis J., RA Degroeve S., Dejardin A., dePamphilis C.W., Detter J., Dirks B., RA Dubchak I., Duplessis S., Ehlting J., Ellis B., Gendler K., RA Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L., RA Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., RA Holt R., Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., RA Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., Kelleher C., RA Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F., RA Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., RA Martin F., Montanini B., Napoli C., Nelson D.R., Nelson C., RA Nieminen K., Nilsson O., Pereda V., Peter G., Philippe R., Pilate G., RA Poliakov A., Razumovskaya J., Richardson P., Rinaldi C., Ritland K., RA Rouze P., Ryaboy D., Schmutz J., Schrader J., Segerman B., Shin H., RA Siddiqui A., Sterky F., Terry A., Tsai C.-J., Uberbacher E., RA Unneberg P., Vahala J., Wall K., Wessler S., Yang G., Yin T., RA Douglas C., Marra M., Sandberg G., Van de Peer Y., Rokhsar D.S.; RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray)."; RL Science 313:1596-1604(2006). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Nisqually; RG US DOE Joint Genome Institute (JGI-PGF); RA Grigoriev I.V., Terry A., Salamov A.A., Otillar R., Lou Y., Lucas S., RA Hammon N., Glavina del Rio T., Detter J., Kalin E., Tice H., RA Pitluck S., Chapman J., Putnam N.H., Brunner A., Busov V., RA Campbell M., Chalot M., Covert S., Davis J., DiFazio S., Gribskov M., RA Gunter L., Hamberger B., Jansson S., Joshi C., Larimer F., Martin F., RA Napoli C., Nelson D., Ralph S., Rombauts S., Rouze P., Schrader J., RA Tsai C., Vahala J., Tuskan G., Rokhsar D.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000339; EEE79035.2; -; Genomic_DNA. DR RefSeq; XP_002304056.2; XM_002304020.2. DR ProteinModelPortal; B9GZ65; -. DR GeneID; 7461531; -. DR OMA; NTKANNP; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 531 AA; 55665 MW; 391683C1B0012E3B CRC64; MAYGGVIFSN SFSFYQKRIV MSSRMQEKNG GASVPHVLSV AGSDSGAGAG IQADLKACSA RGVYCSTVIT SVTAQNTVGV QAVHAVPEDF VAQQLKSVLS DMQVDVVKTG MLPSVGVVKV LLQSLTELSV RALVVDPVMV STSGDVLAGP SILSTFREEL LPMANIVTPN IKEASALLGG IRLETVADMR NAAELLHALG PRNVLVKGGD LPDSLDAVDI FFNGEHFYEL RSSRIKTRNT HGTGCTLASC IAAELAKGSP MLTAVRVAKR YVETALEYSK DILIGNGIQG PFDHLLRLKS GSHSFRRKDA FNPSDLFLYA VTDSGMNKKW GRSVVDAVAA AIQGGATIVQ LRDKDAGTKD FLETAKSCLA VCRSHGVPLL INDCVDVALA SDADGVHVGQ SDMPATVART LLGPEKIIGV SCKTIEQAQQ AWIGGADYIG CGGVYSTNTK ANNPTIGLDG LKTVCSASKL PVVAIGGINA SNAGTVMEMG VPNLKGVAVV SALFDRENVL AETKKLHALL MEASSSSSKI Q // ID B9J520_BACCQ Unreviewed; 206 AA. AC B9J520; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=BCQ_0820; OS Bacillus cereus (strain Q1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=361100; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Q1; RX PubMed=19060151; DOI=10.1128/JB.01629-08; RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., RA Xu X., Xue Y., Zhu Y., Jin Q.; RT "Complete genome sequence of the extremophilic Bacillus cereus strain RT Q1 with industrial applications."; RL J. Bacteriol. 191:1120-1121(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000227; ACM11250.1; -; Genomic_DNA. DR RefSeq; YP_002528542.1; NC_011969.1. DR ProteinModelPortal; B9J520; -. DR STRING; 361100.BCQ_0820; -. DR EnsemblBacteria; ACM11250; ACM11250; BCQ_0820. DR GeneID; 7375357; -. DR KEGG; bcq:BCQ_0820; -. DR PATRIC; 18909110; VBIBacCer120424_0727. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER361100:GJ7M-807-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22763 MW; F47D7D6EE053B78B CRC64; MKNELHVISN GHMSFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK IVINDRIDIA ILLNIPRVQL GYRSADVRSV KEKFSYLHVG YSVHSLEEAI DAFKNGADSL VYGHVFPTDC KKGVPARGVE EISDIARCLS IPITAIGGIT PENTGDVLTN GVSGIAVMSG IISSSNPYSK AKSYKESIRK WAEKHV // ID B9J9N6_AGRRK Unreviewed; 217 AA. AC B9J9N6; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Thiamine-phosphate pyrophosphorylase protein; GN Name=thiEch; OrderedLocusNames=Arad_3764; OS Agrobacterium radiobacter (strain K84 / ATCC BAA-868). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=311403; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K84 / ATCC BAA-868; RX PubMed=19251847; DOI=10.1128/JB.01779-08; RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K., RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., RA Otten L., Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., RA Du Z., Ewing A., Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., RA Miller N.M., Norton S., Chen Q., Phoolcharoen W., Ohlin V., RA Ondrusek D., Pride N., Stricklin S.L., Sun J., Wheeler C., Wilson L., RA Zhu H., Wood D.W.; RT "Genome sequences of three Agrobacterium biovars help elucidate the RT evolution of multichromosome genomes in bacteria."; RL J. Bacteriol. 191:2501-2511(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000628; ACM27637.1; -; Genomic_DNA. DR RefSeq; YP_002545568.1; NC_011985.1. DR ProteinModelPortal; B9J9N6; -. DR STRING; 311403.Arad_3764; -. DR EnsemblBacteria; ACM27637; ACM27637; Arad_3764. DR GeneID; 7369277; -. DR KEGG; ara:Arad_3764; -. DR PATRIC; 20806711; VBIAgrRad129173_5434. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; ARAD311403:GHU8-2920-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 217 AA; 22905 MW; 31B3A6B0691BC3C1 CRC64; MTVPEDRCRL VLIVPDIADV DEQAKVVADA LRGGDVASVI LPQYGLDDST FQKHAEKLVP LVQEAGAAAL IAGDSRVAGR AKADGLHITG NLAEFTEAVE KHVPKLIVGG GNATDRHHAL EIGELRPDYI FFGKLDGDIK PEAHPKNVAL GEWWASMIAI PCIVMGGTDP KSALEVALSG AEFVALRTAV FADPAAAASI VAEVNALLDE KAPRFED // ID B9JK66_AGRRK Unreviewed; 211 AA. AC B9JK66; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiEe; Synonyms=thiE; OrderedLocusNames=Arad_9220; OS Agrobacterium radiobacter (strain K84 / ATCC BAA-868). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=311403; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K84 / ATCC BAA-868; RX PubMed=19251847; DOI=10.1128/JB.01779-08; RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K., RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., RA Otten L., Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., RA Du Z., Ewing A., Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., RA Miller N.M., Norton S., Chen Q., Phoolcharoen W., Ohlin V., RA Ondrusek D., Pride N., Stricklin S.L., Sun J., Wheeler C., Wilson L., RA Zhu H., Wood D.W.; RT "Genome sequences of three Agrobacterium biovars help elucidate the RT evolution of multichromosome genomes in bacteria."; RL J. Bacteriol. 191:2501-2511(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000629; ACM30308.1; -; Genomic_DNA. DR RefSeq; YP_002541905.1; NC_011983.1. DR ProteinModelPortal; B9JK66; -. DR STRING; 311403.Arad_9220; -. DR EnsemblBacteria; ACM30308; ACM30308; Arad_9220. DR GeneID; 7366970; -. DR KEGG; ara:Arad_9220; -. DR PATRIC; 20799304; VBIAgrRad129173_1779. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ARAD311403:GHU8-5584-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21581 MW; E1F3EFB6DC2C872C CRC64; MKHFDLSLYL VLDPVLCAGI GMVETTRAAV AGGATIVQLR DKHASTASMI ETGLALKQAL ADTSARLIVN DDVEAAIAIG ADGLHIGQDD MDALTARRLI GPDMILGLSV ETETLAAAID PAVVDYAGIG PVFATPTKPD HKRPIGFAGL ARMIDLCPVP SVAIGGLKAE HAAEALLAGA DGIAVVSAIC GTPDPRTAAA EIAKTIREAR S // ID B9JMX7_AGRRK Unreviewed; 204 AA. AC B9JMX7; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiEb; Synonyms=thiE; OrderedLocusNames=Arad_7391; OS Agrobacterium radiobacter (strain K84 / ATCC BAA-868). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=311403; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K84 / ATCC BAA-868; RX PubMed=19251847; DOI=10.1128/JB.01779-08; RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K., RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., RA Otten L., Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., RA Du Z., Ewing A., Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., RA Miller N.M., Norton S., Chen Q., Phoolcharoen W., Ohlin V., RA Ondrusek D., Pride N., Stricklin S.L., Sun J., Wheeler C., Wilson L., RA Zhu H., Wood D.W.; RT "Genome sequences of three Agrobacterium biovars help elucidate the RT evolution of multichromosome genomes in bacteria."; RL J. Bacteriol. 191:2501-2511(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000629; ACM28908.1; -; Genomic_DNA. DR RefSeq; YP_002540503.1; NC_011983.1. DR ProteinModelPortal; B9JMX7; -. DR STRING; 311403.Arad_7391; -. DR EnsemblBacteria; ACM28908; ACM28908; Arad_7391. DR GeneID; 7365632; -. DR KEGG; ara:Arad_7391; -. DR PATRIC; 20796402; VBIAgrRad129173_0328. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ARAD311403:GHU8-4172-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 177 178 THZ-P binding (By similarity). FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22361 MW; C10C02A552B8A73E CRC64; MRLDPFYLIV DSADWIARLV PLGVKLVQLR IKDRTPSEIR AEIQRAKAIC AAHQCQLIVN DYWQLAIEEG CDFIHLGQED LAVADLSAIR KAGLKLGLST HDEAELATAL AASPDYIALG PVYPTILKKM PWAPQGLDRL REWKDRIGGL PLVAIGGLNL DRIAGVFENG ADSAAVVTDI TLNADPEART LEWIAVTHIH AVDQ // ID B9JS15_AGRVS Unreviewed; 227 AA. AC B9JS15; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Avi_3675; OS Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis OS (strain S4)). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=311402; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S4 / ATCC BAA-846; RX PubMed=19251847; DOI=10.1128/JB.01779-08; RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K., RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., RA Otten L., Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., RA Du Z., Ewing A., Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., RA Miller N.M., Norton S., Chen Q., Phoolcharoen W., Ohlin V., RA Ondrusek D., Pride N., Stricklin S.L., Sun J., Wheeler C., Wilson L., RA Zhu H., Wood D.W.; RT "Genome sequences of three Agrobacterium biovars help elucidate the RT evolution of multichromosome genomes in bacteria."; RL J. Bacteriol. 191:2501-2511(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000633; ACM37643.1; -; Genomic_DNA. DR RefSeq; YP_002550655.1; NC_011989.1. DR ProteinModelPortal; B9JS15; -. DR STRING; 311402.Avi_3675; -. DR EnsemblBacteria; ACM37643; ACM37643; Avi_3675. DR GeneID; 7388076; -. DR KEGG; avi:Avi_3675; -. DR PATRIC; 20831072; VBIAgrVit37146_5184. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; AVIT311402:GH2Y-2750-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 227 AA; 23909 MW; DD70393448BD0210 CRC64; MKKTEIAMSK SPKFQSRCRL VLITPQIADV QMLATTVGNA LKGGDVASVI IPQYDFDDDT FQAQAEAVVP LVQAAGAAAI IADNSRVAGR AKADGLHISG DVEALAEAVE KFTPKMIVGS GAARDRHHAL EAGDADPDYM FFGKLDGDIK PEAHSKNLAL GEWWSSMVEI PCIVMGGADP QSALAVAETG AEFAALSRAV FDDPEAAATV VAQVNALLDE KAPRFED // ID B9K257_AGRVS Unreviewed; 203 AA. AC B9K257; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Avi_5922; OS Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis OS (strain S4)). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=311402; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S4 / ATCC BAA-846; RX PubMed=19251847; DOI=10.1128/JB.01779-08; RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K., RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., RA Otten L., Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., RA Du Z., Ewing A., Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., RA Miller N.M., Norton S., Chen Q., Phoolcharoen W., Ohlin V., RA Ondrusek D., Pride N., Stricklin S.L., Sun J., Wheeler C., Wilson L., RA Zhu H., Wood D.W.; RT "Genome sequences of three Agrobacterium biovars help elucidate the RT evolution of multichromosome genomes in bacteria."; RL J. Bacteriol. 191:2501-2511(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000634; ACM38955.1; -; Genomic_DNA. DR RefSeq; YP_002547671.1; NC_011988.1. DR ProteinModelPortal; B9K257; -. DR STRING; 311402.Avi_5922; -. DR EnsemblBacteria; ACM38955; ACM38955; Avi_5922. DR GeneID; 7381012; -. DR KEGG; avi:Avi_5922; -. DR PATRIC; 20824399; VBIAgrVit37146_1903. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; AVIT311402:GH2Y-4069-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22711 MW; 601BA2ED7BE533C8 CRC64; MKLDPFYLIV DSADWIERLI PLGVKLVQLR MKDIVESDLR AHIRTAKAIC QVHDCQLIIN DYWQVALDEG CDFIHLGQED LAQADVAAIR AAHARLGIST HDEAELETAL AAMPDYVALG PIWPTVLKQM KWAPQGLPKL STWKATIGDI PIVAIGGVTA ERLDDVFSHG ADSAAVVTDI TRHENPEKRT EEWLEKTEKW REA // ID B9KD05_CAMLR Unreviewed; 208 AA. AC B9KD05; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cla_1122; OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=306263; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM2100 / D67 / ATCC BAA-1060; RX PubMed=18713059; DOI=10.1089/fpd.2008.0101; RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.; RT "The complete genome sequence and analysis of the human pathogen RT Campylobacter lari."; RL Foodborne Pathog. Dis. 5:371-386(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000932; ACM64444.1; -; Genomic_DNA. DR RefSeq; YP_002575695.1; NC_012039.1. DR ProteinModelPortal; B9KD05; -. DR STRING; 306263.Cla_1122; -. DR EnsemblBacteria; ACM64444; ACM64444; Cla_1122. DR GeneID; 7410856; -. DR KEGG; cla:Cla_1122; -. DR PATRIC; 20062725; VBICamLar15090_1107. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CLAR306263:GH7X-1120-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22848 MW; 5981B8F552489C46 CRC64; MKSFKIYLVA SKGEKSESEF LNILEASLKA KIDILQLREK NLSTLEFYKL ALKVKTLCEK YNTAFVINDR IDIAMAVNAD GVHIGQKDMP LKKARELLGE DKIIGLTINH KSELANIQDA TYLGVGAVFA TPSKQDCAIL GIDGLKEISN LSTLPIVAIG GIDETNLNLL KDCNIQGIAV IRAIMQASDP YMATLNLRSN FDKTFIGK // ID B9KD29_CAMLR Unreviewed; 200 AA. AC B9KD29; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE SubName: Full=Thiamine-phosphate pyrophosphorylase/regulatory protein TenI, putative; GN OrderedLocusNames=Cla_1146; OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=306263; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM2100 / D67 / ATCC BAA-1060; RX PubMed=18713059; DOI=10.1089/fpd.2008.0101; RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.; RT "The complete genome sequence and analysis of the human pathogen RT Campylobacter lari."; RL Foodborne Pathog. Dis. 5:371-386(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000932; ACM64468.1; -; Genomic_DNA. DR RefSeq; YP_002575719.1; NC_012039.1. DR ProteinModelPortal; B9KD29; -. DR STRING; 306263.Cla_1146; -. DR EnsemblBacteria; ACM64468; ACM64468; Cla_1146. DR GeneID; 7410880; -. DR KEGG; cla:Cla_1146; -. DR PATRIC; 20062775; VBICamLar15090_1132. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CIREALY; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CLAR306263:GH7X-1144-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 200 AA; 23115 MW; 373BB6DF2D1EEC26 CRC64; MWGKKIIAIS DSQNTQGDFL NFIEKLSQSS IDALVLREKH LDELGYAKLA KEVLKIFNKT QKICFLHYHY EVCLKLNHYF FHAPLFILQN YPQSYKKFEL LGTSIHSKEE LDLAYELKVN HAFFGHVFES SCKANLTPKG IKNLKDLLKV SKIPIYAIGG INIQTINHLK KLNLAGVCIR EALYKNNDLN EYILSCKMYL // ID B9KI00_ANAMF Unreviewed; 340 AA. AC B9KI00; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AMF_236; OS Anaplasma marginale (strain Florida). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Anaplasma. OX NCBI_TaxID=320483; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Florida; RX PubMed=19134224; DOI=10.1186/1471-2164-10-16; RA Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E., RA Palmer G.H., Knowles D.P.Jr., Brayton K.A.; RT "Conservation in the face of diversity: multistrain analysis of an RT intracellular bacterium."; RL BMC Genomics 10:16-16(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001079; ACM49112.1; -; Genomic_DNA. DR RefSeq; YP_002563368.1; NC_012026.1. DR ProteinModelPortal; B9KI00; -. DR STRING; 320483.AMF_236; -. DR EnsemblBacteria; ACM49112; ACM49112; AMF_236. DR GeneID; 7398350; -. DR KEGG; amf:AMF_236; -. DR PATRIC; 20944249; VBIAnaMar82315_0270. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; AMAR320483:GIWE-232-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 170 174 HMP-PP binding (By similarity). FT REGION 267 269 THZ-P binding (By similarity). FT REGION 318 319 THZ-P binding (By similarity). FT METAL 203 203 Magnesium (By similarity). FT METAL 222 222 Magnesium (By similarity). FT BINDING 202 202 HMP-PP (By similarity). FT BINDING 241 241 HMP-PP (By similarity). FT BINDING 270 270 HMP-PP (By similarity). FT BINDING 298 298 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 340 AA; 37299 MW; D404DAB1BEFC0D69 CRC64; MHLMRGDNMA SCAVAEAVRD AHLQGEGDVY AVNAECADGT YADYYFDGNE EIKLLYKCPG PTDCDTFARS YRHVADHVLN TTKCKDMKDA RLDCIVLARM LASAVVSGGS VADWNPYNIN GEYFPRIASG FDCRDTMYGF DKLENIGLYL IVPDDTWFER AVRCGVKTIQ LRAKEAPIGE VDRMVRRCAQ LSKDKGVCLI VNDHWNIAIE HGAHGVHLGQ EDVQTADLES ILKSKMKLGL STHCYHELAR ACFIRPSYVA LGPVFHTTSK DMRFKPQGLQ LLKQWVQCAK LPVVGIGGID ASNIGSVVNC GVSGVAVISA VTGAEDPEAA MLNLQRAFDV // ID B9KL68_RHOSK Unreviewed; 203 AA. AC B9KL68; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=RSKD131_2005; OS Rhodobacter sphaeroides (strain KD131 / KCTC 12085). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=557760; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KD131 / KCTC 12085; RX PubMed=19028901; DOI=10.1128/JB.01565-08; RA Lim S.K., Kim S.J., Cha S.H., Oh Y.K., Rhee H.J., Kim M.S., Lee J.K.; RT "Complete genome sequence of Rhodobacter sphaeroides KD131."; RL J. Bacteriol. 191:1118-1119(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001150; ACM01865.1; -; Genomic_DNA. DR RefSeq; YP_002526366.1; NC_011963.1. DR ProteinModelPortal; B9KL68; -. DR STRING; 557760.RSKD131_2005; -. DR EnsemblBacteria; ACM01865; ACM01865; RSKD131_2005. DR GeneID; 7358593; -. DR KEGG; rsk:RSKD131_2005; -. DR PATRIC; 23183123; VBIRhoSph125910_3408. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RSPH557760:GH1P-2031-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 20328 MW; 3F48C674653192B6 CRC64; MNLSLYFVTP DGAEGLEQLV AAAVRGGATL VQLRDKHRSD AELIPLARRL VAALEAQGVP LIVNDRIEVV LASGAAGLHV GQGDLGVAEA RRRIGPDRLL GLSVEAPEHL EALPLGIVDY VGAGPVRATA SKPDHAPPIG FEGLARLVAA APVPAVAIGG LGAGDAHAVK AAGAAGMAIV SAIGAAADPE AAARALALEW GRA // ID B9KW10_RHOSK Unreviewed; 206 AA. AC B9KW10; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=RSKD131_3154; OS Rhodobacter sphaeroides (strain KD131 / KCTC 12085). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=557760; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KD131 / KCTC 12085; RX PubMed=19028901; DOI=10.1128/JB.01565-08; RA Lim S.K., Kim S.J., Cha S.H., Oh Y.K., Rhee H.J., Kim M.S., Lee J.K.; RT "Complete genome sequence of Rhodobacter sphaeroides KD131."; RL J. Bacteriol. 191:1118-1119(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001151; ACM03014.1; -; Genomic_DNA. DR RefSeq; YP_002520087.1; NC_011958.1. DR ProteinModelPortal; B9KW10; -. DR STRING; 557760.RSKD131_3154; -. DR EnsemblBacteria; ACM03014; ACM03014; RSKD131_3154. DR GeneID; 7353150; -. DR KEGG; rsk:RSKD131_3154; -. DR PATRIC; 23176300; VBIRhoSph125910_0051. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RSPH557760:GH1P-3199-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22171 MW; 11DDB967817BEAEA CRC64; MAEVERPQLY LVTPPEIDLE IFPDRLAAVL DSTEVACLRL ALAGKDEDRI ARTGDALREV AHARDVALVI ENHVLMVERL GLDGVHLTDG ARLVRKLRKD LGPDAILGAF CGRTRHEGIN AAEAGADYVA FGPVGTTALG DGSLAEAELF GWWSEMIEVP VVAEGALTPE KVAELAPLTD FFAVGEEIWR EEDAAAALRR LLAPLG // ID B9KY57_THERP Unreviewed; 222 AA. AC B9KY57; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=trd_0400; OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2). OC Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae; OC Thermomicrobium. OX NCBI_TaxID=309801; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27502 / DSM 5159 / P-2; RX PubMed=19148287; DOI=10.1371/journal.pone.0004207; RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., RA Bryant D.A., Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., RA Ward N.L., Eisen J.A.; RT "Complete genome sequence of the aerobic CO-oxidizing thermophile RT Thermomicrobium roseum."; RL PLoS ONE 4:E4207-E4207(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001275; ACM04795.1; -; Genomic_DNA. DR RefSeq; YP_002521649.1; NC_011959.1. DR ProteinModelPortal; B9KY57; -. DR STRING; 309801.trd_0400; -. DR EnsemblBacteria; ACM04795; ACM04795; trd_0400. DR GeneID; 7355664; -. DR KEGG; tro:trd_0400; -. DR PATRIC; 23912020; VBITheRos91376_0394. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TROS309801:GI0S-398-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 22855 MW; 30A27C52DEFDC2CD CRC64; MTTWRGVRLR EALRLYVITD RALARGRPDI EIAREAIAGG ATALQLRWKA GPLSEALQVG HALRALCREA GVLFVVNDRV DLALALEADG VHVGVSDLPV PETRKLVGES MVVGFSPETL EQALAAEAAG ADYLGVGPVY PTTTKPDAGP AVGLEHLAQI AGAVGIPVVG IGGITAVNAA AVIRAGAVGV AVISAVVGAE DVREAARQLR EVVDAALAER GR // ID B9KY58_THERP Unreviewed; 208 AA. AC B9KY58; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=trd_0401; OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2). OC Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae; OC Thermomicrobium. OX NCBI_TaxID=309801; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27502 / DSM 5159 / P-2; RX PubMed=19148287; DOI=10.1371/journal.pone.0004207; RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., RA Bryant D.A., Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., RA Ward N.L., Eisen J.A.; RT "Complete genome sequence of the aerobic CO-oxidizing thermophile RT Thermomicrobium roseum."; RL PLoS ONE 4:E4207-E4207(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001275; ACM05154.1; -; Genomic_DNA. DR RefSeq; YP_002521650.1; NC_011959.1. DR ProteinModelPortal; B9KY58; -. DR STRING; 309801.trd_0401; -. DR EnsemblBacteria; ACM05154; ACM05154; trd_0401. DR GeneID; 7356247; -. DR KEGG; tro:trd_0401; -. DR PATRIC; 23912022; VBITheRos91376_0395. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PCPVIAI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TROS309801:GI0S-399-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 132 134 THZ-P binding (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21420 MW; 051C3A02C2DEB091 CRC64; MRVPRLHLVT DPEVCPFDRL LALLPALVAA GVDGVHLRAP DRAAAELLAV AQVARRVVVP PAVLLVNDRI DAALLSEADG VQLPERGLPP EGARRLLGRG RFIGCSVHSV TAAERAAQAG ADFLLFGNVF ETASKPGRAA AGLEALRAVT RAVPCPVIAI GGITPERVPE VVATGAHGVA VIRGILAAPD PVAAVHAFRA ALDRVGAV // ID B9L679_NAUPA Unreviewed; 173 AA. AC B9L679; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 13-NOV-2013, entry version 31. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=NAMH_1476; OS Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales; OC Nautiliaceae; Nautilia. OX NCBI_TaxID=598659; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1463 / DSM 18972 / AmH; RX PubMed=19197347; DOI=10.1371/journal.pgen.1000362; RA Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., RA Lee C.K., Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.; RT "Adaptations to submarine hydrothermal environments exemplified by the RT genome of Nautilia profundicola."; RL PLoS Genet. 5:E1000362-E1000362(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001279; ACM92640.1; -; Genomic_DNA. DR RefSeq; YP_002607867.1; NC_012115.1. DR ProteinModelPortal; B9L679; -. DR STRING; 598659.NAMH_1476; -. DR EnsemblBacteria; ACM92640; ACM92640; NAMH_1476. DR GeneID; 7504892; -. DR KEGG; nam:NAMH_1476; -. DR PATRIC; 22677643; VBINauPro131435_1424. DR eggNOG; NOG119803; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IASTHNT; -. DR OrthoDB; EOG6FJNJD; -. DR BioCyc; NPRO598659:GH7N-1470-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 173 AA; 20058 MW; 14C0F8781548A05C CRC64; MRKLIKYMIT DPKYTLEETK TTILKHKPDF VCYRNKQYYN ENEIIEFAKF AKDYAKVFIN IDSLKNTRLL YLFDGVHLPS SKLSLIDSFE NKTIIASTHN TEEVKKSQKA DFITFSPIFE SKNRPGLGIE TLNRICELHK NVIALGGIVS DKEVEEIKKS KAVGFASIRY FFT // ID B9L784_NAUPA Unreviewed; 231 AA. AC B9L784; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=NAMH_0050; OS Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales; OC Nautiliaceae; Nautilia. OX NCBI_TaxID=598659; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1463 / DSM 18972 / AmH; RX PubMed=19197347; DOI=10.1371/journal.pgen.1000362; RA Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., RA Lee C.K., Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.; RT "Adaptations to submarine hydrothermal environments exemplified by the RT genome of Nautilia profundicola."; RL PLoS Genet. 5:E1000362-E1000362(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001279; ACM92641.1; -; Genomic_DNA. DR RefSeq; YP_002606492.1; NC_012115.1. DR STRING; 598659.NAMH_0050; -. DR EnsemblBacteria; ACM92641; ACM92641; NAMH_0050. DR GeneID; 7504565; -. DR KEGG; nam:NAMH_0050; -. DR PATRIC; 22674819; VBINauPro131435_0050. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NADIAFI; -. DR OrthoDB; EOG6WX4T9; -. DR BioCyc; NPRO598659:GH7N-50-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 231 AA; 26674 MW; 0D584CB91F4049AA CRC64; MAIYALLDWD TLKKYDISIK DFCKTAKGLK AKILQYRDKN SSLEEKKERL LEIKKHWKKP LIINDTVELL PFCDGIHIGQ EDLESLSQKF NLPKYDVIQK LRTGELLEWK MENGKWKINK KTKINNSPLS IVHCPFIVGL STHNKEEILE ANTYPLSYIG LGAYRPTDTK NTDNIIGEKV IDLIKFSNHP VAVIGGVKIY DKIPSKFKVI GSDICRLTSS RLRKKKIFRQ K // ID B9LIA4_CHLSY Unreviewed; 216 AA. AC B9LIA4; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Chy400_0400; OS Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl). OC Bacteria; Chloroflexi; Chloroflexales; Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=480224; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29364 / DSM 637 / Y-400-fl; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Kiss H., RA Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., RA Kyrpides N., Ovchinnikova G., Bryant D.A., Richardson P.; RT "Complete sequence of Chloroflexus sp. Y-400-fl."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001364; ACM51839.1; -; Genomic_DNA. DR RefSeq; YP_002568164.1; NC_012032.1. DR ProteinModelPortal; B9LIA4; -. DR STRING; 480224.Chy400_0400; -. DR EnsemblBacteria; ACM51839; ACM51839; Chy400_0400. DR GeneID; 7405304; -. DR KEGG; chl:Chy400_0400; -. DR PATRIC; 21420204; VBIChlSp61043_0420. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CSP480224:GHIY-404-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22596 MW; 28BE1FA1C780A5FE CRC64; MSIAHIVDWR LYVVTDAGLS RGRSHRAVIE AAIVGGATVV QYREKHASTR QMIEEALELR DLTRRAGVPL IVNDRVDVAL AVDADGVHVG QDDMPVALAR RLIGNKLLGV SAHNLSEALQ AVRDGADYLG VGPIFATTTK PDAAAPIGLD GLRAIRQHVS IPIVAIGGIN QANAADVMRA GADGIAVVSA VVAADDVTAA ARQLRALVSV TQEKAL // ID B9M4Q2_GEODF Unreviewed; 497 AA. AC B9M4Q2; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE SubName: Full=Phosphomethylpyrimidine kinase; GN OrderedLocusNames=Geob_1418; OS Geobacter daltonii (strain DSM 22248 / JCM 15807 / FRC-32). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=316067; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22248 / JCM 15807 / FRC-32; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Kostka J., Richardson P.; RT "Complete sequence of Geobacter sp. FRC-32."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001390; ACM19778.1; -; Genomic_DNA. DR RefSeq; YP_002536879.1; NC_011979.1. DR ProteinModelPortal; B9M4Q2; -. DR STRING; 316067.Geob_1418; -. DR EnsemblBacteria; ACM19778; ACM19778; Geob_1418. DR GeneID; 7362099; -. DR KEGG; geo:Geob_1418; -. DR PATRIC; 22009373; VBIGeoSp137169_1457. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; GSP316067:GHSV-1434-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 497 AA; 52720 MW; 594330C643DB0E3E CRC64; MENRKDFLRL VVDRELNNSP IRGVYLVTDE GIRLAERVKV AINSGVSVVQ YRKKTGEPGE KLSIGLQLKK QCAEAGVTFL VNDDLALAKA LDADGLHLGQ DDGSPLEARR ELGPRKIIGV STHNMEEALK AQSDGADYIG LGAMFPTDSK EISHLAGPEA LPAIKERVKL PVVAIGGINR DNGSQIVDNG ADALAVISAI LGHREPGLAA AELALLFNRR AQFPRGNVLT IAGSDSGGGA GIQADLKTIT LLGSYGASAM TALTAQNTRG VAAIHGVPAE FLAQQLDSVL SDIHVDVVKT GMLFSADNIG IIADKLQQYG KKIIIIDPVM LAKGGAELID REALAIFKKR LLPCAYLLTP NIPEAEKLTG FTVSCEDDMQ RAAKTLHQMG ARNVLVKGGH LAEGTAVDIL FDGKNFSQFP VPRILTKNTH GTGCTLASAI STFLAQGEPL PQAVARAKEF ITAAIKLAHP LGKGHGPVNH YMAAQKVRCQ QGVPCQE // ID B9M5W3_GEODF Unreviewed; 219 AA. AC B9M5W3; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Geob_1586; OS Geobacter daltonii (strain DSM 22248 / JCM 15807 / FRC-32). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=316067; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22248 / JCM 15807 / FRC-32; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Kostka J., Richardson P.; RT "Complete sequence of Geobacter sp. FRC-32."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001390; ACM19944.1; -; Genomic_DNA. DR RefSeq; YP_002537045.1; NC_011979.1. DR ProteinModelPortal; B9M5W3; -. DR STRING; 316067.Geob_1586; -. DR EnsemblBacteria; ACM19944; ACM19944; Geob_1586. DR GeneID; 7361778; -. DR KEGG; geo:Geob_1586; -. DR PATRIC; 22009719; VBIGeoSp137169_1629. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GSP316067:GHSV-1603-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24084 MW; 364AFE762A6CBE98 CRC64; MRSSSPWIDF DLYLITDRKQ TGGRNLEFVV EDALRGGVRA IQLREKDLSS KELYELAYEM RKLTTRHNAR LIINDRIDIA LAVDADGVHL GYNSMPIYRA RMVLGEKKLI GVSCHNQVQA IIAQEKGADF ITFGPIYNTP SKALYGDPVG LKRLQEATNI VQIPIFALGG IKTDNVAEVM AAAPHGIGIV SAILSAEEPR LAARTLLSLL PAPESDLET // ID B9MA23_ACIET Unreviewed; 309 AA. AC B9MA23; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Dtpsy_1939; OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=535289; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TPSY; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Coates J.D.; RT "Complete sequence of Diaphorobacter sp. TPSY."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001392; ACM33395.1; -; Genomic_DNA. DR RefSeq; YP_002553395.1; NC_011992.1. DR ProteinModelPortal; B9MA23; -. DR STRING; 535289.Dtpsy_1939; -. DR EnsemblBacteria; ACM33395; ACM33395; Dtpsy_1939. DR GeneID; 7382057; -. DR KEGG; dia:Dtpsy_1939; -. DR PATRIC; 21780987; VBIDiaSp55748_1979. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; AEBR535289:GHOO-1971-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 309 AA; 32642 MW; 90F7FD4F3AC3EB03 CRC64; MPQAAAPLPS AAAMEQAIRQ HHASAFADFP PQPMPATTVE DPVYRAALAA CSALGFIAHD ADCLARAWAA QTRRTGRFDP AQWPDEPADF GLQPRPHAHP FAACPQNLGL YAVLPDAQWV GRMAQAGVPT VQLRFKSDDP AAITREVRAA VQAVQGTASL LFINDHWRQA IAAGAYGVHL GQEDLDALSP EELRTLRESG VRLGVSTHGY AEMVRADAAS PSYIAMGAVF PTTLKKMATV PQGVARLAGY ARLMRGYPLV AIGGIGLAQF PQVLATGVGS IAVVRAVVAA DQPEAAAAQL MRAMDAGRR // ID B9NQV7_9RHOB Unreviewed; 205 AA. AC B9NQV7; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=RKLH11_1216; OS Rhodobacteraceae bacterium KLH11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=467661; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KLH11; RA Hill R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999531; EEE37380.1; -; Genomic_DNA. DR ProteinModelPortal; B9NQV7; -. DR EnsemblBacteria; EEE37380; EEE37380; RKLH11_1216. DR PATRIC; 28448916; VBIRhoBac95025_2022. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 205 AA; 21492 MW; 6024734BA6F57CD3 CRC64; MDTPEQPQIY LITPPTIALS SFPDQLGRVL DGAEIACIRL ALAGQDEDMI ARAADACREV AHARDVAIVI SNHVMLAQRL GLDGVHLDDA ARSVRAARKE LGADAVVGSF CGASSHDGMT AGETGADYIA FGPVGTSALG DGTTAGQDLF QWWSEMIEVP VVAEGGLTPD LIHTLAPCTD FFGIGDEIWS QDDPLATLKA LTSAM // ID B9NU18_9RHOB Unreviewed; 198 AA. AC B9NU18; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 16-OCT-2013, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RKLH11_2472; OS Rhodobacteraceae bacterium KLH11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=467661; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KLH11; RA Hill R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999531; EEE38628.1; -; Genomic_DNA. DR ProteinModelPortal; B9NU18; -. DR EnsemblBacteria; EEE38628; EEE38628; RKLH11_2472. DR PATRIC; 28445914; VBIRhoBac95025_0503. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 198 AA; 22333 MW; 0E635D2E104F4B41 CRC64; MTLDRFYPIF DHSDWLRRML PLGVKLVQLR IKDQPDDVMR RQIAISRDLC RAHDAVLVVN DHWQIAIDLG CDWIHLGQED LDDADLKVIQ KAGLKLGVST HDDDELERVL TMGPDYVALG PVYPTILKKM KWHQQGLPRV TEWKARLGDI PLVGIGGMSV ERAAGVLDAG ADIVSAVTDI TLNVNPEARV REWIEATR // ID B9P380_PROMR Unreviewed; 351 AA. AC B9P380; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=P9202_342; OS Prochlorococcus marinus str. MIT 9202. OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=93058; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MIT 9202; RA Chisholm P., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999537; EEE39570.1; -; Genomic_DNA. DR ProteinModelPortal; B9P380; -. DR EnsemblBacteria; EEE39570; EEE39570; P9202_342. DR PATRIC; 26391361; VBIProMar1821_0354. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 351 AA; 40134 MW; CFDF2B9A82C4F281 CRC64; MLNSNAKDIE DLRIYQIIDA NLDRAREGLR VLEDWARFGL GKEKYVEKIK NFRQILGKNH LEVYKQSRNH IEDKCKGLTH QEQINRKTSG QIISSNSARV QEALRVIEEF SRPQNDELSK IASEIRYEIY TIEIDLLSYN KCKKSEEILK ENDLYVITDQ KDNLLEIIEE ILIAGVRIIQ HRFKMGNDQD HLQEAIQIKN LCERYNSLFI VNDRLDIALA SNADGIHLGQ NDLDLKTARK LLGHSKIVGI SANNAIDISN ALKEGCNYIG IGPVFETTTK KDKKPLGIEN IKTLTKDLNI PWFAIGGIKS NNISYLKRNG FKKVALVSQL MNSEDPKEDA IMILKELSNE N // ID B9QWE3_9RHOB Unreviewed; 201 AA. AC B9QWE3; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 16-OCT-2013, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=SADFL11_633; OS Labrenzia alexandrii DFL-11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=244592; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFL-11; RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973121; EEE43347.1; -; Genomic_DNA. DR ProteinModelPortal; B9QWE3; -. DR EnsemblBacteria; EEE43347; EEE43347; SADFL11_633. DR PATRIC; 30174116; VBILabAle118631_4917. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22215 MW; ECB55B310D150272 CRC64; MKLDPFYLIV DSTDWIARLV PIGVKLVQLR IKDQPEEEIA RQIRNAKSIC ADHGCQLVVN DYWRLAISEG CDFIHLGQED LADADVDTIR NAGLKLGVST HDGAELSTAL AVQPEYVALG PVYPTVTKKL KWAPQGLEKI TRWKADIGDL PLVTIGGLTV ERLSGVFEHG ADSAAVVTDI TRSADPEART REWISATEQW R // ID B9R607_9RHOB Unreviewed; 204 AA. AC B9R607; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase/TENI subfamily; GN ORFNames=SADFL11_3321; OS Labrenzia alexandrii DFL-11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=244592; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFL-11; RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973121; EEE46032.1; -; Genomic_DNA. DR ProteinModelPortal; B9R607; -. DR EnsemblBacteria; EEE46032; EEE46032; SADFL11_3321. DR PATRIC; 30177230; VBILabAle118631_1560. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 204 AA; 21455 MW; A0A68F20E99C6BD2 CRC64; MTPPAFDTAT LADQLKQAFA GGDIACVMIY MPDASTKDIQ AAADVLVPII QDGSAAALVY GDTQAAGRSG ADGVHVDKSP EDVKLAVESF QPDRVVGTGG TKTKHDAMEL AETGVDYLFF GKLDLTEKET AHDKTLSGAN WWAELFETPC VALAGNTLDT LAEVAATGAD FVALKDAVWH SEDIAKTISD ANTVLEAHPF PEVD // ID B9S430_RICCO Unreviewed; 921 AA. AC B9S430; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 29. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=RCOM_0558170; OS Ricinus communis (Castor bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae; OC Acalyphoideae; Acalypheae; Ricinus. OX NCBI_TaxID=3988; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Hale; RX PubMed=20729833; DOI=10.1038/nbt.1674; RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D., RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., RA Gedil M., Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., RA Ravel J., Rabinowicz P.D.; RT "Draft genome sequence of the oilseed species Ricinus communis."; RL Nat. Biotechnol. 28:951-956(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973863; EEF41711.1; -; Genomic_DNA. DR RefSeq; XP_002520749.1; XM_002520703.1. DR ProteinModelPortal; B9S430; -. DR PRIDE; B9S430; -. DR GeneID; 8272048; -. DR KEGG; rcu:RCOM_0558170; -. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. PE 4: Predicted; KW Complete proteome; GTP-binding; Nucleotide-binding. SQ SEQUENCE 921 AA; 103123 MW; 0180304FD9D3A55D CRC64; MIPFLSLNTT SPSLSLSLSF PFFSPFKSSP LRTHRFPILS LPNNPFHQSI NQSLPTQQSQ QSPRTLFPGG YKRPEIKVPS IVLQLYPDDV LRDGALDFLD KALSKWVGIV VLNGADVTGK TLYEAACLLK SVVKDRVYFL IGERVDIAAA VNASGVVLSD QGLPSIVARN MMRDSKSESI LLPLVGRNVQ SPTAALDASN SEGADFLIYS PEQEEHFDLK IYSGFADVKI PIFIIHGSRR PAMSVMEASE LLKSGAGGLV MSLEDLRLFS DEFLSQVFYT LSAMENKSEN GLESFNKHKS LDIGNDVHGK KRVAGFVNVE DREKQLIETE RSVLLQAINV IQKAAPQMEE VSLLIDAVSQ IDEPFLLAIV GEFNSGKSTV INALLGERYL KEGVVPTTNE ITFLRYSQYN SEEPQRCERH PDGQYVCYLP APILNEMNIV DTPGTNVILQ RQQRLTEEFV PRADLLLFVI SADRPLTESE VAFLRYTQQW KKKVVFVLNK SDLYQNASEL EEAKSFIKEN TRKLLNTESV ILYPVSARSA LEAKLSASSD SERDYTESLN SESHWKTSSF DEFEKFLYSF LDGSTETGME RMKLKLETPI AIANCIISSC EAFVKQETQY AEQDLATVSD IVDSVKDYTL KMEKDSISWR KKALSKIETT KSRVLELIES TLQISNLDLA TSYLLKGEKS TMTPTSLRVQ HDIIGPAVSD VQKLLEEYAL WLKSNSAHES KLYKEAFEKR WPSIINPDSR MHSETYELLE KADDLGLKAI QNFSTAAASK LFEQEIREVY LGTFGGLGAA GLSASLLTSV LPTTLEDLLA LGLCSAGGFI AISSFPYRKQ EMVDKVRRIA DGLMREVEEA MQKDLLETLV NLDNFLKIIS KPYQDAAQQR LDDLLNIQNE LSEMEEKIRT LQVEIQNLHL S // ID B9SXF8_RICCO Unreviewed; 546 AA. AC B9SXF8; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 29. DE SubName: Full=Phosphomethylpyrimidine kinase, putative; DE EC=2.5.1.3; DE EC=2.7.4.7; GN ORFNames=RCOM_0321500; OS Ricinus communis (Castor bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae; OC Acalyphoideae; Acalypheae; Ricinus. OX NCBI_TaxID=3988; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Hale; RX PubMed=20729833; DOI=10.1038/nbt.1674; RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D., RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., RA Gedil M., Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., RA Ravel J., Rabinowicz P.D.; RT "Draft genome sequence of the oilseed species Ricinus communis."; RL Nat. Biotechnol. 28:951-956(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ974224; EEF31708.1; -; Genomic_DNA. DR RefSeq; XP_002530677.1; XM_002530631.1. DR ProteinModelPortal; B9SXF8; -. DR GeneID; 8267035; -. DR KEGG; rcu:RCOM_0321500; -. DR KO; K14153; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 546 AA; 57934 MW; 2785B3A1F7AF2033 CRC64; MAFCGILSNS SSIFNKERVA QRSRFSNWKV NQTLMTMEGN GAAANKKIPH VLSVAGSDSG AGAGIQADLK ACAARGVYCS TVITAVTAQN TAGVQGVDIV RNDFVAEQLK SVLSDMQVDV VKTGMLPSIG IVKILHQNLR EFPVRALVVD PVMVSTSGDV LAGPSIVSCF REELLPMANI VTPNIKEASA LLGGMPLETL ADMRSAAKLL HALGPQNVLV KGGDLPDSLD AVDIFFDGED YHELRSSRIK TRNTHGTGCT LASCIAAELA KGSPMLSAVK VAKCYIETAL EYSKDIFIGN GRQGPFDHLL RLKSSVQNSG RQGTFNPNNL FLYAVPDSRM NKMWGRPMVD ATREAIEGGA TIVQLREKNT ETRDFINTAK ACLEICRSHG VPLLINDRVD VALACDADGV HVGQSDIPAR TARILLGPDK IIGVSCKTPE QAQQAWIDGA DYIGCGGVYP TTTKANNSTV GFDGLKAVCL ASKLPVVAIG GINATNAVSV MESGVANLKG VAVVSALFDK ESVLDATRNL HAILTEAASR TNETYM // ID B9TEA0_RICCO Unreviewed; 166 AA. AC B9TEA0; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 18. DE SubName: Full=Putative uncharacterized protein; DE Flags: Fragment; GN ORFNames=RCOM_1923810; OS Ricinus communis (Castor bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae; OC Acalyphoideae; Acalypheae; Ricinus. OX NCBI_TaxID=3988; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Hale; RX PubMed=20729833; DOI=10.1038/nbt.1674; RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D., RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., RA Gedil M., Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., RA Ravel J., Rabinowicz P.D.; RT "Draft genome sequence of the oilseed species Ricinus communis."; RL Nat. Biotechnol. 28:951-956(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ978850; EEF25813.1; -; Genomic_DNA. DR RefSeq; XP_002536569.1; XM_002536523.1. DR ProteinModelPortal; B9TEA0; -. DR GeneID; 8262514; -. DR KEGG; rcu:RCOM_1923810; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. FT NON_TER 166 166 SQ SEQUENCE 166 AA; 17533 MW; F00CC8357CA47ED1 CRC64; MGSPEDRCRL VLIVPQAEDA GLQAKALEDA LRGGDVASVI IPQYALDDDS FQKRAEVLVP IVQAAGAAAL VAGDSRVAGR VKADGLHVIG GVEPLAEAVE KFTPKMIVGG GNADDRHKAL EQGEANPDYI FFGKLEGDIK PEPHPKNVAL GEWWASMIEI PSIVMG // ID B9WDP8_CANDC Unreviewed; 512 AA. AC B9WDP8; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 19-FEB-2014, entry version 32. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme [includes: thiamine-phosphate pyrophosphorylase (Ec 2.5.1.3) hydroxyethylthiazole kinase (Ec 2.7.1.50)]; DE EC=2.7.1.50; GN ORFNames=CD36_82850; OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF OS 3949 / NRRL Y-17841) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; OC Candida. OX NCBI_TaxID=573826; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841; RX PubMed=19745113; DOI=10.1101/gr.097501.109; RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., RA Harris D., Aslett M., Barrell J.F., Butler G., Citiulo F., RA Coleman D.C., de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., RA Munro C.A., Pain A., Poulter R.T., Rajandream M.A., Renauld H., RA Spiering M.J., Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., RA Berriman M.; RT "Comparative genomics of the fungal pathogens Candida dubliniensis and RT Candida albicans."; RL Genome Res. 19:2231-2244(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM992690; CAX42804.1; -; Genomic_DNA. DR RefSeq; XP_002419215.1; XM_002419170.1. DR ProteinModelPortal; B9WDP8; -. DR STRING; 573826.CD36_82850; -. DR GeneID; 8046697; -. DR KEGG; cdu:CD36_82850; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 512 AA; 55417 MW; 3A7FF26C88226156 CRC64; MKVDYTLYLV TDSGMVPKSS SFLKQVADSI NYGATIVQLR EKSLSTSEFI KRAEQVHELT QKRGIPLIIN DRVDVALAVN AEGVHVGQDD MPAAIARKLI GDDKILGVTC SNVDEVQEVV DQGIADYVGL GTVYKTNTKK DVTNPEGTGP SGIRKMLQVL NKHNSKSGAK KIHSVAIGGI NDLNVRNVMF QCAIPGEKID GVAVVSCIMA NENAAEGTLL LLTLISGSPY WNIPHYDSKY IPDYEAQIKQ LTSSRPLIHH ITNNVVKNFS ANVTLAIGAS PIMSEFEEEF EELASIYNTA LVLNLGTPSK EMMKIFKNAI LAHQPRNPII FDPVGCGASR ARLECCKQLL DTGYFAVIKG NVGEILALQK LTSSYIELQD ISYMRGVDSV SDLTEEDIIY IGKQVSTEFK TVLVITGPTN YIIEGPNKVF KVQGGNKLMG SITGSGCALG STIAAFVTSQ AKSAYGLPSN FNAAVNAVKL YNKAGAAVSE KTPGKFMASF LDNLYRLTHF DS // ID B9XQ85_9BACT Unreviewed; 212 AA. AC B9XQ85; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Cflav_PD0968; OS Pedosphaera parvula Ellin514. OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Verrucomicrobia subdivision 3; Pedosphaera. OX NCBI_TaxID=320771; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ellin514; RX PubMed=21460084; DOI=10.1128/JB.00299-11; RA Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A., RA Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., RA Goodwin L., Pitluck S., Chertkov O., Larimer F.W., Land M.L., RA Hauser L., Brettin T.S., Detter J.C., Han S., de Vos W.M., RA Janssen P.H., Smidt H.; RT "Genome sequence of "Pedosphaera parvula" Ellin514, an aerobic RT Verrucomicrobial isolate from pasture soil."; RL J. Bacteriol. 193:2900-2901(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABOX02000052; EEF58003.1; -; Genomic_DNA. DR ProteinModelPortal; B9XQ85; -. DR EnsemblBacteria; EEF58003; EEF58003; Cflav_PD0968. DR PATRIC; 31332124; VBIBacEll73607_5940. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22633 MW; DBD0C0254226DB6A CRC64; MKSLSDCRLY TFVDTAYLHG RKPEVVAQQL CDGGSDIIQL RAKNSAENEV RRMAEAILPI TRRAGVPLVI NDFLSVAIEV GAEVCHLGQE DFFDGGYTHV SQLKDGKSNV EIGLSTHAPA QAERAIAAGP GYIAIGPIYA TGTKPTAKPV TLDYVRWAAA NVKIPWFAIG GINLTNLDQV LAAGAQRICV VSAILNAPDI AKACGEFKAR IT // ID B9XVM0_HELPX Unreviewed; 210 AA. AC B9XVM0; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 19-MAR-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HP9810_868g4; OS Helicobacter pylori 98-10. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=544405; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=98-10; RX PubMed=19123947; DOI=10.1186/1471-2164-10-3; RA McClain M.S., Shaffer C.L., Israel D.A., Peek R.M.Jr., Cover T.L.; RT "Genome sequence analysis of Helicobacter pylori strains associated RT with gastric ulceration and gastric cancer."; RL BMC Genomics 10:3-3(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABSX01000012; EEC22851.1; -; Genomic_DNA. DR ProteinModelPortal; B9XVM0; -. DR EnsemblBacteria; EEC22851; EEC22851; HP9810_868g4. DR PATRIC; 27521290; VBIHelPyl64770_0909. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22747 MW; B510B3FBE08DEF2F CRC64; MFVAGSQDFY HIKGGKNDRI NTLLDALELA LQSKITAFQF RQKGDLALQD PIEIKQLALK CQKLCQKYGA PFIVNDEVQL ALELKADGVH VGQEDMAIEE VMALCKKRLF IGLSVNTLEQ ALKVHHLDGV AYLGVGPIFP TQSKKDKQVV GVELLKKIKD SGVKKPLIAI GGITTHNASK LCEYGGIAVI SAIAQAKDKA LAVGKLLNNA // ID B9Y0M1_HELPX Unreviewed; 211 AA. AC B9Y0M1; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 19-MAR-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HPB128_180g32; OS Helicobacter pylori B128. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=544406; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B128; RX PubMed=19123947; DOI=10.1186/1471-2164-10-3; RA McClain M.S., Shaffer C.L., Israel D.A., Peek R.M.Jr., Cover T.L.; RT "Genome sequence analysis of Helicobacter pylori strains associated RT with gastric ulceration and gastric cancer."; RL BMC Genomics 10:3-3(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABSY01000015; EEC24434.1; -; Genomic_DNA. DR ProteinModelPortal; B9Y0M1; -. DR EnsemblBacteria; EEC24434; EEC24434; HPB128_180g32. DR PATRIC; 27525203; VBIHelPyl107473_1166. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23147 MW; 97A2BE7507617D1E CRC64; MFVAGSQDFY HIKGDKNDRI NALLETLELA LQSQITAFQF RQKGDLALQD PIEIKQLALE CQKLCQKYGV PFIVNDEVQL ALELKADGVH VGQEDMAIEE VITLCKKRLF IGLSVNTLEQ ALKARHLDAV AYFGVGPIFP TPSKKDAKEV VGINLLKKIH DSGVKKPLIA IGGITMHNAS KLREYGGIAV ISAITQAKDK ALAIEKLLNN A // ID B9Z1N5_9NEIS Unreviewed; 313 AA. AC B9Z1N5; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 16-OCT-2013, entry version 30. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN ORFNames=FuraDRAFT_1270; OS Pseudogulbenkiania ferrooxidans 2002. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Pseudogulbenkiania. OX NCBI_TaxID=279714; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2002; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Coates J.D.; RT "Sequencing of the draft genome and assembly of Lutiella nitroferrum RT 2002."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIS01000003; EEG09330.1; -; Genomic_DNA. DR ProteinModelPortal; B9Z1N5; -. DR EnsemblBacteria; EEG09330; EEG09330; FuraDRAFT_1270. DR PATRIC; 30252152; VBILutNit9412_1269. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 313 AA; 33616 MW; 44A39D5A7A83C77B CRC64; MQSDHKIIPV VAGALMRPDG SFMLGSRPEG KPYAGYWEFP GGKVEPGEAP FAALVREFHE EMGITVTHAT PWLTKVHHYE HASVHLTFYR IWAWEGTPQP HEEQAFAWQQ PGHYTVGPML PANGPILKSL ELPDVYAISC AHEIGIEAFL EALEARPELT LIQLREPQLG RDELAALAER VAAIVHPRGG KVVVNADPAW LAGWPVDGVH LNGKRLAEAT ARPAFAWVGA SVHSTAELNQ AAGLGLDYAL LGHVKATASH PGAAPLGWDG FECRLAGGTP LPVYALGGLS AADLIDARAH GAHGVALMRG AWR // ID B9Z7P1_9NEIS Unreviewed; 205 AA. AC B9Z7P1; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FuraDRAFT_3377; OS Pseudogulbenkiania ferrooxidans 2002. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Pseudogulbenkiania. OX NCBI_TaxID=279714; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2002; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Coates J.D.; RT "Sequencing of the draft genome and assembly of Lutiella nitroferrum RT 2002."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIS01000010; EEG07177.1; -; Genomic_DNA. DR ProteinModelPortal; B9Z7P1; -. DR EnsemblBacteria; EEG07177; EEG07177; FuraDRAFT_3377. DR PATRIC; 30256523; VBILutNit9412_3399. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21207 MW; 3EFC6A671F5ACAE0 CRC64; MATLEGLYAI TPDTDDSERL IERVSDVLPH GVRLLQYRNK SQDPVRRLWQ ANLLASLCHS HGVTFIVNDD VELALAVGAD GVHLGRDDAA IAAARARLGA DAIIGASCYD DIKLAEAAVA AGASYVAFGA VFPSGTKPHA VRAPLELFAQ AKRLGVPSAA IGGITADNAG EVISAGADML AVIGALFDAA DPAQTAEQLA AALRR // ID B9Z983_9NEIS Unreviewed; 213 AA. AC B9Z983; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FuraDRAFT_3920; OS Pseudogulbenkiania ferrooxidans 2002. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Pseudogulbenkiania. OX NCBI_TaxID=279714; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2002; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Coates J.D.; RT "Sequencing of the draft genome and assembly of Lutiella nitroferrum RT 2002."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIS01000019; EEG06665.1; -; Genomic_DNA. DR ProteinModelPortal; B9Z983; -. DR EnsemblBacteria; EEG06665; EEG06665; FuraDRAFT_3920. DR PATRIC; 30257670; VBILutNit9412_3944. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22083 MW; FB6714621084BFD2 CRC64; MNNATQRLTR PVWLDGLYAV TPDTSDSAWL LPRVAAVLAG GASLVQYRNK SRDTALRREQ AAAIQALCRQ HGAWFIVNDD VGLAEELGAD GVHLGQSDTS LCAARQRLGP HAIIGATCHD QPTLAAQAVG NGASYVAFGA LFPSRSKPET VSAPLALFAA LPPLEVPCVA IGGITPANAA LAWQTGVDML AVIGGLFDAP APDEAARAIL AAR // ID C0AXM4_9ENTR Unreviewed; 215 AA. AC C0AXM4; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PROPEN_02590; OS Proteus penneri ATCC 35198. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Proteus. OX NCBI_TaxID=471881; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35198; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35198; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Proteus penneri (ATCC 35198)."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVP01000025; EEG84235.1; -; Genomic_DNA. DR ProteinModelPortal; C0AXM4; -. DR EnsemblBacteria; EEG84235; EEG84235; PROPEN_02590. DR PATRIC; 36110268; VBIProPen132194_1698. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23828 MW; 45E30C98F52EFF88 CRC64; MNKSSNTPFA STEKKLGLYP VVDSIEWIER LLKTGVTTLQ LRIKDKQQED VEQEIIEAIK LGKQYHARLF INDYWQLAIK HQAYGVHLGQ EDLDIADLNA IKHAGLRLGI STHDEAELQK AKALYPSYIA LGHIFPTTTK EMPSKPQGLK ALKHQVEQTP DFPTVAIGGI SLERVPDVVA TGVGSVALVS AITKAPDWQQ VTRKLLELVE GKPSC // ID C0B7L5_9FIRM Unreviewed; 187 AA. AC C0B7L5; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=COPCOM_01138; OS Coprococcus comes ATCC 27758. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=470146; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27758; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27758; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Coprococcus comes (ATCC 27758)."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVR01000038; EEG90402.1; -; Genomic_DNA. DR ProteinModelPortal; C0B7L5; -. DR EnsemblBacteria; EEG90402; EEG90402; COPCOM_01138. DR PATRIC; 29070599; VBICopCom38835_0079. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 187 AA; 20814 MW; 95D6A86BBA0DBE8A CRC64; MYRDLIAVTN RHLCSRPFTE QITRVCKLHP KALILREKDL PEEEYFSLAR QVKEICEQFK VPFIPHFYPA VARELGCDRL HLPLPLLLEN PKVVSDFHTV GTSIHSVSEA VEAEKLGVSY LTAGHIYVTD CKKGLPPRGL PFLQNVCQAV QIPVYGIGGI KIDEAQLHEL KNAGAAGGCV MSGMMHV // ID C0BAI0_9FIRM Unreviewed; 212 AA. AC C0BAI0; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=COPCOM_02083; OS Coprococcus comes ATCC 27758. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=470146; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27758; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27758; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Coprococcus comes (ATCC 27758)."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVR01000041; EEG89104.1; -; Genomic_DNA. DR ProteinModelPortal; C0BAI0; -. DR EnsemblBacteria; EEG89104; EEG89104; COPCOM_02083. DR PATRIC; 29075864; VBICopCom38835_2667. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23007 MW; CFB623103376BC6B CRC64; MRLDKKDMVL YAVTDRHWLN GESLYSQVEK ALKGGATFIQ LREKNLGEEE FLAEAKEIAR LCKSYHVPFV INDNVEIAKK VDADGVHVGQ SDMEALDVRK TLGEDKIIGV TAKTVEQALK AQAHGADYLG VGAVFGTTSK ADATKLDHKI LKEICEKVEI PVVAIGGITE ENVTELAGNG ICGVAVISAV FGQPDIEQAT KELKEKVEGM LK // ID C0BSF4_9BIFI Unreviewed; 242 AA. AC C0BSF4; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BIFPSEUDO_03072; OS Bifidobacterium pseudocatenulatum DSM 20438 = JCM 1200 = LMG 10505. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=547043; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20438; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bifidobacterium pseudocatenulatum (DSM RT 20438)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20438; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXX02000002; EEG71104.1; -; Genomic_DNA. DR ProteinModelPortal; C0BSF4; -. DR EnsemblBacteria; EEG71104; EEG71104; BIFPSEUDO_03072. DR PATRIC; 26500333; VBIBifPse46839_0690. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 207 208 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 187 187 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 242 AA; 25668 MW; 573D3786A880CBF1 CRC64; MRDTFDMSAY FVVGPQDCKS RTITGVIEDA LRGGATFIQL RAKNTDAKDI TSMARDIAQV IENNGKSDSV AFVIDDRVDV VWQARHKGIK VDGVHIGQTD LEPQEARALL GEDAIVGLSA ETESLVKLIN ELPAGCIDYI GAGPLHVSTT KPEASVGGND GSGHTLDEAQ INAICDASDF PVVVGGGVTA DDMEMLAHSK AAGWFVVSAI AGASDPEEAT RNMVSRWKAV RGDAKHGHVL RK // ID C0BT93_9BIFI Unreviewed; 871 AA. AC C0BT93; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; ORFNames=BIFPSEUDO_03613; OS Bifidobacterium pseudocatenulatum DSM 20438 = JCM 1200 = LMG 10505. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=547043; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20438; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bifidobacterium pseudocatenulatum (DSM RT 20438)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20438; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXX02000003; EEG70594.1; -; Genomic_DNA. DR ProteinModelPortal; C0BT93; -. DR EnsemblBacteria; EEG70594; EEG70594; BIFPSEUDO_03613. DR PATRIC; 26501280; VBIBifPse46839_1152. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 871 AA; 96202 MW; B11F45F07A0B9F37 CRC64; MRDSFDLSAY FVVGPQDCKG RPITDVIDDA LRGGASFIQL RVKDADAKDL TDMARDIAQI IEDNNKSDSV AFVIDDRVDV VWQARSKGIK VDGVHIGQTD MEPREARALL GEDAIVGLSA ETESLVKLIN ELPDGCIDYI GAAPLHVSVT KPEASVGGND GSGRTLDEEQ INTICSASGF PVVVGGGVTA DDMEMLAHSK AAGWFVVSAI AGADDPEAAT RNMVARWKAV RGDTKHGYAP RVKAQKTAEI NTDNTADGAS GEKKFTNAKE AKAASKLAKQ QRVDIAARDS KQRDKAHIRK TTPVHFENEF GSYDLQVPYT EIKLSDTPGV GPNAPFKDYN TEGPKCDPKE GLAPLRLDWI LDRGDVEEYE GRRRNLEDDG KRAIKRGKAS KEWRGRQHKP MKAKDHPVTQ MWYARHNIIT PEMRYVAERE HCSVELVRSE LAAGRAVMPC NINHPEAEPM IIGSKFLTKL NANMGNSAVT SSIDEEVEKL TWATKWGADT VMDLSTGNDI HTTREWILRN SPVPIGTVPM YQALEKVEDD ASKLSWELFR DTVIEQCEQG VDYMTIHAGV LLRFVPLTAN RMTGIVSRGG SIMAEWCLQH HQESFLYTHF DELCEIFAKY DVAFSLGDGL RPGSLADAND AAQFAELMTL GELTQRAWEH DVQVMIEGPG HIPFDTVRMN IEMEKAICKD APFYTLGPLT TDTAPGYDHI TSAIGGVEIA RYGTAMLCYV TPKEHLGLPN KDDVKQGVIA YKIACHAADI AKHHPHAIDR DNAMSKARFE FRWLDQFNLS YDPDTAIAFH DDTLPAEPAK MAHFCSMCGP KFCSMAISQN IRKKFGNAEA QEKLVADAQT IAAGMQEMSE RFREQGGHLY Q // ID C0C4F7_9CLOT Unreviewed; 218 AA. AC C0C4F7; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLOHYLEM_06973; OS Clostridium hylemonae DSM 15053. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=553973; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15053; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium hylemonae (DSM 15053)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15053; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYI02000034; EEG72950.1; -; Genomic_DNA. DR ProteinModelPortal; C0C4F7; -. DR EnsemblBacteria; EEG72950; EEG72950; CLOHYLEM_06973. DR PATRIC; 30579549; VBICloHyl57588_2826. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23441 MW; AF8A3F599BE49800 CRC64; MKEHVMKFDK KSLLLYAVTD RRWLKGSTLT AQVEEAIRGG ATFIQLREKN LDEEQFLREA REVQQLCRSF HVPFVVNDNV EIAAAIDADG VHVGQSDMEA GDVRARLGHD KIIGVSAQTV EQALLAQERG ADYLGVGAVF STGSKADAVE VSHDTLKEIC RAVEIPVIAI GGIGRENVDM LAGSGICGVA VISAVFGAPD IRQAARELRG AAEKMVGV // ID C0C4N4_9CLOT Unreviewed; 194 AA. AC C0C4N4; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=CLOHYLEM_07050; OS Clostridium hylemonae DSM 15053. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=553973; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15053; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium hylemonae (DSM 15053)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15053; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYI02000034; EEG73027.1; -; Genomic_DNA. DR ProteinModelPortal; C0C4N4; -. DR EnsemblBacteria; EEG73027; EEG73027; CLOHYLEM_07050. DR PATRIC; 30579689; VBICloHyl57588_2896. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 21758 MW; 82EE5955E2361C76 CRC64; MHDNMEMSRG GIIAVTNRHL CRRPYLEQVE RICLRHPPAL IVREKDLAEE AYERLICEVR DICDAYDVFC IPHTYMEAAE RLRSCAVHLP LPLFRSCRDR ALRFRWAGTS VHSVQEALEA EALGAAYMTA GHVFSTDCKR GVLPRGTGFL KGVCEAVNVP VYAIGGMQGT ETCVREMSAF GASGICVMSE CMRW // ID C0CH78_9FIRM Unreviewed; 486 AA. AC C0CH78; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=RUMHYD_00191; OS Blautia hydrogenotrophica DSM 10507. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=476272; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 10507; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 10507; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Blautia hydrogenotrophica DSM 10507 RT (Ruminococcus hydrogenotrophicus DSM 10507)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACBZ01000004; EEG50897.1; -; Genomic_DNA. DR ProteinModelPortal; C0CH78; -. DR EnsemblBacteria; EEG50897; EEG50897; RUMHYD_00191. DR PATRIC; 38358121; VBIBlaHyd72091_0603. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 486 AA; 51766 MW; 26BCB32927EEA1B5 CRC64; MNFSKEEIRH SMLLYAITDR TWLKEGETLT SICEDVLKHG ATFLQIREKD LEPSAFQKEA LELKALCAKY QVPFVVNDSV EIALAIDADG VHVGQGDIQG KNLRALIGKD KILGISAATV AEAVAAQAAG ADYIGVGAVF GTSTKKNARN LSVEKLREIC AAVTIPVVAI GGIHALNLRK LSGSQVDGVA VISAIFSSDN PGKATSDLLS LARQLVQPTP RLMRTALSIA GSDCSGGAGI QADLKTMTMN GVYAMSAITA LTAQNTTKVE KIVETSPDFL KSQLDMIFTD IFPDAVKIGM LPNARLIEVL AERLRFYQAK HIVLDPVMVA TSGSILMETS AVLTLKKELL PLAELVTPNI PEAEILSERK ITTPEEIEAA AEFIGKTYHC AVLIKGGHSV NTANDLLWAD GQMEWFYGRC IPNPNTHGTG CTLSSAIAAN LAKGYSLSTS VQRAKKYLSG ALSAMLDLGA GSGPMNHAFC LTGEFS // ID C0CXB5_9CLOT Unreviewed; 212 AA. AC C0CXB5; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN Name=thiE; ORFNames=CLOSTASPAR_01636; OS Clostridium asparagiforme DSM 15981. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=518636; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15981; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15981; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium asparagiforme (DSM 15981)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCJ01000080; EEG56295.1; -; Genomic_DNA. DR ProteinModelPortal; C0CXB5; -. DR EnsemblBacteria; EEG56295; EEG56295; CLOSTASPAR_01636. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT NON_TER 212 212 SQ SEQUENCE 212 AA; 22635 MW; 1B43AECD1BECA48B CRC64; MRCDKKDLLL YAVTDRSWLN GATLYEQVEA ALRGGATFIQ LREKALDQER FLAEARELKA LCRRFGVPFL INDNVEIAAA VDADGVHVGQ SDMEAGDVRA RLGADKIIGV SAQTVEQALL AQQRGADYLG VGAVFPTGTK QDATDVSYET LRDICRAVDI PVIAIGGIGR GNVERLAGSG ICGVAVVSAI FAQKQIEAAT ADLKAAVERM VK // ID C0DUN4_EIKCO Unreviewed; 206 AA. AC C0DUN4; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EIKCOROL_01070; OS Eikenella corrodens ATCC 23834. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Eikenella. OX NCBI_TaxID=546274; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23834; RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E., RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEA01000017; EEG24432.1; -; Genomic_DNA. DR ProteinModelPortal; C0DUN4; -. DR EnsemblBacteria; EEG24432; EEG24432; EIKCOROL_01070. DR PATRIC; 29267171; VBIEikCor39471_1099. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22133 MW; 6A2DC1F64320EAE0 CRC64; MQPFPPVVRP LKFYAVVPDA DWVARMVEAG ADTVQLRSKH LTGEALRREI RRVIAATRDS HSQLFINDHW QLALEEGAYG VHLGQEDMDS ADFAALARAG IRLGLSTHDE AEMARALAVQ PSYVACGAVF ATNTKAMPTE PQGLDKLRRY VQQAGNTPTV AIGGITLENA PAVLATGVSS LAVVSAVTHA PDPAAAVRAF QKLWPE // ID C0E0G1_9CORY Unreviewed; 730 AA. AC C0E0G1; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.7.4.7; GN Name=thiD; ORFNames=CORMATOL_00461; OS Corynebacterium matruchotii ATCC 33806. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=566549; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33806; RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E., RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEB01000004; EEG28052.1; -; Genomic_DNA. DR ProteinModelPortal; C0E0G1; -. DR EnsemblBacteria; EEG28052; EEG28052; CORMATOL_00461. DR PATRIC; 25303818; VBICorMat118582_0527. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.910.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF03070; TENA_THI-4; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; SSF48613; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Transferase. SQ SEQUENCE 730 AA; 77752 MW; 030EF0BA7A4670B5 CRC64; MREPIWDLYL VTDPGSDPDA VPAIVTQAIT GGVTVVQLRD KHATKPQIRQ RAQALKDAIQ AVTAVSNADP STIPLFINDH VDIAAELGLH AHIGQGDLSY VAARRQLPAE LMLGLSIETA DQLEHVVETC HASGVRLPDV VGIGPVRATE TKPDHATPLG VARVQRIARM AAAHGIKSVA IGGVDKHIAA ELQQVDGVCV VSAIMSSPDP AAAAGELRAA FAMRRPSAPR VLSIAGTDPT GGAGAQADLK SIAAAGGYGM NAITALVAQN THGVRSIHTP PLSFLREQLD AVVSDVTIDA VKIGMLGSAD IVACVRQWLA EHPMPLVVLD PVMVATSGDR LLDPDAEQAV IEFAHHVDIV TPNVPELAVL LSAPEPARTF EEALSQAAEF AQKSNTIVIA KGGHLDGKLA NNAVVYPDGR ITTITTPRID TTNTHGTGCS LSSALATRLA AGDTITEAIE WVSYWLADSI RAGAALEVGT PGGHGPIDHF HQVRRQAACA STKPWKFTGE VRYRPTIPAA GPYTQSLWDS MGEVWSQIMG LPFIMGLRDG SLSKREFDFY LNQDAHYLAN YSRALAVLAA KAGEPQYQVE WAESARDCLV VEAQLHHEWL GGISGDTSPV TLGYTNFLTA TAYGDDYVVG AAAVLPCYWI YAEVGACLAA SNHPDHPYHE WLKTYGDQSF VTTTEAALRR VEHALVQATG VQRAAATAAF QVACAYEREF FDQASRSEIR // ID C0EIR1_9CLOT Unreviewed; 201 AA. AC C0EIR1; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=CLOSTMETH_03756; OS Clostridium methylpentosum DSM 5476. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=537013; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 5476; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 5476; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium methylpentosum (DSM 5476)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEC01000129; EEG28648.1; -; Genomic_DNA. DR ProteinModelPortal; C0EIR1; -. DR EnsemblBacteria; EEG28648; EEG28648; CLOSTMETH_03756. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 22012 MW; 6CF904EB2551306C CRC64; MIICVTNRIL CRDDFLVRLE EIAAARPWGI LLREKDLAAE EYATLAMTCS AICQRHQTRL LVHSHPALAE QLPPHWLHLP FPLFERSKRE GLHTSVSVHS AEEAVRAETV GAHCLVAGHI FSTACKPGLP PRGIGFLRAV CQSVSIPVFA IGGMSAERVS EVMGAGAAGI CVMSELMTCS DPGNRIREYK RRIGAVKEGY Q // ID C0EIR5_9CLOT Unreviewed; 216 AA. AC C0EIR5; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLOSTMETH_03760; OS Clostridium methylpentosum DSM 5476. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=537013; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 5476; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 5476; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium methylpentosum (DSM 5476)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEC01000129; EEG28652.1; -; Genomic_DNA. DR ProteinModelPortal; C0EIR5; -. DR EnsemblBacteria; EEG28652; EEG28652; CLOSTMETH_03760. DR PATRIC; 30592600; VBICloMet71124_2419. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23167 MW; 420420C2872B44AA CRC64; MFDQEKLRRA LRLYAVTSRN WLGKWTLAEQ VEQALRGGAT MVQLREKTLG DDELLLEAQA IRLVTAQYGS PLILNDRPDL VERCGADGVH IGQGDCSAKQ ARREIGPERI LGISAHSVDE ALRAQEEGAD YLGVGAAFGS ATKTDAVTTS PDVIRAICHA VEIPVVAIGG IEQENIHKLS GCGLAGVAVV SALFAQPDVR EAAQRMRVLS ERVTAG // ID C0ERB4_NEIFL Unreviewed; 205 AA. AC C0ERB4; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NEIFLAOT_02515; OS Neisseria flavescens NRL30031/H210. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=546264; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRL30031/H210; RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E., RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEN01000110; EEG32411.1; -; Genomic_DNA. DR ProteinModelPortal; C0ERB4; -. DR EnsemblBacteria; EEG32411; EEG32411; NEIFLAOT_02515. DR PATRIC; 29957153; VBINeiFla114371_2143. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22018 MW; 66567F5B4B96B821 CRC64; MTFPPLKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKTL HGDELKREIE RCVTACQNSA TQLFINDHWR EAIAAGAYGV HLGQEDMDTA DLAAIEAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV RQAHGTPVVA IGGIDLNNAQ AVLATGVSSL AVVRAVTEAE NPEAVVKAFQ ALWNE // ID C0EVF8_9FIRM Unreviewed; 249 AA. AC C0EVF8; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=EUBHAL_01396; OS Eubacterium hallii DSM 3353. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=411469; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3353; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3353; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Eubacterium hallii (DSM 3353)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEP01000064; EEG36813.1; -; Genomic_DNA. DR ProteinModelPortal; C0EVF8; -. DR EnsemblBacteria; EEG36813; EEG36813; EUBHAL_01396. DR PATRIC; 30667648; VBIEubHal63356_1229. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 249 AA; 27858 MW; 8EC7D0D251519248 CRC64; MIIFMCKRRN QNSTKDLKQQ LIKNGTYQNR DYQGKNFEKK NTTGGEFNSI LKNSVLEKSD ILCITNRKLC KDDFLKRIQI IAAAQPKAIV LREKDLSEEA YTILAEKVMH ICEKYSVPCI LHSFAKAAMA LNVKAIHMPL PLLRKMTPQE KNHFEIIGAS CHSLEEAKEA ERLGCTYITA GHIFLTDCKK GLPGRGLTFL QNICENVSIP VYAIGGISNE NINDVRQTGA AGACIMSGFM KCNNIAEII // ID C0EZ08_9FIRM Unreviewed; 217 AA. AC C0EZ08; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUBHAL_02664; OS Eubacterium hallii DSM 3353. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=411469; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3353; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3353; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Eubacterium hallii (DSM 3353)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEP01000117; EEG35493.1; -; Genomic_DNA. DR ProteinModelPortal; C0EZ08; -. DR EnsemblBacteria; EEG35493; EEG35493; EUBHAL_02664. DR PATRIC; 30669981; VBIEubHal63356_2352. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23912 MW; CDAA65AC5708EB64 CRC64; MSCVNREQLR KDLLLYAVTD RSWLGNETLY EQVEKALKGG ATFIQLREKE LMRNISWKKR WLSKNCVISI MFHLLSMIMS ESQKIWMRME VHVGQSDMEA DDVRKILGED KILGVSAQTV EQAVLAEKMG ADYLGVGAVF STSTKKDAAD VSKETLKAIC EAVNIPVIAI GGIGADNILS LQGSGICGIA VVSAIFAAKD IEAATKVLKD RTEKMLK // ID C0FNC9_9FIRM Unreviewed; 243 AA. AC C0FNC9; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ROSEINA2194_00223; OS Roseburia inulinivorans DSM 16841. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=622312; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16841; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16841; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Roseburia inulinivorans (DSM 16841)."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFY01000008; EEG95914.1; -; Genomic_DNA. DR ProteinModelPortal; C0FNC9; -. DR EnsemblBacteria; EEG95914; EEG95914; ROSEINA2194_00223. DR PATRIC; 30045915; VBIRosInu13871_0199. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 72 76 HMP-PP binding (By similarity). FT REGION 169 171 THZ-P binding (By similarity). FT REGION 219 220 THZ-P binding (By similarity). FT METAL 105 105 Magnesium (By similarity). FT METAL 124 124 Magnesium (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 HMP-PP (By similarity). FT BINDING 199 199 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 243 AA; 26596 MW; 5A584E221852B061 CRC64; MKNKFFTLEI CVCAHLTQTR YAQKACAEMR IKMNITREQL KLYAVTDRSW LGSETLYEQV EKALKGGVTL VQLREKTLDE AAFEKEGQEL LELCHHYNVP LIINDNVELA KKIHADGVHI GQSDMEIKNA RELLGADKII GVTAKTIEQA KAAETAGADY LGSGAVFGTS TKADAKPMEL DLFQEICESV TIPVVAIGGI NADNVLRLKG RKMAGAAVVS GIFACEDIEK GTRELLEKVA SII // ID C0G3Y0_9RHIZ Unreviewed; 203 AA. AC C0G3Y0; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-MAR-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BCETI_1000384; OS Brucella ceti str. Cudo. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=595497; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cudo; RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., RA Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Bruce D.H., Detter C., Munk C., Brettin T.S., Ficht T.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJD01000001; EEH15445.1; -; Genomic_DNA. DR ProteinModelPortal; C0G3Y0; -. DR EnsemblBacteria; EEH15445; EEH15445; BCETI_1000384. DR PATRIC; 35209175; VBIBruCet28239_0406. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C0G8A6_9RHIZ Unreviewed; 221 AA. AC C0G8A6; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-MAR-2014, entry version 23. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BCETI_6000072; OS Brucella ceti str. Cudo. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=595497; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cudo; RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., RA Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Bruce D.H., Detter C., Munk C., Brettin T.S., Ficht T.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJD01000006; EEH13170.1; -; Genomic_DNA. DR ProteinModelPortal; C0G8A6; -. DR EnsemblBacteria; EEH13170; EEH13170; BCETI_6000072. DR PATRIC; 35212700; VBIBruCet28239_2127. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C0GEC4_9FIRM Unreviewed; 197 AA. AC C0GEC4; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 22. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=DealDRAFT_0833; OS Dethiobacter alkaliphilus AHT 1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae; OC Dethiobacter. OX NCBI_TaxID=555088; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AHT 1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Muyzer G.; RT "Sequencing of the draft genome and assembly of Dethiobacter RT alkaliphilus AHT 1."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJM01000003; EEG78418.1; -; Genomic_DNA. DR ProteinModelPortal; C0GEC4; -. DR EnsemblBacteria; EEG78418; EEG78418; DealDRAFT_0833. DR PATRIC; 26638335; VBIDetAlk125442_0796. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 197 AA; 21231 MW; 35C6779BAEBD4F91 CRC64; MKNKLFVVTN RKLVKDGTLC DAVNRACPFA DAIILREKDL SHQELLDLAQ QVKKITDSYN TPLIINNNLQ VAGQIEAFGY HSGIKNYRQE NVRTRLGLSI HTIEEALTAQ KLGADYIIAG NIFKTDCKPG LGGKGLSFVE AVTSSVSIPV IAIGGISTDN VSAVIKAGAH GIAVMSSAME DADGSYLKSL RSRLEEI // ID C0GKK2_9FIRM Unreviewed; 216 AA. AC C0GKK2; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DealDRAFT_3011; OS Dethiobacter alkaliphilus AHT 1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae; OC Dethiobacter. OX NCBI_TaxID=555088; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AHT 1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Muyzer G.; RT "Sequencing of the draft genome and assembly of Dethiobacter RT alkaliphilus AHT 1."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJM01000024; EEG76169.1; -; Genomic_DNA. DR ProteinModelPortal; C0GKK2; -. DR EnsemblBacteria; EEG76169; EEG76169; DealDRAFT_3011. DR PATRIC; 26642756; VBIDetAlk125442_2955. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23302 MW; 976B12802B2FD2CE CRC64; MRKNVAEIFQ TDIYGVTCES LSACKDNLEV VRRMIDAGVK IIQYREKDKT KREKYEECRV IREMCKPAGV LFIVNDDVDI AILSKAGGVH VGPDDLPANA VRKLVGEEMI IGVSADTPAD VEDAMVRGAD YVGVGPVFKT GTKADAGEPV GLDLIEHIAK NYKIPLVAIG GINGENIVDV RRRGVPCSAM VSALVSCADV EAEVKKIRQL IAESGC // ID C0N961_9GAMM Unreviewed; 480 AA. AC C0N961; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=MDMS009_2833; OS Methylophaga thiooxydans DMS010. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Methylophaga. OX NCBI_TaxID=637616; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DMS010; RA Schaefer H., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DMS010; RX PubMed=21478352; DOI=10.1128/JB.00388-11; RA Boden R., Ferriera S., Johnson J., Kelly D.P., Murrell J.C., RA Schafer H.; RT "Draft Genome Sequence of the Chemolithoheterotrophic, Halophilic RT Methylotroph Methylophaga thiooxydans DMS010."; RL J. Bacteriol. 193:3154-3155(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657906; EEF78660.1; -; Genomic_DNA. DR ProteinModelPortal; C0N961; -. DR EnsemblBacteria; EEF78660; EEF78660; MDMS009_2833. DR PATRIC; 26229341; VBIMetThi34374_2846. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 480 AA; 52667 MW; 78B19515CDBB5055 CRC64; MAKPAVLLIG GLDPQGCAGI AADIATVQHH DCHPLPLITA MTEQSSAGLT ALGAVNTNKL MAQYRNCKAD FDIQAIKVGL IPDLIIAEKV KQILLDNPGI PVVMDPVLAS SSGGKTVADG VRQYIRDELL QHLTLLTPNL PELSLLTDNL EDVEQATTIL SQKGLQACLV KGGHADSEFA TDFFISEQVR FYCYQTKYAS DVRGTGCVLA SAIASHLASG QDMRDAVVLA KTYVSRGIRQ AQTVGSYRLI KHSHEPWALE DIPRLCYQKT LIGQQFNFPS CPSRLGIYPV VDNAEWVQKL VDIGIETIQL RVKDRDEKTT SQQIKQAVEY LGHKPVNFFV NDHWQIAIEQ GAYGVHLGQE DLHDANLKQI VDAGLRLGIS THSYWELARA LAVNPSYIAL GPIFETTSKQ MPFSPQGVER LKQWVTMLDG NYPIVAIGGI NYERARLLKP TGVGSVAMIT AITLADDYQK TTRDLLALWQ // ID C0NLZ3_AJECG Unreviewed; 520 AA. AC C0NLZ3; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 16-APR-2014, entry version 29. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HCBG_04523; OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC OS 2432) (Darling's disease fungus) (Histoplasma capsulatum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Ajellomyces. OX NCBI_TaxID=447093; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432; RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B., RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Walk T., White J., Yandava C., Klein B., McEwen J.G., Puccia R., RA Goldman G.H., Felipe M.S., Nino-Vega G., San-Blas G., Taylor J., RA Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.; RT "The genome sequence of Ajellomyces capsulatus strain G186AR."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG663367; EEH07644.1; -; Genomic_DNA. DR ProteinModelPortal; C0NLZ3; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 2. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 520 AA; 55114 MW; 9987F4B69D6091B5 CRC64; MDLSVYLVTD STPAILRGRD LCVVVQDAIQ GGVTVVQYRD KHSDSGVMIE TAKRLHEITK KHNVPLIIND RVDVALAVGA EGVHLGQDDM ISSNKEALKA VQDGADYLGI GTVFATPTKT NTKSIIGPAG TREILAFLST MPRRVGTVAI GGINLSNVQR VIYQSQAPLK SLDGAAIVSA IMAAENPREA AALFCKLVKQ IPALATIPLP PRENEVTLLL DQVPDIVNLV ATRRPLCHNM INFVVANFAA NVAIAIGASP IMSGYGPEAV DLAKNGGSLL INMGTLNNES IDNYLQALQA YNAEGNPVVF DPVGAGATDV RRKAAKQLMA GGYFDLIKGN ESELIQVYGK VRGQQIGVDS GPSTLNCKEK ARLVMDLAKR ERNIALLTGA VDYLSDGERT LAIGNGHSLL GHITGTGCII GTIAASFLAV HRSDKLLAVL ASLLLLEIAA ERAAVKDGVH GPGTFLPALI DELFALRMWA VERKNGGTSS GEASKTSNCE AATVDENIFK KMAKVHLIHP // ID C0Q2S5_SALPC Unreviewed; 211 AA. AC C0Q2S5; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPC_3994; OS Salmonella paratyphi C (strain RKS4594). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=476213; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RKS4594; RX PubMed=19229335; DOI=10.1371/journal.pone.0004510; RA Liu W.Q., Feng Y., Wang Y., Zou Q.H., Chen F., Guo J.T., Peng Y.H., RA Jin Y., Li Y.G., Hu S.N., Johnston R.N., Liu G.R., Liu S.L.; RT "Salmonella paratyphi C: genetic divergence from Salmonella RT choleraesuis and pathogenic convergence with Salmonella typhi."; RL PLoS ONE 4:E4510-E4510(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000857; ACN48061.1; -; Genomic_DNA. DR RefSeq; YP_002639502.1; NC_012125.1. DR ProteinModelPortal; C0Q2S5; -. DR STRING; 476213.SPC_3994; -. DR EnsemblBacteria; ACN48061; ACN48061; SPC_3994. DR PATRIC; 32366968; VBISalEnt12305_4056. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT476213:GH8J-4064-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22950 MW; 088AE10486472682 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE VGVRTIQLRI KDKRNEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSVAVVSAIT QAADWREATA QLLAIVGVGD E // ID C0QA61_DESAH Unreviewed; 219 AA. AC C0QA61; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HRM2_15370; OS Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfobacterium. OX NCBI_TaxID=177437; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43914 / DSM 3382 / HRM2; RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x; RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., RA Andres S., Henne A., Fricke W.F., Martinez-Arias R., Bartels D., RA Goesmann A., Krause L., Puhler A., Klenk H.P., Richter M., Schuler M., RA Glockner F.O., Meyerdierks A., Gottschalk G., Amann R.; RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine RT sulfate reducer oxidizing organic carbon completely to carbon RT dioxide."; RL Environ. Microbiol. 11:1038-1055(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001087; ACN14646.1; -; Genomic_DNA. DR RefSeq; YP_002602809.1; NC_012108.1. DR ProteinModelPortal; C0QA61; -. DR STRING; 177437.HRM2_15370; -. DR EnsemblBacteria; ACN14646; ACN14646; HRM2_15370. DR GeneID; 7500892; -. DR KEGG; dat:HRM2_15370; -. DR PATRIC; 21682725; VBIDesAut25181_1640. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HVAANIA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DAUT177437:GHLR-1537-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23595 MW; 66CF0628159EACE2 CRC64; MTARLNPGIY GILTEKFSRG RSNIQVAQEM VNAGVTTLQY REKPASKSMG EMYKECVAIR QITRDAGVTF IVNDHADLAL MVEADGIHTG QDDLPLRPLR KLVGDMIIGR STHSLDQARQ AVLEGADYIG VGPIFTTQTK EGVCDAVGLA YLDHVAANIA IPFVAIGGIK AHNLGQVVSH GARTVCMITE IIGAEDIKAT IQGLQTIYKD TSAKLYQAL // ID C0QQG3_PERMH Unreviewed; 186 AA. AC C0QQG3; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Thiamine-phosphate pyrophosphorylase (TMPpyrophosphorylase) (TMP-PPase) (Thiamine-phosphate synthase); DE EC=2.5.1.3; GN OrderedLocusNames=PERMA_1123; OS Persephonella marina (strain DSM 14350 / EX-H1). OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; Persephonella. OX NCBI_TaxID=123214; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14350 / EX-H1; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the RT Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001230; ACO04246.1; -; Genomic_DNA. DR RefSeq; YP_002730909.1; NC_012440.1. DR ProteinModelPortal; C0QQG3; -. DR STRING; 123214.PERMA_1123; -. DR EnsemblBacteria; ACO04246; ACO04246; PERMA_1123. DR GeneID; 7675385; -. DR KEGG; pmx:PERMA_1123; -. DR PATRIC; 22915711; VBIPerMar119911_1162. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR123214:GIZP-1122-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 186 AA; 20985 MW; 6ED3742359CE6306 CRC64; MHQILKKFYA ITDRKQFKYD FETQIKRMLD AGIRFFQLRE KDLPSSELFR YAKIMEDLLK GYDAFFTVNE RVDIAVLTGA AGVHLPENSI PLDVVKHKFP DLIVGKSCHS LESALKAEED GADYIFFSPI FETPGKGKPV GLEELKKVVE NVNIPVYALG GITEDRIPDV LKTGVYGIAG IRLFIS // ID C0R1J5_BRAHW Unreviewed; 233 AA. AC C0R1J5; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BHWA1_01513; OS Brachyspira hyodysenteriae (strain ATCC 49526 / WA1). OC Bacteria; Spirochaetes; Spirochaetales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=565034; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49526 / WA1; RX PubMed=19262690; DOI=10.1371/journal.pone.0004641; RA Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P., RA Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A., RA Barrero R., Phillips N.D., Hampson D.J.; RT "Genome sequence of the pathogenic intestinal spirochete Brachyspira RT hyodysenteriae reveals adaptations to its lifestyle in the porcine RT large intestine."; RL PLoS ONE 4:E4641-E4641(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001357; ACN83983.1; -; Genomic_DNA. DR RefSeq; YP_002721687.1; NC_012225.1. DR ProteinModelPortal; C0R1J5; -. DR STRING; 565034.BHWA1_01513; -. DR EnsemblBacteria; ACN83983; ACN83983; BHWA1_01513. DR GeneID; 7666608; -. DR KEGG; bhy:BHWA1_01513; -. DR PATRIC; 21181093; VBIBraHyo62857_1475. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BHYO565034:GJI7-1504-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 59 63 HMP-PP binding (By similarity). FT REGION 159 161 THZ-P binding (By similarity). FT REGION 210 211 THZ-P binding (By similarity). FT METAL 95 95 Magnesium (By similarity). FT METAL 114 114 Magnesium (By similarity). FT BINDING 94 94 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 162 162 HMP-PP (By similarity). FT BINDING 190 190 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 26423 MW; 4E521B7BED5324F9 CRC64; MKGIEDIINT KDINKRREIL KEKYFKDSIY CVTAEDFSNG RNNIEVVKSM LEAGIKIIQY REKDNPNKYM REKYGECLKI RELTKEYDAL FIIDDYADLA IAVEADGVHI GQKDMPIEAV RKIVGYDKIV GLSTTNEKQA MEAVKTSADY IGIGPIFSTN TKPDANEATG IDYLDYVVKN LDVPFVCIGG IKLNNMDLLI EHKAMSLCML TEIVSSEDIK SKCELLIKKM KKL // ID C0REX0_BRUMB Unreviewed; 221 AA. AC C0REX0; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=BMEA_A1760; OS Brucella melitensis biotype 2 (strain ATCC 23457). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=546272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23457; RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., RA Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Munk C., Tapia R., Han C., Detter J.C., Bruce D., Brettin T.S.; RT "Brucella melitensis ATCC 23457 whole genome shotgun sequencing RT project."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001488; ACO01442.1; -; Genomic_DNA. DR RefSeq; YP_002733396.1; NC_012441.1. DR ProteinModelPortal; C0REX0; -. DR STRING; 546272.BMEA_A1760; -. DR EnsemblBacteria; ACO01442; ACO01442; BMEA_A1760. DR GeneID; 7676940; -. DR KEGG; bmi:BMEA_A1760; -. DR PATRIC; 17839308; VBIBruMel14466_1779. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BMEL546272:GJOX-1716-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23242 MW; 9838EBF5FD9C7A47 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAIEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C0RGR2_BRUMB Unreviewed; 203 AA. AC C0RGR2; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BMEA_A0221; OS Brucella melitensis biotype 2 (strain ATCC 23457). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=546272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23457; RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., RA Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Munk C., Tapia R., Han C., Detter J.C., Bruce D., Brettin T.S.; RT "Brucella melitensis ATCC 23457 whole genome shotgun sequencing RT project."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001488; ACO00020.1; -; Genomic_DNA. DR RefSeq; YP_002731974.1; NC_012441.1. DR ProteinModelPortal; C0RGR2; -. DR STRING; 546272.BMEA_A0221; -. DR EnsemblBacteria; ACO00020; ACO00020; BMEA_A0221. DR GeneID; 7677442; -. DR KEGG; bmi:BMEA_A0221; -. DR PATRIC; 17836140; VBIBruMel14466_0233. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BMEL546272:GJOX-211-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C0SAM9_PARBP Unreviewed; 91 AA. AC C0SAM9; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=PABG_04734; OS Paracoccidioides brasiliensis (strain Pb03). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; mitosporic Onygenales; Paracoccidioides. OX NCBI_TaxID=482561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pb03; RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345; RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., RA Goldberg J., Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., RA Grynberg M., Gujja S., Heiman D.I., Henn M.R., Kodira C.D., RA Leon-Narvaez H., Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., RA Morais F.V., Pereira M., Rodriguez-Brito S., Sakthikumar S., RA Salem-Izacc S.M., Sykes S.M., Teixeira M.M., Vallejo M.C., RA Walter M.E., Yandava C., Young S., Zeng Q., Zucker J., Felipe M.S., RA Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G., Puccia R., RA San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.; RT "Comparative genomic analysis of human fungal pathogens causing RT paracoccidioidomycosis."; RL PLoS Genet. 7:E1002345-E1002345(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS544809; EEH22523.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 91 AA; 9878 MW; 2FAA0AEEF425999A CRC64; MDLSVYLVTD STPAILGDRD LCEVVRDAIE GGVTVVQYRD KHSDTGVLIE TAKKLHEITK AYNVPLIIND RVDVALVVGA EGVHLGQDDM S // ID C0VJL7_9GAMM Unreviewed; 203 AA. AC C0VJL7; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0023_1336; OS Acinetobacter sp. ATCC 27244. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=525244; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27244; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYN01000080; EEH69116.1; -; Genomic_DNA. DR ProteinModelPortal; C0VJL7; -. DR EnsemblBacteria; EEH69116; EEH69116; HMPREF0023_1336. DR PATRIC; 24343584; VBIAciSp60119_0348. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21678 MW; 6AE268F81E1EA12A CRC64; MRGLYLITND DPIQLLLEKL EVALATGKVA ILQYRRKKVA KIDQPMEVEQ IKTLCEKYQV PFVINDDLAL AEQFGLGVHL GQSDGEISDA AARLPHGVII GRTCLNSLEL AEKAIADGAT YVAFGAVYAT STKPEAGNVG IEVIKQAKQK FAVPICAIGG LTVENSQVVI EAGASLCAVI SDILGRSTAE IPARVNAWAT LFD // ID C0VPI5_9GAMM Unreviewed; 303 AA. AC C0VPI5; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 16-OCT-2013, entry version 29. DE SubName: Full=Mutator mutT protein; DE EC=3.6.1.-; GN ORFNames=HMPREF0023_3054; OS Acinetobacter sp. ATCC 27244. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=525244; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27244; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYN01000218; EEH67414.1; -; Genomic_DNA. DR ProteinModelPortal; C0VPI5; -. DR EnsemblBacteria; EEH67414; EEH67414; HMPREF0023_3054. DR PATRIC; 24345628; VBIAciSp60119_0997. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 303 AA; 34849 MW; 11F0112765CB9AF0 CRC64; MAKSIVEVAI AILLHKSKVL VGWRQANQHQ GNKHEFPGGK VEQHETPEQA CRREIYEEVG IGLKDWHKFD VIQHEYDDLI VRLHLFHAHV PDQFLDLIHQ PWTWYSRDQL QNLNFPKANK TIIERLVWSH LIKISDLLSA LPHSDAQFYW RNEKLNIVEV QQQLSILTDD QLNKLIINFS LWQQLDSKLQ AKIQTIHLKQ SQLMRFKNGE LIVGKRFIAA CHDAVSLKHA HDIGCDAVFL SPVNQTETHL QAKVLGWDGF SELAENSDIP VFALGGVAPK DIEQAQKHHA YGLAGIREFE SIE // ID C0VS22_9CORY Unreviewed; 217 AA. AC C0VS22; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0294_0505; OS Corynebacterium glucuronolyticum ATCC 51867. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=548477; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51867; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYP01000006; EEI27891.1; -; Genomic_DNA. DR ProteinModelPortal; C0VS22; -. DR EnsemblBacteria; EEI27891; EEI27891; HMPREF0294_0505. DR PATRIC; 25287439; VBICorGlu132174_1797. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22747 MW; 880CB9E978619D1C CRC64; MATNWSLYLV TDPQQGGGPE NVAPIVDKAI KGGVSVVQLR DKDATEAEFL ARAIKLKELM EPTGVPLFVD DRLDVACELG LNLHIGQNDV DYLEARKKLP GNLMLGLSVG NHRELDEVER MDPALRPDVI GVGPVADTTT KKDAPAGIGV QAFAEIATRA KGLGVPAVAI GGVNLTNASE LGGTDGAGIC VVSAIMKAAD PEEAARELRA AFENGRN // ID C0VS26_9CORY Unreviewed; 51 AA. AC C0VS26; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 11-DEC-2013, entry version 21. DE SubName: Full=Multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN ORFNames=HMPREF0294_0509; OS Corynebacterium glucuronolyticum ATCC 51867. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=548477; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51867; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYP01000006; EEI27895.1; -; Genomic_DNA. DR EnsemblBacteria; EEI27895; EEI27895; HMPREF0294_0509. DR PATRIC; 25287445; VBICorGlu132174_1800. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Kinase; Transferase. SQ SEQUENCE 51 AA; 5493 MW; 68E5B2A296232E9D CRC64; MATDWTLYLV TDPDLGGGPE RVPEIVDKAV KGGVSVVQLR EKHAQLPSGD F // ID C0WAH0_9FIRM Unreviewed; 205 AA. AC C0WAH0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=ACDG_00461; OS Acidaminococcus sp. D21. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=563191; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D21; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Sibley C., White A., Lander E., Nusbaum C., RA Galagan J., Birren B.; RT "The Genome Sequence of Acidaminococcus sp. D21."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGB01000005; EEH90102.1; -; Genomic_DNA. DR ProteinModelPortal; C0WAH0; -. DR EnsemblBacteria; EEH90102; EEH90102; ACDG_00461. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 205 AA; 22587 MW; 6033630CB147FF90 CRC64; MNASFPYVLV TDRTIYPEPL IPYLKKRIPD LSPFPSALIL REKDLSKEAY EDLFKETAHL CKAWKLPLLA HNHPDLALDD AIAGVHMPLR SWTAWSKMHP QEAGCLLEKG KTKLPYPHGV GISIHFLSEV ETALQSGASY LIVSPLFPTS CKPNNLPLGL TPLPNFIHSS PLPIYVLGGL SWPDPRASLL EALGVRGAVI RSAIV // ID C0WDK8_9FIRM Unreviewed; 215 AA. AC C0WDK8; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ACDG_01549; OS Acidaminococcus sp. D21. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=563191; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D21; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Sibley C., White A., Lander E., Nusbaum C., RA Galagan J., Birren B.; RT "The Genome Sequence of Acidaminococcus sp. D21."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGB01000033; EEH91190.1; -; Genomic_DNA. DR ProteinModelPortal; C0WDK8; -. DR EnsemblBacteria; EEH91190; EEH91190; ACDG_01549. DR PATRIC; 24313817; VBIAciSp85863_1629. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22985 MW; 6EE00CC7C93FDFBF CRC64; MKRTIDYSLY LVTDRKVTDK KGRDFYEAVE EALQAGITLV QLREKDVTTE ERIAIGRKVK ILCDHYDVPL LVDDDIACAK AIGADGVHLG QSDESLARGR QELGNDAIIG ISAHNLEEAQ AALRGGADYL GVGALYPTET KKDASCLGLG PFREIIAAIS LPIVGIGGIG KKEFPEVMKC GAAGCAMISS ILGAEDITAT VKAMKMAYEA LRKGE // ID C0WG54_9CORY Unreviewed; 226 AA. AC C0WG54; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0276_0440; OS Corynebacterium accolens ATCC 49725. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=525260; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49725; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGD01000001; EEI15825.1; -; Genomic_DNA. DR ProteinModelPortal; C0WG54; -. DR EnsemblBacteria; EEI15825; EEI15825; HMPREF0276_0440. DR PATRIC; 29086904; VBICorAcc98353_2203. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). SQ SEQUENCE 226 AA; 23146 MW; EA9D478DF8F8BA65 CRC64; MSANQPDLRC YHVTGVPQEK VVQVAAAAAA GGAGVIQVRS KPISVRDLTA LAIDVAAAVE EANPATRVLI DDRVDVAAAL MGNHNIHGVH IGQDDLDPRL ARRILGEDAI IGLTTGTLEL VQGANEYADV IDYIGAGPFR PTPTKNSGRT PLGLDGYPPL VSASAVPVVA IGDVQATDAE ALAQTGVAGV AIVRAFMDSD DQAALATTVV DAFDRADKNA ATGSHA // ID C0WLC5_9CORY Unreviewed; 209 AA. AC C0WLC5; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0276_2261; OS Corynebacterium accolens ATCC 49725. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=525260; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49725; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGD01000045; EEI13657.1; -; Genomic_DNA. DR ProteinModelPortal; C0WLC5; -. DR EnsemblBacteria; EEI13657; EEI13657; HMPREF0276_2261. DR PATRIC; 29085300; VBICorAcc98353_1423. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21883 MW; BF26A76789EDC103 CRC64; MSIDWTLYLI TDPELAGGRD KVIPIVQEAV RGGATVVQLR DKEASDEEVE ATARDLLEVL GDVPLFINDR VEVAAKVGCH LHIGQDDMDL SQARALLGPD KFIGLSVGTR EELDAIDPQE APDIIGIGPV HSTATKKNAP AGIGAEAARH LATAARERGI ESVAIGGIKA HNAHELSGSG FAGICVVSDI MAADDPAAAA HNLKEAYRG // ID C0WNV6_LACBU Unreviewed; 218 AA. AC C0WNV6; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0497_0809; OS Lactobacillus buchneri ATCC 11577. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525318; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11577; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGH01000024; EEI20389.1; -; Genomic_DNA. DR ProteinModelPortal; C0WNV6; -. DR EnsemblBacteria; EEI20389; EEI20389; HMPREF0497_0809. DR PATRIC; 30697212; VBILacBuc113131_0324. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23420 MW; C9FD050402E90CFD CRC64; MAMAFKVGML RAYFIAGTQD IKKSNLTLPE VLTQALQSGI TAFQYREKGP GSLSEEKKVD MAHTLRKLCE TYKIPFIVDD DIDLALETAA DGIHVGQKDE RVTKVIQQVG TTMFVGLSCD TKEQVAIANE TEGISYIGSG PVYPTGSKAD ADPVIGIAGL KRLVQSSRLP VVAIGGITEE NISELPQTGV AGASVISMIA QSNDIKRAVT RMRAVFEK // ID C0WQR8_LACBU Unreviewed; 210 AA. AC C0WQR8; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0497_1471; OS Lactobacillus buchneri ATCC 11577. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525318; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11577; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGH01000107; EEI19634.1; -; Genomic_DNA. DR ProteinModelPortal; C0WQR8; -. DR EnsemblBacteria; EEI19634; EEI19634; HMPREF0497_1471. DR PATRIC; 30697958; VBILacBuc113131_1090. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22943 MW; B94A02614C359B9A CRC64; MKVTNRPLYL VTDHTNLNDE DFLQQIDLAC ESGVSLLQLR EKNRSSRDIY EWAVKVKDIA DRHRVPLIID DRLDIAQAVD AAGVHLGQSD LPVEVARRIL GNKKIIGATT KTLKQAKFAE EQGADYLGVG AIFPTQTHVK TVHTSIETLG KIKEVVNIPI YAIGGLKAHN IQAIEPAHVD GVAVVSAIMQ AKNAKATTRE LLNAVEEAIG // ID C0WXA6_LACFE Unreviewed; 213 AA. AC C0WXA6; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0511_0757; OS Lactobacillus fermentum ATCC 14931. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525325; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14931; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGI01000069; EEI22360.1; -; Genomic_DNA. DR ProteinModelPortal; C0WXA6; -. DR EnsemblBacteria; EEI22360; EEI22360; HMPREF0511_0757. DR PATRIC; 30722807; VBILacFer68609_0472. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22436 MW; 6ECEBE14089A08EB CRC64; MLFKNEMLRC YLIGGSQDTH HDPDEFLTKV EAAMQAGITA FQYREKGTST LSKAETLALG QQVRELATKY GVPLFVDDDL ELAAAIKADG IHVGQKDQRI EEVLAAVGDQ LMVGYSCNTA AQVAHANQLN VDYIGTGPVF PTISKDDAGS ALGVDGLADF VEQSTHPVVA IGGISLDNAG TTLTSGCAGL SMISMVLGAD DVAGTVKKIL ELY // ID C0X7E0_ENTFL Unreviewed; 211 AA. AC C0X7E0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0348_2425; OS Enterococcus faecalis TX0104. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=491074; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0104; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGL01000167; EEI11017.1; -; Genomic_DNA. DR ProteinModelPortal; C0X7E0; -. DR EnsemblBacteria; EEI11017; EEI11017; HMPREF0348_2425. DR PATRIC; 26761780; VBIEntFae109560_1053. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22881 MW; E4C24F8F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID C0XGD8_LACHI Unreviewed; 210 AA. AC C0XGD8; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0519_0299; OS Lactobacillus hilgardii ATCC 8290. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525327; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8290; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGP01000083; EEI25562.1; -; Genomic_DNA. DR ProteinModelPortal; C0XGD8; -. DR EnsemblBacteria; EEI25562; EEI25562; HMPREF0519_0299. DR PATRIC; 27429188; VBILacHil40002_1375. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22943 MW; B94A02614C359B9A CRC64; MKVTNRPLYL VTDHTNLNDE DFLQQIDLAC ESGVSLLQLR EKNRSSRDIY EWAVKVKDIA DRHRVPLIID DRLDIAQAVD AAGVHLGQSD LPVEVARRIL GNKKIIGATT KTLKQAKFAE EQGADYLGVG AIFPTQTHVK TVHTSIETLG KIKEVVNIPI YAIGGLKAHN IQAIEPAHVD GVAVVSAIMQ AKNAKATTRE LLNAVEEAIG // ID C0XK36_LACHI Unreviewed; 218 AA. AC C0XK36; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0519_1597; OS Lactobacillus hilgardii ATCC 8290. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525327; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8290; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGP01000149; EEI24220.1; -; Genomic_DNA. DR ProteinModelPortal; C0XK36; -. DR EnsemblBacteria; EEI24220; EEI24220; HMPREF0519_1597. DR PATRIC; 27427742; VBILacHil40002_0574. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23433 MW; EB43049688C1B6D4 CRC64; MAMAFKVGML RAYFIAGTQD IKKSNLTLPE VLTQALQSGI TAFQYREKGP GSLSEEKKVD MAHTLRKLCE TYKIPFIVDD DVDLALETAA DGIHVGQKDE RVTKVIQQVG TKMFVGLSCD TKEQVAIANE TEGISYIGSG PVYPTGSKAD ADPVIGIAGL KRLVQSSRLP VVAIGGITEE NISELPQTGV AGASVISMIA QSNDIKRAVT RMRAVFEK // ID C0XTA9_9CORY Unreviewed; 219 AA. AC C0XTA9; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0298_1679; OS Corynebacterium lipophiloflavum DSM 44291. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=525263; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 44291; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHJ01000136; EEI16514.1; -; Genomic_DNA. DR ProteinModelPortal; C0XTA9; -. DR EnsemblBacteria; EEI16514; EEI16514; HMPREF0298_1679. DR PATRIC; 25297443; VBICorLip134717_1974. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). SQ SEQUENCE 219 AA; 23041 MW; 66EA9BCCA7D3C20B CRC64; MLSCQLDLRC YFVTGSGSER DIVTLARDAA RAGAGVIQVR SKPISARDLY SLGREVAHAV REANPATRVL IDDRVDVALA LRDEGVHGVH LGQDDLDVRV ARRLLGPEAI IGLTTGTLQL VRAANELAGD IDYVGAGPFR ATPTKDSGRP LLGVDGYRPL VAESLVPVVA IGDVTVDDAA ELASTGVDGL ALVRGIMNAE DTGAYVARVL SEFERGAVD // ID C0Y3H8_BURPE Unreviewed; 209 AA. AC C0Y3H8; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-MAR-2014, entry version 24. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BUH_6806; OS Burkholderia pseudomallei Pakistan 9. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=595498; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pakistan 9; RA Harkins D.M., Brinkac L.M., Rogers Y.C., Detter J.C., Munk A.C., RA Bruce D.C., Sims D.R., Brettin T.S.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKA01000027; EEH28125.1; -; Genomic_DNA. DR ProteinModelPortal; C0Y3H8; -. DR EnsemblBacteria; EEH28125; EEH28125; BUH_6806. DR PATRIC; 27912027; VBIBurPse53205_2617. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID C0Y9W4_BURPE Unreviewed; 81 AA. AC C0Y9W4; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-MAR-2014, entry version 22. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=BUH_5947; OS Burkholderia pseudomallei Pakistan 9. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=595498; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pakistan 9; RA Harkins D.M., Brinkac L.M., Rogers Y.C., Detter J.C., Munk A.C., RA Bruce D.C., Sims D.R., Brettin T.S.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKA01000042; EEH25929.1; -; Genomic_DNA. DR EnsemblBacteria; EEH25929; EEH25929; BUH_5947. DR PATRIC; 27916184; VBIBurPse53205_4669. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 81 AA; 8587 MW; 0DE94E2B22B385C3 CRC64; MRHADSIGVD LITISPVMPT ATHTTAEPLG WPRFRELATL TSVPVYALGG MSVDSLAEAR NAGAYGIAAI RAFWGSNVDR S // ID C0YAJ7_BURPE Unreviewed; 367 AA. AC C0YAJ7; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-MAR-2014, entry version 31. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=BUH_3787; OS Burkholderia pseudomallei Pakistan 9. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=595498; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pakistan 9; RA Harkins D.M., Brinkac L.M., Rogers Y.C., Detter J.C., Munk A.C., RA Bruce D.C., Sims D.R., Brettin T.S.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKA01000043; EEH25759.1; -; Genomic_DNA. DR ProteinModelPortal; C0YAJ7; -. DR EnsemblBacteria; EEH25759; EEH25759; BUH_3787. DR PATRIC; 27916611; VBIBurPse53205_4876. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Transferase. SQ SEQUENCE 367 AA; 38308 MW; E8F50A360B15395D CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAQIARL NAAGAQAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDTLRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID C0Z0N1_LACRE Unreviewed; 215 AA. AC C0Z0N1; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0535_1596; OS Lactobacillus reuteri MM2-3. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=585517; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MM2-3; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLB01000088; EEI08634.1; -; Genomic_DNA. DR ProteinModelPortal; C0Z0N1; -. DR EnsemblBacteria; EEI08634; EEI08634; HMPREF0535_1596. DR PATRIC; 37024064; VBILacReu127513_0780. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23849 MW; BE51CB250D92566D CRC64; MIFDPKMLQV YLVGGTQDVH NDVVKFLEKV ELAMKSGITA FQYREKGNSK LRPNERVDLG LELRTLCTHY GIPLIVDDDY ELAQQINADG VHVGQNDTKI EQVSVAVGHQ MFIGYSCNTP EQVERANTMD FIDYIGCGPV FPTKSKSDAD TAIGINRLER LNMISERPVV AIGGIDEENM KVVHDTGVAG LAVISLVFDS KDLVATVKKM KNLYK // ID C0ZEJ0_BREBN Unreviewed; 220 AA. AC C0ZEJ0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BBR47_32220; OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=358681; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=47 / JCM 6285 / NBRC 100599; RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W., RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S., RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., RA Yoshikawa H., Udaka S., Tanikawa S., Fujita N.; RT "Brevibacillus brevis strain 47, complete genome."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008955; BAH44199.1; -; Genomic_DNA. DR RefSeq; YP_002772703.1; NC_012491.1. DR ProteinModelPortal; C0ZEJ0; -. DR STRING; 358681.BBR47_32220; -. DR EnsemblBacteria; BAH44199; BAH44199; BBR47_32220. DR GeneID; 7720199; -. DR KEGG; bbe:BBR47_32220; -. DR PATRIC; 21236762; VBIBreBre96763_3198. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BBRE358681:GHYS-3353-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23368 MW; 2DA491946F1A16FB CRC64; MRDRQRLREK MGVYFVIGTQ DCGYSSEKTV QTVEAALRGG VGTLQLRDKG SKLTAQEQYE LGIQLQQLCR EHDTVFFVND DVDLAIRLQA DGVHVGQDDM TLSEVRAKVG SEMYIGVSAG TVEEALAAQN GGVDCIGVGA MFATRSKADA GEPIGPVGLE EIRKAVGHDL PIVGIGGITL ENATEVLAAG ADGVAIISAI SRAESPEKAA QALQRIVRTR // ID C0ZEJ1_BREBN Unreviewed; 207 AA. AC C0ZEJ1; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 13-NOV-2013, entry version 31. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=BBR47_32230; OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=358681; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=47 / JCM 6285 / NBRC 100599; RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W., RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S., RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., RA Yoshikawa H., Udaka S., Tanikawa S., Fujita N.; RT "Brevibacillus brevis strain 47, complete genome."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008955; BAH44200.1; -; Genomic_DNA. DR RefSeq; YP_002772704.1; NC_012491.1. DR ProteinModelPortal; C0ZEJ1; -. DR STRING; 358681.BBR47_32230; -. DR EnsemblBacteria; BAH44200; BAH44200; BBR47_32230. DR GeneID; 7720722; -. DR KEGG; bbe:BBR47_32230; -. DR PATRIC; 21236764; VBIBreBre96763_3199. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BBRE358681:GHYS-3354-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 207 AA; 22050 MW; E883944D832F4969 CRC64; MSSTRELHVI TSGRHSLDDA MRMAEAAYAG GMNFLHIREK QRTAKECMNW VKALSNVIPL SSLIMNDRVD VAAASGCAGA HLAYHSLSPA EARMVLKTGQ KIGRSVHSVV EAQEAIAAKV DYLLYGHIFA SGSKPGLAPR GTNELAQMTA RWHVPIIGLG GITPDRTTHV LEAGCAGIAV LSGITDATDA KSAASAYREA LDRWEGK // ID C0ZUE2_RHOE4 Unreviewed; 231 AA. AC C0ZUE2; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=RER_14790; OS Rhodococcus erythropolis (strain PR4 / NBRC 100887). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=234621; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR4 / NBRC 100887; RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.; RT "Comparison of the complete genome sequences of Rhodococcus RT erythropolis PR4 and Rhodococcus opacus B4."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008957; BAH32187.1; -; Genomic_DNA. DR RefSeq; YP_002764926.1; NC_012490.1. DR ProteinModelPortal; C0ZUE2; -. DR STRING; 234621.RER_14790; -. DR EnsemblBacteria; BAH32187; BAH32187; RER_14790. DR GeneID; 7711214; -. DR KEGG; rer:RER_14790; -. DR PATRIC; 23189316; VBIRhoEry66701_1959. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RERY234621:GHDE-1498-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 157 159 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 160 160 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 231 AA; 24330 MW; 01AC612E1C36F2B8 CRC64; MHPTHPSNVI DRRERLAAAR LYLCTDARRE KGDLAQFAEA ALSGGVDIIQ LRDKGSAGER EFGPLEAKDE LVALGILAAA ARRHGALLAV NDRADLAMAS GADILHLGQN DIPVPYARTV VGEDVVIGRS TSSRAQASLA AIEEGVDYFC TGPVWATPTK PNRSASGLEL VRSTADAAPP RPWFAIGGID EERLPELLDA GATRIVVVRA ITQASDPQAA AQRLAAAVAG R // ID C1AE24_GEMAT Unreviewed; 493 AA. AC C1AE24; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE SubName: Full=Thiamine-phosphate pyrophosphorylase/phosphomethylpyrimidine kinase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN Name=thiD; Synonyms=thiE; OrderedLocusNames=GAU_3709; OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC OS 100505). OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae; OC Gemmatimonas. OX NCBI_TaxID=379066; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505; RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., RA Oguchi A., Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., RA Yokoyama H., Tanikawa S., Hanada S., Kamagata Y., Fujita N.; RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that RT represents a novel phylum Gemmatimonadetes."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009153; BAH40751.1; -; Genomic_DNA. DR RefSeq; YP_002763221.1; NC_012489.1. DR ProteinModelPortal; C1AE24; -. DR STRING; 379066.GAU_3709; -. DR EnsemblBacteria; BAH40751; BAH40751; GAU_3709. DR GeneID; 7706178; -. DR KEGG; gau:GAU_3709; -. DR PATRIC; 21960436; VBIGemAur55831_3794. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; GAUR379066:GI3W-3762-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 493 AA; 51595 MW; 49D0F44C9E9AA69A CRC64; MERSMTRDAN TMRACLRLYL VTDPLLCAKA GLLHTVREAI AGGISMVQLR DKTATTEERI AIGRALMRVL HGTGVPLIIN DDIDAALAIG AHGVHVGQSD LTPRIVRERM GPSAIVGLSC ETVAQAAAAD PLLVDYVGMS PVLATPTKRD HAAALGFTGL EAARAATTLP AVAIGGMHLE HVTRVMRTGV DGIAVVSAVC GQPDPRAASL ALRQAIDEAV RDMTHPRIPN ALTIAGSDPS GGAGIQADLK TFAAQRVYGM AALTALTAQN TRGVAGVHVV PPVFVLQQLE SLFDDIRIDA VKIGMIATAD IATTVADVLE ERMRGPVVLD PVMIAKGGAE LLRPDAVDAV RTRLLPLATV ITPNLAEAAH LLNMPMASTR AEMETQATLL RALGPQAVLL KGGHLTEERS PDCLVTSDGV HWFDGPRVAT ANTHGTGCTL SAAIAAGLAG GGNLLTVVRT AKQYVTDAIA SAHRLTVGHG HGPTHHFHNL WNR // ID C1AK90_MYCBT Unreviewed; 222 AA. AC C1AK90; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=JTY_0423; OS Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=561275; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019; RX PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034; RA Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.; RT "Whole genome sequence analysis of Mycobacterium bovis bacillus RT Calmette-Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine RT substrains."; RL Vaccine 27:1710-1716(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010918; BAH24719.1; -; Genomic_DNA. DR RefSeq; YP_002643487.1; NC_012207.1. DR ProteinModelPortal; C1AK90; -. DR SMR; C1AK90; 1-221. DR STRING; 561275.JTY_0423; -. DR EnsemblBacteria; BAH24719; BAH24719; JTY_0423. DR GeneID; 7563583; -. DR KEGG; mbt:JTY_0423; -. DR PATRIC; 18020122; VBIMycBov85238_0459. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MBOV561275:GHDN-427-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID C1B0F3_RHOOB Unreviewed; 232 AA. AC C1B0F3; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ROP_19060; OS Rhodococcus opacus (strain B4). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=632772; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4; RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.; RT "Comparison of the complete genome sequences of Rhodococcus RT erythropolis PR4 and Rhodococcus opacus B4."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011115; BAH50153.1; -; Genomic_DNA. DR RefSeq; YP_002779098.1; NC_012522.1. DR ProteinModelPortal; C1B0F3; -. DR STRING; 632772.ROP_19060; -. DR EnsemblBacteria; BAH50153; BAH50153; ROP_19060. DR GeneID; 7743874; -. DR KEGG; rop:ROP_19060; -. DR PATRIC; 23221053; VBIRhoOpa21106_1921. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ROPA632772:GH0Q-1930-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 157 159 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 160 160 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 232 AA; 24563 MW; D198A4A56402747A CRC64; MTTSHHSNLT DRRRRLGTAR LYLCTDARRE KGDLAQFAEA ALSGGVDIIQ LRDKGSAGEK KFGTMDARDE LAALSVLAAA ARRHGALLAV NDRADMALAA GADVLHLGQG DLPVPYARTV VGSEVLIGRS THSRAQASLA AIEDGVDYFC TGPVWETPTK PGRTASGIDL VRSTADSEPN RPWFAIGGID ESRVPEILAA GADRIVVVRA ITEARDPQAA ARSLSALLQK NA // ID C1C667_STRP7 Unreviewed; 209 AA. AC C1C667; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; OrderedLocusNames=SP70585_0765; OS Streptococcus pneumoniae (strain 70585). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=488221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=70585; RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.; RT "Complete genome sequence of Streptococcus pneumoniae strain 70585."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000918; ACO17608.1; -; Genomic_DNA. DR RefSeq; YP_002740043.1; NC_012468.1. DR ProteinModelPortal; C1C667; -. DR STRING; 488221.SP70585_0765; -. DR EnsemblBacteria; ACO17608; ACO17608; SP70585_0765. DR GeneID; 7683409; -. DR KEGG; snm:SP70585_0765; -. DR PATRIC; 19667842; VBIStrPne83895_0788. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE488221:GH4U-751-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23244 MW; 69798D236EB6C679 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID C1C674_STRP7 Unreviewed; 210 AA. AC C1C674; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; OrderedLocusNames=SP70585_0772; OS Streptococcus pneumoniae (strain 70585). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=488221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=70585; RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.; RT "Complete genome sequence of Streptococcus pneumoniae strain 70585."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000918; ACO16935.1; -; Genomic_DNA. DR RefSeq; YP_002740050.1; NC_012468.1. DR ProteinModelPortal; C1C674; -. DR STRING; 488221.SP70585_0772; -. DR EnsemblBacteria; ACO16935; ACO16935; SP70585_0772. DR GeneID; 7682994; -. DR KEGG; snm:SP70585_0772; -. DR PATRIC; 19667856; VBIStrPne83895_0795. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE488221:GH4U-758-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22744 MW; E8E490415C77D48E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID C1CD70_STRZJ Unreviewed; 209 AA. AC C1CD70; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; OrderedLocusNames=SPJ_0658; OS Streptococcus pneumoniae (strain JJA). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=488222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JJA; RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.; RT "Complete genome sequence of Streptococcus pneumoniae strain JJA."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000919; ACO18208.1; -; Genomic_DNA. DR RefSeq; YP_002735741.1; NC_012466.1. DR ProteinModelPortal; C1CD70; -. DR STRING; 488222.SPJ_0658; -. DR EnsemblBacteria; ACO18208; ACO18208; SPJ_0658. DR GeneID; 7679182; -. DR KEGG; sjj:SPJ_0658; -. DR PATRIC; 19696425; VBIStrPne71544_0698. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MLARYFI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE488222:GI12-642-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID C1CD77_STRZJ Unreviewed; 210 AA. AC C1CD77; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; OrderedLocusNames=SPJ_0665; OS Streptococcus pneumoniae (strain JJA). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=488222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JJA; RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.; RT "Complete genome sequence of Streptococcus pneumoniae strain JJA."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000919; ACO19021.1; -; Genomic_DNA. DR RefSeq; YP_002735748.1; NC_012466.1. DR ProteinModelPortal; C1CD77; -. DR STRING; 488222.SPJ_0665; -. DR EnsemblBacteria; ACO19021; ACO19021; SPJ_0665. DR GeneID; 7678833; -. DR KEGG; sjj:SPJ_0665; -. DR PATRIC; 19696439; VBIStrPne71544_0705. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE488222:GI12-649-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID C1CJG9_STRZP Unreviewed; 209 AA. AC C1CJG9; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; OrderedLocusNames=SPP_0729; OS Streptococcus pneumoniae (strain P1031). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=488223; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1031; RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.; RT "Complete genome sequence of Streptococcus pneumoniae strain P1031."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000920; ACO20903.1; -; Genomic_DNA. DR RefSeq; YP_002737907.1; NC_012467.1. DR ProteinModelPortal; C1CJG9; -. DR STRING; 488223.SPP_0729; -. DR EnsemblBacteria; ACO20903; ACO20903; SPP_0729. DR GeneID; 7682449; -. DR KEGG; spp:SPP_0729; -. DR PATRIC; 32458710; VBIStrPne91701_0757. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE488223:GHE7-713-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23244 MW; 69798D236EB6C679 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID C1CJH6_STRZP Unreviewed; 210 AA. AC C1CJH6; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; OrderedLocusNames=SPP_0736; OS Streptococcus pneumoniae (strain P1031). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=488223; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1031; RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.; RT "Complete genome sequence of Streptococcus pneumoniae strain P1031."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000920; ACO20599.1; -; Genomic_DNA. DR RefSeq; YP_002737914.1; NC_012467.1. DR ProteinModelPortal; C1CJH6; -. DR STRING; 488223.SPP_0736; -. DR EnsemblBacteria; ACO20599; ACO20599; SPP_0736. DR GeneID; 7681849; -. DR KEGG; spp:SPP_0736; -. DR PATRIC; 32458724; VBIStrPne91701_0764. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE488223:GHE7-720-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22744 MW; A3239DF7871A7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID C1CQI3_STRZT Unreviewed; 209 AA. AC C1CQI3; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; OrderedLocusNames=SPT_0734; OS Streptococcus pneumoniae (strain Taiwan19F-14). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=487213; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Taiwan19F-14; RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.; RT "Complete genome sequence of Streptococcus pneumoniae strain RT Taiwan19F-14."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000921; ACO22970.1; -; Genomic_DNA. DR RefSeq; YP_002742205.1; NC_012469.1. DR ProteinModelPortal; C1CQI3; -. DR STRING; 487213.SPT_0734; -. DR EnsemblBacteria; ACO22970; ACO22970; SPT_0734. DR GeneID; 7686789; -. DR KEGG; snt:SPT_0734; -. DR PATRIC; 19710617; VBIStrPne22502_0762. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE487213:GI07-723-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID C1CQJ0_STRZT Unreviewed; 210 AA. AC C1CQJ0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; OrderedLocusNames=SPT_0741; OS Streptococcus pneumoniae (strain Taiwan19F-14). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=487213; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Taiwan19F-14; RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.; RT "Complete genome sequence of Streptococcus pneumoniae strain RT Taiwan19F-14."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000921; ACO22674.1; -; Genomic_DNA. DR RefSeq; YP_002742212.1; NC_012469.1. DR ProteinModelPortal; C1CQJ0; -. DR STRING; 487213.SPT_0741; -. DR EnsemblBacteria; ACO22674; ACO22674; SPT_0741. DR GeneID; 7687268; -. DR KEGG; snt:SPT_0741; -. DR PATRIC; 19710631; VBIStrPne22502_0769. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE487213:GI07-730-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID C1D029_DEIDV Unreviewed; 227 AA. AC C1D029; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Deide_04520; OS Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=546414; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VCD115 / DSM 17065 / LMG 22923; RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434; RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., RA Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., RA Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., RA Achouak W., Armengaud J.; RT "Alliance of proteomics and genomics to unravel the specificities of RT Sahara bacterium Deinococcus deserti."; RL PLoS Genet. 5:E1000434-E1000434(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001114; ACO45281.1; -; Genomic_DNA. DR RefSeq; YP_002785035.1; NC_012526.1. DR ProteinModelPortal; C1D029; -. DR STRING; 546414.Deide_04520; -. DR EnsemblBacteria; ACO45281; ACO45281; Deide_04520. DR GeneID; 7737978; -. DR KEGG; ddr:Deide_04520; -. DR PATRIC; 21614408; VBIDeiDes121019_0507. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTLLQYR; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DDES546414:GHOM-508-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 23384 MW; BF4AD1E2D023F7AB CRC64; MTRPLGRLYL VATPRPGQSE DDFVARVEAA LDGGVDTLQL RCKADSPAYG EARAVIRLAG RLRDLAHARG VPLFMNDRVD IAAASGADGV HLGQEDLPLS WARALAPGVQ VGLSTHAPAQ AAAAVAQRPA YFAVGPVHTT PTKPGREATG LEYVRHVAAT HGEAQTGIPW YAIGGVDLGN VQDVLAAGAT RIAVVRAVLD APDPARAAAA LCSALAAPAV QEVAACR // ID C1DCZ7_LARHH Unreviewed; 487 AA. AC C1DCZ7; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 16-APR-2014, entry version 46. DE SubName: Full=CoaD; DE EC=2.7.7.3; GN Name=coaD; OrderedLocusNames=LHK_00639; OS Laribacter hongkongensis (strain HLHK9). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Laribacter. OX NCBI_TaxID=557598; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLHK9; RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416; RA Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., RA Fan R.Y., Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., RA Huang J.D., Mak W., Pallen M.J., Lok S., Yuen K.Y.; RT "The complete genome and proteome of Laribacter hongkongensis reveal RT potential mechanisms for adaptations to different temperatures and RT habitats."; RL PLoS Genet. 5:E1000416-E1000416(2009). CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'- CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and CC pyrophosphate (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate + CC 3'-dephospho-CoA. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 4/5. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001154; ACO73632.1; -; Genomic_DNA. DR RefSeq; YP_002794641.1; NC_012559.1. DR ProteinModelPortal; C1DCZ7; -. DR STRING; 557598.LHK_00639; -. DR EnsemblBacteria; ACO73632; ACO73632; LHK_00639. DR GeneID; 7756262; -. DR KEGG; lhk:LHK_00639; -. DR PATRIC; 22298373; VBILarHon49832_0609. DR eggNOG; COG0494; -. DR KO; K03574; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LHON557598:GHO5-647-MONOMER; -. DR UniPathway; UPA00241; UER00355. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR HAMAP; MF_00151; PPAT_bact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR001980; LPS_biosynth. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01467; CTP_transf_2; 1. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01020; LPSBIOSNTHSS. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 3: Inferred from homology; KW ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm; KW Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Transferase. SQ SEQUENCE 487 AA; 52884 MW; A4743935C8572E4A CRC64; MKRAVYAGSF DPVTNGHLWM IQQAVELFDE LIVAIGVNPD KHCTFSAEDR AAMLRETTQQ YPNLRVEVFD NQFLVSYAQS VGANYIVRGI RTTSDYEYER AMRYINSDLY PNINTIFLLP PREFAEVSST MVRGLVGPDG LGKHHSPIRT RPGVPAAAPV GRAPWHPALR GYKATGIMTK WVDVVAGVLL APNGDFFLSS RPQGKPYAGY WEFPGGKLEA GETPYQALVR ELDEELGLTV EEATPWLTQH FHYEHASVRL SFWRVTRWQG QPQAREGQTW AWQPAAGALN VAPVLPANTP VFRALSLPAT LALTCAGETG AAAILARIGA DPAAFPLVVV REPGWAEADR VQLAHEIRAL TAGCGGRVLL AGATTLVAGL DGVHLTAAQL MALDTRPAAD WAGASVHRQE ELEQAARLGL DYVMLGHVMP TPSHPGVPPL GWSRFAGLAG GRWPMPVYAL GGMQPQDMQA AQAHGAHGIA MMRGAWQ // ID C1DQB1_AZOVD Unreviewed; 313 AA. AC C1DQB1; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 46. DE SubName: Full=MutT/ NUDIX family protein; GN OrderedLocusNames=Avin_13370; OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=322710; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJ / ATCC BAA-1303; RX PubMed=19429624; DOI=10.1128/JB.00504-09; RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G., RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L., RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., RA Hernandez J.A., Houmiel K., Imperial J., Kennedy C., Larson T.J., RA Latreille P., Ligon L.S., Lu J., Maerk M., Miller N.M., Norton S., RA O'Carroll I.P., Paulsen I., Raulfs E.C., Roemer R., Rosser J., RA Segura D., Slater S., Stricklin S.L., Studholme D.J., Sun J., RA Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H., Dean D.R., RA Dixon R., Wood D.; RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe RT specialized to support diverse anaerobic metabolic processes."; RL J. Bacteriol. 191:4534-4545(2009). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001157; ACO77563.1; -; Genomic_DNA. DR RefSeq; YP_002798538.1; NC_012560.1. DR ProteinModelPortal; C1DQB1; -. DR STRING; 322710.Avin_13370; -. DR EnsemblBacteria; ACO77563; ACO77563; Avin_13370. DR GeneID; 7760279; -. DR KEGG; avn:Avin_13370; -. DR PATRIC; 21028951; VBIAzoVin72790_1264. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AVIN322710:GJ0M-1337-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 313 AA; 34178 MW; D02A5067ACB034AC CRC64; MKRIHVAAAV IRGADGRVLI ARRPEEKHQG GLWEFPGGKV EAGEAVEAAL ARELEEELGI RVSAARPLIQ VRHDYPDQYV LLDVWEVAAF AGEPHGAEGQ ALAWVAPRQL PDYRFPAANH PIVAAARLPE RYLITPEDLS PQALLRGLRS ALEGGIRLIQ LRAPNMFDPQ YRDLAVDVQG LCAGRAQLML KGPLEWLGDF PAAGWHLTAR QLREYAANGR PFPAERWLAA SCHDAEELAL ATRMGVDFVT LSPIEATSSH PGASPLGWER AAELLRGFNR PAFLLGGLGS QDLARAWRTG AQGIAAIRGL WSE // ID C1DUZ3_SULAA Unreviewed; 204 AA. AC C1DUZ3; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SULAZ_0957; OS Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825). OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; OC Sulfurihydrogenibium. OX NCBI_TaxID=204536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Az-Fu1 / DSM 15241 / OCM 825; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the RT Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001229; ACN98921.1; -; Genomic_DNA. DR RefSeq; YP_002728930.1; NC_012438.1. DR ProteinModelPortal; C1DUZ3; -. DR STRING; 204536.SULAZ_0957; -. DR EnsemblBacteria; ACN98921; ACN98921; SULAZ_0957. DR GeneID; 7673110; -. DR KEGG; saf:SULAZ_0957; -. DR PATRIC; 23763042; VBISulAzo123226_0924. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAZO204536:GHRE-956-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22714 MW; 9FC87374629F5ED5 CRC64; MKLKGLYVIT DEKLTPYDKM LDMVEKALKG GASIVQLRDK NNSDEFLIPY CNQLKDLCHK YDAIFIVNDR VDLALKVDAD GVHIGEEDPD VVEVREKTKG KIMGVSCYGS VERALQMQEL GADYVAFGSF YPSPTKPKSR IVPKSVISEA KKVLKIPVCV IGGLTVENSK ELIDLGADLV AVISDVWTAP DVEKRCQEYL KLFK // ID C1DXM0_SULAA Unreviewed; 181 AA. AC C1DXM0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Thiamine-phosphate pyrophosphorylase (TMPpyrophosphorylase) (TMP-PPase) (Thiamine-phosphate synthase); DE EC=2.5.1.3; GN OrderedLocusNames=SULAZ_0135; OS Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825). OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; OC Sulfurihydrogenibium. OX NCBI_TaxID=204536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Az-Fu1 / DSM 15241 / OCM 825; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the RT Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001229; ACN98865.1; -; Genomic_DNA. DR RefSeq; YP_002728132.1; NC_012438.1. DR ProteinModelPortal; C1DXM0; -. DR STRING; 204536.SULAZ_0135; -. DR EnsemblBacteria; ACN98865; ACN98865; SULAZ_0135. DR GeneID; 7673386; -. DR KEGG; saf:SULAZ_0135; -. DR PATRIC; 23761402; VBISulAzo123226_0129. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HRFYFIT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAZO204536:GHRE-133-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 181 AA; 20272 MW; 1C9D500DB8024DB7 CRC64; MHRFYFITDR KKFKKPFLDT VKEVLEKGVR LIQIREKDLP DDELYKLAES VLEISKGYDA KIFINSRVDI AYMLGLDGVH LTSRSVPVSV VKRKFPDLIV GKSCHSVEDV LNAEDEGADY VFISPIFEVE GKGKPIGIEG LKKVLEVAKI PVYALGGINN SNVEEILKTG VYGVAGIRLF L // ID C1EYJ0_BACC3 Unreviewed; 208 AA. AC C1EYJ0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=BCA_0792; OS Bacillus cereus (strain 03BB102). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=572264; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=03BB102; RA Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C., RA Tapia R., Han C., Sutton G., Sims D.; RT "Genome sequence of Bacillus cereus 03BB102."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001407; ACO26333.1; -; Genomic_DNA. DR RefSeq; YP_002748085.1; NC_012472.1. DR ProteinModelPortal; C1EYJ0; -. DR STRING; 572264.BCA_0792; -. DR EnsemblBacteria; ACO26333; ACO26333; BCA_0792. DR GeneID; 7688808; -. DR KEGG; bcx:BCA_0792; -. DR PATRIC; 18814699; VBIBacCer84800_0667. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER572264:GH22-764-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 23210 MW; 7B3263F944B18D3C CRC64; MNMKNELHVI SNGNMSFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLKKGFPP SKLVINDRID IAILLNIPRV QLGYRSTDVR SVKEKFSYLH VGYSVHSLEE AIEAFKNGAD SLVYGHVFPT DCKKDVPARG LEEISDIARS LSIPIIAIGG ITPENTKDIL ASEVSGIAVM SGIVSSSNPY SKAKSYKESI RKWAEKHV // ID C1F178_ACIC5 Unreviewed; 220 AA. AC C1F178; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=ACP_2381; OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Acidobacterium. OX NCBI_TaxID=240015; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51196 / DSM 11244 / JCM 7670; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., RA Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., RA Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., RA Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C., RA Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., RA Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., RA Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., RA Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., RA Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001472; ACO34323.1; -; Genomic_DNA. DR RefSeq; YP_002755422.1; NC_012483.1. DR ProteinModelPortal; C1F178; -. DR STRING; 240015.ACP_2381; -. DR EnsemblBacteria; ACO34323; ACO34323; ACP_2381. DR GeneID; 7699073; -. DR KEGG; aca:ACP_2381; -. DR PATRIC; 20668015; VBIAciCap40988_2283. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FGPPQGL; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ACAP240015:GKF4-2332-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 220 AA; 23105 MW; 6E11FAE88CD4F3C3 CRC64; MLHCAITERA LFPGNEFQRL SQLLEQVREL ACTGLAYLQI REKDLPASDL ESLAASICGL VRQQGSSMRV LLNGPAEIAL RTGCHGVHLP GHASPEAAAQ ARRLYAQAGR TAILSAACHT IADVEQRSNY ADLLVFAPVF EKVLPDRALP GLGLEALASA VRAAQGKPVL ALGGVTAANA PLCIEAGAAG IAAIRLFMTQ DWKTLLSPPE ACQAPAVPGR // ID C1F8J4_ACIC5 Unreviewed; 250 AA. AC C1F8J4; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ACP_0120; OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Acidobacterium. OX NCBI_TaxID=240015; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51196 / DSM 11244 / JCM 7670; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., RA Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., RA Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., RA Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C., RA Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., RA Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., RA Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., RA Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., RA Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001472; ACO31456.1; -; Genomic_DNA. DR RefSeq; YP_002753268.1; NC_012483.1. DR ProteinModelPortal; C1F8J4; -. DR STRING; 240015.ACP_0120; -. DR EnsemblBacteria; ACO31456; ACO31456; ACP_0120. DR GeneID; 7699394; -. DR KEGG; aca:ACP_0120; -. DR PATRIC; 20663639; VBIAciCap40988_0120. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ACAP240015:GKF4-119-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 70 74 HMP-PP binding (By similarity). FT REGION 166 168 THZ-P binding (By similarity). FT REGION 217 218 THZ-P binding (By similarity). FT METAL 102 102 Magnesium (By similarity). FT METAL 121 121 Magnesium (By similarity). FT BINDING 101 101 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 HMP-PP (By similarity). FT BINDING 197 197 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 250 AA; 26436 MW; 1E4E8D5F48720DEB CRC64; MCGAVPSCLE SGFPGEGDSA YTRGVSPRAV FPTLYPILDA GVLSQDPTLR RGELLRLVRC VVDAGVTILQ YRNKQDTDTQ VLEDARWIRD AAGPEPTLIL NDRVHLVEQA AFDGVHVGQH DMTPAEARRI LGPDRVLGIS THNPDQVAAV ADAAVDYIAI GPVFATASKQ NPDPVVGLEG VRTARQRTQK PLVAIGGITP QTALAVMEAG ADSVAVISAI FGTGLGAERG PAIAPEQAGK NAKDFLRLFR // ID C1FJN2_MICSR Unreviewed; 1014 AA. AC C1FJN2; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 25. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=MICPUN_62927; OS Micromonas sp. (strain RCC299 / NOUM17) (Picoplanktonic green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales; OC Micromonas. OX NCBI_TaxID=296587; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCC299 / NOUM17; RX PubMed=19359590; DOI=10.1126/science.1167222; RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L., RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E., RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M., RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H., RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., RA Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., RA Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., RA Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., RA Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., RA Van de Peer Y., Grigoriev I.V.; RT "Green evolution and dynamic adaptations revealed by genomes of the RT marine picoeukaryotes Micromonas."; RL Science 324:268-272(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001577; ACO70375.1; -; Genomic_DNA. DR RefSeq; XP_002509117.1; XM_002509071.1. DR ProteinModelPortal; C1FJN2; -. DR GeneID; 8248257; -. DR KEGG; mis:MICPUN_62927; -. DR HOGENOM; HOG000241410; -. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. PE 4: Predicted; KW Complete proteome; GTP-binding; Nucleotide-binding. SQ SEQUENCE 1014 AA; 105479 MW; 7E822B20D6E9C021 CRC64; MPTQGMVVSA SAASGFLPRR AAPGRRVTAS PRAVFDGSAA STMRSSGSRL SIHRARSPRV SGGTPRGRRL TARVSAIGRF FGGGGGGASD DDDGKAVFAA KSRRQVRIPG FVFAVSPAVV NGEDADALAA LEAAVASGAT AVILADDTGD ATTRELFNAA LALKESLRGR ASLLVADRTD IAASAECDGV VLSDDGVPVV VARKSLSSAS GVVACGVKDE QAALIAAKEG ADLILAPNGR VADAVRGKIS VPVFASPRNG WAGVSAPDAI QALVDAGAKG AVLPTPPPSV DVARGITAAL APIAAAVKKD SDDSEPGAAP SASTTPTPVG TSVGTTTMAG KIIDPTTQAL LERERVLLDD AVAFLVESTP SLEEIGLLVE ARKGLEELFL LVIVGEFNAG KSSVINAMLG QKALKEGILP TTNEITVLKF GNEPRTEQSK DGFYTQLIPA DLLREVNIVD TPGTNVILER QQRLTEEFVP RADLVLFVLS ADRPMTESEV KFLSYIRKWG KKVAFVVNKC DRLENQGEVD EVKGFVADNA ERLLGVTDPA VLPVSAKAAL AAKERGGSET DFAQLEDYIL SFLGAGDKKG KNSGEGLRLK LGTPLQVGTM LFGAAEEILA QERAEAVEEL SQAEGVDAAM DKYREAMEAD FGAQVQAVRT AVMGAVGRCD DLLDATLRLT NGADLFTTYV LGNGANGAIR ERYKKEVLGD SEAKLRAAIK EHTGWLARNN DNQLRAYADA VRARGFDPSA TDLNLFEREE RIAAEEAEAI AAVRAEVAAK QTAAAEAEAK AAEAKAAEAK ARAAAKEAAG DDGAAAGDGA DDSNDDSKEN SSSLADELAG PAPAQTSASS LITRASSDLT SPATVAAGFD QAGAARLLEE EVKDAVYSTV GAAGASFFFA VFLSGFLDNF AEDVLAFSLT AAVGYVSVLS LPLKRAETKA KARAVAESFL DEVEGAMRAE FERKVGATTA QVRATTAPWV ASAREAEAAV AASQSRRDRI AEDMDQLQRD VQSI // ID C1GDM1_PARBD Unreviewed; 543 AA. AC C1GDM1; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 16-APR-2014, entry version 26. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=PADG_05357; OS Paracoccidioides brasiliensis (strain Pb18). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; mitosporic Onygenales; Paracoccidioides. OX NCBI_TaxID=502780; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pb18; RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345; RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., RA Goldberg J., Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., RA Grynberg M., Gujja S., Heiman D.I., Henn M.R., Kodira C.D., RA Leon-Narvaez H., Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., RA Morais F.V., Pereira M., Rodriguez-Brito S., Sakthikumar S., RA Salem-Izacc S.M., Sykes S.M., Teixeira M.M., Vallejo M.C., RA Walter M.E., Yandava C., Young S., Zeng Q., Zucker J., Felipe M.S., RA Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G., Puccia R., RA San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.; RT "Comparative genomic analysis of human fungal pathogens causing RT paracoccidioidomycosis."; RL PLoS Genet. 7:E1002345-E1002345(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS572755; EEH49278.1; -; Genomic_DNA. DR ProteinModelPortal; C1GDM1; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 543 AA; 57465 MW; 13A08626CB6CF30E CRC64; MDLSVYLVTD STPAILGDRD LCEVVRDAIE GGVTVVQYRD KHSDTGVLIE TAKKLHEITK AYNVPLIIND RVDVALVVGA EGVHLGQDDM KIPEAKKLLS PNAYIGATVC SNEEAFRAVE DGADYLGIGT VFATPTKTDT KAIIGTAGTK EILAFLSTMP RKVGTVAIGG INLSNVQRVI YQSQAPLKSL DGAAIVSAIM AAENPKEAAA AFSRLVKENP ASATFPAAPR ENEVTMLLDE VPNIIRAVAL KRPLCHNMIN FVVANFAANV AIAIGASPIM SGYGPEASDL AKNGGSLLIN MGTLNDEAID HYIQALRAYN AEGNPVVFDP VGAGATDIRR RAVKQLLAGG YFDVIKGNES ELIQVYGKTP GRQVGVDSGP SILSRREKAK LVRDLARRER NVVLLTGRVD YLSDGERVLA IGNGHELLGH ITGTGCIIGT MAASFLAVHR NDKLLAVLSS LLLLEIAGER AAARDGINGP GTFLPALIDE LFALKNWAVE WKTSGSAGID VDAGSMNGNA AAAAAATDEN IFRRAAKVHL MQL // ID C1GVE2_PARBA Unreviewed; 540 AA. AC C1GVE2; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 16-APR-2014, entry version 29. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=PAAG_02219; OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides OS brasiliensis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; mitosporic Onygenales; Paracoccidioides. OX NCBI_TaxID=502779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-826 / Pb01; RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345; RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., RA Goldberg J., Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., RA Grynberg M., Gujja S., Heiman D.I., Henn M.R., Kodira C.D., RA Leon-Narvaez H., Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., RA Morais F.V., Pereira M., Rodriguez-Brito S., Sakthikumar S., RA Salem-Izacc S.M., Sykes S.M., Teixeira M.M., Vallejo M.C., RA Walter M.E., Yandava C., Young S., Zeng Q., Zucker J., Felipe M.S., RA Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G., Puccia R., RA San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.; RT "Comparative genomic analysis of human fungal pathogens causing RT paracoccidioidomycosis."; RL PLoS Genet. 7:E1002345-E1002345(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS572815; EEH40164.1; -; Genomic_DNA. DR RefSeq; XP_002795513.1; XM_002795467.1. DR ProteinModelPortal; C1GVE2; -. DR GeneID; 9099020; -. DR KEGG; pbl:PAAG_02219; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 57394 MW; E5B09DD973BB007A CRC64; MDLSVYLVTD STPAILGDRD LCEIVRDAIE GGVTVVQYRD KHSDTGVLIE TAKKLHEITK AYNVPLIIND RVDVALAVRA EGVHLGQDDM KIPEAKKLLP PNAYIGATVC SNEEAFRAVE DGADYLGIGT VFATPTKTDT KAIIGTAGTK EILAFLSTMP RKVGTVAIGG INLSNVQRVI YQSQAPLKSL DGAAIVSAIM AAENPKEAAA AFSRLVKETP ASATFPAAPR ENEVAMLLDE VPNIIRAVAL KRPLCHNMIN FVVANFAANV AIAIGASPIM SGYGPEASDL AKNGGSLLIN MGTLNNEAID HYIQALRAYN AEGNPVVFDP VGAGASDIRR RAVKQLLAGG YFDVIKGNES ELIQVYGKTT WRQVGVDSGP SILSRREKAK LVRDLARRER NVVLLTGRVD YLSDGERVLA IGNGHELLGH ITGTGCIIGT MAASFLAVHR NDKLLAVLSS LLLLEIAGER AAAKDGINGP GTFLPALIDE LFALKNWAVE WKTSGSAGID VDAGSMNGNA AAATDENIFR RAAKVHLMQL // ID C1HTT5_9ESCH Unreviewed; 212 AA. AC C1HTT5; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ESAG_05044; OS Escherichia sp. 3_2_53FAA. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=469598; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_2_53FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Ilzarbe M., Galagan J., RA Birren B.; RT "The Genome Sequence of Escherichia sp. strain 3_2_53FAA."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999467; EEH89332.1; -; Genomic_DNA. DR ProteinModelPortal; C1HTT5; -. DR EnsemblBacteria; EEH89332; EEH89332; ESAG_05044. DR PATRIC; 29418749; VBIEscSp50726_4846. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23160 MW; ADFF72089BA3EBBA CRC64; MMYQPEFPPV PFRLGLYPVV DSVQWIERLL DAGVRTLQLR IKDRRDEEVE ADVVAAIALG RRYNARLFIN DYWRLAIKHQ AYGVHLGQED LQATDLSAIR AAGLRLGVST HDDMEIDVAL AARPSYIALG HVFPTQTKQM PSAPQGLEQL ARHVERLADY PTVAIGGISL ARAPAVIATG VGSIAVVSAI TQAADWRLAT AQLLEIAGVG DE // ID C1HUV6_NEIGO Unreviewed; 205 AA. AC C1HUV6; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NGAG_00033; OS Neisseria gonorrhoeae 1291. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=528345; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1291; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Yandava C., RA Gujja S., Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Apicella M.A., Steichen C., RA Lander E., Nusbaum C., Galagan J., Birren B.; RT "Annotation of Neisseria gonorrhoeae strain 1291."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999919; EEH61117.1; -; Genomic_DNA. DR ProteinModelPortal; C1HUV6; -. DR EnsemblBacteria; EEH61117; EEH61117; NGAG_00033. DR PATRIC; 29961777; VBINeiGon17328_0202. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21721 MW; 6080772E2E3D96ED CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFP TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVTAFQ ALWDG // ID C1MGB2_9ENTR Unreviewed; 211 AA. AC C1MGB2; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CSAG_04700; OS Citrobacter sp. 30_2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=469595; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=30_2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Ambrose C., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Citrobacter sp. 30_2."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDJ02000004; EEH96346.1; -; Genomic_DNA. DR ProteinModelPortal; C1MGB2; -. DR EnsemblBacteria; EEH96346; EEH96346; CSAG_04700. DR PATRIC; 27104688; VBICitSp98337_4692. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23067 MW; 8D10ACC0AF74A5F2 CRC64; MYQPDSPTVP FRLGLYPVVD SVQWIERLLQ AGVRTIQLRI KDKRDEEVET DVMAAIELGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGISTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLTQLA NHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWQVATA QLLDIAGVGD E // ID C1N5C6_MICPC Unreviewed; 507 AA. AC C1N5C6; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 26. DE SubName: Full=HMPP-kinase/thiamine monophosphate synthetase; GN ORFNames=MICPUCDRAFT_52893; OS Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales; OC Micromonas. OX NCBI_TaxID=564608; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1545; RX PubMed=19359590; DOI=10.1126/science.1167222; RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L., RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E., RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M., RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H., RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., RA Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., RA Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., RA Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., RA Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., RA Van de Peer Y., Grigoriev I.V.; RT "Green evolution and dynamic adaptations revealed by genomes of the RT marine picoeukaryotes Micromonas."; RL Science 324:268-272(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG663747; EEH52883.1; -; Genomic_DNA. DR RefSeq; XP_003062944.1; XM_003062898.1. DR ProteinModelPortal; C1N5C6; -. DR GeneID; 9688384; -. DR KEGG; mpp:MICPUCDRAFT_52893; -. DR KO; K14153; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 507 AA; 51869 MW; C19BE4F9AAE0D159 CRC64; MVRGKVLVVA GSDSGGGAGI QADIKTCLAL GAFATTAITA LTAQNTLGVH GVHPTPLDFV DAQIDAVVSD LPPDAVKTGM LANAETVTRV ASAIKSRALK NVVVDTVMIA KGGASLLEAD AIGALRGALI PLATVITPNV PEAAALLGMD EKDFNRDAME SRCRELGKLG CAWVLLKGGH VVDDLASATD HLYDVRNDLM RSFTAPRITT HNTHGTGCTF ASAIAASLAQ GMDVPSAVRR AKAYVSAAIA SNPGFGSGHG PLNHLPFYAA SAGGLSALNT DRSSSGDDSG SSGGDSGSRG STERPFDRRA LRLYLVTCDA LTEDKLRDAL AAGVTMVQMR DKTTASTREL IAKARAMKRV CDAAGVPFIV NDRVDVAIAV DACGVHLGQS DAPCSFARAL LGPGKIVGVS ARTPELASEA KRDGADYVGS GACFGTESKG DAKVIGLEGV RAVAERCEAL DLPVVAIGGI TTETGKRARE ETRADGIAVI SCVANAPDVA AAVRALL // ID C2BF39_9FIRM Unreviewed; 204 AA. AC C2BF39; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0072_0959; OS Anaerococcus lactolyticus ATCC 51172. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Anaerococcus. OX NCBI_TaxID=525254; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51172; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYO01000193; EEI86437.1; -; Genomic_DNA. DR ProteinModelPortal; C2BF39; -. DR EnsemblBacteria; EEI86437; EEI86437; HMPREF0072_0959. DR PATRIC; 24478732; VBIAnaLac40995_0308. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22387 MW; 1973E61A81DE0CD4 CRC64; MKKLYLVTNS DKYSEEEFLE RVEAALKGGV DILQLREKDK SDLEILNLGK KVKALCDSYK VPMLIDDKPH IAWALGLGVH LGADDMPIAL GRKLLGEKAL IGATAKSVEA AQKAEKEGAD YLGVGAIFET KTHVKTKRTS VETLKEIKKN VGIEVYAIGG LNIDNVDILK GTEVDGICVV RAIMDSPNVE EDTRKLKEKI NKIL // ID C2C5C2_VIBCL Unreviewed; 440 AA. AC C2C5C2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VCG_000254; OS Vibrio cholerae 12129(1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=592313; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=12129; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D., RA Vonstein V.; RT "Genome Assortment, Not Serogroup, Defines Vibrio cholerae Pandemic RT Strains."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFQ01000006; EEO00903.1; -; Genomic_DNA. DR EnsemblBacteria; EEO00903; EEO00903; VCG_000254. DR PATRIC; 29688959; VBIVibCho6176_0252. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48927 MW; 2A90133D1902DEB6 CRC64; MVRLVFPRHL SALIGHVQCA LLQAKEQGFA IQHIRLDVGS EAQFILEKSD ESLRIGSSLC SQEEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGNAAEQLII YSSETHRLNS KLNQHLAWVL ATLTLDFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPA MQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CSNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSVFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID C2CJY9_9FIRM Unreviewed; 204 AA. AC C2CJY9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0077_1775; OS Anaerococcus tetradius ATCC 35098. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Anaerococcus. OX NCBI_TaxID=525255; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35098; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGC01000116; EEI82077.1; -; Genomic_DNA. DR ProteinModelPortal; C2CJY9; -. DR EnsemblBacteria; EEI82077; EEI82077; HMPREF0077_1775. DR PATRIC; 24491861; VBIAnaTet98364_0765. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22452 MW; B70AE5EF8B480D72 CRC64; MKKLYLVTNS DKYTEEEFLQ RIEDALKGGV DILQLREKDK TDREILALGK KVKDLCDSYK VPMLIDDKPH LAWALGVGVH LGSDDMPISL ARKLLGKDAL IGATAKSVEA GKKCEEEGAD YLGVGAIYET KTHVKTKRTS VETLREIKKN VAIDVYAIGG LNIDNIDILQ GSGADGICVV RAIMDSPRVL EDTKKLKAKI QEIL // ID C2CNS6_CORST Unreviewed; 213 AA. AC C2CNS6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0308_1055; OS Corynebacterium striatum ATCC 6940. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=525268; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 6940; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGE01000045; EEI78683.1; -; Genomic_DNA. DR ProteinModelPortal; C2CNS6; -. DR EnsemblBacteria; EEI78683; EEI78683; HMPREF0308_1055. DR PATRIC; 27673218; VBICorStr83233_0606. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 31 35 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). SQ SEQUENCE 213 AA; 22268 MW; F29BC686B6BF3CBA CRC64; MLDLRCYFVT GTNMTPEIAA AAVRGGAGVV QVRSKPISAR ALYDLGARVA ETVHEVNPRA HVLIDDRVDV ALALRCAGAP VHGVHIGQDD LCPRAARELL GPDAIIGLTT GTLELIRDAN QYADVLDYVG CGPFRATPTK DSGRTPLGLQ GYPEIVAASQ LPVVAIGDVT ADDAAELAAT GVDGLAVVRG IMNAPDPAAY CERLLSEFEK GRA // ID C2CZZ3_LACBR Unreviewed; 218 AA. AC C2CZZ3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0496_0865; OS Lactobacillus brevis subsp. gravesensis ATCC 27305. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525310; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27305; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGG01000020; EEI71903.1; -; Genomic_DNA. DR ProteinModelPortal; C2CZZ3; -. DR EnsemblBacteria; EEI71903; EEI71903; HMPREF0496_0865. DR PATRIC; 30189508; VBILacBre13134_0436. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23338 MW; E044C0146091034D CRC64; MAMAFKVGML RAYFIAGTQD IKKSNLTLPE VLTQALQSGI TAFQYREKGA GSLSEEKKVD MAHTLRKLCE TYKIPFIVDD DVDLALETAA DGIHVGQKDE RVTKVIQQVG TTMFVGLSCD TKEQVAIANE TEGISYIGSG PVYPTGSKAD ADPVIGIAGL KKLVQSSRLP VVAIGGITEG NISELPQTGV AGASVISMIA QSNDIRRTVT RMRAVFEK // ID C2D270_LACBR Unreviewed; 210 AA. AC C2D270; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0496_1642; OS Lactobacillus brevis subsp. gravesensis ATCC 27305. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525310; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27305; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGG01000100; EEI71089.1; -; Genomic_DNA. DR ProteinModelPortal; C2D270; -. DR EnsemblBacteria; EEI71089; EEI71089; HMPREF0496_1642. DR PATRIC; 30190538; VBILacBre13134_1353. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22856 MW; BFD6C29480255939 CRC64; MKVTNRPLYL VTDHTNLNDE DFLQQIDLAC ESGVSLLQLR EKNRSSRDIY EWAVKVKDIA DRHRVPLMID DRLDIAQAVD AAGVHLGQSD LPVEIARRIL GNKKIIGATT KTLKQAKLAE EQGADYLGVG AIFPTQTHVK TVHTSIETLG KIKEAVNIPV YAIGGLKAHN IQAIEPAHVD GVAVVSAIMQ AKNAKAATRE LLDAVEDAIG // ID C2DA00_ENTFL Unreviewed; 211 AA. AC C2DA00; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0349_0060; OS Enterococcus faecalis TX1322. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=525278; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX1322; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGM01000004; EEN75998.1; -; Genomic_DNA. DR ProteinModelPortal; C2DA00; -. DR EnsemblBacteria; EEN75998; EEN75998; HMPREF0349_0060. DR PATRIC; 26766504; VBIEntFae10621_0717. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 44C250957E384C82 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVAFVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQELM RVTERMLEVR K // ID C2DPB5_ECOLX Unreviewed; 211 AA. AC C2DPB5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0358_2069; OS Escherichia coli 83972. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=525281; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=83972; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGN01000087; EEJ48017.1; -; Genomic_DNA. DR ProteinModelPortal; C2DPB5; -. DR SMR; C2DPB5; 9-208. DR EnsemblBacteria; EEJ48017; EEJ48017; HMPREF0358_2069. DR PATRIC; 31226702; VBIEscCol21464_4731. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23030 MW; D9436839F2B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSTIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID C2ESH6_9LACO Unreviewed; 215 AA. AC C2ESH6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0549_0412; OS Lactobacillus vaginalis ATCC 49540. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525366; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49540; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGV01000026; EEJ41141.1; -; Genomic_DNA. DR ProteinModelPortal; C2ESH6; -. DR EnsemblBacteria; EEJ41141; EEJ41141; HMPREF0549_0412. DR PATRIC; 29222709; VBILacVag81158_0634. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23427 MW; DF883E9A0E1528B8 CRC64; MNFNPKMLQI YLVGGTQDTH HDSYEFLAKV EEAMQGGITA FQYREKDSST MTADAQLVMA RRLVEMGNRY SIPVLIDDDV QMALRVGADG VHVGQDDEKI EQVIKEAADK LIIGYSCNTA AEVEKANQLS AIDYLGCGPV FETTSKVDAD PVLGLTKLKE LNKLSTHPLV AIGGLSLENI PEVLKTGVAG LSMISLVLNS KNITETIEKI KTLVK // ID C2FA10_LACPA Unreviewed; 213 AA. AC C2FA10; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0530_0418; OS Lactobacillus paracasei subsp. paracasei ATCC 25302. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525337; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25302; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGY01000036; EEI69301.1; -; Genomic_DNA. DR ProteinModelPortal; C2FA10; -. DR EnsemblBacteria; EEI69301; EEI69301; HMPREF0530_0418. DR PATRIC; 37008175; VBILacPar51859_1152. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22607 MW; 1C71894D5791C1D5 CRC64; MNATDLKLYL VTHRYDDNEA TFLAKIAAAC ENGVTMVQLR EKMLSTRAYF ELAQRVKLIT DRYQIPLIID DRVDICLAVD AAGVHIGDDE LPVAMTRQLI GPDKVLGVST KTVETAVAAV AAGADYLGVG AIFPTQTKAN AAVTPIATLK AITAQVAVPV VAIGGVKEAN LATFKDTGIA GVAIVSEIMQ APDIAHKVQA LRTKLKAVLP NDR // ID C2FVP7_9SPHI Unreviewed; 212 AA. AC C2FVP7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0765_1403; OS Sphingobacterium spiritivorum ATCC 33300. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=525372; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33300; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHB01000033; EEI93105.1; -; Genomic_DNA. DR ProteinModelPortal; C2FVP7; -. DR EnsemblBacteria; EEI93105; EEI93105; HMPREF0765_1403. DR PATRIC; 29430447; VBISphSpi19069_1646. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). SQ SEQUENCE 212 AA; 23293 MW; 02BE64136D0FBA6C CRC64; MSIHPGFPYP LYLVISEADC QGKDILHVAE QAILGGVDII QLREKYASTP EFIEKALRLK EITEKHRIPL IINDNLRVAI EVNAFGIHVG NSDTPPTVIR DKWPDCSCLG YSIEYLEQLD NPETATADYL GISPIFVTDT KTDTVTEWGL EGIQQIRQRS DKPLIAIGHM NLQNIASVLQ AGADAIAVVS AICAASDPKQ AAYELKNKIL IA // ID C2FVT2_9SPHI Unreviewed; 198 AA. AC C2FVT2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0765_1438; OS Sphingobacterium spiritivorum ATCC 33300. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=525372; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33300; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHB01000034; EEI92924.1; -; Genomic_DNA. DR ProteinModelPortal; C2FVT2; -. DR EnsemblBacteria; EEI92924; EEI92924; HMPREF0765_1438. DR PATRIC; 29430511; VBISphSpi19069_1678. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 198 AA; 22352 MW; 81FB4BE6DD98F7B8 CRC64; MIIISPDTIT PQHIELIHAI PWSDALLYHL RLPSAAKDDI AHILEDIDKH LYPFIVLHYH KETALKAGIR RIHISTDKKK EISIPDTDLI LSVSTHHVDE FNSLDADIAY AFISPVYPSI SKEGYQATAE FKIHNIQHRS NLNSKMIALG GITEYNISEL KALGYDDVAL CGYIWQHSDP LFAADKCFSI SQTTSYVQ // ID C2FVT3_9SPHI Unreviewed; 209 AA. AC C2FVT3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; ORFNames=HMPREF0765_1439; OS Sphingobacterium spiritivorum ATCC 33300. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=525372; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33300; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHB01000034; EEI92925.1; -; Genomic_DNA. DR ProteinModelPortal; C2FVT3; -. DR EnsemblBacteria; EEI92925; EEI92925; HMPREF0765_1439. DR PATRIC; 29430513; VBISphSpi19069_1679. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23610 MW; 8B20A657EE752D31 CRC64; MYSRLQYIST GNTVNEQLNN IRKVLENKGN WIQLRWKNAP KTALIDLAFQ VTELKKQFDF TYIINDHVSI AYKVNSDGVH LGLKDLSVQQ ARNFLGSDKI IGGTANTAED VRQRIAENCD YIGLGPLRFT SSKQNLSPVL GYEGYQNIIQ EIQKEDQHHP PIYAIGGIKQ EDILQLQHIG IYGVAVSSLL THSVSTQSII QHINHEFYG // ID C2GET3_9CORY Unreviewed; 181 AA. AC C2GET3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-OCT-2013, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF0293_0426; OS Corynebacterium glucuronolyticum ATCC 51866. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=548478; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51866; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHF01000014; EEI64095.1; -; Genomic_DNA. DR ProteinModelPortal; C2GET3; -. DR EnsemblBacteria; EEI64095; EEI64095; HMPREF0293_0426. DR PATRIC; 25278729; VBICorGlu69621_0044. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 181 AA; 19084 MW; 1584EA6FB8C25885 CRC64; MQLRDKDATE AEFLARAIKL KELMEPTGVP LFVDDRLDVA CELGLNLHIG QNDVDYLEAR KKLPGNLMLG LSVGNHRELD EVERMDPALR PDVIGVGPVA DTTTKKDAPA GIGVQAFAEI ATRAKGLGVP AVAIGGVNLT NASELGGTDG AGICVVSAIM KAADPEEAAR ELRAAFENGR N // ID C2GET7_9CORY Unreviewed; 51 AA. AC C2GET7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; GN ORFNames=HMPREF0293_0430; OS Corynebacterium glucuronolyticum ATCC 51866. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=548478; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51866; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHF01000014; EEI64099.1; -; Genomic_DNA. DR EnsemblBacteria; EEI64099; EEI64099; HMPREF0293_0430. DR PATRIC; 25278735; VBICorGlu69621_0047. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Kinase; Transferase. SQ SEQUENCE 51 AA; 5493 MW; 68E5B2A296232E9D CRC64; MATDWTLYLV TDPDLGGGPE RVPEIVDKAV KGGVSVVQLR EKHAQLPSGD F // ID C2GW91_BIFLN Unreviewed; 917 AA. AC C2GW91; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 37. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; ORFNames=HMPREF0175_1277; OS Bifidobacterium longum subsp. longum ATCC 55813. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=548480; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 55813; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHI01000023; EEI80696.1; -; Genomic_DNA. DR ProteinModelPortal; C2GW91; -. DR EnsemblBacteria; EEI80696; EEI80696; HMPREF0175_1277. DR PATRIC; 36943336; VBIBifLon7869_0952. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100404 MW; 83F0334D12552216 CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLADTKA AGWFVVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF RDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE TEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID C2H2D3_ENTFL Unreviewed; 211 AA. AC C2H2D3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0345_1321, UMK_02339; OS Enterococcus faecalis ATCC 29200. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=525271; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29200; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29200; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., RA McCowan C., Murphy C., Neiman D., Pearson M., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis ATCC_29200."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHK01000085; EEN71730.1; -; Genomic_DNA. DR EMBL; AJEK01000016; EOJ08074.1; -; Genomic_DNA. DR ProteinModelPortal; C2H2D3; -. DR EnsemblBacteria; EEN71730; EEN71730; HMPREF0345_1321. DR EnsemblBacteria; EOJ08074; EOJ08074; UMK_02339. DR PATRIC; 29308988; VBIEntFae2828_0958. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22866 MW; A6E43F880C487223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID C2HT08_VIBAB Unreviewed; 440 AA. AC C2HT08; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VCA_002574; OS Vibrio albensis VL426. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=593585; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VL426; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Chertkov O., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D., RA Vonstein V.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHV01000001; EEO03563.1; -; Genomic_DNA. DR EnsemblBacteria; EEO03563; EEO03563; VCA_002574. DR PATRIC; 30089319; VBIVibCho6562_1554. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48957 MW; 11C875BA62AC9EDE CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGFA IQHIRLDVGS DAQFILEKSE ESLRIGSSLC SQEETSEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGFHD KYAFTLDKWQ YGNAAEQLII YPSENHRLNS KVNQHLAWVL ASLALGFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQC DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID RSNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSVFAD FVDAEYKLMP ASESCEPLSC LAREVADAHR // ID C2I1Z8_VIBCL Unreviewed; 440 AA. AC C2I1Z8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VIF_000656; OS Vibrio cholerae TM 11079-80. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=593586; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TM 11079-80; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D., RA Vonstein V.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHW01000014; EEO07918.1; -; Genomic_DNA. DR ProteinModelPortal; C2I1Z8; -. DR EnsemblBacteria; EEO07918; EEO07918; VIF_000656. DR PATRIC; 30071550; VBIVibCho131272_0343. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48792 MW; 3C026C66CB734686 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGFA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQEETSEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGFHD EYGFTRDKWQ YGNAAEQLII YPSETHRLNS KLNQHLAWVL ASLALGFPIE DGLCIARAAI TQGDSVSCET WPTQFERFPA VQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVKTV QLRIKDPTQG DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQSSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CSNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID C2IEJ4_VIBCL Unreviewed; 440 AA. AC C2IEJ4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VCC_001107; OS Vibrio cholerae RC9. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=593589; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RC9; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Meinecke L.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., RA Bartels D., Vonstein V.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHX01000008; EEO11121.1; -; Genomic_DNA. DR ProteinModelPortal; C2IEJ4; -. DR EnsemblBacteria; EEO11121; EEO11121; VCC_001107. DR PATRIC; 31175501; VBIVibCho32669_1049. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID C2IX66_VIBCL Unreviewed; 440 AA. AC C2IX66; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VCB_003556; OS Vibrio cholerae TMA 21. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=593590; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TMA 21; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Saunders E.H., Hasan N.A., Munk A.C., Tapia R., Green L., Rogers Y., RA Detter J.C., Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., RA Bartels D., Vonstein V.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHY01000019; EEO12121.1; -; Genomic_DNA. DR EnsemblBacteria; EEO12121; EEO12121; VCB_003556. DR PATRIC; 30085903; VBIVibCho23640_3591. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48804 MW; 95A1F842FDF11A8A CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGFA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQEETSEPCD YYLDYVSENR VLPEAMMCNA RCSVTVGLHD EYGFTLDKWQ YGNAAEQLII YSSETHRLNS KLNQHLAWVL ATLTLDFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPA MQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QVDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQIPYQGQHG IPTVAIGGID CSNIRDVLDC GVTAVAVVRA ITESSDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVAGANR // ID C2JI01_VIBCL Unreviewed; 440 AA. AC C2JI01; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VCF_003581; OS Vibrio cholerae BX 330286. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=593587; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BX 330286; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D., RA Vonstein V.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIA01000007; EEO19541.1; -; Genomic_DNA. DR ProteinModelPortal; C2JI01; -. DR EnsemblBacteria; EEO19541; EEO19541; VCF_003581. DR PATRIC; 28053672; VBIVibCho109173_3450. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID C2JMR0_ENTFL Unreviewed; 211 AA. AC C2JMR0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0346_1421, UKU_02441; OS Enterococcus faecalis EnGen0297. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=491075; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HH22; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HH22; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., RA McCowan C., Murphy C., Neiman D., Pearson M., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis HH22."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIX01000109; EEI57590.1; -; Genomic_DNA. DR EMBL; AJDY01000027; EOI79325.1; -; Genomic_DNA. DR EnsemblBacteria; EEI57590; EEI57590; HMPREF0346_1421. DR EnsemblBacteria; EOI79325; EOI79325; UKU_02441. DR PATRIC; 28700947; VBIEntFae71477_1439. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; FA22A90EE15C1754 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKVVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID C2K0H8_LACRH Unreviewed; 209 AA. AC C2K0H8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0539_2663; OS Lactobacillus rhamnosus LMS2-1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525361; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMS2-1; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIZ01000111; EEN79260.1; -; Genomic_DNA. DR ProteinModelPortal; C2K0H8; -. DR EnsemblBacteria; EEN79260; EEN79260; HMPREF0539_2663. DR PATRIC; 37038185; VBILacRha123537_1818. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21826 MW; DB2D7C7B82C165F7 CRC64; MNAEALQLYL VTNRYADSPE VFLAKIAAAC ENGVTMVQLR EKSLTTRDYY ALAKQVKLIT DRYRIPLIID DRVDVCLAVD AAGVHIGDDE LPVAVTRQLL GSDKILGVST KTVATATAAV AAGADYLGVG AIFPTQTKAA APLTSLATLK AITAAVSVPV VAIGGIKADN LDTFKATGIA GVAIVSEIMQ APDTAQKVQT LSAKLKEVL // ID C2KLC9_LEUMC Unreviewed; 212 AA. AC C2KLC9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0555_1445; OS Leuconostoc mesenteroides subsp. cremoris ATCC 19254. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=586220; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19254; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKV01000078; EEJ41947.1; -; Genomic_DNA. DR ProteinModelPortal; C2KLC9; -. DR EnsemblBacteria; EEJ41947; EEJ41947; HMPREF0555_1445. DR PATRIC; 27458582; VBILeuMes33277_0710. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23066 MW; E0FB8426441A772F CRC64; MFDPSILVNY FVLGTQDTNG ERHFFEVLEE ALQSKISVFQ YREKGQLALS GSEKLRVAKK VRQLTADYHV PLIIDDDIQL AHEIDAEGVH FGQKDGDIIN NIQLAGNLAV GVSVSNDSQY KRIENIKGID YIGIGPVFAT VSKADANPEI GVEGLKYLTS KSKWPSVAIG GISETNLSSV LSTGVNGAAV ISMISQSANI SATLKYWRSL HL // ID C2KZ67_9FIRM Unreviewed; 220 AA. AC C2KZ67; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF6123_1786; OS Oribacterium sinus F0268. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Oribacterium. OX NCBI_TaxID=585501; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0268; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKX01000181; EEJ50919.1; -; Genomic_DNA. DR ProteinModelPortal; C2KZ67; -. DR EnsemblBacteria; EEJ50919; EEJ50919; HMPREF6123_1786. DR PATRIC; 28541257; VBIOriSin4127_0984. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23942 MW; D8457BC09B46BDD5 CRC64; MKFDKDSLLL YAVTDRHWLK GRSLKEDVES ALKGGASFIQ LREKEDMALD HDAYLQEALE IGRLCRSYGV PFVLDDEVEL AIEADADGVH VGQEDMEAGM VREKLGKEKI LGVSVQTVEE AILARERGAD YLGVGAVFTT GSKKDAVDVS FETLKAICEA VDLPVVAIGG ISRENVMELK DSGIAGIAVI SAIFAKPDIE GATADLRKQC LKALFPEKER // ID C2LF60_PROMI Unreviewed; 184 AA. AC C2LF60; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-OCT-2013, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0693_0500; OS Proteus mirabilis ATCC 29906. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Proteus. OX NCBI_TaxID=525369; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29906; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLE01000012; EEI49563.1; -; Genomic_DNA. DR ProteinModelPortal; C2LF60; -. DR EnsemblBacteria; EEI49563; EEI49563; HMPREF0693_0500. DR PATRIC; 36138555; VBIProMir92659_3398. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 184 AA; 20229 MW; D1536439F972D8F6 CRC64; MKIGVTTIQL RIKDKQPKDV EQDIITAIKL GRKYNARLFI NDYWELAIKH HAYGVHLGQE DLDIADLDAI KQSGLCLGIS THNDTELQRA KRLLPSYIAL GHIFPTTTKD MPSKPQGLRA LKHQVEQTHD FPTVAIGGIS LEKVSDVVAT GVGGVALVSA ITKASDWQQV TLKLLELVEG KPSC // ID C2LWF8_STAHO Unreviewed; 196 AA. AC C2LWF8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=STAHO0001_1071; OS Staphylococcus hominis SK119. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=629742; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK119; RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLP01000007; EEK12813.1; -; Genomic_DNA. DR ProteinModelPortal; C2LWF8; -. DR EnsemblBacteria; EEK12813; EEK12813; STAHO0001_1071. DR PATRIC; 31405207; VBIStaHom49788_0393. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 22493 MW; 732E689430ED16E1 CRC64; MFIFIAITKY KDLTNDDVQH FLDISDGIDG LLFRTPMSSS DLSSFLTSLI EKGFPKSKII IHSDVHLLEQ LHLSHIHFRE MDEDAFSYKS THPEIEVSMS THSIESVKAA YEHDLDYVFF GHIFKTPSKP NQWPRSKAEI QRVLEIPIPI YAIGGITEKT ILQLPHGFKG ICAISFFMNA SLQQIELLRK EWLKDA // ID C2LXI1_STAHO Unreviewed; 212 AA. AC C2LXI1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=STAHO0001_2055; OS Staphylococcus hominis SK119. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=629742; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK119; RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLP01000009; EEK12525.1; -; Genomic_DNA. DR ProteinModelPortal; C2LXI1; -. DR EnsemblBacteria; EEK12525; EEK12525; STAHO0001_2055. DR PATRIC; 31405970; VBIStaHom49788_0767. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23190 MW; 7FB8A445669AF2A9 CRC64; MFDSKSLQVY FICGTQDIIG DQNIKDVLKA ALESGITLFQ FREKGPNALV GDEKEALAKE LKTLCHEYKV PFLINDDVDL AEKIDADGIH VGQDDEIIAS FANRFKNKII GLSVGNVKEY QQSDLEHVDY IGVGPMYETS SKSDASAPVG PEMIATLKNI NPSLPMVAIG GITEDNCELI AKEGADGVSV ISVITHSQNI DKTVNKLKHY FK // ID C2MC79_9PORP Unreviewed; 673 AA. AC C2MC79; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=PORUE0001_0856; OS Porphyromonas uenonis 60-3. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=596327; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=60-3; RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLR01000170; EEK16708.1; -; Genomic_DNA. DR ProteinModelPortal; C2MC79; -. DR EnsemblBacteria; EEK16708; EEK16708; PORUE0001_0856. DR PATRIC; 29517320; VBIPorUen60963_0986. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 673 AA; 74223 MW; 8D88EB8B0FC21E66 CRC64; MIVITPPERQ LVEDVAGDII DVASSCICKV HLRMPGASEA DFRKVLDSLE PAYHQHVVLC DHYALLAEYD VAGVYLPYRR VAEWRNIPLA PHQTIAVGAH SIQELQELPF TPHYALLSPL FDSISKEGYQ GNPALLSCRE ALIKLPYPVY ALGGITPEKQ EAVAKAGYAG VAVLGDIWSQ PWKQLPERLA QYQLPAILTV AGHDPTSGAG ISVDTRIAND LSVQCYSVIS TLTAQSLHRF VSTTATPSDQ LQASLTTLLT DHPVTVAKLG MVQDLQQAVH IVAQMKALGV KRIIWDPILQ PTATEVTQPN LWTEEQDKLA TLLNEVSLVT PNKPEAQALF GTDDPAELQR IAQKHDVAIL LKGGHDTTSP HLVVNQLITS DGIHPYYTHR YDKSIHGTGC MLSAAIASYW AMEYSLVSSV QRACHYLATI FAGQPNLPER QLLCPKIFRG SRKKQHLYFD FDLQYVTNES DPDRLYNKVS QYLEAGGRWV QLRLKEATTE ERIEMGLRLR RLTDCYDACL LIDDDIIATI AVDADGVHLG KRDCPPQEAR RILGDEYIIG YTVNSLDDLP RALAANIDYI GVGPYRDTQT KALLAPILGL EGISQIAQQV KETNRQFIVP QIVAIGGIRP EDAETLFSNK DIDGIAVSGA IEHATDMGHT VSQLLRDTSS FPN // ID C2MFJ5_BACCE Unreviewed; 201 AA. AC C2MFJ5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0001_3350; OS Bacillus cereus m1293. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526973; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M1293; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLS01000016; EEK46746.1; -; Genomic_DNA. DR ProteinModelPortal; C2MFJ5; -. DR EnsemblBacteria; EEK46746; EEK46746; bcere0001_3350. DR PATRIC; 25117272; VBIBacCer121715_1430. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 26 30 HMP-PP binding (By similarity). FT REGION 125 127 THZ-P binding (By similarity). FT REGION 177 178 THZ-P binding (By similarity). FT METAL 62 62 Magnesium (By similarity). FT METAL 81 81 Magnesium (By similarity). FT BINDING 61 61 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 201 AA; 21410 MW; 1E77038FFBBE49D8 CRC64; MGSNNCTKDP LQVLREALEG GITIFQFREK GEGALTGEER ICFAKELQAI CKEYGVPFIV NDDVELALEL DADGVHVGQD DEGITSVREK MGDKIIGVST HTIEEARWAI ENGADYLGVG PIFPTSTKKD TKAVQGTKGL AHFREQGITI PIVGIGGISI ENTASVIEAG ADGVSVISAI SLAESAYEST KRLVEEVSKS L // ID C2MVD1_BACCE Unreviewed; 222 AA. AC C2MVD1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0002_3360; OS Bacillus cereus ATCC 10876. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526980; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10876; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLT01000013; EEK52610.1; -; Genomic_DNA. DR ProteinModelPortal; C2MVD1; -. DR EnsemblBacteria; EEK52610; EEK52610; bcere0002_3360. DR PATRIC; 24858041; VBIBacCer12024_0855. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23962 MW; 9DCF7ACB92C3E1F5 CRC64; MKEMARIEID KMSTLLQVYF IMGSNNCTRD PLAVLKEALD GGVTLFQFRE KGEGSLIGED RVRFAKELQT LCKEYSVPFI VNDDVELAIE LDADGVHVGQ DDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TRKLAEEVKR SL // ID C2MWG3_BACCE Unreviewed; 194 AA. AC C2MWG3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0002_6240; OS Bacillus cereus ATCC 10876. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526980; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10876; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLT01000022; EEK52328.1; -; Genomic_DNA. DR ProteinModelPortal; C2MWG3; -. DR EnsemblBacteria; EEK52328; EEK52328; bcere0002_6240. DR PATRIC; 24858681; VBIBacCer12024_1512. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21485 MW; 63EEC055EFC6FA42 CRC64; MPFEELVNVA MQIESEIDYL HIREREKSTK ELYEGVESLL RKGFPASKIV INDRIDIAIL LNIPRVQLGY RSTDVKSVKE KFSYLHVGYS VHSLEEAIDA FKNGADSLVY GHVFPTDCKK GVPARGLEEI SDIARCLSIP ITAIGGITPE NTVDVLTNGV SGIAVMSGIV SSSNPYSKAK SYKESIRKWA EKHV // ID C2NCE6_BACCE Unreviewed; 219 AA. AC C2NCE6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0004_3430; OS Bacillus cereus BGSC 6E1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526970; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 6E1; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLU01000015; EEK58314.1; -; Genomic_DNA. DR ProteinModelPortal; C2NCE6; -. DR EnsemblBacteria; EEK58314; EEK58314; bcere0004_3430. DR PATRIC; 24928198; VBIBacCer134364_1253. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23482 MW; D33A0EEF285CFD9C CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID C2NTN0_BACCE Unreviewed; 222 AA. AC C2NTN0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0005_3420; OS Bacillus cereus 172560W. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526967; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=172560W; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLV01000013; EEK63863.1; -; Genomic_DNA. DR ProteinModelPortal; C2NTN0; -. DR EnsemblBacteria; EEK63863; EEK63863; bcere0005_3420. DR PATRIC; 24749698; VBIBacCer25702_0576. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23963 MW; DFB1903340CD9232 CRC64; MKEMARIEID KMSKLLQVYF IMGSNNCTRD PLAVLKEALD GGVTLFQFRE KGEGSLIGED RVRFAKELQT LCKEYSVPFI VNDDVELAIE LDADGVHVGQ DDEGITSVRE KMGDKIIGVS AHTIEEACFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA INLAESAYES TRKLAEEVKR SL // ID C2NUG5_BACCE Unreviewed; 194 AA. AC C2NUG5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0005_6300; OS Bacillus cereus 172560W. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526967; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=172560W; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLV01000024; EEK63574.1; -; Genomic_DNA. DR ProteinModelPortal; C2NUG5; -. DR EnsemblBacteria; EEK63574; EEK63574; bcere0005_6300. DR PATRIC; 24750322; VBIBacCer25702_0995. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21445 MW; B3626EC0B3663FB5 CRC64; MPFEELVNVA MQIESEIDYL HIREREKSTK ELYEGVESLL MEGFPASKIV INDRIDIAIL LNIPRVQLGY RSTDVKSVKE KFSYLHVGYS VHSLDEAIVA FKNGADSLVY GHVFPTDCKK GVPARGLEEI SDIARCLSIP ITAIGGITPE NTVDVLTNGV SGIAVMSGII SSSNPYSKAK SYKESIRKWA EKHV // ID C2P9S9_BACCE Unreviewed; 219 AA. AC C2P9S9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0006_3490; OS Bacillus cereus MM3. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526971; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MM3; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLW01000014; EEK69467.1; -; Genomic_DNA. DR ProteinModelPortal; C2P9S9; -. DR EnsemblBacteria; EEK69467; EEK69467; bcere0006_3490. DR PATRIC; 24977681; VBIBacCer63122_0735. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23585 MW; 08A49FBCDFA5810A CRC64; MSRITKAEMS RLLSVYFIMG SNNCAKEPLQ VLRDALEGGI TIFQFREKGE GALTGEKRIC FAKEIQTVCK EYGVPFIVND DVELAMELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQEITIPI VGIGGITIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSKSL // ID C2PRH5_BACCE Unreviewed; 208 AA. AC C2PRH5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0007_6470; OS Bacillus cereus AH621. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526972; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH621; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLX01000031; EEK74728.1; -; Genomic_DNA. DR ProteinModelPortal; C2PRH5; -. DR EnsemblBacteria; EEK74728; EEK74728; bcere0007_6470. DR PATRIC; 24835102; VBIBacCer129149_1511. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 22941 MW; 80451FC5A6BD6FFB CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLFKKGFPP SKLVINDRID IAILLNIPRV QLGYRSADVR LVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEIAHMASC LSIPITAIGG ITPENTGDVL ANGVSGIAVM SGIISSSNPY SKAKSYKESI RKWAGKHV // ID C2Q4N1_BACCE Unreviewed; 219 AA. AC C2Q4N1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0007_52990; OS Bacillus cereus AH621. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526972; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH621; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLX01000126; EEK70220.1; -; Genomic_DNA. DR ProteinModelPortal; C2Q4N1; -. DR EnsemblBacteria; EEK70220; EEK70220; bcere0007_52990. DR PATRIC; 24844594; VBIBacCer129149_0745. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23773 MW; B4612AB4575E5335 CRC64; MSRITMDEMS RLLPVYFIMG SNNCTKEPLQ VLRDALEGGI TIFQFREKGE GALTGEKRID FAKELQALCK EYGVPFLVND DVELALELDA DGVHVGQDDE GITSVRKKMG DKIIGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLKY FREQEITIPI VGIGGITIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVNKSL // ID C2Q6T2_BACCE Unreviewed; 155 AA. AC C2Q6T2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=bcere0009_3280; OS Bacillus cereus R309803. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526968; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R309803; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLY01000012; EEK80738.1; -; Genomic_DNA. DR ProteinModelPortal; C2Q6T2; -. DR EnsemblBacteria; EEK80738; EEK80738; bcere0009_3280. DR PATRIC; 25001022; VBIBacCer63003_0108. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 155 AA; 16359 MW; 7A4534ED8C02DCAF CRC64; MQALCKEYGV PFIVNDDVEL AIELDADGVH VGQDDEGITS VRERMGDKII GVSTHTIEEA RWAIENGADY LGVGPIFPTS TKKDTKAVQG TKGLAHFREQ GIMIPIVGIG GITIENTASV IEAGADGVSI ISAISLAESA YESTKELVEA VSKSL // ID C2QMN7_BACCE Unreviewed; 219 AA. AC C2QMN7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0010_3410; OS Bacillus cereus ATCC 4342. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526977; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 4342; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLZ01000008; EEK86120.1; -; Genomic_DNA. DR ProteinModelPortal; C2QMN7; -. DR EnsemblBacteria; EEK86120; EEK86120; bcere0010_3410. DR PATRIC; 24870294; VBIBacCer13872_5364. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23547 MW; 7F80D03FBB675691 CRC64; MSRISKAEMS RLLSVYFIMG SNNCTKDPLQ VLRDALEGGI TIFQFREKGE GALTGEKRIY FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSIREKMG DKIIGVSTHT IEEAHWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN AASVIEAGAD GISVISAISL AESAYESTKK LVEEVSKNL // ID C2QNL4_BACCE Unreviewed; 208 AA. AC C2QNL4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0010_6280; OS Bacillus cereus ATCC 4342. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526977; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 4342; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLZ01000016; EEK85539.1; -; Genomic_DNA. DR ProteinModelPortal; C2QNL4; -. DR EnsemblBacteria; EEK85539; EEK85539; bcere0010_6280. DR PATRIC; 24870942; VBIBacCer13872_0268. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 22998 MW; C544BDC658764C35 CRC64; MNMKNELHVI SNGHMSFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLKKGFPA SKIVINDRID IAILLNIPRV QLGYRSADVR SVKEKFSYLH VGYSVHSLEE AIDAFKNGAD SLVYGHVFPT DCKKGVPARG LEEISDIAKC LSIPITAIGG ITTENTGDVL TNGVSGIAVM SGIISSSNPY SKAKSYKESI RKWAEKHV // ID C2R2X2_BACCE Unreviewed; 219 AA. AC C2R2X2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0011_3450; OS Bacillus cereus m1550. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526969; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M1550; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMA01000009; EEK91360.1; -; Genomic_DNA. DR ProteinModelPortal; C2R2X2; -. DR EnsemblBacteria; EEK91360; EEK91360; bcere0011_3450. DR PATRIC; 25128257; VBIBacCer61419_5266. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23589 MW; E42FE4B932DC5785 CRC64; MMRIETKKMS KLLQVYFIMG SNNCTRDPLA VLKEALDGGV TLFQFREKGE GSLIGGDRVR FAKELQTLCK EYSVPFIVND DVELAIELDA DGVHVGQDDE GITSVREKMG DKIIGVSAHT IEEARFAIKN GADYLGVGPI FPTSTKKDTK AVQGTKGLAY FREQGITVPI VGIGGITIEN TAAVIEAGAD GISVVSAISL AESAYESTRK LAEEVKRSL // ID C2R3Q8_BACCE Unreviewed; 194 AA. AC C2R3Q8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0011_6330; OS Bacillus cereus m1550. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526969; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M1550; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMA01000018; EEK90855.1; -; Genomic_DNA. DR ProteinModelPortal; C2R3Q8; -. DR EnsemblBacteria; EEK90855; EEK90855; bcere0011_6330. DR PATRIC; 25129070; VBIBacCer61419_0353. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21431 MW; AD9381C0B3663FB5 CRC64; MPFEELVNVA MQIESEIDYL HIREREKSTK ELYEGVESLL MEGFPASKIV INDRIDIAIL LNIPRVQLGY RSTDVKSVKE KFSYLHVGYS VHSLDEAIVA FKNGADSLVY GHVFPTDCKK GVPARGLEEI SDIARCLSIP ITAIGGITPE NTVDVLTNGV SGIAVMSGIV SSSNPYSKAK SYKESIRKWA EKHV // ID C2RHV5_BACCE Unreviewed; 222 AA. AC C2RHV5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0012_3350; OS Bacillus cereus BDRD-ST24. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526974; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-ST24; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMB01000013; EEK96641.1; -; Genomic_DNA. DR ProteinModelPortal; C2RHV5; -. DR EnsemblBacteria; EEK96641; EEK96641; bcere0012_3350. DR PATRIC; 24904347; VBIBacCer11397_0669. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23917 MW; 91FB50402DD80922 CRC64; MKEMARIEID KMSKLLQVYF IMGSNNCTRD PLAVLKEALD GGVTIFQFRE KGEGSLIGED RVRFAKALQT LCNEYSVPFI VNDDVELAIE LDADGVHVGQ DDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TRKLAEEVKR SL // ID C2RIP0_BACCE Unreviewed; 208 AA. AC C2RIP0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0012_6210; OS Bacillus cereus BDRD-ST24. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526974; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-ST24; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMB01000019; EEK96359.1; -; Genomic_DNA. DR ProteinModelPortal; C2RIP0; -. DR EnsemblBacteria; EEK96359; EEK96359; bcere0012_6210. DR PATRIC; 24905083; VBIBacCer11397_1267. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 23036 MW; 316214A22E470F4E CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLMEGFPA SKIVINDRID IAILLNIPRV QLGYRSTDVK SVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEISDIARC LSIPITAIGG ITPENTVDVL TNGVSGIAVM SGIVSSSNPY SKAKSYKESI RKWAEKHV // ID C2RYF7_BACCE Unreviewed; 201 AA. AC C2RYF7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0013_3690; OS Bacillus cereus BDRD-ST26. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526975; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-ST26; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMC01000013; EEL02446.1; -; Genomic_DNA. DR ProteinModelPortal; C2RYF7; -. DR EnsemblBacteria; EEL02446; EEL02446; bcere0013_3690. DR PATRIC; 24915852; VBIBacCer77638_0825. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 26 30 HMP-PP binding (By similarity). FT REGION 125 127 THZ-P binding (By similarity). FT REGION 177 178 THZ-P binding (By similarity). FT METAL 62 62 Magnesium (By similarity). FT METAL 81 81 Magnesium (By similarity). FT BINDING 61 61 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 201 AA; 21453 MW; F8F984CE6C96F5D5 CRC64; MGSNNCTKDP LQVLREALEG GITIFQFREK GEGALTEEKR ICFAKELQAI CKEYGVPFIV NDDVELALEL DADGVHVGQD DEGITSVREK MGDKIVGVST HTIEEARWAI ENGADYLGVG PIFPTSTKKD TKAVQGTKGL AHFREQGITI PIVGIGGISI ENTASVIEAG ADGVSVISAI SLAESAYEST KRLVEEVSNS L // ID C2RZ93_BACCE Unreviewed; 194 AA. AC C2RZ93; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0013_6600; OS Bacillus cereus BDRD-ST26. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526975; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-ST26; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMC01000023; EEL02117.1; -; Genomic_DNA. DR ProteinModelPortal; C2RZ93; -. DR EnsemblBacteria; EEL02117; EEL02117; bcere0013_6600. DR PATRIC; 24916579; VBIBacCer77638_1534. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21417 MW; 287528BDDC5220C3 CRC64; MSFEELVNVA MQIESEIDYL HIREREKSTK ELYEGVESLL KKGFPASKIV INDRIDIAIL LNIPRVQLGY RSADVRSVKE KFSYLHVGYS VHSLEEAIDA FKNGADSLVY GHVFPTDCKK GVPARGLEEI SDIARCLSIP ITAIGGITPE NTGDVLTNGV SGIAVMSGII SSSNPYSKAK SYKESIRKWA EKHV // ID C2SEV6_BACCE Unreviewed; 214 AA. AC C2SEV6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0014_3440; OS Bacillus cereus BDRD-ST196. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526976; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-ST196; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMD01000017; EEL08054.1; -; Genomic_DNA. DR ProteinModelPortal; C2SEV6; -. DR EnsemblBacteria; EEL08054; EEL08054; bcere0014_3440. DR PATRIC; 24892814; VBIBacCer6084_2220. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23108 MW; E1B80F89C48AE5E2 CRC64; MDEMSRLLPV YFIMGSNNCT KEPLQVLRDA LEGGITIFQL REKGEGALTG EKRIDFAKEL QALCKEYGVP FIVNDDVELA LELDADGVHV GQDDEGITSV REKMGDKIVG VSTHTIEEAR WAIENGADYL GVGPIFPTST KKDTKAVQGT EGLKYFREQE ITIPIVGIGG ITIENTASVI EAGADGVSVI SAISLAESAY EGTKKLVEEV NKSL // ID C2SFN9_BACCE Unreviewed; 194 AA. AC C2SFN9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0014_6320; OS Bacillus cereus BDRD-ST196. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526976; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-ST196; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMD01000040; EEL07693.1; -; Genomic_DNA. DR ProteinModelPortal; C2SFN9; -. DR EnsemblBacteria; EEL07693; EEL07693; bcere0014_6320. DR PATRIC; 24893440; VBIBacCer6084_3002. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21276 MW; 1754EC6720DD9866 CRC64; MPFEELVNVA MQIESEIDYL HIREREKSTK ELYEGVESLL GKGFPASKIV INDRIDIAIL LNIPRVQLGY RSADVRLVKE KFSYLHVGYS VHSLDEAIVA FKNGADSLVY GHVFPTDCKK GVPARGLEEI AHMASCLSIP ITAIGGITPE NTGDVLANGV SGIAVMSGII SSSNPYSKAK SYKESIRKWA EKHV // ID C2SVP8_BACCE Unreviewed; 222 AA. AC C2SVP8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0015_3330; OS Bacillus cereus BDRD-Cer4. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526978; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-Cer4; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACME01000010; EEL13340.1; -; Genomic_DNA. DR ProteinModelPortal; C2SVP8; -. DR EnsemblBacteria; EEL13340; EEL13340; bcere0015_3330. DR PATRIC; 24881463; VBIBacCer94942_0059. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23975 MW; 91FDFC2801F28966 CRC64; MKEMARIEID KMSKLLQVYF IMGSNNCTRD PLAVLKEALD GGVTIFQFRE KGEGSLIGED RVRFAKELQT LCNEYSVPFI VNDDVELAIE LDADGVHVGQ DDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TRKLAEEVKR SL // ID C2SWH8_BACCE Unreviewed; 208 AA. AC C2SWH8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0015_6160; OS Bacillus cereus BDRD-Cer4. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526978; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-Cer4; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACME01000017; EEL12968.1; -; Genomic_DNA. DR ProteinModelPortal; C2SWH8; -. DR EnsemblBacteria; EEL12968; EEL12968; bcere0015_6160. DR PATRIC; 24882091; VBIBacCer94942_0484. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 23036 MW; 316214A22E470F4E CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLMEGFPA SKIVINDRID IAILLNIPRV QLGYRSTDVK SVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEISDIARC LSIPITAIGG ITPENTVDVL TNGVSGIAVM SGIVSSSNPY SKAKSYKESI RKWAEKHV // ID C2TB40_BACCE Unreviewed; 219 AA. AC C2TB40; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0016_3530; OS Bacillus cereus 95/8201. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526979; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=95/8201; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMF01000010; EEL19085.1; -; Genomic_DNA. DR ProteinModelPortal; C2TB40; -. DR EnsemblBacteria; EEL19085; EEL19085; bcere0016_3530. DR PATRIC; 24761341; VBIBacCer42905_0022. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23509 MW; D33A0EEF3D86CD9C CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAINL AESAYESTKK LVEEVSRSL // ID C2TS59_BACCE Unreviewed; 219 AA. AC C2TS59; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0017_3480; OS Bacillus cereus Rock1-3. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526981; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock1-3; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMG01000012; EEL24917.1; -; Genomic_DNA. DR ProteinModelPortal; C2TS59; -. DR EnsemblBacteria; EEL24917; EEL24917; bcere0017_3480. DR PATRIC; 25024703; VBIBacCer118415_0208. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23464 MW; 53FF6E42627A8867 CRC64; MMRIETKKMS NLLQVYFIMG SNNCMKDPLA ILKEALDGGV TLFQFREKGE GTLTGEDRVR FAKKLQALCK EYGVPFIVND DVELAVELDA DGVHVGQDDE GIASVREKMG DKIIGVSTHT IEEAKWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITVPI VGIGGITIEN TAAVIEAGAD GVSVISAISL ADSAYESTKR LAGEVNKCL // ID C2U8R1_BACCE Unreviewed; 222 AA. AC C2U8R1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0018_3340; OS Bacillus cereus Rock1-15. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526982; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock1-15; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMH01000013; EEL30660.1; -; Genomic_DNA. DR ProteinModelPortal; C2U8R1; -. DR EnsemblBacteria; EEL30660; EEL30660; bcere0018_3340. DR PATRIC; 25012573; VBIBacCer37058_0811. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23975 MW; 91FDFC2801F28966 CRC64; MKEMARIEID KMSKLLQVYF IMGSNNCTRD PLAVLKEALD GGVTIFQFRE KGEGSLIGED RVRFAKELQT LCNEYSVPFI VNDDVELAIE LDADGVHVGQ DDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TRKLAEEVKR SL // ID C2U9Z6_BACCE Unreviewed; 208 AA. AC C2U9Z6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0018_6230; OS Bacillus cereus Rock1-15. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526982; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock1-15; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMH01000022; EEL30191.1; -; Genomic_DNA. DR ProteinModelPortal; C2U9Z6; -. DR EnsemblBacteria; EEL30191; EEL30191; bcere0018_6230. DR PATRIC; 25013293; VBIBacCer37058_1881. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 23036 MW; 316214A22E470F4E CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLMEGFPA SKIVINDRID IAILLNIPRV QLGYRSTDVK SVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEISDIARC LSIPITAIGG ITPENTVDVL TNGVSGIAVM SGIVSSSNPY SKAKSYKESI RKWAEKHV // ID C2UQB4_BACCE Unreviewed; 195 AA. AC C2UQB4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0019_3770; OS Bacillus cereus Rock3-28. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526983; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-28; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMI01000055; EEL36429.1; -; Genomic_DNA. DR ProteinModelPortal; C2UQB4; -. DR EnsemblBacteria; EEL36429; EEL36429; bcere0019_3770. DR PATRIC; 25036610; VBIBacCer113327_4930. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 119 121 THZ-P binding (By similarity). FT REGION 171 172 THZ-P binding (By similarity). FT METAL 56 56 Magnesium (By similarity). FT METAL 75 75 Magnesium (By similarity). FT BINDING 55 55 HMP-PP (By similarity). FT BINDING 93 93 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 195 AA; 20659 MW; 73A3C63C70B19745 CRC64; MKDPLAILKE ALDGGVTLFQ FREKGEGTLT GEDRVRFAKK LQALCKEYGV PFIVNDDVEL AVELDADGVH VGQDDEGITS VREKMGDKII GVSTHTIEEA KWAIENGADY LGVGPIFPTS TKKDTKAVQG TKGLAHFREQ GITVPIVGIG GITIENTAAV IEAGADGVSV ISAISLADSA YESTKRLAGE VNKCL // ID C2UR36_BACCE Unreviewed; 194 AA. AC C2UR36; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0019_6660; OS Bacillus cereus Rock3-28. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526983; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-28; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMI01000084; EEL36065.1; -; Genomic_DNA. DR ProteinModelPortal; C2UR36; -. DR EnsemblBacteria; EEL36065; EEL36065; bcere0019_6660. DR PATRIC; 25037414; VBIBacCer113327_5700. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21396 MW; E6A252D699098DB3 CRC64; MPFEELVNVA MQIESEIDYL HIREREKSTK ELYEGVESLL KKGFPASKLV INDRIDIAIL LNIPRVQLGY RSADVRLVKE KFSYLHVGYS VHSLEEAIVA FKNGADSLVY GHVFPTDCKK GVPARGLEEI SDIASCLSIP ITAIGGITPE NTVDVLTNGV SGIAVMSGIV SSSNPYSKAK SYKESIRKWA EKHV // ID C2V6N8_BACCE Unreviewed; 219 AA. AC C2V6N8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0020_3460; OS Bacillus cereus Rock3-29. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526984; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-29; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMJ01000013; EEL42300.1; -; Genomic_DNA. DR ProteinModelPortal; C2V6N8; -. DR EnsemblBacteria; EEL42300; EEL42300; bcere0020_3460. DR PATRIC; 25048574; VBIBacCer100535_0264. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23494 MW; 53FF7B426DD03867 CRC64; MMRIETKKMS NLLQVYFIMG SNNCMKDPLA ILKEALDGGV TLFQFREKGE GTLTGEDRVR FAKKLQALCK EYGVPFIVND DVELAVELDA DGVHVGQDDE GITSVREKMG DKIIGVSTHT IEEAKWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITVPI VGIGGITIEN TAAVIEAGAD GVSVISAISL ADSAYESTKR LAGEVNKCL // ID C2VNE9_BACCE Unreviewed; 219 AA. AC C2VNE9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0021_3410; OS Bacillus cereus Rock3-42. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526985; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-42; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMK01000017; EEL47496.1; -; Genomic_DNA. DR ProteinModelPortal; C2VNE9; -. DR EnsemblBacteria; EEL47496; EEL47496; bcere0021_3410. DR PATRIC; 25060905; VBIBacCer34651_2123. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23512 MW; 399B055F394DFD90 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GTLTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID C2W3J4_BACCE Unreviewed; 218 AA. AC C2W3J4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0022_3390; OS Bacillus cereus Rock3-44. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526986; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-44; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACML01000039; EEL52295.1; -; Genomic_DNA. DR ProteinModelPortal; C2W3J4; -. DR EnsemblBacteria; EEL52295; EEL52295; bcere0022_3390. DR PATRIC; 25072180; VBIBacCer125783_3571. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23541 MW; 5B330EDA2735CEFC CRC64; MRGMARIETE QMSKLLQVYF IMGSNNCKRD PLQVMKEALD GGITLFQFRE KGEGALTREE RVRFAKQLQA LCKEYDVPFI VNDDVELAIE LDADGVHVGQ DDEGITSVRE KMGDKIVGVS AHTIEEARFA IANGADYLGV GPIFPTSTKK DTKAVQGTKG LRHFREAGIT VPIVGIGGIT VENAASVIEA GADGVSVISA ISLADSPYES TKKMAGLY // ID C2W4A9_BACCE Unreviewed; 194 AA. AC C2W4A9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0022_6100; OS Bacillus cereus Rock3-44. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526986; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-44; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACML01000063; EEL52036.1; -; Genomic_DNA. DR ProteinModelPortal; C2W4A9; -. DR EnsemblBacteria; EEL52036; EEL52036; bcere0022_6100. DR PATRIC; 25072756; VBIBacCer125783_3935. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21721 MW; 282AB2BBFB7D2887 CRC64; MTFEELANVA MQIESEIDYL HIREREKSTK ELYEGVESLL KRGFPASKLV MNDRIDVAIL LHIPRVQLGY RSADVKSVKE KFSYLHVGYS VHSLEEAIIA FKNGADSLVY GHVFSTDCKK GVPARGLEEI SDIARRLTIP ITAIGGITPQ NTAEVLKSGV SGIAVMSGIV SDRNPYEKAR LYKETIRKWA ENHE // ID C2WH87_BACCE Unreviewed; 222 AA. AC C2WH87; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0023_4320; OS Bacillus cereus Rock4-2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526987; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock4-2; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMM01000057; EEL58026.1; -; Genomic_DNA. DR ProteinModelPortal; C2WH87; -. DR EnsemblBacteria; EEL58026; EEL58026; bcere0023_4320. DR PATRIC; 25094307; VBIBacCer64089_5522. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23989 MW; DFAB3EA554A7B22C CRC64; MKEMARIEID KMSKLLQVYF IMGSNNCTRD PLAVLKEALD GGVTLFQFRE KGEGSLIGED RVRFAKELQT LCKEYSVPFI VNDDVELAIE LDADGVHVGQ DDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TKKLVEEVKR SL // ID C2WI60_BACCE Unreviewed; 194 AA. AC C2WI60; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0023_7280; OS Bacillus cereus Rock4-2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526987; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock4-2; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMM01000079; EEL57656.1; -; Genomic_DNA. DR ProteinModelPortal; C2WI60; -. DR EnsemblBacteria; EEL57656; EEL57656; bcere0023_7280. DR PATRIC; 25094917; VBIBacCer64089_5841. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21431 MW; AD9381C0B3663FB5 CRC64; MPFEELVNVA MQIESEIDYL HIREREKSTK ELYEGVESLL MEGFPASKIV INDRIDIAIL LNIPRVQLGY RSTDVKSVKE KFSYLHVGYS VHSLDEAIVA FKNGADSLVY GHVFPTDCKK GVPARGLEEI SDIARCLSIP ITAIGGITPE NTVDVLTNGV SGIAVMSGIV SSSNPYSKAK SYKESIRKWA EKHV // ID C2X6L9_BACCE Unreviewed; 222 AA. AC C2X6L9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0025_3410; OS Bacillus cereus F65185. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526989; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F65185; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMO01000012; EEL66807.1; -; Genomic_DNA. DR ProteinModelPortal; C2X6L9; -. DR EnsemblBacteria; EEL66807; EEL66807; bcere0025_3410. DR PATRIC; 24940146; VBIBacCer123234_1408. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 24017 MW; 7AA8FC2D51A46F9A CRC64; MKEMARIEID KMSKLLQVYF IMGSNNCTRD PLAVLKEALD GGVTIFQFRE KGEGSLIGED RVRFAKELQT LCKEYSVPFI VNDDVELAIE LDADGVHVGQ DDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TRKLVEEVKR SL // ID C2X7F1_BACCE Unreviewed; 208 AA. AC C2X7F1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0025_6270; OS Bacillus cereus F65185. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526989; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F65185; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMO01000018; EEL66429.1; -; Genomic_DNA. DR ProteinModelPortal; C2X7F1; -. DR EnsemblBacteria; EEL66429; EEL66429; bcere0025_6270. DR PATRIC; 24940786; VBIBacCer123234_2280. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 23003 MW; 110332F7BCD4DD53 CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIREHE KSTKELYEGV ESLLMEGFPA SKIVINDRID IAILLNIPRV QLGYRSTDVK SVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEISDIARC LSIPITAIGG ITPENTVDVL TNGVSGIAVM SGIVSSSNPY SNAKSYKESI RKWAEKHV // ID C2XNV1_BACCE Unreviewed; 219 AA. AC C2XNV1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0026_3450; OS Bacillus cereus AH603. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526990; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH603; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMP01000013; EEL72663.1; -; Genomic_DNA. DR ProteinModelPortal; C2XNV1; -. DR EnsemblBacteria; EEL72663; EEL72663; bcere0026_3450. DR PATRIC; 24822371; VBIBacCer18372_1103. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23578 MW; 0FE908A2027D4065 CRC64; MPCITKAEMS RLLPVYFIMG SNNCTKEPLQ VLRDALEGGI TIFQLREKGE GALTGEKRID FAKELQALCK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVRKKMG DKIIGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTEGLKY FREQEITIPI VGIGGITIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEGVNKSL // ID C2XPL8_BACCE Unreviewed; 208 AA. AC C2XPL8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0026_6210; OS Bacillus cereus AH603. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526990; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH603; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMP01000030; EEL72377.1; -; Genomic_DNA. DR ProteinModelPortal; C2XPL8; -. DR EnsemblBacteria; EEL72377; EEL72377; bcere0026_6210. DR PATRIC; 24823003; VBIBacCer18372_2619. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 23040 MW; 5EBB66B0F6E884B5 CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLKKSFPP SKLVINDRID IAILLNIPRV QLGYRSADVR LVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEITHMASC LSIPITAIGG ITPENTGDVL ANGVSGIAVM SGIISSSNPY SKAKSYKESI RKWAEKHV // ID C2Y5G4_BACCE Unreviewed; 222 AA. AC C2Y5G4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0027_3580; OS Bacillus cereus AH676. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526991; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH676; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMQ01000015; EEL78284.1; -; Genomic_DNA. DR EnsemblBacteria; EEL78284; EEL78284; bcere0027_3580. DR PATRIC; 24846263; VBIBacCer88826_0860. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23989 MW; 61A8FC2D51A46F85 CRC64; MKEMARIEID KMSKLLQVYF IMGSNNCTRD PLAVLKEALD GGVTIFQFRE KGEGSLIGED RVRFAKELQT LCKEYSVPFI VNDDVELAIE LDADGVHVGQ DDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TRKLAEEVKR SL // ID C2Y6A6_BACCE Unreviewed; 208 AA. AC C2Y6A6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0027_6540; OS Bacillus cereus AH676. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526991; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH676; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMQ01000026; EEL77900.1; -; Genomic_DNA. DR ProteinModelPortal; C2Y6A6; -. DR EnsemblBacteria; EEL77900; EEL77900; bcere0027_6540. DR PATRIC; 24846934; VBIBacCer88826_3521. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 23036 MW; 316214A22E470F4E CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLMEGFPA SKIVINDRID IAILLNIPRV QLGYRSTDVK SVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEISDIARC LSIPITAIGG ITPENTVDVL TNGVSGIAVM SGIVSSSNPY SKAKSYKESI RKWAEKHV // ID C2YLG3_BACCE Unreviewed; 219 AA. AC C2YLG3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0028_3510; OS Bacillus cereus AH1271. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526992; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1271; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMR01000019; EEL83937.1; -; Genomic_DNA. DR ProteinModelPortal; C2YLG3; -. DR EnsemblBacteria; EEL83937; EEL83937; bcere0028_3510. DR PATRIC; 24785897; VBIBacCer17091_2586. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23571 MW; 18A180337F05A935 CRC64; MSRISKAEMS RLLSVYFIMG SNNCTKDPLQ VLRDALEGGI TIFQFREKGE DALTGEKRIY FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEANWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGITIEN TASVIEAGAD GVSIISAISL AESAYESTKK LVEEVSKSL // ID C2Z2K4_BACCE Unreviewed; 219 AA. AC C2Z2K4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0029_3330; OS Bacillus cereus AH1272. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526993; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1272; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMS01000029; EEL89777.1; -; Genomic_DNA. DR ProteinModelPortal; C2Z2K4; -. DR EnsemblBacteria; EEL89777; EEL89777; bcere0029_3330. DR PATRIC; 24797776; VBIBacCer63391_3554. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23579 MW; FBC0F60B806A4D69 CRC64; MPRITKAEMS RLLSVYFIMG SNNCTKEPLQ VLRDALEGGI TIFQFREKGE GALTGEKRIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGIMIPI VGIGGIMIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSKSL // ID C2Z3E9_BACCE Unreviewed; 194 AA. AC C2Z3E9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0029_6360; OS Bacillus cereus AH1272. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526993; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1272; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMS01000048; EEL89474.1; -; Genomic_DNA. DR ProteinModelPortal; C2Z3E9; -. DR EnsemblBacteria; EEL89474; EEL89474; bcere0029_6360. DR PATRIC; 24798458; VBIBacCer63391_4510. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21383 MW; B04F03984D68BF2D CRC64; MPFEELVNVA MQIESEIDYL HIREREKSTK ELHEGVESLL KKGFPASKIV INDRIDIAIL LNIPRVQLGY RSADVRLVKE KFSYLHVGYS VHSLDEAIVA FKNGADSLVY GHVFPTACKK DVPARGLEEI ADMARCLSIP ITAIGGITPE NTGDVLANGV SGIAVMSGII SSSNPYSKAK SYKESIRKWA EKHV // ID C2ZJ75_BACCE Unreviewed; 219 AA. AC C2ZJ75; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcere0030_3470; OS Bacillus cereus AH1273. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526994; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1273; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMT01000028; EEL95540.1; -; Genomic_DNA. DR ProteinModelPortal; C2ZJ75; -. DR EnsemblBacteria; EEL95540; EEL95540; bcere0030_3470. DR PATRIC; 24810097; VBIBacCer6853_3652. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23579 MW; FBC0F60B806A4D69 CRC64; MPRITKAEMS RLLSVYFIMG SNNCTKEPLQ VLRDALEGGI TIFQFREKGE GALTGEKRIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGIMIPI VGIGGIMIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSKSL // ID C2ZJZ8_BACCE Unreviewed; 194 AA. AC C2ZJZ8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bcere0030_6380; OS Bacillus cereus AH1273. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526994; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1273; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMT01000053; EEL95255.1; -; Genomic_DNA. DR ProteinModelPortal; C2ZJZ8; -. DR EnsemblBacteria; EEL95255; EEL95255; bcere0030_6380. DR PATRIC; 24810707; VBIBacCer6853_4769. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21383 MW; B04F03984D68BF2D CRC64; MPFEELVNVA MQIESEIDYL HIREREKSTK ELHEGVESLL KKGFPASKIV INDRIDIAIL LNIPRVQLGY RSADVRLVKE KFSYLHVGYS VHSLDEAIVA FKNGADSLVY GHVFPTACKK DVPARGLEEI ADMARCLSIP ITAIGGITPE NTGDVLANGV SGIAVMSGII SSSNPYSKAK SYKESIRKWA EKHV // ID C3A0S4_BACMY Unreviewed; 214 AA. AC C3A0S4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bmyco0001_3320; OS Bacillus mycoides DSM 2048. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526997; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2048; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMU01000010; EEM01286.1; -; Genomic_DNA. DR ProteinModelPortal; C3A0S4; -. DR EnsemblBacteria; EEM01286; EEM01286; bmyco0001_3320. DR PATRIC; 25155964; VBIBacMyc112645_0036. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23108 MW; E1B80F89C48AE5E2 CRC64; MDEMSRLLPV YFIMGSNNCT KEPLQVLRDA LEGGITIFQL REKGEGALTG EKRIDFAKEL QALCKEYGVP FIVNDDVELA LELDADGVHV GQDDEGITSV REKMGDKIVG VSTHTIEEAR WAIENGADYL GVGPIFPTST KKDTKAVQGT EGLKYFREQE ITIPIVGIGG ITIENTASVI EAGADGVSVI SAISLAESAY EGTKKLVEEV NKSL // ID C3A1L1_BACMY Unreviewed; 194 AA. AC C3A1L1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bmyco0001_6240; OS Bacillus mycoides DSM 2048. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526997; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2048; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMU01000020; EEM00825.1; -; Genomic_DNA. DR ProteinModelPortal; C3A1L1; -. DR EnsemblBacteria; EEM00825; EEM00825; bmyco0001_6240. DR PATRIC; 25156732; VBIBacMyc112645_0999. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21276 MW; 1754EC6720DD9866 CRC64; MPFEELVNVA MQIESEIDYL HIREREKSTK ELYEGVESLL GKGFPASKIV INDRIDIAIL LNIPRVQLGY RSADVRLVKE KFSYLHVGYS VHSLDEAIVA FKNGADSLVY GHVFPTDCKK GVPARGLEEI AHMASCLSIP ITAIGGITPE NTGDVLANGV SGIAVMSGII SSSNPYSKAK SYKESIRKWA EKHV // ID C3AHR3_BACMY Unreviewed; 194 AA. AC C3AHR3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 25. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bmyco0002_6370; OS Bacillus mycoides Rock1-4. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526998; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock1-4; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMV01000048; EEM06736.1; -; Genomic_DNA. DR ProteinModelPortal; C3AHR3; -. DR EnsemblBacteria; EEM06736; EEM06736; bmyco0002_6370. DR PATRIC; 25168381; VBIBacMyc56145_4728. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21528 MW; 50BD8FFDCC3F9759 CRC64; MAFEELANVA MKIESEIDYL HIREREKSTK ELYEGVEGLL KGGFPASKLV INDRIDIAIL LNIPRVQLGY RSADVRSVKE KFSYLHVGYS VHSLEEAIVA FKNGADSLVY GHVFPTSCKK DVPARGLEEI SDIARRLTIP ITAIGGITPK NIGEVLRAGV SGIAVMSGIV SDSNPYKQAR LYKETIRKWA KNHE // ID C3AX85_BACMY Unreviewed; 70 AA. AC C3AX85; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=bmyco0002_59490; OS Bacillus mycoides Rock1-4. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526998; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock1-4; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMV01000548; EEM01746.1; -; Genomic_DNA. DR EnsemblBacteria; EEM01746; EEM01746; bmyco0002_59490. DR PATRIC; 25178701; VBIBacMyc56145_5388. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 70 AA; 7272 MW; D2C97DDA2E4AA65D CRC64; MQGTKGLRYF REEGITIPIV GIGGITVENA ASVIEAGADG VSVISTISLA DSPYESTSLL TGIFNDKVKL // ID C3AYS4_BACMY Unreviewed; 224 AA. AC C3AYS4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bmyco0003_3420; OS Bacillus mycoides Rock3-17. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526999; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-17; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMW01000012; EEM12873.1; -; Genomic_DNA. DR ProteinModelPortal; C3AYS4; -. DR EnsemblBacteria; EEM12873; EEM12873; bmyco0003_3420. DR PATRIC; 25179888; VBIBacMyc8660_0763. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24256 MW; 39C3261923FC6F0C CRC64; MREMARINQQ QMSKLLQVYF IMGSNNCQKD PLRVMKEALD GGVTLFQFRE KGEGALTGKE RVHFAKQLQA LCKEYNVPFI VNDDVDLAIE LDADGIHVGQ DDEGITSVRE KMGDKIVGVS AHTIEEARFA IANGADYLGV GPIFPTSTKK DTKAVQGTKG LRYFREEGIT IPIVGIGGIT VENAASVIEA GADGVSVIST ISLADSPYES TSLLTGIFND KVKL // ID C3AZM4_BACMY Unreviewed; 194 AA. AC C3AZM4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bmyco0003_6440; OS Bacillus mycoides Rock3-17. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526999; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-17; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMW01000021; EEM12512.1; -; Genomic_DNA. DR ProteinModelPortal; C3AZM4; -. DR EnsemblBacteria; EEM12512; EEM12512; bmyco0003_6440. DR PATRIC; 25180550; VBIBacMyc8660_1439. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21528 MW; 50BD8FFDCC3F9759 CRC64; MAFEELANVA MKIESEIDYL HIREREKSTK ELYEGVEGLL KGGFPASKLV INDRIDIAIL LNIPRVQLGY RSADVRSVKE KFSYLHVGYS VHSLEEAIVA FKNGADSLVY GHVFPTSCKK DVPARGLEEI SDIARRLTIP ITAIGGITPK NIGEVLRAGV SGIAVMSGIV SDSNPYKQAR LYKETIRKWA KNHE // ID C3BFH2_9BACI Unreviewed; 224 AA. AC C3BFH2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bpmyx0001_3210; OS Bacillus pseudomycoides DSM 12442. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=527000; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 12442; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMX01000011; EEM18666.1; -; Genomic_DNA. DR ProteinModelPortal; C3BFH2; -. DR EnsemblBacteria; EEM18666; EEM18666; bpmyx0001_3210. DR PATRIC; 25191835; VBIBacPse118422_0215. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24187 MW; D823DA619127DFD1 CRC64; MREMARINQQ QMSKLLQVYF IMGSNNCQKD PLRVMKEALD GGVTLFQFRE KGEGALTGKE RVHFAKQLQA LCKEYNVPFI VNDDVDLAIE LDADGIHVGQ DDEGITFVRE KMGDKIVGVS AHTIEEARFA IANGADYLGV GPIFPTSTKK DTKAVQGTKG LRHFREAGIT VPIVGIGGIT VKNAASVIEA GADGVSVISA ISLADSPYES TSLLTGIFND KVKL // ID C3BG57_9BACI Unreviewed; 194 AA. AC C3BG57; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bpmyx0001_6260; OS Bacillus pseudomycoides DSM 12442. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=527000; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 12442; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMX01000017; EEM18380.1; -; Genomic_DNA. DR ProteinModelPortal; C3BG57; -. DR EnsemblBacteria; EEM18380; EEM18380; bpmyx0001_6260. DR PATRIC; 25192295; VBIBacPse118422_0585. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21518 MW; FC876118CEF59C8F CRC64; MAFEELANVA MQIESEIDYL HIREREKSTK ELYEGVEGLL KGGFPASKLV INDRIDIAIL LNISRVQLGY RSADVRSVKE KFSYLHVGYS VHSLEEAIVA FKNGADSLVY GHVFPTSCKK DVPARGLEEI SDIARRLTIP ITAIGGITPK NIGEVLRAGV SGIAVMSGIV SDSNPYKQAR LYKETIRKWA KNHE // ID C3BX25_BACTU Unreviewed; 219 AA. AC C3BX25; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0001_3530; OS Bacillus thuringiensis serovar tochigiensis BGSC 4Y1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527024; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4Y1; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMY01000012; EEM24477.1; -; Genomic_DNA. DR ProteinModelPortal; C3BX25; -. DR EnsemblBacteria; EEM24477; EEM24477; bthur0001_3530. DR PATRIC; 31015631; VBIBacThu51894_0785. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23466 MW; 098B661E3CCA694B CRC64; MSRISKAEMS RLLSVYFIMG SNNCTKDPLQ VLRDALEGGI TIFQFREKGE GALTGEKRIY FAKELQAICK GYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG NKIIGVSTHT IEEALWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GISVISAISL AESAYESTKK LVEEVSKNL // ID C3BXX5_BACTU Unreviewed; 194 AA. AC C3BXX5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bthur0001_6440; OS Bacillus thuringiensis serovar tochigiensis BGSC 4Y1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527024; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4Y1; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMY01000026; EEM24127.1; -; Genomic_DNA. DR ProteinModelPortal; C3BXX5; -. DR EnsemblBacteria; EEM24127; EEM24127; bthur0001_6440. DR PATRIC; 31016268; VBIBacThu51894_1878. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21392 MW; 59B528A4C5577CCE CRC64; MSFEELVNVA MQIESEIDYL HIREREKSTK ELYEGVESLL KKGFPASKIV INDRIDIAIL LNIPRVQLGY RSADVRSVKE KFSYLHVGYS VHSLEEAIDA FKNGADSLVY GHVFPTDCKK GVPARGLEEI SDIAKCLSIP ITAIGGITTE NTGDVLTNGV SGIAVMSGII SSSNPYSKAK SYKESIRKWA EKHV // ID C3CDF7_BACTU Unreviewed; 219 AA. AC C3CDF7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BTB_c04350, bthur0002_3410; OS Bacillus thuringiensis Bt407. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527021; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Bt407; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RX PubMed=23405326; RA Sheppard A.E., Poehlein A., Rosenstiel P., Liesegang H., RA Schulenburg H.; RT "Complete Genome Sequence of Bacillus thuringiensis Strain 407 Cry-."; RL Genome Announc. 1:E00158-12(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003889; AFV16172.1; -; Genomic_DNA. DR EMBL; ACMZ01000014; EEM30747.1; -; Genomic_DNA. DR RefSeq; YP_006925109.1; NC_018877.1. DR EnsemblBacteria; AFV16172; AFV16172; BTB_c04350. DR EnsemblBacteria; EEM30747; EEM30747; bthur0002_3410. DR GeneID; 13851399; -. DR KEGG; btg:BTB_c04350; -. DR PATRIC; 26089967; VBIBacThu117809_1668. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23594 MW; 7794A889CDD6A89F CRC64; MMRIETKKMS KLLQVYFIMG SNNCTRDPLA VLKEALDGGV TLFQFREKGE GSLIGGDRVR FAKELQTLCK EYSVPFIVND DVELAIELDA DGVHVGQDDE GITSVREKMG DKIIGVSAHT IEEARFAIEN GADYLGVGPI FTTSTKKDTK AVQGTKGLAY FREQGITVPI VGIGGITIEN TAAVIEAGAD GVSVISAISL AESAYESTRK LAEEVKRSL // ID C3CWF1_BACTU Unreviewed; 219 AA. AC C3CWF1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0003_3430; OS Bacillus thuringiensis serovar thuringiensis str. T01001. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527025; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T01001; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNA01000012; EEM37068.1; -; Genomic_DNA. DR ProteinModelPortal; C3CWF1; -. DR EnsemblBacteria; EEM37068; EEM37068; bthur0003_3430. DR PATRIC; 28966330; VBIBacThu29322_0937. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23594 MW; 7794A889CDD6A89F CRC64; MMRIETKKMS KLLQVYFIMG SNNCTRDPLA VLKEALDGGV TLFQFREKGE GSLIGGDRVR FAKELQTLCK EYSVPFIVND DVELAIELDA DGVHVGQDDE GITSVREKMG DKIIGVSAHT IEEARFAIEN GADYLGVGPI FTTSTKKDTK AVQGTKGLAY FREQGITVPI VGIGGITIEN TAAVIEAGAD GVSVISAISL AESAYESTRK LAEEVKRSL // ID C3DEJ8_BACTS Unreviewed; 222 AA. AC C3DEJ8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0004_3610; OS Bacillus thuringiensis serovar sotto str. T04001. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527026; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T04001; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNB01000015; EEM43625.1; -; Genomic_DNA. DR ProteinModelPortal; C3DEJ8; -. DR EnsemblBacteria; EEM43625; EEM43625; bthur0004_3610. DR PATRIC; 28952479; VBIBacThu7424_1922. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23955 MW; 180CFC6889BF439A CRC64; MKHTMRIETK KMSKLLQVYF IMGSNNCTRD PLAVLKEALD GGVTLFQFRE KGEGSLIGGD RVRFAKELQT LCKEYSVPFI VNDDVELAIE LDADGVHVGQ NDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TRKLAEEVKR SL // ID C3DYE2_BACTU Unreviewed; 222 AA. AC C3DYE2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0005_3740; OS Bacillus thuringiensis serovar pakistani str. T13001. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527027; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T13001; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNC01000014; EEM49709.1; -; Genomic_DNA. DR ProteinModelPortal; C3DYE2; -. DR EnsemblBacteria; EEM49709; EEM49709; bthur0005_3740. DR PATRIC; 28914435; VBIBacThu54181_1103. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 24003 MW; 9179FC5D87F0F1BD CRC64; MKEMARIEID KMSKLLQLYF IMGSNNCTRD PLAVLKEALD GGVTIFQFRE KGEGSLIGED RVRFAKELQT LCKEYSVPFI VNDDVELAIE LDADGVHVGQ DDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TRKLAEEVKR SL // ID C3DZB5_BACTU Unreviewed; 208 AA. AC C3DZB5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bthur0005_6750; OS Bacillus thuringiensis serovar pakistani str. T13001. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527027; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T13001; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNC01000031; EEM49326.1; -; Genomic_DNA. DR ProteinModelPortal; C3DZB5; -. DR EnsemblBacteria; EEM49326; EEM49326; bthur0005_6750. DR PATRIC; 28915263; VBIBacThu54181_3444. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 23036 MW; 316214A22E470F4E CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLMEGFPA SKIVINDRID IAILLNIPRV QLGYRSTDVK SVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEISDIARC LSIPITAIGG ITPENTVDVL TNGVSGIAVM SGIVSSSNPY SKAKSYKESI RKWAEKHV // ID C3EFK5_BACTK Unreviewed; 222 AA. AC C3EFK5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0006_3590; OS Bacillus thuringiensis serovar kurstaki str. T03a001. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527023; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T03a001; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACND01000016; EEM55153.1; -; Genomic_DNA. DR ProteinModelPortal; C3EFK5; -. DR EnsemblBacteria; EEM55153; EEM55153; bthur0006_3590. DR PATRIC; 28889416; VBIBacThu4961_2105. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 24017 MW; DFAB219854A7B22C CRC64; MKEMARIEID KMSKLLQVYF IMGSNNCTRD PLAVLKEALD GGVTLFQFRE KGEGSLIGED RVRFAKELQT LCKEYSVPFI VNDDVELAIE LDADGVHVGQ DDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TRKLVEEVKR SL // ID C3EGE6_BACTK Unreviewed; 194 AA. AC C3EGE6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 25. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bthur0006_6510; OS Bacillus thuringiensis serovar kurstaki str. T03a001. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527023; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T03a001; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACND01000025; EEM54933.1; -; Genomic_DNA. DR ProteinModelPortal; C3EGE6; -. DR EnsemblBacteria; EEM54933; EEM54933; bthur0006_6510. DR PATRIC; 28889888; VBIBacThu4961_2555. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21430 MW; AD9381C0A3377AB1 CRC64; MPFEELVNVA MQIESEIDYL HIREREKSTK ELYEGVESLL MEGFPASKIV INDRIDIAIL LNIPRVQLGY RSTDVKSVKE KFSYLHVGYS VHSLDEAIVA FKNGADSLVY GHVFPTDCKK GVPARGLEEI SDIARCLSIP ITAIGGITPQ NTVDVLTNGV SGIAVMSGIV SSSNPYSKAK SYKESIRKWA EKHV // ID C3EWG2_BACTU Unreviewed; 219 AA. AC C3EWG2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0007_3570; OS Bacillus thuringiensis serovar monterrey BGSC 4AJ1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527022; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4AJ1; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNE01000010; EEM61812.1; -; Genomic_DNA. DR ProteinModelPortal; C3EWG2; -. DR EnsemblBacteria; EEM61812; EEM61812; bthur0007_3570. DR PATRIC; 28900708; VBIBacThu130558_0022. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23454 MW; D32C7F88285CFD9C CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSAISAISL AESAYESTKK LVEEVSRSL // ID C3FEY5_BACTB Unreviewed; 219 AA. AC C3FEY5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0008_3430; OS Bacillus thuringiensis serovar berliner ATCC 10792. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527031; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10792; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNF01000012; EEM68028.1; -; Genomic_DNA. DR ProteinModelPortal; C3FEY5; -. DR EnsemblBacteria; EEM68028; EEM68028; bthur0008_3430. DR PATRIC; 26142522; VBIBacThu124489_1020. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23594 MW; 7794A889CDD6A89F CRC64; MMRIETKKMS KLLQVYFIMG SNNCTRDPLA VLKEALDGGV TLFQFREKGE GSLIGGDRVR FAKELQTLCK EYSVPFIVND DVELAIELDA DGVHVGQDDE GITSVREKMG DKIIGVSAHT IEEARFAIEN GADYLGVGPI FTTSTKKDTK AVQGTKGLAY FREQGITVPI VGIGGITIEN TAAVIEAGAD GVSVISAISL AESAYESTRK LAEEVKRSL // ID C3FFV2_BACTB Unreviewed; 208 AA. AC C3FFV2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 25. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bthur0008_6670; OS Bacillus thuringiensis serovar berliner ATCC 10792. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527031; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10792; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNF01000025; EEM67626.1; -; Genomic_DNA. DR ProteinModelPortal; C3FFV2; -. DR EnsemblBacteria; EEM67626; EEM67626; bthur0008_6670. DR PATRIC; 26143243; VBIBacThu124489_2319. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 23007 MW; 316205A2233B6F4E CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLMEGFPA SKIVINDRID IAILLNIPRV QLGYRSTDVK SVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEISDIARC LSIPITAIGG ITPENAVDVL TNGVSGIAVM SGIVSSSDPY SKAKSYKESI RKWAEKHV // ID C3FXL7_BACTU Unreviewed; 219 AA. AC C3FXL7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0009_3620; OS Bacillus thuringiensis serovar andalousiensis BGSC 4AW1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527032; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4AW1; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNG01000016; EEM73594.1; -; Genomic_DNA. DR ProteinModelPortal; C3FXL7; -. DR EnsemblBacteria; EEM73594; EEM73594; bthur0009_3620. DR PATRIC; 26130712; VBIBacThu67491_1214. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23482 MW; D33A0EEF285CFD9C CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID C3GDP0_BACTU Unreviewed; 219 AA. AC C3GDP0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0010_3550; OS Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527029; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4BA1; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNH01000011; EEM79654.1; -; Genomic_DNA. DR ProteinModelPortal; C3GDP0; -. DR EnsemblBacteria; EEM79654; EEM79654; bthur0010_3550. DR PATRIC; 28927128; VBIBacThu130330_0234. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23482 MW; D33A0EEF285CFD9C CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID C3GVW9_BACTU Unreviewed; 218 AA. AC C3GVW9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0011_3320; OS Bacillus thuringiensis serovar huazhongensis BGSC 4BD1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527030; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4BD1; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNI01000012; EEM85682.1; -; Genomic_DNA. DR ProteinModelPortal; C3GVW9; -. DR EnsemblBacteria; EEM85682; EEM85682; bthur0011_3320. DR PATRIC; 26155563; VBIBacThu93808_0875. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23485 MW; 8CD74E0F9D16BCCE CRC64; MRIETKKMSK LLQVYFIMGS NNCAKDPLSV LKEALDGGVT LFQFREKGEG ALIGEERVRF AKELQALCKE YSVPFIVNDD VELAIELDAD GVHVGQDDEG ITSVREKMGD KIIGVSAHTI EEARFAIENG ADYLGVGPIF PTSTKKDTKA VQGTKGLAYF REQGITVPIV GIGGITIENT VAVIEAGADG VSVISAISLA ESAYESTRKL AEEVKRSL // ID C3HD69_BACTU Unreviewed; 219 AA. AC C3HD69; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0012_3660; OS Bacillus thuringiensis serovar pulsiensis BGSC 4CC1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527028; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4CC1; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNJ01000012; EEM91540.1; -; Genomic_DNA. DR ProteinModelPortal; C3HD69; -. DR EnsemblBacteria; EEM91540; EEM91540; bthur0012_3660. DR PATRIC; 28939909; VBIBacThu66700_0717. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23500 MW; EF108EAB2858BDDB CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAMCK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID C3HV42_BACTU Unreviewed; 222 AA. AC C3HV42; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0013_3430; OS Bacillus thuringiensis IBL 200. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527019; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IBL 200; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNK01000011; EEM98335.1; -; Genomic_DNA. DR ProteinModelPortal; C3HV42; -. DR EnsemblBacteria; EEM98335; EEM98335; bthur0013_3430. DR PATRIC; 26103052; VBIBacThu121489_0288. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23963 MW; 30A9EC2C51B81F99 CRC64; MKEMARIEID KMSKLLQVYF IMGSNNCTRD PLAVLKEALD GGVTIFQFRE KGEGSLIGED RVRFAKELQT LCKEYSVPFI VNDDVELAIE LDADGVHVGQ DDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADHLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TRKLAEEVKR SL // ID C3HW07_BACTU Unreviewed; 208 AA. AC C3HW07; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=bthur0013_6630; OS Bacillus thuringiensis IBL 200. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527019; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IBL 200; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNK01000021; EEM97813.1; -; Genomic_DNA. DR ProteinModelPortal; C3HW07; -. DR EnsemblBacteria; EEM97813; EEM97813; bthur0013_6630. DR PATRIC; 26103743; VBIBacThu121489_1421. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 23056 MW; F188E81D9DD51B88 CRC64; MNMKNELHVI SNGHMSFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV EGLLMEGFPA SKIVINDRID IAILLNIPRV QLGYRSTDVK SVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT ECKKGVPARG LEEIADISRC LSIPITAIGG ITPENTMDVL TNGVSGIAVM SGIISSSNPY SKAKSYKESI RKWAEKHV // ID C3IE52_BACTU Unreviewed; 222 AA. AC C3IE52; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bthur0014_3220; OS Bacillus thuringiensis IBL 4222. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527020; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IBL 4222; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNL01000013; EEN04923.1; -; Genomic_DNA. DR ProteinModelPortal; C3IE52; -. DR EnsemblBacteria; EEN04923; EEN04923; bthur0014_3220. DR PATRIC; 26116921; VBIBacThu2650_1068. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23955 MW; 180CFC6889BF439A CRC64; MKHTMRIETK KMSKLLQVYF IMGSNNCTRD PLAVLKEALD GGVTLFQFRE KGEGSLIGGD RVRFAKELQT LCKEYSVPFI VNDDVELAIE LDADGVHVGQ NDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TRKLAEEVKR SL // ID C3JCL4_9PORP Unreviewed; 658 AA. AC C3JCL4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=POREN0001_1629; OS Porphyromonas endodontalis ATCC 35406. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=553175; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35406; RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNN01000034; EEN82078.1; -; Genomic_DNA. DR ProteinModelPortal; C3JCL4; -. DR EnsemblBacteria; EEN82078; EEN82078; POREN0001_1629. DR PATRIC; 29514684; VBIPorEnd1195_1596. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 658 AA; 71962 MW; 62431FE338BCD941 CRC64; MLLAITPPNA TPKVVQHYNA LLGAGLSMLL LRLPDATQEQ YEDCIRAIEP RHRSKVILAD YFHLVPVAGL GGIHLKASRQ KEWKHWQEVA QTQRITASAH SLDELESLPF CPDLALLSPV FDSISKGGYH ANIDLDECRS RLPKLPFPVL ALGGITPDNY PLVCSYGFAG GATLGYLAEQ EDAMEEAFSR FARPEVLTIA GHDPSSGAGL TADVRTIERL GAYPLSITTA LTIQDEFEFV ACQSVDFIPA LRQLLKHHKP HAAKIGLVAS LQDVYTIADM LQEAGVRQIV WDPILQPSYG RDPLHADWTP DLLHKIFSYC SLITPNLPEA ELLFGTDWEH KLQQVADTFH VAILLKGGHS SNRDSSCDVL YQPHREAQSS RVPRTPYDKH GTGCALSAAI ATALAQGETL SEACRKGQWY IDALRRSGKT RLAILPPSGE RLKAEKLRRG KLQFITDSPD LEEILNQCRA ALQGGVRWIQ LRMKTASTEE RVIAARAIRQ EMQSYPSAIL IIDDDVEAAL RSDADGVHVG LDDLPPADVR RILGTDKIVG ATCNRIEDLA LRSLQGVDYV GIGPFRTTQT KKLLSPLLGE EGMAALVRFN HTLPQPIPLI AIGGITAGDF STLAGVGVQG IALSGIINHA TDPQAESSRL VQLSDQYF // ID C3JRA6_RHOER Unreviewed; 231 AA. AC C3JRA6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RHOER0001_4702; OS Rhodococcus erythropolis SK121. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=596309; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK121; RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNO01000072; EEN85942.1; -; Genomic_DNA. DR ProteinModelPortal; C3JRA6; -. DR EnsemblBacteria; EEN85942; EEN85942; RHOER0001_4702. DR PATRIC; 29999876; VBIRhoEry47619_4437. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 157 159 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 160 160 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 231 AA; 24375 MW; E5F9768681AB6BA2 CRC64; MHPTHPSNDI DRRERLAAAR LYLCTDARRE KGDLAQFAEA ALSGGVDIIQ LRDKGSAGER EFGPLEAKDE LVALGILATA ARRHGALLAV NDRADLAMAS GADILHLGQN DIPVPYARTV VGEDVVIGRS TSSRAQASLA AIEEGVDYFC TGPVWATPTK PNRSASGLEL VRSTADAAPP RPWFAIGGID EERLPELLDA GATRIVVVRA ITQASDPQAA AQRLAAAVAG R // ID C3JYU5_PSEFS Unreviewed; 314 AA. AC C3JYU5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 14-MAY-2014, entry version 45. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=PFLU_4931; OS Pseudomonas fluorescens (strain SBW25). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=216595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBW25; RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51; RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R., RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M., RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J., RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L., RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K., RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M., RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.; RT "Genomic and genetic analyses of diversity and plant interactions of RT Pseudomonas fluorescens."; RL Genome Biol. 10:R51.1-R51.16(2009). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM181176; CAY51848.1; -; Genomic_DNA. DR RefSeq; YP_002874437.1; NC_012660.1. DR ProteinModelPortal; C3JYU5; -. DR STRING; 216595.PFLU4931; -. DR EnsemblBacteria; CAY51848; CAY51848; PFLU_4931. DR GeneID; 7821715; -. DR KEGG; pfs:PFLU4931; -. DR PATRIC; 19903966; VBIPseFlu98510_5065. DR eggNOG; COG0494; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 34111 MW; 72D03324BB5FBFD2 CRC64; MKRVHVAAAV IRGVDGRILL ARRADTQHQG GLWEFPGGKV EADESVASAL SRELQEELGI QVTTARPLIK VQHDYPDKQV LLDVWEVSAF TGEPQGVEGQ PLEWVAPRDL INYEFPAANA PIVAAARLPA EYLITPDELE TPALLRGIQK AIAGGIKLVQ LRAPNGYDPK YRDLAVDAVG LCAGKAQLML KGPFEWLGDF PAAGWHMTAA QLRKYASKGR PLPKDRWLAA SCHNAEELAL AQMMDVDFVT LSPVQPTQTH PDAQPLGWAQ AAELIRGFSK PVFLLGGVGP AEREQAWEAG AQGVAGIRAF WPQT // ID C3KNU7_RHISN Unreviewed; 201 AA. AC C3KNU7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=NGR_b02900; OS Rhizobium sp. (strain NGR234). OG Plasmid sym pNGR234b. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NGR234; RX PubMed=14702322; DOI=10.1128/JB.186.2.535-542.2004; RA Streit W.R., Schmitz R.A., Perret X., Staehelin C., Deakin W.J., RA Raasch C., Liesegang H., Broughton W.J.; RT "An evolutionary hot spot: the pNGR234b replicon of Rhizobium sp. RT strain NGR234."; RL J. Bacteriol. 186:535-542(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NGR234; RX PubMed=19376903; DOI=10.1128/AEM.00515-09; RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A., RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roser A., RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A., RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.; RT "Rhizobium sp. strain NGR234 possesses a remarkable number of RT secretion systems."; RL Appl. Environ. Microbiol. 75:4035-4045(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000874; ACP21755.1; -; Genomic_DNA. DR RefSeq; YP_002822508.1; NC_012586.1. DR ProteinModelPortal; C3KNU7; -. DR STRING; 394.NGR_b02900; -. DR EnsemblBacteria; ACP21755; ACP21755; NGR_b02900. DR GeneID; 7789827; -. DR KEGG; rhi:NGR_b02900; -. DR PATRIC; 32302206; VBIRhiSp122450_0738. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SFRE394:GBYN-3987-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Plasmid; Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22419 MW; 07AC206F5EE5750C CRC64; MTLDPFYLIV DSARWIERLV PLGVKLVQLR IKERSDEDIR NQIRIAKSIC TAHRCQLIVN DFWRLAIEEG CDFVHLGQED LAEADLGAIR AAGLKLGLST HDEAELEAAL AAAPDYVALG PIYPTILKKM KWAPQGLARL SAWRERVHPL PLVAIGGLNP ERIDGVFAHG ADSAAVVTDI TLNADPEART REWIRKTEAW R // ID C3LFA9_BACAC Unreviewed; 206 AA. AC C3LFA9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=BAMEG_3830; OS Bacillus anthracis (strain CDC 684 / NRRL 3495). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=568206; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 684 / NRRL 3495; RA Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., RA Han C., Sutton G., Sims D.; RT "Genome sequence of Bacillus anthracis str. CDC 684."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001215; ACP15095.1; -; Genomic_DNA. DR RefSeq; YP_002816408.1; NC_012581.1. DR ProteinModelPortal; C3LFA9; -. DR STRING; 568206.BAMEG_3830; -. DR EnsemblBacteria; ACP15095; ACP15095; BAMEG_3830. DR GeneID; 7786586; -. DR KEGG; bah:BAMEG_3830; -. DR PATRIC; 18797478; VBIBacAnt127120_4113. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BANT568206:GHVT-3782-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID C3LPQ4_VIBCM Unreviewed; 440 AA. AC C3LPQ4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=VCM66_0062; OS Vibrio cholerae serotype O1 (strain M66-2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=579112; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M66-2; RX PubMed=19115014; DOI=10.1371/journal.pone.0004053; RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., RA Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.; RT "A recalibrated molecular clock and independent origins for the RT cholera pandemic clones."; RL PLoS ONE 3:E4053-E4053(2008). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001233; ACP04398.1; -; Genomic_DNA. DR RefSeq; YP_002808849.1; NC_012578.1. DR ProteinModelPortal; C3LPQ4; -. DR STRING; 579112.VCM66_0062; -. DR EnsemblBacteria; ACP04398; ACP04398; VCM66_0062. DR GeneID; 7771359; -. DR KEGG; vcm:VCM66_0062; -. DR PATRIC; 20063875; VBIVibCho108967_0060. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RIKDSTH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; VCHO579112:GJAW-67-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID C3MIK8_RHISN Unreviewed; 217 AA. AC C3MIK8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=NGR_c28250; OS Rhizobium sp. (strain NGR234). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NGR234; RX PubMed=19376903; DOI=10.1128/AEM.00515-09; RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A., RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roser A., RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A., RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.; RT "Rhizobium sp. strain NGR234 possesses a remarkable number of RT secretion systems."; RL Appl. Environ. Microbiol. 75:4035-4045(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001389; ACP26571.1; -; Genomic_DNA. DR RefSeq; YP_002827324.1; NC_012587.1. DR ProteinModelPortal; C3MIK8; -. DR STRING; 394.NGR_c28250; -. DR EnsemblBacteria; ACP26571; ACP26571; NGR_c28250. DR GeneID; 7790479; -. DR KEGG; rhi:NGR_c28250; -. DR PATRIC; 32312143; VBIRhiSp122450_5661. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; SFRE394:GBYN-2816-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 217 AA; 22934 MW; 7F025DE8F69036EB CRC64; MSNTDNRCRL VLIAPDMPDL AERSKVLADA LKGGDVASVI VPQYGLNETD FQKHAEALVP VIQKAGAAAL IEGDTRVAGR SKADGLHIAA GADVLGEAIE RHTPKMIVGG GNATDRHHAL EIGELRPDYV FFGRTDGDIK PEAHPKNLAL AEWWASMIEI PCIVMGGTDP QSALAVAETG AEFVALRLAV FAEPGQAPSV VAAVNALLDE KAPRFED // ID C3NTR6_VIBCJ Unreviewed; 440 AA. AC C3NTR6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=VCD_001530; OS Vibrio cholerae serotype O1 (strain MJ-1236). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=593588; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MJ-1236; RX PubMed=19720995; DOI=10.1073/pnas.0907787106; RA Chun J., Grim C.J., Hasan N.A., Lee J.H., Choi S.Y., Haley B.J., RA Taviani E., Jeon Y.-S., Kim D.W., Lee J.-H., Brettin T.S., Bruce D.C., RA Challacombe J.F., Detter J.C., Han C.S., Munk A.C., Chertkov O., RA Meincke L., Saunders E., Walters R.A., Huq A., Nair G.B., RA Colwell R.R.; RT "Comparative genomics reveals mechanism for short-term and long-term RT clonal transitions in pandemic Vibrio cholerae."; RL Proc. Natl. Acad. Sci. U.S.A. 106:15442-15447(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001485; ACQ59699.1; -; Genomic_DNA. DR RefSeq; YP_002877269.1; NC_012668.1. DR ProteinModelPortal; C3NTR6; -. DR STRING; 593588.VCD_001530; -. DR EnsemblBacteria; ACQ59699; ACQ59699; VCD_001530. DR GeneID; 7856815; -. DR KEGG; vcj:VCD_001530; -. DR PATRIC; 20074380; VBIVibCho20143_1548. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RIKDSTH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; VCHO593588:GI2R-567-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID C3P0L1_BACAA Unreviewed; 206 AA. AC C3P0L1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=BAA_0836; OS Bacillus anthracis (strain A0248). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=592021; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A0248; RA Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., RA Sims D., Brettin T.; RT "Genome sequence of Bacillus anthracis A0248."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001598; ACQ46948.1; -; Genomic_DNA. DR RefSeq; YP_002865324.1; NC_012659.1. DR ProteinModelPortal; C3P0L1; -. DR STRING; 592021.BAA_0836; -. DR EnsemblBacteria; ACQ46948; ACQ46948; BAA_0836. DR GeneID; 7851202; -. DR KEGG; bai:BAA_0836; -. DR PATRIC; 18767416; VBIBacAnt132916_1040. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BANT592021:GJAQ-818-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID C3PH63_CORA7 Unreviewed; 197 AA. AC C3PH63; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=cauri_1574; OS Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CN-1) OS (Corynebacterium nigricans). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=548476; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700975 / DSM 44827 / CN-1; RX PubMed=20137072; DOI=10.1186/1471-2164-11-91; RA Trost E., Gotker S., Schneider J., Schneiker-Bekel S., RA Szczepanowski R., Tilker A., Viehoever P., Arnold W., Bekel T., RA Blom J., Gartemann K.H., Linke B., Goesmann A., Puhler A., RA Shukla S.K., Tauch A.; RT "Complete genome sequence and lifestyle of black-pigmented RT Corynebacterium aurimucosum ATCC 700975 (formerly C. nigricans CN-1) RT isolated from a vaginal swab of a woman with spontaneous abortion."; RL BMC Genomics 11:91-91(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001601; ACP33167.1; -; Genomic_DNA. DR RefSeq; YP_002835105.1; NC_012590.1. DR ProteinModelPortal; C3PH63; -. DR STRING; 169292.cauri_1574; -. DR EnsemblBacteria; ACP33167; ACP33167; cauri_1574. DR GeneID; 7800853; -. DR KEGG; car:cauri_1574; -. DR PATRIC; 21479184; VBICorAur68407_1612. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6PZXB0; -. DR BioCyc; CAUR548476:GH9E-1612-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 16 20 HMP-PP binding (By similarity). FT REGION 122 124 THZ-P binding (By similarity). FT METAL 51 51 Magnesium (By similarity). FT METAL 75 75 Magnesium (By similarity). FT BINDING 50 50 HMP-PP (By similarity). FT BINDING 94 94 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). SQ SEQUENCE 197 AA; 20274 MW; 717C6D6F522FF44E CRC64; MRIAAAAARG GAGVVQVRSK PISARDLYCL GRDVARAVAK ANPETRVLID DRVDVAAALR HAGEPVHGVH VGQDDLPVAA ARALLGPDAI IGLTTGTREL VESANDVADV IDYIGCGPFR ATPTKDSGRT PLGLHAYPEL VKLSRVPLVA IGDVTAEDAA DLAATGVAGL AVVRGIMHAA DPEAYCRELL SGFDEGA // ID C3Q220_9BACE Unreviewed; 202 AA. AC C3Q220; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BSBG_02591; OS Bacteroides sp. 9_1_42FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457395; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=9_1_42FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Ilzarbe M., Galagan J., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 9_1_42FAA."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973130; EEO61619.1; -; Genomic_DNA. DR ProteinModelPortal; C3Q220; -. DR EnsemblBacteria; EEO61619; EEO61619; BSBG_02591. DR PATRIC; 30539829; VBIBacSp125524_2551. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 22884 MW; 8737ADB47025626C CRC64; MKLILITPPT YFVEEDKIIT ALFEEGLDTL HLRKPGTAPM FAERLLTLIP EQYHKRIVVH GHFYLKEEYK LKGIHLNGRN PNLPEGYKGH VSCSCHSLDE VKEHKSGCDY VFLSPVFNSI SKLNYNSAYT AEELRAAAKA SIIDKKVIAL GGIDEENLLE VKDFGFGGAA ILGALWNKFD ACTDRDYRCV IEHFRKLRDL AD // ID C3Q230_9BACE Unreviewed; 208 AA. AC C3Q230; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSBG_02601; OS Bacteroides sp. 9_1_42FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457395; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=9_1_42FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Ilzarbe M., Galagan J., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 9_1_42FAA."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973130; EEO61629.1; -; Genomic_DNA. DR ProteinModelPortal; C3Q230; -. DR EnsemblBacteria; EEO61629; EEO61629; BSBG_02601. DR PATRIC; 30539847; VBIBacSp125524_2560. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 23142 MW; 21FF7CB1B792EA98 CRC64; MEDKTVELQF ITHFTDTYSY YDSARMALEG GCRWIQLRMK DTSVDEVERE AIRLQGLCKD YGATFIIDDH VELVNKIHAD GVHLGKKDMP VAEARKILGK EFIIGGTANT FDDVKMHYEA GADYIGCGPF RFTTTKKDLS PVLGLEGYRS IIQQMKEADI HLPIVAIGGI TLEDIPSIME TGITGIALSG TILRAKDPVA ETKRIMNL // ID C3QGQ5_9BACE Unreviewed; 202 AA. AC C3QGQ5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-OCT-2013, entry version 25. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BSAG_02850; OS Bacteroides sp. D1. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=556258; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D1; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C., RA White A., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. D1."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACAB02000071; EEO51139.1; -; Genomic_DNA. DR ProteinModelPortal; C3QGQ5; -. DR EnsemblBacteria; EEO51139; EEO51139; BSAG_02850. DR PATRIC; 30549982; VBIBacSp27461_2787. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23627 MW; 6FBE04FC6BF5D5DD CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNRFD ACQDQNYLAV IEHFKKLKKL SD // ID C3QGR0_9BACE Unreviewed; 206 AA. AC C3QGR0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSAG_02855; OS Bacteroides sp. D1. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=556258; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D1; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C., RA White A., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. D1."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACAB02000071; EEO51144.1; -; Genomic_DNA. DR ProteinModelPortal; C3QGR0; -. DR EnsemblBacteria; EEO51144; EEO51144; BSAG_02855. DR PATRIC; 30549992; VBIBacSp27461_2792. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22655 MW; C71D2CE7B5A79C06 CRC64; MISLQFITHQ TERYSYLESA RMALEGGCKW IQLRMKDALL EEVEAVALQL KPLCKEHEAI LILDDHVELA KKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYSSILSQ MKEANIEIPV VAIGGITFED IPAILHTGVN GIALSGTILG ADNPVEETRR IIESDL // ID C3QZ01_9BACE Unreviewed; 202 AA. AC C3QZ01; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BSCG_04113; OS Bacteroides sp. 2_2_4. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469590; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_2_4; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Ilzarbe M., Galagan J., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 2_2_4."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973363; EEO57185.1; -; Genomic_DNA. DR ProteinModelPortal; C3QZ01; -. DR SMR; C3QZ01; 1-202. DR EnsemblBacteria; EEO57185; EEO57185; BSCG_04113. DR PATRIC; 30512229; VBIBacSp4777_3907. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23599 MW; 772F8DFC6BF5D5DD CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNKFD ACQDQNYLAV IEHFKKLKKL SD // ID C3QZ06_9BACE Unreviewed; 205 AA. AC C3QZ06; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSCG_04118; OS Bacteroides sp. 2_2_4. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469590; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_2_4; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Ilzarbe M., Galagan J., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 2_2_4."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973363; EEO57190.1; -; Genomic_DNA. DR ProteinModelPortal; C3QZ06; -. DR EnsemblBacteria; EEO57190; EEO57190; BSCG_04118. DR PATRIC; 30512241; VBIBacSp4777_3913. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22563 MW; 1202DD2FC8A91CE3 CRC64; MISLQFIMHQ TERYSYLESA RMALEGGCKW IQLRMKDALL EEVEAVALQL KPLCKEHEAI LILDDHVELA KKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYSSILSQ MKEANIEIPV VAIGGITFED IPAILHTGVN GIALSGTILG ADNPVEETRR ILNHA // ID C3RBF7_9BACE Unreviewed; 208 AA. AC C3RBF7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSEG_02523; OS Bacteroides dorei 5_1_36/D4. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=556260; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_36/D4; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C., RA White A., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides dorei 5_1_36/D4."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDI02000027; EEO46382.1; -; Genomic_DNA. DR ProteinModelPortal; C3RBF7; -. DR EnsemblBacteria; EEO46382; EEO46382; BSEG_02523. DR PATRIC; 30569812; VBIBacSp91558_2634. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 23200 MW; 71CC7CB1B792EA9A CRC64; MEDKTVELQF ITHFTDTYSY YDSARMALEG GCRWIQLRMK DTSVDEVERE AIRLQGLCKD YGATFIIDDH VELVNKIHAD GVHLGKKDMP VAEARKILGK EFIIGGTANT FDDVKMHYEA GADYIGCGPF RFTTTKKDLS PVLGLEGYRS IIQQMKEADI HLPIVAIGGI TLEDIPSIME TGITDIALSG TILRAKDPVA ETKRIMNL // ID C3RBG6_9BACE Unreviewed; 202 AA. AC C3RBG6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-OCT-2013, entry version 27. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BSEG_02532; OS Bacteroides dorei 5_1_36/D4. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=556260; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_36/D4; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C., RA White A., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides dorei 5_1_36/D4."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDI02000027; EEO46391.1; -; Genomic_DNA. DR ProteinModelPortal; C3RBG6; -. DR EnsemblBacteria; EEO46391; EEO46391; BSEG_02532. DR PATRIC; 30569830; VBIBacSp91558_2643. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 22884 MW; 8737ADB47025626C CRC64; MKLILITPPT YFVEEDKIIT ALFEEGLDTL HLRKPGTAPM FAERLLTLIP EQYHKRIVVH GHFYLKEEYK LKGIHLNGRN PNLPEGYKGH VSCSCHSLDE VKEHKSGCDY VFLSPVFNSI SKLNYNSAYT AEELRAAAKA SIIDKKVIAL GGIDEENLLE VKDFGFGGAA ILGALWNKFD ACTDRDYRCV IEHFRKLRDL AD // ID C3RJD3_9FIRM Unreviewed; 206 AA. AC C3RJD3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MBAG_00852; OS Coprobacillus sp. D7. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Coprobacillus. OX NCBI_TaxID=556270; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D7; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Ambrose C., White A., RA Sibley C., Strauss J., Allen-Vercoe E., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Erysipelotrichaceae bacterium D7."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDT02000098; EEO31900.1; -; Genomic_DNA. DR ProteinModelPortal; C3RJD3; -. DR EnsemblBacteria; EEO31900; EEO31900; MBAG_00852. DR PATRIC; 26287678; VBIMolBac20654_0858. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22303 MW; 6C761418F7B6EC8A CRC64; MLELYLVSDR SWLNDRSLEE DIEQAILGGV TMVQLREKNL TDEEFTIQAK KVKTICSKYH IPFIINDNVA VALAVDSDGI HIGQDDQPVK RVRKIIGPHK IIGVSAHNLK EALAAKEDGA DYLGVGAMFN TSTKDDATAV SFTQLHEITT KIGLPVVAIG GINQDNCLLL KGTKIDGIAV VSAIMSAPDI KEAAAKLKAH ARGIYD // ID C3SI77_ECOLX Unreviewed; 211 AA. AC C3SI77; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECs4916; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=493/89, 86-24, 87-14, TB182A, and TW14359; RX PubMed=19439656; DOI=10.1073/pnas.0812949106; RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J., RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E., RA Sawyer S.A., Whittam T.S., Tarr P.I.; RT "A precise reconstruction of the emergence and constrained radiations RT of Escherichia coli O157 portrayed by backbone concatenomic RT analysis."; RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EU891600; ACI74181.1; -; Genomic_DNA. DR EMBL; EU891601; ACI74182.1; -; Genomic_DNA. DR EMBL; EU891602; ACI74183.1; -; Genomic_DNA. DR EMBL; EU891603; ACI74184.1; -; Genomic_DNA. DR EMBL; EU891604; ACI74185.1; -; Genomic_DNA. DR ProteinModelPortal; C3SI77; -. DR SMR; C3SI77; 10-209. DR PRIDE; C3SI77; -. DR HOGENOM; HOG000155781; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID C3WE30_FUSMR Unreviewed; 210 AA. AC C3WE30; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FMAG_01698; OS Fusobacterium mortiferum ATCC 9817. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469616; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 9817; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium mortiferum ATCC 9817."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDB02000044; EEO36136.1; -; Genomic_DNA. DR ProteinModelPortal; C3WE30; -. DR EnsemblBacteria; EEO36136; EEO36136; FMAG_01698. DR PATRIC; 30261178; VBIFusMor134737_1629. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23251 MW; F37FFF847BE89253 CRC64; MRNRIEIPKG IYGITGDNFS NGRSNYFCVE EMIKGGIKIV QYRAKTKDTR EKVKEAREIR ELCRKNGVIF IVNDNVDIAL LVDADGVHIG QEDMHPDDVR KLIGDNKIIG LSTHSEKQGM EAYKNPNVDY IGVGPIFPTT TKDTTPVGLG YLEYAVKNLD LPFVAIGGIK AHNIDAIIAK GAQRVCLVSE IVGADSISDM ARNLQEKFNK // ID C3WEN0_FUSMR Unreviewed; 475 AA. AC C3WEN0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE SubName: Full=Hydroxyethylthiazole kinase; DE EC=2.7.1.50; GN Name=thiM; ORFNames=FMAG_01898; OS Fusobacterium mortiferum ATCC 9817. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469616; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 9817; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium mortiferum ATCC 9817."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDB02000025; EEO36336.1; -; Genomic_DNA. DR ProteinModelPortal; C3WEN0; -. DR EnsemblBacteria; EEO36336; EEO36336; FMAG_01898. DR PATRIC; 30261588; VBIFusMor134737_1833. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 475 AA; 51168 MW; 73536A054F2825D6 CRC64; MNKIDYSVYL VTDRDILQGR DLCEAVEESI LGGATVVQLR EKYISFEEFV KLGKKLHKIT QKYNIPLIIN DNVDVAIEVG AEGVHVGQGD EELSKVRAKI GDKIIGVSVE NVEEALIAQE GGADYLGIGS IFYTGSKKDI NIPIGLEGLK KIVESVNIPN VAIGGIHLDN VREVMKTKTD GVAVISEILG KEDIKEATAI LKNYVKEGIK MNNFAKVISE IREKKPIVYQ ITNTVTINDC ANVTLAIGAS PIMSFCEDEL EDVLSFASAL VINIGTMDKS MRKIVVKAGK IANKLGKPVI LDPVGAGATQ ARKELVEKLL EKVKFAVIKG NVAEIKAIYG MKNESNRGVD SVESSDNIEE IAKELAIKYN CVIAATGKVD LVTDGKRVAK IENGDIVLGS VTGTGCMTGA LIGSACGATE DYFTGAITMI STMGIAGEKA KLQGNGNGSF RQIIMDTVYQ MNEEEFLNSA KIRVE // ID C3WJX3_9FUSO Unreviewed; 206 AA. AC C3WJX3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 2. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FSAG_01189; OS Fusobacterium periodonticum 2_1_31. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469599; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_31; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 2_1_31."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDC02000032; EEO38179.2; -; Genomic_DNA. DR EnsemblBacteria; EEO38179; EEO38179; FSAG_01189. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22550 MW; EC69B9F6984F42CE CRC64; MELKACKIYL VTDEKACLGK GFYVCIEEAI KGGVKIVQLR EKNISTKDFY EKALKVKEIC ENYGALFIIN DRLDIAQAVG ADGVHLGQSD MPIEKAREIL KDKFLIGATA RNIEEAKRAE LLGADYIGSG AIFGTNTKDN AKKLEMEELK KIVTSVKIPV FAIGGINIDN VSSLKNIGLQ GICAVSGILS EKDCKKAVDM MLKKFN // ID C3WJX9_9FUSO Unreviewed; 205 AA. AC C3WJX9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=FSAG_01195; OS Fusobacterium periodonticum 2_1_31. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469599; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_31; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 2_1_31."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDC02000032; EEO38185.1; -; Genomic_DNA. DR ProteinModelPortal; C3WJX9; -. DR EnsemblBacteria; EEO38185; EEO38185; FSAG_01195. DR PATRIC; 30280333; VBIFusSp41726_1074. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 205 AA; 23670 MW; E2B3EA04869DAE4B CRC64; MINKIKLNII SNRKLCENEN LEKQIEKIFL AYERKIILKN FDIVAFTLRE KDLNKNEYLK LIEKVYPICQ KYKINLILHQ NYDLNLDDKY KIDGIHLSYN IFKSLNENIK AELIKKYKRI GVSIHSLDEA KEVENLGASY VIAGHIFETD CKKGLKPRGL KFVEDLSSAL TIPIFAIGGI DEKNSQSVID SGAFSVCMMS NLMKY // ID C3WR55_FUSNV Unreviewed; 206 AA. AC C3WR55; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=FSCG_01396; OS Fusobacterium nucleatum subsp. vincentii 4_1_13. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469606; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_1_13; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 4_1_13."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657999; EEO40683.1; -; Genomic_DNA. DR ProteinModelPortal; C3WR55; -. DR EnsemblBacteria; EEO40683; EEO40683; FSCG_01396. DR PATRIC; 30298211; VBIFusSp49854_0904. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 23935 MW; 04B7AF8D602400CF CRC64; MIENKIKLNI ISNRKLCENE NLEKQIEKIF SAYQRKIILE NFEIVALTLR EKDLYKNEYL KLVEKIYPIC QKYRIDLILH QNYDLVLEDK YNIEGIHLSY NTFKSLNKNI RKELIKKYKK IGVSIHSIDE AKEAENLGAT YIVAGHIFKT DCKKDLEPRG LEFIQELSSA LIIPIFAIGG INQENSHLVI NNGAFGVCMM SSLMKH // ID C3WR61_FUSNV Unreviewed; 206 AA. AC C3WR61; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FSCG_01402; OS Fusobacterium nucleatum subsp. vincentii 4_1_13. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469606; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_1_13; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 4_1_13."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657999; EEO40689.1; -; Genomic_DNA. DR ProteinModelPortal; C3WR61; -. DR EnsemblBacteria; EEO40689; EEO40689; FSCG_01402. DR PATRIC; 30298223; VBIFusSp49854_0910. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22790 MW; 3B9658706C49BA6C CRC64; MDLKDCKIYL VTDEKSCNGK DFYKCIEEAI KGGVKIVQLR EKTLSTKDFF IKALKVKEIC KSYGVLFIIN DRLDITQAVE ADGVHLGQSD MPIEKAREIL KNKFLIGATA RNIEEAKKAE LLGADYIGSG AIFGTSTKDN AKKLEMEDLK KIVNSVKIPV FAIGGININN VWILKNIGLQ GICSVSGILS EKDCKKAVEN ILKNFN // ID C3X0V6_FUSNU Unreviewed; 206 AA. AC C3X0V6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-APR-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FSDG_02321; OS Fusobacterium nucleatum subsp. animalis 7_1. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=457405; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_1; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 7_1."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007062; EEO43762.1; -; Genomic_DNA. DR ProteinModelPortal; C3X0V6; -. DR EnsemblBacteria; EEO43762; EEO43762; FSDG_02321. DR PATRIC; 30304612; VBIFusSp38687_2362. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22821 MW; DD796D41845C55F1 CRC64; MKLKDCKIYL VTDEKACSGK DFYKCIEESI KGGVKIVQLR EKNISTKDFY EKALKVKEIC KNYGVLFIIN DRLDITQAVE ADGVHLGQSD MPIEKAREIL KDKFLIGATA KNIEEAKKAE LLGADYIGSG AIFGTSTKDN AKKLEIEDLK KIVNSVKIPV FAIGGININN VWMLKNIGLQ GICSVSGILS EKDCKKAVEN ILKNFN // ID C3X0W2_FUSNU Unreviewed; 206 AA. AC C3X0W2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-APR-2014, entry version 23. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=FSDG_02327; OS Fusobacterium nucleatum subsp. animalis 7_1. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=457405; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_1; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 7_1."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007062; EEO43768.1; -; Genomic_DNA. DR ProteinModelPortal; C3X0W2; -. DR EnsemblBacteria; EEO43768; EEO43768; FSDG_02327. DR PATRIC; 30304624; VBIFusSp38687_2368. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 23932 MW; D80B78263413E9F8 CRC64; MIENKIKLNI ISNRKLCENE NLEKQIEKIF SAYQRKIILE NFEIVSLTLR EKDLNKNKYL KLVEKIYPIC QKYRIDLILH QNYDLRLDNK YNIKGLHLSY NTFKSLNKNI REELIRKYKK IGVSIHSVDE AKEVENLGAN YVVAGHIFKT DCKKALEPRG LKFIQELSVI LTIPIFAIGG INQENSHLVI NSGAFGVCMM SSLMKD // ID C3X5F5_OXAFO Unreviewed; 203 AA. AC C3X5F5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=OFAG_01594; OS Oxalobacter formigenes HOxBLS. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Oxalobacter. OX NCBI_TaxID=556268; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HOxBLS; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Allison M.J., Humphrey S., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Oxalobacter formigenes HOxBLS."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDP02000002; EEO28441.1; -; Genomic_DNA. DR ProteinModelPortal; C3X5F5; -. DR EnsemblBacteria; EEO28441; EEO28441; OFAG_01594. DR PATRIC; 28553453; VBIOxaFor11927_2016. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 22176 MW; C9D18C87AFBAD796 CRC64; MKGLYIVTPD WDDTAKMVEV TEKALTGGAQ IVQYRHKTAG PELLLEQARA LRDLCRRYEK PFIINDYVDL CLELDTDGIH VGGMDVPVKK VRAAVGPDKI VGASCYGDLE LARKATRDGA SYVAFGGFYP SRVKKYPVTT PQNIVSDWKK ETPSMPVCVI GGMSVENAIP LVELGADMVA VVSGVYFQDD PEAAARGFAQ LFK // ID C3XBM9_OXAFO Unreviewed; 219 AA. AC C3XBM9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=OFBG_01633; OS Oxalobacter formigenes OXCC13. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Oxalobacter. OX NCBI_TaxID=556269; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OXCC13; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allison M.J., RA Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Oxalobacter formigenes OXCC13."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG658170; EEO30605.1; -; Genomic_DNA. DR ProteinModelPortal; C3XBM9; -. DR EnsemblBacteria; EEO30605; EEO30605; OFBG_01633. DR PATRIC; 25833107; VBIOxaFor91597_0765. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 49 53 HMP-PP binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23855 MW; 2E97FBBC1D2292FD CRC64; MPVCLNEALL KKDEESMKGL YIVTPDWDDT AKMVEVTEKA LKGGAEIVQY RHKTAGPQLR LEQAKALQAV CKKYNKPFII NDYVDLCLEL DADGIHVGGM DAPVKKVRAA VGPDKIVGAS CYGDLNLARS ATHDGATYVA FGGFYPSRVK KYPVTTPLDI VSEWKKEQPD MPVCVIGGMD VEKGAPLVAK GAEMVAVVSG VYFQDDPEAA AREFVKLFK // ID C3XEY5_9HELI Unreviewed; 269 AA. AC C3XEY5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 13-NOV-2013, entry version 22. DE SubName: Full=Uncharacterized protein; GN ORFNames=HRAG_00631; OS Helicobacter bilis ATCC 43879. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=613026; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43879; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Fox J.G., Shen Z., RA Charoenlap N., Schauer D.B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Helicobacter bilis ATCC 43879."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDN02000018; EEO23574.1; -; Genomic_DNA. DR ProteinModelPortal; C3XEY5; -. DR EnsemblBacteria; EEO23574; EEO23574; HRAG_00631. DR PATRIC; 26831322; VBIHelBil77108_0528. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 269 AA; 30931 MW; F40C10E9FC6443B6 CRC64; MLSYLILSPA YYADDTLYTK LQYAYAMLES KGMTLDFIAF RYDNSDILSA NEYHKLFETY RFCQTHNIAL LLNLSIYKLE TLVLLWLHGF NLGIHFKESD ISLLRDNICK DLKQSHALIY SLQDNMSLHE KLKILYSTLS HTSIAKSLKL LCDIESFSYF LTPLNQALNT YENLMQENRL DKRFYPIFVS THNLKDLSKV LSLGANYATI SPIFYDKGNK ALGLPYLQNL PLHVKERAFA LGGINSDLRV HEIKSCGVAG FASISYFLR // ID C3XIG6_9HELI Unreviewed; 378 AA. AC C3XIG6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HRAG_01841; OS Helicobacter bilis ATCC 43879. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=613026; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43879; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Fox J.G., Shen Z., RA Charoenlap N., Schauer D.B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Helicobacter bilis ATCC 43879."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDN02000065; EEO24784.1; -; Genomic_DNA. DR ProteinModelPortal; C3XIG6; -. DR EnsemblBacteria; EEO24784; EEO24784; HRAG_01841. DR PATRIC; 26833872; VBIHelBil77108_1906. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 378 AA; 41560 MW; B3ECF0966FCE3E72 CRC64; MKNTRLKGLY GISDTKLTPT KTLIAQLQKA IQGGLKIFQY RDKDSKDSEI IGLVGELQAL CNENNVLFVL NDRYELAIKL GVSGLHLGKD EVSQLLDIRE SFKGIIGVSC YDSIELAQRY ESAKVDYVAF GSLFPSPTKR DAKPCPLSVI VEAKHKLKIP ICGIGGICVD NVSLLKECDM IAVISSLWNI DSKNYAPNPA AYPNLADKLD TKITTCHTEP LGEVSSMESK KDFSPMTQND KQILDSITTS HKDISPFSKA QYDKILESIT TNHANKTTNS SSCSMALEAL SELEDMSYLS DMTIHHNSLN LSNCIDKGAN LENQNSSQNA PLNPAPTQAV KNQDSKNLAP FKAEDLKDSD YNYITANAKN LIAAWQTK // ID C3XKS9_9HELI Unreviewed; 143 AA. AC C3XKS9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Uncharacterized protein; GN ORFNames=HWAG_00410; OS Helicobacter winghamensis ATCC BAA-430. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=556267; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-430; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Fox J.G., Shen Z., RA Charoenlap N., Schauer D.B., Lander E., Galagan J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Helicobacter winghamensis ATCC BAA-430."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG661973; EEO25618.1; -; Genomic_DNA. DR ProteinModelPortal; C3XKS9; -. DR EnsemblBacteria; EEO25618; EEO25618; HWAG_00410. DR PATRIC; 27527578; VBIHelWin108846_0532. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 143 AA; 16215 MW; A364DAA5127FBF7A CRC64; MLFDSRLLEI FLELNCKFNV ISLINSNANL GLKLGFDGVH CNGAQLDQIQ NYKKRFQYVF YSAHNLQDLD KADKMGASGI TISPIFQSPN KGIPLGIEFL KRINPKDYQA EIFALGGIVT EIEIDVLKQT QIHNFASIRY FLN // ID C3XM43_9HELI Unreviewed; 213 AA. AC C3XM43; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HWAG_00874; OS Helicobacter winghamensis ATCC BAA-430. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=556267; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-430; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Fox J.G., Shen Z., RA Charoenlap N., Schauer D.B., Lander E., Galagan J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Helicobacter winghamensis ATCC BAA-430."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG661974; EEO26082.1; -; Genomic_DNA. DR ProteinModelPortal; C3XM43; -. DR EnsemblBacteria; EEO26082; EEO26082; HWAG_00874. DR PATRIC; 27528593; VBIHelWin108846_1183. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23788 MW; A3F2F26CE7107AAC CRC64; MIRIYQMFHG IYAISDTRLT PYHALKDMLK QAIRGGITLF QLRDKNTPDS TLAPLCLPLM DLCHLHQIPF ILNDRIELAI SLQTQGLHIG KKQDNTPYNL DELRQIRTKF QGILGISCYG DLTLAKNAKL IGADYIAFGS CFKSTTKPSA KTIPLDIFTQ AKPLNIPMCA IGGIQKDNIA QLKNAQMAAC ISSIWQNDIP SNVKELLKNF KQG // ID C4AQF0_BURML Unreviewed; 209 AA. AC C4AQF0; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 23. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=BMAGB8_A0324; OS Burkholderia mallei GB8 horse 4. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320390; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GB8 horse 4; RA Harkins D.M., Brinkac L.M., Nierman W.C.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAHO01000006; EEP87888.1; -; Genomic_DNA. DR ProteinModelPortal; C4AQF0; -. DR EnsemblBacteria; EEP87888; EEP87888; BMAGB8_A0324. DR PATRIC; 26923528; VBIBurMal32783_1030. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID C4AW06_BURML Unreviewed; 367 AA. AC C4AW06; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=BMAGB8_2845; OS Burkholderia mallei GB8 horse 4. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320390; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GB8 horse 4; RA Harkins D.M., Brinkac L.M., Nierman W.C.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAHO01000029; EEP86003.1; -; Genomic_DNA. DR ProteinModelPortal; C4AW06; -. DR EnsemblBacteria; EEP86003; EEP86003; BMAGB8_2845. DR PATRIC; 26927403; VBIBurMal32783_2940. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; SQ SEQUENCE 367 AA; 38315 MW; 3E9B351CCB7F5C2B CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGARAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID C4EZD9_HAEIF Unreviewed; 226 AA. AC C4EZD9; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSHi7P49H1_07525; OS Haemophilus influenzae 7P49H1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=521005; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7P49H1; RX PubMed=22970300; DOI=10.1371/journal.pone.0044730; RA Zhang L., Xie J., Patel M., Bakhtyar A., Ehrlich G.D., Ahmed A., RA Earl J., Marrs C.F., Clemans D., Murphy T.F., Gilsdorf J.R.; RT "Nontypeable Haemophilus influenzae Genetic Islands Associated with RT Chronic Pulmonary Infection."; RL PLoS ONE 7:E44730-E44730(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWV01000002; EEP46315.1; -; Genomic_DNA. DR ProteinModelPortal; C4EZD9; -. DR EnsemblBacteria; EEP46315; EEP46315; CGSHi7P49H1_07525. DR PATRIC; 28862394; VBIHaeInf63612_0750. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24691 MW; E0E62253176C5443 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL AIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNV GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID C4F3R4_HAEIF Unreviewed; 226 AA. AC C4F3R4; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSHi6P18H1_08870; OS Haemophilus influenzae 6P18H1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=521004; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6P18H1; RX PubMed=22970300; DOI=10.1371/journal.pone.0044730; RA Zhang L., Xie J., Patel M., Bakhtyar A., Ehrlich G.D., Ahmed A., RA Earl J., Marrs C.F., Clemans D., Murphy T.F., Gilsdorf J.R.; RT "Nontypeable Haemophilus influenzae Genetic Islands Associated with RT Chronic Pulmonary Infection."; RL PLoS ONE 7:E44730-E44730(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWW01000002; EEP48360.1; -; Genomic_DNA. DR ProteinModelPortal; C4F3R4; -. DR EnsemblBacteria; EEP48360; EEP48360; CGSHi6P18H1_08870. DR PATRIC; 28857978; VBIHaeInf24200_0576. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24736 MW; CC2434460079404F CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVAEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA EITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID C4FE55_9BIFI Unreviewed; 847 AA. AC C4FE55; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 32. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; ORFNames=BIFANG_02595; OS Bifidobacterium angulatum DSM 20098 = JCM 7096. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=518635; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20098; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYS02000004; EEP21236.1; -; Genomic_DNA. DR ProteinModelPortal; C4FE55; -. DR EnsemblBacteria; EEP21236; EEP21236; BIFANG_02595. DR PATRIC; 27191560; VBIBifAng79419_0662. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 847 AA; 93655 MW; 6CCBA80A8096F123 CRC64; MRGCFDLSAY FVVGPEDCKG RPVTDVVDDA LRGGATFIQL RAKKMDAKEL TETARDIAQI IEDNNKSDTV PFVIDDRVDV VWQARNKGIK VDGVHIGQTD MEPREARALL GEDAIVGLSA ETESLVKLIN ELPAGCIDYI GAGPLHVSTT KPEASVGGND GSGHTLDEEQ INTICAASDF PVVVGGGVHA DDMEMLASTD AAGWFVVSAI AGADDPEAAT REMVTRWKAV RGDRRHGYAQ RPAAVAENAS QQPAQPAAKK FTNAKEAKAA SKLAKQQRVD IAARGCTQRD KAHIRKTTPI HFENQFGTYD LEVPYTEIKL SDTPGVGPNP PFKDYNTEGP KCDPKEGLAP LRLDWIRDRG DVEEYEGRRR NLEDDGKRAI KRGKASKEWR GRQHKPMRAK DHPVTQMWYA RHNIITPEMR YVAEREHCSV ELVRSELAAG RAVMPCNINH PEAEPMIIGA KFLTKLNANM GNSAVTSSID EEVEKLTWAT KWGADTVMDL STGNDIHTTR EWILRNSPVP IGTVPMYQAL EKVEDDASKL SWELFRDTVI EQCEQGVDYM TIHAGVLMRY VPLTANRMTG IVSRGGSIMA EWCLQHHQES FLYTHFDELC DIFAKYDVAF SLGDGLRPGS LADANDQAQL AELMTLGELT KRAWAKDVQV MIEGPGHIPF DTVRMNIEME KAICNDAPFY TLGPLTTDTA PGYDHITSAI GGVEIARYGT AMLCYVTPKE HLGLPNKDDV KQGVIAYKIA CHAADIAKHH PHAMDRDNAM SKARFEFRWL DQFNLSYDPD TAIAYHDETL PAEPAKMAHF CSMCGPKFCS MAISQNIRKK FGDAAAQERL VAEARQD // ID C4FI48_9AQUI Unreviewed; 183 AA. AC C4FI48; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 22. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=SULYE_0232; OS Sulfurihydrogenibium yellowstonense SS-5. OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; OC Sulfurihydrogenibium. OX NCBI_TaxID=432331; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS-5; RA Reysenbach A.-L., Heidelberg J.F., Nelson W.C.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABZS01000014; EEP61235.1; -; Genomic_DNA. DR ProteinModelPortal; C4FI48; -. DR EnsemblBacteria; EEP61235; EEP61235; SULYE_0232. DR PATRIC; 28315507; VBISulYel28410_0207. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 183 AA; 20725 MW; B7BAF9B11B66E8B8 CRC64; MLHRFYFITD RKKFKKPFLD TIKEVLDKGI RLLQIREKDL PDNELFKLTE DVLKIAEGYD AKIIINSRLD IALLLNLDGV HLPENGLPIE PIKKKFPNLI VGKSCHSLEC GLQAYQDGAD YVFISPIFQV EGKAPPIGVE KLREIVNKLP LPVYALGGIN KFNVQSVLDT GVYGIASIRY FLD // ID C4FLH4_9AQUI Unreviewed; 204 AA. AC C4FLH4; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SULYE_1428; OS Sulfurihydrogenibium yellowstonense SS-5. OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; OC Sulfurihydrogenibium. OX NCBI_TaxID=432331; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS-5; RA Reysenbach A.-L., Heidelberg J.F., Nelson W.C.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABZS01000156; EEP60070.1; -; Genomic_DNA. DR ProteinModelPortal; C4FLH4; -. DR EnsemblBacteria; EEP60070; EEP60070; SULYE_1428. DR PATRIC; 28317805; VBISulYel28410_1257. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22978 MW; D988AB0145D5E130 CRC64; MLKGLYVITD EKLTPYDKIF DMVEQALKGG AKLVQLRDKN NSDDFLLPIS KDLKKLCHKY DALFIVNDRL ELTLKSDADG IHVGEEDVDI SEIRKALKDK IIGVSCYGDV ERAILMERLS ATYVAFGSFY FSPTKPKSKI VDKSVITEAK RFLKIPVCVI GGITVERAKE LVELGADLVA VISDIWTAEN IEERARQYTE LFRG // ID C4FSH9_9FIRM Unreviewed; 512 AA. AC C4FSH9; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 27. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=VEIDISOL_01869; OS Veillonella dispar ATCC 17748. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=546273; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17748; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIK02000019; EEP64807.1; -; Genomic_DNA. DR ProteinModelPortal; C4FSH9; -. DR EnsemblBacteria; EEP64807; EEP64807; VEIDISOL_01869. DR PATRIC; 29651892; VBIVeiDis1254_1733. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 512 AA; 55025 MW; 40E7CE431AA173FB CRC64; MTRGDSDMTH ENPYMNGQIW PELNILEILR QRNPLVICIT NDVVRTFTAN GLLAIGASPV MSECSEDLKD LIVHASALLI NIGTLTPDKV SYYKDAIALA KKHEVPIVLD PVGCHAGAYR LSVVLDLIKT GEISLVRGNQ SEIKAIYDAL SPNNQADTST TGKGVDGGQI EDSAVIAYRL ARLINCPVVA TGEEDYVSDG TRVFAVPHGH PIMTAVTGTG CLLGAVLAAF FSAYYPCKNR LSIGEFLAYA LAYYGLAGES AVQVSGVQPG SFSVAFMDSL YTLDDAVLIS ENRIRPVVVP DQLQVYFISG TQDVELNENR LLSIVEDACR GGVTCFQFRE KGVGTLIGQQ KLELAQQLQQ ICAKYNVLYI INDDVDLAMA VNADGIHVGQ EDMRLEEVRN LVGHKVVGIS IHSVEELHKT DVIYADCVGV GPMYATSSKP DAQAPCGPNR ITELQAEGLT LPCVGIGGIT LDNAKLVLQA GAYGVAVISA IAHADNPYEA VQQFKHLVDS TK // ID C4HB19_YERPE Unreviewed; 215 AA. AC C4HB19; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YPF_4489; OS Yersinia pestis biovar Orientalis str. India 195. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=547047; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=India 195; RA Plunkett G.III., Anderson B.D., Baumler D.J., Burland V., Cabot E.L., RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., RA Tapia R., Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., RA Brettin T.S.; RT "Yersinia pestis India 195 whole genome shotgun sequencing project."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNR01000024; EEO79045.1; -; Genomic_DNA. DR ProteinModelPortal; C4HB19; -. DR EnsemblBacteria; EEO79045; EEO79045; YPF_4489. DR PATRIC; 30853026; VBIYerPes43691_4455. DR OMA; GRSTHEP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23275 MW; EE560D5E7AB02574 CRC64; MATPGFPSTE QRLGLYPVVD SLLWIERLLA AGVTTLQLRI KNADDAQVEQ DIVAAIELGK RYQARLFIND YWQLAVKHGA YGVHLGQEDL EAADLAAIQQ AGLRLGISTH DEHELAVAKT LRPSYIALGH IFPTQTKQMP SSPQGLASLS RQVKNTPDYP TVAIGGISIE RVPHVLATGV GSVAVVSAIT LASDWQRATA QLLHLIEGKE LADEK // ID C4HEQ9_YERPE Unreviewed; 215 AA. AC C4HEQ9; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YPH_1711; OS Yersinia pestis biovar Orientalis str. PEXU2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=547046; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEXU2; RA Plunkett G.III., Anderson B.D., Baumler D.J., Burland V., Cabot E.L., RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., RA Tapia R., Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., RA Brettin T.S.; RT "Yersinia pestis PEXU2 whole genome shotgun sequencing project."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNS01000001; EEO85835.1; -; Genomic_DNA. DR ProteinModelPortal; C4HEQ9; -. DR EnsemblBacteria; EEO85835; EEO85835; YPH_1711. DR PATRIC; 30857356; VBIYerPes134055_1695. DR OMA; GRSTHEP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23275 MW; EE560D5E7AB02574 CRC64; MATPGFPSTE QRLGLYPVVD SLLWIERLLA AGVTTLQLRI KNADDAQVEQ DIVAAIELGK RYQARLFIND YWQLAVKHGA YGVHLGQEDL EAADLAAIQQ AGLRLGISTH DEHELAVAKT LRPSYIALGH IFPTQTKQMP SSPQGLASLS RQVKNTPDYP TVAIGGISIE RVPHVLATGV GSVAVVSAIT LASDWQRATA QLLHLIEGKE LADEK // ID C4HRM0_YERPE Unreviewed; 215 AA. AC C4HRM0; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YPS_1406; OS Yersinia pestis Pestoides A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=545431; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pestoides A; RA Plunkett G.III., Anderson B.D., Baumler D.J., Burland V., Cabot E.L., RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Nikolich M.P., RA Lindler L.E., Munk A.C., Tapia R., Green L.D., Rogers Y.C., RA Detter J.C., Bruce D.C., Brettin T.S.; RT "Yersinia pestis Pestoides A whole genome shotgun sequencing RT project."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNT01000007; EEO91186.1; -; Genomic_DNA. DR ProteinModelPortal; C4HRM0; -. DR EnsemblBacteria; EEO91186; EEO91186; YPS_1406. DR PATRIC; 29588350; VBIYerPes43853_1418. DR OMA; GRSTHEP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23275 MW; EE560D5E7AB02574 CRC64; MATPGFPSTE QRLGLYPVVD SLLWIERLLA AGVTTLQLRI KNADDAQVEQ DIVAAIELGK RYQARLFIND YWQLAVKHGA YGVHLGQEDL EAADLAAIQQ AGLRLGISTH DEHELAVAKT LRPSYIALGH IFPTQTKQMP SSPQGLASLS RQVKNTPDYP TVAIGGISIE RVPHVLATGV GSVAVVSAIT LASDWQRATA QLLHLIEGKE LADEK // ID C4I3M8_BURPE Unreviewed; 212 AA. AC C4I3M8; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-MAR-2014, entry version 21. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=GBP346_B0950; OS Burkholderia pseudomallei MSHR346. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=536230; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MSHR346; RA Harkins D.M., Brinkac L.M., Rogers Y.C., Detter J.C., Munk A.C., RA Bruce D.C., Keim P., Sims D.R., Brettin T.S.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACOJ01000001; EEP50868.1; -; Genomic_DNA. DR EnsemblBacteria; EEP50868; EEP50868; GBP346_B0950. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 212 AA; 22914 MW; E9490D3DCDB2EE86 CRC64; MIESIIHHHL KIIVNKSANL PSEYLITPEP PGDEALSDYL ATLERTLKAG ISLVQLRAKA VTAPYYARLT EYALACCRRY NARLLVNAAP EVALGLHTDG VHLTSTRLMT CSTRPLPAGL LVSAACHDED QVRHADSIGV DLITISPVMP TATHTTAEPL GWPRFRELAT LTSVPVYALG GMSVDSLAEA RNAGAYGIAA IRAFWESNVD RS // ID C4I8T7_BURPE Unreviewed; 209 AA. AC C4I8T7; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-MAR-2014, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=GBP346_B1878; OS Burkholderia pseudomallei MSHR346. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=536230; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MSHR346; RA Harkins D.M., Brinkac L.M., Rogers Y.C., Detter J.C., Munk A.C., RA Bruce D.C., Keim P., Sims D.R., Brettin T.S.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACOJ01000001; EEP51967.1; -; Genomic_DNA. DR EnsemblBacteria; EEP51967; EEP51967; GBP346_B1878. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 209 AA; 21746 MW; 1CEF4D05DD11B9CE CRC64; MSARDGDRAP DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID C4IFI7_CLOBU Unreviewed; 213 AA. AC C4IFI7; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-MAR-2014, entry version 23. DE SubName: Full=Regulatory protein teni; GN ORFNames=CLP_1691; OS Clostridium butyricum E4 str. BoNT E BL5262. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=632245; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BoNT E BL5262; RA Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C., RA Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A., RA Smith T.J., Sutton G., Brettin T.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACOM01000005; EEP54124.1; -; Genomic_DNA. DR ProteinModelPortal; C4IFI7; -. DR EnsemblBacteria; EEP54124; EEP54124; CLP_1691. DR PATRIC; 26458559; VBICloBut121738_2258. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 213 AA; 23885 MW; B1E5AB0AD50C8BA7 CRC64; MYNILAITNR HLCKGDFLEQ IKKICLYNNK IQHMNSSKNY NKKSVNNISS ISIVLREKDL NERDYELLAS KVIRICEEYN TECILHTYYN VARKLGCSKI HLPLHILKSK PYIAEIFDVV GVSIHSVGDA LDAKNMNVTY VTAGHIFNTD CKKDIPARGL AFLNNIVNSV DIPVFAIGGI ASSNIGSVIN YGAFGVCIMS GFMNIENPED FFL // ID C4IM80_CLOBU Unreviewed; 210 AA. AC C4IM80; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-MAR-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLP_0259; OS Clostridium butyricum E4 str. BoNT E BL5262. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=632245; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BoNT E BL5262; RA Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C., RA Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A., RA Smith T.J., Sutton G., Brettin T.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACOM01000007; EEP52717.1; -; Genomic_DNA. DR ProteinModelPortal; C4IM80; -. DR EnsemblBacteria; EEP52717; EEP52717; CLP_0259. DR PATRIC; 26461927; VBICloBut121738_3934. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; D18E32489B35C17B CRC64; MKPKIDYSIY LVTDRDLMST ETLEEAVEEA IKGGCTLVQL REKDCSSLDF YNTAINLKRI TDKYNVPLLI NDRLDIALAV DAAGVHIGQS DLPCSVVRKV IGEDKIIGVS AGTLENAIKA ENDGADYIGV GAMYETGTKK DAKHTSMDEL KKIRENISIP IVVIGGINKE RITNFNGTDI DGLAIVSAII SQKDIYKATS ELKDLFFKLK // ID C4IN77_BRUAO Unreviewed; 203 AA. AC C4IN77; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-MAR-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAAA_1000216; OS Brucella abortus str. 2308 A. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=641140; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2308 A; RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., RA Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Munk C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACOR01000001; EEP63723.1; -; Genomic_DNA. DR ProteinModelPortal; C4IN77; -. DR EnsemblBacteria; EEP63723; EEP63723; BAAA_1000216. DR PATRIC; 35201689; VBIBruAbo135566_0226. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C4ISS4_BRUAO Unreviewed; 221 AA. AC C4ISS4; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-MAR-2014, entry version 25. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAAA_3000071; OS Brucella abortus str. 2308 A. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=641140; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2308 A; RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., RA Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Munk C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACOR01000003; EEP62959.1; -; Genomic_DNA. DR ProteinModelPortal; C4ISS4; -. DR EnsemblBacteria; EEP62959; EEP62959; BAAA_3000071. DR PATRIC; 35204891; VBIBruAbo135566_1784. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C4J962_MAIZE Unreviewed; 179 AA. AC C4J962; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-MAR-2014, entry version 29. DE SubName: Full=Uncharacterized protein; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B73; RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740; RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J., RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., RA Fernandes J., Walbot V., Yu Y.; RT "Sequencing, mapping, and analysis of 27,455 maize full-length RT cDNAs."; RL PLoS Genet. 5:E1000740-E1000740(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BT087359; ACR37712.1; -; mRNA. DR ProteinModelPortal; C4J962; -. DR Gramene; C4J962; -. DR HOGENOM; HOG000155781; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 179 AA; 18935 MW; 818195828B9512DF CRC64; MFREKDAETR EFLEAAKACV EICKSSGVPL LINDRVDVAL ACDADGVHVG QSDMPAWEVR RLLGPGKIIG VSCKTPAQAE QAWKDGADYI GCGGVFPTTT KANNPTLGFE GLRTVCLASK LPVVAIGGIN AGNAGSVMEL GLPNLKGVAV VSALFDRERV AAETRNLRSI LMKNAYSRS // ID C4JDI7_UNCRE Unreviewed; 479 AA. AC C4JDI7; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 16-APR-2014, entry version 27. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=UREG_00763; OS Uncinocarpus reesii (strain UAMH 1704). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus. OX NCBI_TaxID=336963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UAMH 1704; RX PubMed=19717792; DOI=10.1101/gr.087551.108; RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., RA Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., RA Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., RA Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J., RA Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.; RT "Comparative genomic analyses of the human fungal pathogens RT Coccidioides and their relatives."; RL Genome Res. 19:1722-1731(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH476615; EEP75916.1; -; Genomic_DNA. DR RefSeq; XP_002541249.1; XM_002541203.1. DR ProteinModelPortal; C4JDI7; -. DR GeneID; 8443709; -. DR KEGG; ure:UREG_00763; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 2. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 479 AA; 51367 MW; 75250FCF00ACB570 CRC64; MPIDLSLYLV TDSTPKILGD RDLCAVVEQA AKGGVTIVQY RDKHADTGAL IETAATLHKI TRAHNIPLII NDRVMWPCVG AEESSRQDDM GNRYQVYHRY SGVKQILEFL STSSRRIGTV AIGGINLGNA QRVIYQSQAL RKGLDGIAIV SAVMAASEPQ KAAAILAKAI TKNPPFATMP PELRKDELGY FLDNAIHTVQ KVATDMPLVH SMINYVVANF AANVSLQIGA SPIMSPYGAE ADDLANAGGS LLINMGTLNA DSEKNYLQAM EVYNRRGNPV VLDPVGGGAT DVRQNMVKAL MAGGYFDLIK GNEGEIKAIY GQSPTRQIGV DSGPSTLGPK EKVAMVQDLA SRERNIVLMT GPVDFLSDGI RTIAISNGHP YLGQITGTGC VIGLVAAAFL AVERTDKLLA VLAGVLMFEI AAENAASKEH VHGPGTFVPA LLDELYALRE ATKADVKKNW IKDRAKFVVL KVDRKSNGS // ID C4KBS7_THASP Unreviewed; 316 AA. AC C4KBS7; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Tmz1t_3659; OS Thauera sp. (strain MZ1T). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Thauera. OX NCBI_TaxID=85643; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MZ1T; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Sayler G.S.; RT "Complete sequence of chromosome of Thauera sp. MZ1T."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001281; ACR02252.1; -; Genomic_DNA. DR RefSeq; YP_002890629.1; NC_011662.2. DR ProteinModelPortal; C4KBS7; -. DR STRING; 85643.Tmz1t_3659; -. DR EnsemblBacteria; ACR02252; ACR02252; Tmz1t_3659. DR GeneID; 7873164; -. DR KEGG; tmz:Tmz1t_3659; -. DR PATRIC; 23883502; VBIThaSp83776_3581. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TSP85643:GHEJ-3623-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 316 AA; 34248 MW; 2B014F0D2F3A971B CRC64; MTRKRVEVAA GVLLREDGCY LLGQRAPDAV YAGYWEFPGG KVEPGESPAQ ALVRELDEEL GIRVTRLRPW LCREHLYEHA HVRLHFQEVA AWEGELADRV HSALAWVRPE GPAREPMLPA NGPILKALRL PRTMGITQAA EIGVEVQLDA LERALAGGLR LVQVREATLP DAAREAFARA ALARVRAHGG LLVVNEDEVL ARRIGADGVH LPARRLMAVQ ARPDFPWVGA SCHDRAGLER AAALELDYAL LGPVQPTLTH PGQAGMGWEG FASTAAGLPL PVFALGGLAA DDMERARDAG AHGIAAIRAI WRPVRD // ID C4KC87_THASP Unreviewed; 210 AA. AC C4KC87; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tmz1t_3685; OS Thauera sp. (strain MZ1T). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Thauera. OX NCBI_TaxID=85643; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MZ1T; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Sayler G.S.; RT "Complete sequence of chromosome of Thauera sp. MZ1T."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001281; ACR02278.1; -; Genomic_DNA. DR RefSeq; YP_002890655.1; NC_011662.2. DR ProteinModelPortal; C4KC87; -. DR STRING; 85643.Tmz1t_3685; -. DR EnsemblBacteria; ACR02278; ACR02278; Tmz1t_3685. DR GeneID; 7873190; -. DR KEGG; tmz:Tmz1t_3685; -. DR PATRIC; 23883568; VBIThaSp83776_3609. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TSP85643:GHEJ-3654-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 21973 MW; 2E20DEACEED97F62 CRC64; MTERFPVRTL RGLYAVTPDE PDTGRLLALA QSVLAGHPAL LQYRNKGADA GLRREQALAL RDACRAAGVP FIVNDDLALA LAIDADGAHL GREDGPPAAA RAALGPQRIL GLTCYADWSR ATEGAEIGAD YIAFGAMFPS TTKPHAPPAP FALVERARRE LGLPVAAIGG ITLERAPQVI AAGADLLAVV GDVFGAADPA ARARMYRALF // ID C4KWQ7_BURPE Unreviewed; 367 AA. AC C4KWQ7; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=GBP346_A3863; OS Burkholderia pseudomallei MSHR346. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=536230; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MSHR346; RA Harkins D.M., Brinkac L.M., Rogers Y.C., Detter J.C., Munk A.C., RA Bruce D.C., Keim P., Sims D.R., Brettin T.S.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001408; ACQ95539.1; -; Genomic_DNA. DR RefSeq; YP_002898529.1; NC_012695.1. DR ProteinModelPortal; C4KWQ7; -. DR STRING; 536230.GBP346_A3863; -. DR EnsemblBacteria; ACQ95539; ACQ95539; GBP346_A3863. DR GeneID; 7887426; -. DR KEGG; bpr:GBP346_A3863; -. DR PATRIC; 32576474; VBIBurPse130472_3531. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BPSE536230:GHVQ-3855-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 367 AA; 38273 MW; 8C82851C6E850E63 CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGAQAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEVE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID C4KZE0_EXISA Unreviewed; 213 AA. AC C4KZE0; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EAT1b_1527; OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b). OC Bacteria; Firmicutes; Bacilli; Bacillales; OC Bacillales Family XII. Incertae Sedis; Exiguobacterium. OX NCBI_TaxID=360911; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1283 / AT1b; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Ramaley R.F., Rodrigues D.F., Vishnivetskaya T.A., RA Kathariou S., Tiedje J.M., Richardson P.; RT "Complete sequence of Exiguobacterium sp. AT1b."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001615; ACQ70453.1; -; Genomic_DNA. DR RefSeq; YP_002885898.1; NC_012673.1. DR ProteinModelPortal; C4KZE0; -. DR STRING; 360911.EAT1b_1527; -. DR EnsemblBacteria; ACQ70453; ACQ70453; EAT1b_1527. DR GeneID; 7869843; -. DR KEGG; eat:EAT1b_1527; -. DR PATRIC; 21878140; VBIExiSp39724_1506. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ESP360911:GI4R-1533-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22983 MW; 60FB5C23B92961C2 CRC64; MTFCTKQALA KQLRLYFVCG TTDASDLVAT VKTALLCGVT CFQFREKGKD ALYGDEKEAM ARTLHRLCRE AGVPFIVNDD VDLALAIDAD GIHVGQDDLP AKQVRERLGP DKWLGVSVHT MEEVRTALPF ADYVGIGPIH ETQSKLDAGQ VRGTELIQQV RRHHPLLPIV GIGGIRPEHV PAIMADGADG VAVISAIASA PDVATATRRF ACL // ID C4L8H8_TOLAT Unreviewed; 211 AA. AC C4L8H8; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tola_0218; OS Tolumonas auensis (strain DSM 9187 / TA4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Tolumonas. OX NCBI_TaxID=595494; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9187 / TA4; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Spring S., Beller H.; RT "Complete sequence of Tolumonas auensis DSM 9187."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001616; ACQ91848.1; -; Genomic_DNA. DR RefSeq; YP_002891434.1; NC_012691.1. DR ProteinModelPortal; C4L8H8; -. DR STRING; 595494.Tola_0218; -. DR EnsemblBacteria; ACQ91848; ACQ91848; Tola_0218. DR GeneID; 7885731; -. DR KEGG; tau:Tola_0218; -. DR PATRIC; 23977029; VBITolAue42623_0222. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TAUE595494:GHEF-235-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22539 MW; 50EF68EE8261AE58 CRC64; MKLDLSLYLV LDPVMCGGFD ATIKLTQQVL DAGVTVIQLR APQWKKRDWL RLSQQILPMS REARVPFLIN DHIDIALACD ADGVHLGQGD LPLAMARQLL GPDKILGLSI SKAHHLQGDD CLLADYLGIG PVFPTGTKQD ADPAIGLATF RDWMTQIHQP VVAIGGIGAS ETSDIIRAGA DGIAVVSAIC AVADPALATR TLGQLIHEAR P // ID C4LDA5_TOLAT Unreviewed; 218 AA. AC C4LDA5; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tola_1075; OS Tolumonas auensis (strain DSM 9187 / TA4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Tolumonas. OX NCBI_TaxID=595494; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9187 / TA4; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Spring S., Beller H.; RT "Complete sequence of Tolumonas auensis DSM 9187."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001616; ACQ92701.1; -; Genomic_DNA. DR RefSeq; YP_002892287.1; NC_012691.1. DR ProteinModelPortal; C4LDA5; -. DR STRING; 595494.Tola_1075; -. DR EnsemblBacteria; ACQ92701; ACQ92701; Tola_1075. DR GeneID; 7883617; -. DR KEGG; tau:Tola_1075; -. DR PATRIC; 23978761; VBITolAue42623_1069. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; TAUE595494:GHEF-1114-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23766 MW; C3833FB3B0B6F627 CRC64; MNPSFAFPKT DHQLGLYPVV DSVDWIARLL EWGVKTLQLR IKDPQAADLE QQIMQAIELG RRYQARLFIN DYWQLAIKHG AYGVHLGQED IQIADLDALR NAGLRLGIST HDPVELAEAL TIRPSYVALG HIFPTQTKDM PSQPQGLARL RECVLQSGDC PTVAIGGISE ERVPQVLATG VGSVALVSAI TKAADPQAAT ERLLRMVEGT TSGVTAYA // ID C4LKS6_CORK4 Unreviewed; 221 AA. AC C4LKS6; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ckrop_1710; OS Corynebacterium kroppenstedtii (strain DSM 44385 / CCUG 35717). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=645127; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44385 / CCUG 35717; RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004; RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P., RA Gartemann K.H., Arnold W., Blom J., Brinkrolf K., Brune I., Gotker S., RA Weisshaar B., Goesmann A., Droge M., Puhler A.; RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385 RT revealed insights into the physiology of a lipophilic corynebacterium RT that lacks mycolic acids."; RL J. Biotechnol. 136:22-30(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001620; ACR18431.1; -; Genomic_DNA. DR RefSeq; YP_002906974.1; NC_012704.1. DR ProteinModelPortal; C4LKS6; -. DR STRING; 645127.ckrop_1710; -. DR EnsemblBacteria; ACR18431; ACR18431; ckrop_1710. DR GeneID; 7877178; -. DR KEGG; ckp:ckrop_1710; -. DR PATRIC; 21518825; VBICorKro120627_1766. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6PZXB0; -. DR BioCyc; CKRO645127:GI7D-1688-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). SQ SEQUENCE 221 AA; 22924 MW; 4BF96C3A3DEC05A4 CRC64; MASTDTDFRL YLVTSGTDRH TVDTAAKVAA AGAGVVQVRA KDLSTRDLLS LVTECATAVH RANPHTKVVV DDRADVAYAA RRAGTPVNGV HLGLDDLPPD AARDMLGPDA LIGLTTGTLP LVEAAEEFHQ SHPGVIDYIG AGPFRPTPTK DSGRAPIGVD GYRPLVAATS LPIVAIGDVT PDDVAALSAT GIAGCAMVRA LMHADNPGDL ARRALESFRS E // ID C4R5Q8_PICPG Unreviewed; 560 AA. AC C4R5Q8; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 16-APR-2014, entry version 35. DE SubName: Full=Bifunctional enzyme; GN OrderedLocusNames=PAS_chr3_0843; OS Komagataella pastoris (strain GS115 / ATCC 20864) (Yeast) (Pichia OS pastoris). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Komagataella. OX NCBI_TaxID=644223; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GS115 / ATCC 20864; RX PubMed=19465926; DOI=10.1038/nbt.1544; RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S., RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.; RT "Genome sequence of the recombinant protein production host Pichia RT pastoris."; RL Nat. Biotechnol. 27:561-566(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN392321; CAY70894.1; -; Genomic_DNA. DR RefSeq; XP_002493073.1; XM_002493028.1. DR ProteinModelPortal; C4R5Q8; -. DR STRING; 644223.PAS_chr3_0843; -. DR EnsemblFungi; CAY70894; CAY70894; PAS_chr3_0843. DR GeneID; 8200332; -. DR KEGG; ppa:PAS_chr3_0843; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 560 AA; 60335 MW; 4B3FC58A6A014908 CRC64; MNRTDFDLSI YLVTNAEMVP EGLSFLDQVR KAIDNGVTTI QLREKNIETR DFIERASQVH ELTKAAGIPL IINDRVDVAL AVDAEGVHVG QTDMPVPLVR KLVGEDKIIG VSTGKVEEAR QAIKDGADYV GIGIVYDTKT KDHKKIPFGT LGIREILTVL LNEGGAGIKT CAIGGVNQTN VQKVLYQGSI PGKKLDGVAI VSCIMAQEDA AEATRVLVEK FHSHAPWLSD DHRADNDFFN NVTEKAKKVA DTNPMIHHIT NAVVKNFSAN VTLAVGASPI MSESYQEFEE FARLPTTGLV LNTGTQSAEN FVQMVIAAAK AYNATGNPIV FDPVGCGASE MRKHRTRLFL DAGYYTVIKG NVSEILTVAG EANQMRGVDT GDLSNLTEEA IVAAAKRAAL NNRCIVVVTG AVDYIVDGIL DGANYYESQP TQRVFKVQGG SSIMGDVTGT GCSLGSAIAA YITTFPATPL EATIAAVHHY KYVGAVAARR STTPNGISDS GPRPGSFMSN FLDDLYGFRT QESKVGHKIL LGPNPDKTFY TKLESSENGR YPAEVEEIFI // ID C4RAT8_9ACTO Unreviewed; 218 AA. AC C4RAT8; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 11-DEC-2013, entry version 24. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=MCAG_02047; OS Micromonospora sp. ATCC 39149. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Micromonospora. OX NCBI_TaxID=219305; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 39149; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., RA Walker S., Walsh C.T., Wieland-Brown L.C., Galagan J., Nusbaum C., RA Birren B.; RT "The genome sequence of Micromonospora carbonacea var. africana strain RT ATCC 39149."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657738; EEP71720.1; -; Genomic_DNA. DR ProteinModelPortal; C4RAT8; -. DR EnsemblBacteria; EEP71720; EEP71720; MCAG_02047. DR PATRIC; 26262061; VBIMicSp97049_1195. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 4: Predicted; SQ SEQUENCE 218 AA; 22185 MW; 1D7A625511D93876 CRC64; MTPGRSGGAD RSVGGPGGPR ARWWKVPVAG GVRWVVLREK DLPRAERAAL AADLRPILAE AGGTLVVAGP DPLGGDAVHL PAAGPYPPPP RRSLVGRSCH DAAELARLTT EDYVTLSPVY PSRSKPGYGP HLGPQGLGEL IRASTVPVLA LGGVETPAQV RACVDAGAVG VAVLGAIMRA GDPAEAAATL TAAYEEILPP RPATATPEDR ATATAGDR // ID C4RAU2_9ACTO Unreviewed; 208 AA. AC C4RAU2; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MCAG_02051; OS Micromonospora sp. ATCC 39149. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Micromonospora. OX NCBI_TaxID=219305; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 39149; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., RA Walker S., Walsh C.T., Wieland-Brown L.C., Galagan J., Nusbaum C., RA Birren B.; RT "The genome sequence of Micromonospora carbonacea var. africana strain RT ATCC 39149."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657738; EEP71724.1; -; Genomic_DNA. DR ProteinModelPortal; C4RAU2; -. DR EnsemblBacteria; EEP71724; EEP71724; MCAG_02051. DR PATRIC; 26262069; VBIMicSp97049_1199. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 20328 MW; DA567063331C5177 CRC64; MPSLGRLHLI TDTRPGRDPL AVLRAALPVA RAELVVQVRV TDDATDREAY DLAGRVVALC APYGATCLVN DRLHVALAVG AAGGHVGADD LPVAAARRVL GPTAVLGATA RAPGPAAEAE AAGASYLGVG PCHATDTKAG LPDPIGPAGV RAVARAVAVP VIAIGGVTAA GVPALRAAGA YGVAVVGALS AAVDPARVTA ELLGALTC // ID C4S4S2_YERBE Unreviewed; 197 AA. AC C4S4S2; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=yberc0001_1670; OS Yersinia bercovieri ATCC 43970. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=349968; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43970; RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., RA Willner K., Zwick M.E.; RT "Annotation of the Yersinia bercovieri ATCC 43970 genome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALC02000051; EEQ05572.1; -; Genomic_DNA. DR ProteinModelPortal; C4S4S2; -. DR EnsemblBacteria; EEQ05572; EEQ05572; yberc0001_1670. DR PATRIC; 26369416; VBIYerBer741_3156. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 117 119 THZ-P binding (By similarity). FT REGION 169 170 THZ-P binding (By similarity). FT METAL 53 53 Magnesium (By similarity). FT METAL 72 72 Magnesium (By similarity). FT BINDING 52 52 HMP-PP (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 197 AA; 21381 MW; B44010F325906E4F CRC64; MVDSLLWITR LLASGVTTIQ LRIKELDETE VEQDIAAAIE LGKRYNARLF INDYWRLAIK HGAYGVHLGQ EDLEIADLMA IQQAGLRLGV STHDEQELAL ARELRPSYIA LGHIFPTQTK QMPSAPQGVE ALARQVSNTP DYPTVAIGGI SLARVPQVVA SGVGSVAVVS AITQAADWQH ATAQLLQLVE GKESTYA // ID C4SGK0_YERMO Unreviewed; 203 AA. AC C4SGK0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ymoll0001_36630; OS Yersinia mollaretii ATCC 43969. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=349967; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43969; RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., RA Willner K., Zwick M.E.; RT "Annotation of the Yersinia mollaretii ATCC 43969 genome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALD02000042; EEQ09331.1; -; Genomic_DNA. DR ProteinModelPortal; C4SGK0; -. DR EnsemblBacteria; EEQ09331; EEQ09331; ymoll0001_36630. DR PATRIC; 29553830; VBIYerMol36980_3402. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 25 29 HMP-PP binding (By similarity). FT REGION 122 124 THZ-P binding (By similarity). FT REGION 174 175 THZ-P binding (By similarity). FT METAL 58 58 Magnesium (By similarity). FT METAL 77 77 Magnesium (By similarity). FT BINDING 57 57 HMP-PP (By similarity). FT BINDING 96 96 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). FT BINDING 154 154 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 22088 MW; F06D19FE07BEF3DA CRC64; MGLYPVVDSL LWITRLLASG VTTIQLRIKT LDEIQGEQDI AAAIALGKRY NARLFINDYW RLAIKHGAYG VHLGQEDLEV ADLVAIQQAG LRLGVSTHDE QELARARELR PSYIALGHIF PTQTKQMPSS PQGLAALTRQ VINTPDYPTV AIGGINLERV PQVVASGVGS VAVVSAITQA ADWQHATAQL LRLVEGKEST YAR // ID C4SV24_YERFR Unreviewed; 199 AA. AC C4SV24; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=yfred0001_22200; OS Yersinia frederiksenii ATCC 33641. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=349966; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33641; RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., RA Willner K., Zwick M.E.; RT "Annotation of the Yersinia frederiksenii ATCC 33641 genome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALE02000037; EEQ12966.1; -; Genomic_DNA. DR ProteinModelPortal; C4SV24; -. DR EnsemblBacteria; EEQ12966; EEQ12966; yfred0001_22200. DR PATRIC; 26379959; VBIYerFre50381_4160. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 19 23 HMP-PP binding (By similarity). FT REGION 116 118 THZ-P binding (By similarity). FT REGION 168 169 THZ-P binding (By similarity). FT METAL 52 52 Magnesium (By similarity). FT METAL 71 71 Magnesium (By similarity). FT BINDING 51 51 HMP-PP (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 199 AA; 21515 MW; 597B7A2A4429693F CRC64; MDSLLWIERL LAAGVTTIQL RIKDLADAQV EQDIAAAIEL GKRYQARLFI NDYWRLAIKH GAYGVHLGQE DLETTDLAAI QQAGLRLGVS THDEHELAIA KAVRPSYIAM GHIFPTQTKQ MPSSPQGLAV LKQMVDNTPD YPTVAIGGIS IARVPAVLAT GVGSVAVVSA ITQADDWQQA TAQLLHLIEG KELSDDQQA // ID C4T6Y7_YERIN Unreviewed; 170 AA. AC C4T6Y7; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-OCT-2013, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=yinte0001_41350; OS Yersinia intermedia ATCC 29909. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=349965; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29909; RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., RA Willner K., Zwick M.E.; RT "Annotation of the Yersinia intermedia ATCC 29909 genome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALF02000043; EEQ17268.1; -; Genomic_DNA. DR ProteinModelPortal; C4T6Y7; -. DR EnsemblBacteria; EEQ17268; EEQ17268; yinte0001_41350. DR PATRIC; 36092817; VBIYerInt66761_3956. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 170 AA; 18286 MW; DB1B62A0224B964F CRC64; MEQDIAAAIA LGKRYQARLF INDYWRLAIK HGAYGVHLGQ EDLETADLAA IQQAGLRLGV STHDEQELAI AKAVRPSYIA MGHIFPTQTK QMPSSPQGLT VLKQMVDNTP DYPTVAIGGI SIERVPAVLA TGVGSVAVVS AITLSDDWQQ ATAQLLHLIE GKELADDKQA // ID C4U2N9_YERKR Unreviewed; 200 AA. AC C4U2N9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ykris0001_44380; OS Yersinia kristensenii ATCC 33638. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=527012; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33638; RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., RA Willner K., Zwick M.E.; RT "Annotation of the Yersinia kristensenii ATCC 33638 genome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCA01000052; EEP89253.1; -; Genomic_DNA. DR ProteinModelPortal; C4U2N9; -. DR EnsemblBacteria; EEP89253; EEP89253; ykris0001_44380. DR PATRIC; 26389964; VBIYerKri124070_4454. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 117 119 THZ-P binding (By similarity). FT REGION 169 170 THZ-P binding (By similarity). FT METAL 53 53 Magnesium (By similarity). FT METAL 72 72 Magnesium (By similarity). FT BINDING 52 52 HMP-PP (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 200 AA; 21750 MW; E6F84DA2C4430CD1 CRC64; MVDSVLWIER LLAAGVTTIQ LRIKALEDAQ VEQDIATAIQ LGKRYQARLF INDYWRLAIK HGAYGVHLGQ EDLETTDLAA IQQAGLRLGV STHDEHELAI AKAVRPSYIA MGHIFPTQTK QMPSSPQGLA VLKQMVDNTP DYPTVAIGGI SVERVPAVLA TGVGSVAVVS AITQADNWQQ VTAQLLHLIE GKERADDQHA // ID C4UD43_YERAL Unreviewed; 128 AA. AC C4UD43; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=yaldo0001_30860; OS Yersinia aldovae ATCC 35236. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=527002; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35236; RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., RA Willner K., Zwick M.E.; RT "Annotation of the Yersinia aldovae ATCC 35236 genome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCB01000045; EEP94099.1; -; Genomic_DNA. DR EnsemblBacteria; EEP94099; EEP94099; yaldo0001_30860. DR PATRIC; 26361607; VBIYerAld45352_3564. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 128 AA; 13541 MW; 6A8C6698CFC3BCB3 CRC64; METTDLAAIQ QAGLRLGVST HDDQELAIAK AVRPSYIAIG HIFPTQTKQM PSSPQGLAVL KQMVENTPDY PTVAIGGISI ERVPAVLATG VGSVAVVSAI TQAEDWQQAT AQLLHLIEGK ELVDDKQA // ID C4UMJ6_YERRU Unreviewed; 202 AA. AC C4UMJ6; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=yruck0001_1400; OS Yersinia ruckeri ATCC 29473. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=527005; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29473; RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., RA Willner K., Zwick M.E.; RT "Annotation of the Yersinia ruckeri ATCC 29473 genome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCC01000041; EEP98115.1; -; Genomic_DNA. DR ProteinModelPortal; C4UMJ6; -. DR EnsemblBacteria; EEP98115; EEP98115; yruck0001_1400. DR PATRIC; 31314463; VBIYerRuc77443_2760. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 25 29 HMP-PP binding (By similarity). FT REGION 122 124 THZ-P binding (By similarity). FT REGION 174 175 THZ-P binding (By similarity). FT METAL 58 58 Magnesium (By similarity). FT METAL 77 77 Magnesium (By similarity). FT BINDING 57 57 HMP-PP (By similarity). FT BINDING 96 96 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). FT BINDING 154 154 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 202 AA; 21869 MW; A02820CEB74296B3 CRC64; MGLYPVVDSL LWIARLLDAG VTTLQLRIKD ANDVQVEDTI AAAISLATSY QARLFINDYW QLAIQQGAYG VHLGQEDLEI ADLPAIQRAG LRLGISTHNE YELALARNLQ PSYIALGHIF PTQTKQMPSA PQGVEALTRQ VINTPDYPTV AIGGINLERV PQVIASGVGS IAVVSAITQA ADWQYATGQL LRLVEGKEST YA // ID C4UZA0_YERRO Unreviewed; 200 AA. AC C4UZA0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=yrohd0001_8750; OS Yersinia rohdei ATCC 43380. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=527004; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43380; RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., RA Willner K., Zwick M.E.; RT "Annotation of the Yersinia rohdei ATCC 43380 genome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCD01000038; EEQ01243.1; -; Genomic_DNA. DR ProteinModelPortal; C4UZA0; -. DR EnsemblBacteria; EEQ01243; EEQ01243; yrohd0001_8750. DR PATRIC; 30871067; VBIYerRoh124190_3592. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 117 119 THZ-P binding (By similarity). FT REGION 169 170 THZ-P binding (By similarity). FT METAL 53 53 Magnesium (By similarity). FT METAL 72 72 Magnesium (By similarity). FT BINDING 52 52 HMP-PP (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 200 AA; 21792 MW; 2783E8F162854146 CRC64; MVDSLLWIER LLSVGVTTIQ LRIKDLDDAQ VEQDIAAAIE LGKRYQARLF INDYWRLAIK HGAYGVHLGQ EDLETTDLAA IQQAGLRLGV STHDEHELAI AKAVRPSYIA MGHIFPTQTK QMPSSPQGLA ILKQMVDNTP EYPTVAIGGI SLERVPAVLA TGVGSVAVVS AITQADDWQQ ATAQLLQLIE GKERTDAQQA // ID C4V5F3_9FIRM Unreviewed; 219 AA. AC C4V5F3; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0908_1747; OS Selenomonas flueggei ATCC 43531. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=638302; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43531; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLA01000029; EEQ47930.1; -; Genomic_DNA. DR ProteinModelPortal; C4V5F3; -. DR EnsemblBacteria; EEQ47930; EEQ47930; HMPREF0908_1747. DR PATRIC; 25818980; VBISelFlu67833_1477. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23589 MW; 22BB30A750FFF454 CRC64; MSEMAVRKDD LLLYAVTDRR WLHGKRLYDA AESALQGGVT FLQLREKSAG TMPRASLLKE ARELLTLCRR YRVPFVIDDD VELAMAIGAD GVHVGQSDME AGTARRRIGK DKILGVSVQT VKEARIAAAC GADYLGVGAV FPTDSKEDAE IVRYETLKEI CSAAAVPVVA IGGINDENVM QLAGSGIAGI AVISAIFAKK DIRIAAQRLL CKVKEAKGR // ID C4W861_STAWA Unreviewed; 196 AA. AC C4W861; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=STAWA0001_1824; OS Staphylococcus warneri L37603. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=596319; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L37603; RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACPZ01000015; EEQ80873.1; -; Genomic_DNA. DR ProteinModelPortal; C4W861; -. DR EnsemblBacteria; EEQ80873; EEQ80873; STAWA0001_1824. DR PATRIC; 31409614; VBIStaWar127182_0331. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 22393 MW; A635A6FF2ACA283D CRC64; MYIFIAITYY KELSLQDLKH FMTIEPAIDG LLFRTPMSTL ALQRFITRLI AVGFPKDKIM IHSNLNLLKA LNLQCIHFKE NDKRAFLLKQ QYPELIVGMS THNIEMVKQC HAHQLDYVFF GHIFSTSSHP GEPPRTNQEI HDVLKIDMPI YAIGGISPST ISQLPTGFDG LCAISFFMTS TVSDINSLKR KWHSHA // ID C4WBP5_STAWA Unreviewed; 213 AA. AC C4WBP5; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=STAWA0001_0026; OS Staphylococcus warneri L37603. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=596319; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L37603; RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACPZ01000047; EEQ79500.1; -; Genomic_DNA. DR ProteinModelPortal; C4WBP5; -. DR EnsemblBacteria; EEQ79500; EEQ79500; STAWA0001_0026. DR PATRIC; 31412126; VBIStaWar127182_1549. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23171 MW; A819EF4D86D6942D CRC64; MSFKATDLKI YFICGTQDIP EHQTIQGILT QALEAGITMF QFREKGDKAL TGLKKEKLAK ELQALCQSYD VPFIVNDDVS LAKSINADGI HVGQDDEDVR ALANDFQEKI IGLSVGNLNE YEKSDLTNVD YIGVGPMFET PSKSDASAPV GPDMITQLRQ KMGDFPMVAI GGINEENVAL IANAGADGIS VISAISKSNN IDNTVNEFKK YFN // ID C4WH28_9RHIZ Unreviewed; 209 AA. AC C4WH28; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-MAR-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=OINT_1000226; OS Ochrobactrum intermedium LMG 3301. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Ochrobactrum. OX NCBI_TaxID=641118; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 3301; RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., RA Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Munk C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Tsolis R.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACQA01000001; EEQ94892.1; -; Genomic_DNA. DR ProteinModelPortal; C4WH28; -. DR EnsemblBacteria; EEQ94892; EEQ94892; OINT_1000226. DR PATRIC; 28504650; VBIOchInt64846_0234. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 209 AA; 23241 MW; 79AF8A93B052AD44 CRC64; MALDPFYPIF DSASWLERMV PLGVRLVQLR IKDKSEPELR GEIRAAREIC LAHDCQLVVN DYWKLALEEG CDFIHLGQED LDDADLDAIR AGGLKLGVSS HDEAELDRAL SVKPDYIALG PVYPTILKKM KWHEQGLPRI GQWKARIGDI PLVGIGGMSV ERAPGVFEAG ADIVSVVTDI TLNADPESRL RQWIETTRAY AGHALEQTL // ID C4WHW4_9RHIZ Unreviewed; 221 AA. AC C4WHW4; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-MAR-2014, entry version 22. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=OINT_1002082; OS Ochrobactrum intermedium LMG 3301. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Ochrobactrum. OX NCBI_TaxID=641118; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 3301; RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., RA Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Munk C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Tsolis R.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACQA01000001; EEQ96630.1; -; Genomic_DNA. DR ProteinModelPortal; C4WHW4; -. DR EnsemblBacteria; EEQ96630; EEQ96630; OINT_1002082. DR PATRIC; 28508464; VBIOchInt64846_2101. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23170 MW; 4E96F7A240A6AC06 CRC64; MNTPAHQTET DRCRIVLVAP PLADGAALAK LLTAALSGGD VASVILDPGD LDEATFQAAA EKAIPVIQEK GAAALILNDT RIAGRVGADG IHIEGKAADL AEAIEKHTPK MIVGTGNLRD RHGAMEIGEL QPDYVFFGKI GADNKPDAHP RNLALAEWWA QMVEIPCIAQ AGSALESIIP AAETGADFVA LGRAVFDAED PAQAVAEANR LLDEKAPRFE N // ID C4WZZ6_KLEPN Unreviewed; 211 AA. AC C4WZZ6; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=KP1_0233; OS Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=484021; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NTUH-K2044; RA Wu K.M., Tsai S.F.; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NTUH-K2044; RX PubMed=19447910; DOI=10.1128/JB.00315-09; RA Wu K.-M., Li L.-H., Yan J.-J., Tsao N., Liao T.-L., Tsai H.-C., RA Fung C.-P., Chen H.-J., Liu Y.-M., Wang J.-T., Fang C.-T., RA Chang S.-C., Shu H.-Y., Liu T.-T., Chen Y.-T., Shiau Y.-R., RA Lauderdale T.-L., Su I.-J., Kirby R., Tsai S.-F.; RT "Genome sequencing and comparative analysis of Klebsiella pneumoniae RT NTUH-K2044, a strain causing liver abscess and meningitis."; RL J. Bacteriol. 191:4492-4501(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006725; BAH61135.1; -; Genomic_DNA. DR RefSeq; YP_002917202.1; NC_012731.1. DR ProteinModelPortal; C4WZZ6; -. DR STRING; 484021.KP1_0233; -. DR EnsemblBacteria; BAH61135; BAH61135; KP1_0233. DR GeneID; 7948725; -. DR KEGG; kpu:KP1_0233; -. DR PATRIC; 20444693; VBIKlePne21779_0208. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; KPNE484021:GCWL-237-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 21B54D01518D3CB0 CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIERLLE AGVRTLQLRI KDRRDSEVED DVIAAIALGR RYHARLFIND YWQLAIKHQA YGVHLGQEDL ETTDLSAIRQ AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIQRLADYP TVAIGGISLE KAPGVLATGV GSIAVVSAIT QAADWRAATD QLLALAGAGD E // ID C4Y5T8_CLAL4 Unreviewed; 505 AA. AC C4Y5T8; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-APR-2014, entry version 28. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=CLUG_03522; OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida OS lusitaniae). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Metschnikowiaceae; Clavispora. OX NCBI_TaxID=306902; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 42720; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., RA Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., RA Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D., RA Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., RA Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., RA Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., RA Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., RA Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., RA Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., RA Kellis M., Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH408079; EEQ39394.1; -; Genomic_DNA. DR RefSeq; XP_002616281.1; XM_002616235.1. DR ProteinModelPortal; C4Y5T8; -. DR GeneID; 8497172; -. DR KEGG; clu:CLUG_03522; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 505 AA; 53746 MW; 996C0113B362CFF1 CRC64; MAKMKLDLSA YLVTDSTMIP ESSSFLSQVQ QAVENGVTIV QLREKNISTR DFIDRAKDVL KITRPRGVPL IINDRVDVAL AVDADGVHVG QDDMPARIVR QLIGPHKILG VSCGNEEETT EVCEQKVADY VGLGTLYPTQ TKDVKNVCGP IGVRRSLQVL KKYKEQGTYV QSVAIGGINS SNASKVMYQC RVPGYAVNGV AFVSCIMAAP DATQATKKLL DQLKNSPPWV TASTATLESL QSKPLVHHIT NNVVKHFSAN VTLAVGGSPI MSELPDEFDE LASLPLPTAL VINLGTPSST LMSVFLEGIK VYNNHGRPIV FDPVAAGASK ARLDACRVLL NAGQVSVIKG NLGEILAIDK LTSSSPFAKE ANLMRGVDSV AEMGPAEISE VCKRVALEFQ CVTVITGEVN HIFDGTRPDS QVVTIQGGSP LMGSVVGIGC ALGSVIGVFV ACAQAQKAQL GQAVELALKV YNSAGRQAAV DHKQGLGSYM IKFLDELSES AKPYA // ID C4YQ52_CANAW Unreviewed; 514 AA. AC C4YQ52; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-APR-2014, entry version 28. DE SubName: Full=Uncharacterized protein; GN ORFNames=CAWG_02606; OS Candida albicans (strain WO-1) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; OC Candida. OX NCBI_TaxID=294748; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WO-1; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., RA Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., RA Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D., RA Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., RA Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., RA Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., RA Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., RA Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., RA Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., RA Kellis M., Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000310; EEQ44341.1; -; Genomic_DNA. DR ProteinModelPortal; C4YQ52; -. DR HOGENOM; HOG000214306; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 514 AA; 55473 MW; 773C6CEBF0C9CBE6 CRC64; MTLSKMKVDY TLYLVTDSGM VPESSSFLKQ VEDSINSGAT IVQLREKSLS TLEFIKRAEQ VHKLTQKQGI PLIINDRVDV ALAVNAEGVH VGQDDMPAAI ARKLIGDDKI LGVTCSNVTE VQEVVEQGIA DYVGLGTVYK TNTKKDVTDP EGTGPSGIRR MLRVLQKHNS KSGAKKIQSV AIGGINHSNV RNVMFQCAVP GEKINGVAVV SCIMANENAA EATLLLSQLI SSAPYGYEPY EESQYLDDYQ HSLKQLSSSS PMIHHITNNV VKNFSANVTL AIGASPIMSE FDEEFNELAS TPNTALVLNL GTPSKEMMKI FKNSIIAHQS RNPIVFDPVG CGASKGRLKC CRQLLDTGYF AVIKGNVGEI SALRKLTSSY RESQSKSYMR GVDSISNLTE EEIIEIGKDV SIEFKAVVVI TGPTNYIIEG EDKVVKVEGG NKLMGSITGS GCALGSTIAA FVSSQARSPQ GPNNFYAAVH AVKLYNKAGA AVSEKTPGKF MASFIDELYK LTHS // ID C4Z3M4_EUBE2 Unreviewed; 208 AA. AC C4Z3M4; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=EUBELI_00479; OS Eubacterium eligens (strain ATCC 27750 / VPI C15-48). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=515620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27750 / VPI C15-48; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of RT its two dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001104; ACR71493.1; -; Genomic_DNA. DR RefSeq; YP_002929940.1; NC_012778.1. DR ProteinModelPortal; C4Z3M4; -. DR STRING; 515620.EUBELI_00479; -. DR EnsemblBacteria; ACR71493; ACR71493; EUBELI_00479. DR GeneID; 7957592; -. DR KEGG; eel:EUBELI_00479; -. DR PATRIC; 21864144; VBIEubEli113401_0438. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEEAVIA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; EELI515620:GH1N-479-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 23172 MW; A3F8223434909684 CRC64; MNTFMYRKYI CITNKHLVSG SGGAECTMNE YIMQLEKCVA LHPYAMILRE KDMDRQNYRK LARRIQVMCK KASVKMFVHS DISAAEYAGC GNVHFSMEHF KQMCDEQADV IKGLDCMSVS CHSMEEAVIA VRAGADQIVL GTIFETQCKP GKMGAGLSFL EEVCRAVHTV NPTVKVFAIG GIKPDNIEEV LEAGADGGCM MSWFMQQD // ID C4Z6C0_EUBE2 Unreviewed; 446 AA. AC C4Z6C0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=EUBELI_20367; OS Eubacterium eligens (strain ATCC 27750 / VPI C15-48). OG Plasmid pEubeli2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=515620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27750 / VPI C15-48; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of RT its two dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001106; ACR73512.1; -; Genomic_DNA. DR RefSeq; YP_002935646.1; NC_012780.1. DR ProteinModelPortal; C4Z6C0; -. DR STRING; 515620.EUBELI_20367; -. DR EnsemblBacteria; ACR73512; ACR73512; EUBELI_20367. DR GeneID; 7962874; -. DR KEGG; eel:EUBELI_20367; -. DR PATRIC; 21867873; VBIEubEli113401_2275. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; EELI515620:GH1N-2434-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF13419; HAD_2; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Plasmid; Thiamine biosynthesis; Transferase. SQ SEQUENCE 446 AA; 49849 MW; 28236D2582F70C5A CRC64; MCQKMYAKGT GRCVIIHIEF DSGELIMIRK EQLRLYAITD TSWLNGASLI DVVENVLKNG ATFLQLREKN ATHEEIVAKA KAIKPITRKY GIPFVIDDDV QAALEADADG VHIGQSDTDY MTARSILGDN KIIGMTAKTV EQAKEAEKLG ADYIGTGAVF GSSTKKDAVY MPRERLIEVA GSVNIPVVAI GGIDYDNCGE LAGTGVDGIA VVSAIFAADD PGLATKELYL KTGRVFNYHR DFIFDMDGTI LDSMPYWRNV SKEYAMQYVD KLPDDFDERT YVMDLDECSA YFRDELGIST DAATMRQTAV DIMTRHYSTD IPAKDGMLEL IRREHEAGSD MCIFTSSDRG CVDAALNRLG ITDCFNNIFT VYDIPYNKKN PESYKLIAEK MHFKPEDTWV YEDVLHGIES AKQGGFKICA VYDEDSKKHW NEICAFADEI RDIRND // ID C4ZAG5_EUBR3 Unreviewed; 242 AA. AC C4ZAG5; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=EUBREC_0222; OS Eubacterium rectale (strain ATCC 33656 / VPI 0990). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=515619; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33656 / VPI 0990; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of RT its two dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001107; ACR74026.1; -; Genomic_DNA. DR RefSeq; YP_002936160.1; NC_012781.1. DR ProteinModelPortal; C4ZAG5; -. DR STRING; 515619.EUBREC_0222; -. DR EnsemblBacteria; ACR74026; ACR74026; EUBREC_0222. DR GeneID; 7964482; -. DR KEGG; ere:EUBREC_0222; -. DR PATRIC; 21869001; VBIEubRec107985_0200. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; EREC515619:GHMX-221-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 242 AA; 26685 MW; 8227E32055FE339A CRC64; MNKEKLLYEY ENSKHALQSD NIIAITNRHL CSRPFMEQLE RVCKLHPHAI VLREKDMPEA EYLSLARDVI ALCKKYDVQC MLHSFINVAM ELEHPYIHLP LPILEAYVKK NVSGNISTGM SKSTDNYQQF FKVIGTSVHS VEDAIKAEQL GATYMTAGHI FATDCKKGLP PRGLDFLKNV CDAVGIPVYA IGGINIASND DSTASDSPST YDAVPDISVP RLADVMECGA AGGCIMSGMM RV // ID C4ZG54_EUBR3 Unreviewed; 216 AA. AC C4ZG54; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EUBREC_2529; OS Eubacterium rectale (strain ATCC 33656 / VPI 0990). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=515619; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33656 / VPI 0990; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of RT its two dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001107; ACR76260.1; -; Genomic_DNA. DR RefSeq; YP_002938394.1; NC_012781.1. DR ProteinModelPortal; C4ZG54; -. DR STRING; 515619.EUBREC_2529; -. DR EnsemblBacteria; ACR76260; ACR76260; EUBREC_2529. DR GeneID; 7966554; -. DR KEGG; ere:EUBREC_2529; -. DR PATRIC; 21873117; VBIEubRec107985_2198. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; EREC515619:GHMX-2518-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22841 MW; C44372DD8B3D9DC5 CRC64; MNETDLKLYA ITDRQWLHGA RLSEHVKLAI EGGATMIQIR DKDILSTDSD AGLKDEYSEA LEIKRICHEH KVPLIINDNV QFAIDIAADG VHLGQDDMNP AEARKLLGTD KIIGVTAKTV EQAKRAEADG ADYLGSGAVF GSTTKLNAKP MTKELLREIT AAVDIPVVAI GGINADNAVT LKGTGIAGIA VVGAIFASAD IKAAAKELAG ICDKIL // ID C5A0T4_ECOBW Unreviewed; 211 AA. AC C5A0T4; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BWG_3653; OS Escherichia coli (strain K12 / MC4100 / BW2952). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=595496; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MC4100 / BW2952; RX PubMed=19376874; DOI=10.1128/JB.00118-09; RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., RA Reeves P.R., Wang L.; RT "Genomic sequencing reveals regulatory mutations and recombinational RT events in the widely used MC4100 lineage of Escherichia coli K-12."; RL J. Bacteriol. 191:4025-4029(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001396; ACR65636.1; -; Genomic_DNA. DR RefSeq; YP_002928846.1; NC_012759.1. DR ProteinModelPortal; C5A0T4; -. DR SMR; C5A0T4; 20-202. DR STRING; 595496.BWG_3653; -. DR EnsemblBacteria; ACR65636; ACR65636; BWG_3653. DR GeneID; 7956123; -. DR KEGG; ebw:BWG_3653; -. DR PATRIC; 18277051; VBIEscCol60876_3991. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL595496:GI18-3810-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID C5A9L9_BURGB Unreviewed; 365 AA. AC C5A9L9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=bglu_1g03190; OS Burkholderia glumae (strain BGR1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=626418; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGR1; RX PubMed=19329631; DOI=10.1128/JB.00349-09; RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.; RT "Complete genome sequence of Burkholderia glumae BGR1."; RL J. Bacteriol. 191:3758-3759(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001503; ACR27520.1; -; Genomic_DNA. DR RefSeq; YP_002910224.1; NC_012724.2. DR ProteinModelPortal; C5A9L9; -. DR STRING; 626418.bglu_1g03190; -. DR EnsemblBacteria; ACR27520; ACR27520; bglu_1g03190. DR GeneID; 7907654; -. DR KEGG; bgl:bglu_1g03190; -. DR PATRIC; 19107960; VBIBurGlu130723_3081. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR BioCyc; BGLU626418:GJI5-330-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 365 AA; 37824 MW; 20EC9853EFA48BC5 CRC64; MSTGFGDMFW PPVDDLAAAA ERIRARLGEW PVRRAPMRIC VAAPERAQPG DLLVVTSGDA EAGRAAEVIA AGGAALEIDE RHATLTHAGA RYALTAAAPL ADDWIAALAA FADCGFEAHD ALVLALAWRD GDEAADGDPW PTDPARFPSI AAAPGAPEPA FAPCPARLGL YPVVPSAEWV ERVLDYGART VQLRVKDAAP NALAAEIARA VAAGRRYPEA RVFINDHWRL AIEAGAYGVH LGQEDLQEAG LGAIAAAGLR LGLSSHGYYE MLVALRLRPS YLALGPVFAT ATKAVAAPPQ GLARLARYAR FAGRRAPLVA IGGVTAASLP EVIAAGVGSV AVVSAITQAA DPRAAVGALA ACFER // ID C5AJ91_BURGB Unreviewed; 203 AA. AC C5AJ91; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN OrderedLocusNames=bglu_2g16310; OS Burkholderia glumae (strain BGR1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=626418; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGR1; RX PubMed=19329631; DOI=10.1128/JB.00349-09; RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.; RT "Complete genome sequence of Burkholderia glumae BGR1."; RL J. Bacteriol. 191:3758-3759(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001504; ACR31971.1; -; Genomic_DNA. DR RefSeq; YP_002909206.1; NC_012721.2. DR ProteinModelPortal; C5AJ91; -. DR STRING; 626418.bglu_2g16310; -. DR EnsemblBacteria; ACR31971; ACR31971; bglu_2g16310. DR GeneID; 7903080; -. DR KEGG; bgl:bglu_2g16310; -. DR PATRIC; 19105612; VBIBurGlu130723_1920. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BGLU626418:GJI5-5132-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 203 AA; 20566 MW; 89B2602C3B4859C2 CRC64; MCGSEPVPTP ALPPLYLITP EPASNARADL DAFVSRLDAA FATGIALVQL RVKTFDAADY AALAERVIGR AHAAGARVVC NGPVTLQAAR ALGADGIHFG HAALAAAASR PEAAGLLLSA ACHDAASLRH ADRIGADLAT LSPVKPTLSH PGAPGLGWPR FAEWVAGTRL AVYALGGMTR DDLPIARAHG AHGVAGIRGL VAG // ID C5AQQ7_METEA Unreviewed; 222 AA. AC C5AQQ7; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase (TMP pyrophosphorylase) (TMP-PPase) (Thiamine-phosphate synthase); GN OrderedLocusNames=MexAM1_META1p2371; OS Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=272630; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14718 / DSM 1338 / AM1; RX PubMed=19440302; DOI=10.1371/journal.pone.0005584; RA Vuilleumier S., Chistoserdova L., Lee M.C., Bringel F., Lajus A., RA Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., RA Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., RA Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., RA Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., RA Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., RA Medigue C., Lidstrom M.E.; RT "Methylobacterium genome sequences: a reference blueprint to RT investigate microbial metabolism of C1 compounds from natural and RT industrial sources."; RL PLoS ONE 4:E5584-E5584(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001510; ACS40154.1; -; Genomic_DNA. DR RefSeq; YP_002963431.1; NC_012808.1. DR ProteinModelPortal; C5AQQ7; -. DR STRING; 272630.MexAM1_META1p2371; -. DR EnsemblBacteria; ACS40154; ACS40154; MexAM1_META1p2371. DR GeneID; 7992278; -. DR KEGG; mea:Mex_1p2371; -. DR PATRIC; 22510515; VBIMetExt101010_2329. DR eggNOG; NOG280778; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; MEXT272630:GBY6-2238-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 222 AA; 22870 MW; 7F842D26C8146888 CRC64; MAESESAAPR PRLALLTPYG LGASEAEATA RALDAACAAG DVAAVILRLA ASDERSLVAL VKRLAPPAQE RGAAVLVSVP GFTGDIVSVA ARGGADGVHL DRADEEALRD LRGRLRDGRI LGTGGVLGSR NAAMVAGETG VDYLMVGGLF PDGVAPDAEE VRERAAWWAE IFETPCIAVA TSAEDVAALV LTGSEFVGLE SALWLDDPEG VRAAQAQLDR AR // ID C5ASR0_METEA Unreviewed; 241 AA. AC C5ASR0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MexAM1_META1p4916; OS Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=272630; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14718 / DSM 1338 / AM1; RX PubMed=19440302; DOI=10.1371/journal.pone.0005584; RA Vuilleumier S., Chistoserdova L., Lee M.C., Bringel F., Lajus A., RA Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., RA Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., RA Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., RA Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., RA Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., RA Medigue C., Lidstrom M.E.; RT "Methylobacterium genome sequences: a reference blueprint to RT investigate microbial metabolism of C1 compounds from natural and RT industrial sources."; RL PLoS ONE 4:E5584-E5584(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001510; ACS42523.1; -; Genomic_DNA. DR RefSeq; YP_002965800.1; NC_012808.1. DR ProteinModelPortal; C5ASR0; -. DR STRING; 272630.MexAM1_META1p4916; -. DR EnsemblBacteria; ACS42523; ACS42523; MexAM1_META1p4916. DR GeneID; 7994685; -. DR KEGG; mea:Mex_1p4916; -. DR PATRIC; 22515467; VBIMetExt101010_4783. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MEXT272630:GBY6-4644-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT METAL 87 87 Magnesium (By similarity). FT METAL 106 106 Magnesium (By similarity). FT BINDING 86 86 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 241 AA; 24468 MW; 0265DCCA37059A80 CRC64; MGSGTGLGLS RPSAGVALDL RLYGILDVGV LGGDATALAT LAAEAVAGGA TLLQYRDKDL TDARAALARI RAIHAALAGR APLLVNDRVD LALAAGVEGV HLGQSDLHPE DARRLLGPRA IIGLTVKTGA QADELYRLPI DYACIGGVFA TTSKDNPDPP VGLDGLQRIV FRARLARGQS LPLGAIAGID ASNTASVIRA GADGVALIGA LFKGGATEAK ARDLLARVDE ALGQRGSTGT R // ID C5AT60_METEA Unreviewed; 205 AA. AC C5AT60; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MexAM1_META1p0427; OS Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=272630; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14718 / DSM 1338 / AM1; RX PubMed=19440302; DOI=10.1371/journal.pone.0005584; RA Vuilleumier S., Chistoserdova L., Lee M.C., Bringel F., Lajus A., RA Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., RA Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., RA Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., RA Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., RA Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., RA Medigue C., Lidstrom M.E.; RT "Methylobacterium genome sequences: a reference blueprint to RT investigate microbial metabolism of C1 compounds from natural and RT industrial sources."; RL PLoS ONE 4:E5584-E5584(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001510; ACS38370.1; -; Genomic_DNA. DR RefSeq; YP_002961647.1; NC_012808.1. DR ProteinModelPortal; C5AT60; -. DR STRING; 272630.MexAM1_META1p0427; -. DR EnsemblBacteria; ACS38370; ACS38370; MexAM1_META1p0427. DR GeneID; 7990447; -. DR KEGG; mea:Mex_1p0427; -. DR PATRIC; 22506685; VBIMetExt101010_0452. DR eggNOG; NOG131844; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MEXT272630:GBY6-410-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 134 136 THZ-P binding (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 20364 MW; 801781346B1F380C CRC64; MTLPPLLVVT DRHGAARPLT ETVRAAVAGG ARFVWLRDRD LDRDARRDLA RDLIGLLQPV GGRLVVGGDT DLAAEIGAQG VHLSSSAGID GIRAARMALG AAALIGFSAH SVAEIAAAGA AGADYATLSP IFPTASKPGY GPALGLASLR AAAAHGVPVF ALGGIDGGNA RACREAGAAG VAVMGGVMRG SDPRAATGRF VAALT // ID C5BHE5_EDWI9 Unreviewed; 214 AA. AC C5BHE5; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NT01EI_0176; OS Edwardsiella ictaluri (strain 93-146). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Edwardsiella. OX NCBI_TaxID=634503; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=93-146; RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C., RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.; RT "Complete genome sequence of Edwardsiella ictaluri 93-146."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001600; ACR67423.1; -; Genomic_DNA. DR RefSeq; YP_002931658.1; NC_012779.2. DR ProteinModelPortal; C5BHE5; -. DR STRING; 634503.NT01EI_0176; -. DR EnsemblBacteria; ACR67423; ACR67423; NT01EI_0176. DR GeneID; 7958768; -. DR KEGG; eic:NT01EI_0176; -. DR PATRIC; 21833636; VBIEdwIct114273_0159. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; EICT634503:GCMY-174-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23465 MW; D3A7AE9EA1D75AE6 CRC64; MAQPVFAPVP MRLGLYPIVD SVEWIERLLR AGVRTLQLRI KDCREDQIGD EIAQAIALGR HYQARLFIND YWRPAIRLGA YGVHLGQEDL DQADLAAIRR AGLRLGLSTH DDAEMDRALA EGPSYVALGH VFPTDSKLMD TAPQGLSDLR RQMTRLDTYP SVAIGGISIA RVPDVLACGV GSIALVSAIT RAPDWLAATD TLLQLIEGRR ANDV // ID C5BP24_TERTT Unreviewed; 319 AA. AC C5BP24; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-APR-2014, entry version 43. DE SubName: Full=Fusion of MutT/nudix family protein and thiamine monophosphate synthase; GN OrderedLocusNames=TERTU_3038; OS Teredinibacter turnerae (strain ATCC 39867 / T7901). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadales genera incertae sedis; Teredinibacter. OX NCBI_TaxID=377629; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39867 / T7901; RX PubMed=19568419; DOI=10.1371/journal.pone.0006085; RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S., RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M., RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A., Elshahawi S., RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., RA Madinger C., Nove J., Anton B., Chaudhary K., Foster J., Holman A., RA Kumar S., Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., RA Teplitski M., Mougous J.D., Ward N., Eisen J.A., Badger J.H., RA Distel D.L.; RT "The complete genome of Teredinibacter turnerae T7901: an RT intracellular endosymbiont of marine wood-boring bivalves RT (shipworms)."; RL PLoS ONE 4:E6085-E6085(2009). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001614; ACR11253.1; -; Genomic_DNA. DR RefSeq; YP_003074416.1; NC_012997.1. DR ProteinModelPortal; C5BP24; -. DR STRING; 377629.TERTU_3038; -. DR EnsemblBacteria; ACR11253; ACR11253; TERTU_3038. DR GeneID; 8213573; -. DR KEGG; ttu:TERTU_3038; -. DR PATRIC; 23872993; VBITerTur118718_2823. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TTUR377629:GHSU-2755-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 319 AA; 34792 MW; 40D73692ED6500BF CRC64; MLNIAHKVIH VAVGVVRNAK GEVLIAKRQA GQHLAGFWEF PGGKVEQGEC VTTALARELR EELGIEVSEA QPLITIPYDY PEKRVLLDVH EVTQYSDSPV SGEGQSIRWV SQSDLRDYTF PPANAPIVTA VQLPAVFCIS GEFEGFAALR DRCGSLQSQG ITHIQLRAPH LEPAEYLQVY RRLSGEIEGV SLFANTDWQH PNVSQVEQMP RYIHLSSRVL RAGYKPVAGG VISAACHDVE ELKLAEHAGA HFVFFSPVKP TSSHPNTPGV GWEALRDFCA VAKVPVYALG GLSELDISQA RQCGAQGIAA ISALWGRIQ // ID C5BP53_TERTT Unreviewed; 212 AA. AC C5BP53; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TERTU_3068; OS Teredinibacter turnerae (strain ATCC 39867 / T7901). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadales genera incertae sedis; Teredinibacter. OX NCBI_TaxID=377629; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39867 / T7901; RX PubMed=19568419; DOI=10.1371/journal.pone.0006085; RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S., RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M., RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A., Elshahawi S., RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., RA Madinger C., Nove J., Anton B., Chaudhary K., Foster J., Holman A., RA Kumar S., Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., RA Teplitski M., Mougous J.D., Ward N., Eisen J.A., Badger J.H., RA Distel D.L.; RT "The complete genome of Teredinibacter turnerae T7901: an RT intracellular endosymbiont of marine wood-boring bivalves RT (shipworms)."; RL PLoS ONE 4:E6085-E6085(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001614; ACR14356.1; -; Genomic_DNA. DR RefSeq; YP_003074445.1; NC_012997.1. DR ProteinModelPortal; C5BP53; -. DR STRING; 377629.TERTU_3068; -. DR EnsemblBacteria; ACR14356; ACR14356; TERTU_3068. DR GeneID; 8212576; -. DR KEGG; ttu:TERTU_3068; -. DR PATRIC; 23873051; VBITerTur118718_2852. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TTUR377629:GHSU-2785-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22715 MW; 10EEE139AAAC1C50 CRC64; MPTHSLPRIY GITDSGLLPT THQLVTAVET ALLAGVTWIQ YRAKQLDPDT KLKQAERLIA LCQTLNGVLI VNDDVHLAQR IGAHGVHLGQ SDMPVVQARA ILGPEALIGV TCHSDLALAR KAADEGASYL AFGRFFRSST KPDAPVAPLS VLKKAKTQFQ LPIVAIGGID AANALEVYRA GADSLACCNS LFDGNNVKSR AEMLFRSLSH HE // ID C5CA55_MICLC Unreviewed; 247 AA. AC C5CA55; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mlut_07950; OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC OS 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus OS lysodeikticus). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Micrococcus. OX NCBI_TaxID=465515; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / RC NCTC 2665 / VKM Ac-2230; RX PubMed=19948807; DOI=10.1128/JB.01254-09; RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., RA Dover L.G., Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., RA Lapidus A., Lowry S.R., Lykidis A., Mahillon J., Markowitz V., RA Mavromatis K., Mukamolova G.V., Oren A., Rokem J.S., Smith M.C., RA Young D.I., Greenblatt C.L.; RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple RT free-living actinobacterium."; RL J. Bacteriol. 192:841-860(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001628; ACS30324.1; -; Genomic_DNA. DR RefSeq; YP_002956878.1; NC_012803.1. DR ProteinModelPortal; C5CA55; -. DR STRING; 465515.Mlut_07950; -. DR EnsemblBacteria; ACS30324; ACS30324; Mlut_07950. DR GeneID; 7984746; -. DR KEGG; mlu:Mlut_07950; -. DR PATRIC; 22622229; VBIMicLut29563_0758. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MLUT465515:GHH6-793-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 71 75 HMP-PP binding (By similarity). FT REGION 169 171 THZ-P binding (By similarity). FT METAL 104 104 Magnesium (By similarity). FT METAL 123 123 Magnesium (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 172 172 HMP-PP (By similarity). FT BINDING 205 205 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 247 AA; 25500 MW; 826C58912C94FD80 CRC64; MHSPDPLLMT AAGRDDGDTG PGAGRRARLA ASRLYVCTDL QRFLRPDGTL DAAAFAGFCA AAFRGGVDLI QVRDKAVDVA VELAAFVVLV PLAREHGALS AANDRADVAA LAGVDVFHTG QTDLTTAQCR ALLGPDVVLG RSCHTEAQVR AARAEDGLDY FCTGPVLATP TKPGRAAVGL ALPSFAARLD AEDPAGARPW FAIGGVDADR LPEVRAAGAE RIVVVRAVTQ AEDPEAAARS LRAGLPG // ID C5CJG9_VARPS Unreviewed; 309 AA. AC C5CJG9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Precursor; GN OrderedLocusNames=Vapar_2395; OS Variovorax paradoxus (strain S110). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=543728; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S110; RX PubMed=21183664; DOI=10.1128/JB.00925-10; RA Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., RA Kim T.G., O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C., RA Ovchinnikova G., Goodwin L., Han C.; RT "Complete genome sequence of the metabolically versatile plant growth- RT promoting endophyte, Variovorax paradoxus S110."; RL J. Bacteriol. 193:1183-1190(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001635; ACS19022.1; -; Genomic_DNA. DR RefSeq; YP_002944288.1; NC_012791.1. DR ProteinModelPortal; C5CJG9; -. DR STRING; 543728.Vapar_2395; -. DR EnsemblBacteria; ACS19022; ACS19022; Vapar_2395. DR GeneID; 7970439; -. DR KEGG; vap:Vapar_2395; -. DR PATRIC; 24005222; VBIVarPar36677_2409. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; VPAR543728:GHLL-2415-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 309 AA; 32581 MW; 3C975617CBC377A1 CRC64; MSASTDARAI SQAIVATHGL RFGTNMPAAI SAGRFSSDEP VYRGAKQACT ALGFIEIDAE CLARAWQAQT ARTGAFDANQ WPETPVDFGM RAFPPTERDD AFAPCPERLG LYAVLPDAQW VGRMARAGVP TVQLRFKSDD AAATEREVHS AVDAVRGTGA LLFINDHWQT AIAAGAYGVH LGQEDLDALA PEQVQQIRDA DLRLGVSTHG YAEMVRADAV SPSYIAMGAV YPTTLKKMAT APQGVARLAA YARLLRGYPQ VGIGGIDAVR LPEVLATGVG SVAVVRALVA AEDPEATAAQ WMASIAAAT // ID C5D2M8_GEOSW Unreviewed; 219 AA. AC C5D2M8; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GWCH70_1937; OS Geobacillus sp. (strain WCH70). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=471223; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WCH70; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Brumm P., Mead D.A., Richardson P.; RT "Complete sequence of chromosome of Geopacillus sp. WCH70."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001638; ACS24670.1; -; Genomic_DNA. DR RefSeq; YP_002949936.1; NC_012793.1. DR ProteinModelPortal; C5D2M8; -. DR SMR; C5D2M8; 1-218. DR STRING; 471223.GWCH70_1937; -. DR EnsemblBacteria; ACS24670; ACS24670; GWCH70_1937. DR GeneID; 7978761; -. DR KEGG; gwc:GWCH70_1937; -. DR PATRIC; 21972868; VBIGeoSp101709_2045. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GSP471223:GH2C-2022-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23369 MW; 1E26EF364011490F CRC64; MARIASEVMR ERLKVYFIMG STNCKKQPLE VLTEAIDGGI TLFQFREKGS GALVGEQKYE FARQLQNICK NRGIPFIVND DVELALALDA DGVHIGQDDE DARIVREKIG DKILGVSAHN LKEAQAAIAA GADYIGVGPI YPTKSKEDAK KAQGPEIIRF LRGQGVDIPL VAIGGITAEN AGEVMNAGAD GVSVISAIAS ASSPFLAAKQ LVQTVFNNK // ID C5D6I9_GEOSW Unreviewed; 202 AA. AC C5D6I9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=GWCH70_0610; OS Geobacillus sp. (strain WCH70). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=471223; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WCH70; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Brumm P., Mead D.A., Richardson P.; RT "Complete sequence of chromosome of Geopacillus sp. WCH70."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001638; ACS23506.1; -; Genomic_DNA. DR RefSeq; YP_002948772.1; NC_012793.1. DR ProteinModelPortal; C5D6I9; -. DR STRING; 471223.GWCH70_0610; -. DR EnsemblBacteria; ACS23506; ACS23506; GWCH70_0610. DR GeneID; 7978799; -. DR KEGG; gwc:GWCH70_0610; -. DR PATRIC; 21970099; VBIGeoSp101709_0666. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GSP471223:GH2C-695-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 21849 MW; 66425C38E755D6FD CRC64; MERQLHIIST GKQSLDQFVA ICARVHPYVD AIHVREKMKT AREISEFLAA LLKRGVPPGK IVVNDRVDVA VVFGVKGVQL AYHSLSVRQV KRHFPSLAVG CSVHSIEEAM EAEESGADYC LYGHIFSTAS KLGVPPCGIE SLRSVVNRVN IPVIAIGGIH SNNAEQVLKA GAHGIAVMSA VFFAEDPVSE AKKLAKIVKK MV // ID C5E2C3_LACTC Unreviewed; 538 AA. AC C5E2C3; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-APR-2014, entry version 34. DE SubName: Full=KLTH0H03784p; GN OrderedLocusNames=KLTH0H03784g; OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284) OS (Yeast) (Kluyveromyces thermotolerans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea. OX NCBI_TaxID=559295; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284; RX PubMed=19525356; DOI=10.1101/gr.091546.109; RG The Genolevures Consortium; RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V., RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., RA Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F., RA Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., RA Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T., RA Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G., RA Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C., RA Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E., RA Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C., RA Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C., RA Straub M.-L., Talla E.; RT "Comparative genomics of protoploid Saccharomycetaceae."; RL Genome Res. 19:1696-1709(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU928180; CAR30184.1; -; Genomic_DNA. DR RefSeq; XP_002556046.1; XM_002556000.1. DR ProteinModelPortal; C5E2C3; -. DR STRING; 559295.KLTH0H03784g; -. DR GeneID; 8294359; -. DR KEGG; lth:KLTH0H03784g; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 538 AA; 57639 MW; FA466E4E51A3ADF6 CRC64; MFDKNKVDYS LYLVTDSTML PPGTTLESQV EAALKNGVTL VQLREKETET KVFIEQALKV QKLCHKFQVP LIINDRVDVA LAIDADGVHV GQDDMPIKMV RQLLGPSKII GWSVGYEHEV EQLAAMGPGA VDYIGLGMVY PTLTKKNPKK APMGPRGVSK LLDKLQSTNA EWCRTVAIGG LHPDNIPRVL YQIASSDGKR SLDGISVVSD IMASPEAGNA AQTLRALIDQ SSFHYAQGLS PCRKDFSSEL AKECVQQMTE ASPLVQHITN KVHQNFGANV TLALGSSPIM SEVEPEFEEL SQISHATLLL NTGTVAPFNT LLQAMCAYNA AKRPIVFDPV GYSATSTRLE LNNQLLAYGQ FACIKGNVGE ILSLADLNKG KMRGVDAGSV GSDISLCVEA TKIVAYRYRT IAVCTGQQDI VVDGTCGGTF ELSEGSAARA SDLPALIVEA GEIPVMGKIT ASGCSLGSTI ACLVGGISDK QHLFHAVTTA VCLYKSAGKI ASERCNGSGS FQVELIDALD QLFTKNQPES WVAKVSRI // ID C5E4M1_ZYGRC Unreviewed; 542 AA. AC C5E4M1; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-APR-2014, entry version 35. DE SubName: Full=ZYRO0E07216p; GN OrderedLocusNames=ZYRO0E07216g; OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / OS NCYC 568 / NRRL Y-229) (Candida mogii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; OC Zygosaccharomyces. OX NCBI_TaxID=559307; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229; RX PubMed=19525356; DOI=10.1101/gr.091546.109; RG The Genolevures Consortium; RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V., RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., RA Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F., RA Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., RA Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T., RA Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G., RA Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C., RA Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E., RA Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C., RA Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C., RA Straub M.-L., Talla E.; RT "Comparative genomics of protoploid Saccharomycetaceae."; RL Genome Res. 19:1696-1709(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU928181; CAR30982.1; -; Genomic_DNA. DR RefSeq; XP_002499237.1; XM_002499192.1. DR ProteinModelPortal; C5E4M1; -. DR STRING; 559307.ZYRO0E07216g; -. DR GeneID; 8204792; -. DR KEGG; zro:ZYRO0E07216g; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 542 AA; 58860 MW; D4E177971BEB1408 CRC64; MVFAKDEVDY SLYLVTDSTM LPEGTTLYSQ VENALENGVS LVQLREKNVD TKKFIEEAIE IQKLCKKFEV PLIINDRIDV ALAIDADGVH VGQDDMPIPM VRKLVGPDKI IGWSVGYTHE VEQLAQWGPD YVDYIGIGMV FPTNTKKNAK KSPMGPRGVA RILDALENNN VDWCRTVAIG GLHPDNISRV LYQCNSLSGQ RSIDGISVVS DIMAAKDAGA ATKNLRDILD KGYYSFVNLQ LSIKTIYDLD FSSHTKRFLE QVAKNRPLVQ HITNKVHQNF GANVTLAIGS SPIMSEIKEE ANDLAHIPHA ALLVNTGSVA PLEVVKTAIQ AYNDVKRPIV FDPVGYSATT TRIVLNDTLL ASGQFTCIKG NTGEILSLAG FSGKMRGVDA HEGDFDKNLL AQATREVAFR FRTIAVCTGE LDFIADGTLG GTYSLSDGTK DRVLKDLPCV VVSNGPIPLM GDITASGCSL GSTIASLLGG ANSDENPFEL VVAAVELYKE AGRLASLSSE GSGSFHVQLI DKLYNCFRSN PRTWAPKVET LN // ID C5EE30_BIFLI Unreviewed; 917 AA. AC C5EE30; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; ORFNames=BLIG_01943; OS Bifidobacterium longum subsp. infantis CCUG 52486. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=537937; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 52486; RG The Broad Institute Genome Sequencing Platform; RA Gougoulias C., Tuohy K.M., Gibson G.R., Ward D., Mehta T., Young S., RA Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., RA Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., RA Galagan J., Nusbaum C., Birren B.; RT "Annotation of Bifidobacterium longum subsp. infantis CCUG 52486."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990259; EEQ56274.1; -; Genomic_DNA. DR ProteinModelPortal; C5EE30; -. DR EnsemblBacteria; EEQ56274; EEQ56274; BLIG_01943. DR PATRIC; 26498866; VBIBifLon94805_2068. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100338 MW; 6812F9EA40270F47 CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL RGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAILADTKA AGWFVVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIARYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AVDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID C5EFB0_9FIRM Unreviewed; 237 AA. AC C5EFB0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CBFG_02608; OS Clostridiales bacterium 1_7_47FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=457421; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_7_47_FAA; RG The Broad Institute Genome Sequencing Platform; RA Allen-Vercoe E., Strauss J., Ambrose C., Ward D., Gujja S., Young S., RA Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., RA Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., RA Galagan J., Nusbaum C., Birren B.; RT "Annotation of Clostridiales bacterium 1_7_47_FAA."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990260; EEQ58898.1; -; Genomic_DNA. DR ProteinModelPortal; C5EFB0; -. DR EnsemblBacteria; EEQ58898; EEQ58898; CBFG_02608. DR PATRIC; 27119341; VBICloBac45081_1778. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 237 AA; 25666 MW; 6A13D7264EA93E4C CRC64; MTGCWKEGKK LRFHRNQLLI YAVTDRAWTK GRSLSEQVEE TLKGGATMVQ FREKSLGQGN YDRMLDEALE LRKLTERYQV PLIIDDDIEL ALACGADGLH VGQDDMDAGL ARKLLGPDRI LGVTAKTVEQ AKRACAQGAD YLGSGAVFGT TTKADARPMT METLRSICDC SDVPVVAIGG INLGNIGLLE GSHVAGAAIV SGIFAAQDIC LATARLKEAM IKIRDKNSSY FQKTVDI // ID C5ENR2_9FIRM Unreviewed; 199 AA. AC C5ENR2; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=CBFG_03502; OS Clostridiales bacterium 1_7_47FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=457421; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_7_47_FAA; RG The Broad Institute Genome Sequencing Platform; RA Allen-Vercoe E., Strauss J., Ambrose C., Ward D., Gujja S., Young S., RA Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., RA Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., RA Galagan J., Nusbaum C., Birren B.; RT "Annotation of Clostridiales bacterium 1_7_47_FAA."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990261; EEQ59792.1; -; Genomic_DNA. DR ProteinModelPortal; C5ENR2; -. DR PRIDE; C5ENR2; -. DR EnsemblBacteria; EEQ59792; EEQ59792; CBFG_03502. DR PATRIC; 27121140; VBICloBac45081_3777. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 21573 MW; 66E698A13F3F1F7D CRC64; MYENLITDPG LKGHILAVTN RNLCSRPFAE QIRRVCWFHP AALILREKDL PDAEYGELAK EVMKICREYQ VPFIAHSFME TARQLGADTI HLPLWRLREA SGTGLLDGFK TIGVSVHSVE EALEAAALGA SYLTAGHIYA TDCKKGLPPR GTGFLRAVCE AVDIPVYGIG GIRLDEAQIK EVLGCGAAGG CIMSGMMGI // ID C5EZH9_9HELI Unreviewed; 132 AA. AC C5EZH9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Uncharacterized protein; GN ORFNames=HPMG_00751; OS Helicobacter pullorum MIT 98-5489. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=537972; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MIT 98-5489; RG The Broad Institute Genome Sequencing Platform; RA Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T., RA Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., RA Shea T., Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., RA Galagan J., Nusbaum C., Birren B.; RT "Annotation of Helicobacter pullorum strain MIT 98-5489."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990442; EEQ63294.1; -; Genomic_DNA. DR ProteinModelPortal; C5EZH9; -. DR EnsemblBacteria; EEQ63294; EEQ63294; HPMG_00751. DR PATRIC; 27516867; VBIHelPul71015_0628. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 132 AA; 14573 MW; A16DF2419706E759 CRC64; MKLNQYYKIP SLVNSNLAIA LKFGFDGLHC NGMQMQQIAE AKKKISLVFY SAHSSKEILQ ADLEGANGIT ISPIFKTQNK GQPLGIDFLE KLNPKNYQAE IFALGGIIGA KEVEAISKTS IKNFASIRYF LS // ID C5F0N4_9HELI Unreviewed; 211 AA. AC C5F0N4; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HPMG_01245; OS Helicobacter pullorum MIT 98-5489. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=537972; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MIT 98-5489; RG The Broad Institute Genome Sequencing Platform; RA Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T., RA Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., RA Shea T., Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., RA Galagan J., Nusbaum C., Birren B.; RT "Annotation of Helicobacter pullorum strain MIT 98-5489."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990444; EEQ63788.1; -; Genomic_DNA. DR ProteinModelPortal; C5F0N4; -. DR EnsemblBacteria; EEQ63788; EEQ63788; HPMG_01245. DR PATRIC; 27517899; VBIHelPul71015_1276. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 211 AA; 23871 MW; D763262E8896B0D4 CRC64; MLEGIYAISD EKLTPYQKIF EMLELAIRGG ISIFQLRDKT HKDNEIKQLC IELMDYCGQN NVLFVLNDRV ELACEIKSKG LHIGKKDEIE SYSVQELRGI RKDFCGVLGI SCYGDLQLAQ NAKEMRADYI AFGACFASPT KAQAKVIPLD LFQKVTDIKK CAIGGITPSN IHYLTKADMI ACISSVWNGD IVQNLYNLKK NWKKESFNEM L // ID C5FAN6_LACPA Unreviewed; 213 AA. AC C5FAN6; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LBPG_02487; OS Lactobacillus paracasei subsp. paracasei 8700:2. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=537973; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=8700:2; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Saulnier D., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Lactobacillus paracasei subsp. paracasei RT strain 8700:2."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002391; EEQ67038.1; -; Genomic_DNA. DR RefSeq; YP_008445668.1; NC_022112.1. DR ProteinModelPortal; C5FAN6; -. DR EnsemblBacteria; EEQ67038; EEQ67038; LBPG_02487. DR GeneID; 16639203; -. DR KEGG; lpi:LBPG_02487; -. DR PATRIC; 26513402; VBILacPar66337_2362. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22607 MW; 1C71894D5791C1D5 CRC64; MNATDLKLYL VTHRYDDNEA TFLAKIAAAC ENGVTMVQLR EKMLSTRAYF ELAQRVKLIT DRYQIPLIID DRVDICLAVD AAGVHIGDDE LPVAMTRQLI GPDKVLGVST KTVETAVAAV AAGADYLGVG AIFPTQTKAN AAVTPIATLK AITAQVAVPV VAIGGVKEAN LATFKDTGIA GVAIVSEIMQ APDIAHKVQA LRTKLKAVLP NDR // ID C5FNJ8_ARTOC Unreviewed; 502 AA. AC C5FNJ8; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-APR-2014, entry version 30. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=MCYG_04431; OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum OS canis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Arthroderma. OX NCBI_TaxID=554155; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4605 / CBS 113480; RX PubMed=22951933; DOI=10.1128/mBio.00259-12; RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W., RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E., RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I., RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., RA Summerbell R.C., Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., RA White T.C.; RT "Comparative genome analysis of Trichophyton rubrum and related RT dermatophytes reveals candidate genes involved in infection."; RL MBio 3:E259-E259(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995704; EEQ31612.1; -; Genomic_DNA. DR RefSeq; XP_002846694.1; XM_002846648.1. DR ProteinModelPortal; C5FNJ8; -. DR GeneID; 9229805; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 502 AA; 52791 MW; D6AAB3D265ACED74 CRC64; MPVNLSLYLV TDSTPKILGD RDLCSVVEQA VKGGVTIVQY RDKHSDTREL IETAAKLHSI TLDHGIPLII NDRVDVAIAV GAEGVHLGQD DMDIYVARKM LPKGTIIGVT VSSIEEAQAA VESGADYLGI GTVHATPTKT NTKSIIGTAG VKHILNHVSS ISHNVGTVAI GGINLNNAQR VIYQSQGTTK GLDGVAVVSA IMAADDPQAA AASFLEKLSQ NPAFATIPIT PRENEESLLL NGVNSLVRKV AIFNPLCHNM INYVVANFAA NVALAIGASP IMSGYGLEAP DLAKNNGALL INMGTLNNES MDNYLQAIRA YNETGNPVVL DPVGAAATQL RRQSVKTLMQ GGYFDLIKGN ESEISYIYGY TGGHQVGVDS GPRCVVLLTG STDYLSDGSR TVAIRNGHPL LGQVTGTGCA IGTITAAFLA VERHDKLLAV LSALLMFEVA AERAASNGVK GPGSFVPALL DELYSLRTQA MGSNAAPMDT IKNAAKLNFI HL // ID C5G959_AJEDR Unreviewed; 540 AA. AC C5G959; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-APR-2014, entry version 26. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BDCG_00108; OS Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces OS dermatitidis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Ajellomyces. OX NCBI_TaxID=559297; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ER-3 / ATCC MYA-2586; RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Klein B., Goldman B., RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A.M., Heiman D.I., Hepburn T.A., Saif S., Shea T.D., Shenoy N., RA Sykes S., Galagan J.E., Nusbaum C., Birren B.W.; RT "The genome sequence of Blastomyces dermatitidis strain ER-3."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999973; EEQ83303.1; -; Genomic_DNA. DR ProteinModelPortal; C5G959; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 57216 MW; 783CDD8F8F214EAD CRC64; MDLSVYLVTD STPAILGNRD LCEVVQDALE GGVTVVQYRD KHSDTGVMID MAKRLHGITK KYNVPLIIND RVDVALAVGA EGVHLGQDDM KITEAKKLLP PNTYIGVSVR SNEEAFRAVQ DGADYVGIGT VFATPTKTDT KSIIGTAGTR DILAFLSTMP RKVGAVAIGG INLTNVQRVI YQSQAPLKSL DGAAIVSAIM AAESPREAAA SFCRLVKQIP ASATLPVPPR ENEVSLLLDQ VPDIVSLVAT KRPLCHNMIN FVVANFAANV AIAIGASPIM SGYGPEAPDL AKNGGSLLIN MGTLNNESLD NYLQALRAYN AEGNPVVFDP VGAGATDIRR KATKQLLAGG YFDLIKGNES ELIQVYGKAR GNQVGVDSGP STLNPEEKAK LVKDLARRER NIVLLTGSVD YLSDGERTLA IGNGHQFLGH ITGTGCIIGT MAASFLAVHR SDKLLAVFAS LLLLEIAAER AAMKDGVHGP GTFLPAFIDE LFTLRQWAVD WKSGDAAGGT GAGAKTSNGD ASAVDENIFR KMAKVHLINM // ID C5JZQ6_AJEDS Unreviewed; 540 AA. AC C5JZQ6; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-APR-2014, entry version 25. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BDBG_08049; OS Ajellomyces dermatitidis (strain SLH14081) (Blastomyces dermatitidis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Ajellomyces. OX NCBI_TaxID=559298; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SLH14081; RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Klein B., Goldman B., RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A.M., Heiman D.I., Hepburn T.A., Saif S., Shea T.D., Shenoy N., RA Sykes S., Galagan J.E., Nusbaum C., Birren B.W.; RT "The genome sequence of Blastomyces dermatitidis strain SLH14081."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657469; EEQ73835.1; -; Genomic_DNA. DR RefSeq; XP_002621426.1; XM_002621380.1. DR ProteinModelPortal; C5JZQ6; -. DR GeneID; 8508696; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 57216 MW; 783CDD8F8F214EAD CRC64; MDLSVYLVTD STPAILGNRD LCEVVQDALE GGVTVVQYRD KHSDTGVMID MAKRLHGITK KYNVPLIIND RVDVALAVGA EGVHLGQDDM KITEAKKLLP PNTYIGVSVR SNEEAFRAVQ DGADYVGIGT VFATPTKTDT KSIIGTAGTR DILAFLSTMP RKVGAVAIGG INLTNVQRVI YQSQAPLKSL DGAAIVSAIM AAESPREAAA SFCRLVKQIP ASATLPVPPR ENEVSLLLDQ VPDIVSLVAT KRPLCHNMIN FVVANFAANV AIAIGASPIM SGYGPEAPDL AKNGGSLLIN MGTLNNESLD NYLQALRAYN AEGNPVVFDP VGAGATDIRR KATKQLLAGG YFDLIKGNES ELIQVYGKAR GNQVGVDSGP STLNPEEKAK LVKDLARRER NIVLLTGSVD YLSDGERTLA IGNGHQFLGH ITGTGCIIGT MAASFLAVHR SDKLLAVFAS LLLLEIAAER AAMKDGVHGP GTFLPAFIDE LFTLRQWAVD WKSGDAAGGT GAGAKTSNGD ASAVDENIFR KMAKVHLINM // ID C5KTS2_PERM5 Unreviewed; 495 AA. AC C5KTS2; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 24. DE SubName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase, putative; GN ORFNames=Pmar_PMAR019066; OS Perkinsus marinus (strain ATCC 50983 / TXsc). OC Eukaryota; Alveolata; Perkinsea; Perkinsida; Perkinsidae; Perkinsus. OX NCBI_TaxID=423536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50983 / TXsc; RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG676180; EER11964.1; -; Genomic_DNA. DR RefSeq; XP_002780169.1; XM_002780123.1. DR ProteinModelPortal; C5KTS2; -. DR GeneID; 9060802; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 495 AA; 51950 MW; DCA14A8EA731E522 CRC64; MSSSELYKVY ACTNGKFSLE LPRMVASAVA GGATCVQLRL KDVSTGDYVK LAKETKKLMP RHVPLIIDDR VDVCMASGAD GVHVGDTDMS VKDARSIIGP DKILGVSTYG RQEDAIAAIR DGADYIATGA VYPTVTKPGA VAQGLGQIDI LKAALKATGK TLPIVAIGGI SPVTAIDCVQ RGADGVCAVS QIFDSWESPE SRARKFLKSY CSGMEIRSKM STHKQYDSDM VTGLWAKLAD MNPLTQCITN YVSMNFMANS LLAAGASPAM AHAKEEAPQF LDMASALNVN IGTLSSNWVE SMRLCAKKAN EIGKPWVLDP VAAGATAFRT GVATELLGYK PTVLRGNGGE ILALAGETGS VKGVDSTVGS DAALTAAKHI ARKFGIVVCI SGATDFVTDG KRVIEICHDV PMLPTITATG CTLSALMTSF CAVAEDPLDA AVAACAGWSL AAQEASVAAQ GPGGLALELL DTLPKLRDPT WPAWKRLVIF EHNCQ // ID C5L5N6_PERM5 Unreviewed; 297 AA. AC C5L5N6; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 25. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative; DE Flags: Fragment; GN ORFNames=Pmar_PMAR006904; OS Perkinsus marinus (strain ATCC 50983 / TXsc). OC Eukaryota; Alveolata; Perkinsea; Perkinsida; Perkinsidae; Perkinsus. OX NCBI_TaxID=423536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50983 / TXsc; RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG679439; EER07957.1; -; Genomic_DNA. DR RefSeq; XP_002776141.1; XM_002776095.1. DR ProteinModelPortal; C5L5N6; -. DR GeneID; 9064055; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. FT NON_TER 297 297 SQ SEQUENCE 297 AA; 31442 MW; 08B9E4298B54B4B9 CRC64; MVASAVAGGA TCVQLRLKDV STGDYVKLAK ETKKLMPRHV PLIIDDRVDV CMASGADGVH VGDTDMSVKD ARSIIGPNKI LGVSTYGRQE DAIAAIRDGA DYIATGAVYP TVTKPGAVAQ GLGQIDILKA ALKATGKTLP IVAIGGISPV TATDCVQRGA DGVCAVSQIF DSWESPESRA RKFLKSYCSG MEIRSKMSTH KQYDSDMVTS LWAKLAAMNP LTQCITNYVS MNFMANSLLA AGASPAMAHA KEEAPQFLDM ASALNVNIGT LSSNWVESMR LCAKKANEIG KPWVLDP // ID C5LCI5_PERM5 Unreviewed; 494 AA. AC C5LCI5; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 24. DE SubName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase, putative; GN ORFNames=Pmar_PMAR011714; OS Perkinsus marinus (strain ATCC 50983 / TXsc). OC Eukaryota; Alveolata; Perkinsea; Perkinsida; Perkinsidae; Perkinsus. OX NCBI_TaxID=423536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50983 / TXsc; RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG680918; EER05668.1; -; Genomic_DNA. DR RefSeq; XP_002773852.1; XM_002773806.1. DR ProteinModelPortal; C5LCI5; -. DR GeneID; 9064763; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 494 AA; 52211 MW; A16BC058F5590358 CRC64; MSSELYKVYA CTNGKFSLEL PRMVASAVAG GATCVQLRLK DVSTGDYVRM AKETKRLMPR HVPLIIDDRV DVCMASGADG VHVGDTDMTV KDARSIIGPN KILGVSTYGR RVDAIAAIED GADYIATGAV YPTVTKPGAV PKGLDQIDVL KEALKTTGKT LPIVAIGGIS PVTAIDCVQR GADGVCAVSQ IFDSWESPES RARKFLKSYC SGMEIRSKLS THKRYNNDMV TSLWGQLGKV NPLTQCITNY VSMNFTANSL LAAGASPAMV HAEEEAPQFL EMAAALNVNI GTLSSNWVES MRLCAKKAME IGKPWVLDPV AAGATAFRTG VATELLAYKP TVLRGNGGEI LALAGETGAV KGVDSTIGSD AALEAAKHIA RKFGTVVCIS GATDFVTDGK RVIEICHDVP MLPTVTATGC TLSALMTSFC AVAKNPLDAA VAACAGWSLA AQEASVTAEG PGSLALKMLN ILPRLRDPAW PAWRRLAIFE HNCQ // ID C5M838_CANTT Unreviewed; 509 AA. AC C5M838; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 16-APR-2014, entry version 27. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=CTRG_02560; OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; OC Candida. OX NCBI_TaxID=294747; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-3404 / T1; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., RA Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., RA Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D., RA Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., RA Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., RA Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., RA Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., RA Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., RA Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., RA Kellis M., Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG692397; EER33742.1; -; Genomic_DNA. DR RefSeq; XP_002548263.1; XM_002548217.1. DR ProteinModelPortal; C5M838; -. DR GeneID; 8299159; -. DR KEGG; ctp:CTRG_02560; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 509 AA; 54772 MW; 53CA9FAC9325FCAA CRC64; MVDVDYSLYL VTDSTMIPES STFLKQVEAA INNGATLIQL REKLLTTRQF ITRAEQVHEL TKKKGIPLII NDRVDVALAI DAEGVHVGQK DMPAKLARKL IGPNKILGVT CSSYDETQQV VGEGIADYVG LGTLYPTQTK KDLKEPGGTG PLGIRKSLQV LKKYNQSHRE KPIRCVGIGG VNHSNADKVL YQCAVPGQKL DGVAVVSCIM ANENAAQATI DLLKVINRQP IWANITSDGT DDLSVKIKQL SKAHPLVHHI TNNTVKNFSA NVTLAIGASP IMSELDEEYE EFASSIPNLA LVLNVGTPTE GLHKVFKQAI HMYNKYGKPI VFDPVACGAT KARLECSKSL LKSGQFTVIK GNVGEIMGLY KLTSEYIDTG NQALMRGVDS IVEYGEDDII KIAKTVSVDF QTVVVVTGEV NYIIDGDKRI AKVKGGNPLM GNVTGTGCSL GSTIAAFLGA KADGNKGTDV FSATVGAVEL YNKAGSLVKA EASGSFMIEF INELYKLTH // ID C5N2P5_STAA3 Unreviewed; 213 AA. AC C5N2P5; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0776_1454; OS Staphylococcus aureus subsp. aureus USA300_TCH959. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=450394; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=USA300_TCH959; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AASB02000195; EES93928.1; -; Genomic_DNA. DR ProteinModelPortal; C5N2P5; -. DR EnsemblBacteria; EES93928; EES93928; HMPREF0776_1454. DR PATRIC; 27165728; VBIStaAur104985_2623. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23428 MW; 72CEFFE40BF6349B CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLET ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PKMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C5NHN7_BURML Unreviewed; 367 AA. AC C5NHN7; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 27. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=BMAPRL20_A2936; OS Burkholderia mallei PRL-20. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=436115; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PRL-20; RA Harkins D.M., Brinkac L.M., DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZP01000061; EES43900.1; -; Genomic_DNA. DR ProteinModelPortal; C5NHN7; -. DR EnsemblBacteria; EES43900; EES43900; BMAPRL20_A2936. DR PATRIC; 26952531; VBIBurMal20566_3837. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Transferase. SQ SEQUENCE 367 AA; 38315 MW; 3E9B351CCB7F5C2B CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGARAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID C5NIB0_BURML Unreviewed; 209 AA. AC C5NIB0; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 23. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BMAPRL20_0274; OS Burkholderia mallei PRL-20. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=436115; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PRL-20; RA Harkins D.M., Brinkac L.M., DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAZP01000069; EES43671.1; -; Genomic_DNA. DR ProteinModelPortal; C5NIB0; -. DR EnsemblBacteria; EES43671; EES43671; BMAPRL20_0274. DR PATRIC; 26953011; VBIBurMal20566_4076. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID C5NUI4_9BACL Unreviewed; 210 AA. AC C5NUI4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GEMHA0001_0087; OS Gemella haemolysans ATCC 10379. OC Bacteria; Firmicutes; Bacilli; Bacillales; OC Bacillales Family XI. Incertae Sedis; Gemella. OX NCBI_TaxID=546270; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10379; RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E., RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10379; RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDZ02000004; EER69160.1; -; Genomic_DNA. DR ProteinModelPortal; C5NUI4; -. DR EnsemblBacteria; EER69160; EER69160; GEMHA0001_0087. DR PATRIC; 28763264; VBIGemHae122965_0119. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23402 MW; F6C939E29396FB88 CRC64; MFNKELLKLY FICGTTTCLG KDLYTVVEDA LKGGITLFQF REKGEGALEG REKVELAIKL QELCKKYNVP FIVNDDIELA LEIDADGVHV GQDDLGVDEI RKLMPNKIIG LSIGNEEEFK QSKVEYVDYV GVGPVYVTQS KDDAGGAIGY EGLELMRRFL PQMPLVAIGG IQTQHIKDIM KTNVDGVSII SAISYSDNIE KTVREMIEQF // ID C5PHY2_COCP7 Unreviewed; 529 AA. AC C5PHY2; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 16-APR-2014, entry version 28. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; DE EC=2.5.1.3; GN ORFNames=CPC735_055050; OS Coccidioides posadasii (strain C735) (Valley fever fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; mitosporic Onygenales; Coccidioides. OX NCBI_TaxID=222929; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C735; RX PubMed=19717792; DOI=10.1101/gr.087551.108; RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., RA Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., RA Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., RA Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J., RA Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.; RT "Comparative genomic analyses of the human fungal pathogens RT Coccidioides and their relatives."; RL Genome Res. 19:1722-1731(2009). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFW01000049; EER24135.1; -; Genomic_DNA. DR RefSeq; XP_003066280.1; XM_003066234.1. DR UniGene; Cpo.3033; -. DR ProteinModelPortal; C5PHY2; -. DR STRING; 222929.C5PHY2; -. DR GeneID; 9691750; -. DR KEGG; cpw:CPC735_055050; -. DR eggNOG; COG0352; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 529 AA; 56081 MW; FD866ABABDB05B12 CRC64; MPIDLSLYLV TDSTPNILGD RDLCTVVEQA IQGGVTIVQY RDKHADTGVL IETASRLHTI TKAHGVPLVI NDRVDVALAV GAEGVHLGQD DMDIETARKL LPKNCFIGAT VSSVEEARIA VEKGANYLGI GTVFATPTKT NTKSIIGTAG VRQILDFLST LPRKVGTVAI GGINLSNTQR VIYQSAAATK GLDGVAIVSA IVAAEDPYKA AALLARAITK SPSFATIPPD PREDEFSYLL NNAISVARKV AVRMPLVHSM INYVVANFAA NVSLQIGASP IMSPYGPEAT DLSKAGGSLL INMGTLNADS LNNYTQAVQA YNQRGSPVVF DPVGGGATEV RQNAIRTLMA GGYFDLIKGN ESEIKVIYGQ SSSRQIGVDS GPSTLTLQEK VAMVRDLATR ERNIVLMTGP VDFLSDGIRT VAIKNGHRYL GQITGTGCVI GLVAAAFLAV ERTDKLLAVL AGVLMFEIAA ENAALKEYVR GPGTFMPAFL DELYALREDT KASPENNWIK QRAQITVFTA ESDGAASSS // ID C5PZC1_STAAU Unreviewed; 214 AA. AC C5PZC1; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0774_0551; OS Staphylococcus aureus subsp. aureus TCH130. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=548474; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TCH130; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHD01000013; EES97712.1; -; Genomic_DNA. DR ProteinModelPortal; C5PZC1; -. DR EnsemblBacteria; EES97712; EES97712; HMPREF0774_0551. DR PATRIC; 27147560; VBIStaAur127522_1938. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23450 MW; B09BFBAD7D6EF82F CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF LIIS // ID C5QBX7_STAEP Unreviewed; 199 AA. AC C5QBX7; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0789_2101; OS Staphylococcus epidermidis BCM-HMP0060. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525374; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BCM-HMP0060; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHE01000090; EES57274.1; -; Genomic_DNA. DR ProteinModelPortal; C5QBX7; -. DR EnsemblBacteria; EES57274; EES57274; HMPREF0789_2101. DR PATRIC; 31390241; VBIStaEpi34063_0497. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 22752 MW; A468A47409C7D4D7 CRC64; MGGIFIFIAI TYHKQLTRDD LQHYKHIEEA IDGLLFRTSM NNEENKDMIQ SLLQLGFSKD KIIIHSDVTL LEDLHLKRIH FKENDTTAFT YKEAHPDICV SMSTHDVETV KRCYENGLDS VFFGHIFPTS SHPNVPPRSK EAIQQALNVP IPIYAIGGIN EHSLQKMPPG FKGICAISYF NNASLEEIKQ LRKEWSTHA // ID C5QD00_STAEP Unreviewed; 215 AA. AC C5QD00; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0789_2474; OS Staphylococcus epidermidis BCM-HMP0060. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525374; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BCM-HMP0060; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHE01000108; EES56947.1; -; Genomic_DNA. DR ProteinModelPortal; C5QD00; -. DR EnsemblBacteria; EES56947; EES56947; HMPREF0789_2474. DR PATRIC; 31393822; VBIStaEpi34063_2280. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23998 MW; 87DCB45162513A97 CRC64; MNMMFDSKQL SVYFICGTQD IPKNKSIEQV LKEALEAGIT LYQFREKGPN ALKGEKKKQL ALKLKQLCHS YHVPMIVNDD VQLAQEINAD GIHVGQDDME IQQFASQFKN KIIGLSVGNL KEYQQSDLSK VDYIGVGPMY TTSSKDDASK PVGPSMISQL RLYIHDFPIV AIGGINETNV QPIVDEGADG ISVISAITRS TNIDKTVKYF LRYFT // ID C5QLB8_9STAP Unreviewed; 212 AA. AC C5QLB8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0793_0024; OS Staphylococcus caprae M23864:W1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525378; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23864:W1; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJB01000002; EES42303.1; -; Genomic_DNA. DR ProteinModelPortal; C5QLB8; -. DR EnsemblBacteria; EES42303; EES42303; HMPREF0793_0024. DR PATRIC; 31399020; VBIStaEpi14170_2379. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23262 MW; 9B102C26594BC706 CRC64; MFNPKQLQVY FICGTQDIPE GRTIEQVLEE ALQAGITLYQ FREKGPTALK GEDKKQLALK LKSLCQTYQV PFIVNDDVAL AKEIDADGIH VGQDDEAVKA FAAEFENKII GLSIGNLDEY QHSDLSQVNY IGVGPMYATP SKDDASEPVG PSMIKKLREY LDDFPIVAIG GINESNVASI AEADADGISV ISAISRSDNI DKTVKHFLSY FK // ID C5QMX6_9STAP Unreviewed; 197 AA. AC C5QMX6; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 13-NOV-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0793_0582; OS Staphylococcus caprae M23864:W1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525378; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23864:W1; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJB01000022; EES41680.1; -; Genomic_DNA. DR ProteinModelPortal; C5QMX6; -. DR EnsemblBacteria; EES41680; EES41680; HMPREF0793_0582. DR PATRIC; 31397557; VBIStaEpi14170_2150. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 197 AA; 22615 MW; 7402425C4654745C CRC64; MIHIFIAVTY DKVLTAQDLE HYLDIAEGID GLLFRTSMPQ KELKQSMIHL MNQGFAKDKI IVHSDIALLE DLNLKRIHFK ENDETAFSYK KTHPDIQVSM STHNAKSVRQ CIDRGLDYVF FGHIFPTTSH PNELPRTNDE IEEVLNLPFP IYAIGGISQQ TIAQVTKRFA GICAISFFMN ASLEDIKELK RKWLKHA // ID C5QTN1_STAEP Unreviewed; 213 AA. AC C5QTN1; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0791_0024; OS Staphylococcus epidermidis W23144. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525376; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=W23144; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJC01000001; EES37352.1; -; Genomic_DNA. DR ProteinModelPortal; C5QTN1; -. DR EnsemblBacteria; EES37352; EES37352; HMPREF0791_0024. DR PATRIC; 31403966; VBIStaEpi125410_2289. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23704 MW; 0E35EA2716A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDVPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID C5R009_STAEP Unreviewed; 160 AA. AC C5R009; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0791_2252; OS Staphylococcus epidermidis W23144. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525376; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=W23144; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJC01000156; EES35137.1; -; Genomic_DNA. DR ProteinModelPortal; C5R009; -. DR EnsemblBacteria; EES35137; EES35137; HMPREF0791_2252. DR PATRIC; 31402501; VBIStaEpi125410_1293. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18252 MW; D44AF318920FBC36 CRC64; MNNEENKDMI QSLLQLGFSK DKIIIHSDTT LLEELNLKRI HFKSNDTTAF AYKAAHPDIY VSMSTHDVET VKRCYENNLD YVFLGHIFPT ASHPDTPPRS KKTIQQALDV PIPIYAIGGI NEHSIYKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID C5RCR1_WEIPA Unreviewed; 205 AA. AC C5RCR1; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0877_1778; OS Weissella paramesenteroides ATCC 33313. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Weissella. OX NCBI_TaxID=585506; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33313; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKU01000033; EER73980.1; -; Genomic_DNA. DR ProteinModelPortal; C5RCR1; -. DR EnsemblBacteria; EER73980; EER73980; HMPREF0877_1778. DR PATRIC; 25678657; VBIWeiPar9200_0377. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22317 MW; 76F2AECBC76A8317 CRC64; MTKQLYLVTA RYDESENEFL NKIETACANG VTVVQLREKN LSTRDYYELA LKVKQITDKY DLPLIIDDRI DICLAVDAHG AHIGDDELPV KVARKLLGKD KILGVSAKTV TRATEAAADG ADYLGTGAIF PTQTKVVTKQ TSIDTLKAIT AAVNIPVVAI GGITEERIDV FKESGIVGVA IVSEIMKATN IAQKVQRLKK ALEML // ID C5S2K9_9PAST Unreviewed; 220 AA. AC C5S2K9; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-MAR-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AM305_10551; OS Actinobacillus minor NM305. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=637911; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NM305; RX PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030; RA Arya G., Niven D.F.; RT "Production of haemolysins by strains of the Actinobacillus RT minor/"porcitonsillarum" complex."; RL Vet. Microbiol. 141:332-341(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACQL01000099; EER46881.1; -; Genomic_DNA. DR ProteinModelPortal; C5S2K9; -. DR EnsemblBacteria; EER46881; EER46881; AM305_10551. DR PATRIC; 24363360; VBIActMin14942_1366. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24131 MW; EC0817D6CA7C85E4 CRC64; MNDIEKYLRL YFIAGSQDYR HLAGDPAQQL LNSLEQALAN GITCFQFRDK GVFSLEKSPQ EQKKLALKCR DLCRHYQVPF IINDNLALAL AINADGIHLG QTDLDIKLAQ EKISKPFILG LSINNLEQAL KSQSLEKVDY LGVGPIFPTS SKDDAAPAVG IGLIHQLNKH NITKPLVAIG GITEQNISLL TQCKIAGIAV ISAIIQSKNM LQTIKSLTII // ID C5T8R2_ACIDE Unreviewed; 302 AA. AC C5T8R2; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=AcdelDRAFT_3292; OS Acidovorax delafieldii 2AN. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=573060; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2AN; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Shelobolina E.S., Picardal F., Roden E., Emerson D.; RT "The draft genome of Acidovorax delafieldii 2AN."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACQT01000159; EER59129.1; -; Genomic_DNA. DR ProteinModelPortal; C5T8R2; -. DR EnsemblBacteria; EER59129; EER59129; AcdelDRAFT_3292. DR PATRIC; 38322590; VBIAciDel137164_3183. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 302 AA; 31995 MW; B51B67FF6439901F CRC64; MRDIAALRRA IVQHHAAAFP GFPPQPAPAP ASTEPVYQAA LQACSDLGFV AHDAECLARA WQARALRTGH FAPEQWPHEP QDFGLQTLPR AHGFAACPQD LGLYAVLPDA QWVGRMARAG VPTVQLRFKS DDPSAVAREV AAAVQAVQGT PALLFINDHW RQAIAAGAYG VHLGQEDLDA LLPAELHALR ASGLRLGVST HGYAEMVRAD AVGPSYIAMG AVFPTTLKKM ATVPQGVGRL SVYARLMRSY PLVAIGGIGA EQFAEVLATG VGSIAVVRAL VNAPDPEAAA RTLMAHMEQN TD // ID C5TLK3_NEIFL Unreviewed; 205 AA. AC C5TLK3; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NEIFL0001_0024; OS Neisseria flavescens SK114. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=596320; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK114; RA Shrivastava S., Sebastian Y., Madupu R., Durkin A.S., Torralba M., RA Methe B., Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACQV01000019; EER56490.1; -; Genomic_DNA. DR ProteinModelPortal; C5TLK3; -. DR EnsemblBacteria; EER56490; EER56490; NEIFL0001_0024. DR PATRIC; 29959306; VBINeiFla25453_0951. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21968 MW; 70E928F27ACDC4A1 CRC64; MTFLPLKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKTL HGDELKREIA RCVAACRGGR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAADL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAE DVLATGVSSL AVVRAVTEAE NPEAVVKAFQ ALWDE // ID C5UXN9_CLOBO Unreviewed; 210 AA. AC C5UXN9; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-MAR-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLO_0433; OS Clostridium botulinum E1 str. 'BoNT E Beluga'. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=536233; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BoNT E Beluga; RA Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C., RA Green L.D., Munk C.A., Rogers Y.C., Sims D.R., Smith L.A., Smith T.J., RA Sutton G., Tapia R., Brettin T.; RT "Genome sequence of Clostridium botulinum E1 BoNT E Beluga."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACSC01000002; EES50108.1; -; Genomic_DNA. DR ProteinModelPortal; C5UXN9; -. DR EnsemblBacteria; EES50108; EES50108; CLO_0433. DR PATRIC; 26430868; VBICloBot69965_0397. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23200 MW; 697DB02715FA13D8 CRC64; MKNKIDYSIY LVTDRDLMST NTLEEAVEKS ILGGATLIQL REKECSSHDF YETALKIKKT TQKYNIPLII NDRVDIALAV DADGIHIGQS DLPATVVRNI IGEDKILGVS AGNLEQALKA QKDSADYIGV GAMYSTVTKK DATSTTMSEL KEMTQKVSIP VVVIGGINKE RIKDFKETDI DGLAIVSAII AQKDIEKATR ELKEEFYKIK // ID C5VVR0_STRSE Unreviewed; 229 AA. AC C5VVR0; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SSU0687; OS Streptococcus suis (strain P1/7). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=218494; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1/7; RX PubMed=19603075; DOI=10.1371/journal.pone.0006072; RA Holden M.T.G., Hauser H., Sanders M., Ngo T.H., Cherevach I., RA Cronin A., Goodhead I., Mungall K., Quail M.A., Price C., RA Rabbinowitsch E., Sharp S., Croucher N.J., Chieu T.B., Mai N.T.H., RA Diep T.S., Chinh N.T., Kehoe M., Leigh J.A., Ward P.N., Dowson C.G., RA Whatmore A.M., Chanter N., Iversen P., Gottschalk M., Slater J.D., RA Smith H.E., Spratt B.G., Xu J., Ye C., Bentley S., Barrell B.G., RA Schultsz C., Maskell D.J., Parkhill J.; RT "Rapid evolution of virulence and drug resistance in the emerging RT zoonotic pathogen Streptococcus suis."; RL PLoS ONE 4:E6072-E6072(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM946016; CAR45467.1; -; Genomic_DNA. DR RefSeq; YP_003026576.1; NC_012925.1. DR ProteinModelPortal; C5VVR0; -. DR STRING; 218494.SSU0687; -. DR EnsemblBacteria; CAR45467; CAR45467; SSU0687. DR GeneID; 8152878; -. DR KEGG; ssi:SSU0687; -. DR PATRIC; 19786304; VBIStrSui84581_0661. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSUI218494:GJDS-736-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 24866 MW; 13EC09C5B3734B31 CRC64; MNRKMLQVYF ICGTSDCPKG KFLDVLEKAL QAGITCFQFR EKGEQGLTGA DKLLLAKQVQ HLCHRYQVPL IINDDVELAR AIDADGIHLG QEDLSVVEAR QLFPGKIIGL SVGTKEEYLN SPIDLVDYIG SGPVFPTLSK DDASPAIGMD GLKQLRKLNS DIPMVAIGGL SAKDCKEVLQ AGADGIAVIS AISHAEDPYK ATKILVDGMQ AMILKFNQVE SNKQILKNP // ID C5YTC8_SORBI Unreviewed; 547 AA. AC C5YTC8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE SubName: Full=Putative uncharacterized protein Sb08g005560; GN Name=Sb08g005560; ORFNames=SORBIDRAFT_08g005560; OS Sorghum bicolor (Sorghum) (Sorghum vulgare). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogoneae; Sorghum. OX NCBI_TaxID=4558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623; RX PubMed=19189423; DOI=10.1038/nature07723; RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., RA Schmutz J., Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., RA Chapman J., Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., RA Maher C.A., Martis M., Narechania A., Otillar R.P., Penning B.W., RA Salamov A.A., Wang Y., Zhang L., Carpita N.C., Freeling M., RA Gingle A.R., Hash C.T., Keller B., Klein P., Kresovich S., RA McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman M., Ware D., RA Westhoff P., Mayer K.F.X., Messing J., Rokhsar D.S.; RT "The Sorghum bicolor genome and the diversification of grasses."; RL Nature 457:551-556(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000767; EES16808.1; -; Genomic_DNA. DR RefSeq; XP_002442970.1; XM_002442925.1. DR ProteinModelPortal; C5YTC8; -. DR STRING; 4558.Sb08g005560.1; -. DR EnsemblPlants; Sb08g005560.1; Sb08g005560.1; Sb08g005560. DR GeneID; 8084752; -. DR KEGG; sbi:SORBI_08g005560; -. DR Gramene; C5YTC8; -. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 547 AA; 57782 MW; E3F4ECB2D2B5B687 CRC64; MASVPPLPPY RPRHSDAAAL LFRSPSFSPG VSPASATRPP RRFPVVASAR DMPWPHVLTV AGSDSGAGAG IQADIKACAA LGAYCSSVIT AVTAQNTVGV QGVHAVPEEF VGEQLRSVLS DMSVDVVKTG MLPSAGVVKV LCESLRKFPV KALVVDPVMV STSGDTLSGP STLATYRDEL FSVADIVTPN VKEASKLLGD VSLHTISDMR NAAESIYKLG PKYVLVKGGD MPDSSDAIDV LFDGKEFTEL RGPRIKTRNT HGTGCTLASC IAAELAKGAT MLHAVQVAKK FVESALYHSK DLVIGNGPQG PFDHLFELKS PLYKMGSLQK FNPDNLFLYA VTDSGMNKKW DRSIKDAVKA AIEGGATIVQ LREKDADTRE FLEAAKACVQ ICKSSGVPLL INDRIDVALA CNADGVHVGQ SDMPAWEVRE LLGPGKIIGV SCKTLDQAEQ AWKDGADYIG CGGVFPTTTK KNNPTLGFEG LRTVCLASKL PVVAIGGINA GNAGSVMELG FPNLKGVAVV SALFDQECVA IETRNLRSIL KNACSRS // ID C5ZDZ9_BURPE Unreviewed; 367 AA. AC C5ZDZ9; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=BURPS1106B_A2949; OS Burkholderia pseudomallei 1106b. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=357347; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1106b; RA Harkins D.M., DeShazer D., Woods D.E., Brinkac L.M., Brown K.A., RA Hung G.C., Tuanyok A., Zhang B., Nierman W.C.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000774; EES23872.1; -; Genomic_DNA. DR ProteinModelPortal; C5ZDZ9; -. DR EnsemblBacteria; EES23872; EES23872; BURPS1106B_A2949. DR PATRIC; 27814860; VBIBurPse45763_3768. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 367 AA; 38266 MW; 130C8EEBCCFAAA13 CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PQPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAQIARL NAAGAQAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEVE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA ATDYREAIVA LQQNFGR // ID C5ZSI9_BURPE Unreviewed; 209 AA. AC C5ZSI9; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 22-JAN-2014, entry version 23. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BURPS1106B_2740; OS Burkholderia pseudomallei 1106b. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=357347; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1106b; RA Harkins D.M., DeShazer D., Woods D.E., Brinkac L.M., Brown K.A., RA Hung G.C., Tuanyok A., Zhang B., Nierman W.C.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000775; EES22922.1; -; Genomic_DNA. DR ProteinModelPortal; C5ZSI9; -. DR EnsemblBacteria; EES22922; EES22922; BURPS1106B_2740. DR PATRIC; 27821929; VBIBurPse45763_4681. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID C5ZVE4_9HELI Unreviewed; 188 AA. AC C5ZVE4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 22-JAN-2014, entry version 23. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HCAN_0079, HCMG_01072; OS Helicobacter canadensis MIT 98-5491. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=537970; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MIT 98-5491; RG The Broad Institute Genome Sequencing Platform; RA Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T., RA Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., RA Shea T., Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., RA Galagan J., Nusbaum C., Birren B.; RT "Annotation of Helicobacter canadensis strain MIT 98-5491."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MIT 98-5491; RX PubMed=19542273; DOI=10.1128/JB.00729-09; RA Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J., RA Weinstock G.M., Wren B.W., Pallen M.J.; RT "Genome sequence of the emerging pathogen Helicobacter canadensis."; RL J. Bacteriol. 191:5566-5567(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000776; EES88803.1; -; Genomic_DNA. DR EMBL; DS990369; EFR48899.1; -; Genomic_DNA. DR EnsemblBacteria; EES88803; EES88803; HCAN_0079. DR EnsemblBacteria; EFR48899; EFR48899; HCMG_01072. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 188 AA; 21561 MW; F8E690757B348A08 CRC64; MRKHIKAYLI TDPNLYPNSP LKFYDFYKNI LDSQAISFAC YRDKESPNPK LFEVFLKLNQ SYQIPSLLNS HFDMALQYGF DGLHCNSKQM HQISNAKQKL PLVFFSAHNE QEIKEADSYG ANGITISPIF QTPNKGQPLG VDFLKRLDLN CYKAEIFALG GIISQKEILE ISQIPFCSFA SIRYFLNS // ID C5ZZ63_9HELI Unreviewed; 205 AA. AC C5ZZ63; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; GN Name=thiE; ORFNames=HCAN_0604; OS Helicobacter canadensis MIT 98-5491. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=537970; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MIT 98-5491; RX PubMed=19542273; DOI=10.1128/JB.00729-09; RA Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J., RA Weinstock G.M., Wren B.W., Pallen M.J.; RT "Genome sequence of the emerging pathogen Helicobacter canadensis."; RL J. Bacteriol. 191:5566-5567(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000776; EES89321.1; -; Genomic_DNA. DR ProteinModelPortal; C5ZZ63; -. DR EnsemblBacteria; EES89321; EES89321; HCAN_0604. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 23206 MW; 6371C8B41046A80D CRC64; MLQGIYAISD EILTPYQEIF AMLQKAIEGG ISIFQFRDKS HQDNQIESLV AELMDYCEQE QILFVLNDRI ELAMKLQTKG LHIGKKQEVH PYSLEELYMI RKSYGGILGI SCYGDLQLAQ NAKEIGADYI AFGSCFASPT KTQAKVISLD LFQKIQGIKK CAIGGINQQN IHQLQNVDMV ACISSIWKGD IIKNIDNLKR NWKNL // ID C6A1N5_THESM Unreviewed; 197 AA. AC C6A1N5; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TSIB_0464; OS Thermococcus sibiricus (strain MM 739 / DSM 12597). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=604354; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MM 739 / DSM 12597; RX PubMed=19447963; DOI=10.1128/AEM.00718-09; RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V., RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.; RT "Metabolic versatility and indigenous origin of the archaeon RT Thermococcus sibiricus, isolated from a siberian oil reservoir, as RT revealed by genome analysis."; RL Appl. Environ. Microbiol. 75:4580-4588(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001463; ACS89530.1; -; Genomic_DNA. DR RefSeq; YP_002993879.1; NC_012883.1. DR ProteinModelPortal; C6A1N5; -. DR STRING; 604354.TSIB_0464; -. DR EnsemblBacteria; ACS89530; ACS89530; TSIB_0464. DR GeneID; 8095451; -. DR KEGG; tsi:TSIB_0464; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; TSIB604354:GHMS-484-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 26 30 HMP-PP binding (By similarity). FT REGION 122 124 THZ-P binding (By similarity). FT REGION 172 173 THZ-P binding (By similarity). FT METAL 59 59 Magnesium (By similarity). FT METAL 78 78 Magnesium (By similarity). FT BINDING 58 58 HMP-PP (By similarity). FT BINDING 96 96 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). FT BINDING 152 152 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 197 AA; 21354 MW; DCFECF876C035AD5 CRC64; MITDRRLKSE IESVREALEG GATSIQLRIK NAPTGEMIKI GKEIRELTKE YDALYFVDDR LDVALATDAD GVQLGPEDMP ISLAKEIGPN LIIGASVYSL EEALKAEKEG ADYLGAGSVF PTPTKRDVKV IGLEGLKRIV ESVKIPVVAI GGINHKNARD VLKTGVDGIA IISAIMGAED VKRATEEMRK IIEEVLR // ID C6A8Z5_BIFLB Unreviewed; 516 AA. AC C6A8Z5; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE SubName: Full=Phosphomethylpyrimidine kinase; GN OrderedLocusNames=Balac_1237; OS Bifidobacterium animalis subsp. lactis (strain Bl-04 / DGCC2908 / RB OS 4825 / SD5219). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=580050; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bl-04 / DGCC2908 / RB 4825 / SD5219; RX PubMed=19376856; DOI=10.1128/JB.00155-09; RA Barrangou R., Briczinski E.P., Traeger L.L., Loquasto J.R., RA Richards M., Horvath P., Coute-Monvoisin A.C., Leyer G., Rendulic S., RA Steele J.L., Broadbent J.R., Oberg T., Dudley E.G., Schuster S., RA Romero D.A., Roberts R.F.; RT "Comparison of the complete genome sequences of Bifidobacterium RT animalis subsp. lactis DSM 10140 and Bl-04."; RL J. Bacteriol. 191:4144-4151(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001515; ACS46593.1; -; Genomic_DNA. DR RefSeq; YP_002968655.1; NC_012814.1. DR ProteinModelPortal; C6A8Z5; -. DR STRING; 580050.Balac_1237; -. DR EnsemblBacteria; ACS46593; ACS46593; Balac_1237. DR GeneID; 8009186; -. DR KEGG; blc:Balac_1237; -. DR PATRIC; 21108719; VBIBifAni84420_1240. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BANI580050:GI23-1237-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 516 AA; 54334 MW; BA2BECA74309264A CRC64; MNSFPYPSMR DRFDLRFYFV VGPDDCGNRP ILDVVAKALD GGASFIQLRA KTQDVAEIVS LANDIAEEIA GHHVEHSVAF VVDDRVDAAL EARAKGIKVD GVHIGQDDLD PVVARKLLGP DAIIGLSAKT VDEVREANHL PEGTIDYIGA GPLHMTATKP ESMIVDENGD ITTLNVSSID EMRTMSKYPL IVGGGVKADD IPMLAKTKAD GWFVVSAIAG ATDPEQATRR LVDDWTAIRG DEKPRYTGRK PAATKLPAVL TIATTDSSGG AGIPADLKTM LANDVFGECV VAGITAQNTT GVQAIAAVDP SIVGAQIDSV FDDIRPTAVK IGVIVGVESV KTVARKLRDH QATNIVVDPV MVATSGSSLA ADDTIAEEIS SLFPIATVIT PNIPEAQVLA QMPIGNQADM ETAAVQLAKD YGTCVLVKGG HGVKDADDVL AFPTGAVTWF EGERIANDNT HGTGCTLSSA IASYLAQGED LEDAVRDAKA YLSGALRANL NLGKGHGPMD HAWAMH // ID C6AAK1_BARGA Unreviewed; 220 AA. AC C6AAK1; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Thiamine-phosphate pyrophosphorylase ThiE2; GN Name=thiE2; OrderedLocusNames=Bgr_18340; OS Bartonella grahamii (strain as4aup). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=634504; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=as4aup; RX PubMed=19578403; DOI=10.1371/journal.pgen.1000546; RA Berglund E.C., Frank A.C., Calteau A., Vinnere Pettersson O., RA Granberg F., Eriksson A.S., Naslund K., Holmberg M., Lindroos H., RA Andersson S.G.; RT "Run-off replication of host-adaptability genes is associated with RT gene transfer agents in the genome of mouse-infecting Bartonella RT grahamii."; RL PLoS Genet. 5:E1000546-E1000546(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001562; ACS51940.1; -; Genomic_DNA. DR RefSeq; YP_002972632.1; NC_012846.1. DR STRING; 634504.Bgr_18340; -. DR EnsemblBacteria; ACS51940; ACS51940; Bgr_18340. DR GeneID; 7998798; -. DR KEGG; bgr:Bgr_18340; -. DR PATRIC; 20543151; VBIBarGra67450_1992. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FACVILY; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BGRA634504:GJI6-1827-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 220 AA; 24876 MW; 06DACD25A915DAC8 CRC64; MTKQKNKPID PPLFPQLILT LDVRRNTPHT FLQQILQTKS FACVILYDSE KLKDDSSFLQ QQAQTYAEDI QHHDAALLIA DDSRIVGRIK ADGLHIEDDL NALESFKNQQ KEQKIIGFGN LRNRHSAMLA AETGVDYLFF GKLGADKKPH AHPRNLQLAT WWAEIMQTPA IIQAGSDFST FDEALKTGCE FIAVEEVIFG NDNPLILLKT MQEKCENTPL // ID C6ACH4_BARGA Unreviewed; 201 AA. AC C6ACH4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; OrderedLocusNames=Bgr_05680; OS Bartonella grahamii (strain as4aup). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=634504; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=as4aup; RX PubMed=19578403; DOI=10.1371/journal.pgen.1000546; RA Berglund E.C., Frank A.C., Calteau A., Vinnere Pettersson O., RA Granberg F., Eriksson A.S., Naslund K., Holmberg M., Lindroos H., RA Andersson S.G.; RT "Run-off replication of host-adaptability genes is associated with RT gene transfer agents in the genome of mouse-infecting Bartonella RT grahamii."; RL PLoS Genet. 5:E1000546-E1000546(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001562; ACS50886.1; -; Genomic_DNA. DR RefSeq; YP_002971568.1; NC_012846.1. DR ProteinModelPortal; C6ACH4; -. DR STRING; 634504.Bgr_05680; -. DR EnsemblBacteria; ACS50886; ACS50886; Bgr_05680. DR GeneID; 7997541; -. DR KEGG; bgr:Bgr_05680; -. DR PATRIC; 20540280; VBIBarGra67450_0595. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BGRA634504:GJI6-567-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22943 MW; 8073922190022595 CRC64; MKLDPFYLIV DNADWVERLL PLGIKLVQLR MKHENQQIIR QHIKRAKNIC NKLGAQLIIN DHWEIAIDEK CNFIHLGQED LSNADLHAIR KSGIKVGLST HDEHELDIAL SVNPEYIALG PIYPTILKKM KWMPQGLEKI KQWRKRIGAL PLVGIGGLTP ERAVGVLKAG ANSAAVVTDI ILHKKPEERL QQWIKVTQTW R // ID C6AF37_BIFAS Unreviewed; 516 AA. AC C6AF37; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE SubName: Full=Phosphomethylpyrimidine kinase; GN OrderedLocusNames=Balat_1237; OS Bifidobacterium animalis subsp. lactis (strain DSM 10140 / JCM 10602 / OS LMG 18314). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=555970; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10140 / JCM 10602 / LMG 18314; RX PubMed=19376856; DOI=10.1128/JB.00155-09; RA Barrangou R., Briczinski E.P., Traeger L.L., Loquasto J.R., RA Richards M., Horvath P., Coute-Monvoisin A.C., Leyer G., Rendulic S., RA Steele J.L., Broadbent J.R., Oberg T., Dudley E.G., Schuster S., RA Romero D.A., Roberts R.F.; RT "Comparison of the complete genome sequences of Bifidobacterium RT animalis subsp. lactis DSM 10140 and Bl-04."; RL J. Bacteriol. 191:4144-4151(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001606; ACS48160.1; -; Genomic_DNA. DR RefSeq; YP_002970222.1; NC_012815.1. DR ProteinModelPortal; C6AF37; -. DR STRING; 555970.Balat_1237; -. DR EnsemblBacteria; ACS48160; ACS48160; Balat_1237. DR GeneID; 8010858; -. DR KEGG; blt:Balat_1237; -. DR PATRIC; 21112074; VBIBifAni93544_1241. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OMA; YLAQGEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BANI555970:GJ22-1236-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 516 AA; 54334 MW; BA2BECA74309264A CRC64; MNSFPYPSMR DRFDLRFYFV VGPDDCGNRP ILDVVAKALD GGASFIQLRA KTQDVAEIVS LANDIAEEIA GHHVEHSVAF VVDDRVDAAL EARAKGIKVD GVHIGQDDLD PVVARKLLGP DAIIGLSAKT VDEVREANHL PEGTIDYIGA GPLHMTATKP ESMIVDENGD ITTLNVSSID EMRTMSKYPL IVGGGVKADD IPMLAKTKAD GWFVVSAIAG ATDPEQATRR LVDDWTAIRG DEKPRYTGRK PAATKLPAVL TIATTDSSGG AGIPADLKTM LANDVFGECV VAGITAQNTT GVQAIAAVDP SIVGAQIDSV FDDIRPTAVK IGVIVGVESV KTVARKLRDH QATNIVVDPV MVATSGSSLA ADDTIAEEIS SLFPIATVIT PNIPEAQVLA QMPIGNQADM ETAAVQLAKD YGTCVLVKGG HGVKDADDVL AFPTGAVTWF EGERIANDNT HGTGCTLSSA IASYLAQGED LEDAVRDAKA YLSGALRANL NLGKGHGPMD HAWAMH // ID C6AQJ8_AGGAN Unreviewed; 220 AA. AC C6AQJ8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NT05HA_1780; OS Aggregatibacter aphrophilus (strain NJ8700) (Haemophilus aphrophilus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=634176; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NJ8700; RX PubMed=19447908; DOI=10.1128/JB.00447-09; RA Di Bonaventura M.P., DeSalle R., Pop M., Nagarajan N., Figurski D.H., RA Fine D.H., Kaplan J.B., Planet P.J.; RT "Complete genome sequence of Aggregatibacter (Haemophilus) aphrophilus RT NJ8700."; RL J. Bacteriol. 191:4693-4694(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001607; ACS98107.1; -; Genomic_DNA. DR RefSeq; YP_003008194.1; NC_012913.1. DR ProteinModelPortal; C6AQJ8; -. DR STRING; 634176.NT05HA_1780; -. DR EnsemblBacteria; ACS98107; ACS98107; NT05HA_1780. DR GeneID; 8122150; -. DR KEGG; aap:NT05HA_1780; -. DR PATRIC; 31918576; VBIAggAph86045_1666. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; AAPH634176:GHVL-1743-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 49 53 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24139 MW; 6068529F0E0FE2F8 CRC64; MPTSVSHLAE IVPPNAPFAP TEFKLGLYVI VDSYEWIERL IHAGVKTLQI RIKDRSPEQA KEEIARCIAL AKQHQVRLFV DDFWQLAIKY QSYGVHLGQE DLLTADLNAI QQAGLRLGVS THNREEIELV LPLRPSYIAL GHIFPTQSKI MPSAPQGIAN LAAQVKDLGD IPTVAIGGIT VSHFADVLTT GVGSIAVISA VTQAEDWQSA VQNLLHYFDA // ID C6AVZ2_RHILS Unreviewed; 217 AA. AC C6AVZ2; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Rleg_3568; OS Rhizobium leguminosarum bv. trifolii (strain WSM1325). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=395491; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM1325; RX PubMed=21304718; RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., RA Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M., RA Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., RA Melino V., Denton M., Yates R., Howieson J.; RT "Complete genome sequence of Rhizobium leguminosarum bv. trifolii RT strain WSM1325, an effective microsymbiont of annual Mediterranean RT clovers."; RL Stand. Genomic Sci. 2:347-356(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001622; ACS57814.1; -; Genomic_DNA. DR RefSeq; YP_002977353.1; NC_012850.1. DR ProteinModelPortal; C6AVZ2; -. DR STRING; 395491.Rleg_3568; -. DR EnsemblBacteria; ACS57814; ACS57814; Rleg_3568. DR GeneID; 8015818; -. DR KEGG; rlg:Rleg_3568; -. DR PATRIC; 23114609; VBIRhiLeg48398_4351. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RLEG395491:GHX2-3609-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 217 AA; 22842 MW; F146B743B202A163 CRC64; MTEPENRCRL VLIVPDIADA DEQAKIVADA LKGGDVASVI VPQYGLDDGT FQKHAEKLVP LIQDAGAAAL ISGDSRVAGR AKADGLHLSS NAEALSEAID KHAPKLIVGG GNAADRHHAL EIGEVRPDYI FFGKLDGDIK PEAHPKNLAL GEWWASMIEI PCIVMGGTDP ASALAVAETG AEFVALRLAV FAEPARAPSV VAEINALLDE KAPRFED // ID C6B6L1_RHILS Unreviewed; 211 AA. AC C6B6L1; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rleg_6680; OS Rhizobium leguminosarum bv. trifolii (strain WSM1325). OG Plasmid pR132502. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=395491; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM1325; PLASMID=pR132502; RX PubMed=21304718; RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., RA Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M., RA Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., RA Melino V., Denton M., Yates R., Howieson J.; RT "Complete genome sequence of Rhizobium leguminosarum bv. trifolii RT strain WSM1325, an effective microsymbiont of annual Mediterranean RT clovers."; RL Stand. Genomic Sci. 2:347-356(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001624; ACS59719.1; -; Genomic_DNA. DR RefSeq; YP_002984681.1; NC_012858.1. DR ProteinModelPortal; C6B6L1; -. DR STRING; 395491.Rleg_6680; -. DR EnsemblBacteria; ACS59719; ACS59719; Rleg_6680. DR GeneID; 8022590; -. DR KEGG; rlg:Rleg_6680; -. DR PATRIC; 23119237; VBIRhiLeg48398_6643. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RLEG395491:GHX2-5579-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Plasmid; KW Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21579 MW; 07F2B44F038F050F CRC64; MKAFDLSLYL VLDPDLCAGI GMVETARLAI AGGATMVQLR DKHAGTIGMI ETGRALKQAL DGTGALLIVN DDVEAAIAIG ADGLHIGQED MDAMRARTMI GPDMILGLSV ESEALANAVD PDLVDYTGVG PVFATPTKAD HKQPIGFDGL ARLVKASPVP SVAIGGLKAD HVAQVFAAGA SGLAVVSAIC GTPDPEAATR RIAAEIRKAR A // ID C6BHZ0_RALP1 Unreviewed; 384 AA. AC C6BHZ0; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Rpic12D_3322; OS Ralstonia pickettii (strain 12D). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=428406; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12D; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., RA Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., RA Kyrpides N., Ovchinnikova G., Marsh T., Richardson P.; RT "Complete sequence chromosome 1 of Ralstonia pickettii 12D."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001644; ACS64586.1; -; Genomic_DNA. DR RefSeq; YP_002983258.1; NC_012856.1. DR ProteinModelPortal; C6BHZ0; -. DR STRING; 428406.Rpic12D_3322; -. DR EnsemblBacteria; ACS64586; ACS64586; Rpic12D_3322. DR GeneID; 8021006; -. DR KEGG; rpf:Rpic12D_3322; -. DR PATRIC; 20245723; VBIRalPic57998_3926. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; RPIC428406:GH9Y-3382-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 384 AA; 40267 MW; 3332B7BB1183E924 CRC64; MSLSALRFSA AWPEAAALAA QIVDRHAEAF GRASHAWSVT DRADEATSAA TVLLTTDAGQ AERARSAGAA VVLTAVEGDL LIDTVHDRLG TYRFTSAAQG DAFDARFVAV FGAALALAFE PRDALCVARA WIAEANADAL AWPTQFDALP RVLEPALPCP TAADLAFAPC PTQLGIYAVV PDADWVARLV ALKVPTVQLR FKSDDAQAVV DQVRRAEAAA RGSATRLFIN DHWQVALDVH TQAPDSGIYG IHLGQEDIDE ADLVAIRSAG LRLGISTHGF AEMLRVAPLN PSYLALGAVF ATPTKTMPTV PQGLGRLFAY AAAMRTREPA PPLVAIGGID LAAMPRVLES GVGCVAVVRA ITQAPDVPAA VDALQATFAA HVRA // ID C6BYU8_DESAD Unreviewed; 216 AA. AC C6BYU8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Desal_2651; OS Desulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIB 8403 / OS VKM B-1763). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=526222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., RA Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., RA Anderson I., Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., RA Hazen T.C.; RT "Complete sequence of Desulfovibrio salexigens DSM 2638."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001649; ACS80705.1; -; Genomic_DNA. DR RefSeq; YP_002992244.1; NC_012881.1. DR ProteinModelPortal; C6BYU8; -. DR STRING; 526222.Desal_2651; -. DR EnsemblBacteria; ACS80705; ACS80705; Desal_2651. DR GeneID; 8093699; -. DR KEGG; dsa:Desal_2651; -. DR PATRIC; 21760853; VBIDesSal121003_2651. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DSAL526222:GHES-2715-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23931 MW; DE82DD51A36AA7BE CRC64; MSIRKITRQN ILDTDIYCLT ALKFSKDRSN IEVVREMLDN GIKLIQYREK EIKSGQKYEE CMEIRRMTRE AGAAFIVNDD IDLAMMVGAD GIHIGQEDFP VHAVRKLIGD EMAIGLSTHA PEEALAAVEA GVDYIGVGPI FKTYTKDDVV DPVGFEYLDW VVKNINIPFV AIGGIKEHNI AEVMNRGAKC VALVTEIVGA DDIGGMIKDL RSAMPK // ID C6C4R4_DICDC Unreviewed; 211 AA. AC C6C4R4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dd703_3716; OS Dickeya dadantii (strain Ech703). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Dickeya. OX NCBI_TaxID=579405; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ech703; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Balakrishnan V., Glasner J., Perna N.T.; RT "Complete sequence of Dickeya dadantii Ech703."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001654; ACS87471.1; -; Genomic_DNA. DR RefSeq; YP_002989293.1; NC_012880.1. DR ProteinModelPortal; C6C4R4; -. DR STRING; 579405.Dd703_3716; -. DR EnsemblBacteria; ACS87471; ACS87471; Dd703_3716. DR GeneID; 8087086; -. DR KEGG; dda:Dd703_3716; -. DR PATRIC; 21795097; VBIDicDad95084_3937. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; DDAD579405:GHJU-3795-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22938 MW; CDF5037565FE3180 CRC64; MNAAFPATEK RLGLYPVVDS VEWIARLLEA GVRTIQLRIK DLPDDQVEPA VMQAVALGRR YQARLFINDY WRLAITHRAY GVHLGQEDLD LADLAAIRQA GLRLGVSTHD DAELARAVAI QPSYIALGHI FPTQTKDMPS APQGLDELAR HINALDDRVP TVAIGGISID RAPAVLATGV GSIAVVSAIT QAPDWRQATA ALLRLIENRE A // ID C6CN78_DICZE Unreviewed; 211 AA. AC C6CN78; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dd1591_3871; OS Dickeya zeae (strain Ech1591). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Dickeya. OX NCBI_TaxID=561229; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ech1591; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Balakrishnan V., Glasner J., Perna N.T.; RT "Complete sequence of Dickeya zeae Ech1591."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001655; ACT08671.1; -; Genomic_DNA. DR RefSeq; YP_003006150.1; NC_012912.1. DR ProteinModelPortal; C6CN78; -. DR STRING; 561229.Dd1591_3871; -. DR EnsemblBacteria; ACT08671; ACT08671; Dd1591_3871. DR GeneID; 8118828; -. DR KEGG; dze:Dd1591_3871; -. DR PATRIC; 21803845; VBIDicZea111179_3941. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; DZEA561229:GJ85-3958-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22833 MW; CE823507EBC90803 CRC64; MKRAFPTTDA RLGLYPVVDS IAWIERLLDA GVRTLQLRIK DLPAEQAEPD ITRAIALGRQ YQARLFINDY WQLAVKHQAY GVHLGQEDLD TADLDAIRAA GLRLGVSTHD DAELARAVAL APSYIALGHI FPTQTKAMPS APQGLVELAR HIRTLDGRFP TVAIGGISID RVPAVLETGV GSIAVVSAIT QAADWRAATA TLLRLIEGRE A // ID C6D365_PAESJ Unreviewed; 214 AA. AC C6D365; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Pjdr2_5402; OS Paenibacillus sp. (strain JDR-2). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=324057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JDR-2; RX PubMed=22675593; DOI=10.4056/sigs.2374349; RA Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O., RA Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S., RA Nolan M., Pati A., Martin J., Copeland A., Land M.L., Goodwin L., RA Jones J.B., Ingram L.O., Shanmugam K.T., Preston J.F.; RT "Complete genome sequence of Paenibacillus sp. strain JDR-2."; RL Stand. Genomic Sci. 6:1-10(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001656; ACT04012.1; -; Genomic_DNA. DR RefSeq; YP_003014098.1; NC_012914.1. DR ProteinModelPortal; C6D365; -. DR STRING; 324057.Pjdr2_5402; -. DR EnsemblBacteria; ACT04012; ACT04012; Pjdr2_5402. DR GeneID; 8128355; -. DR KEGG; pjd:Pjdr2_5402; -. DR PATRIC; 22841287; VBIPaeSp118865_5345. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PSP324057:GH5H-5505-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23047 MW; 7EA65E68CE8E7269 CRC64; MKDFRLYAIT GEQFHPGRDM LEVMEEAIKG GVDIIQLRDK DGSPEEVLRK AKALRELTRK YGVTFIVNDY IDIALEVDAD GVHLGQNDVS LTEARQRVGD KIIGISTHAI EEALLAEEQG ADYIGVGPVF PTKTKVDVVD PVTVAYVRQV AEKVNIPFVA IGGIKLGNVD EVLAAGATRI CAVSEIVGSS DVAGTCQAFL RKLEGAGESH AADR // ID C6DHS5_PECCP Unreviewed; 213 AA. AC C6DHS5; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PC1_0215; OS Pectobacterium carotovorum subsp. carotovorum (strain PC1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pectobacterium. OX NCBI_TaxID=561230; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PC1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., RA Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Balakrishnan V., Glasner J., Perna N.T.; RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum RT PC1."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001657; ACT11275.1; -; Genomic_DNA. DR RefSeq; YP_003015811.1; NC_012917.1. DR ProteinModelPortal; C6DHS5; -. DR STRING; 561230.PC1_0215; -. DR EnsemblBacteria; ACT11275; ACT11275; PC1_0215. DR GeneID; 8131123; -. DR KEGG; pct:PC1_0215; -. DR PATRIC; 20484998; VBIPecCar70489_0218. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PCAR561230:GKCK-223-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23346 MW; 72126A1E20FB0D38 CRC64; MTDSTPFAPT AQRLGLYPVV DSVEWIERLL GVGVKTIQLR IKDRSDEQAE ADVIQAIALG RRYQAQLFIN DYWKLAVKHQ AYGVHLGQED LDTADLTAIK QAGLRLGIST HDDRELARAV AINPSYIALG HIFPTQTKDM PSAPQGLAEL TRHITDLQDR FPTVAIGGIS IDRVPAVRKT GVGSIAVVSA ITQAPDWRQA TATLLRMIEG REA // ID C6DSK4_MYCTK Unreviewed; 222 AA. AC C6DSK4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TBMG_00415; OS Mycobacterium tuberculosis (strain KZN 1435 / MDR). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=478434; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KZN 1435 / MDR; RA Murray M., Pillay M., Borowsky M.L., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Nusbaum C., Galagan J., Birren B.; RT "The genome sequence of Mycobacterium tuberculosis strain KZN 1435."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001658; ACT23443.1; -; Genomic_DNA. DR RefSeq; YP_003030338.1; NC_012943.1. DR ProteinModelPortal; C6DSK4; -. DR SMR; C6DSK4; 1-221. DR STRING; 478434.TBMG_00415; -. DR EnsemblBacteria; ACT23443; ACT23443; TBMG_00415. DR GeneID; 8164249; -. DR KEGG; mtb:TBMG_00415; -. DR PATRIC; 18158251; VBIMycTub122270_0451. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MTUB478434:GH8E-426-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID C6E0C3_GEOSM Unreviewed; 218 AA. AC C6E0C3; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GM21_0665; OS Geobacter sp. (strain M21). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=443144; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M21; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Lovley D.; RT "Complete sequence of Geobacter sp. M21."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001661; ACT16739.1; -; Genomic_DNA. DR RefSeq; YP_003020497.1; NC_012918.1. DR ProteinModelPortal; C6E0C3; -. DR STRING; 443144.GM21_0665; -. DR EnsemblBacteria; ACT16739; ACT16739; GM21_0665. DR GeneID; 8135980; -. DR KEGG; gem:GM21_0665; -. DR PATRIC; 22015824; VBIGeoSp56140_0659. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GSP443144:GHKM-681-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23631 MW; DF39679643773AD1 CRC64; MKELESPWID FNLYLITGRE ETKGRPLEYV VEEALKGGVR AVQYRDKDAS SKELYETAHE LRRLTSRYGA KLIVNDRADI ALAVEADGVH IGSASIPIYK VRRILGERKL IGVSCHNKAQ AIAAQEMGAD FITFGPVYYT PSKAPYGDPV GTAKLKAVAE LLQVPIFALG GINKENCAEA SDCGVRGVAL ISAILSAADP REAAKKLIAL LPPLEHAD // ID C6E5Z7_GEOSM Unreviewed; 484 AA. AC C6E5Z7; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE SubName: Full=Phosphomethylpyrimidine kinase; GN OrderedLocusNames=GM21_3528; OS Geobacter sp. (strain M21). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=443144; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M21; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Lovley D.; RT "Complete sequence of Geobacter sp. M21."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001661; ACT19549.1; -; Genomic_DNA. DR RefSeq; YP_003023307.1; NC_012918.1. DR ProteinModelPortal; C6E5Z7; -. DR STRING; 443144.GM21_3528; -. DR EnsemblBacteria; ACT19549; ACT19549; GM21_3528. DR GeneID; 8138900; -. DR KEGG; gem:GM21_3528; -. DR PATRIC; 22021504; VBIGeoSp56140_3444. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OMA; YLAQGEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; GSP443144:GHKM-3602-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 484 AA; 50631 MW; 0C05DFC80C4654C3 CRC64; MLRLVVDHSG KERRIGGLYL ITDQAERLVH RVREALSSGG VAVLQYRDKV RAYEERLELG QELKHLCTEF QVEFIVNDDV ELALALDADG VHLGQDDGDP AAAREALGPK KMIGISTHSL TEALEAQEAG ADYVGFGALY PTDSKEVEHI QGPEKLALLK GKLRIPVVAI GGIARDNACA VIDAGADAIA VISAVLSARS PGLAATELAL LFNRKAMQPR GGVLTVAGSD SGGGAGIQAD LKTVTLLGSY GASAITALTA QNTRGVNAIH PVPPAFLAEQ IDAVLSDIPI DVVKVGMLSS AENAAILADR LTAHGMRMVV LDPVMSAKGG VALLEGEALG VLKQRLIPLC YLLTPNIPEA EALTGLTITD TAGMELAARA LHLMGAKHVL VKGGHLTEGV VTDILFDGAG FTRFTAPRVL TRNTHGTGCT LASAIASYLA QGEPLPGAVL RAKLFVTRAI KYAQPLGKGH GPVNHFLAAK DQAE // ID C6EE25_ECOBD Unreviewed; 211 AA. AC C6EE25; C5WBM8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=B21_03823, ECBD_4039, ECD_03870; OS Escherichia coli (strain B / BL21-DE3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=469008; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BL21; RA Krempl P.M., Mairhofer J., Eisenkolb M., Specht T., Leparc G.G., RA Kreil D.P., Bayer K., Striedner G.; RT "Sequencing and gene expression analysis of Escherichia coli RT BL21(DE3)."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B / BL21-DE3 [Korea], and BL21; RX PubMed=19786035; DOI=10.1016/j.jmb.2009.09.052; RA Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., RA Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., RA Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W., RA Daegelen P., Kim J.F.; RT "Genome sequences of Escherichia coli B strains REL606 and RT BL21(DE3)."; RL J. Mol. Biol. 394:644-652(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B / BL21-DE3 [Austria]; RA Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.; RT "Sequencing and gene expression analysis of Escherichia coli BL21."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BL21-Gold; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., RA Rubin E.; RT "Complete sequence of Escherichia coli 'BL21-Gold(DE3)pLysS AG'."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B / BL21-DE3 [JGI]; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., RA Rubin E.; RT "Complete sequence of Escherichia coli BL21(DE3)."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BL21; RA Jeong H., Shim J.-H., Studier F.W., Oh T.K., Kim J.F.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001665; ACT31023.1; -; Genomic_DNA. DR EMBL; CP001509; ACT45662.1; -; Genomic_DNA. DR EMBL; AM946981; CAQ34340.1; -; Genomic_DNA. DR RefSeq; YP_003001555.1; NC_012892.2. DR RefSeq; YP_003038208.1; NC_012947.1. DR RefSeq; YP_003056433.1; NC_012971.2. DR SMR; C6EE25; 20-202. DR STRING; 469008.ECBD_4039; -. DR EnsemblBacteria; ACT31023; ACT31023; ECBD_4039. DR EnsemblBacteria; ACT45662; ACT45662; ECD_03870. DR EnsemblBacteria; CAQ34340; CAQ34340; B21_03823. DR GeneID; 8112793; -. DR GeneID; 8156547; -. DR GeneID; 8182435; -. DR KEGG; ebd:ECBD_4039; -. DR KEGG; ebe:B21_03823; -. DR KEGG; ebl:ECD_03870; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID C6GRF3_STRSX Unreviewed; 229 AA. AC C6GRF3; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SSUSC84_0653; OS Streptococcus suis (strain SC84). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=568813; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC84; RX PubMed=19603075; DOI=10.1371/journal.pone.0006072; RA Holden M.T.G., Hauser H., Sanders M., Ngo T.H., Cherevach I., RA Cronin A., Goodhead I., Mungall K., Quail M.A., Price C., RA Rabbinowitsch E., Sharp S., Croucher N.J., Chieu T.B., Mai N.T.H., RA Diep T.S., Chinh N.T., Kehoe M., Leigh J.A., Ward P.N., Dowson C.G., RA Whatmore A.M., Chanter N., Iversen P., Gottschalk M., Slater J.D., RA Smith H.E., Spratt B.G., Xu J., Ye C., Bentley S., Barrell B.G., RA Schultsz C., Maskell D.J., Parkhill J.; RT "Rapid evolution of virulence and drug resistance in the emerging RT zoonotic pathogen Streptococcus suis."; RL PLoS ONE 4:E6072-E6072(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM252031; CAZ51431.1; -; Genomic_DNA. DR RefSeq; YP_003024675.1; NC_012924.1. DR ProteinModelPortal; C6GRF3; -. DR STRING; 568813.SSUSC84_0653; -. DR EnsemblBacteria; CAZ51431; CAZ51431; SSUSC84_0653. DR GeneID; 8150962; -. DR KEGG; sss:SSUSC84_0653; -. DR PATRIC; 19790256; VBIStrSui134201_0661. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSUI568813:GJFC-716-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 24866 MW; 13EC09C5B3734B31 CRC64; MNRKMLQVYF ICGTSDCPKG KFLDVLEKAL QAGITCFQFR EKGEQGLTGA DKLLLAKQVQ HLCHRYQVPL IINDDVELAR AIDADGIHLG QEDLSVVEAR QLFPGKIIGL SVGTKEEYLN SPIDLVDYIG SGPVFPTLSK DDASPAIGMD GLKQLRKLNS DIPMVAIGGL SAKDCKEVLQ AGADGIAVIS AISHAEDPYK ATKILVDGMQ AMILKFNQVE SNKQILKNP // ID C6GTL3_STRS4 Unreviewed; 229 AA. AC C6GTL3; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SSUBM407_1144; OS Streptococcus suis (strain BM407). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=568814; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BM407; RX PubMed=19603075; DOI=10.1371/journal.pone.0006072; RA Holden M.T.G., Hauser H., Sanders M., Ngo T.H., Cherevach I., RA Cronin A., Goodhead I., Mungall K., Quail M.A., Price C., RA Rabbinowitsch E., Sharp S., Croucher N.J., Chieu T.B., Mai N.T.H., RA Diep T.S., Chinh N.T., Kehoe M., Leigh J.A., Ward P.N., Dowson C.G., RA Whatmore A.M., Chanter N., Iversen P., Gottschalk M., Slater J.D., RA Smith H.E., Spratt B.G., Xu J., Ye C., Bentley S., Barrell B.G., RA Schultsz C., Maskell D.J., Parkhill J.; RT "Rapid evolution of virulence and drug resistance in the emerging RT zoonotic pathogen Streptococcus suis."; RL PLoS ONE 4:E6072-E6072(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM252032; CAZ56002.1; -; Genomic_DNA. DR RefSeq; YP_003028877.1; NC_012926.1. DR ProteinModelPortal; C6GTL3; -. DR STRING; 568814.SSUBM407_1144; -. DR EnsemblBacteria; CAZ56002; CAZ56002; SSUBM407_1144. DR GeneID; 8153732; -. DR KEGG; ssb:SSUBM407_1144; -. DR PATRIC; 19783075; VBIStrSui1141_1175. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSUI568814:GJD0-1217-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 24866 MW; 13EC09C5B3734B31 CRC64; MNRKMLQVYF ICGTSDCPKG KFLDVLEKAL QAGITCFQFR EKGEQGLTGA DKLLLAKQVQ HLCHRYQVPL IINDDVELAR AIDADGIHLG QEDLSVVEAR QLFPGKIIGL SVGTKEEYLN SPIDLVDYIG SGPVFPTLSK DDASPAIGMD GLKQLRKLNS DIPMVAIGGL SAKDCKEVLQ AGADGIAVIS AISHAEDPYK ATKILVDGMQ AMILKFNQVE SNKQILKNP // ID C6H4D7_AJECH Unreviewed; 647 AA. AC C6H4D7; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 16-APR-2014, entry version 24. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HCDG_01376; OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus) OS (Histoplasma capsulatum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Ajellomyces. OX NCBI_TaxID=544712; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H143; RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B., RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A.M., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B., RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G., RA San-Blas G., Taylor J.W., Mendoza L., Galagan J.E., Nusbaum C., RA Birren B.W.; RT "The genome sequence of Ajellomyces capsulatus strain H143."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG692419; EER45797.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.25.10.10; -; 1. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 2. DR Pfam; PF02581; TMP-TENI; 2. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF48371; SSF48371; 1. DR SUPFAM; SSF51391; SSF51391; 2. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 647 AA; 68700 MW; 6AAADF092EA30EAC CRC64; MDLSVYLVTD STPAILRGRD LCEVVQDAIQ GGVTVVQYRD KHSDSGVMIA TAKRLHEITK KHNVPLIIND RVDVALAVGA EGVHLGQDDM TGGPPTQIRD RNQRKPESEE LTVAAFDCIA TVCQVLVGPT AAAEIFNEIG TSTIVDQTVY LLLEGITDGT SDQVQLAAAR ALRTLTARVT HRVVLASLLP RSVSALTKAL QPTTQMRRSY QVLCCCIQAL TEMLKAVLND TNVSAPTPQK TDAKTQPGGN TLVLDDSWLN ATASQDGADY LGIGTVFATP TKTNTKSIIG PAGTREILAF LSTMPRRVGT VAIGGINLAN VQRVIYQSQA PLKSLDGAAI VSAIMAAENP REAAALFCKL VKQIPALATI PLPPRENEVT LLLDQVPDIV NLVATRRPLC HNMINFVVAN FAANVAIAIG ASPIMSGYGP EAVDLAKNGV GAGATDVRRK AAKQLMAGGY FDLIKGNESE LIQVYGKVRG HQVGVDSGPS TLNCKEKARL VMDLAKRERN IVLLTGAVDY LSDGERTLAI GNGHSLLGHI TGTGCIIGTI AASFLAVHRS DKLLAVLASL LLLEIAAERA AVKDGVHGPG TFLPAFIDEL FALRMWAVER KNGGTSSGEA SKTSNCEAAT VDENIFKKMA KVHLIHL // ID C6HXY1_9BACT Unreviewed; 211 AA. AC C6HXY1; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=UBAL3_93200095; OS Leptospirillum ferrodiazotrophum. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=412449; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=19429552; DOI=10.1128/AEM.02943-08; RA Goltsman D.S., Denef V.J., Singer S.W., VerBerkmoes N.C., Lefsrud M., RA Mueller R.S., Dick G.J., Sun C.L., Wheeler K.E., Zemla A., Baker B.J., RA Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., RA Banfield J.F.; RT "Community genomic and proteomic analyses of chemoautotrophic iron- RT oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum RT ferrodiazotrophum" (Group III) bacteria in acid mine drainage RT biofilms."; RL Appl. Environ. Microbiol. 75:4599-4615(2009). RN [2] RP NUCLEOTIDE SEQUENCE. RA Goltsman D.S.A., Denef V.J., Singer S.W., Verberkmoes N.C., RA Lefsrud M., Mueller R., Dick G.J., Sun C., Wheeler K., Zemla A., RA Baker B.J., Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., RA Banfield J.F.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG693875; EES52593.1; -; Genomic_DNA. DR ProteinModelPortal; C6HXY1; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT REGION 137 139 THZ-P binding (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22831 MW; F4CB6D9FC45BBEB6 CRC64; MDSPCSETLG PLLYVTPEEV PVRDLVRRAI ESTRGGVSAV ILRRKLSTSW EFSELVRHFR DNVPRGIPWL VNRRMDFALD GGATGLHLPE SHPPLPRIRQ RVFQGFLVGV SVHGPEAAEE AVREGADYLI AGPVFDTPSK RPFGPPLGLT RLKEIIRSVS VPVFAIGGIG PEEASMLRST GAAGMVVMGA LSYAPDPVAA AYALRKAWAR G // ID C6I0K2_9BACT Unreviewed; 217 AA. AC C6I0K2; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=UBAL3_95680095; OS Leptospirillum ferrodiazotrophum. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=412449; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=19429552; DOI=10.1128/AEM.02943-08; RA Goltsman D.S., Denef V.J., Singer S.W., VerBerkmoes N.C., Lefsrud M., RA Mueller R.S., Dick G.J., Sun C.L., Wheeler K.E., Zemla A., Baker B.J., RA Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., RA Banfield J.F.; RT "Community genomic and proteomic analyses of chemoautotrophic iron- RT oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum RT ferrodiazotrophum" (Group III) bacteria in acid mine drainage RT biofilms."; RL Appl. Environ. Microbiol. 75:4599-4615(2009). RN [2] RP NUCLEOTIDE SEQUENCE. RA Goltsman D.S.A., Denef V.J., Singer S.W., Verberkmoes N.C., RA Lefsrud M., Mueller R., Dick G.J., Sun C., Wheeler K., Zemla A., RA Baker B.J., Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., RA Banfield J.F.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG693887; EES51657.1; -; Genomic_DNA. DR ProteinModelPortal; C6I0K2; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23409 MW; 78EFDBC635990F02 CRC64; MNPPFPRLLY LAGTQDFDSV DSFERHLRTL LDAGLPWFQL RDKRLDDRSL SLLADRVRLW TRESGALFTL NDRPDIALLC EADGVHLGQE DLSALDEVHS SDERKRRAIH LGISTHNKNE VLRALTHRPD YLGVGPIFAS TTKETGVAPR GVSALFETRE LTALPLVAIG GITRENGAAL LAAGAGTLAV SSLLARADSP GGVLKALLAM PAKPSSG // ID C6I939_9BACE Unreviewed; 204 AA. AC C6I939; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSHG_2765; OS Bacteroides sp. 3_2_5. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457392; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_2_5; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., RA Strauss J., Ambrose C., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. 3_2_5."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIB02000014; EES86476.1; -; Genomic_DNA. DR ProteinModelPortal; C6I939; -. DR EnsemblBacteria; EES86476; EES86476; BSHG_2765. DR PATRIC; 30521445; VBIBacSp21143_2695. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22145 MW; 39E07889150674CF CRC64; MLSLQFITHQ TENYSYLESA RMALEGGCKW IQLRMKEASP EEVEAVALQL KPLCKAKEAI LILDDHVELA KKLEVDGVHL GKKDMPIGEA RQMLGEAFII GGTANTFEDV KLHHAAGADY LGIGPFRFTT TKKNLSPVLG LEGYTSILAQ MNEADIRIPV VAIGGIVAED IPPIMETGVN GIALSGAILQ APDPIEETKR ILNI // ID C6I945_9BACE Unreviewed; 202 AA. AC C6I945; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 13-NOV-2013, entry version 23. DE SubName: Full=Uncharacterized protein; GN ORFNames=BSHG_2771; OS Bacteroides sp. 3_2_5. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457392; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_2_5; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., RA Strauss J., Ambrose C., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. 3_2_5."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIB02000014; EES86482.1; -; Genomic_DNA. DR ProteinModelPortal; C6I945; -. DR SMR; C6I945; 1-202. DR EnsemblBacteria; EES86482; EES86482; BSHG_2771. DR PATRIC; 30521457; VBIBacSp21143_2701. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23245 MW; A6533F52928C16DB CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHKRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYSGH ISCSCHSVEE VKNKKHFYDY VFMSPVYDSI SKEGYNSPYT AEELRLAAKD KIIDNKVMAL GGITPDNILE VKDFGFGGAV VLGDLWGKFD ACSDQDYLAV IEHFKKLKRM AD // ID C6IGS5_9BACE Unreviewed; 209 AA. AC C6IGS5; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSIG_0946; OS Bacteroides sp. 1_1_6. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469586; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_6; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., RA Strauss J., Ambrose C., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. 1_1_6."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIC02000043; EES70673.1; -; Genomic_DNA. DR ProteinModelPortal; C6IGS5; -. DR EnsemblBacteria; EES70673; EES70673; BSIG_0946. DR PATRIC; 30486893; VBIBacSp91036_0877. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22914 MW; 3A0A0BC8ACE7CA8E CRC64; MVSLQFITHQ TDRYTYFESA LMALEGGCKW IQLRMKEAPC EEVEAVALQL KPLCKEKEAI LLLDDHVELA KKLEVDGVHL GKKDMPIDQA RQLLGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYAAILSQ MKEANIELPV VAIGGITCED IPAILETGVN GIALSGTILR AEDPAAETRK ILNMKCIIK // ID C6IGT1_9BACE Unreviewed; 202 AA. AC C6IGT1; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 13-NOV-2013, entry version 23. DE SubName: Full=Uncharacterized protein; GN ORFNames=BSIG_0952; OS Bacteroides sp. 1_1_6. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469586; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_6; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., RA Strauss J., Ambrose C., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. 1_1_6."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIC02000042; EES70679.1; -; Genomic_DNA. DR ProteinModelPortal; C6IGT1; -. DR EnsemblBacteria; EES70679; EES70679; BSIG_0952. DR PATRIC; 30486903; VBIBacSp91036_0882. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23435 MW; 47E2A222E5AEB243 CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHRRIVTH EHFYLKEEFN LMGIHLNARN PSEPHDYAGH VSCSCHSVEE VKNRKHFYDY IFMSPIYDSI SKVNYYSTYT AEELREAQKA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNKFD ACLDQNYLAV IEHFKKLKKL AD // ID C6IZJ0_9BACL Unreviewed; 214 AA. AC C6IZJ0; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=POTG_01436; OS Paenibacillus sp. oral taxon 786 str. D14. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=621372; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D14; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Sibley C., White A., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Paenibacillus sp. D14."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG695973; EES73729.1; -; Genomic_DNA. DR ProteinModelPortal; C6IZJ0; -. DR EnsemblBacteria; EES73729; EES73729; POTG_01436. DR PATRIC; 25844017; VBIPaeSp50414_1676. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 214 AA; 23041 MW; EE2B0DF9E6A3168C CRC64; MTSQKLTLTA PELHLISISP IHVSELLRVS LKALPYLDYI HVRDKQLTAK GQLEIIQQMF ESGIPLNKIV VNDRLDVALA ARAVNVHLAG HSLPVDSARP LASGMRLGRS VHSVEETVQA AVDGADYCLF GHVYDTSSKP GLPGRGLAAL TATAKACPVP MIAIGGIRPD QAGEIIRCGA QGIAVMTRLF HAPDPAEEAQ AYRKAMQAAW LERR // ID C6J7A6_9BACL Unreviewed; 228 AA. AC C6J7A6; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=POTG_04283; OS Paenibacillus sp. oral taxon 786 str. D14. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=621372; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D14; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Sibley C., White A., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Paenibacillus sp. D14."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG696000; EES71124.1; -; Genomic_DNA. DR ProteinModelPortal; C6J7A6; -. DR EnsemblBacteria; EES71124; EES71124; POTG_04283. DR PATRIC; 25849927; VBIPaeSp50414_4346. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 23448 MW; C5C2FBB68571DA52 CRC64; MSGGGGSGRI AADWMRKLLR TYLVLGSPNC RDHPLRVLEA ALDGGVTLVQ FREKGPGALT GEPLRALAVQ LLAACRRRGV PFLVNDDVEL ALAIGADGVH VGQEDEAAAQ VRARIGDRIL GVSAHTFAEA EAAVRHGADY LGIGPIYPTA SKADAKAPQG PAILRELRDR GITLPLVGIG GITAETAGDV IRAGADGVAV ISAITLADDV RQAAAQLYAT TDAGTSTT // ID C6JDJ7_9FIRM Unreviewed; 212 AA. AC C6JDJ7; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RSAG_02014; OS Ruminococcus sp. 5_1_39BFAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=457412; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_39BFAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_39BFAA; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., RA Strauss J., Ambrose C., Walker B., Young S., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Ruminococcus sp. 5_1_39BFAA."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACII02000003; EES76746.1; -; Genomic_DNA. DR ProteinModelPortal; C6JDJ7; -. DR EnsemblBacteria; EES76746; EES76746; RSAG_02014. DR PATRIC; 29805815; VBIRumSp107365_1958. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22879 MW; B2A6A109E447350C CRC64; MKFDKEKMRL YAITDRHWLN GRSLKEVVKE SLDGGVTFLQ LRDKNSDDET FLQEAAELQE LCRDYKVPLI INDNVEIALK MNADGVHVGQ SDMEAGAVRE KLGPDKILGV SARTVEQALL AQERGADYLG VGAVFATGSK ADAAELPHET LKAICEAVSI PVVAIGGITA ENISQLKGTG ICGVAVISAI YAQNNIKEAA EELKEAVDKI VL // ID C6JFL5_9FIRM Unreviewed; 191 AA. AC C6JFL5; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 2. DT 19-FEB-2014, entry version 24. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=RSAG_02729; OS Ruminococcus sp. 5_1_39BFAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=457412; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_39BFAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_39BFAA; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., RA Strauss J., Ambrose C., Walker B., Young S., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Ruminococcus sp. 5_1_39BFAA."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACII02000002; EES76198.2; -; Genomic_DNA. DR EnsemblBacteria; EES76198; EES76198; RSAG_02729. DR PATRIC; 29807282; VBIRumSp107365_2681. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 191 AA; 21402 MW; 981C77F6BA102F37 CRC64; MQKNPYENVI AVTNRSLCQR PFAEQIERVC SLHPKAVILR EKDLPEEEYS RLAEQILEIC KRYQVPCILH TYVNVAEKLH HPYIHLPIFL LEKYEGKLGG FRQIGSSVHS VEDALKAESL GADYLTAGHI YTTDCKKGLP PRGLEFLENV CKAVKIPVYA IGGIHPGTGQ LNEIMEHGSA GGCIMSDMMK I // ID C6JRE4_FUSVA Unreviewed; 211 AA. AC C6JRE4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FVAG_01176; OS Fusobacterium varium ATCC 27725. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469618; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27725; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium varium ATCC 27725."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIE02000012; EES63487.1; -; Genomic_DNA. DR ProteinModelPortal; C6JRE4; -. DR EnsemblBacteria; EES63487; EES63487; FVAG_01176. DR PATRIC; 28754331; VBIFusVar73376_2785. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23436 MW; 935B904B65A831A7 CRC64; MRNRIDIPKG LYGITGDNFA NGKSNYECVE EMIKGGIKIV QYRDKFKSTR EKVEEAKAIK KLCHKNNVLF IVNDDVAVAM LVDADGVHVG QDDMKPDDVR KLIGINKIIG LSTHSEEQGM AAYNNENVDY IGVGPIFPTT TKDTAPVGLE YLEFAVKNLH LPFIAIGGIK EYNIDEIIKR GAQRICLVSD IVGAENICKK IINLNSKILK K // ID C6KSY2_PLAF7 Unreviewed; 538 AA. AC C6KSY2; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE SubName: Full=Thiamin-phosphate pyrophosphorylase, putative; DE EC=2.5.1.3; GN ORFNames=PFF0680c; OS Plasmodium falciparum (isolate 3D7). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=36329; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate 3D7; RX PubMed=12368864; DOI=10.1038/nature01097; RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., RA James K.D., Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., RA Kyes S., Chan M.-S., Nene V., Shallom S.J., Suh B., Peterson J., RA Angiuoli S., Pertea M., Allen J., Selengut J., Haft D., Mather M.W., RA Vaidya A.B., Martin D.M.A., Fairlamb A.H., Fraunholz M.J., Roos D.S., RA Ralph S.A., McFadden G.I., Cummings L.M., Subramanian G.M., RA Mungall C., Venter J.C., Carucci D.J., Hoffman S.L., Newbold C., RA Davis R.W., Fraser C.M., Barrell B.G.; RT "Genome sequence of the human malaria parasite Plasmodium RT falciparum."; RL Nature 419:498-511(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate 3D7; RX PubMed=12368867; DOI=10.1038/nature01095; RA Hall N., Pain A., Berriman M., Churcher C., Harris B., Harris D., RA Mungall K., Bowman S., Atkin R., Baker S., Barron A., Brooks K., RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., RA Chillingworth T., Christodoulou Z., Clark L., Clark R., Corton C., RA Cronin A., Davies R., Davis P., Dear P., Dearden F., Doggett J., RA Feltwell T., Goble A., Goodhead I., Gwilliam R., Hamlin N., Hance Z., RA Harper D., Hauser H., Hornsby T., Holroyd S., Horrocks P., RA Humphray S., Jagels K., James K.D., Johnson D., Kerhornou A., RA Knights A., Konfortov B., Kyes S., Larke N., Lawson D., Lennard N., RA Line A., Maddison M., Mclean J., Mooney P., Moule S., Murphy L., RA Oliver K., Ormond D., Price C., Quail M.A., Rabbinowitsch E., RA Rajandream M.A., Rutter S., Rutherford K.M., Sanders M., Simmonds M., RA Seeger K., Sharp S., Smith R., Squares R., Squares S., Stevens K., RA Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J., RA Sulston J.E., Craig A., Newbold C., Barrell B.G.; RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13."; RL Nature 419:527-531(2002). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL844505; CAG25379.2; -; Genomic_DNA. DR RefSeq; XP_966127.2; XM_961034.2. DR ProteinModelPortal; C6KSY2; -. DR SMR; C6KSY2; 11-256. DR STRING; 5833.PFF0680c-1; -. DR EnsemblProtists; PFF0680c:mRNA; PFF0680c:pep; PFF0680c. DR GeneID; 3885718; -. DR KEGG; pfa:PFF0680c; -. DR EuPathDB; PlasmoDB:PF3D7_0614000; -. DR HOGENOM; HOG000281504; -. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 2. PE 4: Predicted; KW Complete proteome; Reference proteome; Transferase. SQ SEQUENCE 538 AA; 62651 MW; 54FF307A7EC6F3EE CRC64; MNIGKSGKSL KKCVDYSLYL VTDDKFLKDK ENVCGTFVNK IIQGVLGGVG LIQLRLKKSD DIYFYNTAVK MKNLLLPFNV PLIINNRLDI CLSVNADGVH LGKSDLPLYH ARNILGENKI IGATINFSDE KDIEMCINNK IDYIAHDHTL YESTTKKTIV SNEQGLKEQI QILENKIKYL YHKGKIIKSH NNTDDNFKNI IPPIILIGGI NTNNIQNTMI SFSNTCEGLA VVSCILDENS PSFVNTLKLK YIIDKYKKSD HVAFINMYSN CLNYLYYQHI EIEEQLNLPI IFHSTKKKNI NTFLVTNMIL DKNKSYFIPF KNNDYFDIIS LNEFFKNNEK ANLFLFHSSY DLFLNNNNKI DNNINGILNK EKHDDHIYEN IKEQIIKRII QLKHIKKEHM GHNIFILIGE EIWDLFNKHC YPQFFNSNFF FVIKKHSTIQ STMSEQWLYY DTQNACIQYN HNIINIFLKN AHFFSEENIK KFTLLMSYFL IVQDKEITPQ FLQQIATQGG TNFHEQTLWK FIATVDISLK LVEKSMGI // ID C6LBN2_9FIRM Unreviewed; 224 AA. AC C6LBN2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BRYFOR_06027; OS Marvinbryantia formatexigens DSM 14469. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Marvinbryantia. OX NCBI_TaxID=478749; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14469; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCL02000004; EET61835.1; -; Genomic_DNA. DR ProteinModelPortal; C6LBN2; -. DR EnsemblBacteria; EET61835; EET61835; BRYFOR_06027. DR PATRIC; 29033024; VBIBryFor99582_0897. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24412 MW; 6386E6388E0955F7 CRC64; MKFAKSTQSV RDAMLLYAVT DRMWLNGRRL CDVVEEAVKG GATMVQLREK ELSFTEFLSE AAEIKKVCEK YRVPFIINDN IEVALACDAD GVHVGQSDME AARVREKIGA GKILGVSAQT VQQALEAEKM GADYLGVGAV FTTSTKSDAD YVPYEELKAI CHAVKIPVCA IGGIYRHNMM QLAGSGIDGV ALVSAVFAAE HIETECRKLL AMSKKMTALK TDRL // ID C6M6Q7_NEISI Unreviewed; 205 AA. AC C6M6Q7; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NEISICOT_02209; OS Neisseria sicca ATCC 29256. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=547045; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29256; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKO02000013; EET44028.1; -; Genomic_DNA. DR ProteinModelPortal; C6M6Q7; -. DR EnsemblBacteria; EET44028; EET44028; NEISICOT_02209. DR PATRIC; 28213833; VBINeiSic1915_1780. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21894 MW; 2B86352A83F75CDC CRC64; MTFPPLKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKTL HGDELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAE DVLATGVSSL AVVRAVTKAE NPEAVVKAFQ ALWNE // ID C6NSS7_9GAMM Unreviewed; 315 AA. AC C6NSS7; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-MAR-2014, entry version 28. DE SubName: Full=Mutator mutT protein (7,8-dihydro-8-oxoguanine-triphosphatase) / Thiamin-phosphate pyrophosphorylase-like protein; DE EC=3.6.1.-; GN ORFNames=ACA_1205; OS Acidithiobacillus caldus ATCC 51756. OC Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=637389; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51756; RX PubMed=19617360; DOI=10.1128/JB.00843-09; RA Valdes J., Quatrini R., Hallberg K., Dopson M., Valenzuela P.D., RA Holmes D.S.; RT "Draft genome sequence of the extremely acidophilic bacterium RT Acidithiobacillus caldus ATCC 51756 reveals metabolic versatility in RT the genus Acidithiobacillus."; RL J. Bacteriol. 191:5877-5878(2009). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVD01000053; EET28013.1; -; Genomic_DNA. DR ProteinModelPortal; C6NSS7; -. DR EnsemblBacteria; EET28013; EET28013; ACA_1205. DR PATRIC; 24324955; VBIAciCal31047_0628. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 33501 MW; 1EA075213DEF9DB0 CRC64; MLLDLRPADK PWPGYWEFPG GKMEAGESPE AALHRELAEE LGITVRAATP WQVREYAYPE RRVRLHLYKV TAWEGRVHGR EGQELRWLSP AAAAALHLLP ANRGILADLS AEALPCPPLF LIADPQRAAA GAFLKILEQS TAAGLRALIL RIKGPLPAGL DAETLADWLA RAKGRGVQVY LNHPDPLPSW PVVGRHFTEA QLADCDASPS SPFGVSCHSA AGLARAEALG ASYALLSPLF PTATHPHTPA LGLARFAELA AAVAVPVIAL GGIDARRIPE ARRAGARGAA VLSEILSASD PHAATQTLIH AWNAA // ID C6NTD3_9GAMM Unreviewed; 219 AA. AC C6NTD3; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-MAR-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ACA_0942; OS Acidithiobacillus caldus ATCC 51756. OC Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=637389; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51756; RX PubMed=19617360; DOI=10.1128/JB.00843-09; RA Valdes J., Quatrini R., Hallberg K., Dopson M., Valenzuela P.D., RA Holmes D.S.; RT "Draft genome sequence of the extremely acidophilic bacterium RT Acidithiobacillus caldus ATCC 51756 reveals metabolic versatility in RT the genus Acidithiobacillus."; RL J. Bacteriol. 191:5877-5878(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVD01000057; EET27840.1; -; Genomic_DNA. DR ProteinModelPortal; C6NTD3; -. DR EnsemblBacteria; EET27840; EET27840; ACA_0942. DR PATRIC; 24325375; VBIAciCal31047_0833. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22950 MW; D4A6049206BDC078 CRC64; MTTTAIAGVY GITDSTLMPG DALLCKSEAA LRAGLRILQY RDKSDDAARR LREAAALHAL CRDYGALFVV NDDAALAAKI AAPALHVGRE DAPLAELRRH FGGSLCIGVS CYDDLARAER AQAEGADYVA FGAFFPSPSK PDTSRAPLHL LREARRRLQV PVVAIGGIRA DNGADLLAAG ADALAVISAL FGSADVAAAM RRLQALFVLA GGSQTMEES // ID C6PN80_9CLOT Unreviewed; 204 AA. AC C6PN80; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CcarbDRAFT_0247, CLCAR_3736; OS Clostridium carboxidivorans P7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=536227; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P7; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Hemme C.L.; RT "The draft genome of Clostridium carboxidivorans P7."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P7; RX PubMed=20729368; DOI=10.1128/JB.00877-10; RA Paul D., Austin F.W., Arick T., Bridges S.M., Burgess S.C., RA Dandass Y.S., Lawrence M.L.; RT "Genome sequence of the solvent-producing bacterium Clostridium RT carboxidivorans strain P7T."; RL J. Bacteriol. 192:5554-5555(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVI01000003; EET89201.1; -; Genomic_DNA. DR EMBL; GG770696; EFG86780.1; -; Genomic_DNA. DR EnsemblBacteria; EET89201; EET89201; CcarbDRAFT_0247. DR EnsemblBacteria; EFG86780; EFG86780; CLCAR_3736. DR PATRIC; 26463182; VBICloCar96475_0241. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22234 MW; F76F6A960D8BBB07 CRC64; MEIDYGLYLI TDRSFLKGRD LKKVVEEAIL GGVTLVQVRE KDISTREFYN VALEVKEVTK HYKVPIIIND RLDIAQAIDA EGVHLGQSDM PIKFARKILG KEKIIGISAG NVKEAVEAER DGADYLGIGT VFYTGTKKDI KTPIGIEGLK EVCNSVKIPS VAIGGVNETN FKEVLSTGVN GISVISAILG KDDIRQASKN LNSK // ID C6PR52_9CLOT Unreviewed; 163 AA. AC C6PR52; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=CcarbDRAFT_1269; OS Clostridium carboxidivorans P7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=536227; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P7; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Hemme C.L.; RT "The draft genome of Clostridium carboxidivorans P7."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVI01000015; EET88276.1; -; Genomic_DNA. DR ProteinModelPortal; C6PR52; -. DR EnsemblBacteria; EET88276; EET88276; CcarbDRAFT_1269. DR PATRIC; 26465200; VBICloCar96475_1239. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 163 AA; 18345 MW; F2D39A0DA6279C9E CRC64; MFNLKEDKKI YVVTNRHLID KSSNLCEVIE KCAFKGADGV ILREKDLENE ALKHLGEKIK IITDKYNIPL IINGNIKVAL DINAYGFHTG FENFKNMKGN ETICEKIAVG VSVHKVEEAV EAEKLGANYL LAGHIFETDC KLGLKGRGMG FLEKYVKVLL YQL // ID C6R5F4_9MICC Unreviewed; 206 AA. AC C6R5F4; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ROTMU0001_1467; OS Rothia mucilaginosa ATCC 25296. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Rothia. OX NCBI_TaxID=553201; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25296; RA Dodson R., Sebastian Y., Madupu R., Durkin A.S., Torralba M., RA Methe B., Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVO01000017; EET75031.1; -; Genomic_DNA. DR ProteinModelPortal; C6R5F4; -. DR EnsemblBacteria; EET75031; EET75031; ROTMU0001_1467. DR PATRIC; 28163932; VBIRotMuc23969_1447. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). SQ SEQUENCE 206 AA; 22016 MW; 41DFA8F76132082F CRC64; MTRETHPYTT PARPLDLNLY LVTGDNPLET VRAAKHATCI QVRSKPISAR ELYQLTEAIA GIIQPHQTLL VDDRVDVALA LRARGVRVDG VHIGQDDLPV ADARALLGAD AVIGLTTGTR QLVEESNKIA HLIDYIGTGP FRPSPTKQSN RPPLGIDGLR ELAELSAVPT VAIGDITPED CPAIRTTGVA GIAMVRAFVD NPALQA // ID C6RBT5_9CORY Unreviewed; 209 AA. AC C6RBT5; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CORTU0001_0476; OS Corynebacterium tuberculostearicum SK141. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=553206; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK141; RA Dodson R., Sebastian Y., Madupu R., Durkin A.S., Torralba M., RA Methe B., Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVP01000032; EET76599.1; -; Genomic_DNA. DR ProteinModelPortal; C6RBT5; -. DR EnsemblBacteria; EET76599; EET76599; CORTU0001_0476. DR PATRIC; 27680789; VBICorTub52766_1939. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR000652; Triosephosphate_isomerase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS51440; TIM_2; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21811 MW; 23E62B8470D2E4C9 CRC64; MSIDWTLYLV TDPDLAGGRD NVVPIVQEAV RGGVTVVQLR DKEASDEQIE RTARELLDVL GDVPLFINDR VEVAAKLGCH LHIGQDDMAF REAREKLGEG QLIGLSIGSN EELAAIADDA RPDVIGIGPV HSTATKKNAP AGMGTAAAAA LAHAARERGI ESVAIGGIKT HNAHELAGSD FAGICVVSDI MAAEDPAAAA AHLKEAFHG // ID C6RDJ3_9PROT Unreviewed; 217 AA. AC C6RDJ3; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN ORFNames=CAMSH0001_0024; OS Campylobacter showae RM3277. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=553219; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RM3277; RA Madupu R., Sebastian Y., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVQ01000006; EET80554.1; -; Genomic_DNA. DR ProteinModelPortal; C6RDJ3; -. DR EnsemblBacteria; EET80554; EET80554; CAMSH0001_0024. DR PATRIC; 27770320; VBICamSho45867_0336. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. PE 4: Predicted; KW Transferase. SQ SEQUENCE 217 AA; 23917 MW; 6C26D7C001C272FF CRC64; MKFDKFELVW VTNRRLSEDF FADVRRVAQS GKADKILLRE SDLPEHEYEK LASKTLEIIA ECDSGARLVL HTHASVASKL GVGELHLPFA KFRALSSESA TNLRDLAKFD GVRTDKERGG GICASNLTQK LKIGVSVHSL QEALTAQDFG ADYVVAGHIF DTPSHALERG RGLKFLREIC ENLSIKTYAI GGINFENLDK IKDAGAAGAY MMRGFLS // ID C6RG00_9PROT Unreviewed; 200 AA. AC C6RG00; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CAMSH0001_2263; OS Campylobacter showae RM3277. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=553219; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RM3277; RA Madupu R., Sebastian Y., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVQ01000018; EET79695.1; -; Genomic_DNA. DR ProteinModelPortal; C6RG00; -. DR EnsemblBacteria; EET79695; EET79695; CAMSH0001_2263. DR PATRIC; 27772010; VBICamSho45867_1164. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 200 AA; 21577 MW; 4FA706139774C535 CRC64; MAEIYAITDD ILTPESSVLA QAGELLECGV KLLQYRTKIE PKNECVAFAL KELCERYGAR FIVNDDVKFA AKIGANAVHI GKDDGGVKAA RKILGEDAFI GVSCYDDLNL ALRAQDEGAS YAAFGALFAS PTKPNAPLCK FETIRRAKEI LRIPVCVIGG INAANIAQIA ALNPDYVAVI SALYRPASIK ENLRNLQAFL // ID C6RKA2_ACIRA Unreviewed; 209 AA. AC C6RKA2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ACIRA0001_2348; OS Acinetobacter radioresistens SK82. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=596318; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK82; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVR01000013; EET83556.1; -; Genomic_DNA. DR ProteinModelPortal; C6RKA2; -. DR EnsemblBacteria; EET83556; EET83556; ACIRA0001_2348. DR PATRIC; 24337705; VBIAciRad20771_0328. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22777 MW; 3BC3B58EEAE0A317 CRC64; MRGLYLITND DPIELLLEKL EAALATHQIE ILQYRRKKVE KADQLHEVER IKALCDFYKV PLVINDDIRL AAQCGLGVHL GQTDGEIIEA KTQLPENMII GRTCANSIEL AEQAIADGAT YIAFGAIYAT YSKPEAGNIG LETLKLARQK FSLPICAIGG LKVENAQPVI QAGADLCAVI SDILALPAEE IPSRVQAWAI LFAETQPAI // ID C6RSR2_ACIRA Unreviewed; 299 AA. AC C6RSR2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 16-OCT-2013, entry version 26. DE SubName: Full=Mutator mutT protein; DE EC=3.6.1.-; GN ORFNames=ACIRA0001_1537; OS Acinetobacter radioresistens SK82. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=596318; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK82; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVR01000076; EET81124.1; -; Genomic_DNA. DR ProteinModelPortal; C6RSR2; -. DR EnsemblBacteria; EET81124; EET81124; ACIRA0001_1537. DR PATRIC; 24342854; VBIAciRad20771_2820. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 299 AA; 34112 MW; 7EBBAE044A13DD2F CRC64; MSKPIVHVAV ALLFHRSKVL VGWREAKQHQ GNKYEFPGGK VEGNETPEET CRREIYEEVG VGLSDWHPFS LICHEYDDIT VHLHLFFAHV PEEMLNQIQK PWAWYTREKL QTLDFPAANQ PVIERLYWPH SIRIGTAFSA IEQLAQDMLF YWRPEQAEID KNWLLEYSIQ QLNKLIVPYQ VWRSLNVEQQ HHIAAVHLKQ SEQMSLKKGE LCIGIRYIAA CHDAASVQHA VQIGCEAVLI SPVQATPTHP EAPALGWDAF AELAHQADVP VFALGGLSRE DLECARQYGA YGIAGIRHI // ID C6RU47_VIBCL Unreviewed; 440 AA. AC C6RU47; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VCH_000274; OS Vibrio cholerae CIRS101. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=661513; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIRS 101; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D., RA Vonstein V.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVW01000006; EET93849.1; -; Genomic_DNA. DR ProteinModelPortal; C6RU47; -. DR EnsemblBacteria; EET93849; EET93849; VCH_000274. DR PATRIC; 31160831; VBIVibCho146863_0281. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID C6S4K6_NEIML Unreviewed; 205 AA. AC C6S4K6; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NMO_0097; OS Neisseria meningitidis (strain alpha14). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=662598; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=alpha14; RX PubMed=18305155; DOI=10.1073/pnas.0800151105; RA Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., RA Mueller T., Goesmann A., Joseph B., Konietzny S., Kurzai O., RA Schmitt C., Friedrich T., Linke B., Vogel U., Frosch M.; RT "Whole-genome comparison of disease and carriage strains provides RT insights into virulence evolution in Neisseria meningitidis."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM889136; CBA03487.1; -; Genomic_DNA. DR RefSeq; YP_003082341.1; NC_013016.1. DR ProteinModelPortal; C6S4K6; -. DR STRING; 662598.NMO_0097; -. DR EnsemblBacteria; CBA03487; CBA03487; NMO_0097. DR GeneID; 8222962; -. DR KEGG; nmi:NMO_0097; -. DR PATRIC; 20366269; VBINeiMen141067_0114. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NMEN662598:GJMX-100-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21561 MW; 8A9C7F4164DC2A47 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKAL HGDELKREIA RCVAACQGSH TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYIASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID C6SET0_NEIME Unreviewed; 205 AA. AC C6SET0; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NME_1799; OS Neisseria meningitidis alpha153. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=663926; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Alpha153; RX PubMed=18305155; DOI=10.1073/pnas.0800151105; RA Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., RA Mueller T., Goesmann A., Joseph B., Konietzny S., Kurzai O., RA Schmitt C., Friedrich T., Linke B., Vogel U., Frosch M.; RT "Whole-genome comparison of disease and carriage strains provides RT insights into virulence evolution in Neisseria meningitidis."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM889137; CBA08455.1; -; Genomic_DNA. DR ProteinModelPortal; C6SET0; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21644 MW; 242DD35C037C80FB CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKAL HGDELKREIA RCVAACQGSH TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLEKLREYV KQAGSTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID C6SH57_NEIME Unreviewed; 205 AA. AC C6SH57; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NMW_0274; OS Neisseria meningitidis alpha275. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=295996; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Alpha275; RX PubMed=18305155; DOI=10.1073/pnas.0800151105; RA Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., RA Mueller T., Goesmann A., Joseph B., Konietzny S., Kurzai O., RA Schmitt C., Friedrich T., Linke B., Vogel U., Frosch M.; RT "Whole-genome comparison of disease and carriage strains provides RT insights into virulence evolution in Neisseria meningitidis."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM889138; CBA04670.1; -; Genomic_DNA. DR ProteinModelPortal; C6SH57; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21629 MW; AEDC3B60825249A2 CRC64; MTFPPLKSPL KFYAVVSTAD WVERMVEAGA DTVQLRCKAL HGDELKREIA RCAAACRGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID C6TZV6_BURPE Unreviewed; 367 AA. AC C6TZV6; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=BURPS1710A_4236; OS Burkholderia pseudomallei 1710a. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320371; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1710a; RA Harkins D.M., DeShazer D., Woods D.E., Brinkac L.M., Brown K.A., RA Hung G.C., Tuanyok A., Zhang B., Nierman W.C.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000832; EET06529.1; -; Genomic_DNA. DR ProteinModelPortal; C6TZV6; -. DR EnsemblBacteria; EET06529; EET06529; BURPS1710A_4236. DR PATRIC; 27844478; VBIBurPse76422_3550. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 367 AA; 38315 MW; 3E9B351CCB7F5C2B CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGARAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID C6U3P0_BURPE Unreviewed; 79 AA. AC C6U3P0; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine phosphate synthase; DE Flags: Fragment; GN ORFNames=BURPS1710A_A0836; OS Burkholderia pseudomallei 1710a. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320371; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1710a; RA Harkins D.M., DeShazer D., Woods D.E., Brinkac L.M., Brown K.A., RA Hung G.C., Tuanyok A., Zhang B., Nierman W.C.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000833; EET05941.1; -; Genomic_DNA. DR EnsemblBacteria; EET05941; EET05941; BURPS1710A_A0836. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. FT NON_TER 79 79 SQ SEQUENCE 79 AA; 8842 MW; 63A4AD22DCD70A45 CRC64; MIESIIHRHL KIIVNKSANL PSEYLITPEP PGDEALSDYL ATLERTLKAG ISLVQLRAKA VTAPYYARLT EYALACCRR // ID C6U3P2_BURPE Unreviewed; 199 AA. AC C6U3P2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 22-JAN-2014, entry version 23. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=BURPS1710A_A0839; OS Burkholderia pseudomallei 1710a. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320371; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1710a; RA Harkins D.M., DeShazer D., Woods D.E., Brinkac L.M., Brown K.A., RA Hung G.C., Tuanyok A., Zhang B., Nierman W.C.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000833; EET05389.1; -; Genomic_DNA. DR ProteinModelPortal; C6U3P2; -. DR EnsemblBacteria; EET05389; EET05389; BURPS1710A_A0839. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 199 AA; 21351 MW; F4C4456E8E187770 CRC64; MNKSANLPSE YLITPEPPGD EALSDYLATL ERTLKAGISL VQLRAKAVTA PYYARLTEYA LACCRRYNAR LLVNAAPEVA RGLHTDGVHL TSTRLMTCST RPLPAGLLVS AACHDEDQVR HADSIGVDLI TISPVMPTAT HTTAEPLGWP RFRELATLTS VPVYALGGMS VDSLAEARNA GAYGIAAIRA FWGSNVDRS // ID C6U8N4_BURPE Unreviewed; 209 AA. AC C6U8N4; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN ORFNames=BURPS1710A_A1715; OS Burkholderia pseudomallei 1710a. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320371; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1710a; RA Harkins D.M., DeShazer D., Woods D.E., Brinkac L.M., Brown K.A., RA Hung G.C., Tuanyok A., Zhang B., Nierman W.C.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000833; EET03875.1; -; Genomic_DNA. DR ProteinModelPortal; C6U8N4; -. DR EnsemblBacteria; EET03875; EET03875; BURPS1710A_A1715. DR PATRIC; 27847551; VBIBurPse76422_5248. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 209 AA; 21720 MW; E0832810C174ACD4 CRC64; MSARDGDRAA DHDMHDDLAL PPYYLITPEP ASGSDADLAA FLDRLSDALA TGLTLVQLRV KTLDAPAYAA LAAGALARCR AQRARMIVNG PIAVEAALAL GAAGVHLGSA ALRAATARPL GSEGLLSAAC HSLDELRHAQ RIGADLATLS PVLPTLTHPG APTLGWTRFA ECAAHTRVPV YALGGMTRTH LETARAHHAH GIASIRGLW // ID C6UJM3_ECOBR Unreviewed; 211 AA. AC C6UJM3; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECB_03870; OS Escherichia coli (strain B / REL606). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=413997; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B / REL606; RX PubMed=19786035; DOI=10.1016/j.jmb.2009.09.052; RA Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., RA Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., RA Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W., RA Daegelen P., Kim J.F.; RT "Genome sequences of Escherichia coli B strains REL606 and RT BL21(DE3)."; RL J. Mol. Biol. 394:644-652(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000819; ACT41507.1; -; Genomic_DNA. DR RefSeq; YP_003047043.1; NC_012967.1. DR ProteinModelPortal; C6UJM3; -. DR SMR; C6UJM3; 20-202. DR STRING; 413997.ECB_03870; -. DR EnsemblBacteria; ACT41507; ACT41507; ECB_03870. DR GeneID; 8177988; -. DR KEGG; ebr:ECB_03870; -. DR PATRIC; 18240209; VBIEscCol118196_4068. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL413997:GCQD-4127-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID C6V1V1_ECO5T Unreviewed; 211 AA. AC C6V1V1; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECSP_5063; OS Escherichia coli O157:H7 (strain TW14359 / EHEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=544404; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TW14359 / EHEC; RX PubMed=19564389; DOI=10.1128/IAI.00198-09; RA Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., RA Saenphimmachak C., Rohmer L., Ritchie J.M., Radey M., McKevitt M., RA Freeman T.L., Hayden H., Haugen E., Gillett W., Fong C., Chang J., RA Beskhlebnaya V., Waldor M.K., Samadpour M., Whittam T.S., Kaul R., RA Brittnacher M., Miller S.I.; RT "Analysis of the genome of the Escherichia coli O157:H7 2006 spinach- RT associated outbreak isolate indicates candidate genes that may enhance RT virulence."; RL Infect. Immun. 77:3713-3721(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001368; ACT74752.1; -; Genomic_DNA. DR RefSeq; YP_003080828.1; NC_013008.1. DR ProteinModelPortal; C6V1V1; -. DR SMR; C6V1V1; 10-209. DR STRING; 544404.ECSP_5063; -. DR EnsemblBacteria; ACT74752; ACT74752; ECSP_5063. DR GeneID; 8219629; -. DR KEGG; etw:ECSP_5063; -. DR PATRIC; 18394327; VBIEscCol9396_5126. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL544404:GKCX-5055-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID C6V488_NEORI Unreviewed; 214 AA. AC C6V488; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 31. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=NRI_0212; OS Neorickettsia risticii (strain Illinois). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Neorickettsia. OX NCBI_TaxID=434131; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Illinois; RX PubMed=19661282; DOI=10.1093/nar/gkp642; RA Lin M., Zhang C., Gibson K., Rikihisa Y.; RT "Analysis of complete genome sequence of Neorickettsia risticii: RT causative agent of Potomac horse fever."; RL Nucleic Acids Res. 37:6076-6091(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001431; ACT69200.1; -; Genomic_DNA. DR RefSeq; YP_003081442.1; NC_013009.1. DR ProteinModelPortal; C6V488; -. DR STRING; 434131.NRI_0212; -. DR EnsemblBacteria; ACT69200; ACT69200; NRI_0212. DR GeneID; 8220306; -. DR KEGG; nri:NRI_0212; -. DR PATRIC; 22678720; VBINeoRis104330_0203. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CIGGINE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NRIS434131:GJCC-214-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 214 AA; 24565 MW; E084AD4D27799E38 CRC64; MQLSKAFYIL SPNRRITTAE YADLARLFKD FFIYVYAFQL RIKDRNLLER EIPRLSELCH EYKIPLIVND FIDLALKFET DGVHIGVADN TLEQCQYLLP SGKIVGISCY NDIERAKKNL LADYVSFGCF FESRTKPNPP AKATLTILDK WKKIIPRISC VCIGGINEKN FAQLLRNGAD IVAFSDYLWK GKSPYGKFAA LVETSKHYGK LLYK // ID C6V4K9_NEORI Unreviewed; 192 AA. AC C6V4K9; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 30. DE SubName: Full=Thiamine monophosphate synthase/teni subfamily; GN OrderedLocusNames=NRI_0339; OS Neorickettsia risticii (strain Illinois). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Neorickettsia. OX NCBI_TaxID=434131; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Illinois; RX PubMed=19661282; DOI=10.1093/nar/gkp642; RA Lin M., Zhang C., Gibson K., Rikihisa Y.; RT "Analysis of complete genome sequence of Neorickettsia risticii: RT causative agent of Potomac horse fever."; RL Nucleic Acids Res. 37:6076-6091(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001431; ACT69337.1; -; Genomic_DNA. DR RefSeq; YP_003081563.1; NC_013009.1. DR STRING; 434131.NRI_0339; -. DR EnsemblBacteria; ACT69337; ACT69337; NRI_0339. DR GeneID; 8220430; -. DR KEGG; nri:NRI_0339; -. DR PATRIC; 22678970; VBINeoRis104330_0322. DR eggNOG; NOG323178; -. DR HOGENOM; HOG000127309; -. DR KO; K00788; -. DR OrthoDB; EOG679THR; -. DR BioCyc; NRIS434131:GJCC-341-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 192 AA; 22243 MW; 14FD4D4EE74B2788 CRC64; MFFKRYAHLF RWLFVIDVIS SPSEIVFVLK QLPLESLVVL RCYEHLQRKN LAHWLSRICR KLRLIFLVAG DPFTALATRA SGLHVRESSF SKMRKWRYLK KRWFISCASH SVKQNLKIQA AGFDAALFSP VFHSKKTNFK AMGATKFLKY QAFTRKIDVF ALGGTAKANI SKLRETRQKV GIAGINLYND RL // ID C6VJ69_LACPJ Unreviewed; 217 AA. AC C6VJ69; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=JDM1_0115; OS Lactobacillus plantarum (strain JDM1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=644042; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JDM1; RX PubMed=19465650; DOI=10.1128/JB.00587-09; RA Zhang Z.Y., Liu C., Zhu Y.Z., Zhong Y., Zhu Y.Q., Zheng H.J., RA Zhao G.P., Wang S.Y., Guo X.K.; RT "Complete genome sequence of Lactobacillus plantarum JDM1."; RL J. Bacteriol. 191:5020-5021(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001617; ACT61004.1; -; Genomic_DNA. DR RefSeq; YP_003061701.1; NC_012984.1. DR ProteinModelPortal; C6VJ69; -. DR STRING; 644042.JDM1_0115; -. DR EnsemblBacteria; ACT61004; ACT61004; JDM1_0115. DR GeneID; 8189856; -. DR KEGG; lpj:JDM1_0115; -. DR PATRIC; 22240741; VBILacPla68346_0112. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LPLA644042:GHFY-117-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22784 MW; 867E38666A8A6DA4 CRC64; MTLKFELTQL RAYFVCGTQD VPGQDLNVVV QTALDAGITA FQYRDKGNSQ LTTAERFALG QQLRERCAQA HVPFIVDDDV KLALALQADG IHVGQKDDRV TQVIQRVANQ MFVGLSCSTL AEVQIANQLE GIAYLGSGPI FPTTSKADAD PVVGLTGLRQ LVMTASCPVV AIGGITVAQL PAIAATGAAG AAVISMLTRS PDMAATVKAM LTATEGH // ID C6W0S2_DYAFD Unreviewed; 409 AA. AC C6W0S2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Dfer_2460; OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / NS114). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Dyadobacter. OX NCBI_TaxID=471854; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700827 / DSM 18053 / NS114; RX DOI=10.4056/sigs.19262; RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C., RA Copeland A., Glavina del Rio T., Nolan M., Chen F., Lucas S., Tice H., RA Cheng J.-F., Land M., Hauser L., Chang Y.-J., Jeffries C.C., RA Kopitz M., Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., RA Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P., RA Bristow J., Dalin E., Eisen J.A., Markowitz V., Hugenholtz P., RA Goeker M., Rohde M., Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Dyadobacter fermentans type strain RT (NS114)."; RL Stand. Genomic Sci. 1:133-140(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001619; ACT93678.1; -; Genomic_DNA. DR RefSeq; YP_003086843.1; NC_013037.1. DR ProteinModelPortal; C6W0S2; -. DR STRING; 471854.Dfer_2460; -. DR EnsemblBacteria; ACT93678; ACT93678; Dfer_2460. DR GeneID; 8226032; -. DR KEGG; dfe:Dfer_2460; -. DR PATRIC; 21826356; VBIDyaFer416_2527. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; ENITPAF; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DFER471854:GI24-2467-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 409 AA; 44722 MW; 83EF94EA3E4AED59 CRC64; MELIVITHPE MLPGEAGIIN QLFQSGLARL HLRKPDVPKE VVQDLLENIT PAFRNRIALH QHHELADAFG ITGLHFTERA RLDVAPETWS ALKSRAYTLS TSLHDPAQLE TLSHDFDYAF LGPVFDSISK VGYAAKLPSD FKLNPFTFPN KVIALGGMDA ENLGLASQMG FAGAALLGAI WQNPEQAVTR FAHLKSLQVE RPFVDRLHFI SNETPDMSHI DSIRLALEAG CRWIQLRVKH RPEAEVLPIA WEATRLCDAY GARLIINDFP RVALAVQAYG LHLGLTDMPV PEARALVGNK IVVGGTANSW EDIELRIREG ADYIGLGPFR FTSTKENLSP ILGVEGYAAL MQKMADAGFS KPIIAIGGVT PADIPIIRST GIYGVAMSAA LTGATDPAET FYEIQQALC // ID C6W5T9_DYAFD Unreviewed; 224 AA. AC C6W5T9; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dfer_4827; OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / NS114). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Dyadobacter. OX NCBI_TaxID=471854; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700827 / DSM 18053 / NS114; RX DOI=10.4056/sigs.19262; RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C., RA Copeland A., Glavina del Rio T., Nolan M., Chen F., Lucas S., Tice H., RA Cheng J.-F., Land M., Hauser L., Chang Y.-J., Jeffries C.C., RA Kopitz M., Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., RA Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P., RA Bristow J., Dalin E., Eisen J.A., Markowitz V., Hugenholtz P., RA Goeker M., Rohde M., Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Dyadobacter fermentans type strain RT (NS114)."; RL Stand. Genomic Sci. 1:133-140(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001619; ACT96028.1; -; Genomic_DNA. DR RefSeq; YP_003089193.1; NC_013037.1. DR ProteinModelPortal; C6W5T9; -. DR STRING; 471854.Dfer_4827; -. DR EnsemblBacteria; ACT96028; ACT96028; Dfer_4827. DR GeneID; 8228433; -. DR KEGG; dfe:Dfer_4827; -. DR PATRIC; 21831289; VBIDyaFer416_4963. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DFER471854:GI24-4869-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24640 MW; 6047B3148DC2CFA0 CRC64; MVATTKMHMN SNLELYLVTD EAACLGRDFY WVVEEAVKGG VTMVQLREKS LSTRAFIERA KRLKAILETY NVPLIINDRL DVALAVDADG VHIGQSDMPF QTAHRLLGEG KIIGLSAEKQ DDVLEAEQWN LSYLAVSPLF ATPTKTDTEK PWELDGLQWA RQQSRHPLVV IGGLHPENVH DAITNGANGV AVVSAICSAP SPREAAQALK SIIQNSILWP AKNF // ID C6WGQ8_ACTMD Unreviewed; 252 AA. AC C6WGQ8; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Amir_0407; OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU OS 3971). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Actinosynnema. OX NCBI_TaxID=446462; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971; RX PubMed=21304636; DOI=10.4056/sigs.21137; RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G., RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., RA Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., RA Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J., RA Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P., RA Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Actinosynnema mirum type strain (101)."; RL Stand. Genomic Sci. 1:46-53(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001630; ACU34374.1; -; Genomic_DNA. DR RefSeq; YP_003098220.1; NC_013093.1. DR ProteinModelPortal; C6WGQ8; -. DR STRING; 446462.Amir_0407; -. DR EnsemblBacteria; ACU34374; ACU34374; Amir_0407. DR GeneID; 8324566; -. DR KEGG; ami:Amir_0407; -. DR PATRIC; 20763575; VBIActMir80567_0413. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CVGPVHA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AMIR446462:GH7R-423-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 205 205 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 252 AA; 25682 MW; 323D82068CD37A64 CRC64; MPGLDATQIR RRLADARLYL CTPHRPDLAE FADAALAGGV DVVQLREKGM EARQELAALE VLAEACARHG ALLAVNDRAD VALAAGADVL HLGQDDLPVP LARRVVGEEV VIGRSTHDVA QASAAAVEPG VDYFCTGPCW PTPTKPGRPA PGLDLVRAVA GWDAARASAA GGPGGLGASG AGRPGAGAPG AGAAPPARPW FAIGGIDRHR LPEVISAGAR RVVVVRAITE SSDPRAAAAW LKIQLSGVPS SP // ID C6WTS2_METML Unreviewed; 206 AA. AC C6WTS2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mmol_2311; OS Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylotenera. OX NCBI_TaxID=583345; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., RA Chistoserdova L.; RT "Complete sequence of Methylotenera mobilis JLW8."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001672; ACT49213.1; -; Genomic_DNA. DR RefSeq; YP_003049740.1; NC_012968.1. DR ProteinModelPortal; C6WTS2; -. DR STRING; 583345.Mmol_2311; -. DR EnsemblBacteria; ACT49213; ACT49213; Mmol_2311. DR GeneID; 8170564; -. DR KEGG; mmb:Mmol_2311; -. DR PATRIC; 22614875; VBIMetMob89187_2327. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MMOB583345:GHCF-2366-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21799 MW; 5A798772757FEEB1 CRC64; MSVIKGLYAI TPDEQDTDTL LSKVEAALQG GIGVLQYRNK LADHKLQTQQ ARALLPLCRQ YQVPFIINDS IKLCLTLDAD GVHLGADDGN LAEARARLGS HKLLGASCYN RFDLALSAQQ LGADYVAFGA CFASSTKPNA PVAGLHLFTQ AKAELKVPSV AIGGITLENA ALAIAAGANS IAVINAIFNA DDVKLTSQQF TKLFQS // ID C6WU24_METML Unreviewed; 352 AA. AC C6WU24; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Mmol_0513; OS Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylotenera. OX NCBI_TaxID=583345; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., RA Chistoserdova L.; RT "Complete sequence of Methylotenera mobilis JLW8."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001672; ACT47423.1; -; Genomic_DNA. DR RefSeq; YP_003047950.1; NC_012968.1. DR ProteinModelPortal; C6WU24; -. DR STRING; 583345.Mmol_0513; -. DR EnsemblBacteria; ACT47423; ACT47423; Mmol_0513. DR GeneID; 8171374; -. DR KEGG; mmb:Mmol_0513; -. DR PATRIC; 22611189; VBIMetMob89187_0518. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MMOB583345:GHCF-530-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 352 AA; 38330 MW; 6C554EBB6FB38F12 CRC64; MSTSALNLST KGPAGASPAE GSAAGDSVTK VTEAAVGIVQ RDNGMVLLGE RPVGKPWEGY WEFPGGKVEP NETPAQALKR ELQEELGIIV TRFHSWMTRT YEYEARYDQS GKLITPAKAV KLHFFIVVEW QGDPVGLEDQ QLSWQNPEKL TVGPMLPANT PILTALSLAP VYAISNLKEM GEVQFFERLK MALENGLMMI QVREPDLSKQ DLMLFAEHVI ALAKPFEAKV FVNTDVESAQ QLNAAGVHLS AQRLMQLKVK PEGLLVGASC HNAAELAHAK MLALDYVTLS PVKSTLSHPN TAPLGWATFN QLVAGYSLPV FALGGMLRED LDPARTYGAH GIAMQRDVWG AL // ID C6X9D2_METSD Unreviewed; 316 AA. AC C6X9D2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE SubName: Full=Mutator MutT protein; DE Flags: Precursor; GN OrderedLocusNames=Msip34_0504; OS Methylovorus sp. (strain SIP3-4) (Methylotenera sp. (strain SIP3-4)). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylovorus. OX NCBI_TaxID=582744; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIP3-4; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Clum A., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., RA Chistoserdova L.; RT "Complete sequence of chromosome of Methylovorus sp. SIP3-4."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001674; ACT49752.1; -; Genomic_DNA. DR RefSeq; YP_003050279.1; NC_012969.1. DR ProteinModelPortal; C6X9D2; -. DR STRING; 582744.Msip34_0504; -. DR EnsemblBacteria; ACT49752; ACT49752; Msip34_0504. DR GeneID; 8172071; -. DR KEGG; mei:Msip34_0504; -. DR PATRIC; 22615998; VBIMetSp110381_0509. DR eggNOG; COG0494; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MGLU582744:GHXQ-518-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 316 AA; 34638 MW; 05DDCA0F12613209 CRC64; MTDKPVVHAA VAVLVRDDGK VLLAQRPEGK PWAGWWEFPG GKIEQGESVL QALKREIEEE LGTAIVEAYP WITRRFAYPE RTVQLHFYQV RRWTGEPHGR EGQALSWQSP AAVNVGPLLP ANEPLLRMLS LPSIYAITQL EALGEPVFLA RLERALQGGL KLIQVREKHL SEEALLAFAT KVLALARPYG ARVLLNASPE LASRVHADGV HLSSQALMAL EQKPEGLVVG ASCHDAPELA RAAELELDFV VFSPVLRTLS HPDAKPLGWH GFAEGIAGYA LPVYALGGLQ ASHLQEAWRH GAHGIAMLRG CWNENS // ID C6XBR8_METSD Unreviewed; 208 AA. AC C6XBR8; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Msip34_2801; OS Methylovorus sp. (strain SIP3-4) (Methylotenera sp. (strain SIP3-4)). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylovorus. OX NCBI_TaxID=582744; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIP3-4; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Clum A., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., RA Chistoserdova L.; RT "Complete sequence of chromosome of Methylovorus sp. SIP3-4."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001674; ACT52038.1; -; Genomic_DNA. DR RefSeq; YP_003052565.1; NC_012969.1. DR ProteinModelPortal; C6XBR8; -. DR STRING; 582744.Msip34_2801; -. DR EnsemblBacteria; ACT52038; ACT52038; Msip34_2801. DR GeneID; 8173654; -. DR KEGG; mei:Msip34_2801; -. DR PATRIC; 22620498; VBIMetSp110381_2719. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MGLU582744:GHXQ-2857-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21776 MW; 496E966C2383CD88 CRC64; MTPIKGLYAV TPDLEDTERL CEIVTEAILG GATLVQYRNK QAGHVLRIAQ AQALLAICRQ HGVPLIINDH VKLCLALDAD GVHIGGTDGD IAATRQRIGN KLLGASCYNR IDLALQAQAA GADYVAFGAC FSSQTKPQAP EAALSLFNMN PALTVPKVAI GGITLDNAPQ AVAAGADMLA VIGSLWGSSD IRHTAQQFSR LYNGPSSS // ID C6XKB5_HIRBI Unreviewed; 179 AA. AC C6XKB5; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Hbal_0011; OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hirschia. OX NCBI_TaxID=582402; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001678; ACT57713.1; -; Genomic_DNA. DR RefSeq; YP_003058410.1; NC_012982.1. DR ProteinModelPortal; C6XKB5; -. DR STRING; 582402.Hbal_0011; -. DR EnsemblBacteria; ACT57713; ACT57713; Hbal_0011. DR GeneID; 8185368; -. DR KEGG; hba:Hbal_0011; -. DR PATRIC; 22127926; VBIHirBal9878_0011. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ACHSERA; -. DR OrthoDB; EOG699751; -. DR BioCyc; HBAL582402:GHMV-11-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 179 AA; 19981 MW; D1F73FA2477B57B1 CRC64; MESVLPASIF VTDPNRTPDP VSIARQLPQG SGILYRHFGK NDRFTIGEEL KIIARKNRLK LIISHDPKLA DFIQPDGVHW PKKYIRHFLQ HKRFYKLNTC SAHSFRQISN AGKLNFDACF VSAVFPSRSP SAPNAMGPAK LRFLCQESQI PIYGLGGLNP KNAHAIIQHA GYAGVDGFT // ID C6XRN5_HIRBI Unreviewed; 217 AA. AC C6XRN5; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Hbal_2977; OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hirschia. OX NCBI_TaxID=582402; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001678; ACT60645.1; -; Genomic_DNA. DR RefSeq; YP_003061342.1; NC_012982.1. DR ProteinModelPortal; C6XRN5; -. DR STRING; 582402.Hbal_2977; -. DR EnsemblBacteria; ACT60645; ACT60645; Hbal_2977. DR GeneID; 8186026; -. DR KEGG; hba:Hbal_2977; -. DR PATRIC; 22134102; VBIHirBal9878_3056. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HBAL582402:GHMV-3024-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23271 MW; 3F1A2760BAA7E770 CRC64; MMNQECRLYL ITPPVIEDVE AFARDCEQAL DGGDVACLQI RLKTREGVAA SDAHIEAVAK RILPMAQAKD VAVLINDRPD LAKKFGADGV HIGQDDVTLK DARQIVGDDA IVGVTCHDSR HLGMEAGEAG ADYVAFGAFY PTQTKDPKAK AELETLTWWQ QFIEVPCVAI GGITVENAKP LIDAGADFLA VSSGVWNYAD GPKAAVEAFN VLMQSKG // ID C6XY78_PEDHD Unreviewed; 210 AA. AC C6XY78; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 16-APR-2014, entry version 32. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN OrderedLocusNames=Phep_0119; OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=485917; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13125 / DSM 2366 / NCIB 9290; RX PubMed=21304637; DOI=10.4056/sigs.22138; RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A., RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., RA Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.C., Saunders E., Chertkov O., Brettin T., Goker M., RA Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Pedobacter heparinus type strain (HIM RT 762-3)."; RL Stand. Genomic Sci. 1:54-62(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001681; ACU02345.1; -; Genomic_DNA. DR RefSeq; YP_003090407.1; NC_013061.1. DR ProteinModelPortal; C6XY78; -. DR STRING; 485917.Phep_0119; -. DR EnsemblBacteria; ACU02345; ACU02345; Phep_0119. DR GeneID; 8251204; -. DR KEGG; phe:Phep_0119; -. DR PATRIC; 22877239; VBIPedHep98714_0119. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GAKWIQY; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PHEP485917:GHL9-120-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 210 AA; 22992 MW; E735FC326CE3348D CRC64; MKKFIEKLHF ITHDIEHLSH LEQAQIACTA GAKWIQYRCL TKNDNELPAD INAIAEICDD WGATLIVTDH VHLNGMADIQ GFHIEDMAAD FVKLRQQLGE ALTIGGSANT VEGLIRLAAE GADYAGFGPF YTTLTKPNDL PLLGIEGYRK AMGLLKEKTI DLPVLAVGGI TANDIDPLMN TGIFGIAASA AINRADDMRE AYLSFYDRIM // ID C6XZH5_PEDHD Unreviewed; 203 AA. AC C6XZH5; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 16-APR-2014, entry version 32. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Phep_2467; OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=485917; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13125 / DSM 2366 / NCIB 9290; RX PubMed=21304637; DOI=10.4056/sigs.22138; RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A., RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., RA Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.C., Saunders E., Chertkov O., Brettin T., Goker M., RA Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Pedobacter heparinus type strain (HIM RT 762-3)."; RL Stand. Genomic Sci. 1:54-62(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001681; ACU04671.1; -; Genomic_DNA. DR RefSeq; YP_003092733.1; NC_013061.1. DR ProteinModelPortal; C6XZH5; -. DR STRING; 485917.Phep_2467; -. DR EnsemblBacteria; ACU04671; ACU04671; Phep_2467. DR GeneID; 8253574; -. DR KEGG; phe:Phep_2467; -. DR PATRIC; 22882015; VBIPedHep98714_2484. DR eggNOG; NOG86118; -. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR OrthoDB; EOG6RC3V1; -. DR BioCyc; PHEP485917:GHL9-2491-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 203 AA; 22581 MW; 4E369502E4B4D3B0 CRC64; MEVIVISDPL YFKAEARLIN QLFEAGMPIF HLRKVGRNRA DYAALLGGID EDYHDRLALH QFHELQADFP LVKRLHYPEQ LRKELDAKGL PSPSGNDVLS TSIHHPDALL ELTRFEYTFY GPVFNSLSKP GYTGIAEADA GFTLPVKRTG PKIIALGGID AGKVNAVRAM GFDGLALLGA VWMDKEQALN RFKLIKDKCD SDD // ID C6XZH7_PEDHD Unreviewed; 207 AA. AC C6XZH7; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Phep_2469; OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=485917; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13125 / DSM 2366 / NCIB 9290; RX PubMed=21304637; DOI=10.4056/sigs.22138; RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A., RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., RA Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.C., Saunders E., Chertkov O., Brettin T., Goker M., RA Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Pedobacter heparinus type strain (HIM RT 762-3)."; RL Stand. Genomic Sci. 1:54-62(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001681; ACU04673.1; -; Genomic_DNA. DR RefSeq; YP_003092735.1; NC_013061.1. DR ProteinModelPortal; C6XZH7; -. DR STRING; 485917.Phep_2469; -. DR EnsemblBacteria; ACU04673; ACU04673; Phep_2469. DR GeneID; 8253576; -. DR KEGG; phe:Phep_2469; -. DR PATRIC; 22882019; VBIPedHep98714_2486. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PHEP485917:GHL9-2493-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21796 MW; 03C80E47B8A07F99 CRC64; MRIDQLHYIS QASREGHLEA IERVLLAGGK WIQLRVKNEP EAVVLSLAIA AAALCKKHAA RLIVNDYPEI ALKAGADGVH LGLDDMPVAA ARAILGPDLI IGGTANTFGQ LQQRVAEGAD YIGLGPYRFT TTKQNLSPVI GLQGYVKLME QAKAAGIGTP VIAIGGITAD DIPLLMQAGL YGVAVSGALS HPQDTSVVLN HINHLLC // ID C6YLN1_VIBCL Unreviewed; 440 AA. AC C6YLN1; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VchoM_03594; OS Vibrio cholerae MO10. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=345072; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MO10; RA Colwell R., Grim C.J., Young S., Jaffe D., Gnerre S., Berlin A., RA Heiman D., Hepburn T., Shea T., Sykes S., Yandava C., Alvarado L., RA Kodira C., Borodovsky M., Heidelberg J., Lander E., Galagan J., RA Nusbaum C., Birren B.; RT "Annotation of Vibrio cholerae MO10."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990141; EET25567.1; -; Genomic_DNA. DR ProteinModelPortal; C6YLN1; -. DR EnsemblBacteria; EET25567; EET25567; VchoM_03594. DR PATRIC; 28068736; VBIVibCho130181_3405. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID C6Z1X5_9BACE Unreviewed; 202 AA. AC C6Z1X5; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BSFG_01031; OS Bacteroides sp. 4_3_47FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457394; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_3_47FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. 4_3_47FAA."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDR02000039; EET14884.1; -; Genomic_DNA. DR ProteinModelPortal; C6Z1X5; -. DR SMR; C6Z1X5; 1-202. DR EnsemblBacteria; EET14884; EET14884; BSFG_01031. DR PATRIC; 30527181; VBIBacSp78517_1073. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 22933 MW; 0AE478B2289391FD CRC64; MKLILITPPT YFVEEDKIIT ALFEEGLDTL HLRKPGTAPM FAERLLTLIP EQYHKRIVVH GHFYLKEEYK LKGIHLNGRN PNLPEGYKGH VSCSCHSLDE VKERKSSCDY VFLSPVFNSI SKLNYNSAYT AEELRTAAKA GIIDKKVIAL GGIDEENLLE VKDFGFGGAA ILGALWNKFD ACTDRDYRCV IEHFRKLRDL AD // ID C6Z1Y4_9BACE Unreviewed; 208 AA. AC C6Z1Y4; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSFG_01040; OS Bacteroides sp. 4_3_47FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457394; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_3_47FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. 4_3_47FAA."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDR02000039; EET14893.1; -; Genomic_DNA. DR ProteinModelPortal; C6Z1Y4; -. DR EnsemblBacteria; EET14893; EET14893; BSFG_01040. DR PATRIC; 30527199; VBIBacSp78517_1082. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 23078 MW; C08790A5F80A9015 CRC64; MEDKTVELQF ITHFTDTYSY YDSARMALEG GCRWIQLRMK DTPVDEVERE AIRLQGLCKD YGATFIIDDH VELVKKIHAD GVHLGKKDMP VAEARGILGK EFIIGGTANT FDDVKMHYKA GADYIGCGPF RFTTTKKDLS PVLGLEGYRS IILQMKEANI HLPIVAIGGI TLEDIPSIME TGITGIALSG TILRAKDPVA ETKRIMNL // ID C7BIY2_PHOAA Unreviewed; 223 AA. AC C7BIY2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PAU_00393; OS Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / OS 3105-77) (Xenorhabdus luminescens (strain 2)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Photorhabdus. OX NCBI_TaxID=553480; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43949 / 3105-77; RX PubMed=19583835; DOI=10.1186/1471-2164-10-302; RA Wilkinson P., Waterfield N.R., Crossman L., Corton C., RA Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L., RA Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C., RA Harris D., Thompson N.R., Quail M., Parkhill J., RA ffrench-Constant R.H.; RT "Comparative genomics of the emerging human pathogen Photorhabdus RT asymbiotica with the insect pathogen Photorhabdus luminescens."; RL BMC Genomics 10:302-302(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM162591; CAQ82486.1; -; Genomic_DNA. DR RefSeq; YP_003039231.1; NC_012962.1. DR ProteinModelPortal; C7BIY2; -. DR STRING; 291112.PAU_00393; -. DR EnsemblBacteria; CAQ82486; CAQ82486; PAU_00393. DR GeneID; 13859377; -. DR KEGG; pay:PAU_00393; -. DR PATRIC; 20494335; VBIPhoAsy71438_0463. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PASY291112:GJQ0-403-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24514 MW; E3639238760C868D CRC64; MNNLPNSPFA STEYKLGLYP VVNSLEWISR LLKAGVTTIQ LRIKDLPEAQ VEEDIQQAIL LGRQYNARLF INDYWQLAIK HGAYGVHLGQ EDLVTADLNA IQKTGLRLGI STHDEQELAR AKSLRPSYIA LGHIFPTTTK VMPSSPQGLK ALKRQVENTP DYPTVAIGGI SLERVPDVIA TGVGGVALVS AITQAKDWRQ ATSQLLQRVE GIESKVLRGS YAE // ID C7BZ49_HELPB Unreviewed; 220 AA. AC C7BZ49; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HELPY_0512; OS Helicobacter pylori (strain B38). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=592205; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B38; RX PubMed=20537153; DOI=10.1186/1471-2164-11-368; RA Thiberge J.M., Boursaux-Eude C., Lehours P., Dillies M.A., Creno S., RA Coppee J.Y., Rouy Z., Lajus A., Ma L., Burucoa C., RA Ruskone-Foumestraux A., Courillon-Mallet A., De Reuse H., Boneca I.G., RA Lamarque D., Megraud F., Delchier J.C., Medigue C., Bouchier C., RA Labigne A., Raymond J.; RT "From array-based hybridization of Helicobacter pylori isolates to the RT complete genome sequence of an isolate associated with MALT RT lymphoma."; RL BMC Genomics 11:368-368(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM991728; CAX29051.1; -; Genomic_DNA. DR RefSeq; YP_003057290.1; NC_012973.1. DR ProteinModelPortal; C7BZ49; -. DR STRING; 592205.HELPY_0512; -. DR EnsemblBacteria; CAX29051; CAX29051; HELPY_0512. DR GeneID; 8209030; -. DR KEGG; hpb:HELPY_0512; -. DR PATRIC; 20595663; VBIHelPyl144313_0510. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HPYL592205:GJAG-506-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24122 MW; 2387E106CB44BA0C CRC64; MFDADCLKLM FVAGSQDFYH IKGGKNDRIN ALLETLELAL QSQITAFQFR QKGDLALQDP VEIKRLALEC QKLCQKYGTP FIINDEVRLA LELKADGVHV GQEDMAIEEV ITLCQKRLFI GLSVNTLEQA LKARHLDGVA YLGVGPIFPT PSKKDAKQVV GVELLKKIHD SGVKKPLIAI GGITMHNASK LREYGGIAVI SAITQAKDKA LAVEKLLNNA // ID C7C7I9_METED Unreviewed; 241 AA. AC C7C7I9; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=METDI5507; OS Methylobacterium extorquens (strain DSM 5838 / DM4) (Methylobacterium OS dichloromethanicum (strain DM4)). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=661410; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5838 / DM4; RX PubMed=19440302; DOI=10.1371/journal.pone.0005584; RA Vuilleumier S., Chistoserdova L., Lee M.C., Bringel F., Lajus A., RA Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., RA Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., RA Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., RA Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., RA Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., RA Medigue C., Lidstrom M.E.; RT "Methylobacterium genome sequences: a reference blueprint to RT investigate microbial metabolism of C1 compounds from natural and RT industrial sources."; RL PLoS ONE 4:E5584-E5584(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP103042; CAX27115.1; -; Genomic_DNA. DR RefSeq; YP_003070925.1; NC_012988.1. DR ProteinModelPortal; C7C7I9; -. DR STRING; 661410.METDI5507; -. DR EnsemblBacteria; CAX27115; CAX27115; METDI5507. DR GeneID; 8196186; -. DR KEGG; mdi:METDI5507; -. DR PATRIC; 22529474; VBIMetExt143287_5241. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MEXT661410:GJA1-5418-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT METAL 87 87 Magnesium (By similarity). FT METAL 106 106 Magnesium (By similarity). FT BINDING 86 86 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 241 AA; 24424 MW; 72123553CADA576A CRC64; MGSGTGLGLS RPSAGVAVDL RLYGILDVGV LGGDAAALAT LAAEAVAGGA TLLQYRDKDL TDARAALARI RAIHAALAGR APLLVNDRVD LALAAGVEGV HLGQSDLHPE DARRLLGPRA IIGLTVKTGA QADELYRLPI DYACIGGVFA TTSKDNPDPP VGLDGLQRIV FRARLARGQS LPLGAIAGID ASNTASVIRA GADGVALIGA LFKGGATEAK ARDLLARVDE ALGQRGSTGT R // ID C7CAK7_METED Unreviewed; 205 AA. AC C7CAK7; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=METDI0581; OS Methylobacterium extorquens (strain DSM 5838 / DM4) (Methylobacterium OS dichloromethanicum (strain DM4)). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=661410; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5838 / DM4; RX PubMed=19440302; DOI=10.1371/journal.pone.0005584; RA Vuilleumier S., Chistoserdova L., Lee M.C., Bringel F., Lajus A., RA Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., RA Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., RA Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., RA Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., RA Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., RA Medigue C., Lidstrom M.E.; RT "Methylobacterium genome sequences: a reference blueprint to RT investigate microbial metabolism of C1 compounds from natural and RT industrial sources."; RL PLoS ONE 4:E5584-E5584(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP103042; CAX22232.1; -; Genomic_DNA. DR RefSeq; YP_003066285.1; NC_012988.1. DR ProteinModelPortal; C7CAK7; -. DR STRING; 661410.METDI0581; -. DR EnsemblBacteria; CAX22232; CAX22232; METDI0581. DR GeneID; 8196175; -. DR KEGG; mdi:METDI0581; -. DR PATRIC; 22520175; VBIMetExt143287_0653. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MEXT661410:GJA1-564-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 134 136 THZ-P binding (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 20343 MW; 7CBC53E5EEDF66A2 CRC64; MTLPPLLIVT DRHGAARPLT ETVRAAVAGG ARFVWLRDRD LDRDARRDLA HDLIALLQPA GGRLVVGGDA ELAAETGAQG VHLSGSAGID GIRAARTSLG AAALIGFSAH SVAEVAAAAA AGADYATLSP IFPTPSKPGY GPALGLASLR AAAAHGVPVF ALGGIDGGNA RACREAGAAG VAVMGGVMRG SDPRDATGRF VAALT // ID C7CLH4_METED Unreviewed; 222 AA. AC C7CLH4; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase (TMP pyrophosphorylase) (TMP-PPase) (Thiamine-phosphate synthase); GN OrderedLocusNames=METDI3151; OS Methylobacterium extorquens (strain DSM 5838 / DM4) (Methylobacterium OS dichloromethanicum (strain DM4)). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=661410; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5838 / DM4; RX PubMed=19440302; DOI=10.1371/journal.pone.0005584; RA Vuilleumier S., Chistoserdova L., Lee M.C., Bringel F., Lajus A., RA Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., RA Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., RA Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., RA Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., RA Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., RA Medigue C., Lidstrom M.E.; RT "Methylobacterium genome sequences: a reference blueprint to RT investigate microbial metabolism of C1 compounds from natural and RT industrial sources."; RL PLoS ONE 4:E5584-E5584(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP103042; CAX24803.1; -; Genomic_DNA. DR RefSeq; YP_003068659.1; NC_012988.1. DR ProteinModelPortal; C7CLH4; -. DR STRING; 661410.METDI3151; -. DR EnsemblBacteria; CAX24803; CAX24803; METDI3151. DR GeneID; 8195149; -. DR KEGG; mdi:METDI3151; -. DR PATRIC; 22524832; VBIMetExt143287_2943. DR eggNOG; NOG280778; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; MEXT661410:GJA1-3081-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 222 AA; 22870 MW; 7F842D26C8146888 CRC64; MAESESAAPR PRLALLTPYG LGASEAEATA RALDAACAAG DVAAVILRLA ASDERSLVAL VKRLAPPAQE RGAAVLVSVP GFTGDIVSVA ARGGADGVHL DRADEEALRD LRGRLRDGRI LGTGGVLGSR NAAMVAGETG VDYLMVGGLF PDGVAPDAEE VRERAAWWAE IFETPCIAVA TSAEDVAALV LTGSEFVGLE SALWLDDPEG VRAAQAQLDR AR // ID C7CUD9_ENTFL Unreviewed; 211 AA. AC C7CUD9; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFAG_00058; OS Enterococcus faecalis T1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565636; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T1; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain T1."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG670358; EET95322.1; -; Genomic_DNA. DR ProteinModelPortal; C7CUD9; -. DR EnsemblBacteria; EET95322; EET95322; EFAG_00058. DR PATRIC; 28729177; VBIEntFae10069_1867. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22866 MW; A6E43F880C487223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID C7D0M2_ENTFL Unreviewed; 211 AA. AC C7D0M2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFBG_00055; OS Enterococcus faecalis T2. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565637; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T2; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain T2."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG692851; EET98317.1; -; Genomic_DNA. DR ProteinModelPortal; C7D0M2; -. DR EnsemblBacteria; EET98317; EET98317; EFBG_00055. DR PATRIC; 26740381; VBIEntFae135593_1905. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22866 MW; 98C1A43B92687A05 CRC64; MREQLKVYLV TGRYDFSDTK FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID C7GCF3_9FIRM Unreviewed; 214 AA. AC C7GCF3; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=ROSINTL182_07590; OS Roseburia intestinalis L1-82. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=536231; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L1-82; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYJ02000115; EEV00494.1; -; Genomic_DNA. DR ProteinModelPortal; C7GCF3; -. DR EnsemblBacteria; EEV00494; EEV00494; ROSINTL182_07590. DR PATRIC; 30041826; VBIRosInt114022_2304. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 214 AA; 23826 MW; 8540E76FB974DA77 CRC64; MCKKENPIPG KIIAVTNRSL CERPFLEQIK RVCETKPAAL ILREKDLPET EYEEMARQVL AICEEYGVIC ILHSYIETAK RLERQYVHLP LPLLRTCMQK TENEEKQIKF MSGNLSMDQK NKNKLILGCS VHSVEDAIEA EKLGASYLTA GHIFATDCKR GLPPRGMEFL KQVCETVNIP VYAIGGIGLN DGKIDSVCEC GAAGACIMSA FMAI // ID C7GD13_9FIRM Unreviewed; 212 AA. AC C7GD13; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ROSINTL182_07813; OS Roseburia intestinalis L1-82. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=536231; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L1-82; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYJ02000141; EEV00320.1; -; Genomic_DNA. DR ProteinModelPortal; C7GD13; -. DR EnsemblBacteria; EEV00320; EEV00320; ROSINTL182_07813. DR PATRIC; 30042215; VBIRosInt114022_2437. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23258 MW; 3DBDC4E387FB1C15 CRC64; MRFDRKQLLL YGVTDRSWLN GQTLYEQVRQ ALEGGVSFLQ LREKNLSEQA FLEEAKEIQK LCREYKVPFI INDNVDLALE IDADGVHVGQ DDMEAGEVRK RLGEDKIIGV SAHSVEEALR AEKCGATYLG SGAVFGSGTK KDVGTLDHEV LKEICAAVQI PVVAIGGISR DNILQLKGTG IDGVAVISAI FAQKDIRAAA QELRKLSEEV CR // ID C7GN41_YEAS2 Unreviewed; 540 AA. AC C7GN41; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 16-APR-2014, entry version 24. DE SubName: Full=Thi6p; GN Name=THI6; ORFNames=C1Q_01673; OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=574961; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JAY291; RX PubMed=19812109; DOI=10.1101/gr.091777.109; RA Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., RA Netto O.V.C., Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., RA Noronha M.F., Dominska M., Andrietta M.G.S., Andrietta S.R., RA Cunha A.F., Gomes L.H., Tavares F.C.A., Alcarde A.R., Dietrich F.S., RA McCusker J.H., Petes T.D., Pereira G.A.G.; RT "Genome structure of a Saccharomyces cerevisiae strain widely used in RT bioethanol production."; RL Genome Res. 19:2258-2270(2009). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFL01000069; EEU07774.1; -; Genomic_DNA. DR ProteinModelPortal; C7GN41; -. DR SMR; C7GN41; 3-536. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 58059 MW; F34FA1E0B76E3930 CRC64; MVFTKEEVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDIE TKNFVAEALE VQKICKKYNV PLIINDRIDV AMAIDADGVH VGQDDMPIPM VRKLLGPSKI LGWSVGKPSE VETLAKWGPD MVDYIGVGTL FPTSTKKNPK KSPMGPQGAI AILDALEEFK ATWCRTVGIG GLHPDNIQRV LCQCVASNGK RSLDGISLVS DIMAAPDACA ATKRLRGLLD ATRYQFVECE LNNTFPTTTS IQNVISQVSN NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL ARIPNASLLL NTGSVAPIEM LKAAINAYNE VNRPITFDPV GYSATETRLC LNNTLLTYGQ FACIKGNCSE ILSLAKLNNH KMKGVDSSSG KTNIDTLVRA TQIVAFQYRT VAVCTGEFDC VADGTFGGEY KLSSGTEGIT AEDLPCVIIE DGPIPIMGDI TASGCSLGST IASFIGGLDS TGKLFDAVVG AVLLYKSAGK LASTRCQGSG SFHVELIDAL YQLFHENKPE KWSASLKKFK // ID C7H300_9FIRM Unreviewed; 210 AA. AC C7H300; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FAEPRAA2165_00648; OS Faecalibacterium prausnitzii A2-165. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=411483; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A2-165; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACOP02000009; EEU97734.1; -; Genomic_DNA. DR ProteinModelPortal; C7H300; -. DR EnsemblBacteria; EEU97734; EEU97734; FAEPRAA2165_00648. DR PATRIC; 30679089; VBIFaePra59507_0522. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22858 MW; 9D2B5A65F36F9A39 CRC64; MKCAEEYMRL YAVTDRAWVG GQTLYQQVES ALKGGVTCVQ LREKELDEEA FLKEAFELHD LCKKYNVPFF INDNVDIAIR CHAEGIHVGQ EDMAAAQVRQ RVGDEMMIGV SVHSVEEALE AVRHGADCLG VGAAFSTHTK ADVDVLPEGM MKAICDAVDI PVVAIGGIHK ENLLRLKGTG VNGVALVSAI FGAEDIEAEC RELKALAEQL // ID C7HDK2_CLOTM Unreviewed; 280 AA. AC C7HDK2; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ClothDRAFT_3019; OS Clostridium thermocellum DSM 2360. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=572545; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2360; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Hemme C.L.; RT "The draft genome of Clostridium thermocellum DSM 2360."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVX01000007; EEU02138.1; -; Genomic_DNA. DR ProteinModelPortal; C7HDK2; -. DR EnsemblBacteria; EEU02138; EEU02138; ClothDRAFT_3019. DR PATRIC; 27273144; VBICloThe106508_0900. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 107 111 HMP-PP binding (By similarity). FT REGION 204 206 THZ-P binding (By similarity). FT REGION 255 256 THZ-P binding (By similarity). FT METAL 140 140 Magnesium (By similarity). FT METAL 159 159 Magnesium (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 178 178 HMP-PP (By similarity). FT BINDING 207 207 HMP-PP (By similarity). FT BINDING 235 235 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 280 AA; 31802 MW; ECA8EFF75476B153 CRC64; MDIDRKASLL DLARANFKRV QEALRTVEES LKVLNENDLS KFYESCRFET YSIEKEYFKV LTFENKKGRL NEIITGLYCI TSEEHSKGRS NIEVVEKMIK AGVKIIQYRE KKKSLLEKYN ECKKIREMTL DSGVTFIVND NIDIAMMVKA DGVHIGQDDL PIEKVRELVG DEMIIGISTH SPTQAEDAVR RGADYIGVGP LYRTYTKEDV CEPVGLEYLD YVVKNINIPY VAIGGIKEHN MDEVLARGAR CIAMVTEIVG ADDIEEKISK VKSKFSRGVL // ID C7HVH0_9FIRM Unreviewed; 203 AA. AC C7HVH0; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0078_1271; OS Anaerococcus vaginalis ATCC 51170. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Anaerococcus. OX NCBI_TaxID=655811; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51170; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACXU01000020; EEU12253.1; -; Genomic_DNA. DR ProteinModelPortal; C7HVH0; -. DR EnsemblBacteria; EEU12253; EEU12253; HMPREF0078_1271. DR PATRIC; 24497028; VBIAnaVag63565_0612. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 22687 MW; BC47C5A724397A2E CRC64; MKKLYLVTNS DKYNEEEFLE RIEDAIKGGV DIVQLREKEK SDIEILNLGK KVKKICDKYD IPLLIDDKVH LAWALGCGVH VGKDDMPIAL CRKLLGEKAI IGATAKSVEA SKKAKKDGAN YLGVGAIFET KTHVKTKRTS IETLKKIKEE VDIDIYAIGG LNIENVEILK NTKVDGICVV RAIMDAKDVY QTSLELKEKI QEL // ID C7ITL1_THEET Unreviewed; 148 AA. AC C7ITL1; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=TeCCSD1DRAFT_1622; OS Thermoanaerobacter ethanolicus CCSD1. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=589861; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCSD1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Mouttaki H., Dong H., Zhou J., Hemme C.L.; RT "The draft genome of Thermoanaerobacter ethanolicus CCSD1."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACXY01000023; EEU61912.1; -; Genomic_DNA. DR ProteinModelPortal; C7ITL1; -. DR EnsemblBacteria; EEU61912; EEU61912; TeCCSD1DRAFT_1622. DR PATRIC; 30826967; VBITheEth125011_1684. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 148 AA; 16202 MW; 99F147CFC4C43404 CRC64; MDLTLYAITD RSYIKNMDIA EAVELAIKGG ATVIQLREKD ISSREFYEIA LKVKEVTKRN RIPLIINDRV DIALAVDADG VHVGQEDLPA DIVRKIIGRD KIVGVSARTV EEALKAQRDG ADYLGVGAVF KTPTKPEAEA IGIEGLKK // ID C7JBZ6_ACEP3 Unreviewed; 190 AA. AC C7JBZ6; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 13-NOV-2013, entry version 29. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN OrderedLocusNames=APA01_02610; OS Acetobacter pasteurianus (strain NBRC 3283 / LMG 1513 / CCTM 1153). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634452; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 3283 / LMG 1513 / CCTM 1153; RX PubMed=19638423; DOI=10.1093/nar/gkp612; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Nucleic Acids Res. 37:5768-5783(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011121; BAH98413.1; -; Genomic_DNA. DR RefSeq; YP_003186793.1; NC_013209.1. DR ProteinModelPortal; C7JBZ6; -. DR STRING; 634452.APA01_02610; -. DR EnsemblBacteria; BAH98413; BAH98413; APA01_02610. DR GeneID; 8434520; -. DR KEGG; apt:APA01_02610; -. DR PATRIC; 20630768; VBIAcePas139226_0266. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; APAS634452:GI0T-261-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 190 AA; 20113 MW; B0E8B42A9EF2C9A0 CRC64; MSDLYLVTPA VSDAQAFLPV LEAGLAHHQP AAVLLRLVDM PASAARQAVL LLKPVIQARD IALMLENAPT LAQETGCDGV HLSASYTAAS VKDVRRIIGP DLQLGVAVGE SRDAAMCAGE DGADYICFGA EDGASLETVS ALTRWWSLMM ELPVVAQAQT PADLAVLNAS GADFVMPSEQ WWQQPDAWQG // ID C7JGP3_ACEP3 Unreviewed; 201 AA. AC C7JGP3; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 31. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN OrderedLocusNames=APA01_11030; OS Acetobacter pasteurianus (strain NBRC 3283 / LMG 1513 / CCTM 1153). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634452; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 3283 / LMG 1513 / CCTM 1153; RX PubMed=19638423; DOI=10.1093/nar/gkp612; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Nucleic Acids Res. 37:5768-5783(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011121; BAH99252.1; -; Genomic_DNA. DR RefSeq; YP_003187632.1; NC_013209.1. DR ProteinModelPortal; C7JGP3; -. DR STRING; 634452.APA01_11030; -. DR EnsemblBacteria; BAH99252; BAH99252; APA01_11030. DR GeneID; 8435211; -. DR KEGG; apt:APA01_11030; -. DR PATRIC; 20632578; VBIAcePas139226_1166. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; APAS634452:GI0T-1105-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 22025 MW; 95A7C6BC567B0FD6 CRC64; MTALPQKIYP VVDSATWVDR LGGAGARFIQ LRLKDMEEDA LRAEIRQGHA YAKQHGVCLV LNDYWQIALD EGIDYIHLGQ EDLDTADLAA IRKGGIRLGI STHCHEELDR ALSCNPDYVA LGPIWETKLK KMAFGPQGPL KLTEWRKLIG NLPLVAIGGI TLERAWACIE AGADSVSAVS AFIRQPDPEG QVKAWLAAVE G // ID C7JK37_ACEPA Unreviewed; 190 AA. AC C7JK37; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA03_02610; OS Acetobacter pasteurianus IFO 3283-03. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634453; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011128; BAI01464.1; -; Genomic_DNA. DR RefSeq; YP_005476859.1; NC_017100.1. DR ProteinModelPortal; C7JK37; -. DR EnsemblBacteria; BAI01464; BAI01464; APA03_02610. DR GeneID; 12065568; -. DR KEGG; apf:APA03_02610; -. DR PATRIC; 36851095; VBIAcePas145093_0267. DR KO; K00788; -. DR BioCyc; APAS634453:GL7D-261-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 190 AA; 20113 MW; B0E8B42A9EF2C9A0 CRC64; MSDLYLVTPA VSDAQAFLPV LEAGLAHHQP AAVLLRLVDM PASAARQAVL LLKPVIQARD IALMLENAPT LAQETGCDGV HLSASYTAAS VKDVRRIIGP DLQLGVAVGE SRDAAMCAGE DGADYICFGA EDGASLETVS ALTRWWSLMM ELPVVAQAQT PADLAVLNAS GADFVMPSEQ WWQQPDAWQG // ID C7JMH8_ACEPA Unreviewed; 201 AA. AC C7JMH8; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA03_11030; OS Acetobacter pasteurianus IFO 3283-03. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634453; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011128; BAI02305.1; -; Genomic_DNA. DR RefSeq; YP_005477700.1; NC_017100.1. DR ProteinModelPortal; C7JMH8; -. DR EnsemblBacteria; BAI02305; BAI02305; APA03_11030. DR GeneID; 12064876; -. DR KEGG; apf:APA03_11030; -. DR PATRIC; 36852909; VBIAcePas145093_1169. DR KO; K00788; -. DR BioCyc; APAS634453:GL7D-1107-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 22025 MW; 95A7C6BC567B0FD6 CRC64; MTALPQKIYP VVDSATWVDR LGGAGARFIQ LRLKDMEEDA LRAEIRQGHA YAKQHGVCLV LNDYWQIALD EGIDYIHLGQ EDLDTADLAA IRKGGIRLGI STHCHEELDR ALSCNPDYVA LGPIWETKLK KMAFGPQGPL KLTEWRKLIG NLPLVAIGGI TLERAWACIE AGADSVSAVS AFIRQPDPEG QVKAWLAAVE G // ID C7JUA5_ACEPA Unreviewed; 190 AA. AC C7JUA5; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 23. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA07_02610; OS Acetobacter pasteurianus IFO 3283-07. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634454; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011135; BAI04512.1; -; Genomic_DNA. DR RefSeq; YP_005486000.1; NC_017121.1. DR ProteinModelPortal; C7JUA5; -. DR EnsemblBacteria; BAI04512; BAI04512; APA07_02610. DR GeneID; 12073667; -. DR KEGG; apu:APA07_02610; -. DR PATRIC; 36857601; VBIAcePas143188_0268. DR KO; K00788; -. DR BioCyc; APAS634454:GL7B-261-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 190 AA; 20113 MW; B0E8B42A9EF2C9A0 CRC64; MSDLYLVTPA VSDAQAFLPV LEAGLAHHQP AAVLLRLVDM PASAARQAVL LLKPVIQARD IALMLENAPT LAQETGCDGV HLSASYTAAS VKDVRRIIGP DLQLGVAVGE SRDAAMCAGE DGADYICFGA EDGASLETVS ALTRWWSLMM ELPVVAQAQT PADLAVLNAS GADFVMPSEQ WWQQPDAWQG // ID C7JWP4_ACEPA Unreviewed; 201 AA. AC C7JWP4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 23. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA07_11030; OS Acetobacter pasteurianus IFO 3283-07. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634454; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011135; BAI05351.1; -; Genomic_DNA. DR RefSeq; YP_005486839.1; NC_017121.1. DR ProteinModelPortal; C7JWP4; -. DR EnsemblBacteria; BAI05351; BAI05351; APA07_11030. DR GeneID; 12074511; -. DR KEGG; apu:APA07_11030; -. DR PATRIC; 36859417; VBIAcePas143188_1171. DR KO; K00788; -. DR BioCyc; APAS634454:GL7B-1105-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 22025 MW; 95A7C6BC567B0FD6 CRC64; MTALPQKIYP VVDSATWVDR LGGAGARFIQ LRLKDMEEDA LRAEIRQGHA YAKQHGVCLV LNDYWQIALD EGIDYIHLGQ EDLDTADLAA IRKGGIRLGI STHCHEELDR ALSCNPDYVA LGPIWETKLK KMAFGPQGPL KLTEWRKLIG NLPLVAIGGI TLERAWACIE AGADSVSAVS AFIRQPDPEG QVKAWLAAVE G // ID C7K4J7_ACEPA Unreviewed; 190 AA. AC C7K4J7; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 22. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA22_02610; OS Acetobacter pasteurianus IFO 3283-22. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634455; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011142; BAI07559.1; -; Genomic_DNA. DR RefSeq; YP_005488805.1; NC_017125.1. DR ProteinModelPortal; C7K4J7; -. DR EnsemblBacteria; BAI07559; BAI07559; APA22_02610. DR GeneID; 12076967; -. DR KEGG; apq:APA22_02610; -. DR PATRIC; 36870619; VBIAcePas142344_0267. DR KO; K00788; -. DR BioCyc; APAS634455:GL7C-261-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 190 AA; 20113 MW; B0E8B42A9EF2C9A0 CRC64; MSDLYLVTPA VSDAQAFLPV LEAGLAHHQP AAVLLRLVDM PASAARQAVL LLKPVIQARD IALMLENAPT LAQETGCDGV HLSASYTAAS VKDVRRIIGP DLQLGVAVGE SRDAAMCAGE DGADYICFGA EDGASLETVS ALTRWWSLMM ELPVVAQAQT PADLAVLNAS GADFVMPSEQ WWQQPDAWQG // ID C7K6Y8_ACEPA Unreviewed; 201 AA. AC C7K6Y8; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 22. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA22_11030; OS Acetobacter pasteurianus IFO 3283-22. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634455; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011142; BAI08400.1; -; Genomic_DNA. DR RefSeq; YP_005489646.1; NC_017125.1. DR ProteinModelPortal; C7K6Y8; -. DR EnsemblBacteria; BAI08400; BAI08400; APA22_11030. DR GeneID; 12077813; -. DR KEGG; apq:APA22_11030; -. DR PATRIC; 36872437; VBIAcePas142344_1171. DR KO; K00788; -. DR BioCyc; APAS634455:GL7C-1107-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 22025 MW; 95A7C6BC567B0FD6 CRC64; MTALPQKIYP VVDSATWVDR LGGAGARFIQ LRLKDMEEDA LRAEIRQGHA YAKQHGVCLV LNDYWQIALD EGIDYIHLGQ EDLDTADLAA IRKGGIRLGI STHCHEELDR ALSCNPDYVA LGPIWETKLK KMAFGPQGPL KLTEWRKLIG NLPLVAIGGI TLERAWACIE AGADSVSAVS AFIRQPDPEG QVKAWLAAVE G // ID C7KDR6_ACEPA Unreviewed; 190 AA. AC C7KDR6; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA26_02610; OS Acetobacter pasteurianus IFO 3283-26. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634456; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011149; BAI10607.1; -; Genomic_DNA. DR RefSeq; YP_005497907.1; NC_017146.1. DR ProteinModelPortal; C7KDR6; -. DR EnsemblBacteria; BAI10607; BAI10607; APA26_02610. DR GeneID; 12087310; -. DR KEGG; apx:APA26_02610; -. DR PATRIC; 36877131; VBIAcePas144932_0267. DR KO; K00788; -. DR BioCyc; APAS634456:GL79-261-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 190 AA; 20113 MW; B0E8B42A9EF2C9A0 CRC64; MSDLYLVTPA VSDAQAFLPV LEAGLAHHQP AAVLLRLVDM PASAARQAVL LLKPVIQARD IALMLENAPT LAQETGCDGV HLSASYTAAS VKDVRRIIGP DLQLGVAVGE SRDAAMCAGE DGADYICFGA EDGASLETVS ALTRWWSLMM ELPVVAQAQT PADLAVLNAS GADFVMPSEQ WWQQPDAWQG // ID C7KG57_ACEPA Unreviewed; 201 AA. AC C7KG57; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA26_11030; OS Acetobacter pasteurianus IFO 3283-26. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634456; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011149; BAI11448.1; -; Genomic_DNA. DR RefSeq; YP_005498748.1; NC_017146.1. DR ProteinModelPortal; C7KG57; -. DR EnsemblBacteria; BAI11448; BAI11448; APA26_11030. DR GeneID; 12087000; -. DR KEGG; apx:APA26_11030; -. DR PATRIC; 36878945; VBIAcePas144932_1169. DR KO; K00788; -. DR BioCyc; APAS634456:GL79-1107-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 22025 MW; 95A7C6BC567B0FD6 CRC64; MTALPQKIYP VVDSATWVDR LGGAGARFIQ LRLKDMEEDA LRAEIRQGHA YAKQHGVCLV LNDYWQIALD EGIDYIHLGQ EDLDTADLAA IRKGGIRLGI STHCHEELDR ALSCNPDYVA LGPIWETKLK KMAFGPQGPL KLTEWRKLIG NLPLVAIGGI TLERAWACIE AGADSVSAVS AFIRQPDPEG QVKAWLAAVE G // ID C7KN32_ACEPA Unreviewed; 190 AA. AC C7KN32; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA32_02610; OS Acetobacter pasteurianus IFO 3283-32. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634457; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011156; BAI13655.1; -; Genomic_DNA. DR RefSeq; YP_005482715.1; NC_017111.1. DR ProteinModelPortal; C7KN32; -. DR EnsemblBacteria; BAI13655; BAI13655; APA32_02610. DR GeneID; 12071704; -. DR KEGG; apz:APA32_02610; -. DR PATRIC; 36883635; VBIAcePas144801_0267. DR KO; K00788; -. DR BioCyc; APAS634457:GL7K-261-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 190 AA; 20113 MW; B0E8B42A9EF2C9A0 CRC64; MSDLYLVTPA VSDAQAFLPV LEAGLAHHQP AAVLLRLVDM PASAARQAVL LLKPVIQARD IALMLENAPT LAQETGCDGV HLSASYTAAS VKDVRRIIGP DLQLGVAVGE SRDAAMCAGE DGADYICFGA EDGASLETVS ALTRWWSLMM ELPVVAQAQT PADLAVLNAS GADFVMPSEQ WWQQPDAWQG // ID C7KQH1_ACEPA Unreviewed; 201 AA. AC C7KQH1; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA32_11030; OS Acetobacter pasteurianus IFO 3283-32. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634457; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011156; BAI14494.1; -; Genomic_DNA. DR RefSeq; YP_005483554.1; NC_017111.1. DR ProteinModelPortal; C7KQH1; -. DR EnsemblBacteria; BAI14494; BAI14494; APA32_11030. DR GeneID; 12072548; -. DR KEGG; apz:APA32_11030; -. DR PATRIC; 36885457; VBIAcePas144801_1173. DR KO; K00788; -. DR BioCyc; APAS634457:GL7K-1105-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 22025 MW; 95A7C6BC567B0FD6 CRC64; MTALPQKIYP VVDSATWVDR LGGAGARFIQ LRLKDMEEDA LRAEIRQGHA YAKQHGVCLV LNDYWQIALD EGIDYIHLGQ EDLDTADLAA IRKGGIRLGI STHCHEELDR ALSCNPDYVA LGPIWETKLK KMAFGPQGPL KLTEWRKLIG NLPLVAIGGI TLERAWACIE AGADSVSAVS AFIRQPDPEG QVKAWLAAVE G // ID C7KXE7_ACEPA Unreviewed; 190 AA. AC C7KXE7; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 22. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA42C_02610; OS Acetobacter pasteurianus IFO 3283-01-42C. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634458; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011163; BAI16701.1; -; Genomic_DNA. DR RefSeq; YP_005500773.1; NC_017150.1. DR ProteinModelPortal; C7KXE7; -. DR GeneID; 12089691; -. DR KEGG; apw:APA42C_02610; -. DR PATRIC; 36844731; VBIAcePas142730_0267. DR KO; K00788; -. DR BioCyc; APAS634458:GL78-261-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 190 AA; 20113 MW; B0E8B42A9EF2C9A0 CRC64; MSDLYLVTPA VSDAQAFLPV LEAGLAHHQP AAVLLRLVDM PASAARQAVL LLKPVIQARD IALMLENAPT LAQETGCDGV HLSASYTAAS VKDVRRIIGP DLQLGVAVGE SRDAAMCAGE DGADYICFGA EDGASLETVS ALTRWWSLMM ELPVVAQAQT PADLAVLNAS GADFVMPSEQ WWQQPDAWQG // ID C7KZT6_ACEPA Unreviewed; 201 AA. AC C7KZT6; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 22. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA42C_11030; OS Acetobacter pasteurianus IFO 3283-01-42C. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634458; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011163; BAI17540.1; -; Genomic_DNA. DR RefSeq; YP_005501612.1; NC_017150.1. DR ProteinModelPortal; C7KZT6; -. DR GeneID; 12090535; -. DR KEGG; apw:APA42C_11030; -. DR PATRIC; 36846553; VBIAcePas142730_1173. DR KO; K00788; -. DR BioCyc; APAS634458:GL78-1105-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 22025 MW; 95A7C6BC567B0FD6 CRC64; MTALPQKIYP VVDSATWVDR LGGAGARFIQ LRLKDMEEDA LRAEIRQGHA YAKQHGVCLV LNDYWQIALD EGIDYIHLGQ EDLDTADLAA IRKGGIRLGI STHCHEELDR ALSCNPDYVA LGPIWETKLK KMAFGPQGPL KLTEWRKLIG NLPLVAIGGI TLERAWACIE AGADSVSAVS AFIRQPDPEG QVKAWLAAVE G // ID C7L235_ACEPA Unreviewed; 201 AA. AC C7L235; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA12_11030; OS Acetobacter pasteurianus IFO 3283-12. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011170; BAI20524.1; -; Genomic_DNA. DR RefSeq; YP_005480864.1; NC_017108.1. DR ProteinModelPortal; C7L235; -. DR EnsemblBacteria; BAI20524; BAI20524; APA12_11030. DR GeneID; 12068164; -. DR KEGG; apg:APA12_11030; -. DR PATRIC; 36865937; VBIAcePas146001_1175. DR KO; K00788; -. DR BioCyc; APAS634459:GL7A-1105-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 22025 MW; 95A7C6BC567B0FD6 CRC64; MTALPQKIYP VVDSATWVDR LGGAGARFIQ LRLKDMEEDA LRAEIRQGHA YAKQHGVCLV LNDYWQIALD EGIDYIHLGQ EDLDTADLAA IRKGGIRLGI STHCHEELDR ALSCNPDYVA LGPIWETKLK KMAFGPQGPL KLTEWRKLIG NLPLVAIGGI TLERAWACIE AGADSVSAVS AFIRQPDPEG QVKAWLAAVE G // ID C7L771_ACEPA Unreviewed; 190 AA. AC C7L771; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APA12_02610; OS Acetobacter pasteurianus IFO 3283-12. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3283; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011170; BAI19685.1; -; Genomic_DNA. DR RefSeq; YP_005480025.1; NC_017108.1. DR ProteinModelPortal; C7L771; -. DR EnsemblBacteria; BAI19685; BAI19685; APA12_02610. DR GeneID; 12067320; -. DR KEGG; apg:APA12_02610; -. DR PATRIC; 36864111; VBIAcePas146001_0267. DR KO; K00788; -. DR BioCyc; APAS634459:GL7A-261-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 190 AA; 20113 MW; B0E8B42A9EF2C9A0 CRC64; MSDLYLVTPA VSDAQAFLPV LEAGLAHHQP AAVLLRLVDM PASAARQAVL LLKPVIQARD IALMLENAPT LAQETGCDGV HLSASYTAAS VKDVRRIIGP DLQLGVAVGE SRDAAMCAGE DGADYICFGA EDGASLETVS ALTRWWSLMM ELPVVAQAQT PADLAVLNAS GADFVMPSEQ WWQQPDAWQG // ID C7LDU2_BRUMC Unreviewed; 221 AA. AC C7LDU2; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 30. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BMI_I1727; OS Brucella microti (strain CCM 4915). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=568815; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCM 4915; RX PubMed=19653890; DOI=10.1186/1471-2164-10-352; RA Audic S., Lescot M., Claverie J.M., Scholz H.C.; RT "Brucella microti: the genome sequence of an emerging pathogen."; RL BMC Genomics 10:352-352(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001578; ACU48677.1; -; Genomic_DNA. DR RefSeq; YP_003107626.1; NC_013119.1. DR ProteinModelPortal; C7LDU2; -. DR STRING; 568815.BMI_I1727; -. DR EnsemblBacteria; ACU48677; ACU48677; BMI_I1727. DR GeneID; 8321287; -. DR KEGG; bmr:BMI_I1727; -. DR PATRIC; 17808475; VBIBruMic92249_2927. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BMIC568815:GJUE-1723-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C7LFR7_BRUMC Unreviewed; 203 AA. AC C7LFR7; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BMI_I217; OS Brucella microti (strain CCM 4915). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=568815; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCM 4915; RX PubMed=19653890; DOI=10.1186/1471-2164-10-352; RA Audic S., Lescot M., Claverie J.M., Scholz H.C.; RT "Brucella microti: the genome sequence of an emerging pathogen."; RL BMC Genomics 10:352-352(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001578; ACU47232.1; -; Genomic_DNA. DR RefSeq; YP_003106181.1; NC_013119.1. DR ProteinModelPortal; C7LFR7; -. DR STRING; 568815.BMI_I217; -. DR EnsemblBacteria; ACU47232; ACU47232; BMI_I217. DR GeneID; 8319782; -. DR KEGG; bmr:BMI_I217; -. DR PATRIC; 17805401; VBIBruMic92249_1426. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BMIC568815:GJUE-217-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C7LNK7_DESBD Unreviewed; 216 AA. AC C7LNK7; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dbac_0773; OS Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378) OS (Desulfovibrio baculatus). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfomicrobiaceae; Desulfomicrobium. OX NCBI_TaxID=525897; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4028 / VKM B-1378; RX PubMed=21304634; DOI=10.4056/sigs.13134; RA Copeland A., Spring S., Goker M., Schneider S., Lapidus A., RA Del Rio T.G., Tice H., Cheng J.F., Chen F., Nolan M., Bruce D., RA Goodwin L., Pitluck S., Ivanova N., Mavrommatis K., Ovchinnikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.C., Meincke L., Sims D., Brettin T., Detter J.C., Han C., RA Chain P., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Lucas S.; RT "Complete genome sequence of Desulfomicrobium baculatum type strain RT (X)."; RL Stand. Genomic Sci. 1:29-37(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001629; ACU88892.1; -; Genomic_DNA. DR RefSeq; YP_003157308.1; NC_013173.1. DR ProteinModelPortal; C7LNK7; -. DR STRING; 525897.Dbac_0773; -. DR EnsemblBacteria; ACU88892; ACU88892; Dbac_0773. DR GeneID; 8376428; -. DR KEGG; dba:Dbac_0773; -. DR PATRIC; 21703882; VBIDesBac69216_0794. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DBAC525897:GI50-798-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22956 MW; 689AE770EE39E31A CRC64; MNGRELVTSL MRIGGLYGLT AEKFSLGRRN ADVVQAMLDG GIRIIQYREK TKKMGLKYEE CLHLRAMTRE AGAAFIVNDD IDLALLVGAD GVHVGQEDLP LEAVRSLVGE NMAIGLSTHS PEQGLAAEAR GADYIGVGPI FATQTKEDVC APVGFAYLDF VAGNLNLPFV AIGGIKEHNL AEVAAHGARC MALVTEITAA ADIRGKIAAL TRILHG // ID C7LPK1_DESBD Unreviewed; 211 AA. AC C7LPK1; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dbac_0929; OS Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378) OS (Desulfovibrio baculatus). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfomicrobiaceae; Desulfomicrobium. OX NCBI_TaxID=525897; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4028 / VKM B-1378; RX PubMed=21304634; DOI=10.4056/sigs.13134; RA Copeland A., Spring S., Goker M., Schneider S., Lapidus A., RA Del Rio T.G., Tice H., Cheng J.F., Chen F., Nolan M., Bruce D., RA Goodwin L., Pitluck S., Ivanova N., Mavrommatis K., Ovchinnikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.C., Meincke L., Sims D., Brettin T., Detter J.C., Han C., RA Chain P., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Lucas S.; RT "Complete genome sequence of Desulfomicrobium baculatum type strain RT (X)."; RL Stand. Genomic Sci. 1:29-37(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001629; ACU89044.1; -; Genomic_DNA. DR RefSeq; YP_003157460.1; NC_013173.1. DR ProteinModelPortal; C7LPK1; -. DR STRING; 525897.Dbac_0929; -. DR EnsemblBacteria; ACU89044; ACU89044; Dbac_0929. DR GeneID; 8376587; -. DR KEGG; dba:Dbac_0929; -. DR PATRIC; 21704202; VBIDesBac69216_0951. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DBAC525897:GI50-957-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21798 MW; 0B3AD866EBAE4561 CRC64; MPDLSLYLVT DRRLSLGRST VDIVRAAVAG GVTCVQLREK ECSTRQFVTE ARAVRELLAG TGIPLIINDR LDVALAVGAD GVHLGQTDML IADARRLVGT DMLIGISAEC VDDAVRAQAE GADYVGISPV FATPTKTDTA PALGLDGVAL IRAAVSLPLV GIGGIGPGNA TEVIRAGCDG VAVVSAIISA PDPKRAAAEL KTIIRRAKEH P // ID C7LY53_ACIFD Unreviewed; 231 AA. AC C7LY53; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Afer_0711; OS Acidimicrobium ferrooxidans (strain DSM 10331 / JCM 15462 / NBRC OS 103882 / ICP). OC Bacteria; Actinobacteria; Acidimicrobidae; Acidimicrobiales; OC Acidimicrobineae; Acidimicrobiaceae; Acidimicrobium. OX NCBI_TaxID=525909; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10331 / JCM 15462 / NBRC 103882 / ICP; RX PubMed=21304635; DOI=10.4056/sigs.1463; RA Clum A., Nolan M., Lang E., Glavina Del Rio T., Tice H., Copeland A., RA Cheng J.F., Lucas S., Chen F., Bruce D., Goodwin L., Pitluck S., RA Ivanova N., Mavrommatis K., Mikhailova N., Pati A., Chen A., RA Palaniappan K., Goker M., Spring S., Land M., Hauser L., Chang Y.J., RA Jeffries C.C., Chain P., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Acidimicrobium ferrooxidans type strain RT (ICP)."; RL Stand. Genomic Sci. 1:38-45(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001631; ACU53661.1; -; Genomic_DNA. DR RefSeq; YP_003109334.1; NC_013124.1. DR ProteinModelPortal; C7LY53; -. DR STRING; 525909.Afer_0711; -. DR EnsemblBacteria; ACU53661; ACU53661; Afer_0711. DR GeneID; 8322771; -. DR KEGG; afo:Afer_0711; -. DR PATRIC; 20641077; VBIAciFer34262_0747. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AFER525909:GHMR-721-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). SQ SEQUENCE 231 AA; 24522 MW; 2894082C99DA01CB CRC64; MTRSLGDRCL YLCVPLRRDL LAFVDATVRG GVDIVQLRAK DAPDGLVLRA ARDLARLLAR RGVPFIVNDR PDIALASDAD GVHVGQDDLD VGTVRSLVGP DRIVGLSTHA PAEFNAASPL ADYLSVGPVE PTPTKPGRPG TGRSYVAFAH RAAEARPRFI TGNVTAQAIP ALVAAGARRF VVVRALTEAP DPRQAAHDLR AAIELAREQP SWGTPGAATL THNRRSSTPV L // ID C7MH58_BRAFD Unreviewed; 218 AA. AC C7MH58; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Bfae_27370; OS Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / NCIB 9860). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Dermabacteraceae; Brachybacterium. OX NCBI_TaxID=446465; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43885 / DSM 4810 / NCIB 9860; RX PubMed=21304631; DOI=10.4056/sigs.492; RA Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., RA Nolan M., Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., RA Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., RA Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Brachybacterium faecium type strain RT (Schefferle 6-10)."; RL Stand. Genomic Sci. 1:3-11(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001643; ACU86506.1; -; Genomic_DNA. DR RefSeq; YP_003156096.1; NC_013172.1. DR ProteinModelPortal; C7MH58; -. DR STRING; 446465.Bfae_27370; -. DR EnsemblBacteria; ACU86506; ACU86506; Bfae_27370. DR GeneID; 8401281; -. DR KEGG; bfa:Bfae_27370; -. DR PATRIC; 21177165; VBIBraFae133938_2703. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RPTPTKN; -. DR OrthoDB; EOG6PZXB0; -. DR BioCyc; BFAE446465:GH3P-2731-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). SQ SEQUENCE 218 AA; 22024 MW; 2D11788328F1BB7B CRC64; MSPAPALDLR CYLVTSGTGR RTVEVAAAAA AAGAGVVQVR AKDIPTAELL QLVLAVAEAV RAANPGTRVL VDDRADVAAA ARRRGAAVHG VHLGQDDLPV TDARALLGPD ALIGLTTGTL ELVRAAEEVR DQVDYLGAGP FRLTPTKDSG RPPLGIEGYR ALTAASSLPI VAIGDVTPED APALVQAGAA GVALVRAVMD APDPARTVRT VLAGIAGV // ID C7MNZ2_CRYCD Unreviewed; 231 AA. AC C7MNZ2; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ccur_09340; OS Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / 12-3). OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Cryptobacterium. OX NCBI_TaxID=469378; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700683 / DSM 15641 / 12-3; RX PubMed=21304644; DOI=10.40456/sigs.12260; RA Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T., RA Kuske C., Detter J.C., Han C., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D., RA Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N., Chen A., RA Palaniappan K., Chain P., D'haeseleer P., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Rohde M., Klenk H.P., RA Kyrpides N.C.; RT "Complete genome sequence of Cryptobacterium curtum type strain (12- RT 3)."; RL Stand. Genomic Sci. 1:93-100(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001682; ACU94632.1; -; Genomic_DNA. DR RefSeq; YP_003151314.1; NC_013170.1. DR ProteinModelPortal; C7MNZ2; -. DR STRING; 469378.Ccur_09340; -. DR EnsemblBacteria; ACU94632; ACU94632; Ccur_09340. DR GeneID; 8375142; -. DR KEGG; ccu:Ccur_09340; -. DR PATRIC; 21525673; VBICryCur116861_0891. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CCUR469378:GH4Z-937-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 55 59 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT REGION 202 203 THZ-P binding (By similarity). FT METAL 88 88 Magnesium (By similarity). FT METAL 107 107 Magnesium (By similarity). FT BINDING 87 87 HMP-PP (By similarity). FT BINDING 126 126 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 231 AA; 24274 MW; AC51895BBA781C42 CRC64; MPDKELRAVI SATPRQRFSS DDVLLYAVTD RSWLRGRTLE SCVAAAIAGG ATIIQLREKQ ASFDELVALA YSIKQICHDA GVLFVIDDNV QAAVAVDADG VHVGQDDSSC VQARKMLGPD KIVGVSAQTI AQARAAEAAS ADYLGVGALM PTATKPDAVE VTREELYDIC HAVSIPVVGI GGLNEQTIPR LAGSGACGAA VVSAIFAAHD CKAAARQLRT TCNQVFHAQQ R // ID C7MQ06_SACVD Unreviewed; 225 AA. AC C7MQ06; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Svir_34670; OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / OS NBRC 12207 / P101). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=471857; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101; RX DOI=10.4056/sigs.20263; RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A., RA Glavina del Rio T., Lucas S., Chen F., Tice H., Pitluck S., RA Cheng J.-F., Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., RA Bruce D., Goodwin L., Chain P., D'haeseleer P., Chen A., RA Palaniappan K., Ivanova N., Mavromatis K., Mikhailova N., Rohde M., RA Tindall B.J., Goeker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Saccharomonospora viridis type strain RT (P101)."; RL Stand. Genomic Sci. 1:141-149(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001683; ACU98429.1; -; Genomic_DNA. DR RefSeq; YP_003135256.1; NC_013159.1. DR ProteinModelPortal; C7MQ06; -. DR STRING; 471857.Svir_34670; -. DR EnsemblBacteria; ACU98429; ACU98429; Svir_34670. DR GeneID; 8388789; -. DR KEGG; svi:Svir_34670; -. DR PATRIC; 23397516; VBISacVir111818_3531. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SVIR471857:GHAV-3452-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 23734 MW; 8939CBA295FDA61E CRC64; MPGLDGDQIR KRLADAKLYL CTDARLPHGD LAEFVDAALA GGVDIVQLRD KTGGAPLEAA QEIEALEILA QACARHGALL AVNDRADVAL AVDADVLHLG QNDLPVSVAR RIIGERPVIG RSTHSLEQAR AASVEEGVDY FCVGPCWPTP TKPGRPAPGL DLVRAVADGI ETSRPWFAIG GIDRQRLDKV VEAGAHRVVV VRAITEADDP AEAARALRDG LVAVG // ID C7NJY9_KYTSD Unreviewed; 215 AA. AC C7NJY9; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ksed_02990; OS Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541) OS (Micrococcus sedentarius). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Dermacoccaceae; Kytococcus. OX NCBI_TaxID=478801; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541; RX PubMed=21304632; DOI=10.4056/sigs.761; RA Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F., RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., RA Ivanova N., Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., RA Chain P., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Schneider S., Goker M., Pukall R., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Kytococcus sedentarius type strain RT (541)."; RL Stand. Genomic Sci. 1:12-20(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001686; ACV05376.1; -; Genomic_DNA. DR RefSeq; YP_003148141.1; NC_013169.1. DR ProteinModelPortal; C7NJY9; -. DR STRING; 478801.Ksed_02990; -. DR EnsemblBacteria; ACV05376; ACV05376; Ksed_02990. DR GeneID; 8371809; -. DR KEGG; kse:Ksed_02990; -. DR PATRIC; 22190299; VBIKytSed14067_0284. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; KSED478801:GI4L-296-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 21641 MW; 08FF88068DD8F5B2 CRC64; MDLSLYLVTD SAMAGSRGLA DVVARAVAAG VTCVQLREKA ASDEEVVALG RQLVEMLAGT GVPLLIDDRV HLVHPIGADG VHIGQEDTPP TAARAALGPE AIIGLSVHDA AQVDAANALP PATLDYIGLG PVWATGTKDG HAPPIGPEGL ADLRRRSHHP AVAIGGVKAH TLAELAGSGV EGVAVVSAIC AAADVPAATR ELREALAASP LQGEL // ID C7NNW4_HALUD Unreviewed; 211 AA. AC C7NNW4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Huta_1463; OS Halorhabdus utahensis (strain DSM 12940 / JCM 11049 / AX-2). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halorhabdus. OX NCBI_TaxID=519442; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12940 / JCM 11049 / AX-2; RX DOI=10.4056/sigs.31864; RA Anderson I., Tindall B.J., Pomrenke H., Goker M., Lapidus A., RA Nolan M., Copeland A., Glavina Del Rio T., Chen F., Tice H., RA Cheng J.F., Lucas S., Chertkov O., Bruce D., Brettin T., Detter J.C., RA Han C., Goodwin L., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Pitluck S., Pati A., Mavromatis K., Ivanova N., Ovchinnikova G., RA Chen A., Palaniappan K., Chain P., Rohde M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Halorhabdus utahensis type strain (AX- RT 2)."; RL Stand. Genomic Sci. 1:218-225(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001687; ACV11639.1; -; Genomic_DNA. DR RefSeq; YP_003130372.1; NC_013158.1. DR ProteinModelPortal; C7NNW4; -. DR STRING; 519442.Huta_1463; -. DR EnsemblBacteria; ACV11639; ACV11639; Huta_1463. DR GeneID; 8383742; -. DR KEGG; hut:Huta_1463; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; HUTA519442:GH3V-1483-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22094 MW; 6674C689F706FF61 CRC64; MTDWRVYLVT QASLSGDRTT PEIVEAAIEG GVDVVQLREK DVNARERYEM GREVREHTRE AGVPLIVNDR VDLALALEAD GVHLGDEDLP VAVARELLGE DAIIGRSVSF VDDAREAETA GADYLGVGAI FPTGSKDDID DAEYAIGIDR VAAIVDAVDI PVVGIGGVTA ENADSVIDAG AAGVAVITEI TNADDPEAAT GRLIDAVSKG Q // ID C7NXU9_HALMD Unreviewed; 211 AA. AC C7NXU9; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Hmuk_0403; OS Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / OS NCIMB 13541) (Haloarcula mukohataei). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halomicrobium. OX NCBI_TaxID=485914; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541; RX PubMed=21304667; DOI=10.4056/sigs.42644; RA Tindall B.J., Schneider S., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., RA Saunders E., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Pati A., RA Ivanova N., Mavrommatis K., Chen A., Palaniappan K., Chain P., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Han C., RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Klenk H.P., Kyrpides N.C., Detter J.C.; RT "Complete genome sequence of Halomicrobium mukohataei type strain RT (arg-2)."; RL Stand. Genomic Sci. 1:270-277(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001688; ACV46537.1; -; Genomic_DNA. DR RefSeq; YP_003176244.1; NC_013202.1. DR ProteinModelPortal; C7NXU9; -. DR STRING; 485914.Hmuk_0403; -. DR EnsemblBacteria; ACV46537; ACV46537; Hmuk_0403. DR GeneID; 8409901; -. DR KEGG; hmu:Hmuk_0403; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; HMUK485914:GCKD-405-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21732 MW; 54643162AA3953D3 CRC64; MDYGVYLVTQ ASHSAGRSTP EIVSAAIDGG VDVVQLREKD LTARERLAIG RRVRERTRAA GVPLIVNDRI DLARAIDADG VHLGDDDLPL SVARELLGED AVLGRSVSFV EDAVAAEAAG ADYLGVGAVY ATGSKDDIDD DEHAIGPERI ATIVDAVSIP VVGIGGITPD NAAPVVDAGA DGVAVITAIT AADDPAAATR RLSETVDDAR E // ID C7PHE1_CHIPD Unreviewed; 204 AA. AC C7PHE1; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 13-NOV-2013, entry version 28. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Cpin_0622; OS Chitinophaga pinensis (strain ATCC 43595 / DSM 2588 / NCIB 11800 / UQM OS 2034). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Chitinophagaceae; Chitinophaga. OX NCBI_TaxID=485918; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43595 / DSM 2588 / NCIB 11800 / UQM 2034; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Sims D., Meinche L., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of Chitinophaga pinensis DSM 2588."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001699; ACU58120.1; -; Genomic_DNA. DR RefSeq; YP_003120321.1; NC_013132.1. DR ProteinModelPortal; C7PHE1; -. DR STRING; 485918.Cpin_0622; -. DR EnsemblBacteria; ACU58120; ACU58120; Cpin_0622. DR GeneID; 8356733; -. DR KEGG; cpi:Cpin_0622; -. DR PATRIC; 21349867; VBIChiPin99107_0615. DR eggNOG; NOG86118; -. DR KO; K00788; -. DR OMA; ANAVENF; -. DR OrthoDB; EOG6RC3V1; -. DR BioCyc; CPIN485918:GHYR-636-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 204 AA; 22546 MW; 48901CE14AEAF56F CRC64; MIQIITPPAW LPEETLYWQQ LLDEGADSIL LRKPGWSAAD YEQLLLAADA SCYSKLMIAG HPALCEKYGL QGIHFSENAG SLLTAADIAT YRQQGWLLST SVHTTAALQT ADVHWGQQLL APIFDSISKP GHNSLFREDF KLSKGAYQGK VLALGGIDHN TAIKARNMQF DGIALLGAIW QQPATAISRF RHIRKLWHNT AHLS // ID C7PHE3_CHIPD Unreviewed; 204 AA. AC C7PHE3; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cpin_0624; OS Chitinophaga pinensis (strain ATCC 43595 / DSM 2588 / NCIB 11800 / UQM OS 2034). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Chitinophagaceae; Chitinophaga. OX NCBI_TaxID=485918; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43595 / DSM 2588 / NCIB 11800 / UQM 2034; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Sims D., Meinche L., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of Chitinophaga pinensis DSM 2588."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001699; ACU58122.1; -; Genomic_DNA. DR RefSeq; YP_003120323.1; NC_013132.1. DR ProteinModelPortal; C7PHE3; -. DR STRING; 485918.Cpin_0624; -. DR EnsemblBacteria; ACU58122; ACU58122; Cpin_0624. DR GeneID; 8356735; -. DR KEGG; cpi:Cpin_0624; -. DR PATRIC; 21349871; VBIChiPin99107_0617. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPIN485918:GHYR-638-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21534 MW; 45311197AACBE02A CRC64; MISSLHYISQ QTAGATHLDN IQEACEAGCR WIQLRIKNEA SETILSTAMT AKAICSKYNA TLIINDHPDI AKKVGAHGVH VGKLDMTVAE ARVLTGETFI IGGTANTLED ILVHVKDGAD YVGVGPYRFT RTKEKLSPIL GLEGIAGIMQ SLKDMGIHIP VIAIGGILAE DIPALMATGI HGIAVSGLIT HAANKSQTVS SLTI // ID C7QGH1_CATAD Unreviewed; 218 AA. AC C7QGH1; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Caci_5993; OS Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC OS 102108 / JCM 14897). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Catenulisporineae; Catenulisporaceae; Catenulispora. OX NCBI_TaxID=479433; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897; RX DOI=10.4056/sigs.17259; RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., RA Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., RA Mikhailova N., Pati A., Ivanov N., Mavromatis K., Chen A., RA Palaniappan K., Chai P., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z., RA Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Catenulispora acidiphila type strain (ID RT 139908)."; RL Stand. Genomic Sci. 1:119-125(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001700; ACU74851.1; -; Genomic_DNA. DR RefSeq; YP_003116692.1; NC_013131.1. DR ProteinModelPortal; C7QGH1; -. DR STRING; 479433.Caci_5993; -. DR EnsemblBacteria; ACU74851; ACU74851; Caci_5993. DR GeneID; 8337356; -. DR KEGG; cai:Caci_5993; -. DR PATRIC; 21290711; VBICatAci36872_6101. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CACI479433:GI6Z-6032-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23146 MW; 834D852A9897762C CRC64; MTSGEDLRTK LSDARLYLCC DAREQQGDLP QFLDAVLSGG VDIVQLRQKG MEARQELAAL EVFADACRRH GKLLAVNDRA DIALGAGADI LHLGQDDLPV PLARHIIGEQ PLIGRSCHAE AEVDQAAAAP GVDYFCTGPV WPTPTKPGRF APGLGLVKYA ARLAPEGTRP WFAIGGIDTA NLDEVLTAGA RRVVVVRALT EAADPHAAAV ELSGRLRA // ID C7QQF0_CYAP0 Unreviewed; 343 AA. AC C7QQF0; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cyan8802_2684; OS Cyanothece sp. (strain PCC 8802) (Synechococcus sp. (strain RF-2)). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=395962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 8802; RX PubMed=21972240; DOI=10.1128/mBio.00214-11; RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., RA Min H., Sherman L.A., Pakrasi H.B.; RT "Novel metabolic attributes of the genus Cyanothece, comprising a RT group of unicellular nitrogen-fixing Cyanobacteria."; RL MBio 2:E214-E214(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001701; ACV01544.1; -; Genomic_DNA. DR RefSeq; YP_003138379.1; NC_013161.1. DR ProteinModelPortal; C7QQF0; -. DR STRING; 395962.Cyan8802_2684; -. DR EnsemblBacteria; ACV01544; ACV01544; Cyan8802_2684. DR GeneID; 8392010; -. DR KEGG; cyh:Cyan8802_2684; -. DR PATRIC; 21586935; VBICyaSp112625_2782. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; NFNRARE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CSP395962:GJC3-2707-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 125 Unknown (By similarity). FT REGION 126 343 Thiamine-phosphate synthase (By FT similarity). FT REGION 173 177 HMP-PP binding (By similarity). FT REGION 270 272 THZ-P binding (By similarity). FT METAL 206 206 Magnesium (By similarity). FT METAL 225 225 Magnesium (By similarity). FT BINDING 205 205 HMP-PP (By similarity). FT BINDING 244 244 HMP-PP (By similarity). FT BINDING 273 273 HMP-PP (By similarity). FT BINDING 300 300 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 343 AA; 38336 MW; 4238918E130B03E6 CRC64; MLKETHNSLS IPRILDANLN RAREGLRIIE EWCRFGLENS QLADNCKQMR QEIARWHTSE LRIARDTPND PGTALTHPQE ETRSSIDHLL QANLCRIQEA LRVLEEYGKL YQPQMGIAFK NMRYQVYSLE SNLVKQTRYE KYKKSPLYLV TSPDDNILSI VEAALQGGLT LVQYRDKNSE DTIQLEIAQK LCQLCHKYDA LFIMNDRADI ALSVNADGVH LGQQDISIAL ARQIVGPNRI IGRSTTNPQE MAKAIAEGAD YIGVGPVYAT PTKPDKPAVG LDYVKYAKEN SPIPWVAIGG IDLNNLNDVI SAGAQQVAVV RAIMKADNPT KATQELLAKL SLK // ID C7R3Y1_JONDD Unreviewed; 248 AA. AC C7R3Y1; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Jden_1182; OS Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / CIP 55134) OS (Listeria denitrificans). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Jonesiaceae; Jonesia. OX NCBI_TaxID=471856; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14870 / DSM 20603 / CIP 55134; RX PubMed=21304666; DOI=10.4056/sigs.41646; RA Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., RA Cheng J.F., Copeland A., Saunders E., Brettin T., Detter J.C., RA Bruce D., Goodwin L., Pati A., Ivanova N., Mavromatis K., RA Ovchinnikova G., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Chain P., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.; RT "Complete genome sequence of Jonesia denitrificans type strain (Prevot RT 55134)."; RL Stand. Genomic Sci. 1:262-269(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001706; ACV08838.1; -; Genomic_DNA. DR RefSeq; YP_003161141.1; NC_013174.1. DR ProteinModelPortal; C7R3Y1; -. DR STRING; 471856.Jden_1182; -. DR EnsemblBacteria; ACV08838; ACV08838; Jden_1182. DR GeneID; 8380359; -. DR KEGG; jde:Jden_1182; -. DR PATRIC; 22162486; VBIJonDen9837_1237. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RPTPTKN; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; JDEN471856:GH77-1217-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 53 57 HMP-PP binding (By similarity). FT REGION 156 158 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 109 109 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 159 159 HMP-PP (By similarity). FT BINDING 187 187 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 248 AA; 25353 MW; BAC567C92289E3E0 CRC64; MTTQPRTVPP TTWALNEVLR VCVVLDESHC AAAGRSVTQT VADAVAGGAT MIQVRAKNAD DREFYSLIAH VCAVVDGQVP VLVNDRVDLF LAARMDTMAV AGVHVGQRDL PVSVVRRLVG QHALIGVSAS RKEEIRSASH DWAAVSYIGL GALHATGTKA DAPAPLGLEA VAQRIELATV PTVVIGGITV ADVPAVRAVG AAGVAVSSAV CGARDAVAAA AQFRSAWDGT PVGVGKQEGH TTTAGGSQ // ID C7R6N5_KANKD Unreviewed; 493 AA. AC C7R6N5; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Kkor_0130; OS Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Kangiella. OX NCBI_TaxID=523791; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16069 / KCTC 12182 / SW-125; RX DOI=10.4056/sigs.36635; RA Han C., Sikorski J., Lapidus A., Nolan M., Glavina Del Rio T., RA Tice H., Cheng J.F., Lucas S., Chen F., Copeland A., Ivanova N., RA Mavromatis K., Ovchinnikova G., Pati A., Bruce D., Goodwin L., RA Pitluck S., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Chain P., Saunders E., Brettin T., Goker M., RA Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Kangiella koreensis type strain (SW- RT 125)."; RL Stand. Genomic Sci. 1:226-233(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001707; ACV25551.1; -; Genomic_DNA. DR RefSeq; YP_003145319.1; NC_013166.1. DR ProteinModelPortal; C7R6N5; -. DR STRING; 523791.Kkor_0130; -. DR EnsemblBacteria; ACV25551; ACV25551; Kkor_0130. DR GeneID; 8368899; -. DR KEGG; kko:Kkor_0130; -. DR PATRIC; 22165658; VBIKanKor123990_0121. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; KKOR523791:GHCO-130-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 493 AA; 54164 MW; 12D20ED9D6397888 CRC64; MKVTGKPVVW SYAGLDNSGM AGQVADIRTI EALGAHACCV TTALTAQNSQ RVVAINPSAK EQLQSQLEAL QELGQPNAIK VGLLPSEESI QLLITYLEKA SNPIQLVFDP VIESSSGTQF MPDEVLEQLE KLLPLVTVFT PNIDELARIT GQKIQSIDDI ESQAKKLLES GTSAVLVKGG HWPSEQASDF FVNRQHQFWL HSDRQETDNT RGTGCVLSSA IATALALDYS VEDAVVIGKM VLNQGLRHSY GIRDQKGPLA VQSWPGDERD MPRLTKQYAL NEHCFPCLKN QALDLYPVVD SAKWLERLLP LGIPTIQLRV KDLKNKELEN EIVAAIKIAK QNDAKLFIND YWQLAIKHGA FGVHLGQEDL DDADIAAISK AGLHLGISTH CFYEVARAHA IQPSYLACGP VYHTDSKQMP WIPHGIESLG YWNNVMQSYP WVAIGGINAD RIAEVASTGV SGIAMISAIT RSHNPEQTAT NMMQLIEQHR PLV // ID C7REN6_ANAPD Unreviewed; 205 AA. AC C7REN6; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Apre_1628; OS Anaerococcus prevotii (strain ATCC 9321 / DSM 20548 / JCM 6508 / PC1) OS (Peptostreptococcus prevotii) (Peptococcus prevotii). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Anaerococcus. OX NCBI_TaxID=525919; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9321 / DSM 20548 / JCM 6508 / PC1; RX PubMed=21304652; DOI=10.4056/sigs.24194; RA Labutti K., Pukall R., Steenblock K., Glavina Del Rio T., Tice H., RA Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C., Han C., RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Anaerococcus prevotii type strain RT (PC1)."; RL Stand. Genomic Sci. 1:159-165(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001708; ACV29649.1; -; Genomic_DNA. DR RefSeq; YP_003153370.1; NC_013171.1. DR ProteinModelPortal; C7REN6; -. DR STRING; 525919.Apre_1628; -. DR EnsemblBacteria; ACV29649; ACV29649; Apre_1628. DR GeneID; 8398440; -. DR KEGG; apr:Apre_1628; -. DR PATRIC; 20906566; VBIAnaPre102398_1740. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; APRE525919:GI6D-1693-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22735 MW; 6B262D2F8BDA10F3 CRC64; MTKLYLVTNS DKYDEEEFLR RVEEALRGGV DILQLREKDR PDREILELGK KVKALCDKYK VPMLIDDKAH LAWALGVGVH LGQEDMPVDL ARKLLGKDAL IGATAKSVEA AQKAEEDGAD YLGVGAIFDT KTHVKTKRTS VETFKEIKNK VSIDVYAIGG LNIENIDVLK SSGADGICVV RAIMDSPNVY EDTKKLKEKM EDILG // ID C7RJQ1_ACCPU Unreviewed; 322 AA. AC C7RJQ1; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 31. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=CAP2UW1_0258; OS Accumulibacter phosphatis (strain UW-1). OC Bacteria; Proteobacteria; Betaproteobacteria; OC Candidatus Accumulibacter. OX NCBI_TaxID=522306; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UW-1; RG US DOE Joint Genome Institute; RA Martin H.G., Ivanova N., Kunin V., Warnecke F., Barry K., He S., RA Salamov A., Szeto E., Dalin E., Pangilinan J.L., Lapidus A., Lowry S., RA Kyrpides N.C., McMahon K.D., Hugenholtz P.; RT "Complete sequence of chromosome of Candidatus Accumulibacter RT phosphatis clade IIA str. UW-1."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001715; ACV33615.1; -; Genomic_DNA. DR RefSeq; YP_003165544.1; NC_013194.1. DR ProteinModelPortal; C7RJQ1; -. DR STRING; 522306.CAP2UW1_0258; -. DR EnsemblBacteria; ACV33615; ACV33615; CAP2UW1_0258. DR GeneID; 8402386; -. DR KEGG; app:CAP2UW1_0258; -. DR PATRIC; 21256510; VBICanAcc132554_0523. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; APHO522306:GHXL-261-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 322 AA; 35199 MW; 8C7EE19B59127E8B CRC64; MNVVGEGATP ITEVAAAVLL RGDPATPEFL LAQRPVGKVY AGYWEFPGGK VEAGETTRAA LVRELQEELG VTVDQAWPWV CCEFTYPHAR VRLRFFRVTS WHGEIAPIEH SGFVWSKVGA AASVAPILPA NGPILRALAL PPVYALSHAE ERGVEAELTR LAHALSSGLR LIQVRDKTLP RAQRRHFAHM VVTLARGFAG ACVLVNDDPE LARTVSADGL HLSSRRLWEI DRRPDFDRVA ASCHTPADLA RAVELGLDFV VLGPVLPTAS HPEARAMGWE QFSRLLEHSP LPVYALGGLQ PNMLDTARRH GGHGIALMRG WR // ID C7RJZ9_ACCPU Unreviewed; 214 AA. AC C7RJZ9; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CAP2UW1_3583; OS Accumulibacter phosphatis (strain UW-1). OC Bacteria; Proteobacteria; Betaproteobacteria; OC Candidatus Accumulibacter. OX NCBI_TaxID=522306; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UW-1; RG US DOE Joint Genome Institute; RA Martin H.G., Ivanova N., Kunin V., Warnecke F., Barry K., He S., RA Salamov A., Szeto E., Dalin E., Pangilinan J.L., Lapidus A., Lowry S., RA Kyrpides N.C., McMahon K.D., Hugenholtz P.; RT "Complete sequence of chromosome of Candidatus Accumulibacter RT phosphatis clade IIA str. UW-1."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001715; ACV36840.1; -; Genomic_DNA. DR RefSeq; YP_003168769.1; NC_013194.1. DR ProteinModelPortal; C7RJZ9; -. DR STRING; 522306.CAP2UW1_3583; -. DR EnsemblBacteria; ACV36840; ACV36840; CAP2UW1_3583. DR GeneID; 8405751; -. DR KEGG; app:CAP2UW1_3583; -. DR PATRIC; 21263430; VBICanAcc132554_3944. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; APHO522306:GHXL-3616-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22048 MW; 535641261D251ACC CRC64; MAEPASHGLR GLYAITPGGV APSALLARVG AALAGGARLV QYRDKDADAV QRGELARALR SLCKRFDALL LINDDLALAL AVNADGVHLG ATDGDLRAAR QTLGPGRLLG ASCYADFEQA HAAVSAGADY VAFGAVYPSL TKPQAVRAPL SLFRRCRAEL RVPACAIGGI TLDNALPLLA AGADLLAVIT DLFEAADIAS RAAAYQRLCK EASA // ID C7T9H1_LACRG Unreviewed; 209 AA. AC C7T9H1; C8UZB4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LGG_00369, LRHM_0357; OS Lactobacillus rhamnosus (strain ATCC 53103 / GG). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=568703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 53103, and ATCC 53103 / GG [Tokyo]; RX PubMed=19820099; DOI=10.1128/JB.01287-09; RA Morita H., Toh H., Oshima K., Murakami M., Taylor T.D., Igimi S., RA Hattori M.; RT "Complete genome sequence of the probiotic Lactobacillus rhamnosus RT ATCC 53103."; RL J. Bacteriol. 191:7630-7631(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 53103 / GG [Helsinki]; RX PubMed=19805152; DOI=10.1073/pnas.0908876106; RA Kankainen M., Paulin L., Tynkkynen S., von Ossowski I., Reunanen J., RA Partanen P., Satokari R., Vesterlund S., Hendrickx A.P., Lebeer S., RA De Keersmaecker S.C., Vanderleyden J., Hamalainen T., Laukkanen S., RA Salovuori N., Ritari J., Alatalo E., Korpela R., Mattila-Sandholm T., RA Lassig A., Hatakka K., Kinnunen K.T., Karjalainen H., Saxelin M., RA Laakso K., Surakka A., Palva A., Salusjarvi T., Auvinen P., RA de Vos W.M.; RT "Comparative genomic analysis of Lactobacillus rhamnosus GG reveals RT pili containing a human- mucus binding protein."; RL Proc. Natl. Acad. Sci. U.S.A. 106:17193-17198(2009). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 53103; RX PubMed=24116025; RA Toh H., Oshima K., Nakano A., Takahata M., Murakami M., Takaki T., RA Nishiyama H., Igimi S., Hattori M., Morita H.; RT "Genomic Adaptation of the Lactobacillus casei Group."; RL PLoS ONE 8:e75073-e75073(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011548; BAI40884.1; -; Genomic_DNA. DR EMBL; FM179322; CAR86264.1; -; Genomic_DNA. DR RefSeq; YP_003170115.1; NC_013198.1. DR RefSeq; YP_005864849.1; NC_017482.1. DR ProteinModelPortal; C7T9H1; -. DR STRING; 568703.LGG_00369; -. DR EnsemblBacteria; BAI40884; BAI40884; LRHM_0357. DR EnsemblBacteria; CAR86264; CAR86264; LGG_00369. DR GeneID; 12473435; -. DR GeneID; 8423028; -. DR KEGG; lrg:LRHM_0357; -. DR KEGG; lrh:LGG_00369; -. DR PATRIC; 22262064; VBILacRha2892_0356. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LRHA568703:GCGS-360-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21870 MW; E9A42A449639D338 CRC64; MNAEALQLYL VTNRYADSPE VFLAKIAAAC ENGVTMVQLR EKSLTTRDYY ALAKQVKLIT DRYRIPLIID DRVDVCLAVD AAGVHIGDDE LPVAVTRQLL GPDKILGVST KTVATATAAV TAGADYLGVG AIFPTQTKAA APLTSLATLK AITAAVSVPI VAIGGIKADN LDTFKATGIA GVAIVSEIMQ ASDTAQKVQT LSAKLKEVL // ID C7TG64_LACRL Unreviewed; 209 AA. AC C7TG64; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LC705_00359; OS Lactobacillus rhamnosus (strain Lc 705). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=568704; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lc 705; RX PubMed=19805152; DOI=10.1073/pnas.0908876106; RA Kankainen M., Paulin L., Tynkkynen S., von Ossowski I., Reunanen J., RA Partanen P., Satokari R., Vesterlund S., Hendrickx A.P., Lebeer S., RA De Keersmaecker S.C., Vanderleyden J., Hamalainen T., Laukkanen S., RA Salovuori N., Ritari J., Alatalo E., Korpela R., Mattila-Sandholm T., RA Lassig A., Hatakka K., Kinnunen K.T., Karjalainen H., Saxelin M., RA Laakso K., Surakka A., Palva A., Salusjarvi T., Auvinen P., RA de Vos W.M.; RT "Comparative genomic analysis of Lactobacillus rhamnosus GG reveals RT pili containing a human- mucus binding protein."; RL Proc. Natl. Acad. Sci. U.S.A. 106:17193-17198(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM179323; CAR89198.1; -; Genomic_DNA. DR RefSeq; YP_003173049.1; NC_013199.1. DR ProteinModelPortal; C7TG64; -. DR STRING; 568704.LC705_00359; -. DR EnsemblBacteria; CAR89198; CAR89198; LC705_00359. DR GeneID; 8431567; -. DR KEGG; lrl:LC705_00359; -. DR PATRIC; 22267751; VBILacRha58455_0332. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LRHA568704:GHIC-2691-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21826 MW; DB2D7C7B82C165F7 CRC64; MNAEALQLYL VTNRYADSPE VFLAKIAAAC ENGVTMVQLR EKSLTTRDYY ALAKQVKLIT DRYRIPLIID DRVDVCLAVD AAGVHIGDDE LPVAVTRQLL GSDKILGVST KTVATATAAV AAGADYLGVG AIFPTQTKAA APLTSLATLK AITAAVSVPV VAIGGIKADN LDTFKATGIA GVAIVSEIMQ APDTAQKVQT LSAKLKEVL // ID C7U8V1_ENTFL Unreviewed; 211 AA. AC C7U8V1; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFCG_01332; OS Enterococcus faecalis T3. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565638; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T3; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain T3."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG670369; EEU24343.1; -; Genomic_DNA. DR ProteinModelPortal; C7U8V1; -. DR EnsemblBacteria; EEU24343; EEU24343; EFCG_01332. DR PATRIC; 26748681; VBIEntFae71198_1435. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22866 MW; A6E43F880C487223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID C7UAP3_ENTFL Unreviewed; 211 AA. AC C7UAP3; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFDG_01794; OS Enterococcus faecalis ATCC 4200. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565642; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 4200; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain ATCC 4200."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG670372; EEU15427.1; -; Genomic_DNA. DR ProteinModelPortal; C7UAP3; -. DR EnsemblBacteria; EEU15427; EEU15427; EFDG_01794. DR PATRIC; 29314379; VBIEntFae66666_0059. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22866 MW; A6E43F880C487223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID C7UR99_ENTFL Unreviewed; 211 AA. AC C7UR99; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFOG_00056; OS Enterococcus faecalis X98. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565641; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=X98; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain X98 (ATCC RT 27276)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG688434; EEU93398.1; -; Genomic_DNA. DR ProteinModelPortal; C7UR99; -. DR EnsemblBacteria; EEU93398; EEU93398; EFOG_00056. DR PATRIC; 26774989; VBIEntFae133278_1890. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID C7UXU8_ENTFL Unreviewed; 211 AA. AC C7UXU8; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFLG_01331; OS Enterococcus faecalis D6. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565650; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D6; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain D6."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG688629; EEU83072.1; -; Genomic_DNA. DR ProteinModelPortal; C7UXU8; -. DR EnsemblBacteria; EEU83072; EEU83072; EFLG_01331. DR PATRIC; 28679496; VBIEntFae1771_1738. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22881 MW; E4C24F8F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID C7V4C4_ENTFL Unreviewed; 211 AA. AC C7V4C4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFMG_01275; OS Enterococcus faecalis T11. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565640; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T11; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain T11."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG688647; EEU91950.1; -; Genomic_DNA. DR ProteinModelPortal; C7V4C4; -. DR EnsemblBacteria; EEU91950; EEU91950; EFMG_01275. DR PATRIC; 26737147; VBIEntFae41231_1922. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID C7VED0_ENTFL Unreviewed; 211 AA. AC C7VED0; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFNG_02879; OS Enterococcus faecalis CH188. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565644; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CH188; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain CH188."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG688667; EEU86344.1; -; Genomic_DNA. DR ProteinModelPortal; C7VED0; -. DR EnsemblBacteria; EEU86344; EEU86344; EFNG_02879. DR PATRIC; 29325345; VBIEntFae125333_2624. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID C7VJT9_ENTFL Unreviewed; 211 AA. AC C7VJT9; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFHG_01344; OS Enterococcus faecalis HIP11704. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565646; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIP11704; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain HIP11704."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG692646; EEU71006.1; -; Genomic_DNA. DR ProteinModelPortal; C7VJT9; -. DR EnsemblBacteria; EEU71006; EEU71006; EFHG_01344. DR PATRIC; 28706638; VBIEntFae81270_0956. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22866 MW; A6E43F880C487223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID C7VT49_ENTFL Unreviewed; 211 AA. AC C7VT49; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFKG_00055; OS Enterococcus faecalis Fly1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565649; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Fly1; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain Fly1."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG692670; EEU79592.1; -; Genomic_DNA. DR ProteinModelPortal; C7VT49; -. DR EnsemblBacteria; EEU79592; EEU79592; EFKG_00055. DR PATRIC; 28694984; VBIEntFae41172_2250. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22881 MW; E4C24F8F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID C7W452_ENTFL Unreviewed; 211 AA. AC C7W452; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFJG_00108; OS Enterococcus faecalis E1Sol. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565647; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E1Sol; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain E1Sol."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG692683; EEU76996.1; -; Genomic_DNA. DR ProteinModelPortal; C7W452; -. DR EnsemblBacteria; EEU76996; EEU76996; EFJG_00108. DR PATRIC; 28689761; VBIEntFae35263_2317. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22895 MW; A6E420980C487223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID C7W9B6_ENTFL Unreviewed; 211 AA. AC C7W9B6; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFIG_01203; OS Enterococcus faecalis JH1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565648; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JH1; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain JH1."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG692706; EEU75270.1; -; Genomic_DNA. DR ProteinModelPortal; C7W9B6; -. DR EnsemblBacteria; EEU75270; EEU75270; EFIG_01203. DR PATRIC; 28715055; VBIEntFae89018_2251. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22936 MW; A6E424940A930223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTRVAGV SLVSEIMLAE QIAEKVQGLM RVTERMLEAR K // ID C7WHX1_ENTFL Unreviewed; 211 AA. AC C7WHX1; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFEG_02352; OS Enterococcus faecalis DS5. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565643; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DS5; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain DS5 (ATCC RT 14508)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG692881; EEU65129.1; -; Genomic_DNA. DR ProteinModelPortal; C7WHX1; -. DR EnsemblBacteria; EEU65129; EEU65129; EFEG_02352. DR PATRIC; 28684052; VBIEntFae104780_1541. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID C7WRK4_ENTFL Unreviewed; 211 AA. AC C7WRK4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFFG_01886; OS Enterococcus faecalis ARO1/DG. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565651; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AR01/DG; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain AR01/DG."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG692906; EEU88732.1; -; Genomic_DNA. DR ProteinModelPortal; C7WRK4; -. DR EnsemblBacteria; EEU88732; EEU88732; EFFG_01886. DR PATRIC; 29307165; VBIEntFae91541_0979. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID C7WZ76_ENTFL Unreviewed; 211 AA. AC C7WZ76; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFGG_00057; OS Enterococcus faecalis Merz96. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565645; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Merz96; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain Merz96."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG692929; EEU68107.1; -; Genomic_DNA. DR ProteinModelPortal; C7WZ76; -. DR EnsemblBacteria; EEU68107; EEU68107; EFGG_00057. DR PATRIC; 28718592; VBIEntFae79688_1699. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22881 MW; E4C24F8F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID C7X813_9PORP Unreviewed; 242 AA. AC C7X813; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0619_01780; OS Parabacteroides sp. D13. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=563193; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D13; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., RA White A., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Parabacteroides sp. strain D13."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG698739; EEU52221.1; -; Genomic_DNA. DR ProteinModelPortal; C7X813; -. DR EnsemblBacteria; EEU52221; EEU52221; HMPREF0619_01780. DR PATRIC; 25881285; VBIParSp13980_1793. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 163 165 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 HMP-PP (By similarity). FT BINDING 199 199 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 242 AA; 26685 MW; 2093ED69D551878D CRC64; MALNYYFGYD ENGRVGRRTT GLRPPFGGNN RLMFITHRTP KYTECDEVSM AIQGGCSWIQ LRMKDGIYED TVRTCATICA EECERIVDFC VNDDLEAAVT CGATACHLGK NDMPLDIAWE VLRDKLDSNA IFYIGATANT FEDIRLAVER GASYIGLGPY RFTGTKKNLS PILGLDGYRK IIAQCKEAGI DIPIFAIGGI TLEDVGPLME TGITGIAVSG AIINAPDPVE ETRRFIEEIN KY // ID C7X814_9PORP Unreviewed; 198 AA. AC C7X814; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0619_01781; OS Parabacteroides sp. D13. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=563193; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D13; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., RA White A., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Parabacteroides sp. strain D13."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG698739; EEU52222.1; -; Genomic_DNA. DR ProteinModelPortal; C7X814; -. DR EnsemblBacteria; EEU52222; EEU52222; HMPREF0619_01781. DR PATRIC; 25881287; VBIParSp13980_1794. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 198 AA; 22277 MW; 4A9D07FD76F71120 CRC64; MNKLVVITTP YFFADEASLI ELLFAEGMSR LHLRKPDCKR DELEGLLDKI SPAYYDRIVL HDWFTLAEER ALGGIHLNKR NPEAPPLYKG SISRSCHSLE EIIEYKPVCD YVFLSPIFQS ISKERYGSGF SLDGLRNAKG IIDDKVIALG GICPRTITKL KDIPFGGVAV LGALWGNDPS LLVADQLIKQ FKRLQVWP // ID C7XR38_FUSNV Unreviewed; 206 AA. AC C7XR38; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 23. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF0946_01334; OS Fusobacterium nucleatum subsp. vincentii 3_1_36A2. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469604; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_36A2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., White A., RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 3_1_36A2."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003700; EEU33261.1; -; Genomic_DNA. DR RefSeq; YP_008477633.1; NC_022196.1. DR ProteinModelPortal; C7XR38; -. DR EnsemblBacteria; EEU33261; EEU33261; HMPREF0946_01334. DR GeneID; 16728598; -. DR KEGG; fnc:HMPREF0946_01334; -. DR PATRIC; 30289733; VBIFusSp42159_0743. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 23963 MW; F18FB307DB1F8FDC CRC64; MIENKIKLNI ISNRKLCENE NLEKQIEKIF SAYQRKIILE NFEIIALTLR EKDLYKNEYL KLVEKIYPIC QKYRIDLILH QNYDLILEDK YNIEGIHLSY NTFKSLNKNI RKELIKKYKK IGVSIHSIDE AKEAENLGAT YIVAGHIFKT DCKKDLEPRG LEFIQELSSA LIIPIFAIGG INQENSHLVI NNGAFGVCMM SSLMKH // ID C7XR44_FUSNV Unreviewed; 206 AA. AC C7XR44; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0946_01340; OS Fusobacterium nucleatum subsp. vincentii 3_1_36A2. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469604; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_36A2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., White A., RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 3_1_36A2."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003700; EEU33267.1; -; Genomic_DNA. DR RefSeq; YP_008477639.1; NC_022196.1. DR ProteinModelPortal; C7XR44; -. DR EnsemblBacteria; EEU33267; EEU33267; HMPREF0946_01340. DR GeneID; 16728604; -. DR KEGG; fnc:HMPREF0946_01340; -. DR PATRIC; 30289745; VBIFusSp42159_0749. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22696 MW; D3CBB3962FD01E46 CRC64; MKLKDCKIYL VTDEKSCNGK DFYKCIEEAI KGGVKIIQLR EKTLSTKDFF IKALKVKEIC KSYGVLFIIN DRLDITQAVE ADGVHLGQSD MPIEKAREIL KDKFLIGATA KNIEEAKKAE LLGADYIGSG AIFGTSTKDN AKKLDMEDLK KIVNSVKIPV FAIGGININN VCMLKNIGLQ GLCSVSGILS EIDCKKAVEN ILKNFN // ID C7YCM9_ENTFL Unreviewed; 211 AA. AC C7YCM9; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EFYG_02073; OS Enterococcus faecalis T8. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565639; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T8; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Gilmore M., RA Manson J., Palmer K., Carniol K., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis strain T8."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG698883; EEU26056.1; -; Genomic_DNA. DR ProteinModelPortal; C7YCM9; -. DR EnsemblBacteria; EEU26056; EEU26056; EFYG_02073. DR PATRIC; 26752436; VBIEntFae93343_1496. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 44C250957E384C82 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVAFVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQELM RVTERMLEVR K // ID C7YNJ3_NECH7 Unreviewed; 505 AA. AC C7YNJ3; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 14-MAY-2014, entry version 30. DE SubName: Full=Predicted protein; GN ORFNames=NECHADRAFT_68618; OS Nectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 / OS MPVI) (Fusarium solani subsp. pisi). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae; OC Fusarium; Fusarium solani species complex. OX NCBI_TaxID=660122; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI; RX PubMed=19714214; DOI=10.1371/journal.pgen.1000618; RA Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., RA Wasmann C.C., Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., RA Schwartz D.C., Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., RA Coutinho P.M., Nelson D.R., Straney D., Napoli C.A., Barker B.M., RA Gribskov M., Rep M., Kroken S., Molnar I., Rensing C., Kennell J.C., RA Zamora J., Farman M.L., Selker E.U., Salamov A., Shapiro H., RA Pangilinan J., Lindquist E., Lamers C., Grigoriev I.V., Geiser D.M., RA Covert S.F., Temporini E., VanEtten H.D.; RT "The genome of Nectria haematococca: contribution of supernumerary RT chromosomes to gene expansion."; RL PLoS Genet. 5:E1000618-E1000618(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG698898; EEU46577.1; -; Genomic_DNA. DR RefSeq; XP_003052290.1; XM_003052244.1. DR ProteinModelPortal; C7YNJ3; -. DR EnsemblFungi; NechaT68618; NechaP68618; NechaG68618. DR GeneID; 9672852; -. DR KEGG; nhe:NECHADRAFT_68618; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 505 AA; 51910 MW; CA75F8EA3853BFF5 CRC64; MAKPSINYGL YLVTDSTPAI LGDGNLEKIV EAALKGGVTV LQYRDKHSER AVAVETAKKL HAVSQRYSVP LLINDRVDVA VEVGCEGVHI GQDDMAFEEA RNLLRPDKII GVTASSVEEA LKACEAGADY LGLGTVYSTQ TKKDTKSIIG PSGVREILSA LAAAGHGAVP TVCIGGVNGS NAGSVLTAAR SPTKALDGVA VVSAIIAATD PAAASRDLLS QVITAKIPEV VGAVANTTPL THNMTNLVVQ NFAANVALCV GASPIMANYA EEAADLAKLG GALVVNMGTV TPEGLKNYIQ AIKAYNDAGR PIVLDPVGAG ATSVRRNAVK SLLGAGHFTV IKGNEGEIQT VAGATITQRG VDSTSSLTLA QKASLVRSIA KKRRNVVLLT GAVDLVSDGS RTLAISNGHP YLGEVTGTGC TLGTTVSAMV AAYGADPLLA AVAGTVMFEL AAEFAAERSE VRGPGTFVPA FLDELYAIRK ATGNGDLRWL TMVKVKAVEA ADIEA // ID C7ZYY2_STAAU Unreviewed; 213 AA. AC C7ZYY2; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAAG_02304; OS Staphylococcus aureus subsp. aureus 55/2053. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585143; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=55/2053; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain 55-2053."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002388; EEV03108.1; -; Genomic_DNA. DR RefSeq; YP_008449986.1; NC_022113.1. DR ProteinModelPortal; C7ZYY2; -. DR EnsemblBacteria; EEV03108; EEV03108; SAAG_02304. DR GeneID; 16643686; -. DR KEGG; saua:SAAG_02304; -. DR PATRIC; 26212170; VBIStaAur82547_2641. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8A6G9_STAAU Unreviewed; 213 AA. AC C8A6G9; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SABG_02484; OS Staphylococcus aureus subsp. aureus 65-1322. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585145; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=65-1322; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Borenstein D., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain 65-1322."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG700568; EEV05747.1; -; Genomic_DNA. DR ProteinModelPortal; C8A6G9; -. DR EnsemblBacteria; EEV05747; EEV05747; SABG_02484. DR PATRIC; 26217760; VBIStaAur75115_2639. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8ADV8_STAAU Unreviewed; 213 AA. AC C8ADV8; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACG_02228; OS Staphylococcus aureus subsp. aureus 68-397. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585146; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=68-397; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Borenstein D., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain 68-397."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG700588; EEV08409.1; -; Genomic_DNA. DR ProteinModelPortal; C8ADV8; -. DR EnsemblBacteria; EEV08409; EEV08409; SACG_02228. DR PATRIC; 26223298; VBIStaAur3727_2620. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8ALJ4_STAAU Unreviewed; 213 AA. AC C8ALJ4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SADG_02500; OS Staphylococcus aureus subsp. aureus E1410. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585153; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E1410; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Borenstein D., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain E1410."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG700611; EEV10991.1; -; Genomic_DNA. DR ProteinModelPortal; C8ALJ4; -. DR EnsemblBacteria; EEV10991; EEV10991; SADG_02500. DR PATRIC; 26077228; VBIStaAur29047_2706. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8ATZ6_STAAU Unreviewed; 213 AA. AC C8ATZ6; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAEG_02268; OS Staphylococcus aureus subsp. aureus M876. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585158; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M876; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Borenstein D., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain M876."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG700626; EEV13639.1; -; Genomic_DNA. DR ProteinModelPortal; C8ATZ6; -. DR EnsemblBacteria; EEV13639; EEV13639; SAEG_02268. DR PATRIC; 27131865; VBIStaAur79238_2625. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8JWH7_LISMN Unreviewed; 214 AA. AC C8JWH7; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMIG_01859; OS Listeria monocytogenes FSL N3-165. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393124; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL N3-165; RG The Broad Institute Genome Sequencing Platform; RA Borowsky M., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Wiedmann M., RA Swaminathan B., Lauer P., Portnoy D., Cossart P., Buchrieser C., RA Higgins D., Lander E., Galagan J., Nusbaum C., Birren B.; RT "The genome sequence of Listeria monocytogenes strain FSL N3-165."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AARQ02000010; EEW14507.1; -; Genomic_DNA. DR ProteinModelPortal; C8JWH7; -. DR EnsemblBacteria; EEW14507; EEW14507; LMIG_01859. DR PATRIC; 27513474; VBILisMon53965_1990. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22579 MW; 909B00ABC77407EE CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALKCQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAV EAERLGSVDY IGVGPIFPTI SKADAEPVSG TAILKEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GYPS // ID C8K436_LISMN Unreviewed; 214 AA. AC C8K436; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMJG_01764; OS Listeria monocytogenes FSL R2-503. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393125; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL R2-503; RG The Broad Institute Genome Sequencing Platform; RA Borowsky M., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Wiedmann M., RA Swaminathan B., Lauer P., Portnoy D., Cossart P., Buchrieser C., RA Higgins D., Lander E., Galagan J., Nusbaum C., Birren B.; RT "The genome sequence of Listeria monocytogenes strain FSL R2-503."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AARR02000009; EEW19390.1; -; Genomic_DNA. DR ProteinModelPortal; C8K436; -. DR EnsemblBacteria; EEW19390; EEW19390; LMJG_01764. DR PATRIC; 30197464; VBILisMon25358_1804. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22536 MW; 1648C735A6347B57 CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAA EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILKEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GYPS // ID C8KEN1_LISMN Unreviewed; 214 AA. AC C8KEN1; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMMG_02577; OS Listeria monocytogenes F6900. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393128; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F6900; RG The Broad Institute Genome Sequencing Platform; RA Borowsky M., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Wiedmann M., RA Swaminathan B., Lauer P., Portnoy D., Cossart P., Buchrieser C., RA Higgins D., Lander E., Galagan J., Nusbaum C., Birren B.; RT "The genome sequence of Listeria monocytogenes strain F6900."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AARU02000005; EEW23085.1; -; Genomic_DNA. DR ProteinModelPortal; C8KEN1; -. DR EnsemblBacteria; EEW23085; EEW23085; LMMG_02577. DR PATRIC; 27482942; VBILisMon69349_2430. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22392 MW; 67844F688FC140A4 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALKCQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAA EAELLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GITIPIVGIG GINETNLAEV LTAGADGVSV ISAITQSDDC HSVIKQLKNP GSPS // ID C8KT86_STAAU Unreviewed; 213 AA. AC C8KT86; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-MAR-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAD30_0470; OS Staphylococcus aureus D30. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=455227; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D30; RX PubMed=18808706; DOI=10.1186/1471-2164-9-433; RA Sivaraman K., Venkataraman N., Tsai J., Dewell S., Cole A.M.; RT "Genome sequencing and analysis reveals possible determinants of RT Staphylococcus aureus nasal carriage."; RL BMC Genomics 9:433-433(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABFB01000013; EEW47191.1; -; Genomic_DNA. DR ProteinModelPortal; C8KT86; -. DR SMR; C8KT86; 4-209. DR PRIDE; C8KT86; -. DR EnsemblBacteria; EEW47191; EEW47191; SAD30_0470. DR PATRIC; 35532770; VBIStaAur51728_1288. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8L0J4_STAAU Unreviewed; 213 AA. AC C8L0J4; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAFG_02146; OS Staphylococcus aureus A5937. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553565; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A5937; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Peleg A.Y., RA Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A5937."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A5937; RX PubMed=22492855; DOI=10.1093/infdis/jis252; RA Cameron D.R., Ward D.V., Kostoulias X., Howden B.P., RA Moellering R.C.Jr., Eliopoulos G.M., Peleg A.Y.; RT "Serine/threonine phosphatase Stp1 contributes to reduced RT susceptibility to vancomycin and virulence in Staphylococcus aureus."; RL J. Infect. Dis. 205:1677-1687(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKC01000004; EEV87124.1; -; Genomic_DNA. DR ProteinModelPortal; C8L0J4; -. DR SMR; C8L0J4; 4-209. DR PRIDE; C8L0J4; -. DR EnsemblBacteria; EEV87124; EEV87124; SAFG_02146. DR PATRIC; 29466147; VBIStaAur127832_0122. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8LFE2_STAAU Unreviewed; 213 AA. AC C8LFE2; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAGG_01745; OS Staphylococcus aureus A5948. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553567; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A5948; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Peleg A.Y., RA Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A5948."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKD01000061; EEV82001.1; -; Genomic_DNA. DR ProteinModelPortal; C8LFE2; -. DR SMR; C8LFE2; 4-209. DR PRIDE; C8LFE2; -. DR EnsemblBacteria; EEV82001; EEV82001; SAGG_01745. DR PATRIC; 29477181; VBIStaAur101774_2706. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8LMI3_STAAU Unreviewed; 213 AA. AC C8LMI3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAHG_02295; OS Staphylococcus aureus A6224. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553568; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A6224; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Peleg A.Y., RA Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A6224."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A6224; RX PubMed=22492855; DOI=10.1093/infdis/jis252; RA Cameron D.R., Ward D.V., Kostoulias X., Howden B.P., RA Moellering R.C.Jr., Eliopoulos G.M., Peleg A.Y.; RT "Serine/threonine phosphatase Stp1 contributes to reduced RT susceptibility to vancomycin and virulence in Staphylococcus aureus."; RL J. Infect. Dis. 205:1677-1687(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKE01000044; EEV79528.1; -; Genomic_DNA. DR ProteinModelPortal; C8LMI3; -. DR SMR; C8LMI3; 4-209. DR PRIDE; C8LMI3; -. DR EnsemblBacteria; EEV79528; EEV79528; SAHG_02295. DR PATRIC; 29482418; VBIStaAur3166_2489. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8LQJ1_STAAU Unreviewed; 213 AA. AC C8LQJ1; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAIG_02286; OS Staphylococcus aureus A6300. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553571; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A6300; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Peleg A.Y., RA Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A6300."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A6300; RX PubMed=22492855; DOI=10.1093/infdis/jis252; RA Cameron D.R., Ward D.V., Kostoulias X., Howden B.P., RA Moellering R.C.Jr., Eliopoulos G.M., Peleg A.Y.; RT "Serine/threonine phosphatase Stp1 contributes to reduced RT susceptibility to vancomycin and virulence in Staphylococcus aureus."; RL J. Infect. Dis. 205:1677-1687(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKF01000025; EEV78470.1; -; Genomic_DNA. DR ProteinModelPortal; C8LQJ1; -. DR SMR; C8LQJ1; 4-209. DR PRIDE; C8LQJ1; -. DR EnsemblBacteria; EEV78470; EEV78470; SAIG_02286. DR PATRIC; 29484665; VBIStaAur25053_0723. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8LW88_STAAU Unreviewed; 213 AA. AC C8LW88; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAJG_02162; OS Staphylococcus aureus A8115. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553573; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A8115; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Peleg A.Y., RA Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A8115."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKG01000001; EEV76473.1; -; Genomic_DNA. DR ProteinModelPortal; C8LW88; -. DR SMR; C8LW88; 4-209. DR PRIDE; C8LW88; -. DR EnsemblBacteria; EEV76473; EEV76473; SAJG_02162. DR PATRIC; 26167500; VBIStaAur73709_0047. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8M5B0_STAAU Unreviewed; 213 AA. AC C8M5B0; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAKG_02086; OS Staphylococcus aureus A9299. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553581; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A9299; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Peleg A.Y., RA Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A9299."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKH01000023; EEV73301.1; -; Genomic_DNA. DR ProteinModelPortal; C8M5B0; -. DR SMR; C8M5B0; 4-209. DR PRIDE; C8M5B0; -. DR EnsemblBacteria; EEV73301; EEV73301; SAKG_02086. DR PATRIC; 26174362; VBIStaAur10270_0694. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8MC21_STAAU Unreviewed; 213 AA. AC C8MC21; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SALG_01496; OS Staphylococcus aureus A9635. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553583; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A9635; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Peleg A.Y., RA Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A9635."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A9635; RX PubMed=22492855; DOI=10.1093/infdis/jis252; RA Cameron D.R., Ward D.V., Kostoulias X., Howden B.P., RA Moellering R.C.Jr., Eliopoulos G.M., Peleg A.Y.; RT "Serine/threonine phosphatase Stp1 contributes to reduced RT susceptibility to vancomycin and virulence in Staphylococcus aureus."; RL J. Infect. Dis. 205:1677-1687(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKI01000009; EEV70946.1; -; Genomic_DNA. DR ProteinModelPortal; C8MC21; -. DR EnsemblBacteria; EEV70946; EEV70946; SALG_01496. DR PATRIC; 26179414; VBIStaAur71121_0425. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23374 MW; 87C8D3399EE9DFCF CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDEVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8MPX1_STAAU Unreviewed; 213 AA. AC C8MPX1; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAMG_02236; OS Staphylococcus aureus A9719. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553588; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A9719; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Peleg A.Y., RA Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A9719."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKJ01000053; EEV66371.1; -; Genomic_DNA. DR ProteinModelPortal; C8MPX1; -. DR SMR; C8MPX1; 4-209. DR PRIDE; C8MPX1; -. DR EnsemblBacteria; EEV66371; EEV66371; SAMG_02236. DR PATRIC; 26188956; VBIStaAur45793_2375. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8MRJ8_STAAU Unreviewed; 213 AA. AC C8MRJ8; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 16-APR-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SANG_02295; OS Staphylococcus aureus A9763. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553592; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A9763; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Peleg A.Y., RA Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A9763."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKK01000004; EEV65795.1; -; Genomic_DNA. DR ProteinModelPortal; C8MRJ8; -. DR SMR; C8MRJ8; 4-209. DR PRIDE; C8MRJ8; -. DR EnsemblBacteria; EEV65795; EEV65795; SANG_02295. DR PATRIC; 26190147; VBIStaAur6666_0142. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8N0M1_STAAU Unreviewed; 213 AA. AC C8N0M1; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAOG_02179; OS Staphylococcus aureus A9781. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553596; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A9781; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Peleg A.Y., RA Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A9781."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKL01000025; EEV26162.1; -; Genomic_DNA. DR ProteinModelPortal; C8N0M1; -. DR SMR; C8N0M1; 4-209. DR PRIDE; C8N0M1; -. DR EnsemblBacteria; EEV26162; EEV26162; SAOG_02179. DR PATRIC; 26196921; VBIStaAur77373_0718. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID C8NNP9_COREF Unreviewed; 739 AA. AC C8NNP9; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.7.4.7; GN Name=thiD; ORFNames=HMPREF0290_1624; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM OS 11189 / NBRC 100395). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YS-314; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLI01000082; EEW49773.1; -; Genomic_DNA. DR RefSeq; NP_738201.1; NC_004369.1. DR ProteinModelPortal; C8NNP9; -. DR EnsemblBacteria; EEW49773; EEW49773; HMPREF0290_1624. DR GeneID; 1034064; -. DR KEGG; cef:CE1591; -. DR PATRIC; 21489321; VBICorEff9312_1583. DR eggNOG; COG0351; -. DR KO; K14153; -. DR OMA; RHELEFF; -. DR BioCyc; CEFF196164:GJW8-1618-MONOMER; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.910.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF03070; TENA_THI-4; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; SSF48613; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Transferase. SQ SEQUENCE 739 AA; 77744 MW; D6631B0553929077 CRC64; MTDFSLYLVT DPHLGGGPER VAGIVEDAIN GGVTVVQLRD KDADEQTFRE HAMELKRVCD RLGVPLFLND RFAVAAELSC HVHIGQGDLP YVQARRQLPG HLMIGLTIET MDQLETVIAD CTRAGIALPD VVGLGPVQAT DTKPDAPQAV GVDGVAAMAK VARAHGIASV AIGGVGLANA ADLARTGVDG LCVVSAIMAA PSPAEAAREL LDVWEAGRRV AQPRVLTIAG TDPTGGAGVQ ADLKSIAAAG GFGMSVITAL VAQNTHGVTG VHTPPADFLD EQLESVFSDV TVDAVKLGML GRADTVRQVT GWLRTRPHGP VILDPVMVAT SGDSLLDPDA TEALLELATV VDVITPNIPE LAVLCGEQPA PSFDAAIEQA RRFATDVGTT VIVKGGHLTG PRADNAVVYP DGSVHMVANP RVDTTNSHGT GCSLSAALAT RMGAGHPVDK ALDWATRWLN EALRGADALQ VGSGSGPVDH FAVTRRLLRA ADATPWPHLR MGAPSDGIIT PSDTQSPAPA LAPAGPYTRA LWEATGDVLG EILDSGFIRG LGDGTLSREE FLFYIDQDAH YLRQYSRALA TLSSRAPDAP AQVDWATSAA ECITVEAELH RTYLNKGLAE TGVSAPSPVT MAYTDFLIAR SHADDYVVGA AAVLPCYWLY AEIGLILAKQ NHPEHPYTDW LDTYSGEGFL AGTVKAIARV EAAMAGAGPD QQRVAAQTYL SACVHEREFF DQATRQGWN // ID C8NPP1_COREF Unreviewed; 216 AA. AC C8NPP1; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0290_1966; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM OS 11189 / NBRC 100395). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YS-314; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLI01000092; EEW49420.1; -; Genomic_DNA. DR RefSeq; NP_738543.1; NC_004369.1. DR ProteinModelPortal; C8NPP1; -. DR EnsemblBacteria; EEW49420; EEW49420; HMPREF0290_1966. DR GeneID; 1034647; -. DR KEGG; cef:CE1933; -. DR PATRIC; 21490011; VBICorEff9312_1919. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; CEFF196164:GJW8-1969-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 216 AA; 22925 MW; B64A9E583BC15659 CRC64; MRPTPDLRCY FITGHGSHEH IVDVARRAVA GGARTVQVRS KPITARELYA LTEAVALAVG ETAHVLVDDR VDIALALRHR GLPVHGVHVG QDDLPVRDVR ALLGEEAIIG LTTGTRELVE AANEHAEVLD YIGAGPFRPT PTKDSGRPPL GVEGYRELVE LSRLPVVAIG DVTADDAPAL ADTGVAGLAV VRGLMESADP TGYARRLITG FGEGRQ // ID C8P417_9LACO Unreviewed; 213 AA. AC C8P417; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0494_0061; OS Lactobacillus antri DSM 16041. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525309; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16041; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLL01000003; EEW54758.1; -; Genomic_DNA. DR ProteinModelPortal; C8P417; -. DR EnsemblBacteria; EEW54758; EEW54758; HMPREF0494_0061. DR PATRIC; 30187117; VBILacAnt9210_1737. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22320 MW; 7DE156B81C36E5CE CRC64; MLFKDEMLRC YLIGGSQDTH HDPAEFLTKV EAAMQAGITA FQYREKGTST LSKAETLALG QQVQELATKY GVPLFVDDDL ELAAAIQADG IHVGQKDQWI EEVLAAVGDQ LMVGYSCNTA AQVAHANQLA VDYIGTGPVF PTISKDDAGS ALGVDGLADF VEQSVHPVVA IGGISLDNAG ATLTSGCAGL SMISMVLGAD DVAGTVKKIL ELY // ID C8P8J8_9LACO Unreviewed; 217 AA. AC C8P8J8; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0494_1642; OS Lactobacillus antri DSM 16041. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525309; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16041; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLL01000047; EEW53212.1; -; Genomic_DNA. DR ProteinModelPortal; C8P8J8; -. DR EnsemblBacteria; EEW53212; EEW53212; HMPREF0494_1642. DR PATRIC; 30184238; VBILacAnt9210_0039. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23287 MW; 2C372878173FBBEE CRC64; MKFDPTMLRA YLVGGSQDTH HDPAELLTKT EEALQAGITA FQYREKGSSN LSADQRLKLA QQLRELTRHY QVPFFIDDDE ELALAVGADG VHVGQKDQRI EQVIQRAQGK LMIGYSCNRP AQIEKANQLA AVDYVGAGPV FPTQSKADAD PALGLKQLAL LNRLSEQPVV AIGGITADNI AATLATGVAG AAVISMVFQS DDISQTVHQM LTAGSQS // ID C8PHL5_9PROT Unreviewed; 204 AA. AC C8PHL5; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CAMGR0001_0460; OS Campylobacter gracilis RM3268. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=553220; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RM3268; RA Madupu R., Sebastian Y., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYG01000024; EEV17629.1; -; Genomic_DNA. DR ProteinModelPortal; C8PHL5; -. DR EnsemblBacteria; EEV17629; EEV17629; CAMGR0001_0460. DR PATRIC; 30467451; VBICamGra90913_1298. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22147 MW; 2240CB898ABAA301 CRC64; MSEIYALSDD TLTPPQTIFS QIDEILRCGV KLVQYRSKLA VRDEALIRSL IGLCEDYGAK LIINDDAALA KKLGAHGVHI GKDDGETAQV REFLGANKIV GVSCYADLAR AQKAEAQGAS YVAFGSLRRG KTKPDAPLCP DALVQEARKS LNLPIAVIGG ISLENLNEIL ALKPDYIAMV EAIYRPASIT QNLANLKEKM DEYI // ID C8PHZ2_9PROT Unreviewed; 455 AA. AC C8PHZ2; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=CAMGR0001_0588; OS Campylobacter gracilis RM3268. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=553220; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RM3268; RA Madupu R., Sebastian Y., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYG01000024; EEV17756.1; -; Genomic_DNA. DR EnsemblBacteria; EEV17756; EEV17756; CAMGR0001_0588. DR PATRIC; 30467707; VBICamGra90913_1425. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 455 AA; 48784 MW; 63D0B7B6EC179937 CRC64; MLDLELASRI TIITNRVLCG GEAALLARIA DFAAAGVGEI VVREKDLDEA AYAALFENIL RACEFYDRAD RLSFDADRAC PHEISPNEIR AAKFDAAEAH EEGFGTDAAR SDGIFAEEVC ARTIPHKIYD DRACVVQTLV GGLNASAVCA DKISLYERDE DEVLQKKLDL GDGKSELCAD TARKHGAATD EIRSKNSACV LDEILSENFT SAANCENDSA PGEISLRGVV CETKPAVEIA RSAANAESMQ GAQSTENVND VHSAKNAGSS QSTQYTESSE SIEGVENLQS VKEAENSQSV EGARSAESAR RPPAIFVHNF ADFALRAGER NLWLPLGVLR SFSAARGAEF LRANFKKLVA SCHSEAEARE ALELGASAIC LSHIFATDCK AGLMPKGLNL IRAVRGFYGG EIYALGGITP RNFASVLRAG ADRIAVMSSA MAARDASDFI RKFKK // ID C8PUE0_9GAMM Unreviewed; 343 AA. AC C8PUE0; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Mutator mutT protein; DE EC=3.6.1.-; GN ORFNames=ENHAE0001_1776; OS Enhydrobacter aerosaccus SK60. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Enhydrobacter. OX NCBI_TaxID=553217; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK60; RA Madupu R., Yinong S., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYI01000002; EEV24145.1; -; Genomic_DNA. DR ProteinModelPortal; C8PUE0; -. DR EnsemblBacteria; EEV24145; EEV24145; ENHAE0001_1776. DR PATRIC; 29270170; VBIEnhAer50137_0088. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 343 AA; 38225 MW; 5C694312E2C05B75 CRC64; MSKVVNVAVA VIHFNKQYLL GFRHARQHQG NRYEFVGGKI EPAETPTQGL IREVHEEIGL DIAQNTAVKM GVIRHDYADK AVALHVFKIQ VSQAQFDGLQ QGKGKEGQAV KWVHQSDLIA NQYPLPDANA RILQWLKLPR AIYITQPLDS FVSVDKWVDF YSQKLPDDAH CYLRPQTSDE NATAIIDGLL TIRADITPII QYATLACLFE CLPERLFKRL DAWLKNGMVH LNHQQLMTLD FSSLSKNYRY FASCHDQHSL SRLNALATSH TVMGCFLSPV KATPTHPETF QSGGMGWQAF GELAKLSDVP MFALGGVGQA DLATAYEHGA MGIAGIRLLV DKV // ID C8PVD1_9GAMM Unreviewed; 219 AA. AC C8PVD1; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ENHAE0001_1889; OS Enhydrobacter aerosaccus SK60. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Enhydrobacter. OX NCBI_TaxID=553217; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK60; RA Madupu R., Yinong S., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYI01000019; EEV23695.1; -; Genomic_DNA. DR ProteinModelPortal; C8PVD1; -. DR EnsemblBacteria; EEV23695; EEV23695; ENHAE0001_1889. DR PATRIC; 29270855; VBIEnhAer50137_0414. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23529 MW; 4B23F1CC4AAEF1C7 CRC64; MMHNRADYRL YLVTDRNCLQ QQTLEQAVEQ AILGGVTLVQ LREKAIASKA FYERALRIKA ICHRYNVPLL INDRVDIALA VEADGVHIGQ SDLPCGVVRQ ILGKDKIIGV SARTAQQAIQ AQADGADYLG VGAMFATSTK QDAQTVTIAS LTQIRQAVTL PIVAIGGINH TTLPALQQAL QAADTSMGDV IDGVAVVSAI LGQKDVKLAS EQLKEMIKT // ID C8RR25_CORJE Unreviewed; 218 AA. AC C8RR25; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0297_0477; OS Corynebacterium jeikeium ATCC 43734. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=525262; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43734; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYW01000021; EEW17151.1; -; Genomic_DNA. DR ProteinModelPortal; C8RR25; -. DR EnsemblBacteria; EEW17151; EEW17151; HMPREF0297_0477. DR PATRIC; 25292073; VBICorJei17536_1476. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). SQ SEQUENCE 218 AA; 22597 MW; 891B856F0D89A6E9 CRC64; MSASLDLRCY LVTGAPHEKV VDVAAAAAAG GAGVVQVRSK PISVRDLTAL AVEVAAAVQK ANPATRVLID DRVDVAAALM PEHNIHGVHI GQDDLDPRLA RQLLGKDAII GLTTGTLPLV QQANEYADVI DYIGAGPFRP TPTKDSGREP LGLEGYPALV EASRVPVVAI GDVHAEDAAD LAATGVAGLA IVRGIMQAEN PKAYAESVVS QFSEANER // ID C8RW30_9RHOB Unreviewed; 206 AA. AC C8RW30; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 18. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Rsw2DRAFT_0008; OS Rhodobacter sp. SW2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=371731; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SW2; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Emerson D.; RT "The draft genome of Rhodobacter sp. SW2."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYY01000001; EEW26773.1; -; Genomic_DNA. DR ProteinModelPortal; C8RW30; -. DR EnsemblBacteria; EEW26773; EEW26773; Rsw2DRAFT_0008. DR PATRIC; 28436638; VBIRhoSp55960_0008. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 21909 MW; D58538C89B2D0E29 CRC64; MPETERPQIY LVTPPAFDLE VFPDRLAAVL DGAEVACVRL ALASADEDRV ARAADALRQV THARDVALVI ERHVLLVERL GLDGVHLTDG ARSIRKVRKD LGADAIIGAF CGTTRHDGIS AAEAGADYVA FGPVGATPLG DGSLAEHELF EWWSEMIEVP VVAEGALTAE LVASLGPVTD FFGLGEEIWR HDDALAALRA LLAPLG // ID C8T8E3_KLEPR Unreviewed; 211 AA. AC C8T8E3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0484_3889; OS Klebsiella pneumoniae subsp. rhinoscleromatis ATCC 13884. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=667127; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 13884; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZD01000182; EEW40059.1; -; Genomic_DNA. DR ProteinModelPortal; C8T8E3; -. DR EnsemblBacteria; EEW40059; EEW40059; HMPREF0484_3889. DR PATRIC; 35972868; VBIKlePne146004_5012. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23014 MW; 21B54D09F38D3CB0 CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIERLLE AGVRTLQLRI KDRRDSEVED DVIAAIALGR RYHARLFIND YWQLAIKHQA YGVHLGQEDL ETTDLSAIRQ AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIQRLADYP TVAIGGISLE KAPGVLATGV GSIAVVSAIT QAADWRAATN QLLALAGAGD E // ID C8TMN3_ECO26 Unreviewed; 211 AA. AC C8TMN3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECO26_5102; OS Escherichia coli O26:H11 (strain 11368 / EHEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=573235; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=11368 / EHEC; RX PubMed=19815525; DOI=10.1073/pnas.0903585106; RA Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., RA Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., RA Hayashi T.; RT "Comparative genomics reveal the mechanism of the parallel evolution RT of O157 and non-O157 enterohemorrhagic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010953; BAI28254.1; -; Genomic_DNA. DR RefSeq; YP_003231994.1; NC_013361.1. DR ProteinModelPortal; C8TMN3; -. DR SMR; C8TMN3; 10-208. DR STRING; 573235.ECO26_5102; -. DR EnsemblBacteria; BAI28254; BAI28254; ECO26_5102. DR GeneID; 8482729; -. DR KEGG; eoj:ECO26_5102; -. DR PATRIC; 18406168; VBIEscCol24965_5257. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL573235:GCY7-5283-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID C8TZS5_ECO10 Unreviewed; 211 AA. AC C8TZS5; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECO103_4742; OS Escherichia coli O103:H2 (strain 12009 / EHEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585395; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12009 / EHEC; RX PubMed=19815525; DOI=10.1073/pnas.0903585106; RA Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., RA Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., RA Hayashi T.; RT "Comparative genomics reveal the mechanism of the parallel evolution RT of O157 and non-O157 enterohemorrhagic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010958; BAI33437.1; -; Genomic_DNA. DR RefSeq; YP_003224571.1; NC_013353.1. DR ProteinModelPortal; C8TZS5; -. DR SMR; C8TZS5; 10-208. DR STRING; 585395.ECO103_4742; -. DR EnsemblBacteria; BAI33437; BAI33437; ECO103_4742. DR GeneID; 8476917; -. DR KEGG; eoh:ECO103_4742; -. DR PATRIC; 32101694; VBIEscCol146794_4969. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL585395:GJA9-4921-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID C8UKP5_ECO1A Unreviewed; 211 AA. AC C8UKP5; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECO111_4810; OS Escherichia coli O111:H- (strain 11128 / EHEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585396; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=11128 / EHEC; RX PubMed=19815525; DOI=10.1073/pnas.0903585106; RA Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., RA Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., RA Hayashi T.; RT "Comparative genomics reveal the mechanism of the parallel evolution RT of O157 and non-O157 enterohemorrhagic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010960; BAI38555.1; -; Genomic_DNA. DR RefSeq; YP_003237106.1; NC_013364.1. DR ProteinModelPortal; C8UKP5; -. DR SMR; C8UKP5; 10-208. DR STRING; 585396.ECO111_4810; -. DR EnsemblBacteria; BAI38555; BAI38555; ECO111_4810. DR GeneID; 8488185; -. DR KEGG; eoi:ECO111_4810; -. DR PATRIC; 32113226; VBIEscCol143187_4991. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL585396:GJCW-4995-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID C8V6D0_EMENI Unreviewed; 519 AA. AC C8V6D0; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 16-APR-2014, entry version 28. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative (AFU_orthologue AFUA_2G08970); GN ORFNames=ANIA_10472; OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL OS 194 / M139) (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=227321; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=16372000; DOI=10.1038/nature04341; RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., RA Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., RA Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., RA Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., RA Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., RA Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., RA Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., RA Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., RA Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.; RT "Sequencing of Aspergillus nidulans and comparative analysis with A. RT fumigatus and A. oryzae."; RL Nature 438:1105-1115(2005). RN [2] RP GENOME REANNOTATION. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003; RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., RA von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., RA Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G., RA de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., RA Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., RA Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., RA Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., RA Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., RA Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., RA Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., RA Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., RA van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., RA Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., RA de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., RA Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.; RT "The 2008 update of the Aspergillus nidulans genome annotation: a RT community effort."; RL Fungal Genet. Biol. 46:S2-13(2009). CC -!- MISCELLANEOUS: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ third party annotation (TPA) entry. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BN001302; CBF75182.1; -; Genomic_DNA. DR ProteinModelPortal; C8V6D0; -. DR EnsemblFungi; CADANIAT00004823; CADANIAP00004823; CADANIAG00004823. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 519 AA; 54646 MW; 455850C97796C12F CRC64; MKLDLSVYLV TDSTPPILKG RDLCAVVEEA VKGGVTVVQY RDKKSDTGAQ IETARKLHRI TQAHGVPLII NDRVDVALAV GAEGVHLGQD DMVISEAKKL LPENAIIGIS ASSIEEAQAA VAAGADYLGI GTLFATPTKT NTKHIIGTAG TQAILDSIAE SGRDVGTVCI GGINLSNVQR VLYQSASPRK SLNGAAIVSA IMAADDPRAA AAELARAIAT PPPFVRKADG PLVRNVAGLL EKVPHIVQKM VEIHPLVHNM INFVVANFVA NVTLAIGASP IMSPYGDEAT DLCQFDGALL INMGTLTSQS PSEYLKAIRA YNQRGNPVVY DPVGAGATQI RRGVVKELMA GGYFDLIKGN EGEIRQVAGS TSVQQRGVDS GPSTLDHQGK ARLARDLARR EKNIVLLTGA VDYLSDGERI VAVENGHELL GQVTGTGCAV GTVAGCFIAA NPTDKFLAVL SALLMYEIAA ENAAARDSVR GPGSFATTFI DELYAIRQAS LQGDHSWYAG RARVQEISL // ID C8VWW4_DESAS Unreviewed; 218 AA. AC C8VWW4; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dtox_1683; OS Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM OS B-1644). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=485916; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644; RX PubMed=21304664; DOI=10.4056/sigs.39508; RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L., RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., RA Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E., RA Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.; RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain RT (5575)."; RL Stand. Genomic Sci. 1:242-253(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001720; ACV62540.1; -; Genomic_DNA. DR RefSeq; YP_003191163.1; NC_013216.1. DR ProteinModelPortal; C8VWW4; -. DR STRING; 485916.Dtox_1683; -. DR EnsemblBacteria; ACV62540; ACV62540; Dtox_1683. DR GeneID; 8428649; -. DR KEGG; dae:Dtox_1683; -. DR PATRIC; 21720161; VBIDesAce42372_1705. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DACE485916:GHUF-1730-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23923 MW; 3AABC2D889228C8F CRC64; MVSRRGLAEL LQTDIYGITA EEYSLGRSNL EVVSMMIDSG IKLIQYREKE KKTREKYEEC LKIREMTRQV GVAFIVNDHV DLALLVDADG VHLGQDDLPP EQVRQLVGEQ MLIGLSTHCP EQADAAVKAG VDYIGVGPIF ATRTKKDVCD PVGLEYLEYV ADNIRLPFVA IGGIKEHNLA EVSSRGARCV ALVTEIVGAG DIRGKVSALK AILSRKEV // ID C8WCL1_ZYMMN Unreviewed; 238 AA. AC C8WCL1; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Za10_0901; OS Zymomonas mobilis subsp. mobilis (strain NCIB 11163). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=622759; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIB 11163; RX PubMed=19767433; DOI=10.1128/JB.01084-09; RA Kouvelis V.N., Saunders E., Brettin T.S., Bruce D., Detter C., Han C., RA Typas M.A., Pappas K.M.; RT "Complete genome sequence of the ethanol producer Zymomonas mobilis RT NCIMB 11163."; RL J. Bacteriol. 191:7140-7141(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001722; ACV75447.1; -; Genomic_DNA. DR RefSeq; YP_003226031.1; NC_013355.1. DR ProteinModelPortal; C8WCL1; -. DR STRING; 622759.Za10_0901; -. DR EnsemblBacteria; ACV75447; ACV75447; Za10_0901. DR GeneID; 8472005; -. DR KEGG; zmn:Za10_0901; -. DR PATRIC; 24154928; VBIZymMob135463_0985. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ZMOB622759:GI1C-1025-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 158 160 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 161 161 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 238 AA; 25658 MW; B0EC3B7DBA103D9D CRC64; MAENEILTDN DEALDAFTNN YQRPSENPCG LYLISPPEID EHFVERLKKA FDGGDVSAFQ LRLKGLNEHA IARLAEPLQK VCADRDVAFI VNDSVSLAKR LGADGVHLGQ GDGDADEARV ILGPSAQIGV TCHNSRHLAM IAGEKGADYV AFGAFYPTTS KDVRYYARPE ILSWWATLFE LPSVAIGGIT TENVAPIVKA GADFVAVCAG IWKAKEGEDK AVAHFNTVLD QAVKGEIA // ID C8WF11_ZYMMN Unreviewed; 196 AA. AC C8WF11; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 27. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Za10_1763; OS Zymomonas mobilis subsp. mobilis (strain NCIB 11163). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=622759; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIB 11163; RX PubMed=19767433; DOI=10.1128/JB.01084-09; RA Kouvelis V.N., Saunders E., Brettin T.S., Bruce D., Detter C., Han C., RA Typas M.A., Pappas K.M.; RT "Complete genome sequence of the ethanol producer Zymomonas mobilis RT NCIMB 11163."; RL J. Bacteriol. 191:7140-7141(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001722; ACV76297.1; -; Genomic_DNA. DR RefSeq; YP_003226881.1; NC_013355.1. DR ProteinModelPortal; C8WF11; -. DR STRING; 622759.Za10_1763; -. DR EnsemblBacteria; ACV76297; ACV76297; Za10_1763. DR GeneID; 8472899; -. DR KEGG; zmn:Za10_1763; -. DR PATRIC; 24156906; VBIZymMob135463_1943. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG679THR; -. DR BioCyc; ZMOB622759:GI1C-1919-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 196 AA; 22838 MW; 8EB5AF86F9FE10EE CRC64; MNDKLKNTWP RLWLMTDERF GDGLLEAIKK LPQGSGIVFR HYRLPFKIRK NLFQKIQRIA KKQKLVLFLA GSARLAAAWK ADGVHGRFSS QRTARPLLRS QAVHNRRDSI MCRKVDFVFL SPLFSTRSHP GKPFLGRVKF LQLKRSIRQK VFALGGINAK TIRALPACDG FSGIDIWQDD QFRHHRLWSF WANQQR // ID C8WHW9_EGGLE Unreviewed; 211 AA. AC C8WHW9; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 13-NOV-2013, entry version 26. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Elen_1745; OS Eggerthella lenta (strain ATCC 25559 / DSM 2243 / JCM 9979 / NCTC OS 11813 / VPI 0255) (Eubacterium lentum). OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Eggerthella. OX NCBI_TaxID=479437; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25559 / DSM 2243 / JCM 9979 / NCTC 11813 / VPI 0255; RX PubMed=21304654; DOI=10.4056/sigs.33592; RA Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T., RA Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., RA Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., RA Detter J.C., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.; RT "Complete genome sequence of Eggerthella lenta type strain (IPP VPI RT 0255)."; RL Stand. Genomic Sci. 1:174-182(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001726; ACV55710.1; -; Genomic_DNA. DR RefSeq; YP_003182099.1; NC_013204.1. DR ProteinModelPortal; C8WHW9; -. DR STRING; 479437.Elen_1745; -. DR EnsemblBacteria; ACV55710; ACV55710; Elen_1745. DR GeneID; 8416044; -. DR KEGG; ele:Elen_1745; -. DR PATRIC; 21844191; VBIEggLen106823_1801. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ELEN479437:GHWY-1769-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 211 AA; 22392 MW; 15574E913FA607CC CRC64; MFACEPSAAA PTFRRVFVTD RLGCALPLPQ QTAFLAESGA IDAVILREKD LDDAAYELLA AEMAAVCARC GIAFVAHAHV EAARRLGCAA VHLPLPLLRA QGRPDGFAWV GTNVHEADEV AEAEVLGADV LVASPVFAPS CKPASTARGL PFLRAVLDRA HAPVFALGGI TDENERLIRE AGTAGACRMA DYARRRGVRQ AAPCKYERSR G // ID C8WIY4_EGGLE Unreviewed; 216 AA. AC C8WIY4; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Elen_2062; OS Eggerthella lenta (strain ATCC 25559 / DSM 2243 / JCM 9979 / NCTC OS 11813 / VPI 0255) (Eubacterium lentum). OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Eggerthella. OX NCBI_TaxID=479437; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25559 / DSM 2243 / JCM 9979 / NCTC 11813 / VPI 0255; RX PubMed=21304654; DOI=10.4056/sigs.33592; RA Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T., RA Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., RA Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., RA Detter J.C., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.; RT "Complete genome sequence of Eggerthella lenta type strain (IPP VPI RT 0255)."; RL Stand. Genomic Sci. 1:174-182(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001726; ACV56025.1; -; Genomic_DNA. DR RefSeq; YP_003182414.1; NC_013204.1. DR ProteinModelPortal; C8WIY4; -. DR STRING; 479437.Elen_2062; -. DR EnsemblBacteria; ACV56025; ACV56025; Elen_2062. DR GeneID; 8416378; -. DR KEGG; ele:Elen_2062; -. DR PATRIC; 21844869; VBIEggLen106823_2125. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ELEN479437:GHWY-2103-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22146 MW; A0FA3CEEF4636A5A CRC64; MYPRENLRRA MALYAVTDRA WLGERTLSAC VEEALAGGAT FVQLREKDAP RAEVVLRARA LAPLCREAGV PFVVNDDVEA ARIAGADGVH VGQDDAACVE AREKLGPDAI VGVSVQTVEQ ALVAQADGAD YLGVGAVFGT PTKPDAADVG TDGLAAICAA VDIPVVAIGG LNERTIPELA GTGADGAAVV SAIFAAEDIE EETRRLRAAV QAALGA // ID C8WSK5_ALIAD Unreviewed; 230 AA. AC C8WSK5; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Aaci_2484; OS Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC OS 27009 / DSM 446 / 104-1A) (Bacillus acidocaldarius). OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=521098; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27009 / DSM 446 / 104-1A; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Chertkov O., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Klenk H.-P., RA Eisen J.A.; RT "The complete chromosome of Alicyclobacillus acidocaldarius subsp. RT acidocaldarius DSM 446."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001727; ACV59490.1; -; Genomic_DNA. DR RefSeq; YP_003185879.1; NC_013205.1. DR ProteinModelPortal; C8WSK5; -. DR STRING; 521098.Aaci_2484; -. DR EnsemblBacteria; ACV59490; ACV59490; Aaci_2484. DR GeneID; 8426013; -. DR KEGG; aac:Aaci_2484; -. DR PATRIC; 20848466; VBIAliAci73240_2456. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CVGPVHA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AACI521098:GCIO-2555-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 23481 MW; FDD9EF96DED54183 CRC64; MTHVLHVLSD RARGAKVPLK DALWLAALGG ADVIQVREKK APALAVFEFA CALLARIREA GSSARVLVND RLDVAMAARA DGVHLAAKSL PVAAAREVVQ RAGGGLVLGC SVHSLEEAQA AEAAGADYVT FGHIFPTASH PGLPPKGVRE LARVVEAVSI PVVAIGGIDA GNVTEVLATG ASGVAVIGAV VEAADPRAAA ARLKEAMARS PVAPKVPFPT PEGGMRRARL // ID C8WXY4_ALIAD Unreviewed; 212 AA. AC C8WXY4; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Aaci_1934; OS Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC OS 27009 / DSM 446 / 104-1A) (Bacillus acidocaldarius). OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=521098; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27009 / DSM 446 / 104-1A; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Chertkov O., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Klenk H.-P., RA Eisen J.A.; RT "The complete chromosome of Alicyclobacillus acidocaldarius subsp. RT acidocaldarius DSM 446."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001727; ACV58946.1; -; Genomic_DNA. DR RefSeq; YP_003185335.1; NC_013205.1. DR ProteinModelPortal; C8WXY4; -. DR STRING; 521098.Aaci_1934; -. DR EnsemblBacteria; ACV58946; ACV58946; Aaci_1934. DR GeneID; 8425455; -. DR KEGG; aac:Aaci_1934; -. DR PATRIC; 20847312; VBIAliAci73240_1886. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AACI521098:GCIO-1997-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22245 MW; 0C46D1A241386B85 CRC64; MRGMTRRDWT DKLRVYLVTD DRPDHEEVVA IVEQALAGGV TCVQLRRKQE DGGPMLKLAV RLRELASAHG ALFIVNDRLD IALLSDADGV HVGQTDLPAS LVKSRFPELV VGVSARSVDE AVRAEQDGAD YLGVGSVYPT ATKGDAVLTG LDVLAACRRA VRIPIVGIGG ITVDRAPEVM AAGANGVAVV SAIMSAPDPK AAAAALAQRT SL // ID C8X0S5_DESRD Unreviewed; 216 AA. AC C8X0S5; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dret_0730; OS Desulfohalobium retbaense (strain DSM 5692). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfohalobiaceae; Desulfohalobium. OX NCBI_TaxID=485915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5692; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C., Han C., RA Tapia R., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Desulfohalobium retbaense DSM 5692."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001734; ACV68022.1; -; Genomic_DNA. DR RefSeq; YP_003197600.1; NC_013223.1. DR ProteinModelPortal; C8X0S5; -. DR STRING; 485915.Dret_0730; -. DR EnsemblBacteria; ACV68022; ACV68022; Dret_0730. DR GeneID; 8418543; -. DR KEGG; drt:Dret_0730; -. DR PATRIC; 21698378; VBIDesRet71890_0781. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DRET485915:GHRJ-740-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22928 MW; AEC10F180F6A4BED CRC64; MRQRLLATDL YCLTASDLSR GRETVEVVEQ MLAAGIRLVQ YREKSKKAAA QYRECQQLRK MTRDAGAAFV VNDDVALARA VGADGVHIGQ EDLPVPVVRD LVGPDMAIGV STHGPDQALA AVADGADYIG VGPLFATQTK KDVCAPVGLA YLDWVAAHID LPFVAIGGIK EHNVAEVVRH GARCVALVTE ITQAEDIAAT IASVRQTMAA AKGQRG // ID C8X4B3_DESRD Unreviewed; 219 AA. AC C8X4B3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dret_2103; OS Desulfohalobium retbaense (strain DSM 5692). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfohalobiaceae; Desulfohalobium. OX NCBI_TaxID=485915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5692; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C., Han C., RA Tapia R., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Desulfohalobium retbaense DSM 5692."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001734; ACV69387.1; -; Genomic_DNA. DR RefSeq; YP_003198965.1; NC_013223.1. DR ProteinModelPortal; C8X4B3; -. DR STRING; 485915.Dret_2103; -. DR EnsemblBacteria; ACV69387; ACV69387; Dret_2103. DR GeneID; 8419953; -. DR KEGG; drt:Dret_2103; -. DR PATRIC; 21701322; VBIDesRet71890_2218. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DRET485915:GHRJ-2151-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23089 MW; 63E9C986CF497414 CRC64; MSLDLSLYLV TDRGSCQGRD LIEVVLQAVA GGVSVVQLRE KQTETREFVE LARALHDCLQ HRGVPLFIND RVDVALAVGA EGVHVGQEDM DPRDVRRLVG SGMYVGLSAQ TEAHMHMAKQ FPVDYIGLGP IASTPTKEDA GAPLGIAGFA RLRALVSLPV VAIGAVNAAN TSAIIHQGNA DGVAVVSALC AAADPREAAR GLYRQIVDAR SQKDGSGEK // ID C8X9W0_NAKMY Unreviewed; 221 AA. AC C8X9W0; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Namu_4886; OS Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / JCM 9543 / OS Y-104) (Microsphaera multipartita). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Nakamurellaceae; Nakamurella. OX NCBI_TaxID=479431; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700099 / DSM 44233 / JCM 9543 / Y-104; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Sims D., Meincke L., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Klenk H.-P., Eisen J.A.; RT "The complete genome of Nakamurella multipartita DSM 44233."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001737; ACV81160.1; -; Genomic_DNA. DR RefSeq; YP_003204149.1; NC_013235.1. DR ProteinModelPortal; C8X9W0; -. DR STRING; 479431.Namu_4886; -. DR EnsemblBacteria; ACV81160; ACV81160; Namu_4886. DR GeneID; 8450516; -. DR KEGG; nml:Namu_4886; -. DR PATRIC; 22667448; VBINakMul62011_4933. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CVGPVHA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NMUL479431:GHQL-4924-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23483 MW; 98AFDA786BC8AE47 CRC64; MAPVSSPHDA RPALARARLY LCTDSRARQG DLEPFLDAVL ANGVDIVQLR EKGLEARAEL RLLEVLAAAA QRHGKLWAVN DRADVALASG APILHLGQDD LPVPLARRIV GDEVLIGRST HDPAQLDAAR TEPGVDYYCA GPTWTTPTKP GRPAAGLGLL DHGVARQDAR PWFAIGGIEN AARLEEVIAR GARRAVVVRM ITEAEDPGAA ARAAADRLAA L // ID C8XC59_NAKMY Unreviewed; 228 AA. AC C8XC59; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Namu_5185; OS Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / JCM 9543 / OS Y-104) (Microsphaera multipartita). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Nakamurellaceae; Nakamurella. OX NCBI_TaxID=479431; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700099 / DSM 44233 / JCM 9543 / Y-104; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Sims D., Meincke L., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Klenk H.-P., Eisen J.A.; RT "The complete genome of Nakamurella multipartita DSM 44233."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001737; ACV81453.1; -; Genomic_DNA. DR RefSeq; YP_003204442.1; NC_013235.1. DR ProteinModelPortal; C8XC59; -. DR STRING; 479431.Namu_5185; -. DR EnsemblBacteria; ACV81453; ACV81453; Namu_5185. DR GeneID; 8450816; -. DR KEGG; nml:Namu_5185; -. DR PATRIC; 22668062; VBINakMul62011_5239. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IGISCHT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NMUL479431:GHQL-5224-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 197 198 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 22580 MW; 2CDEA5CDDC973DD8 CRC64; MAPRPLDLTL YLVTDTRLCG ATGSNGADGV AATVRAAVAG GVTAVQVRDP DAADEEFVRI GRAVAAVLAG TGVPLIVNDR VHLVARIGAD GAHVGQGDLD PVAARRILGP DKLLGLSVQT LAHAEAAAAL PAGCVDHLGV GPVWWQATKP DAADPGGLSA LSAIVRRSPV PCVAIGGIDA ERAAHVRATG AAGVAVVSAI CGQPDPAAAA RRIRDSWAAA GSSSRGAG // ID C8ZIG5_YEAS8 Unreviewed; 540 AA. AC C8ZIG5; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 16-APR-2014, entry version 24. DE SubName: Full=Thi6p; GN ORFNames=EC1118_1P2_0683g; OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) OS (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=643680; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lalvin EC1118 / Prise de mousse; RX PubMed=19805302; DOI=10.1073/pnas.0904673106; RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., RA Cambon B., Legras J.-L., Wincker P., Casaregola S., Dequin S.; RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome RT sequence of the wine yeast Saccharomyces cerevisiae EC1118."; RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN394217; CAY86746.1; -; Genomic_DNA. DR ProteinModelPortal; C8ZIG5; -. DR SMR; C8ZIG5; 3-536. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 58059 MW; F34FA1E0B76E3930 CRC64; MVFTKEEVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDIE TKNFVAEALE VQKICKKYNV PLIINDRIDV AMAIDADGVH VGQDDMPIPM VRKLLGPSKI LGWSVGKPSE VETLAKWGPD MVDYIGVGTL FPTSTKKNPK KSPMGPQGAI AILDALEEFK ATWCRTVGIG GLHPDNIQRV LCQCVASNGK RSLDGISLVS DIMAAPDACA ATKRLRGLLD ATRYQFVECE LNNTFPTTTS IQNVISQVSN NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL ARIPNASLLL NTGSVAPIEM LKAAINAYNE VNRPITFDPV GYSATETRLC LNNTLLTYGQ FACIKGNCSE ILSLAKLNNH KMKGVDSSSG KTNIDTLVRA TQIVAFQYRT VAVCTGEFDC VADGTFGGEY KLSSGTEGIT AEDLPCVIIE DGPIPIMGDI TASGCSLGST IASFIGGLDS TGKLFDAVVG AVLLYKSAGK LASTRCQGSG SFHVELIDAL YQLFHENKPE KWSASLKKFK // ID C9CXT3_9RHOB Unreviewed; 210 AA. AC C9CXT3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=SCH4B_2306; OS Silicibacter sp. TrichCH4B. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=644076; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TrichCH4B; RA Barbeau K., Mann E., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG703517; EEW59889.1; -; Genomic_DNA. DR ProteinModelPortal; C9CXT3; -. DR EnsemblBacteria; EEW59889; EEW59889; SCH4B_2306. DR PATRIC; 28605891; VBISilSp32447_1795. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 210 AA; 22498 MW; 2A0BDF3A8C874DEA CRC64; MDSAEQTPEQ PQIYLVTPPS FELGQFPGQL ARVLDEIEVA CVRLDLVSRD EDTLSRAADA LREVTHARDI ALVISDHQIL AERLGLDGVH LSDSSKSVRS ARKALGTEAI VGCFCGASRH EGITAGEAGA DYVCFGPVGT SGLGDGAIAE AELFQWWSEM IEVPVVAEGG LTTEVVRKIS PLTDFFAVGE EIWREDDPVA AMKALQAAMT // ID C9D1T3_9RHOB Unreviewed; 198 AA. AC C9D1T3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SCH4B_3742; OS Silicibacter sp. TrichCH4B. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=644076; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TrichCH4B; RA Barbeau K., Mann E., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG703519; EEW57534.1; -; Genomic_DNA. DR ProteinModelPortal; C9D1T3; -. DR EnsemblBacteria; EEW57534; EEW57534; SCH4B_3742. DR PATRIC; 28608694; VBISilSp32447_3505. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 198 AA; 22496 MW; DF38FCDF37C78705 CRC64; MTLDRFYPIF DHADWLRRML PLGVKLVQLR IKDQSRDIVK EQIEQSRDLC RRYGAVLVVN DYWQLAIELG CDWLHLGQED LDDADLKAIR AAGLKLGVST HDEDELDRVL SIDPDYVALG PVYPTILKKM KWHQQGLPRV SEWKTRIGDI PLVGIGGMSV ERAAGVLEAG ADIVSVVTDI TLNPDPETRV RQWIEATR // ID C9KJJ6_9FIRM Unreviewed; 234 AA. AC C9KJJ6; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MITSMUL_03195; OS Mitsuokella multacida DSM 20544. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Mitsuokella. OX NCBI_TaxID=500635; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20544; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWK02000001; EEX70062.1; -; Genomic_DNA. DR ProteinModelPortal; C9KJJ6; -. DR EnsemblBacteria; EEX70062; EEX70062; MITSMUL_03195. DR PATRIC; 37040800; VBIMitMul54707_0116. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 208 209 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 234 AA; 24703 MW; 0B05FE76F0618429 CRC64; MNMRKKLDIS AYLVVGPENT LGRPVGDIIR AAVENGFTCL QIRSKTASAR ELIALCCEAA DVLQALGKAE DVVLLVDDRL DVVLAAREAG IKVDGIHVGQ SDIPVAVCRK FLGPEAVIGL SARTQELLNY VRQADTRDID YFGAGPLHET ATKPDCGRDA AGHIITRSFE ELTELHAISP VPVVVGGGVK ARDLPALRKT GVDGFFVVSA VAGAADPAAA ARELVATWKA APRS // ID C9KKP9_9FIRM Unreviewed; 223 AA. AC C9KKP9; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=MITSMUL_03749; OS Mitsuokella multacida DSM 20544. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Mitsuokella. OX NCBI_TaxID=500635; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20544; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWK02000009; EEX69699.1; -; Genomic_DNA. DR ProteinModelPortal; C9KKP9; -. DR EnsemblBacteria; EEX69699; EEX69699; MITSMUL_03749. DR PATRIC; 37041810; VBIMitMul54707_1118. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 223 AA; 24154 MW; A5D7E1F6CC818316 CRC64; MSISKKFPPA KQEKQSETLN RLICVTNRHL FDDIEDAGGQ PSFLARLERI AAAHPAAIVL REKDMEEGAY EALAREVQAI CLRHQVPFIA HTFVGAAAHL GADGLHLPLP LLRRLRESRA VLPAHLGTSC HSLEDVREAE RLGCSYLIAG HIYATSCKPG LPPRGLAFLR EVTAATELPV YAIGGITPAR LREVLAAGAA GGCAMSSLMQ GNLWLTKIPE NNR // ID C9KZ27_9BACE Unreviewed; 202 AA. AC C9KZ27; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-APR-2014, entry version 20. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BACFIN_07580; OS Bacteroides finegoldii DSM 17565. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=483215; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17565; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXI02000055; EEX44595.1; -; Genomic_DNA. DR ProteinModelPortal; C9KZ27; -. DR EnsemblBacteria; EEX44595; EEX44595; BACFIN_07580. DR PATRIC; 27015212; VBIBacFin117758_2688. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23584 MW; B6FFECCBFEC19DF0 CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHRRIVTH EHFYMKEEFN LMGIHLNARN PKEPHDYDGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQKA KIIDSKVMAL GGINEENLLE IKDFGFGGAV ILGDLWNKFD ACSDRDYLAV IKHFKKLKKL SD // ID C9KZ32_9BACE Unreviewed; 205 AA. AC C9KZ32; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACFIN_07585; OS Bacteroides finegoldii DSM 17565. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=483215; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17565; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXI02000055; EEX44600.1; -; Genomic_DNA. DR ProteinModelPortal; C9KZ32; -. DR EnsemblBacteria; EEX44600; EEX44600; BACFIN_07585. DR PATRIC; 27015222; VBIBacFin117758_2693. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22700 MW; 607A37AB404E01A8 CRC64; MISLQFITHQ TERYSYFESA RMALEGGCKW IQLRMKEAPL EEVEQVALQL KPLCKEHEAI LVLDDHVELV KKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPLLG LEGYASILSQ MKEANINLPV VAIGGITNED IPDILRTGVN GIALSGTILR AENPVEETRK ILSNS // ID C9L8L9_BLAHA Unreviewed; 235 AA. AC C9L8L9; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BLAHAN_05741; OS Blautia hansenii DSM 20583. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=537007; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20583; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYU02000017; EEX21711.1; -; Genomic_DNA. DR ProteinModelPortal; C9L8L9; -. DR EnsemblBacteria; EEX21711; EEX21711; BLAHAN_05741. DR PATRIC; 36959437; VBIBlaHan43885_1570. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 57 61 HMP-PP binding (By similarity). FT REGION 154 156 THZ-P binding (By similarity). FT REGION 204 205 THZ-P binding (By similarity). FT METAL 90 90 Magnesium (By similarity). FT METAL 109 109 Magnesium (By similarity). FT BINDING 89 89 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 HMP-PP (By similarity). FT BINDING 184 184 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 235 AA; 26121 MW; 37DBBBB3E7C3FCAD CRC64; MLEIHSHYNI KNRIGEKMRL ERKNMCLYAV TDRSWIGEKS FLEQIEDSLK GGVTLLQLRE KNLSREEFLK EAQEVKKLTD KYGVPFIIND DVEIALQVDA AGVHVGQKDM EAGEARQKLG ADKILGVSCR TVEDAKKAEQ MGADYLGVGA MFATSTKTEA EVITTERLRS ICQAVAIPVV AIGGIKEENI TKLRDCGISG VAVISGIYAQ KDIESACQRF LKLSKEITQQ EVKEK // ID C9LAL8_BLAHA Unreviewed; 195 AA. AC C9LAL8; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 11-DEC-2013, entry version 20. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=BLAHAN_06471; OS Blautia hansenii DSM 20583. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=537007; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20583; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYU02000030; EEX21016.1; -; Genomic_DNA. DR ProteinModelPortal; C9LAL8; -. DR EnsemblBacteria; EEX21016; EEX21016; BLAHAN_06471. DR PATRIC; 36960826; VBIBlaHan43885_1938. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 195 AA; 22220 MW; 9C3F27611EC5F2E9 CRC64; MCREEIFQNV IAVSNRKLCT RPFPEQIEIV CRHRPQSLIL REKDLNESEY GKLGQEVKEI CKKYQVTCIY HTFYEEAKKA GVRNIHLPLW KLEELNEEDG QRDFDLIGAS IHSVEEAKKA EKLGATYLTA GHIYETGCKP DLPPRGLNFL KEVCQVVDIP VYAIGGIRLE KQQIAEIQKA GARGACIMSE LMKIS // ID C9LIF5_9BACT Unreviewed; 201 AA. AC C9LIF5; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 13-NOV-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=GCWU000325_02014; OS Prevotella tannerae ATCC 51259. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Alloprevotella. OX NCBI_TaxID=626522; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51259; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIJ02000022; EEX71271.1; -; Genomic_DNA. DR ProteinModelPortal; C9LIF5; -. DR EnsemblBacteria; EEX71271; EEX71271; GCWU000325_02014. DR PATRIC; 37140778; VBIPreTan62661_4364. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23446 MW; 567EE712557DDD48 CRC64; MGAFKLVLLT TPYFFVEEHA ILSTLFDEGL ELLHMRKPNS EPVYSERLLS LLPERYRKRI ITHDHFYLKQ EFGLKGIHLN QRNTAAPDNY RGQISCTCRN KEELQQRKKQ MDYVFLSLSP DDNQEASSID PEKELTTMGK LIDKKVYAAG GVTIDNLLQL KERGFGGAVL YGEIWNRFNI FSNQDYKDLI NHFRKLKKII D // ID C9LM32_9FIRM Unreviewed; 217 AA. AC C9LM32; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GCWU000321_00567; OS Dialister invisus DSM 15470. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Dialister. OX NCBI_TaxID=592028; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15470; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIM02000001; EEW96618.1; -; Genomic_DNA. DR ProteinModelPortal; C9LM32; -. DR EnsemblBacteria; EEW96618; EEW96618; GCWU000321_00567. DR PATRIC; 36975796; VBIDiaInv115189_0541. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23521 MW; 558A76ABFD7760BF CRC64; MKFDCSLYLV ADTGTTERRK LDKKVELAIR GGCTMVQLRE KNGNMKEFYH DAAALRRITD TYSIPLIIND RLDLMLAIDA PGIHVGQNDI PASIVRRLIG AEKIMGVSAH NVEEALQAER DGADYIGVGA VFSTNTKKNT KNVTIKMLQE IVKAVSIPVV AIGGINCSNV KYLHETGISG IAVVSAILGA AQAYSAAKKM KKVVISTLNI KNKYSSN // ID C9LXN1_SELS3 Unreviewed; 199 AA. AC C9LXN1; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Selsp_0455, SELSPUOL_02239; OS Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=546271; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35185; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35185, and ATCC 35185 / DSM 20758 / VPI D19B-28; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., RA Wellnitz S., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Selenomonas sputigena DSM 20758."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002637; AEB99427.1; -; Genomic_DNA. DR EMBL; ACKP02000049; EEX76414.1; -; Genomic_DNA. DR RefSeq; YP_004412887.1; NC_015437.1. DR EnsemblBacteria; AEB99427; AEB99427; Selsp_0455. DR EnsemblBacteria; EEX76414; EEX76414; SELSPUOL_02239. DR GeneID; 10496665; -. DR KEGG; ssg:Selsp_0455; -. DR PATRIC; 25828245; VBISelSpu76100_1932. DR KO; K00788; -. DR BioCyc; SSPU546271:GCBU-464-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 199 AA; 21069 MW; 7CDFE19D671F19E0 CRC64; MYRGRIIACI TNRRLVKGDF LAQIERVAAM EMADWIIVRE KDLSVEEYRM LFAKVARIVH KGGKKCLAHG RIALGMMSEL GADGIHLPLD VLREWRAASG RRSAPQAGAV QLVGASAHSA AEIAEAVALG ADYATLSPIF VTACKPGAVP LGIAALAAVC KESPIPIFAL GGIGMDKLDA CIEAGAAGCC MMSELMRCM // ID C9LYI3_SELS3 Unreviewed; 80 AA. AC C9LYI3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Uncharacterized protein; DE Flags: Fragment; GN ORFNames=SELSPUOL_02544; OS Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=546271; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35185; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKP02000053; EEX76112.1; -; Genomic_DNA. DR EnsemblBacteria; EEX76112; EEX76112; SELSPUOL_02544. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; FT NON_TER 80 80 SQ SEQUENCE 80 AA; 8272 MW; ACC8CE0F9586BCE7 CRC64; MGGAPMGFSV SDMTLRSHLA VTAYLVIGPR DTKGRRVGEI VKAAVCAGFT AVQLRAKEES AREQIALLGE AARAIEAAGA // ID C9LYI4_SELS3 Unreviewed; 169 AA. AC C9LYI4; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; DE Flags: Fragment; GN ORFNames=SELSPUOL_02545; OS Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=546271; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35185; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKP02000054; EEX76050.1; -; Genomic_DNA. DR ProteinModelPortal; C9LYI4; -. DR EnsemblBacteria; EEX76050; EEX76050; SELSPUOL_02545. DR PATRIC; 25828786; VBISelSpu76100_2200. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; FT NON_TER 1 1 SQ SEQUENCE 169 AA; 17005 MW; E9AE1C27A1042F7E CRC64; AAGAAASVPL LVDDRLDVAL AAREMGVAVA GVHVGQKDVP AHICRRLLGE AAIVGLSAHP QDLPRLAPED LAAADYIGTG PLHATASKPD AGIEADGSFR TRSLAEIAAF AQKSPVPVIV GGGVKAADLP AIKATGAAGF FVISAVAAAA DAEGAAREMV ARWRDEVIF // ID C9MCA6_HAEIF Unreviewed; 226 AA. AC C9MCA6; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HIAG_00749; OS Haemophilus influenzae NT127. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=656913; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NT127; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Gawronski J.D., Akerley B.J., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Haemophilus influenzae strain NT127."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACSL01000005; EEW78582.1; -; Genomic_DNA. DR ProteinModelPortal; C9MCA6; -. DR EnsemblBacteria; EEW78582; EEW78582; HIAG_00749. DR PATRIC; 28866133; VBIHaeInf51885_0767. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24721 MW; 5E34364400694040 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID C9MHB9_HAEIF Unreviewed; 226 AA. AC C9MHB9; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-APR-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HICG_00703; OS Haemophilus influenzae RdAW. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=656912; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RdAW; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Gawronski J.D., Akerley B.J., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Haemophilus influenzae strain RdAW."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACSM01000003; EEW76797.1; -; Genomic_DNA. DR ProteinModelPortal; C9MHB9; -. DR EnsemblBacteria; EEW76797; EEW76797; HICG_00703. DR PATRIC; 26795240; VBIHaeInf78752_0716. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24730 MW; C5EB00DED081EEE7 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAINCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID C9MLI3_9BACT Unreviewed; 204 AA. AC C9MLI3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 13-NOV-2013, entry version 19. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF0973_00458; OS Prevotella veroralis F0319. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=649761; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0319; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVA01000013; EEX19517.1; -; Genomic_DNA. DR ProteinModelPortal; C9MLI3; -. DR EnsemblBacteria; EEX19517; EEX19517; HMPREF0973_00458. DR PATRIC; 37142945; VBIPreVer83495_0130. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 204 AA; 23344 MW; 2216E646DBA5C46D CRC64; MSMKLVIMTK STFFVEEDKI ISMLFEEGLD CLHISKVDPS PLYLERLLSL IPSHYHSKIV VHQHFQTKGE YGLGGIHLDN PTISAPRGYK GHISRSCDDV MKLKAIKKQS DYVLLKNIHQ PREQSAATEH ILSDIELEEA SRQGLLGKHV YAMGGITVDD FPRLHDLDFG GVVVRNDLWD QFCIHSEQNF NPIIKYFHKL RTIC // ID C9NMC3_9VIBR Unreviewed; 423 AA. AC C9NMC3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VIC_000402; OS Vibrio coralliilyticus ATCC BAA-450. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675814; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-450; RX PubMed=22158392; DOI=10.1038/ismej.2011.154; RA Kimes N.E., Grim C.J., Johnson W.R., Hasan N.A., Tall B.D., RA Kothary M.H., Kiss H., Munk A.C., Tapia R., Green L., Detter C., RA Bruce D.C., Brettin T.S., Colwell R.R., Morris P.J.; RT "Temperature regulation of virulence factors in the pathogen Vibrio RT coralliilyticus."; RL ISME J. 6:835-846(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZN01000011; EEX35107.1; -; Genomic_DNA. DR EnsemblBacteria; EEX35107; EEX35107; VIC_000402. DR PATRIC; 30094501; VBIVibCor144446_0406. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 423 AA; 46804 MW; B8EF3B52A446C7C1 CRC64; MATILIPTAL ADVKPEIEQC LQLAKEKGFE IENIELGVSP AQTVHISHGS EWTKLATDLV ESGVVGDERT FFIEYYSGIT IEPSRPIIAS SHVYINVLDV NQVLDIWLDP SREQICALAS SVNQSELDRK RHFAWVVTLI SLAFTFEDAL TLARAMANVS RETWAENIID FPSPVLEDHR LGISAGWIKS GNQLAFPTVS KCDLGLYPVV DNVEWVKTLL ESGVKTVQLR IKDPLSDDLE QQIEDAVVLG RRYDAQVFIN DHWRLAIKHQ AYGVHLGQED IEESNLAELA KSSLRLGLST HGYYELLRVA QTNPSYLALG HIFPTQTKQI ATNPQGLVKL ALYQKLVNTM PYLNSTGVPT VAIGGITQSN AHLVWNCGVT SLALVSAITQ APLLEQAVEF FTRLTTDERQ NISNDVSNEV SAC // ID C9NY00_9VIBR Unreviewed; 134 AA. AC C9NY00; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Mutator MutT; GN ORFNames=VIC_004324; OS Vibrio coralliilyticus ATCC BAA-450. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675814; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-450; RX PubMed=22158392; DOI=10.1038/ismej.2011.154; RA Kimes N.E., Grim C.J., Johnson W.R., Hasan N.A., Tall B.D., RA Kothary M.H., Kiss H., Munk A.C., Tapia R., Green L., Detter C., RA Bruce D.C., Brettin T.S., Colwell R.R., Morris P.J.; RT "Temperature regulation of virulence factors in the pathogen Vibrio RT coralliilyticus."; RL ISME J. 6:835-846(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZN01000018; EEX31376.1; -; Genomic_DNA. DR ProteinModelPortal; C9NY00; -. DR EnsemblBacteria; EEX31376; EEX31376; VIC_004324. DR PATRIC; 30102558; VBIVibCor144446_4386. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 134 AA; 14406 MW; 44E25C419AD29D00 CRC64; MKGIVLVNSA SYDGSDVAPF YGVHFTSKDL SDKALIQSVR HSGAQYLSAS CHNEQEIELA NKAGCDFITI SPVEATNSHP DATPIGWQRF AELSKLANMP AFALGGQNTH NVEHAQSYGA HGVAGISDFW QVEK // ID C9P0L3_VIBME Unreviewed; 435 AA. AC C9P0L3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VIB_000010; OS Vibrio metschnikovii CIP 69.14. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675813; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 69.14; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D., RA Vonstein V.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZO01000002; EEX38546.1; -; Genomic_DNA. DR EnsemblBacteria; EEX38546; EEX38546; VIB_000010. DR PATRIC; 30104166; VBIVibMet139223_0016. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 435 AA; 47762 MW; 34BE69BC19DCFACE CRC64; MKLLIPAHCI ELTGAVQQVL LLAKQQGFAI ESIELGVSPT QSMQLLGQHR YSLQTDLFPS FSGSEPSRQN LASIAFGYQS RKSDSDIDNL DSATLLIGAA YKGQQRDIWR HTDGELMFLS GAMLSPAQAW HHLAWLVAAL CLEFALEDAL CIARAALNVS RETWPKDYAY FPAVQSCLVD ETRAISFPSL AKQSLGLYPV VDNIAWVESL LKLGINTLQL RIKNPQQVDL EQQIVRAIEL GRQYQAQVFI NDYWPLALKH GAFGVHLGQE DLQSADLDAL AKANIHLGLS THGYFELLTA LKIRPSYIAL GHIFPTTTKQ MPSRPQGLVR LALYQQLVDS STDYRYLVPA SALDQQLTIE RDSTIKGELP TVAIGGIDLT NIQSVVECGV ASVAVVRAIT EADDVHAAVK HLQAQLASKP QEQKLSTQEV ADVNG // ID C9PAC0_VIBFU Unreviewed; 400 AA. AC C9PAC0; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VFA_000538; OS Vibrio furnissii CIP 102972. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675811; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 102972; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., RA Bartels D., Vonstein V.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZP01000011; EEX42571.1; -; Genomic_DNA. DR ProteinModelPortal; C9PAC0; -. DR EnsemblBacteria; EEX42571; EEX42571; VFA_000538. DR PATRIC; 37169743; VBIVibFur145292_0370. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 400 AA; 44489 MW; F61A1E65AEE8517E CRC64; MKLLIPSQCI ELTGDVQRVL LLAEQQGFAI GHIELGVSPT PDLQLVGDTT LRLSCNWFPH VQPDADWVLH YGAVADDYAS TAMHDRWIFI GDEHQGRVTD HWQHSDEVRY LLQVTPLEPR DYGRHLAWVL ACLSLDFPIE DALVLSRAAL NVSRETWPSD YRHFPQPRTQ AEFSAFPTLK PASLGVYPVV DDVRWIAQLL PLGISTIQLR IKDSHQADLE QQVMEAIRLG RQFGAQVFIN DYWQLAVKHG AYGVHLGQED LQAVDLKVLS DNNLRLGLST HGYFELLRIH QLAPSYIALG HIFPTTTKQM PSKPQGLVRL ALYQQLLDSM PYGDTTGVPS VAIGGIDALN AEHVLACGVT SIAVVRAITE AKDVAVATHT LQQIFTLSLA STKERNHVVG // ID C9PCB7_VIBFU Unreviewed; 215 AA. AC C9PCB7; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VFA_001098; OS Vibrio furnissii CIP 102972. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675811; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 102972; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., RA Bartels D., Vonstein V.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZP01000013; EEX41264.1; -; Genomic_DNA. DR ProteinModelPortal; C9PCB7; -. DR EnsemblBacteria; EEX41264; EEX41264; VFA_001098. DR PATRIC; 37170929; VBIVibFur145292_0936. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22979 MW; 1999479709CD4782 CRC64; MTPYTLYLVT DDQQDLNTLC RVVKQAIAGG VSLVQVREKQ GDVRTFIERA AAVKAVLSGS GVPLIINDRV DVALAVDADG VHLGQSDMPA TLARQLLGPD KLIGLSVENE QQFEQAQSLP VDYLGLSAIF ATPTKTNTVK HWGLDGLNWA MARSRLPMVA IGGLNTSNIA AVAQTGVHGI ALVSAISHAP DPQQAARELR LLIEQNRPDS LVRNS // ID C9PP07_9PAST Unreviewed; 222 AA. AC C9PP07; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0621_0739; OS Pasteurella dagmatis ATCC 43325. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=667128; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43325; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZR01000006; EEX50798.1; -; Genomic_DNA. DR ProteinModelPortal; C9PP07; -. DR EnsemblBacteria; EEX50798; EEX50798; HMPREF0621_0739. DR PATRIC; 25897685; VBIPasDag141287_1008. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 202 203 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23823 MW; EBCD896FB6078665 CRC64; MYMNKIEQAM RLYFIAGTQD CPNTGGDPAE NLLRILEQAL KAGITCYQFR EKGKKSLQDP VKVKELAMKC RDLCRQYNVP FVVNDDVQLA IEIGADGIHV GQTDMAVADV AALCHSKCFI GTSVNTLNQG LAAQANPLID YFGTGPIFPT QSKEDPKPVV GVEFISTIRQ NGIDKPIVAI GGVTAQSAGE LRQRGANGVA VISAIAQSNN ITKTVQELLG NA // ID C9PYP8_9BACT Unreviewed; 205 AA. AC C9PYP8; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 13-NOV-2013, entry version 19. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF6745_2071; OS Prevotella sp. oral taxon 472 str. F0295. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=619693; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0295; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZS01000130; EEX52466.1; -; Genomic_DNA. DR ProteinModelPortal; C9PYP8; -. DR EnsemblBacteria; EEX52466; EEX52466; HMPREF6745_2071. DR PATRIC; 29541979; VBIPreSp61738_0162. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 205 AA; 23327 MW; FD0D4B6C13B244D6 CRC64; MAAMKLVIMT KSTFFVEEDK ILTALFDEGM DKLHLYKPGS QLVFSERLLS LVPEGYHDKI VVHEHFRLKN EYDLAGIHLN RPTEFVPNGI KGKVSRTCED LSLLKDMKKS SNYVFLRRIF SCTGDAEKPS SFSVKQLEEA ADKGLIDKRV YALGGIDIDN VRMAKELGFG GVVVCSDLWK RFDIHNGTDF RDLLTLFRNY QKVVG // ID C9Q2Y0_9VIBR Unreviewed; 413 AA. AC C9Q2Y0; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 11-DEC-2013, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VCJ_000469; OS Vibrio sp. RC341. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675810; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RC341; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Sims D.R., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., RA Bartels D., Vonstein V.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZT01000013; EEX67311.1; -; Genomic_DNA. DR ProteinModelPortal; C9Q2Y0; -. DR EnsemblBacteria; EEX67311; EEX67311; VCJ_000469. DR PATRIC; 25643333; VBIVibSp138932_0473. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 413 AA; 45635 MW; C48F2F8F93F3CD75 CRC64; MTRLVFPRGC AEWIGRVQYV LLQAKEQGFD IQNISLDVAT SDCFVLEAKS TLRIGCDLCP SEGTSEPLDY YLQYLSEHRD IEAGCKVKIG LRSHNDYGMD EWQVEGNCCQ CITYPYPLLI SNCQLDQHVA WLLALLALGF SIEDALCVAR AAVSQKQGVS RETWPTSLEF FPSVYSGSEL QSTKGFPAID KTLFTLYPVV DDVSWIELLL KLGVKTVQLR IKDPARVDLE TQIVRAIDLG RKYNAQVFIN DYWQIAIKHH AYGVHLGQED LSTANLAELA QAGLRLGLST HGYYELLNVA CLQPSYIALG HIFPTTTKQM PSKPQGLVRL AAYQGLADQL SYHGQKGMPT VAIGGIDHSN IEEVLRCGVT SAAVVRAITQ SANPAFAVHQ LMFAFNGQKT SEVLQHGMGG EQC // ID C9QC26_VIBOR Unreviewed; 466 AA. AC C9QC26; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 11-DEC-2013, entry version 28. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=VIA_000140, VIOR3934_08971; OS Vibrio orientalis CIP 102891 = ATCC 33934. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675816; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 102891; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Chertkov O., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., RA Bartels D., Vonstein V.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 102891; RA Hoffman M., Strain E.A., Brown E., Allard M.W.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 102891; RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0; RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., RA Naum M., McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.; RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge RT Scleritoderma cyanea."; RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZV01000001; EEX95608.1; -; Genomic_DNA. DR EMBL; AFWH01000034; EGU49055.1; -; Genomic_DNA. DR EnsemblBacteria; EEX95608; EEX95608; VIA_000140. DR EnsemblBacteria; EGU49055; EGU49055; VIOR3934_08971. DR PATRIC; 35986976; VBIVibOri138666_0141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 466 AA; 51803 MW; A7DFA01452F9BCDF CRC64; MSKILIPSSL IELTGLVQQC LLLAKEQGFC IEDFELGVSP TQSIQLVRDQ QITHITTDLI DGYDSEPECS LALYYRSALS VEACARQPSK TIFIGIADSQ VSGEKDEALY LDIWRHPIND EVRALSVKFK VNAMFDPEHH LAWIVTLIVL DFPIEDALTL ARGMLTQQAN VSRETLLSDS LDEGRSTLWA DQFDDFPTPV LEDNRLGIQV GWSAQGEDVN FPTLTKQGLG LYPVVDDVAW IESLLPLGIS TIQLRIKNPL RADLEQQIIR AIELGRQYKA QVFINDYWQL AIKHGAYGVH LGQEDIEESN LAQLTKAGIC LGLSTHGYYE LLRIVQIHPS YIALGHIFPT TTKQMPSKPQ GLVRLALYQK LIDSIPYGNT ERAFRSSKDK AVSGDLLGFP TVAIGGIDQS NADQVWQTGV SSLAVVRAIT LAESAQSVIE FFAQLMKERQ LTFTDQNSEL ADTKRG // ID C9QV83_ECOD1 Unreviewed; 211 AA. AC C9QV83; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EcDH1_4001, ECDH1ME8569_3853; OS Escherichia coli (strain ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / OS DH1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=536056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1, and DH1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Keasling J.D.; RT "Complete sequence of Escherichia coli DH1."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1, and DH1; RX PubMed=21611185; DOI=10.1371/journal.pone.0019534; RA Suzuki S., Ono N., Furusawa C., Ying B.-W., Yomo T.; RT "Comparison of sequence reads obtained from three next-generation RT sequencing platforms."; RL PLoS ONE 6:E19534-E19534(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001637; ACX41601.1; -; Genomic_DNA. DR EMBL; AP012030; BAJ45709.1; -; Genomic_DNA. DR RefSeq; YP_006093890.1; NC_017625.1. DR RefSeq; YP_006131254.1; NC_017638.1. DR EnsemblBacteria; ACX41601; ACX41601; EcDH1_4001. DR EnsemblBacteria; BAJ45709; BAJ45709; ECDH1ME8569_3853. DR GeneID; 12707647; -. DR GeneID; 12871723; -. DR KEGG; edh:EcDH1_4001; -. DR KEGG; edj:ECDH1ME8569_3853; -. DR PATRIC; 36700660; VBIEscCol36761_4253. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23114 MW; 32318E24F7172950 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALRH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID C9RAN9_AMMDK Unreviewed; 344 AA. AC C9RAN9; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Adeg_0144; OS Ammonifex degensii (strain DSM 10501 / KC4). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Moorella group; Ammonifex. OX NCBI_TaxID=429009; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10501 / KC4; RG US DOE Joint Genome Institute; RA Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A., RA Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., RA Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., RA Richardson P.; RT "Complete sequence of chromosome of Ammonifex degensii KC4."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001785; ACX51316.1; -; Genomic_DNA. DR RefSeq; YP_003238166.1; NC_013385.1. DR ProteinModelPortal; C9RAN9; -. DR STRING; 429009.Adeg_0144; -. DR EnsemblBacteria; ACX51316; ACX51316; Adeg_0144. DR GeneID; 8490105; -. DR KEGG; adg:Adeg_0144; -. DR PATRIC; 20879794; VBIAmmDeg104956_0143. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ADEG429009:GHG1-147-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 171 175 HMP-PP binding (By similarity). FT REGION 268 270 THZ-P binding (By similarity). FT METAL 204 204 Magnesium (By similarity). FT METAL 223 223 Magnesium (By similarity). FT BINDING 203 203 HMP-PP (By similarity). FT BINDING 242 242 HMP-PP (By similarity). FT BINDING 271 271 HMP-PP (By similarity). FT BINDING 298 298 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 344 AA; 37950 MW; 5E412D243D16F666 CRC64; MWRMMDANLN RLREGLRVLE DLARFTFQER ALAEEARAFR HQVAWSREPE QAECLVHRDV AGDWGKDYRS LPYPSLKELV LANSRRVQEA ARVLEELARL TLPEREELFR KVRFWAYAAE KKLYSLATGE ERRQRCWRWR LYVIVGSEHT GGREVPAVVR AAIAGGAEVI QLREKKLSTR ALYSLARQLR EITGEAGVDL IINDRVDVAL AVGADGVHLG SEDLPLPEAR RVIGDKLILG ATAHSLEEAL EAQAAGADYL GVGPVFPTAT KPELKPGGLK LLREVASQVS LPVVAIGGIT AENVREVLAQ PGVKCVAVIR AVATAPDVKE AAARLKQAME GMGS // ID C9RP26_FIBSS Unreviewed; 210 AA. AC C9RP26; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Fisuc_2913, FSU_0175; OS Fibrobacter succinogenes (strain ATCC 19169 / S85). OC Bacteria; Fibrobacteres; Fibrobacterales; Fibrobacteraceae; OC Fibrobacter. OX NCBI_TaxID=59374; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19169 / S85, and S85; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Weimer P.J., Stevenson D.M., Boyum J., Brumm P.I., Mead D.; RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes RT S85."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19169 / S85; RA Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B., RA Russell J.B., Cann I.K.O., Mackie R.I., White B.A.; RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes RT S85."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S85; RA Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B., RA Russell J.B., Cann I.K.O., Mackie R.I., White B.A.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001792; ACX76494.1; -; Genomic_DNA. DR EMBL; CP002158; ADL26055.1; -; Genomic_DNA. DR RefSeq; YP_003250976.1; NC_013410.1. DR RefSeq; YP_005820334.1; NC_017448.1. DR STRING; 59374.Fisuc_2913; -. DR EnsemblBacteria; ACX76494; ACX76494; Fisuc_2913. DR EnsemblBacteria; ADL26055; ADL26055; FSU_0175. DR GeneID; 12431824; -. DR GeneID; 8523560; -. DR KEGG; fsc:FSU_0175; -. DR KEGG; fsu:Fisuc_2913; -. DR PATRIC; 32145587; VBIFibSuc28982_2841. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; YLVIDPS; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22400 MW; 460A0B182540B5A8 CRC64; MKKLDTTLYF ITDSTSVPAD RFLPTVEAAC KGGATLIQLR EKNRSTREYM ELAAAAHEVT KRYNIPLIID DRVDVALAIG AEGVHVGQTD MPVKIARQLM GADKIIGATT KTVPQALEAY EQGADYLGVG AIYPTTTKVV TILTSVDTLK AIVKAVPINV NAIGGLNKDN IDVLKGSGIS GICAVSAIMK AADPEKATRE LKDAFLNLNK // ID C9RX53_GEOSY Unreviewed; 201 AA. AC C9RX53; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 13-NOV-2013, entry version 30. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=GYMC61_1414; OS Geobacillus sp. (strain Y412MC61). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=544556; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y412MC61; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Brumm P., Mead D.; RT "Complete sequence of chromosome of Geobacillus sp. Y412MC61."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001794; ACX78055.1; -; Genomic_DNA. DR RefSeq; YP_003252537.1; NC_013411.1. DR ProteinModelPortal; C9RX53; -. DR STRING; 544556.GYMC61_1414; -. DR EnsemblBacteria; ACX78055; ACX78055; GYMC61_1414. DR GeneID; 8525277; -. DR KEGG; gyc:GYMC61_1414; -. DR PATRIC; 32164436; VBIGeoSp85804_1462. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GSP544556:GI3L-1506-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 21097 MW; FA3CD957E8611004 CRC64; MGVLHFVSTG RQTVDEFAAI CAHTHPYADL IHIREKGKTA REVAAFVAAL LRVGVPPQKI IVNDRVDVAA VYGVKGVQLA YHSLPVRAVR RSFPDLTVGC SVHGSEEAKQ AEQDGAHFCL YGHIFPTDSK PGLPPRGLDS LAEIVAAVSI PVIAIGGIHA GNARRVLEAG AAGVAVLSAV FFAADPVAEA KRLADIVKGR G // ID C9S1W3_GEOSY Unreviewed; 221 AA. AC C9S1W3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GYMC61_2347; OS Geobacillus sp. (strain Y412MC61). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=544556; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y412MC61; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Brumm P., Mead D.; RT "Complete sequence of chromosome of Geobacillus sp. Y412MC61."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001794; ACX78951.1; -; Genomic_DNA. DR RefSeq; YP_003253433.1; NC_013411.1. DR ProteinModelPortal; C9S1W3; -. DR STRING; 544556.GYMC61_2347; -. DR EnsemblBacteria; ACX78951; ACX78951; GYMC61_2347. DR GeneID; 8526212; -. DR KEGG; gyc:GYMC61_2347; -. DR PATRIC; 32166372; VBIGeoSp85804_2427. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GSP544556:GI3L-2441-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23055 MW; 40DF21614BB8F035 CRC64; MARIASGEMK ERLAVYFIMG SQNSERPAAD VLKEALDGGV TLFQFREKGP GALKGADKEE LARQLQHLCR AYGVPFIVND DVELALAIDA DGVHVGQDDE DARRVREKIG DKILGVSAHN VEEAMAAVEA GADYLGVGPI YPTSSKEDAK EAQGPDVLRR LREAGITIPI VAIGGITAAN AKTVVEAGAD GVSVISAIAS APSPKAAAAA LAEAVRAART R // ID C9T522_9RHIZ Unreviewed; 203 AA. AC C9T522; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAIG_01517; OS Brucella ceti M644/93/1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M644/93/1; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella ceti M644/93/1."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999670; EEX97129.1; -; Genomic_DNA. DR ProteinModelPortal; C9T522; -. DR EnsemblBacteria; EEX97129; EEX97129; BAIG_01517. DR PATRIC; 24223814; VBIBruCet111375_1391. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C9T7P7_9RHIZ Unreviewed; 221 AA. AC C9T7P7; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAIG_02932; OS Brucella ceti M644/93/1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M644/93/1; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella ceti M644/93/1."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999672; EEX98544.1; -; Genomic_DNA. DR ProteinModelPortal; C9T7P7; -. DR EnsemblBacteria; EEX98544; EEX98544; BAIG_02932. DR PATRIC; 24226885; VBIBruCet111375_3097. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C9TEB7_9RHIZ Unreviewed; 203 AA. AC C9TEB7; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAJG_01654; OS Brucella ceti M13/05/1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520460; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M13/05/1; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella ceti M13/05/1."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999687; EEX89866.1; -; Genomic_DNA. DR ProteinModelPortal; C9TEB7; -. DR EnsemblBacteria; EEX89866; EEX89866; BAJG_01654. DR PATRIC; 24210234; VBIBruCet83544_1364. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C9TGF0_9RHIZ Unreviewed; 221 AA. AC C9TGF0; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAJG_02742; OS Brucella ceti M13/05/1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520460; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M13/05/1; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella ceti M13/05/1."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999690; EEX90954.1; -; Genomic_DNA. DR ProteinModelPortal; C9TGF0; -. DR EnsemblBacteria; EEX90954; EEX90954; BAJG_02742. DR PATRIC; 24212606; VBIBruCet83544_2905. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C9TMS5_9RHIZ Unreviewed; 203 AA. AC C9TMS5; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAGG_01736; OS Brucella pinnipedialis M163/99/10. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520463; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M163/99/10; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella pinnipedialis M163/99/10."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999752; EEY07099.1; -; Genomic_DNA. DR ProteinModelPortal; C9TMS5; -. DR EnsemblBacteria; EEY07099; EEY07099; BAGG_01736. DR PATRIC; 24259429; VBIBruPin128057_1972. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C9TRM3_9RHIZ Unreviewed; 221 AA. AC C9TRM3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAGG_03084; OS Brucella pinnipedialis M163/99/10. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520463; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M163/99/10; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella pinnipedialis M163/99/10."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999755; EEY08447.1; -; Genomic_DNA. DR ProteinModelPortal; C9TRM3; -. DR EnsemblBacteria; EEY08447; EEY08447; BAGG_03084. DR PATRIC; 24262360; VBIBruPin128057_3186. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C9TSG2_BRUPB Unreviewed; 132 AA. AC C9TSG2; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN ORFNames=BAHG_03126; OS Brucella pinnipedialis (strain NCTC 12890 / BCCN 94-73 / B2/94). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520461; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B2/94; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella pinnipedialis B2/94."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999845; EEX98932.1; -; Genomic_DNA. DR EnsemblBacteria; EEX98932; EEX98932; BAHG_03126. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; FT NON_TER 132 132 SQ SEQUENCE 132 AA; 13692 MW; C67800D660D29AAF CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QP // ID C9TT37_BRUPB Unreviewed; 203 AA. AC C9TT37; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-APR-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BPI_I215; ORFNames=BAHG_00517; OS Brucella pinnipedialis (strain NCTC 12890 / BCCN 94-73 / B2/94). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520461; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B2/94; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella pinnipedialis B2/94."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B2/94; RA Zygmunt M., Clockaert A.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B2/94, and NCTC 12890 / BCCN 94-73 / B2/94; RX PubMed=21745361; DOI=10.1186/1471-2148-11-200; RA Audic S., Lescot M., Claverie J.M., Cloeckaert A., Zygmunt M.S.; RT "The genome sequence of Brucella pinnipedialis B2/94 sheds light on RT the evolutionary history of the genus Brucella."; RL BMC Evol. Biol. 11:200-200(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002078; AEK53529.1; -; Genomic_DNA. DR EMBL; DS999848; EEX99587.1; -; Genomic_DNA. DR RefSeq; YP_004755297.1; NC_015857.1. DR EnsemblBacteria; AEK53529; AEK53529; BPI_I215. DR EnsemblBacteria; EEX99587; EEX99587; BAHG_00517. DR GeneID; 10996695; -. DR KEGG; bpp:BPI_I215; -. DR PATRIC; 24250290; VBIBruPin17457_2119. DR KO; K00788; -. DR BioCyc; BPIN520461:GJF0-215-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C9U5I8_BRUAO Unreviewed; 221 AA. AC C9U5I8; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAAG_03072; OS Brucella abortus bv. 6 str. 870. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520454; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=870; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 6 str. 870."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999865; EEX62337.1; -; Genomic_DNA. DR ProteinModelPortal; C9U5I8; -. DR EnsemblBacteria; EEX62337; EEX62337; BAAG_03072. DR PATRIC; 24188804; VBIBruAbo118911_1457. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C9U7E8_BRUAO Unreviewed; 203 AA. AC C9U7E8; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAAG_02411; OS Brucella abortus bv. 6 str. 870. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520454; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=870; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 6 str. 870."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999867; EEX62997.1; -; Genomic_DNA. DR ProteinModelPortal; C9U7E8; -. DR EnsemblBacteria; EEX62997; EEX62997; BAAG_02411. DR PATRIC; 24190234; VBIBruAbo118911_1691. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C9UER0_BRUAO Unreviewed; 221 AA. AC C9UER0; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BABG_03073; OS Brucella abortus bv. 4 str. 292. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520452; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=292; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 4 str. 292."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999877; EEX55888.1; -; Genomic_DNA. DR ProteinModelPortal; C9UER0; -. DR EnsemblBacteria; EEX55888; EEX55888; BABG_03073. DR PATRIC; 24181784; VBIBruAbo93713_1454. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C9UGM2_BRUAO Unreviewed; 203 AA. AC C9UGM2; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BABG_02407; OS Brucella abortus bv. 4 str. 292. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520452; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=292; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 4 str. 292."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999879; EEX56550.1; -; Genomic_DNA. DR ProteinModelPortal; C9UGM2; -. DR EnsemblBacteria; EEX56550; EEX56550; BABG_02407. DR PATRIC; 24183242; VBIBruAbo93713_2170. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C9UNZ7_BRUAO Unreviewed; 221 AA. AC C9UNZ7; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BACG_03111; OS Brucella abortus bv. 3 str. Tulya. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520451; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tulya; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 3 str. Tulya."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999888; EEX83146.1; -; Genomic_DNA. DR ProteinModelPortal; C9UNZ7; -. DR EnsemblBacteria; EEX83146; EEX83146; BACG_03111. DR PATRIC; 24174628; VBIBruAbo20544_1479. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C9UQW2_BRUAO Unreviewed; 203 AA. AC C9UQW2; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BACG_02433; OS Brucella abortus bv. 3 str. Tulya. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520451; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tulya; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 3 str. Tulya."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999890; EEX83811.1; -; Genomic_DNA. DR ProteinModelPortal; C9UQW2; -. DR EnsemblBacteria; EEX83811; EEX83811; BACG_02433. DR PATRIC; 24176123; VBIBruAbo20544_2218. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C9UVV0_BRUAO Unreviewed; 203 AA. AC C9UVV0; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BADG_00521; OS Brucella abortus bv. 2 str. 86/8/59. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520450; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=86/8/59; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 2 str. 86/8/59."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999900; EEX58267.1; -; Genomic_DNA. DR ProteinModelPortal; C9UVV0; -. DR EnsemblBacteria; EEX58267; EEX58267; BADG_00521. DR PATRIC; 24165483; VBIBruAbo60950_0401. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C9UZY0_BRUAO Unreviewed; 221 AA. AC C9UZY0; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BADG_03066; OS Brucella abortus bv. 2 str. 86/8/59. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520450; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=86/8/59; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 2 str. 86/8/59."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999906; EEX59709.1; -; Genomic_DNA. DR ProteinModelPortal; C9UZY0; -. DR EnsemblBacteria; EEX59709; EEX59709; BADG_03066. DR PATRIC; 24168725; VBIBruAbo60950_2178. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C9V890_BRUNE Unreviewed; 203 AA. AC C9V890; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BANG_00513; OS Brucella neotomae 5K33. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520456; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5K33; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella neotomae 5K33."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999582; EEY03802.1; -; Genomic_DNA. DR ProteinModelPortal; C9V890; -. DR EnsemblBacteria; EEY03802; EEY03802; BANG_00513. DR PATRIC; 24245260; VBIBruNeo114381_1368. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C9VD19_BRUNE Unreviewed; 221 AA. AC C9VD19; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BANG_03071; OS Brucella neotomae 5K33. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520456; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5K33; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella neotomae 5K33."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999583; EEY05225.1; -; Genomic_DNA. DR ProteinModelPortal; C9VD19; -. DR EnsemblBacteria; EEY05225; EEY05225; BANG_03071. DR PATRIC; 24248362; VBIBruNeo114381_3281. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C9VKV3_9RHIZ Unreviewed; 203 AA. AC C9VKV3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAQG_00519; OS Brucella ceti B1/94. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520457; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B1/94; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella ceti B1/94."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999621; EEX86675.1; -; Genomic_DNA. DR ProteinModelPortal; C9VKV3; -. DR EnsemblBacteria; EEX86675; EEX86675; BAQG_00519. DR PATRIC; 24203344; VBIBruCet113143_1400. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C9VM66_9RHIZ Unreviewed; 221 AA. AC C9VM66; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAQG_03031; OS Brucella ceti B1/94. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520457; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B1/94; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella ceti B1/94."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999628; EEX88068.1; -; Genomic_DNA. DR ProteinModelPortal; C9VM66; -. DR EnsemblBacteria; EEX88068; EEX88068; BAQG_03031. DR PATRIC; 24206358; VBIBruCet113143_3227. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C9VUL0_BRUAO Unreviewed; 221 AA. AC C9VUL0; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BARG_03038; OS Brucella abortus bv. 9 str. C68. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520455; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C68; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 9 str. C68."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999639; EEX81020.1; -; Genomic_DNA. DR ProteinModelPortal; C9VUL0; -. DR EnsemblBacteria; EEX81020; EEX81020; BARG_03038. DR PATRIC; 24198162; VBIBruAbo122389_2623. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID C9VVV7_BRUAO Unreviewed; 203 AA. AC C9VVV7; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BARG_02376; OS Brucella abortus bv. 9 str. C68. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520455; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C68; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 9 str. C68."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999642; EEX81687.1; -; Genomic_DNA. DR ProteinModelPortal; C9VVV7; -. DR EnsemblBacteria; EEX81687; EEX81687; BARG_02376. DR PATRIC; 24199614; VBIBruAbo122389_3329. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID C9X2T6_NEIM8 Unreviewed; 205 AA. AC C9X2T6; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NMV_2272; OS Neisseria meningitidis serogroup C (strain 8013). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=604162; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8013; RX PubMed=19818133; DOI=10.1186/gb-2009-10-10-r110; RA Rusniok C., Vallenet D., Floquet S., Ewles H., Mouze-Soulama C., RA Brown D., Lajus A., Buchrieser C., Medigue C., Glaser P., Pelicic V.; RT "NeMeSys: a biological resource for narrowing the gap between sequence RT and function in the human pathogen Neisseria meningitidis."; RL Genome Biol. 10:R110.1-R110.13(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM999788; CAX51029.1; -; Genomic_DNA. DR RefSeq; YP_005879445.1; NC_017501.1. DR ProteinModelPortal; C9X2T6; -. DR EnsemblBacteria; CAX51029; CAX51029; NMV_2272. DR GeneID; 12393967; -. DR KEGG; nmt:NMV_2272; -. DR PATRIC; 36835397; VBINeiMen144578_2635. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21577 MW; 9E9249621D921C6B CRC64; MTFLPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKAL HGDELKREIA RCVAACQGSH TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYIASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID C9XC54_SALTD Unreviewed; 211 AA. AC C9XC54; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=STMMW_41161; OS Salmonella typhimurium (strain D23580). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=568708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D23580; RX PubMed=19901036; DOI=10.1101/gr.091017.109; RA Kingsley R.A., Msefula C.L., Thomson N.R., Kariuki S., Holt K.E., RA Gordon M.A., Harris D., Clarke L., Whitehead S., Sangal V., Marsh K., RA Achtman M., Molyneux M.E., Cormican M., Parkhill J., Maclennan C.A., RA Heyderman R.S., Dougan G.; RT "Epidemic multiple drug resistant Salmonella typhimurium causing RT invasive disease in sub-Saharan Africa have a distinct genotype."; RL Genome Res. 19:2279-2287(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN424405; CBG27129.1; -; Genomic_DNA. DR RefSeq; YP_005235120.1; NC_016854.1. DR ProteinModelPortal; C9XC54; -. DR EnsemblBacteria; CBG27129; CBG27129; STMMW_41161. DR PATRIC; 36730047; VBISalEnt111430_4393. DR HOGENOM; HOG000155781; -. DR BioCyc; SENT568708:GJDP-4197-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22983 MW; 803CF861FC550D88 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE SGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID C9XMJ3_CLODC Unreviewed; 210 AA. AC C9XMJ3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; Synonyms=thiE; OrderedLocusNames=CD196_1524; OS Clostridium difficile (strain CD196). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=645462; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CD196; RX PubMed=19781061; DOI=10.1186/gb-2009-10-9-r102; RA Stabler R.A., He M., Dawson L., Martin M., Valiente E., Corton C., RA Lawley T.D., Sebaihia M., Quail M.A., Rose G., Gerding D.N., RA Gibert M., Popoff M.R., Parkhill J., Dougan G., Wren B.W.; RT "Comparative genome and phenotypic analysis of Clostridium difficile RT 027 strains provides insight into the evolution of a hypervirulent RT bacterium."; RL Genome Biol. 10:R102.1-R102.15(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN538970; CBA62919.1; -; Genomic_DNA. DR RefSeq; YP_003214551.1; NC_013315.1. DR ProteinModelPortal; C9XMJ3; -. DR STRING; 645462.CD196_1524; -. DR EnsemblBacteria; CBA62919; CBA62919; CD196_1524. DR GeneID; 8466725; -. DR KEGG; cdc:CD196_1524; -. DR PATRIC; 19449369; VBICloDif125228_1599. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CDIF645462:GJED-1609-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23403 MW; 03240E6F4CFACA7E CRC64; MIDKESLKKC LKLYLVTDSE MLKGRDFYKC LEDAISSGIT TVQLREKNAS GREFLRKAMK LREITERYGV KFIINDRVDI ALICDADGVH VGQSDIDVRE VRKLIGNNKI LGVSARTLEE ATCAKNDGAD YLGVGSIFTT STKLDAKSAS FETVKEIKEK VDMPFVLIGG INLDNIDKLK CLESDGYAII SAILKAEDIS KEVEKWTLKI // ID C9XQY7_CLODC Unreviewed; 229 AA. AC C9XQY7; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 28. DE SubName: Full=Putative thiamine biosynthesis protein; GN Name=thiE2; OrderedLocusNames=CD196_1630; OS Clostridium difficile (strain CD196). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=645462; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CD196; RX PubMed=19781061; DOI=10.1186/gb-2009-10-9-r102; RA Stabler R.A., He M., Dawson L., Martin M., Valiente E., Corton C., RA Lawley T.D., Sebaihia M., Quail M.A., Rose G., Gerding D.N., RA Gibert M., Popoff M.R., Parkhill J., Dougan G., Wren B.W.; RT "Comparative genome and phenotypic analysis of Clostridium difficile RT 027 strains provides insight into the evolution of a hypervirulent RT bacterium."; RL Genome Biol. 10:R102.1-R102.15(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN538970; CBA63124.1; -; Genomic_DNA. DR RefSeq; YP_003214657.1; NC_013315.1. DR ProteinModelPortal; C9XQY7; -. DR STRING; 645462.CD196_1630; -. DR EnsemblBacteria; CBA63124; CBA63124; CD196_1630. DR GeneID; 8466723; -. DR KEGG; cdc:CD196_1630; -. DR PATRIC; 19449589; VBICloDif125228_1708. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CDIF645462:GJED-1716-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 229 AA; 27014 MW; F6F6025B5FFE2E92 CRC64; MYLITNRKLC SEERYLEVIK ESILSGVENI IIREKDLEYQ ELRKLYMKIK TKINCIDFQE QISDESLKTN INQKECRNKF KVNFIINSNI EFFEKVDCQG IHLPFKLFLN LIENKYNFNE NKILGLSLHK VEEVDYLEKL IRNQNIKIDY ITLSHIYETK CKEGLNPKGI ELLKEAKKIT DIKIIALGGI LPSNVKETLK YCDDFAIMST IMRSKDIKKT ISNYNEKLN // ID C9XTD9_CROTZ Unreviewed; 211 AA. AC C9XTD9; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ctu_03040; ORFNames=CTU_03040; OS Cronobacter turicensis (strain DSM 18703 / LMG 23827 / z3032). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=693216; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18703 / LMG 23827 / z3032; RA Tischler P., Lehner A., Rattei T., Stephan R.; RT "The complete genome sequence of Cronobacter turicensis."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN543093; CBA27191.1; -; Genomic_DNA. DR RefSeq; YP_003208667.1; NC_013282.2. DR ProteinModelPortal; C9XTD9; -. DR STRING; 413502.Ctu_03040; -. DR EnsemblBacteria; CBA27191; CBA27191; CTU_03040. DR GeneID; 8461868; -. DR KEGG; ctu:CTU_03040; -. DR PATRIC; 20401314; VBICroTur2449_0293. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CTUR693216:GI0P-324-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22825 MW; 2A825E188C7B0BFB CRC64; MMKPLFAPVP RRLGLYPVVD SVGWITRLLE AGVRTLQLRI KDKSEAEVEA DVAAAIALGQ RYHARLFIND YWRLAIKHQA YGVHLGQEDL ETADPDAVRR AGLRLGVSTH DDMEIDVALA VRPSYIALGH VFPTQTKQMP SAPQGLAQLA AHVERLGDYP TVAIGGISLE RAPAVLETGV GSIAVVSAIT HAPDWRAATQ RLLELAGAGD E // ID C9YEC3_9BURK Unreviewed; 539 AA. AC C9YEC3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=Csp_D29290; OS Curvibacter putative symbiont of Hydra magnipapillata. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Curvibacter. OX NCBI_TaxID=667019; RN [1] RP NUCLEOTIDE SEQUENCE. RA Chapman J.A., Kirkness E.F., Simakov O., Hampson S.E., Mitros T., RA Weinmaier T., Rattei T., Balasubramanian P.G., Borman J., Busam D., RA Disbennett K., Pfannkoch C., Sumin N., Sutton G., Viswanathan L., RA Walenz B., Goodstein D.M., Hellsten U., Kawashima T., Prochnik S.E., RA Putnam N.H., Shu S., Blumberg B., Dana C.E., Gee L., Kibler D.F., RA Law L., Lindgens D., Martinez D.E., Peng J., Wigge P.A., Bertulat B., RA Guder C., Nakamura Y., Ozbek S., Watanabe H., Khalturin K., RA Hemmrich G., Franke A., Augustin R., Fraune S., Hayakawa E., RA Hayakawa S., Hirose M., Hwang J., Ikeo K., Nishimiya-Fujisawa C., RA Ogura A., Takahashi T., Steinmetz P.R., Zhang X., Aufschnaiter R., RA Eder M.K., Gorny A.K., Salvenmoser W., Heimberg A.M., Wheeler B.M., RA Peterson K.J., Boettger A., Tischler P., Wolf A., Gojobori T., RA Remington K.A., Strausberg R.L., Venter J., Technau U., Hobmayer B., RA Bosch T.C., Holstein T.W., Fujisawa T., Bode H.R., David C.N., RA Rokhsar D.S., Steele R.E.; RT "The Dynamic genome of Hydra."; RL Nature 464:592-596(2010). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN543107; CBA31872.1; -; Genomic_DNA. DR ProteinModelPortal; C9YEC3; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 539 AA; 56188 MW; FA246C91CFB84AEB CRC64; MRAIPMGAKS TLDTEFARAP AGRRPVVWSI AGSDSGAGAG VQADLKALQA FGVHGCTALA AITAQSSVEV TRVEPVSAEL LDAQLAALAQ DMPPQAIKTG LLGSVDNLRV VCRWVDALRA QGHPVALVVD PVLGSTTGTP FVDEALLDAY CRQLLPRATL ITPNRREALR LLQAERADHP LHAAPAPELA PALQARWRLG TRERAPADGQ SAYDCFAVAI TGGDDARAQG LASDWLQSAQ ATGWLSLPRV DTAHHHGTGC TFASTAAAAL ASGYCVADAV VLAKMATTHA LRHAYAAGQG AGPVQALPDF AQHVGNLPWL QKTPATQTAF PDLTHPALGV YAVVDSVAWV RRVLAAGIRT VQLRIKDPIE PTLSAQIAES IAAAQATPGA QLFINDHWQL ALQLGAYGVH LGQEDLDTVD LDALRQAGVR LGLSTHSYWE VARAWALRPS YIACGPIFAT QSKDMPWIPQ SLDNLRFWAG VLPVPVVGIA GIDASNVMEV AATGAASAAV ISAITRSADP EAACVALMAG FTAGAATAS // ID C9YLP6_CLODR Unreviewed; 210 AA. AC C9YLP6; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; Synonyms=thiE; OrderedLocusNames=CDR20291_1499; OS Clostridium difficile (strain R20291). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=645463; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R20291; RX PubMed=19781061; DOI=10.1186/gb-2009-10-9-r102; RA Stabler R.A., He M., Dawson L., Martin M., Valiente E., Corton C., RA Lawley T.D., Sebaihia M., Quail M.A., Rose G., Gerding D.N., RA Gibert M., Popoff M.R., Parkhill J., Dougan G., Wren B.W.; RT "Comparative genome and phenotypic analysis of Clostridium difficile RT 027 strains provides insight into the evolution of a hypervirulent RT bacterium."; RL Genome Biol. 10:R102.1-R102.15(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN545816; CBE04103.1; -; Genomic_DNA. DR RefSeq; YP_003217995.1; NC_013316.1. DR ProteinModelPortal; C9YLP6; -. DR STRING; 645463.CDR20291_1499; -. DR EnsemblBacteria; CBE04103; CBE04103; CDR20291_1499. DR GeneID; 8470371; -. DR KEGG; cdl:CDR20291_1499; -. DR PATRIC; 19456908; VBICloDif78408_1603. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CDIF645463:GJP4-1579-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23403 MW; 03240E6F4CFACA7E CRC64; MIDKESLKKC LKLYLVTDSE MLKGRDFYKC LEDAISSGIT TVQLREKNAS GREFLRKAMK LREITERYGV KFIINDRVDI ALICDADGVH VGQSDIDVRE VRKLIGNNKI LGVSARTLEE ATCAKNDGAD YLGVGSIFTT STKLDAKSAS FETVKEIKEK VDMPFVLIGG INLDNIDKLK CLESDGYAII SAILKAEDIS KEVEKWTLKI // ID C9YM02_CLODR Unreviewed; 229 AA. AC C9YM02; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 29. DE SubName: Full=Putative thiamine biosynthesis protein; GN Name=thiE2; OrderedLocusNames=CDR20291_1605; OS Clostridium difficile (strain R20291). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=645463; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R20291; RX PubMed=19781061; DOI=10.1186/gb-2009-10-9-r102; RA Stabler R.A., He M., Dawson L., Martin M., Valiente E., Corton C., RA Lawley T.D., Sebaihia M., Quail M.A., Rose G., Gerding D.N., RA Gibert M., Popoff M.R., Parkhill J., Dougan G., Wren B.W.; RT "Comparative genome and phenotypic analysis of Clostridium difficile RT 027 strains provides insight into the evolution of a hypervirulent RT bacterium."; RL Genome Biol. 10:R102.1-R102.15(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN545816; CBE04289.1; -; Genomic_DNA. DR RefSeq; YP_003218100.1; NC_013316.1. DR ProteinModelPortal; C9YM02; -. DR STRING; 645463.CDR20291_1605; -. DR EnsemblBacteria; CBE04289; CBE04289; CDR20291_1605. DR GeneID; 8470369; -. DR KEGG; cdl:CDR20291_1605; -. DR PATRIC; 19457124; VBICloDif78408_1710. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CDIF645463:GJP4-1686-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 229 AA; 27014 MW; F6F6025B5FFE2E92 CRC64; MYLITNRKLC SEERYLEVIK ESILSGVENI IIREKDLEYQ ELRKLYMKIK TKINCIDFQE QISDESLKTN INQKECRNKF KVNFIINSNI EFFEKVDCQG IHLPFKLFLN LIENKYNFNE NKILGLSLHK VEEVDYLEKL IRNQNIKIDY ITLSHIYETK CKEGLNPKGI ELLKEAKKIT DIKIIALGGI LPSNVKETLK YCDDFAIMST IMRSKDIKKT ISNYNEKLN // ID C9YTY8_STRSW Unreviewed; 214 AA. AC C9YTY8; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SCAB_67781; OS Streptomyces scabies (strain 87.22) (Streptomyces scabiei). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=680198; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=87.22; RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161; RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., RA Parry R.J., Loria R.; RT "Streptomyces scabies 87-22 contains a coronafacic acid-like RT biosynthetic cluster that contributes to plant-microbe interactions."; RL Mol. Plant Microbe Interact. 23:161-175(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN554889; CBG73776.1; -; Genomic_DNA. DR RefSeq; YP_003492316.1; NC_013929.1. DR ProteinModelPortal; C9YTY8; -. DR EnsemblBacteria; CBG73776; CBG73776; SCAB_67781. DR GeneID; 8843551; -. DR KEGG; scb:SCAB_67781; -. DR PATRIC; 35329244; VBIStrSca144334_6672. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; SSCA680198:GJ76-6635-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22722 MW; 7119B294A7A8B2DE CRC64; MPDAAARLAD ARLYLCTDAR KRQGDLPEFL DAVLGGGVDI VQLRDKGMEA AEELEHLQVL ADACRRHGRL LAVNDRADVA HAIGADVLHL GQGDLPVPAA RAVLGDRVLV GRSTHAEEEA AAAAVQEGVD YFCTGPCWPT PTKPGRHAPG LDLVRYTARL GTDRPWFAIG GIDLGNLDEV VEAGARRVVV VRALTEADDP GAAAAEFGKR LRAL // ID D0AZG3_BRUAO Unreviewed; 203 AA. AC D0AZG3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAUG_2278; OS Brucella abortus NCTC 8038. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=575591; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 8038; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Sangari F.J., RA Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella abortus NCTC 8038."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG703764; EEW80464.1; -; Genomic_DNA. DR ProteinModelPortal; D0AZG3; -. DR EnsemblBacteria; EEW80464; EEW80464; BAUG_2278. DR PATRIC; 24162469; VBIBruAbo97623_2573. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D0B1H1_BRUAO Unreviewed; 221 AA. AC D0B1H1; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAUG_2972; OS Brucella abortus NCTC 8038. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=575591; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 8038; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Sangari F.J., RA Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella abortus NCTC 8038."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG703766; EEW79420.1; -; Genomic_DNA. DR ProteinModelPortal; D0B1H1; -. DR EnsemblBacteria; EEW79420; EEW79420; BAUG_2972. DR PATRIC; 24164100; VBIBruAbo97623_3369. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D0BDD1_BRUSS Unreviewed; 203 AA. AC D0BDD1; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAVG_1272; OS Brucella suis bv. 4 str. 40. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520488; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=40; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella suis bv. 4 str. 40."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG703793; EEW91753.1; -; Genomic_DNA. DR ProteinModelPortal; D0BDD1; -. DR EnsemblBacteria; EEW91753; EEW91753; BAVG_1272. DR PATRIC; 24293175; VBIBruSui38587_0789. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D0BIR9_BRUSS Unreviewed; 221 AA. AC D0BIR9; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAVG_2907; OS Brucella suis bv. 4 str. 40. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520488; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=40; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella suis bv. 4 str. 40."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG703795; EEW89258.1; -; Genomic_DNA. DR ProteinModelPortal; D0BIR9; -. DR EnsemblBacteria; EEW89258; EEW89258; BAVG_2907. DR PATRIC; 24296853; VBIBruSui38587_3228. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D0BKI3_9LACT Unreviewed; 217 AA. AC D0BKI3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0446_00468; OS Granulicatella elegans ATCC 700633. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Granulicatella. OX NCBI_TaxID=626369; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700633; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Sibley C.D., Field T.R., Grinwis M., RA Eshaghurshan C.S., Surette M.G., Haas B., Nusbaum C., Birren B.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700633; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R., RA Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Granulicatella elegans ATCC 700633."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACRF02000013; EEW93586.1; -; Genomic_DNA. DR ProteinModelPortal; D0BKI3; -. DR EnsemblBacteria; EEW93586; EEW93586; HMPREF0446_00468. DR PATRIC; 26725196; VBIGraEle24208_0578. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23999 MW; 97D83FD1142D1EBC CRC64; MKKLDKILAL YLVTARYDWK EEDFLNKVEE ACRSGVTLVQ LREKECSTRE YYELAQKVKT ITDTYQIPLM IDDRVDICLA IDASGVHIGA DELPVEVVRK LIGKDKILGV TAKTVERALE AEQHGADYLG VGAIYPTTTK VITQPTSIET LREIATTVTI PIVAIGGIKE DNMEPLKGTG IAGIAIVSEI MKAQDIKQKC YCLRKKVTEI LGGEANE // ID D0BTM3_FUSNU Unreviewed; 206 AA. AC D0BTM3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0406_01607; OS Fusobacterium nucleatum subsp. animalis 3_1_33. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469603; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_33; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 3_1_33."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACQE02000010; EEW94375.1; -; Genomic_DNA. DR ProteinModelPortal; D0BTM3; -. DR EnsemblBacteria; EEW94375; EEW94375; HMPREF0406_01607. DR PATRIC; 30285883; VBIFusSp21658_1640. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22909 MW; 9D1FE192D41DE97E CRC64; MKLKDCKIYL VTDEKSCNGK NFYKCIEESI KGGVKIVQLR EKNISTKDFY EKALKVKEIC KNYGVLFIIN DRLDITQAVE ADGVHLGQSD MPIEKAREIL KDKFLIGATA RNIEEAKKAE LLGADYIGSG AIFGTSTKDN AKKLEMEDLK KIVNSVKIPV FAIGGININN VWMLKNIGLQ GICSVSGILS EKDCKKAVEN ILKNFN // ID D0BTM9_FUSNU Unreviewed; 206 AA. AC D0BTM9; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 13-NOV-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF0406_01613; OS Fusobacterium nucleatum subsp. animalis 3_1_33. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469603; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_33; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 3_1_33."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACQE02000010; EEW94381.1; -; Genomic_DNA. DR ProteinModelPortal; D0BTM9; -. DR EnsemblBacteria; EEW94381; EEW94381; HMPREF0406_01613. DR PATRIC; 30285895; VBIFusSp21658_1646. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 23932 MW; D80B78263413E9F8 CRC64; MIENKIKLNI ISNRKLCENE NLEKQIEKIF SAYQRKIILE NFEIVSLTLR EKDLNKNKYL KLVEKIYPIC QKYRIDLILH QNYDLRLDNK YNIKGLHLSY NTFKSLNKNI REELIRKYKK IGVSIHSVDE AKEVENLGAN YVVAGHIFKT DCKKALEPRG LKFIQELSVI LTIPIFAIGG INQENSHLVI NSGAFGVCMM SSLMKD // ID D0BXQ5_9GAMM Unreviewed; 203 AA. AC D0BXQ5; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0014_00916; OS Acinetobacter sp. RUH2624. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=575564; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RUH2624; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Dijkshoorn L., Haas B., Nusbaum C., RA Birren B.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RUH2624; RX PubMed=23144699; DOI=10.1371/journal.pone.0046984; RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S., RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L., RA Seifert H., Dijkshoorn L.; RT "The success of acinetobacter species; genetic, metabolic and RT virulence attributes."; RL PLoS ONE 7:E46984-E46984(2012). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RUH2624; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Dijkshoorn L., Walker B., RA Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter sp. RUH2624."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACQF02000022; EEX00678.1; -; Genomic_DNA. DR ProteinModelPortal; D0BXQ5; -. DR EnsemblBacteria; EEX00678; EEX00678; HMPREF0014_00916. DR PATRIC; 24350894; VBIAciSp90504_0896. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21661 MW; B4AEBFB4D64EFF6C CRC64; MRGLYLITND DPIELLLEKL DAALATHQIA ILQYRRKKVD KADQPAEVEQ IKGLCEKYQV PFVINDDLKL AAKFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID D0C161_9GAMM Unreviewed; 300 AA. AC D0C161; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 11-DEC-2013, entry version 25. DE SubName: Full=Mutator mutT protein; GN ORFNames=HMPREF0014_02122; OS Acinetobacter sp. RUH2624. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=575564; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RUH2624; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Dijkshoorn L., Haas B., Nusbaum C., RA Birren B.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RUH2624; RX PubMed=23144699; DOI=10.1371/journal.pone.0046984; RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S., RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L., RA Seifert H., Dijkshoorn L.; RT "The success of acinetobacter species; genetic, metabolic and RT virulence attributes."; RL PLoS ONE 7:E46984-E46984(2012). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RUH2624; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Dijkshoorn L., Walker B., RA Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter sp. RUH2624."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACQF02000021; EEW99515.1; -; Genomic_DNA. DR ProteinModelPortal; D0C161; -. DR EnsemblBacteria; EEW99515; EEW99515; HMPREF0014_02122. DR PATRIC; 24353331; VBIAciSp90504_2085. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 300 AA; 34336 MW; ABF6855946ED80C0 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTRDQL VNLNFPKANK DIIKRLYWPH FIKISATLTL PENDETLVYW RSEKDNVSED DLEKLALLDT NQLSKLIMNV DVWHKLKPDL KSRIRTVHLK QSQLMSLHKG DLEVGVRFIA ACHDAVSLQH AQQIGCDAVF VSPVKVTETH PDAIALGWDR FADLIDKCQI PVFALGGMSP DDLATAQQYG AYGLAGIRNF // ID D0C5L5_ACIBA Unreviewed; 303 AA. AC D0C5L5; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Mutator mutT protein; DE EC=3.6.1.-; GN ORFNames=HMPREF0010_00045; OS Acinetobacter baumannii ATCC 19606 = CIP 70.34. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=575584; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19606; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Peleg A., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Acinetobacter baumannii strain ATCC 19606."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704572; EEX04280.1; -; Genomic_DNA. DR ProteinModelPortal; D0C5L5; -. DR EnsemblBacteria; EEX04280; EEX04280; HMPREF0010_00045. DR PATRIC; 24329640; VBIAciBau3967_0482. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 303 AA; 34683 MW; 03271CBBEFCF794D CRC64; MSRKMPKPIV DVAIAILIHR GKILVGWRGE QQHQGGKHEF PGGKVEQGET PEEACRREIY EEVGIGLKDW HQFDYIHHEY DDIIVNLHLF HSYVPDELLN LIHQPWTWYT REQLLHLNFP KANKDIIKRL YWPHFIKISH TLTSVENSDA LLYWRIEDEF GPREVEQLTA LDEGQRSNLI INVDIWQQLS SELKKQIKTV HLKQSQLMSL HKGDLEVGIR FIAACHDAVS LQHAQQIGCD AVFVSPVKVT ATHPDVSALG WDRFADLIEK CQIPVFALGG MSPDDLATAQ QHGAYGLAGI RNF // ID D0CBV8_ACIBA Unreviewed; 203 AA. AC D0CBV8; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=F911_01178, HMPREF0010_02238; OS Acinetobacter baumannii ATCC 19606 = CIP 70.34. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=575584; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19606; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Peleg A., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Acinetobacter baumannii strain ATCC 19606."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 70.34; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B., RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A., RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter baumannii CIP 70.34T."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704575; EEX03196.1; -; Genomic_DNA. DR EMBL; APRG01000011; ENW75897.1; -; Genomic_DNA. DR ProteinModelPortal; D0CBV8; -. DR EnsemblBacteria; EEX03196; EEX03196; HMPREF0010_02238. DR EnsemblBacteria; ENW75897; ENW75897; F911_01178. DR PATRIC; 24334006; VBIAciBau3967_2005. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21750 MW; C30389D6687A22BE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKVD KADQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID D0CPX8_9RHOB Unreviewed; 206 AA. AC D0CPX8; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=SL1157_2717; OS Silicibacter lacuscaerulensis ITI-1157. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=644107; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ITI-1157; RA Zinser E., Buchan A., Ferriera S.F., Johnson J.J., Kravitz S.K., RA Beeson K.B., Sutton G.S., Rogers Y.-H.R., Friedman R.F., Frazier M.F., RA Venter J.C.V.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704596; EEX10655.1; -; Genomic_DNA. DR ProteinModelPortal; D0CPX8; -. DR EnsemblBacteria; EEX10655; EEX10655; SL1157_2717. DR PATRIC; 28600181; VBISilLac12138_2501. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 21906 MW; 0815886158FD6DF7 CRC64; MDTPEQPQIY LITPPTIDPA TFPDRLARVL DGTEIACIRL ALAGSDEDAI ARAADACREV AHARDVALVI SNHVLLAQRL GLDGVHLDDA ARSVRAARKE LGADAIVGSF CGTSRHDGMT AGEAGADYVA FGPVGDLSLG KGTRAERDLF QWWSEMIEVP VVAEGGLTPE LVADLAPCTD FFGVGDEIWG DDDPLRALDT LLAPMR // ID D0CSR2_9RHOB Unreviewed; 198 AA. AC D0CSR2; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SL1157_1135; OS Silicibacter lacuscaerulensis ITI-1157. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=644107; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ITI-1157; RA Zinser E., Buchan A., Ferriera S.F., Johnson J.J., Kravitz S.K., RA Beeson K.B., Sutton G.S., Rogers Y.-H.R., Friedman R.F., Frazier M.F., RA Venter J.C.V.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704596; EEX09099.1; -; Genomic_DNA. DR ProteinModelPortal; D0CSR2; -. DR EnsemblBacteria; EEX09099; EEX09099; SL1157_1135. DR PATRIC; 28597090; VBISilLac12138_0852. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 198 AA; 22240 MW; 7A0271CC1B6327DE CRC64; MTLDRFYPIF DHTDWLRRML PLGVKLVQLR IKDQPDAVVR AEIATAQALC RDHGAVLVVN DYWQAAIDAG CDWIHLGQED LDEADLPAIR KAGLKLGVST HDDDELERVL SMDPDYVALG PVYPTILKKM KWHQQGLPRV TEWKRRVGDI PLVGIGGMSV ERAPGVFQAG ADIVSVVTDI TLNPDPEARV RQWIEVTR // ID D0D1F1_9RHOB Unreviewed; 206 AA. AC D0D1F1; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=CSE45_1566; OS Citreicella sp. SE45. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Citreicella. OX NCBI_TaxID=501479; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SE45; RA Buchan A., Ferriera S.F., Johnson J.J., Kravitz S.K., Beeson K.B., RA Sutton G.S., Rogers Y.-H.R., Friedman R.F., Frazier M.F., RA Venter J.C.V.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704599; EEX13782.1; -; Genomic_DNA. DR ProteinModelPortal; D0D1F1; -. DR EnsemblBacteria; EEX13782; EEX13782; CSE45_1566. DR PATRIC; 27088672; VBICitSp11713_1759. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 21856 MW; 44C82B3AAD04FFC5 CRC64; MAETDLPQLY LITPPEFDLS EFPARLDAVL QAAEIACLRL ALATRDEDKL LRAADAVREI AHAHDVALVI DTHVVLAQRL GLDGVHLTDG SRSVRHARKE LGPDAIVGAF CGASRHDGMG AAEGGADYVS FGPLSGESLG DGTLADRDLF QWWSEMIEVP VVAEGGLTPE LVASLTPVTD FFGIGEEIWS AEDPVAALAA LTAAMR // ID D0D2M6_9RHOB Unreviewed; 201 AA. AC D0D2M6; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 16-OCT-2013, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=CSE45_1997; OS Citreicella sp. SE45. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Citreicella. OX NCBI_TaxID=501479; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SE45; RA Buchan A., Ferriera S.F., Johnson J.J., Kravitz S.K., Beeson K.B., RA Sutton G.S., Rogers Y.-H.R., Friedman R.F., Frazier M.F., RA Venter J.C.V.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704599; EEX14985.1; -; Genomic_DNA. DR ProteinModelPortal; D0D2M6; -. DR EnsemblBacteria; EEX14985; EEX14985; CSE45_1997. DR PATRIC; 27089522; VBICitSp11713_2180. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22288 MW; B81A1D891F385056 CRC64; MRLDPFYLIV GHVSELELLV PRGVRLVQLR LKGAEDREIR RQIARARDLC AVHGAQLVVN DHWQAAMDLN CGAVHLGQED MDEADFAALR RRGVAFGLST HDEAELDRAL ALDPAYVALG PVWPTLLKKM KWGPQGLDRV RSWKRRAGSV PLVGIGGVTP ERLPELFEAG ADSAAVVTDI AQADDREARC DLWIEATAPW R // ID D0DRM3_LACFE Unreviewed; 213 AA. AC D0DRM3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0513_00237; OS Lactobacillus fermentum 28-3-CHN. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=575599; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=28-3-CHN; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Liu Y., Xu Q., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Lactobacillus fermentum 28-3-CHN."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704699; EEX26499.1; -; Genomic_DNA. DR ProteinModelPortal; D0DRM3; -. DR EnsemblBacteria; EEX26499; EEX26499; HMPREF0513_00237. DR PATRIC; 30718667; VBILacFer94112_0333. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22416 MW; C5F1FDE4EE087316 CRC64; MLFKNEILRC YLIGGSQDTH HDPDEFLTKV EAAMQAGITA FQYREKGTST LSKAETLALG QQVRELATKY GVPLFVDDDL ELAAAIKADG IHVGQKDQRI EEVLAAVSDQ LMVGYSCNTA AQVAHANQLN VDYIGTGPVF PTISKDDAGS ALGVDGLADF VEQSAHPVVA IGGISLDNVG ATLTSGCAGL SMISMVLGAD DVAGTVKKIL ELY // ID D0FN51_ERWPE Unreviewed; 214 AA. AC D0FN51; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 14-MAY-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EpC_02600; OS Erwinia pyrifoliae (strain Ep1/96). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=634499; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ep1/96; RX PubMed=20565991; DOI=10.1186/1471-2164-11-393; RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H., RA Knaust F., Geider K., Reinhardt R.; RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E. RT tasmaniensis with the pear pathogen E. pyrifoliae."; RL BMC Genomics 11:393-393(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP236842; CAX54018.1; -; Genomic_DNA. DR RefSeq; YP_002647297.1; NC_012214.1. DR ProteinModelPortal; D0FN51; -. DR STRING; 634499.EpC_02600; -. DR EnsemblBacteria; CAX54018; CAX54018; EpC_02600. DR GeneID; 8540406; -. DR KEGG; epy:EpC_02600; -. DR PATRIC; 20418670; VBIErwPyr67807_0263. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; EPYR634499:GJIP-284-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23269 MW; ED72E41EC054E8D6 CRC64; MSRGAFPTTA ARLGLYPVVD NVQWIARLLD TGVRTLQLRI KDRAEQQVEQ QVAEAIALGK RYQARLFIND YWRLAVKHQA YGVHLGQQDL DIADLDSIHA AGLRLGLSTH DDAELDRALV ERPSYIALGH VFPTQTKYMP SEPQGLAALT RYVKRLSGIP TVAIGGISLA RAPAVLATGV GSIAVVSAIT QASDWQAATR QLLALAEAQR PARV // ID D0GDI3_BRUML Unreviewed; 221 AA. AC D0GDI3; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 14-MAY-2014, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BASG_01981; OS Brucella melitensis bv. 2 str. 63/9. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520465; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=63/9; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella melitensis bv. 2 str. 63/9."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEM01000029; EEZ17414.1; -; Genomic_DNA. DR ProteinModelPortal; D0GDI3; -. DR EnsemblBacteria; EEZ17414; EEZ17414; BASG_01981. DR PATRIC; 35219203; VBIBruMel34509_1684. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23242 MW; 9838EBF5FD9C7A47 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAIEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D0GHJ3_BRUML Unreviewed; 203 AA. AC D0GHJ3; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BASG_01189; OS Brucella melitensis bv. 2 str. 63/9. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520465; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=63/9; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella melitensis bv. 2 str. 63/9."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEM01000055; EEZ18824.1; -; Genomic_DNA. DR ProteinModelPortal; D0GHJ3; -. DR EnsemblBacteria; EEZ18824; EEZ18824; BASG_01189. DR PATRIC; 35222315; VBIBruMel34509_3199. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D0GWA0_VIBMI Unreviewed; 418 AA. AC D0GWA0; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VII_003659; OS Vibrio mimicus MB451. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675806; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MB-451; RX PubMed=21078967; DOI=10.1073/pnas.1013825107; RA Hasan N.A., Grim C.J., Haley B.J., Chun J., Alam M., Taviani E., RA Hoq M., Munk A.C., Saunders E., Brettin T.S., Bruce D.C., RA Challacombe J.F., Detter J.C., Han C.S., Xie G., Nair G.B., Huq A., RA Colwell R.R.; RT "Comparative genomics of clinical and environmental Vibrio mimicus."; RL Proc. Natl. Acad. Sci. U.S.A. 107:21134-21139(2010). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADAF01000001; EEY39889.1; -; Genomic_DNA. DR ProteinModelPortal; D0GWA0; -. DR EnsemblBacteria; EEY39889; EEY39889; VII_003659. DR PATRIC; 36045324; VBIVibMim142692_2570. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 418 AA; 46832 MW; 62551399798852E6 CRC64; MTRLVFPRSS VELIGRVQYV LLQAKEQGFD IQNISLDVAT SDCFVLEAES TLLIGCDLCP CEGTSELLDY YLQYLPEYRD IKARCKVKIG LRSHCDLGVD EWQVEENSCQ RITYPSLISN CQLDQHVAWV LAMLALGFPI EDSLCVARAA VSQKREVSRE TWPINLEFFP SVHSESELQP TKGFPAIDKS QFTLYPVVDD VSWIELLLKL GVKTVQLRIK DPMQVDLEEQ IVRAIDLGRE YNAQVFINDY WQLAIKHKAY GVHLGQEDLT TANLTELTQA GLRLGLSTHG YYELLNVACL QPSYIALGHI FPTTTKQMPS KPQGLVRLAA YQGLANQLSY HGQKGMPTVA IGGIDHSNIE EVLRCGVTSA AVVRAITQSA NPALAVHQLM FAFSGQKESE LRKQAKSYNM EWETSNVE // ID D0H1Z6_VIBCL Unreviewed; 440 AA. AC D0H1Z6; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VIJ_000433; OS Vibrio cholerae RC27. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675807; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RC27; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D., RA Vonstein V.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADAI01000021; EEY43025.1; -; Genomic_DNA. DR ProteinModelPortal; D0H1Z6; -. DR EnsemblBacteria; EEY43025; EEY43025; VIJ_000433. DR PATRIC; 36140010; VBIVibCho146253_0458. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48877 MW; 5602F84C24A2F3D8 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPHQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID D0HAL2_VIBMI Unreviewed; 420 AA. AC D0HAL2; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VMA_000002; OS Vibrio mimicus VM223. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675820; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VM223; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., RA Bartels D., Vonstein V.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VM223; RX PubMed=21078967; DOI=10.1073/pnas.1013825107; RA Hasan N.A., Grim C.J., Haley B.J., Chun J., Alam M., Taviani E., RA Hoq M., Munk A.C., Saunders E., Brettin T.S., Bruce D.C., RA Challacombe J.F., Detter J.C., Han C.S., Xie G., Nair G.B., Huq A., RA Colwell R.R.; RT "Comparative genomics of clinical and environmental Vibrio mimicus."; RL Proc. Natl. Acad. Sci. U.S.A. 107:21134-21139(2010). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADAJ01000001; EEY46647.1; -; Genomic_DNA. DR ProteinModelPortal; D0HAL2; -. DR EnsemblBacteria; EEY46647; EEY46647; VMA_000002. DR PATRIC; 36146788; VBIVibMim144207_0003. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 420 AA; 46827 MW; 5054FE808D6DF226 CRC64; MTRLVFPRSS VELIGRVQYV LLQAKVQGFD IQNISLDVAT SDCFVLEAES TLRIACDLCL CEDTSELLDY YLQYLPEHRD IEARCKVKIG LRSHSDLGVD EWQVEENSSQ RITYPYPSLI SNCQLDQHVA WVLAMLALGF SIADALCVAR AAMSQKQDVS RETWPINLES FPSVHSGSEL QATKGFPAID KSQFTLYPVV DDVSWIELLL KLGVKTVQLR IKDPMQVDLE EQIVRAIDLG REYNAQVFIN DYWQIAIKHK AYGVHLGQED LTTANLTELA QAGLRLGLST HGYYELLNVA CSQPSYIALG HIFPTTTKQM PSKPQGLVRL AAYQGLANQL SYHGQKGMPT VAIGGIDHSN IEEVLRCGVT SAAVVRAITQ SANPALAVHQ LMFAFSGQKE SELRKQAKSY NMEWETSNVE // ID D0HLF0_VIBCL Unreviewed; 440 AA. AC D0HLF0; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VIG_000550; OS Vibrio cholerae INDRE 91/1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675808; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=INDRE 91/1; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D., RA Vonstein V.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADAK01000031; EEY49521.1; -; Genomic_DNA. DR ProteinModelPortal; D0HLF0; -. DR EnsemblBacteria; EEY49521; EEY49521; VIG_000550. DR PATRIC; 36156345; VBIVibCho146581_0619. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID D0I0V9_VIBCL Unreviewed; 440 AA. AC D0I0V9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VIH_002426; OS Vibrio cholerae CT 5369-93. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675809; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CT 5369-93; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., RA Bartels D., Vonstein V.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADAL01000245; EEY50672.1; -; Genomic_DNA. DR EnsemblBacteria; EEY50672; EEY50672; VIH_002426. DR PATRIC; 36168293; VBIVibCho138865_2660. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 49139 MW; 4473C67B06002D43 CRC64; MVRLVFPRHL SALIAHVQYA LLQAKEQGFA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQEETSEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGNAAEQLII YSSETHRLNS KLNQHLAWVL ATLTLDFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLYT QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQC DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID RSNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSVFAD FVDAEYKLMP ASESCEPLSC LAREVADAHR // ID D0I387_GRIHO Unreviewed; 223 AA. AC D0I387; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 11-DEC-2013, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VHA_000218; OS Grimontia hollisae CIP 101886. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Grimontia. OX NCBI_TaxID=675812; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 101886; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., RA Bartels D., Vonstein V.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADAQ01000006; EEY74129.1; -; Genomic_DNA. DR ProteinModelPortal; D0I387; -. DR EnsemblBacteria; EEY74129; EEY74129; VHA_000218. DR PATRIC; 36170350; VBIGriHol144062_0222. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 223 AA; 24084 MW; 8F7D4C1F7C716EC8 CRC64; MTPVYSFPRL DGQFGPLYPV VDDIDLLKRL LALGVRTVQL RVKDPNHPDL DAMINEAVTF GRLCQAQVFI NDHWEKALEA GAYGLHLGQD DLKTADLDAI ARAGIRLGVS TRTAQELELA LSLAPSYLAI GHIFPTPTKQ MPTPPQGVAQ LSKHLATVAG KIPTVAIGGI DLATAPEVWQ TGVDAIAVVR AVTQSCDLAA TLQAFSELLT EEARDERIVF HES // ID D0IMB2_9VIBR Unreviewed; 423 AA. AC D0IMB2; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 11-DEC-2013, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VOA_002805; OS Vibrio sp. RC586. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675815; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RC586; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Chertkov O., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., RA Bartels D., Vonstein V.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADBD01000014; EEY98030.1; -; Genomic_DNA. DR ProteinModelPortal; D0IMB2; -. DR EnsemblBacteria; EEY98030; EEY98030; VOA_002805. DR PATRIC; 36184509; VBIVibSp142240_3471. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 423 AA; 47016 MW; 7A4BAF6AE2143706 CRC64; MARLVFPRHM AAFTGRVQSV LFLAEKQGFS IQHISLDVGD SPYFVLIGGC SVVIGSDVCS LENASEPLDY YIQYLAGQPV HQANCTVKVG LPDPRDGDFQ IDQWFTKANI PQQISYPFVH TSLNYQQNQH LAWVLALLAL DFPLEDTLCI ARAAMSQAQY VSRETWPTQW QHFPVVKTAW HSAKVVAFPA IDKAKFTLYP VVDDVAWIEL LLKLGVTTVQ LRIKDPSRQD LEAQISRAVS LGREYDAQVF INDYWQLAMK YHAYGVHLGQ EDLTCANLEL LSQAGLRLGL STHGYFELVN AACIQPSYIA LGHIFPTTTK QMPSRPQGLV RLAAYQIVAD QMPYHGDLGI PTVAIGGIEL SNIRDVLACG VTSAAVVRAI TLAENPAFAV HQLFSAFYEC KEKQFLDLKQ KIATLTREAS DAQ // ID D0IS00_HELP1 Unreviewed; 219 AA. AC D0IS00; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiB; Synonyms=thiE; OrderedLocusNames=KHP_0485; OS Helicobacter pylori (strain 51). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=290847; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=51; RA Kim S., Lee W.K., Choi S.H., Kang S., Park H.S., Kim Y.S., Lee S.G., RA Byun E.Y., Jeong J.E., Park Y.H., Lee E.J., Kim J.S., Ryu B.D., RA Lee Y.S., Hahn Y., Yeom Y.I., Park S.G., Youn H.S., Ko G.H., RA Choi M.B., Park C.H., Lim J.Y., Bae D.W., Song J.Y., Park J.U., RA Kang H.L., Baik S.C., Cho M.J., Yoo H.S., Rhee K.H.; RT "Genome sequence of Helicobacter pylori strain 51."; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000012; ACX97693.1; -; Genomic_DNA. DR RefSeq; YP_005792881.1; NC_017382.1. DR ProteinModelPortal; D0IS00; -. DR EnsemblBacteria; ACX97693; ACX97693; KHP_0485. DR GeneID; 12910313; -. DR KEGG; hpd:KHP_0485; -. DR PATRIC; 36827824; VBIHelPyl144621_0533. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; HPYL290847:GLE5-497-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23816 MW; C296551039D13C37 CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLALQDP IGIKQLALEC QKLCQKYGAP FIVNDEVQLA LELKADGVHV GQEDMAIEEV MTLCKKRQFI GLSVNTLEQA LKARHLDAVA YLGVGPIFPT QSKKDKQVVG VELLKKIKDS GVKKPLIAIG GITTHNASKL REYGGIAVIS AITQAKDKAL AVGKLLNDA // ID D0J0Q4_COMT2 Unreviewed; 313 AA. AC D0J0Q4; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CtCNB1_2979; OS Comamonas testosteroni (strain CNB-2). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=688245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNB-2; RX PubMed=19734336; DOI=10.1128/AEM.00933-09; RA Ma Y.F., Zhang Y., Zhang J.Y., Chen D.W., Zhu Y., Zheng H., Wang S.Y., RA Jiang C.Y., Zhao G.P., Liu S.J.; RT "The complete genome of Comamonas testosteroni reveals its genetic RT adaptations to changing environments."; RL Appl. Environ. Microbiol. 75:6812-6819(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001220; ACY33725.1; -; Genomic_DNA. DR RefSeq; YP_003279021.1; NC_013446.2. DR ProteinModelPortal; D0J0Q4; -. DR STRING; 688245.CtCNB1_2979; -. DR EnsemblBacteria; ACY33725; ACY33725; CtCNB1_2979. DR GeneID; 8562014; -. DR KEGG; ctt:CtCNB1_2979; -. DR PATRIC; 35267040; VBIComTes153857_3172. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CTES543891:GJCV-3039-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 137 141 HMP-PP binding (By similarity). FT METAL 170 170 Magnesium (By similarity). FT METAL 189 189 Magnesium (By similarity). FT BINDING 169 169 HMP-PP (By similarity). FT BINDING 211 211 HMP-PP (By similarity). FT BINDING 240 240 HMP-PP (By similarity). FT BINDING 269 269 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 313 AA; 33387 MW; CC2AFF85E9519EEA CRC64; MDSAEIKALA QAIIHQHSAN FGARLHHDAN SVELTPQPVP PALRQEPAYL AALEACSQLG FIAVDAQTLA QAWQCQSERT NQFDVTHWPD DPRDFGLGKA DPALAFAHCP SELGLYGVLP TAEWVGRMAR AGVPTVQLRF KSGDQAAVAR EVKAAVEAVK GTNARLFIND HWQAALDAGA YGIHVGQEDL DVIGQRDLQT IRSSGTRLGV STHGYAEMVR AHAVQPSYIA LGAVFPTTLK KMATAPQGLA RLAAYVRLMQ QYPLVAIGGI SEDLFPAVRA TGVGSVAVVR ALVNAPDPEA AAQHLLQRMQ AAA // ID D0JIW7_YERPD Unreviewed; 224 AA. AC D0JIW7; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=YPD4_3292; OS Yersinia pestis (strain D106004). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=637382; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D106004; RX PubMed=19815893; DOI=10.4269/ajtmh.2009.09-0174; RA Zhang Z., Hai R., Song Z., Xia L., Liang Y., Cai H., Liang Y., RA Shen X., Zhang E., Xu J., Yu D., Yu X.J.; RT "Spatial variation of Yersinia pestis from Yunnan Province of China."; RL Am. J. Trop. Med. Hyg. 81:714-717(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001585; ACY60196.1; -; Genomic_DNA. DR RefSeq; YP_005506499.1; NC_017154.1. DR ProteinModelPortal; D0JIW7; -. DR EnsemblBacteria; ACY60196; ACY60196; YPD4_3292. DR GeneID; 12094376; -. DR KEGG; ypd:YPD4_3292; -. DR PATRIC; 36761475; VBIYerPes77623_4370. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; YPES637382:GLMX-3357-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID D0JTC9_YERP1 Unreviewed; 224 AA. AC D0JTC9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=YPD8_3292; OS Yersinia pestis (strain D182038). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=637385; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D182038; RX PubMed=19815893; DOI=10.4269/ajtmh.2009.09-0174; RA Zhang Z., Hai R., Song Z., Xia L., Liang Y., Cai H., Liang Y., RA Shen X., Zhang E., Xu J., Yu D., Yu X.J.; RT "Spatial variation of Yersinia pestis from Yunnan Province of China."; RL Am. J. Trop. Med. Hyg. 81:714-717(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001589; ACY63960.1; -; Genomic_DNA. DR RefSeq; YP_005510353.1; NC_017160.1. DR ProteinModelPortal; D0JTC9; -. DR EnsemblBacteria; ACY63960; ACY63960; YPD8_3292. DR GeneID; 12096548; -. DR KEGG; ypx:YPD8_3292; -. DR PATRIC; 36771791; VBIYerPes93679_4377. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; YPES637385:GLMY-3350-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID D0JZ35_HELP5 Unreviewed; 219 AA. AC D0JZ35; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 14-MAY-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPKB_0502; OS Helicobacter pylori (strain 52). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=684950; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=52; RA Kim S., Lee W.K., Choi S.H., Kang S., Park H.S., Kim Y.S., Lee S.G., RA Byun E.Y., Jeong J.E., Park Y.H., Lee E.J., Kim J.S., Ryu B.D., RA Lee Y.S., Hahn Y., Yeom Y.I., Park S.G., Youn H.S., Ko G.H., RA Choi M.B., Park C.H., Lim J.Y., Bae D.W., Song J.Y., Park J.U., RA Kang H.L., Baik S.C., Cho M.J., Yoo H.S., Rhee K.H.; RT "Genome sequence of Helicobacter pylori strain 52."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001680; ACX99105.1; -; Genomic_DNA. DR RefSeq; YP_005762021.1; NC_017354.1. DR ProteinModelPortal; D0JZ35; -. DR EnsemblBacteria; ACX99105; ACX99105; HPKB_0502. DR GeneID; 12340911; -. DR KEGG; hpz:HPKB_0502; -. DR PATRIC; 36824595; VBIHelPyl145372_0535. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; HPYL684950:GLET-490-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23796 MW; 7EC42433904E0AD2 CRC64; MFDANCLKLM FVAGSQDFCH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLALQDP IEIKQLALKC QKLCQKYGVP FIVNDEVKLA LELKADGVHV GQEDMAIEEV MTLCKKCQFI GLSVNTLEQA LKAHHLDGIA YLGVGPIFPT QSKKDKQVVG VELLKKIKDS GVKKPLIAIG GITTHNASKL REYGGIAVIS AITKAKDKAL AVGKLLKNA // ID D0K6Y0_STAAD Unreviewed; 213 AA. AC D0K6Y0; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SAAV_2145; OS Staphylococcus aureus (strain ED98). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=681288; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ED98; RX PubMed=19884497; DOI=10.1073/pnas.0909285106; RA Lowder B.V., Guinane C.M., Ben Zakour N.L., Weinert L.A., RA Conway-Morris A., Cartwright R.A., Simpson A.J., Rambaut A., Nubel U., RA Fitzgerald J.R.; RT "Recent human-to-poultry host jump, adaptation, and pandemic spread of RT Staphylococcus aureus."; RL Proc. Natl. Acad. Sci. U.S.A. 106:19545-19550(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001781; ACY11990.1; -; Genomic_DNA. DR RefSeq; YP_003282996.1; NC_013450.1. DR ProteinModelPortal; D0K6Y0; -. DR SMR; D0K6Y0; 4-209. DR STRING; 681288.SAAV_2145; -. DR PRIDE; D0K6Y0; -. DR EnsemblBacteria; ACY11990; ACY11990; SAAV_2145. DR GeneID; 8614884; -. DR KEGG; sad:SAAV_2145; -. DR PATRIC; 32448358; VBIStaAur139507_2110. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR681288:GJ8Z-2118-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D0KDN8_PECWW Unreviewed; 213 AA. AC D0KDN8; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Pecwa_0219; OS Pectobacterium wasabiae (strain WPP163). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pectobacterium. OX NCBI_TaxID=561231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WPP163; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Balakrishnan V., Glasner J., Perna N.T.; RT "Complete sequence of Pectobacterium wasabiae WPP163."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001790; ACX86074.1; -; Genomic_DNA. DR RefSeq; YP_003257681.1; NC_013421.1. DR ProteinModelPortal; D0KDN8; -. DR STRING; 561231.Pecwa_0219; -. DR EnsemblBacteria; ACX86074; ACX86074; Pecwa_0219. DR GeneID; 8528577; -. DR KEGG; pwa:Pecwa_0219; -. DR PATRIC; 32274700; VBIPecWas23660_0210. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PWAS561231:GHO0-227-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23203 MW; 0BBD83BC0BD80EA2 CRC64; MTDLMPFAPT AQRLGLYPVV DSVEWVERLL GVGVKTIQLR IKDRSDEQAE ADVIQAIALG RRYQAQLFIN DYWKLAVKHQ AYGVHLGQED LDTADLVAIK EAGLRLGVST HDDRELARAV AINPSYIALG HIFPTQTKDM PSAPQGLAEL TRHIADLQGR FPTVAIGGIS IGKVPAVLET GVGSIAVVSA ITQALDWRQA TTTLLKMIEG REV // ID D0KVI8_HALNC Unreviewed; 352 AA. AC D0KVI8; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 13-NOV-2013, entry version 28. DE SubName: Full=NUDIX hydrolase; GN OrderedLocusNames=Hneap_1996; OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus OS neapolitanus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Halothiobacillaceae; Halothiobacillus. OX NCBI_TaxID=555778; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23641 / c2; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Davenport K., Brettin T., RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Kerfeld C., Cannon G., Heinhort S.; RT "Complete sequence of Halothiobacillus neapolitanus c2."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001801; ACX96818.1; -; Genomic_DNA. DR RefSeq; YP_003263865.1; NC_013422.1. DR ProteinModelPortal; D0KVI8; -. DR STRING; 555778.Hneap_1996; -. DR EnsemblBacteria; ACX96818; ACX96818; Hneap_1996. DR GeneID; 8535155; -. DR KEGG; hna:Hneap_1996; -. DR PATRIC; 32207956; VBIHalNea120669_2042. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HNEA555778:GIVV-2043-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 352 AA; 38184 MW; 3D697FCEB94DCC1B CRC64; MSPPEETRIA LAVLPAGPNQ AGLPQYWLER RPDSAHLGGM LAFPGGKCQP DESPTDALAR ELFEELGILP QASRLLMEIP WVYSANSSDL EGKPKSKHLR LIVYRVEKWQ GELHGREGQS VTAQTLDCSR HGEWMSALPP ANRGIVAALC LPPRIAITAA CGAGDAGFSV WHQALVKTAN ALRQQFRSSF GGRSSIVQLR PGRDLSMAQW TAAVATVQSF ELSAWVNASL DIAISCRADG VHLNRHRLAS VDREALANWR AQNRWVSASG HTLEEVRLAN EVGVDALLIS PILPTLSHPG ESGIGWAQFA ELTREATMPT YALGGILETH LPQVQMLAGQ GVAAIRGYWM DS // ID D0L053_HALNC Unreviewed; 216 AA. AC D0L053; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Hneap_1240; OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus OS neapolitanus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Halothiobacillaceae; Halothiobacillus. OX NCBI_TaxID=555778; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23641 / c2; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Davenport K., Brettin T., RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Kerfeld C., Cannon G., Heinhort S.; RT "Complete sequence of Halothiobacillus neapolitanus c2."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001801; ACX96076.1; -; Genomic_DNA. DR RefSeq; YP_003263123.1; NC_013422.1. DR ProteinModelPortal; D0L053; -. DR STRING; 555778.Hneap_1240; -. DR EnsemblBacteria; ACX96076; ACX96076; Hneap_1240. DR GeneID; 8534394; -. DR KEGG; hna:Hneap_1240; -. DR PATRIC; 32206370; VBIHalNea120669_1254. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HNEA555778:GIVV-1282-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23125 MW; 6DF266029D442379 CRC64; MRAEISMHHR LRGLYVITDT VQFKRDDLVR VVAEAIAGGA RIVQYRDKSD DLERRLAEAS ALRSLTLEHE VLFLINDDLD LAEAVAADGV HLGKEDSAIK AARDRLGSEA VIGASCYNSF ELAQDAVRAG ANYVAFGAFF PSRTKPDAVV ASIPLLIESK QKLGVPICAI GGITRQSAPE LIGAGADMLA VISAVFSATD IQAAARDFST LWPSTV // ID D0L645_GORB4 Unreviewed; 221 AA. AC D0L645; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Gbro_4391; OS Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / JCM 3198 / NCTC OS 10667) (Rhodococcus bronchialis). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=526226; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25592 / DSM 43247 / JCM 3198 / NCTC 10667; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Jando M., Schneider S., Goeker M., RA Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Gordonia bronchialis DSM 43247."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001802; ACY23531.1; -; Genomic_DNA. DR RefSeq; YP_003275424.1; NC_013441.1. DR ProteinModelPortal; D0L645; -. DR STRING; 526226.Gbro_4391; -. DR EnsemblBacteria; ACY23531; ACY23531; Gbro_4391. DR GeneID; 8553773; -. DR KEGG; gbr:Gbro_4391; -. DR PATRIC; 32188550; VBIGorBro114338_4510. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GBRO526226:GHJF-4433-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23197 MW; AC0D6BCB3C90AB97 CRC64; MTTARRCLDS AALYLCTDAR RERGDLVDFV AAALAGGVDI VQLRDKGSAG EQRFGVLEAR EELEILARLR AVTSAQNALL SVNDRADIAR LAGADVLHVG QGDLPPSVAR RIVGPEMVIG QSTHDADQAA AAIADDDVDY FCVGPCWTTP TKPGRQAAGL DLVRSVAASR PSKPWFAIGG IDAVRLPEVT DAGAERIVVV RAITAADDPT AAARELRSAA S // ID D0LFM2_HALO1 Unreviewed; 225 AA. AC D0LFM2; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Hoch_0014; OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Kofleriaceae; Haliangium. OX NCBI_TaxID=502025; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14365 / JCM 11303 / SMP-2; RX PubMed=21304682; DOI=10.4056/sigs.69.1277; RG US DOE Joint Genome Institute (JGI-PGF); RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., RA Lapidus A., Lucas S., Glavina Del Rio T., Nolan M., Tice H., RA Copeland A., Cheng J.F., Chen F., Bruce D., Goodwin L., Pitluck S., RA Mavromatis K., Pati A., Mikhailova N., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., RA Brettin T., Rohde M., Goker M., Bristow J., Markowitz V., Eisen J.A., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Haliangium ochraceum type strain (SMP- RT 2)."; RL Stand. Genomic Sci. 2:96-106(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001804; ACY12656.1; -; Genomic_DNA. DR RefSeq; YP_003264549.1; NC_013440.1. DR ProteinModelPortal; D0LFM2; -. DR STRING; 502025.Hoch_0014; -. DR EnsemblBacteria; ACY12656; ACY12656; Hoch_0014. DR GeneID; 8542384; -. DR KEGG; hoh:Hoch_0014; -. DR PATRIC; 32189710; VBIHalOch22000_0014. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HOCH502025:GI43-14-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 23700 MW; 01F0657FCDFD7F5A CRC64; MRWQQRLTGF YSILDSDDEQ LARLLVRPVE QGGAGATVMQ VRVKPPEPVS VAELLKVARM ARSVTARAGA LLVVDDHIDV ALSVDADGVH LGQDDLPLVE ARALVERWRP ERPFLIGVST HNRAQVEAAV RGGADYLGFG PVYATSSKRN PDPVQGIPGL QEAVQAAGAT PIVAIGGITP ERAEQVAAAG AAAACCISAV NRDAEPAQAG ARIGAAWTPL RQPPR // ID D0LJM9_HALO1 Unreviewed; 228 AA. AC D0LJM9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Hoch_4105; OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Kofleriaceae; Haliangium. OX NCBI_TaxID=502025; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14365 / JCM 11303 / SMP-2; RX PubMed=21304682; DOI=10.4056/sigs.69.1277; RG US DOE Joint Genome Institute (JGI-PGF); RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., RA Lapidus A., Lucas S., Glavina Del Rio T., Nolan M., Tice H., RA Copeland A., Cheng J.F., Chen F., Bruce D., Goodwin L., Pitluck S., RA Mavromatis K., Pati A., Mikhailova N., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., RA Brettin T., Rohde M., Goker M., Bristow J., Markowitz V., Eisen J.A., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Haliangium ochraceum type strain (SMP- RT 2)."; RL Stand. Genomic Sci. 2:96-106(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001804; ACY16603.1; -; Genomic_DNA. DR RefSeq; YP_003268496.1; NC_013440.1. DR ProteinModelPortal; D0LJM9; -. DR STRING; 502025.Hoch_4105; -. DR EnsemblBacteria; ACY16603; ACY16603; Hoch_4105. DR GeneID; 8546506; -. DR KEGG; hoh:Hoch_4105; -. DR PATRIC; 32197975; VBIHalOch22000_4114. DR eggNOG; NOG287972; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; HOCH502025:GI43-4136-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 183 183 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 22598 MW; 7167F93FE1D4AA2A CRC64; MSAARARLAR ARLYLIADRE VAGERDLAAL VEAALAAIPP AAAAVQLRAK GLGADALCAE AERLRALTER RQCALLINDR ADVATLVGAE GVHLPERGLS IARARALLGS DALIAASRHS AEGAAAAAAQ GADLVVCGPV WPTPSKPGAA GLGPEGLRRV ASAMAARASG PGAAPARLFA LGGVDGPERA RAAVAAGACG VAGIRVFVDA QDPGAAASAL YTAIAVRG // ID D0MD64_RHOM4 Unreviewed; 208 AA. AC D0MD64; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-APR-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rmar_2096; OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) OS (Rhodothermus obamensis). OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Rhodothermus. OX NCBI_TaxID=518766; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43812 / DSM 4252 / R-10; RX PubMed=21304669; DOI=10.4056/sigs.46736; RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., RA Saunders E., Han C., Bruce D., Goodwin L., Chain P., Pitluck S., RA Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Brettin T., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Rhodothermus marinus type strain (R- RT 10)."; RL Stand. Genomic Sci. 1:283-291(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001807; ACY48976.1; -; Genomic_DNA. DR RefSeq; YP_003291364.1; NC_013501.1. DR ProteinModelPortal; D0MD64; -. DR STRING; 518766.Rmar_2096; -. DR EnsemblBacteria; ACY48976; ACY48976; Rmar_2096. DR GeneID; 8568757; -. DR KEGG; rmr:Rmar_2096; -. DR PATRIC; 32318319; VBIRhoMar93821_2120. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RMAR518766:GJJ8-2138-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 131 133 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22127 MW; 9B4B86E19709AE78 CRC64; MLPRLLLIAD RFTDPHRARV VRRAVTAGVP WVQLRDHRVD PDTFARAAEA LVPVLQAENP NLLLSVNTHL EVAQRLGLGL HVGRRGPSVA EARRRLGSGT LLGYSAHDLD AARRAADEGA DYLLFSPVFP TASKPGVPAV GLEALAAVCR AVPIPVLALG GITPERVSAC LQQGAHGVAV VSAILDASDP EGAVRQFLAR TENALHHR // ID D0MJE0_RHOM4 Unreviewed; 220 AA. AC D0MJE0; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-APR-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rmar_1712; OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) OS (Rhodothermus obamensis). OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Rhodothermus. OX NCBI_TaxID=518766; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43812 / DSM 4252 / R-10; RX PubMed=21304669; DOI=10.4056/sigs.46736; RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., RA Saunders E., Han C., Bruce D., Goodwin L., Chain P., Pitluck S., RA Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Brettin T., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Rhodothermus marinus type strain (R- RT 10)."; RL Stand. Genomic Sci. 1:283-291(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001807; ACY48598.1; -; Genomic_DNA. DR RefSeq; YP_003290986.1; NC_013501.1. DR ProteinModelPortal; D0MJE0; -. DR STRING; 518766.Rmar_1712; -. DR EnsemblBacteria; ACY48598; ACY48598; Rmar_1712. DR GeneID; 8568364; -. DR KEGG; rmr:Rmar_1712; -. DR PATRIC; 32317529; VBIRhoMar93821_1732. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RMAR518766:GJJ8-1745-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23590 MW; 17A8F35F966BE3BC CRC64; MGKKPIGRLH VLTDFYFQQR YGHAELARLV IAGGADTVQF RQKFGGIRHK LYEARRTAAV CKEAGVPLII DDHIDIALAV EADGVHLGQE DFPVAEARRI LGPDFIIGAT ATTVEQAVEA WRAGADYIGF GPVFPTSSKA NPASVKGIEG LRQVCEAVPI PVIAIAGITV QRVRPVLEAG AYGVAVMTAI TTAPDPRAAT AQFRLEIESV LRALPETPRT // ID D0P8D9_BRUSS Unreviewed; 221 AA. AC D0P8D9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAEG_03081; OS Brucella suis bv. 5 str. 513. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520489; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=513; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella suis bv. 5 str. 513."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999716; EEY28543.1; -; Genomic_DNA. DR ProteinModelPortal; D0P8D9; -. DR EnsemblBacteria; EEY28543; EEY28543; BAEG_03081. DR PATRIC; 24299717; VBIBruSui73489_1231. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D0PAP2_BRUSS Unreviewed; 203 AA. AC D0PAP2; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAEG_00524; OS Brucella suis bv. 5 str. 513. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520489; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=513; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella suis bv. 5 str. 513."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999724; EEY29216.1; -; Genomic_DNA. DR ProteinModelPortal; D0PAP2; -. DR EnsemblBacteria; EEY29216; EEY29216; BAEG_00524. DR PATRIC; 24301163; VBIBruSui73489_1643. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D0PHP2_BRUSS Unreviewed; 221 AA. AC D0PHP2; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAFG_03069; OS Brucella suis bv. 3 str. 686. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520487; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=686; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella suis bv. 3 str. 686."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999734; EEY31796.1; -; Genomic_DNA. DR ProteinModelPortal; D0PHP2; -. DR EnsemblBacteria; EEY31796; EEY31796; BAFG_03069. DR PATRIC; 24285790; VBIBruSui102552_1323. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D0PNC8_BRUSS Unreviewed; 203 AA. AC D0PNC8; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAFG_02434; OS Brucella suis bv. 3 str. 686. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520487; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=686; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella suis bv. 3 str. 686."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999748; EEY33782.1; -; Genomic_DNA. DR ProteinModelPortal; D0PNC8; -. DR EnsemblBacteria; EEY33782; EEY33782; BAFG_02434. DR PATRIC; 24290174; VBIBruSui102552_3190. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D0RFZ2_9RHIZ Unreviewed; 221 AA. AC D0RFZ2; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BATG_03065; OS Brucella sp. F5/99. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=437701; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F5/99; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella sp. F5/99."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG663477; EEY25341.1; -; Genomic_DNA. DR ProteinModelPortal; D0RFZ2; -. DR EnsemblBacteria; EEY25341; EEY25341; BATG_03065. DR PATRIC; 24278796; VBIBruSp65954_1256. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D0RLK7_9RHIZ Unreviewed; 203 AA. AC D0RLK7; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BATG_02426; OS Brucella sp. F5/99. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=437701; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F5/99; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella sp. F5/99."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG663486; EEY27306.1; -; Genomic_DNA. DR ProteinModelPortal; D0RLK7; -. DR EnsemblBacteria; EEY27306; EEY27306; BATG_02426. DR PATRIC; 24283001; VBIBruSp65954_3314. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D0RPT6_9PROT Unreviewed; 199 AA. AC D0RPT6; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 13-NOV-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=HIMB114_00008180; OS alpha proteobacterium HIMB114. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster. OX NCBI_TaxID=684719; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIMB114; RA Rappe M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIMB114; RA Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., RA Giovannoni S.J., Rappe M.S., Brinkac L., Kim M., Beeson K., RA Ferriera S., Sutton G., Friedman R., Venter J.C.; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADAC02000001; EMH80428.1; -; Genomic_DNA. DR ProteinModelPortal; D0RPT6; -. DR EnsemblBacteria; EMH80428; EMH80428; HIMB114_00008180. DR PATRIC; 36034090; VBIAlpPro140191_0883. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 23156 MW; 81526DDD9A1BE273 CRC64; MKRIYLITPN ILTKKFYSFL PKVLASKKVK FLQLRCKSYS RSKIDTHLRK ILTITKKYNV KLIINDESSF VKKYKNTGFH LGQKDLIKKR NISNLDKNNY FGITCHNSIT LAKKALKFKP RYIAFGAFYP TKTKQVKYIA KKDILKKAKK FKTKVVAIGG ITNKNYKELI KSGADYIAIS GFIWKNKQFN PVQAIKLFK // ID D0RQM4_9PROT Unreviewed; 192 AA. AC D0RQM4; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 13-NOV-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=HIMB114_00011150; OS alpha proteobacterium HIMB114. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster. OX NCBI_TaxID=684719; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIMB114; RA Rappe M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIMB114; RA Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., RA Giovannoni S.J., Rappe M.S., Brinkac L., Kim M., Beeson K., RA Ferriera S., Sutton G., Friedman R., Venter J.C.; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADAC02000001; EMH80717.1; -; Genomic_DNA. DR ProteinModelPortal; D0RQM4; -. DR EnsemblBacteria; EMH80717; EMH80717; HIMB114_00011150. DR PATRIC; 36034684; VBIAlpPro140191_1172. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 192 AA; 22625 MW; 5BB01C4B3AF24E0E CRC64; MFKIFFYINE LNDIQKENLN QLKNINIIYR NYQKTDYLGN AFKLQDYCKK RKFRLYISND EKLAIKLRSY GLYIPNFNNK KKYLKSSLHL IGSAHNEIEL RKKINQGCKE IFISPIFNTY SDSNKIGKGL NFYQSLMLKF SKIHIHALGG INEKNIKKII LLKGRGFSSI SMIDKKMKKD FISYLNLIAT NL // ID D0S1L5_ACICA Unreviewed; 203 AA. AC D0S1L5; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0012_00201; OS Acinetobacter calcoaceticus RUH2202. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=575585; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RUH2202; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Dijkshoorn L., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Acinetobacter calcoaceticus strain RUH2202."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704949; EEY77332.1; -; Genomic_DNA. DR ProteinModelPortal; D0S1L5; -. DR EnsemblBacteria; EEY77332; EEY77332; HMPREF0012_00201. DR PATRIC; 35592475; VBIAciCal110308_1994. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21852 MW; 518B93484C5C3411 CRC64; MRGLYLITND DPIQLLLEKL DVALATKQVA ILQYRRKKIE KSNQPAEVEQ IKLLCEKYQV PFVINDDLEL AAEFGLGVHL GQSDGEITDA KSQLPQNVII GRTCLNSLEL AQKAIADGAT YIAFGAVYAT STKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID D0S233_ACICA Unreviewed; 300 AA. AC D0S233; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Mutator mutT protein; DE EC=3.6.1.-; GN ORFNames=HMPREF0012_00369; OS Acinetobacter calcoaceticus RUH2202. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=575585; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RUH2202; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Dijkshoorn L., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Acinetobacter calcoaceticus strain RUH2202."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704949; EEY77500.1; -; Genomic_DNA. DR ProteinModelPortal; D0S233; -. DR EnsemblBacteria; EEY77500; EEY77500; HMPREF0012_00369. DR PATRIC; 35592813; VBIAciCal110308_0151. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 300 AA; 34181 MW; 32C0F830371CD23D CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYEDII VNLHLFHSYV PDELLNLIHQ PWAWYTREQL LHLNFPKANK DIIKRLYWPH LIKISTMLTP VEGSDALLYW RIEEADADQR YLEQLSALDE NQLSNLIINT DFWQQLSPEL KKQIKTVHLK QSQLMNLHKG DLTVGVRYIA ACHNAVSLKQ AEQIGCDAVF ISPVKPTTTH SEALALGWES FADLAQNSQI PVFALGGVHP DDLATAQKHG AYGLAGIRNF // ID D0SC16_ACIJO Unreviewed; 299 AA. AC D0SC16; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Mutator mutT protein; DE EC=3.6.1.-; GN ORFNames=HMPREF0016_01389; OS Acinetobacter johnsonii SH046. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=575586; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH046; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Seifert H., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Acinetobacter johnsonii strain SH046."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704965; EEY96698.1; -; Genomic_DNA. DR ProteinModelPortal; D0SC16; -. DR EnsemblBacteria; EEY96698; EEY96698; HMPREF0016_01389. DR PATRIC; 35601948; VBIAciJoh101986_1251. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 299 AA; 33435 MW; B29FC1EAC1E69880 CRC64; MSKPLVQVAI AILLHQGKVL VGWRQAEQHQ GNKHEFPGGK VEAGETPEQG CRREVLEEVG IDIQDWHAFD CIQFEYDDVI VNLHLFHAVV SNHLLADIHS PWAWFKRAEL QDLNFPKANQ AILKRLYVAP VIKISDQIDL LKDLPEQQVL YWRVPASPEH ILKIAELSVE QLARVIVNIE LWKGLNPLQQ QAVAAIHLKQ SQLMQLSKGE LNVGQRYIAA CHDRSSAEHA QEIGCDALLL SPVLETLSHP NSETLGWEQL SLIAEEIHIP IFALGGLQLA DLAKAQSYGA YGIAGQRSI // ID D0SE52_ACIJO Unreviewed; 206 AA. AC D0SE52; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0016_02125; OS Acinetobacter johnsonii SH046. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=575586; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH046; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Seifert H., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Acinetobacter johnsonii strain SH046."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704967; EEY95712.1; -; Genomic_DNA. DR ProteinModelPortal; D0SE52; -. DR EnsemblBacteria; EEY95712; EEY95712; HMPREF0016_02125. DR PATRIC; 35603456; VBIAciJoh101986_2129. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22196 MW; D1A6AC239EEC1520 CRC64; MRGLYLITND DPLELLLAKL EGAMATREVA ILQYRRKKVP KEEQAYEVEY MKAMCAEYRV PFVINDDLEM AVKYGVGVHL GQGDGEVAEA VARLPKDAVI GRTCLNSIEL AEKAIAEGAT YVAFGAIYAT ETKPEAGNIG LETLKEAKAK LNVPICAIGG LTVENSSEVI EAGADLCAVI SDILGLSMSA IPDRIEQWAD LFASKA // ID D0SI59_ACIJU Unreviewed; 302 AA. AC D0SI59; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0026_00807; OS Acinetobacter junii SH205. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=575587; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH205; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Seifert H., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Acinetobacter junii strain SH205."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705011; EEY93531.1; -; Genomic_DNA. DR ProteinModelPortal; D0SI59; -. DR EnsemblBacteria; EEY93531; EEY93531; HMPREF0026_00807. DR PATRIC; 35607532; VBIAciJun5570_0688. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 302 AA; 34185 MW; 7FD20A1564668304 CRC64; MAKATVDVAI AILLHKSKVL VGWRQANQHQ GNKHEFPGGK IEEGETPEQA CRREVYEEVG IGLKEWHQFD VIRHEYEDII VTLHLFHAYV PDELLSLIHQ PWSWFSRDQL ADLNFPKANS TIIERLIWSH LIKISDQVDE LPKTNSQMYL RIESKDIEKL QQQLIKLSEQ QLLKLIVNVD VWQQLNTVLQ EKIKTVHLKQ SQLMQLKKGD LVVAKRYIAA CHDAVSVQHA HQIGCDAIFL SPVNPTATHP NSKVLGWDGF AALAQNSDIP VFALGGVAPA DLEQAQKHNA YGLAGIRQFS SI // ID D0SM96_ACIJU Unreviewed; 203 AA. AC D0SM96; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0026_00429; OS Acinetobacter junii SH205. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=575587; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH205; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Seifert H., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Acinetobacter junii strain SH205."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705011; EEY93153.1; -; Genomic_DNA. DR ProteinModelPortal; D0SM96; -. DR EnsemblBacteria; EEY93153; EEY93153; HMPREF0026_00429. DR PATRIC; 35606766; VBIAciJun5570_0285. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21761 MW; 43971286E0F0A5DE CRC64; MRGLYLITND DPIQLLLEKL EAALATGHIA ILQYRRKKIE KINQPSEVEL IKVLCEKYQV PFVINDDLAL AEQFGLGVHL GQSDGEITDA IKRLPQGVII GRTCLNSLDL AAKAISEGAT YVAFGAVYAT STKPEAGNVG IEVIKQAQQK YDVPICAIGG LTVENSQVVI EAGASLCAVI SDILGRSTAE IPARVSAWAK LFA // ID D0STK6_ACILW Unreviewed; 302 AA. AC D0STK6; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Mutator mutT protein; DE EC=3.6.1.-; GN ORFNames=HMPREF0017_00630; OS Acinetobacter lwoffii SH145. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=575588; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH145; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Seifert H., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Acinetobacter lwoffii strain SH145."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705056; EEY90860.1; -; Genomic_DNA. DR ProteinModelPortal; D0STK6; -. DR EnsemblBacteria; EEY90860; EEY90860; HMPREF0017_00630. DR PATRIC; 35613616; VBIAciLwo61775_0439. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 302 AA; 34861 MW; E30987882258CD86 CRC64; MYIMTKATIH VAIALLFYQN QVLVGWREAK QHQGNKYEFP GGKVEQGELP VEACRREVIE EVGVDIERWH ASDFISHEYE DLIVNLHIFH ASVQPTQLAE IKQPWRWYSR EEPGQLNFPK ANQSMIQKLQ WPQRIKIAED LDILSSLDTD QMLYWRVEAT PERIMQLQQY PVDQLSKLII NQQLWSQLNE LQQQTIRTIH LKQIQLMDLK QGELKSGYRY LAACHDLSAL MHAEQIGCEA ALLSPVLATA THPDTPALGW EQFKQMAEQV QIPVFALGGM KADELEYAKS QHAYGIAGIR YI // ID D0SVU3_ACILW Unreviewed; 206 AA. AC D0SVU3; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0017_01417; OS Acinetobacter lwoffii SH145. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=575588; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH145; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Seifert H., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Acinetobacter lwoffii strain SH145."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705059; EEY90000.1; -; Genomic_DNA. DR ProteinModelPortal; D0SVU3; -. DR EnsemblBacteria; EEY90000; EEY90000; HMPREF0017_01417. DR PATRIC; 35615220; VBIAciLwo61775_1270. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22098 MW; 54198DD2475B07F6 CRC64; MRGLYLITND DPLELLLAKL EGAMANGGVA VLQYRRKKVA KEDQIYEIEY MKAMCAEYGV PFVINDDLEM AVKYGVGVHL GQDDGSIVDA VARLPKGVLI GRSCNNSLEL AKQAIADGAN YVAFGAIYAT DSKPEAGNIG LETLKLAKEK LKVPLCAIGG LTVENSKDVI ESGADYCAVI SDILGLPMNA IPERLDEWSA LFQATA // ID D0T2B4_ACIRA Unreviewed; 209 AA. AC D0T2B4; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0018_00554; OS Acinetobacter radioresistens SH164. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=575589; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH164; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Seifert H., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Acinetobacter radioresistens strain SH164."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705131; EEY87807.1; -; Genomic_DNA. DR ProteinModelPortal; D0T2B4; -. DR EnsemblBacteria; EEY87807; EEY87807; HMPREF0018_00554. DR PATRIC; 35619749; VBIAciRad99373_0377. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22777 MW; 3BC3B58EEAE0A317 CRC64; MRGLYLITND DPIELLLEKL EAALATHQIE ILQYRRKKVE KADQLHEVER IKALCDFYKV PLVINDDIRL AAQCGLGVHL GQTDGEIIEA KTQLPENMII GRTCANSIEL AEQAIADGAT YIAFGAIYAT YSKPEAGNIG LETLKLARQK FSLPICAIGG LKVENAQPVI QAGADLCAVI SDILALPAEE IPSRVQAWAI LFAETQPAI // ID D0T5E9_ACIRA Unreviewed; 299 AA. AC D0T5E9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Mutator mutT protein; DE EC=3.6.1.-; GN ORFNames=HMPREF0018_01495; OS Acinetobacter radioresistens SH164. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=575589; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH164; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Seifert H., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Acinetobacter radioresistens strain SH164."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705132; EEY86922.1; -; Genomic_DNA. DR ProteinModelPortal; D0T5E9; -. DR EnsemblBacteria; EEY86922; EEY86922; HMPREF0018_01495. DR PATRIC; 35621700; VBIAciRad99373_1091. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 299 AA; 34112 MW; 7EBBAE044A13DD2F CRC64; MSKPIVHVAV ALLFHRSKVL VGWREAKQHQ GNKYEFPGGK VEGNETPEET CRREIYEEVG VGLSDWHPFS LICHEYDDIT VHLHLFFAHV PEEMLNQIQK PWAWYTREKL QTLDFPAANQ PVIERLYWPH SIRIGTAFSA IEQLAQDMLF YWRPEQAEID KNWLLEYSIQ QLNKLIVPYQ VWRSLNVEQQ HHIAAVHLKQ SEQMSLKKGE LCIGIRYIAA CHDAASVQHA VQIGCEAVLI SPVQATPTHP EAPALGWDAF AELAHQADVP VFALGGLSRE DLECARQYGA YGIAGIRHI // ID D0TCC9_9BACE Unreviewed; 198 AA. AC D0TCC9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0103_0836; OS Bacteroides sp. 2_1_33B. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469589; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_33B; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., McDonald J., Allen-Vercoe E., RA Strauss J., Ambrose C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 2_1_33B."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705149; EEY84892.1; -; Genomic_DNA. DR ProteinModelPortal; D0TCC9; -. DR EnsemblBacteria; EEY84892; EEY84892; HMPREF0103_0836. DR PATRIC; 35644996; VBIBacSp88625_0478. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 198 AA; 22150 MW; 38CA86F58455464A CRC64; MNKLVVITTP YFFADEASLI ELLFAEGMSR LHLRKPDCKR DELEGLLDNI SPAYYDRIVL HDWFTLAEER ALGGVHLNKR NPEAPPLYKG SISRSCHSLE EIIEYKPVCD YVFLSPIFQS ISKEGYGSGF PLDGLRNAKG IIDDKVIALG GICSQTITKL RDIPFGGVAV LGALWGNDPS LLVADQLIKQ FKRLQVWP // ID D0TCD0_9BACE Unreviewed; 242 AA. AC D0TCD0; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0103_0837; OS Bacteroides sp. 2_1_33B. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469589; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_33B; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., McDonald J., Allen-Vercoe E., RA Strauss J., Ambrose C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 2_1_33B."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705149; EEY84893.1; -; Genomic_DNA. DR ProteinModelPortal; D0TCD0; -. DR EnsemblBacteria; EEY84893; EEY84893; HMPREF0103_0837. DR PATRIC; 35644998; VBIBacSp88625_0479. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 163 165 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 HMP-PP (By similarity). FT BINDING 199 199 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 242 AA; 26709 MW; 752AF8C80C5DB886 CRC64; MALNYYFGYD ENGRVGRRTT GLRPPFGGSN RLMFITHRTP KYTECDEVRM AIQGGCSWIQ LRMKDGIYED TVRKCATICA DECERIVDFC VNDDLEAAVT CGATACHLGK NDIPLDIAWE VLKDKLDSNA IFYIGATANT FEDIRLAVER GASYIGLGPY RFTGTKKNLS PILGLEGYRK IIAQCKEAGI DIPIFAIGGI TLEDVGPLME TGITGIAVSG AIINAPDPVE ETRRFIEEIN KY // ID D0TPA8_9BACE Unreviewed; 202 AA. AC D0TPA8; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0102_01408; OS Bacteroides sp. 2_1_22. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469588; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_22; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., McDonald J., Allen-Vercoe E., RA Strauss J., Ambrose C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 2_1_22."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705174; EEZ04239.1; -; Genomic_DNA. DR ProteinModelPortal; D0TPA8; -. DR EnsemblBacteria; EEZ04239; EEZ04239; HMPREF0102_01408. DR PATRIC; 35636607; VBIBacSp133744_1942. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23627 MW; 6FBE04FC6BF5D5DD CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNRFD ACQDQNYLAV IEHFKKLKKL SD // ID D0TPB3_9BACE Unreviewed; 206 AA. AC D0TPB3; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0102_01413; OS Bacteroides sp. 2_1_22. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469588; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_22; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., McDonald J., Allen-Vercoe E., RA Strauss J., Ambrose C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 2_1_22."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705174; EEZ04244.1; -; Genomic_DNA. DR ProteinModelPortal; D0TPB3; -. DR EnsemblBacteria; EEZ04244; EEZ04244; HMPREF0102_01413. DR PATRIC; 35636617; VBIBacSp133744_1947. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22655 MW; C71D2CE7B5A79C06 CRC64; MISLQFITHQ TERYSYLESA RMALEGGCKW IQLRMKDALL EEVEAVALQL KPLCKEHEAI LILDDHVELA KKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYSSILSQ MKEANIEIPV VAIGGITFED IPAILHTGVN GIALSGTILG ADNPVEETRR IIESDL // ID D0U4J3_9GAMM Unreviewed; 307 AA. AC D0U4J3; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=SUP05_FGYC49P140008; OS uncultured SUP05 cluster bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC unclassified Oceanospirillales; SUP05 cluster; environmental samples. OX NCBI_TaxID=655186; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=19900896; DOI=10.1126/science.1175309; RA Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J., RA Tringe S.G., Tortell P.D., Hallam S.J.; RT "Metagenome of a versatile chemolithoautotroph from expanding oceanic RT dead zones."; RL Science 326:578-582(2009). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GQ351268; ACX30525.1; -; Genomic_DNA. DR ProteinModelPortal; D0U4J3; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 307 AA; 34797 MW; 6A1FDA9438AB7A3A CRC64; MKTIKAVVGV LHNSKGQLLI AKRQDHQFMP GFWELPGGKI ENGESLEQAM IRELNEELNV QVIELSMNQS MRHQYKDRMV ELNIYNIDEY KNSPIGAEGQ EINWVNIDEL TNYELLPTMK AFYNSVVLPN KYWITPSSNH QSDEWINKFE QKLTSDITLI QLRSKTPLDV SFVKSLHHQC QQNNVKLLLN TPNKTFDESY CDGWHITTNE MFKLDSRPCA DDKLLSASTH NLEEALRAQE VGADFVVISP VQATQTHPDT VPIGWEKAKQ VVDQLNIPVY LLGGMGLDDL DETLKIGAQG IAGVSAF // ID D0W467_NEICI Unreviewed; 205 AA. AC D0W467; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NEICINOT_04462; OS Neisseria cinerea ATCC 14685. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=546262; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14685; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDY02000008; EEZ71389.1; -; Genomic_DNA. DR ProteinModelPortal; D0W467; -. DR EnsemblBacteria; EEZ71389; EEZ71389; NEICINOT_04462. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22018 MW; F4F7483A963EFAA5 CRC64; MTFPPLKSPL KFYTVVPTAD WVERMVKAGA DTVQLRCKTL HGNELKREIA RCVATCQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLHEYV KQARGTPVVA IGGIDLNNAR AVLATGVSSL AVVRAVTEAE NPEAVVKAFQ ALWDE // ID D0W992_NEILA Unreviewed; 205 AA. AC D0W992; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NEILACOT_04100; OS Neisseria lactamica ATCC 23970. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=546265; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23970; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEQ02000011; EEZ75848.1; -; Genomic_DNA. DR ProteinModelPortal; D0W992; -. DR EnsemblBacteria; EEZ75848; EEZ75848; NEILACOT_04100. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21822 MW; 25783DE159EE8C3B CRC64; MTFPPLKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKTL HGDELKRKIE RCAAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSAA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQARGTPVVA IGGIDLNNAQ AVLATGVSSL AAVRAVTEAE NPEAAVKAFQ ALWNG // ID D0WF21_9ACTN Unreviewed; 216 AA. AC D0WF21; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0762_00527; OS Slackia exigua ATCC 700122. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Slackia. OX NCBI_TaxID=649764; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700122; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACUX02000005; EEZ61891.1; -; Genomic_DNA. DR ProteinModelPortal; D0WF21; -. DR EnsemblBacteria; EEZ61891; EEZ61891; HMPREF0762_00527. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22299 MW; 97D8DD989CEEB0EA CRC64; MDSPRAYIAA HPECLLLYGV TDSAWLEGRS LAACVSDAVA GGTTFVQLRE KKMATDALVA FAREVHAACP DVPFVIDDDV DAAARSGADG VHVGQEDAAC ASARARLGDD AIVGVSVQTV AQALRAERDG ADYLGVGAIF KTATKAEAAD VSLETLRAIC DAVDIPVVAI GGLNERTVDV LAETGVQGAA VVSALFSADD VRGAAQRLSE RLHHVL // ID D0WTK8_VIBAL Unreviewed; 204 AA. AC D0WTK8; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-MAR-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VMC_05080; OS Vibrio alginolyticus 40B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=674977; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=40B; RX PubMed=19860885; DOI=10.1186/1471-2148-9-258; RA Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T., RA Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.; RT "Genomic taxonomy of Vibrios."; RL BMC Evol. Biol. 9:258-258(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZB01000007; EEZ84723.1; -; Genomic_DNA. DR ProteinModelPortal; D0WTK8; -. DR EnsemblBacteria; EEZ84723; EEZ84723; VMC_05080. DR PATRIC; 35942132; VBIVibAlg143054_0590. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21877 MW; 188F782CB67CF722 CRC64; MNAYRLYLVT DDQQDLATLK RVVRKAVEGG VTMVQVREKH GDVRAFIERA QAVKDILKDT DVPLIINDRV DVALAVDADG VHLGQSDMPA EIARQLIGPN KILGLSIETE EQLAEADSLP IDYIGLSAIF ATPTKTNTKK HWGIDGLKMA LNTTSLPIVA IGGINETNIP ALSATGVHGL ALVSAICHAE DPKASSEYLL GLMS // ID D0WYK8_VIBAL Unreviewed; 471 AA. AC D0WYK8; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-MAR-2014, entry version 27. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VMC_22580; OS Vibrio alginolyticus 40B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=674977; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=40B; RX PubMed=19860885; DOI=10.1186/1471-2148-9-258; RA Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T., RA Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.; RT "Genomic taxonomy of Vibrios."; RL BMC Evol. Biol. 9:258-258(2009). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZB01000043; EEZ82896.1; -; Genomic_DNA. DR ProteinModelPortal; D0WYK8; -. DR EnsemblBacteria; EEZ82896; EEZ82896; VMC_22580. DR PATRIC; 35946170; VBIVibAlg143054_2529. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 471 AA; 52520 MW; 01821FD7FAA2F8B2 CRC64; MSKILIPSSL IELTGLVQQC LLLAKEQGFS IEDIELGVSP TQSIQLVRGQ QTTHITTDLI DDYDSEHESS FVLYYRSSLS VEACAKQPSK AIYIGIADTQ VSDEKEKVLQ LDIWRHPINN EVRALSVKSK FNAMFDPEHH LAWIVTLTVL DFPIEDALTL ARGMLTQQAN VSRETLLSDN LDEGRPTQWA DQFDDFPTPV LEGNRLGIQV GWSAQGESVS FPTLTKQSLG LYPVVDDVAW IERLLPLGIN TIQLRIKNPQ QADLEQQIIR AIELGRQYQA QVFINDYWQL AIKHGAYGVH LGQEDIEESN LAQLTKAGIR LGLSTHGYYE LLRIVQIHPS YIALGHIFPT TTKQMPSKPQ GLVRLALYQK LIDSIPYTNT EAAFRPAKDK AGSDYVLGFP TVAIGGIDQS NADQVWQTGV SSLAVVRAIT LAESPQSVIE FFAQLMKERQ LTFTDQNSEL ADTKRGEHAH G // ID D0X669_VIBHA Unreviewed; 204 AA. AC D0X669; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-MAR-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VME_05820; OS Vibrio harveyi 1DA3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=673519; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1DA3; RX PubMed=19860885; DOI=10.1186/1471-2148-9-258; RA Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T., RA Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.; RT "Genomic taxonomy of Vibrios."; RL BMC Evol. Biol. 9:258-258(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZC01000007; EEZ89514.1; -; Genomic_DNA. DR ProteinModelPortal; D0X669; -. DR EnsemblBacteria; EEZ89514; EEZ89514; VME_05820. DR PATRIC; 35952699; VBIVibHar146073_0619. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22007 MW; 2A0D3C7EF00A6974 CRC64; MNAYRLYLVT DDQQDLATLK RVVRKAVEGG VTMVQVREKH GDVRAFIERA QAVKDILKDT DVPLVINDRV DVALAVDADG VHLGQSDMPA NIARELIGPN KILGLSIENE EQFAEADSLP IDYIGLSAIF ATPTKTNTKK HWGIDGLKMA LETTSLPIVA IGGINESNIP QLSATGVHGL ALVSAICHAE DPKAASEYLL GLMR // ID D0XHV5_VIBHA Unreviewed; 471 AA. AC D0XHV5; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-MAR-2014, entry version 27. DE SubName: Full=Uncharacterized protein; GN ORFNames=VME_46680; OS Vibrio harveyi 1DA3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=673519; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1DA3; RX PubMed=19860885; DOI=10.1186/1471-2148-9-258; RA Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T., RA Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.; RT "Genomic taxonomy of Vibrios."; RL BMC Evol. Biol. 9:258-258(2009). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZC01000077; EEZ85444.1; -; Genomic_DNA. DR ProteinModelPortal; D0XHV5; -. DR EnsemblBacteria; EEZ85444; EEZ85444; VME_46680. DR PATRIC; 35961781; VBIVibHar146073_5028. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 471 AA; 52683 MW; D2B0AF26665393FC CRC64; MSKILIPSSL IELTGLVQQC LLLAKEQGFS IEDIELGVSP TQSIQLVRDQ QTTRITTDLI DGYDSENESS FVLYYRSALS VEACAKQPSK AIYIGISDTQ VSDEKEKVLQ LDIWRHPINN EVRALSVKSK FNAMFAPKYH LAWIVTLTVL DFPIEDALTL ARGMLTQQAN VSRETLLNDN LDEGRSTQWA DQFDDFPTPV LEDNRLGIQV GWSAQGESVS FPTLTKQSLG LYPVVDDVAW IERLLPLGIN TIQLRIKNPQ QADLEQQIIR AIELGRQYQA QVFINDYWQL AIKHGAYGVH LGQEDIEESN LAQLTKAGIR LGLSTHGYYE LLRIVQIHPS YIALGHIFPT TTKQMPSKPQ GLVRLALYQK LIDSIPYTNT EATFRPSKDK AVSDHVLGFP TVAIGGIDQS NADQVWQTGV SSLAVVRAIT LAESPQSVIE FFAQLMKERQ LTFTEQNSEL AHNKRGEHAH G // ID D0YYE7_LISDA Unreviewed; 203 AA. AC D0YYE7; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VDA_002310; OS Photobacterium damselae subsp. damselae CIP 102761. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=675817; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 102761; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V., RA Bartels D.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADBS01000001; EEZ41278.1; -; Genomic_DNA. DR ProteinModelPortal; D0YYE7; -. DR EnsemblBacteria; EEZ41278; EEZ41278; VDA_002310. DR PATRIC; 36214057; VBIPhoDam144561_1345. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 22053 MW; 1B28E7BED43EF474 CRC64; MHNYRLYLVT DENQDIETLK FVIKEAIAGG VTMVQLREKH GNVQEFIHRA LVVKALLIDT GIPLIINDRV DVALAVDADG IHLGQSDMPV AIARRLLGKD KIIGLSVENS QQLDEAQNLP IDYIGLSAIY PTQTKTDTVY YWGIDGLKQA VETTSLPIVA IGGINDKNIS NVSATKVAGV ALVSAIAHAK SPKEACIKLL QKM // ID D0Z158_LISDA Unreviewed; 415 AA. AC D0Z158; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 11-DEC-2013, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VDA_003272; OS Photobacterium damselae subsp. damselae CIP 102761. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=675817; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 102761; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V., RA Bartels D.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADBS01000001; EEZ42239.1; -; Genomic_DNA. DR EnsemblBacteria; EEZ42239; EEZ42239; VDA_003272. DR PATRIC; 36216533; VBIPhoDam144561_2496. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 415 AA; 46376 MW; 2EE2D81E092D7B24 CRC64; MSALRLSENL MPLLMHIDPI LATAEQFGLG EKVDISLVDH EAVFIRSAQQ NWQVVFNAHH QDQSSDVLLR VLDQWLAPYP SLDEIKQKVL NEPQLVVSGL PVADGFVDLW YHNGKVEMTF CHHLGANEPH RAMLLAALAL DYPLQDACVL ARAYARRYLD QNRDRLLHWP DCLTLFPRVV TRTHEQALTL LGEQSSPVCF EPVNREDFTL YAVVDSATWI DKVLSCGVTT AQLRIKESAT TDLTAQISQA VNSGHTYHSQ VFINDYWQQA IEAEAFGVHL GQEDLDTADL TMIAQAQLRL GISTHGYYEI LRAIELKPSY IALGHVFATT TKEMESSPQG VVRLALYQKL LTGVVPTVAI GGIDLTNIEQ VLRCEVDSVA VVRAITQAEN VEEAIKRLKE KIDQYRGGLD DAIVN // ID D0Z9T4_EDWTE Unreviewed; 214 AA. AC D0Z9T4; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ETAE_0177; OS Edwardsiella tarda (strain EIB202). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Edwardsiella. OX NCBI_TaxID=498217; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EIB202; RX PubMed=19865481; DOI=10.1371/journal.pone.0007646; RA Wang Q., Yang M., Xiao J., Wu H., Wang X., Lv Y., Xu L., Zheng H., RA Wang S., Zhao G., Liu Q., Zhang Y.; RT "Genome sequence of the versatile fish pathogen Edwardsiella tarda RT provides insights into its adaptation to broad host ranges and RT intracellular niches."; RL PLoS ONE 4:E7646-E7646(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001135; ACY83024.1; -; Genomic_DNA. DR RefSeq; YP_003294235.1; NC_013508.1. DR ProteinModelPortal; D0Z9T4; -. DR EnsemblBacteria; ACY83024; ACY83024; ETAE_0177. DR GeneID; 8606529; -. DR KEGG; etr:ETAE_0177; -. DR PATRIC; 32075667; VBIEdwTar116525_0164. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ETAR498217:GJC4-189-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23306 MW; BA231F8E66A67581 CRC64; MRQPLFAPVP TRLGLYPVVD SVEWIERLLR AGVRTLQLRI KDCREDQIGD ELAQAIALGH HYQARLFIND YWRQAIRLGA YGVHLGQEDL DRADLAAIRR AGLRLGLSTH DDAEMDRALA AGPSYVALGH VFPTDSKQMA TAPQGLSDLR RQVARLGTYP SVAIGGISIA RVPDVLACGV GSIALVSAIT RAPDWLAATD TLLQLIEGRH ANDA // ID D0ZQW7_SALT1 Unreviewed; 211 AA. AC D0ZQW7; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=STM14_5004; OS Salmonella typhimurium (strain 14028s / SGSC 2262). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=588858; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=14028s / SGSC 2262; RX PubMed=19897643; DOI=10.1128/JB.01233-09; RA Jarvik T., Smillie C., Groisman E.A., Ochman H.; RT "Short-term signatures of evolutionary change in the Salmonella RT enterica serovar typhimurium 14028 genome."; RL J. Bacteriol. 192:560-567(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001363; ACY91349.1; -; Genomic_DNA. DR RefSeq; YP_005240445.1; NC_016856.1. DR ProteinModelPortal; D0ZQW7; -. DR EnsemblBacteria; ACY91349; ACY91349; STM14_5004. DR PATRIC; 36740263; VBISalEnt101322_4533. DR BioCyc; SENT588858:GJDZ-5008-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22983 MW; 803CF861FC550D88 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE SGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID D1A8T4_THECD Unreviewed; 226 AA. AC D1A8T4; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tcur_3030; OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / OS NCIMB 10081). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptosporangineae; Thermomonosporaceae; Thermomonospora. OX NCBI_TaxID=471852; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / NCIMB 10081; RX DOI=10.4056/sigs.1453580; RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J., Goodwin L., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., RA Pati A., Chen A., Palaniappan K., Djao O., Land M., Hauser L., RA Chang Y., Jeffries C., Brettin T., Han C., Detter J., Rohde M., RA Goker M., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Klenk H., Kyrpides N.; RT "Complete genome sequence of Thermomonospora curvata type strain RT (B9)."; RL Stand. Genomic Sci. 1:13-22(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001738; ACY98572.1; -; Genomic_DNA. DR RefSeq; YP_003300610.1; NC_013510.1. DR ProteinModelPortal; D1A8T4; -. DR EnsemblBacteria; ACY98572; ACY98572; Tcur_3030. DR GeneID; 8604374; -. DR KEGG; tcu:Tcur_3030; -. DR PATRIC; 32515778; VBITheCur33965_3107. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TCUR471852:GHHD-3084-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 51 55 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24435 MW; E93B98405A7889ED CRC64; MPTHLLSDRA VALRARLDRA RLYLCTDARE RQGDLPEFLD AVLAAGVDIV QLRQKGLEAR QELEYLEVFR DACDRHGALL AVNDRADVAY AARADVLHLG QGDLPVPYAR RIVGEDVLIG RSTHSDEQAG EASAQPGVDY FCTGPVWATP TKPGRPAAGL KLVEYAASLR AGRPWFAIGG IDAGNLDRVL EAGARRIVVV RAITEADDPG AATAELARRL RQAPPL // ID D1AFY8_SEBTE Unreviewed; 197 AA. AC D1AFY8; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sterm_1155; OS Sebaldella termitidis (strain ATCC 33386 / NCTC 11300). OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Sebaldella. OX NCBI_TaxID=526218; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33386 / NCTC 11300; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Sims D., Meincke L., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.F., Hugenholtz P., Woyke T., Wu D., Eisen J.A.; RT "The complete chromosome of Sebaldella termitidis ATCC 33386."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001739; ACZ08023.1; -; Genomic_DNA. DR RefSeq; YP_003307954.1; NC_013517.1. DR ProteinModelPortal; D1AFY8; -. DR EnsemblBacteria; ACZ08023; ACZ08023; Sterm_1155. DR GeneID; 8596634; -. DR KEGG; str:Sterm_1155; -. DR PATRIC; 32406272; VBISebTer81212_1191. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; STER526218:GHLD-1165-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 31 35 HMP-PP binding (By similarity). FT REGION 128 130 THZ-P binding (By similarity). FT REGION 178 179 THZ-P binding (By similarity). FT METAL 64 64 Magnesium (By similarity). FT METAL 83 83 Magnesium (By similarity). FT BINDING 63 63 HMP-PP (By similarity). FT BINDING 102 102 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 158 158 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 197 AA; 20951 MW; 848EF30D8596870D CRC64; MYLVADTSFM TLETAEKKVT EAIEGGVTIV QLRAKDISAA EFYNMALKIK MVTGYYNVPL IINDRVDIAI AADADGVHTG QEDLPAGEVR KLIGMNKIMG ISVSNTSEAE KAERESADYL GAGAMFPTDT KLDAKYVNLE ELGEIKKKVQ IPVVAIGGIN AENAGQLFCA GADGIAVVSA ILGEKNIKEA ALKLALK // ID D1ASM1_ANACI Unreviewed; 340 AA. AC D1ASM1; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-APR-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ACIS_00985; OS Anaplasma centrale (strain Israel) (Anaplasma marginale subsp. OS centrale (strain Israel)). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Anaplasma. OX NCBI_TaxID=574556; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Israel; RX PubMed=19854912; DOI=10.1128/JB.01330-09; RA Herndon D.R., Palmer G.H., Shkap V., Knowles D.P.Jr., Brayton K.A.; RT "Complete genome sequence of Anaplasma marginale subsp. centrale."; RL J. Bacteriol. 192:379-380(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001759; ACZ49474.1; -; Genomic_DNA. DR RefSeq; YP_003328788.1; NC_013532.1. DR ProteinModelPortal; D1ASM1; -. DR EnsemblBacteria; ACZ49474; ACZ49474; ACIS_00985. DR GeneID; 8651826; -. DR KEGG; acn:ACIS_00985; -. DR PATRIC; 31928222; VBIAnaCen103588_0932. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ACEN574556:GHF2-784-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 170 174 HMP-PP binding (By similarity). FT REGION 267 269 THZ-P binding (By similarity). FT REGION 318 319 THZ-P binding (By similarity). FT METAL 203 203 Magnesium (By similarity). FT METAL 222 222 Magnesium (By similarity). FT BINDING 202 202 HMP-PP (By similarity). FT BINDING 241 241 HMP-PP (By similarity). FT BINDING 270 270 HMP-PP (By similarity). FT BINDING 298 298 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 340 AA; 37398 MW; D41FDB01BEFC0D69 CRC64; MHLMRGDNMA SCAVAEAVRD AHLQGEGDVY AVNAECADGT YADYYFDGNE EIKLLYKCPG PTDCDTFARS YRHVADHVLN TTKCKDMKDA RLDCIVLARM LASAVVSGGS VADWNPYNIN GEYFPRIASG FDCRDTMYGF DKLENIGLYL IVPDDTWFER AVRCGVKTIQ LRAKEAPIGE VDRMVRRCAQ LSKDKGVCLI VNDHWNIAIE HGAHGVHLGQ EDVQTADLES ILKSKMKLGL STHCYHELAR ACFIRPSYVA LGPVFHTTSK DMRFKPQGLQ LLKQWVQCAK LPVVGIGGID ASNIGSVVNC GVSGVAVISA VTRAEDPEAA MLNLQRAFDV // ID D1B181_SULD5 Unreviewed; 214 AA. AC D1B181; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sdel_0820; OS Sulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Sulfurospirillum. OX NCBI_TaxID=525898; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51133 / DSM 6946 / 5175; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Munk A.C., Lu M., Brettin T., RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., RA Markowitz V., Cheng J.F., Hugenholtz P., Woyke T., Wu D., Aumann P., RA Schneider S., Lang E., Spring S., Klenk H.P., Eisen J.A.; RT "The complete genome of Sulfurospirillum deleyianum DSM 6946."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001816; ACZ11851.1; -; Genomic_DNA. DR RefSeq; YP_003303886.1; NC_013512.1. DR ProteinModelPortal; D1B181; -. DR EnsemblBacteria; ACZ11851; ACZ11851; Sdel_0820. DR GeneID; 8592354; -. DR KEGG; sdl:Sdel_0820; -. DR PATRIC; 32482409; VBISulDel109514_0832. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SDEL525898:GHVA-845-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 24191 MW; E1267AB43FEE9D99 CRC64; MLDRSLLQGL YVLTDEFLTP NETLLEQMER VLKSGVRVLQ YRNKNANEEE ALRDCIRLQA LCDYYEALFI VDDRLDVAYE MNADGLHVGM DDVGYEEARE RLGKDKIIGV SCYGDIERAL HYEALGADYV AFGSFFPSPT KPHSQVVSPS ILEEAKKRLK APICAIGGIN QENISQLHAY ELAMYSVISA VYKEDNIEDN VEKMHAIIQK ASMC // ID D1B235_SULD5 Unreviewed; 185 AA. AC D1B235; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Sdel_1132; OS Sulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Sulfurospirillum. OX NCBI_TaxID=525898; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51133 / DSM 6946 / 5175; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Munk A.C., Lu M., Brettin T., RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., RA Markowitz V., Cheng J.F., Hugenholtz P., Woyke T., Wu D., Aumann P., RA Schneider S., Lang E., Spring S., Klenk H.P., Eisen J.A.; RT "The complete genome of Sulfurospirillum deleyianum DSM 6946."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001816; ACZ12155.1; -; Genomic_DNA. DR RefSeq; YP_003304190.1; NC_013512.1. DR ProteinModelPortal; D1B235; -. DR EnsemblBacteria; ACZ12155; ACZ12155; Sdel_1132. DR GeneID; 8592670; -. DR KEGG; sdl:Sdel_1132; -. DR PATRIC; 32483053; VBISulDel109514_1150. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FATPNKG; -. DR OrthoDB; EOG6FJNJD; -. DR BioCyc; SDEL525898:GHVA-1161-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 185 AA; 20596 MW; A5BACA80565F6B57 CRC64; MIKRYLITDP SFYTSDATQF LQKLLHVKAK HQPDYVCLRD KENVSYKTLA KTLAKSDIQD ENTKLFLHTD FALAHSLGCA GVHLPSHSFD QIEKAKALGL EVIVSTHTFD EACMAEKYGA DAITFSPIFA TPNKGKPVGL EKLKEINDKI KPKCFALGGI INEEHVKACE AIGVYGFASI RFFID // ID D1B7D4_THEAS Unreviewed; 220 AA. AC D1B7D4; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Taci_1711; OS Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / OS Su883) (Selenomonas acidaminovorans). OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Thermanaerovibrio. OX NCBI_TaxID=525903; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49978 / DSM 6589 / Su883; RA Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H., RA Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., RA Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Chain P., Saunders E., Detter J.C., RA Brettin T., Rohde M., Goker M., Spring S., Bristow J., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Eisen J.A.; RT "Complete genome sequence of Thermanaerovibrio acidaminovorans type RT strain (Su883)."; RL Stand. Genomic Sci. 1:254-261(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001818; ACZ19925.1; -; Genomic_DNA. DR RefSeq; YP_003318207.1; NC_013522.1. DR ProteinModelPortal; D1B7D4; -. DR EnsemblBacteria; ACZ19925; ACZ19925; Taci_1711. DR GeneID; 8631584; -. DR KEGG; tai:Taci_1711; -. DR PATRIC; 32494800; VBITheAci125881_1701. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TACI525903:GH4K-1775-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22785 MW; 898EE28183A37418 CRC64; MDDRWLREAL QVYGILDSSL GDEGELIALA EMAIGSGVTA LQLRCKGWDG GRTYRLAREL ARRCASEGVL FIVNDRLDVA LASGARGVHL GASDLPVEAA RRVAGEDFVI GGTARTLERG LELQAAGASY LGCGAAFQSG TKEDTVVIGP HGIGVIARGV SIPCVAIGGI GEHNLERLRG SNVAGIAMCG ALFRRDPGRM GDLCGAVRRT IEDGGGPVGG // ID D1BL86_VEIPT Unreviewed; 215 AA. AC D1BL86; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Vpar_0459; OS Veillonella parvula (strain ATCC 10790 / DSM 2008 / JCM 12972 / Te3) OS (Veillonella alcalescens). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=479436; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10790 / DSM 2008 / JCM 12972 / Te3; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., RA Hugenholtz P., Woyke T., Wu D., Wellnitz S., Schneider S., Gronow S., RA Klenk H.P., Eisen J.A.; RT "The complete genome of Veillonella parvula DSM 2008."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001820; ACZ24143.1; -; Genomic_DNA. DR RefSeq; YP_003311423.1; NC_013520.1. DR ProteinModelPortal; D1BL86; -. DR EnsemblBacteria; ACZ24143; ACZ24143; Vpar_0459. DR GeneID; 8635911; -. DR KEGG; vpr:Vpar_0459; -. DR PATRIC; 32530208; VBIVeiPar80537_0448. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; VPAR479436:GHOS-471-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23894 MW; 32DD1D56B30782C4 CRC64; MNRKDKLTEV MNACPIYGIT GGTRDVVPLV KDMLSAGIRI IQYREKGKTP ILRYQEAMIL RRLTSNYHAL LIIDDYVDLA LAVHADGVHI GQADLPPNTV RRIVGPNMLI GWSTHSISDL KVANRYTGVI DYIGVGPIFS TQTKPNANPV GISYIYWAKQ FSKAPIVAIG GIKTTNADTV WQAHPDFICA VSEITESDNI QNTIYELMMG YSRVR // ID D1BR36_VEIPT Unreviewed; 508 AA. AC D1BR36; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 29. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.1.50; GN OrderedLocusNames=Vpar_0315; OS Veillonella parvula (strain ATCC 10790 / DSM 2008 / JCM 12972 / Te3) OS (Veillonella alcalescens). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=479436; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10790 / DSM 2008 / JCM 12972 / Te3; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., RA Hugenholtz P., Woyke T., Wu D., Wellnitz S., Schneider S., Gronow S., RA Klenk H.P., Eisen J.A.; RT "The complete genome of Veillonella parvula DSM 2008."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001820; ACZ23999.1; -; Genomic_DNA. DR RefSeq; YP_003311279.1; NC_013520.1. DR ProteinModelPortal; D1BR36; -. DR EnsemblBacteria; ACZ23999; ACZ23999; Vpar_0315. DR GeneID; 8635759; -. DR KEGG; vpr:Vpar_0315; -. DR PATRIC; 32529912; VBIVeiPar80537_0307. DR HOGENOM; HOG000097679; -. DR OMA; RECKEND; -. DR OrthoDB; EOG628F8M; -. DR BioCyc; VPAR479436:GHOS-319-MONOMER; -. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Thiamine biosynthesis; Transferase. SQ SEQUENCE 508 AA; 54686 MW; EBB2A23A6DAC425B CRC64; MTYENPYINS STWTELNILE TLRKRNPLII CITNDVVRTF TANGLLAIGA SPVMSECSED LEDLIVHASA LLINIGTVTP DKVTYYKEAI TLAKAHEVPI VLDPVGCHAG AYRLSVVLDL IKTDAISLLR GNQSEIKAIY DALNTNHKID RSLSGKGVDG EQVEDSAIIT YRLARLINCP VVATGEEDYV SDGTRVFAVP HGHPIMTAVT GTGCLLGAVL AAFFSSYYPF MHNMSIGEFL AYALAYYGLA GESAVNVSGV KPGSFSVAFM DALYEFDDAM LLSGNRIRPV VVPDQLKVYF ISGTQDVGFN ESHLLDIVEA ACRGGVTCFQ FREKGIGTLE GQQKLELAQQ LKEICAMYNV LYIINDDVDL AVAVNADGVH VGQEDMRLED VRNLVGNKVV GISIHSMEEL HKTDVVYADC VGVGPMYATS SKPDAQEPCG PDRITELRGE GLTLPCVGIG GITLANAMPV LQAGASGVAV ISAIAHADNP YEAAQEFKNL VDNVDNIK // ID D1BRZ4_XYLCX Unreviewed; 222 AA. AC D1BRZ4; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Precursor; GN Name=thiE; OrderedLocusNames=Xcel_1455; OS Xylanimonas cellulosilytica (strain DSM 15894 / CECT 5975 / LMG 20990 OS / XIL07). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Promicromonosporaceae; Xylanimonas. OX NCBI_TaxID=446471; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Foster B., Clum A., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.F., Hugenholtz P., Woyke T., Wu D., Gehrich-Schroeter G., RA Schneider S., Pukall S.R., Klenk H.P., Eisen J.A.; RT "The complete chromosome of Xylanimonas cellulosilytica DSM 15894."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001821; ACZ30486.1; -; Genomic_DNA. DR RefSeq; YP_003326044.1; NC_013530.1. DR ProteinModelPortal; D1BRZ4; -. DR EnsemblBacteria; ACZ30486; ACZ30486; Xcel_1455. DR GeneID; 8648976; -. DR KEGG; xce:Xcel_1455; -. DR PATRIC; 32551907; VBIXylCel24446_1493. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XCEL446471:GHA2-1484-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23058 MW; 4523587EEC44841E CRC64; MSAVDPRARL SDARLYLCTD AREGRGDLED FLHAVLAGGV DVVQLRDKTL EAARELELQA LVAQVAGEHG ALWAVNDRAD VAALAGAPAV HMGQGDLPTG AVRSLLGPRR VLGRSTHSAA QAADADADPG VDYFCVGPLW ATPTKPGRSA VGLDLLAEVA ASDPVTPWFA IGGIDAERLD AVLDAGARRI VVVRAITQAA DPGRAAAELA ARVRDRVPAV AR // ID D1C3W1_SPHTD Unreviewed; 212 AA. AC D1C3W1; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sthe_1493; OS Sphaerobacter thermophilus (strain DSM 20745 / S 6022). OC Bacteria; Chloroflexi; Sphaerobacteridae; Sphaerobacterales; OC Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter. OX NCBI_TaxID=479434; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20745 / S 6022; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., LaButti K.M., Clum A., Sun H.I., RA Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., RA Markowitz V., Cheng J.F., Hugenholtz P., Woyke T., Wu D., RA Steenblock K., Schneider S., Pukall R., Goeker M., Klenk H.P., RA Eisen J.A.; RT "The complete chromosome 1 of Sphaerobacter thermophilus DSM 20745."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001823; ACZ38928.1; -; Genomic_DNA. DR RefSeq; YP_003319750.1; NC_013523.1. DR ProteinModelPortal; D1C3W1; -. DR EnsemblBacteria; ACZ38928; ACZ38928; Sthe_1493. DR GeneID; 8638904; -. DR KEGG; sti:Sthe_1493; -. DR PATRIC; 32425753; VBISphThe120955_1503. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; STHE479434:GHJN-1533-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 21786 MW; F05809886A65F26F CRC64; MSRAVPRLHL VSDRRRCPLD RFPDVAWAAV KAGFDAVHLR EKDLPAADLI EAARALNRVI GDRAALFIND RVDVALIVGA AGVQLGETAL SPRDVRALAG QSLLIGRSVH DIEGAERAAV EGADFVLAGH IYATGSKPGQ PPRGLDFLAA VTAATPLPVI AVGGITPERV PEVIAAGAYG VAVITGVLAA ADPGAAAAAY RRALETGGSI QA // ID D1C3W2_SPHTD Unreviewed; 225 AA. AC D1C3W2; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sthe_1494; OS Sphaerobacter thermophilus (strain DSM 20745 / S 6022). OC Bacteria; Chloroflexi; Sphaerobacteridae; Sphaerobacterales; OC Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter. OX NCBI_TaxID=479434; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20745 / S 6022; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., LaButti K.M., Clum A., Sun H.I., RA Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., RA Markowitz V., Cheng J.F., Hugenholtz P., Woyke T., Wu D., RA Steenblock K., Schneider S., Pukall R., Goeker M., Klenk H.P., RA Eisen J.A.; RT "The complete chromosome 1 of Sphaerobacter thermophilus DSM 20745."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001823; ACZ38929.1; -; Genomic_DNA. DR RefSeq; YP_003319751.1; NC_013523.1. DR ProteinModelPortal; D1C3W2; -. DR EnsemblBacteria; ACZ38929; ACZ38929; Sthe_1494. DR GeneID; 8638905; -. DR KEGG; sti:Sthe_1494; -. DR PATRIC; 32425755; VBISphThe120955_1504. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; STHE479434:GHJN-1534-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 49 53 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 23231 MW; ADC81D8F57EF0F16 CRC64; MAANRRAELR ERLPDALRLY VLTDRRLARG RDEARIVADA IAGGATAIQL RWKQGPLAEA LRVGREVRQV CRDAGVLFIV NDRVDLALAL DADGVHVGVD DLPVAETRAL VGERMIVGYS PPTLEAALAA ERDGADYLGV GPIYPTGTKA DAGGAVGVEH LARIVEAVGI PVVGIGGINA SNATPVVAAG AVGVAVISAV VAADDVEAAA RALRQAVEAG LRSRA // ID D1CBG6_THET1 Unreviewed; 217 AA. AC D1CBG6; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tter_1223; OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1). OC Bacteria; Thermobaculum. OX NCBI_TaxID=525904; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1; RX DOI=10.4056/sigs.1153107; RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., RA Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M., RA Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H., Cheng J.; RT "Complete genome sequence of Thermobaculum terrenum type strain RT (YNP1T)."; RL Stand. Genomic Sci. 3:153-162(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001825; ACZ42131.1; -; Genomic_DNA. DR RefSeq; YP_003322953.1; NC_013525.1. DR ProteinModelPortal; D1CBG6; -. DR EnsemblBacteria; ACZ42131; ACZ42131; Tter_1223. DR GeneID; 8645718; -. DR KEGG; ttr:Tter_1223; -. DR PATRIC; 32502646; VBITheTer68767_1304. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GAKWIQY; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TTER525904:GHMJ-1263-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23522 MW; 481832DE91FB9139 CRC64; MPTKALNFSL YVITDPDLSG GRMHTEVAKL ALEGGANVIE FRDKRATVRR QYEVAKQLRE LTKQYNAYLI INDRPDIAMA VEADGVHLGP EDLPIEVVRK LVGDTMLIAA SAYDPQEALE AQEAGADFIV ARPLFRTRWA IDKGPSMGID GLRRLTQTVN IPVVPVGGIR VDNLKDVMST GVLCPGVTTA IVGADDPKSA AQEIRKLVDS LRVAASS // ID D1CF56_THET1 Unreviewed; 216 AA. AC D1CF56; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tter_0645; OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1). OC Bacteria; Thermobaculum. OX NCBI_TaxID=525904; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1; RX DOI=10.4056/sigs.1153107; RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., RA Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M., RA Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H., Cheng J.; RT "Complete genome sequence of Thermobaculum terrenum type strain RT (YNP1T)."; RL Stand. Genomic Sci. 3:153-162(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001825; ACZ41562.1; -; Genomic_DNA. DR RefSeq; YP_003322384.1; NC_013525.1. DR ProteinModelPortal; D1CF56; -. DR EnsemblBacteria; ACZ41562; ACZ41562; Tter_0645. DR GeneID; 8645113; -. DR KEGG; ttr:Tter_0645; -. DR PATRIC; 32501378; VBITheTer68767_0693. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TTER525904:GHMJ-657-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22405 MW; C5E1EBE88E9FA72B CRC64; MASLDLRLYV ITDRKISGGR SHEEIAAAAI EGGATVVQFR DKELSGRKQV ETALRLRDIA RASGVTFIVN DRVDVALLSD ADGVHLGQDD IPASMARKIM GNKIIGVSAS TVEEALLAQQ QGADYLGVGP VFPTGSKADA APPIGLTGLA EIVRSVDIPV VAIGGISQEN LVDVLETGVS GVAVISAVVA ASDITQAARN LRAVIDAHSS YGTTHR // ID D1CVE8_9RHIZ Unreviewed; 203 AA. AC D1CVE8; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAKG_01501; OS Brucella sp. 83/13. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520449; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=83/13; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella sp. 83/13."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999649; EEZ32241.1; -; Genomic_DNA. DR ProteinModelPortal; D1CVE8; -. DR EnsemblBacteria; EEZ32241; EEZ32241; BAKG_01501. DR PATRIC; 24270865; VBIBruSp75385_0143. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22285 MW; 22A37428236D936D CRC64; MTALDPFYPI FDSADWLERM VPLGIKLVQL RIKDKADAQL RAEIRAARDN CAAHDCQLIV NDYWKLALEE GCNFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVKPDYIAL GPIYPTILKK MKWHQQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D1CZ85_9RHIZ Unreviewed; 221 AA. AC D1CZ85; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAKG_02779; OS Brucella sp. 83/13. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520449; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=83/13; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella sp. 83/13."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999657; EEZ33578.1; -; Genomic_DNA. DR ProteinModelPortal; D1CZ85; -. DR EnsemblBacteria; EEZ33578; EEZ33578; BAKG_02779. DR PATRIC; 24273751; VBIBruSp75385_1946. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23290 MW; 7E9D87E9975AD09D CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHTPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D1D880_NEIGO Unreviewed; 205 AA. AC D1D880; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NGBG_01820; OS Neisseria gonorrhoeae 35/02. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=528346; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=35/02; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Nicholas R.A., RA Unemo M., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Neisseria gonorrhoeae strain 35/02."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999992; EEZ44526.1; -; Genomic_DNA. DR ProteinModelPortal; D1D880; -. DR EnsemblBacteria; EEZ44526; EEZ44526; NGBG_01820. DR PATRIC; 29970918; VBINeiGon106767_2235. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21779 MW; 1353772F6A7897A9 CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFQ TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID D1DEJ2_NEIGO Unreviewed; 205 AA. AC D1DEJ2; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NGEG_01810; OS Neisseria gonorrhoeae FA19. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=528352; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA19; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Sparling F., RA Thomas C., Seifert H., Lander E., Nusbaum C., Ilzarbe M., Galagan J., RA Birren B.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA19; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Seifert H.S., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., RA Montmayeur A., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Neisseria gonorrhoeae strain MS11."; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABZJ02000001; EEZ46712.1; -; Genomic_DNA. DR ProteinModelPortal; D1DEJ2; -. DR EnsemblBacteria; EEZ46712; EEZ46712; NGEG_01810. DR PATRIC; 29985668; VBINeiGon136030_2382. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21748 MW; 7823772E2E3D96ED CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFP TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID D1DKZ2_NEIGO Unreviewed; 205 AA. AC D1DKZ2; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NGFG_01878; OS Neisseria gonorrhoeae MS11. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=528354; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS11; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Seifert H.S., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., RA Montmayeur A., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Neisseria gonorrhoeae strain MS11."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003909; EEZ48962.1; -; Genomic_DNA. DR RefSeq; YP_008503680.1; NC_022240.1. DR ProteinModelPortal; D1DKZ2; -. DR EnsemblBacteria; EEZ48962; EEZ48962; NGFG_01878. DR GeneID; 16747204; -. DR PATRIC; 28169282; VBINeiGon101288_2372. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21779 MW; 1353772F6A7897A9 CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFQ TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID D1DLF7_NEIGO Unreviewed; 205 AA. AC D1DLF7; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NGGG_00035; OS Neisseria gonorrhoeae PID18. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=528356; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PID18; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Rice P., RA Seifert H., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Neisseria gonorrhoeae strain PID18."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ972836; EEZ49127.1; -; Genomic_DNA. DR ProteinModelPortal; D1DLF7; -. DR EnsemblBacteria; EEZ49127; EEZ49127; NGGG_00035. DR PATRIC; 28174670; VBINeiGon111143_0220. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21779 MW; 1353772F6A7897A9 CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFQ TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID D1DST9_NEIGO Unreviewed; 205 AA. AC D1DST9; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NGHG_01473; OS Neisseria gonorrhoeae PID1. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=528355; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PID1; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Rice P., RA Seifert H., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Neisseria gonorrhoeae strain PID1."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ972883; EEZ51359.1; -; Genomic_DNA. DR ProteinModelPortal; D1DST9; -. DR EnsemblBacteria; EEZ51359; EEZ51359; NGHG_01473. DR PATRIC; 28169640; VBINeiGon45923_0209. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21748 MW; 7823772E2E3D96ED CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFP TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID D1DZR5_NEIGO Unreviewed; 205 AA. AC D1DZR5; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NGJG_00108; OS Neisseria gonorrhoeae PID332. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=528358; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PID332; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Rice P., RA Seifert H., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Neisseria gonorrhoeae strain PID332."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ972989; EEZ53785.1; -; Genomic_DNA. DR ProteinModelPortal; D1DZR5; -. DR EnsemblBacteria; EEZ53785; EEZ53785; NGJG_00108. DR PATRIC; 28184889; VBINeiGon122515_0908. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21748 MW; 7823772E2E3D96ED CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFP TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID D1EBI5_NEIGO Unreviewed; 205 AA. AC D1EBI5; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NGKG_01777; OS Neisseria gonorrhoeae SK-92-679. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=528359; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK-92-679; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whittington W., RA Seifert H., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Neisseria gonorrhoeae strain SK-92-679."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973071; EEZ57905.1; -; Genomic_DNA. DR ProteinModelPortal; D1EBI5; -. DR EnsemblBacteria; EEZ57905; EEZ57905; NGKG_01777. DR PATRIC; 28194104; VBINeiGon30635_2307. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21748 MW; 7823772E2E3D96ED CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFP TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID D1ECJ5_NEIGO Unreviewed; 205 AA. AC D1ECJ5; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NGLG_00105; OS Neisseria gonorrhoeae SK-93-1035. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=528360; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK-93-1035; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whittington W., RA Seifert H., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Neisseria gonorrhoeae strain SK-93-1035."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973086; EEZ58265.1; -; Genomic_DNA. DR ProteinModelPortal; D1ECJ5; -. DR EnsemblBacteria; EEZ58265; EEZ58265; NGLG_00105. DR PATRIC; 28194883; VBINeiGon43547_0940. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21779 MW; 1353772F6A7897A9 CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFQ TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID D1ELU5_9RHIZ Unreviewed; 221 AA. AC D1ELU5; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BALG_03076; OS Brucella pinnipedialis M292/94/1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520462; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M292/94/1; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella pinnipedialis M292/94/1."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999542; EEZ29733.1; -; Genomic_DNA. DR ProteinModelPortal; D1ELU5; -. DR EnsemblBacteria; EEZ29733; EEZ29733; BALG_03076. DR PATRIC; 24265479; VBIBruPin74143_1307. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D1EQ85_9RHIZ Unreviewed; 203 AA. AC D1EQ85; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BALG_00515; OS Brucella pinnipedialis M292/94/1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520462; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M292/94/1; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella pinnipedialis M292/94/1."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999546; EEZ30396.1; -; Genomic_DNA. DR ProteinModelPortal; D1EQ85; -. DR EnsemblBacteria; EEZ30396; EEZ30396; BALG_00515. DR PATRIC; 24266913; VBIBruPin74143_3091. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D1EZL2_BRUML Unreviewed; 221 AA. AC D1EZL2; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAMG_03041; OS Brucella melitensis bv. 1 str. Rev.1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520464; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rev.1; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella melitensis bv. 1 str. Rev.1."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999564; EEZ15101.1; -; Genomic_DNA. DR ProteinModelPortal; D1EZL2; -. DR EnsemblBacteria; EEZ15101; EEZ15101; BAMG_03041. DR PATRIC; 24232990; VBIBruMel106018_2653. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D1F1I2_BRUML Unreviewed; 203 AA. AC D1F1I2; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAMG_02904; OS Brucella melitensis bv. 1 str. Rev.1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520464; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rev.1; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella melitensis bv. 1 str. Rev.1."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999573; EEZ15771.1; -; Genomic_DNA. DR ProteinModelPortal; D1F1I2; -. DR EnsemblBacteria; EEZ15771; EEZ15771; BAMG_02904. DR PATRIC; 24234459; VBIBruMel106018_2984. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D1F6H5_BRUML Unreviewed; 203 AA. AC D1F6H5; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAOG_02946; OS Brucella melitensis bv. 3 str. Ether. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520466; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ether; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella melitensis bv. 3 str. Ether."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999591; EEZ11057.1; -; Genomic_DNA. DR ProteinModelPortal; D1F6H5; -. DR EnsemblBacteria; EEZ11057; EEZ11057; BAOG_02946. DR PATRIC; 24238243; VBIBruMel115656_1664. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D1FAJ6_BRUML Unreviewed; 221 AA. AC D1FAJ6; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAOG_03081; OS Brucella melitensis bv. 3 str. Ether. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520466; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ether; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella melitensis bv. 3 str. Ether."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999596; EEZ12481.1; -; Genomic_DNA. DR ProteinModelPortal; D1FAJ6; -. DR EnsemblBacteria; EEZ12481; EEZ12481; BAOG_03081. DR PATRIC; 24241368; VBIBruMel115656_3309. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23248 MW; 484940FBDE714125 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MTVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D1FHP2_9RHIZ Unreviewed; 203 AA. AC D1FHP2; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAPG_00521; OS Brucella ceti M490/95/1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520458; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M490/95/1; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella ceti M490/95/1."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999608; EEZ07858.1; -; Genomic_DNA. DR ProteinModelPortal; D1FHP2; -. DR EnsemblBacteria; EEZ07858; EEZ07858; BAPG_00521. DR PATRIC; 24217268; VBIBruCet48569_1496. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D1FJR0_9RHIZ Unreviewed; 221 AA. AC D1FJR0; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAPG_03045; OS Brucella ceti M490/95/1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520458; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M490/95/1; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella ceti M490/95/1."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999613; EEZ09248.1; -; Genomic_DNA. DR ProteinModelPortal; D1FJR0; -. DR EnsemblBacteria; EEZ09248; EEZ09248; BAPG_03045. DR PATRIC; 24220253; VBIBruCet48569_3228. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D1GQW4_STAA0 Unreviewed; 213 AA. AC D1GQW4; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SATW20_22300; OS Staphylococcus aureus (strain TW20 / 0582). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=663951; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TW20 / 0582; RX PubMed=19948800; DOI=10.1128/JB.01255-09; RA Holden M.T., Lindsay J.A., Corton C., Quail M.A., Cockfield J.D., RA Pathak S., Batra R., Parkhill J., Bentley S.D., Edgeworth J.D.; RT "Genome sequence of a recently emerged, highly transmissible, multi- RT antibiotic- and antiseptic-resistant variant of methicillin-resistant RT Staphylococcus aureus, sequence type 239 (TW)."; RL J. Bacteriol. 192:888-892(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN433596; CBI50098.1; -; Genomic_DNA. DR RefSeq; YP_005732201.1; NC_017331.1. DR ProteinModelPortal; D1GQW4; -. DR SMR; D1GQW4; 4-209. DR PRIDE; D1GQW4; -. DR EnsemblBacteria; CBI50098; CBI50098; SATW20_22300. DR GeneID; 12863437; -. DR KEGG; suw:SATW20_22300; -. DR PATRIC; 43217812; VBIStaAur147706_2365. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SAUR663951:GLKU-2317-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D1JP32_9BACE Unreviewed; 204 AA. AC D1JP32; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0101_01733; OS Bacteroides sp. 2_1_16. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469587; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_16; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., McDonald J., Allen-Vercoe E., RA Strauss J., Ambrose C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 2_1_16."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705209; EEZ28119.1; -; Genomic_DNA. DR ProteinModelPortal; D1JP32; -. DR EnsemblBacteria; EEZ28119; EEZ28119; HMPREF0101_01733. DR PATRIC; 35628040; VBIBacSp133054_1053. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22090 MW; 7BC369019F0674DC CRC64; MLSLQFITHQ TENYSYLESA RMALEGGCKW IQLRMKEASP EEVEAVALQL KPLCKAKEAI LILDDHVELA KKLEVDGVHL GKKDMPIGEA RQMLGEAFII GGTANTFEDV KLHHAAGADY LGIGPFRFTT TKINLSPVLG LEGYTSILAQ MNEADIRIPV VAIGGIVAED IPAIMETGVN GIALSGAILQ APDPVEETKR ILNI // ID D1JP38_9BACE Unreviewed; 202 AA. AC D1JP38; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0101_01739; OS Bacteroides sp. 2_1_16. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469587; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_16; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., McDonald J., Allen-Vercoe E., RA Strauss J., Ambrose C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 2_1_16."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705209; EEZ28125.1; -; Genomic_DNA. DR ProteinModelPortal; D1JP38; -. DR SMR; D1JP38; 1-202. DR EnsemblBacteria; EEZ28125; EEZ28125; HMPREF0101_01739. DR PATRIC; 35628052; VBIBacSp133054_1059. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23245 MW; A6533F52928C16DB CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHKRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYSGH ISCSCHSVEE VKNKKHFYDY VFMSPVYDSI SKEGYNSPYT AEELRLAAKD KIIDNKVMAL GGITPDNILE VKDFGFGGAV VLGDLWGKFD ACSDQDYLAV IEHFKKLKRM AD // ID D1K4D9_9BACE Unreviewed; 202 AA. AC D1K4D9; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0105_2481; OS Bacteroides sp. 3_1_33FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457391; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_33FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., McDonald J., Allen-Vercoe E., RA Strauss J., Ambrose C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 3_1_33FAA."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705230; EEZ20698.1; -; Genomic_DNA. DR ProteinModelPortal; D1K4D9; -. DR EnsemblBacteria; EEZ20698; EEZ20698; HMPREF0105_2481. DR PATRIC; 35656312; VBIBacSp128056_2430. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 22884 MW; 8737ADB47025626C CRC64; MKLILITPPT YFVEEDKIIT ALFEEGLDTL HLRKPGTAPM FAERLLTLIP EQYHKRIVVH GHFYLKEEYK LKGIHLNGRN PNLPEGYKGH VSCSCHSLDE VKEHKSGCDY VFLSPVFNSI SKLNYNSAYT AEELRAAAKA SIIDKKVIAL GGIDEENLLE VKDFGFGGAA ILGALWNKFD ACTDRDYRCV IEHFRKLRDL AD // ID D1K4E9_9BACE Unreviewed; 208 AA. AC D1K4E9; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0105_2491; OS Bacteroides sp. 3_1_33FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457391; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_33FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., McDonald J., Allen-Vercoe E., RA Strauss J., Ambrose C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 3_1_33FAA."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG705230; EEZ20708.1; -; Genomic_DNA. DR ProteinModelPortal; D1K4E9; -. DR EnsemblBacteria; EEZ20708; EEZ20708; HMPREF0105_2491. DR PATRIC; 35656330; VBIBacSp128056_2439. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 23142 MW; 21FF7CB1B792EA98 CRC64; MEDKTVELQF ITHFTDTYSY YDSARMALEG GCRWIQLRMK DTSVDEVERE AIRLQGLCKD YGATFIIDDH VELVNKIHAD GVHLGKKDMP VAEARKILGK EFIIGGTANT FDDVKMHYEA GADYIGCGPF RFTTTKKDLS PVLGLEGYRS IIQQMKEADI HLPIVAIGGI TLEDIPSIME TGITGIALSG TILRAKDPVA ETKRIMNL // ID D1KAQ6_9GAMM Unreviewed; 307 AA. AC D1KAQ6; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Sup05_0711; OS uncultured SUP05 cluster bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC unclassified Oceanospirillales; SUP05 cluster; environmental samples. OX NCBI_TaxID=655186; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=19900896; DOI=10.1126/science.1175309; RA Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J., RA Tringe S.G., Tortell P.D., Hallam S.J.; RT "Metagenome of a versatile chemolithoautotroph from expanding oceanic RT dead zones."; RL Science 326:578-582(2009). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG729955; EEZ80781.1; -; Genomic_DNA. DR ProteinModelPortal; D1KAQ6; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 307 AA; 34716 MW; F1F9C1C8F8B09BC5 CRC64; MKTIKAVVGV LHNSKGQLLI AKRQDHQFMP GFWELPGGKI KNGESLEQAM TRELNEELNI QVIKLSIRQS MCHQYKDRMV ELNIYNIDEY KNSPIGAEGQ EINWVNIDEL TNYELLPTMK AFYNSVVLPN KYWITPSSNH QSDEWINKFE QKLTSDITLI QLRSKTPLDV SFVKSLHHQC QQNNVKLLLN TPNKTFDESY CDGWHITTNE MFKLDSRPCA DDKLLGASTH NLKEALTAQK LGADFVVISP VQATQTHPDT IPIGWDTAQE VVDKLNIPVY FLGGMTLNDL DKALKLGAQG IAGVSAF // ID D1KAV3_9GAMM Unreviewed; 192 AA. AC D1KAV3; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Sup05_0140; OS uncultured SUP05 cluster bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC unclassified Oceanospirillales; SUP05 cluster; environmental samples. OX NCBI_TaxID=655186; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=19900896; DOI=10.1126/science.1175309; RA Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J., RA Tringe S.G., Tortell P.D., Hallam S.J.; RT "Metagenome of a versatile chemolithoautotroph from expanding oceanic RT dead zones."; RL Science 326:578-582(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG729961; EEZ80734.1; -; Genomic_DNA. DR ProteinModelPortal; D1KAV3; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 192 AA; 21110 MW; 00F43335772E3881 CRC64; MSNLDQRIKG IYAITPNQPI DINQIEKIIT RHKITILQYR HKTNDENTKL DEAQQLRQLC SVHNTLFIVN DDINLAQKIN ADGVHLGKED SPTKQARKQL GNRAIIGVSC YANINLAKQA QDQGASYVAF GALFPSNTKP KAPLCPLELI TEAKQKLNVP IVGIGGVNFS NQQQAFDAGC DAVAMINALF DS // ID D1KC59_9GAMM Unreviewed; 307 AA. AC D1KC59; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Sup05_1240; OS uncultured SUP05 cluster bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC unclassified Oceanospirillales; SUP05 cluster; environmental samples. OX NCBI_TaxID=655186; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=19900896; DOI=10.1126/science.1175309; RA Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J., RA Tringe S.G., Tortell P.D., Hallam S.J.; RT "Metagenome of a versatile chemolithoautotroph from expanding oceanic RT dead zones."; RL Science 326:578-582(2009). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG729997; EEZ80297.1; -; Genomic_DNA. DR ProteinModelPortal; D1KC59; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 307 AA; 34759 MW; C536187DB7FD2177 CRC64; MKTIKAVVGV LHNSKGQLLI AKRQDHQFMP GFWELPGGKI ENGESLEQAM IRELNEELNV QVIELSMNQS MSHQYKDRMV ELNIYNIDEY KNSPIGAEGQ EINWVNIDEL TNYELLPTMK AFYNSVVLPN KYWITPSSNH QSDEWINRFE QKLTSDITLI QLRSKTPLDV SFVKSLHHQC QQNNVKLLLN TPNKTFDESY CDGWHITTNE MFKLDSRPCA DDKLLGASTH NLDEALKAQK IGVDFVVISP VQATQTHPDT VPIGWEKAKQ VVDQLNIPVY FLGGMGLDDL DETLKIGAQG IAGVSAF // ID D1NI19_CLOTM Unreviewed; 356 AA. AC D1NI19; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Cther_1983; OS Clostridium thermocellum JW20. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=492476; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JW20; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Saunders E., Brettin T., Detter J.C., Han C., Bruce D., Goodwin L., RA Pitluck S., Larimer F., Land M.L., Hauser L., Kyrpides N., RA Mikhailova N., Hemme C.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JW20; RG US DOE Joint Genome Institute (JGI-PGF) and the Clostridium Sequencing Consortium; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Saunders E., Brettin T., Detter J.C., Han C., Bruce D., Goodwin L., RA Pitluck S., Larimer F., Land M.L., Hauser L., Kyrpides N., RA Mikhailova N., Hemme C.L., He Q., Wiegel J., Tanner R., Lynd L., RA Lawson P., Fields M.W., He Z., Arkin A., Schadt C., Stevenson B.S., RA McInerney M., Yang Y., Dong H., Huhnke R., Mielenz J.R., Ding S.-Y., RA Himmel M., Taghavi S., van der Lelie D., Zhou J.; RT "The draft genome of Clostridium thermocellum JW20."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVG02000001; EFB38971.1; -; Genomic_DNA. DR ProteinModelPortal; D1NI19; -. DR EnsemblBacteria; EFB38971; EFB38971; Cther_1983. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 183 187 HMP-PP binding (By similarity). FT REGION 280 282 THZ-P binding (By similarity). FT REGION 331 332 THZ-P binding (By similarity). FT METAL 216 216 Magnesium (By similarity). FT METAL 235 235 Magnesium (By similarity). FT BINDING 215 215 HMP-PP (By similarity). FT BINDING 254 254 HMP-PP (By similarity). FT BINDING 283 283 HMP-PP (By similarity). FT BINDING 311 311 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 356 AA; 40444 MW; 3C88F277A3F463FC CRC64; MGLDNLYRVL DANVNRTSEG LRVLEDLARF CYNDRLLSKR IKELRHSVRK NIAGLVPNLI SSRDSVNDVG LKTSMEMDID RKASLLDLAR ANFKRVQEAL RTVEESLKVL NENDLSKFYE SCRFETYSIE KEYFKVLTFE NKKGRLNEII TGLYCITSEE HSKGRSNIEV VEKMIKAGVK IIQYREKKKS LLEKYNECKK IREMTLDSGV TFIVNDNIDI AMMVKADGVH IGQDDLPIEK VRELVGDEMI IGISTHSPTQ AEDAVRRGAD YIGVGPLYRT YTKEDVCEPV GLEYLDYVVK NINIPYVAIG GIKEHNMDEV LARGARCIAM VTEIVGADDI EEKISKVKSK FSRGVL // ID D1NSS6_9BIFI Unreviewed; 521 AA. AC D1NSS6; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.7.4.7; GN Name=thiD; ORFNames=BIFGAL_02836; OS Bifidobacterium gallicum DSM 20093 = LMG 11596. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=561180; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20093; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXB03000001; EFA23728.1; -; Genomic_DNA. DR ProteinModelPortal; D1NSS6; -. DR EnsemblBacteria; EFA23728; EFA23728; BIFGAL_02836. DR PATRIC; 26483513; VBIBifGal19883_0282. DR OrthoDB; EOG6XWV53; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 521 AA; 54629 MW; 5D288437FE83E59E CRC64; MEMFPYASMR DSFDLRSYVV LGPDDTKGRD VADVVRYALH GGASFIQLRA KHADVRDIVA MAADIAAVIE DEGKADTVAF VIDDRVDAAL EARHKGIKVD GVHIGQDDND PQEARRLLGR DAIVGLSAKT PDDMRRAEAL PQGTVDYLGA GPWHETSTKP DCIVVGDDGV KHTLDAATLH ALHALTTLPI VVGGGVKAAD IPDLAASDAD GWFVVSAVTA ADDPEAATRE LVDAWQAVRG DTMHDHPAAA LLPTTLPAAL SIASTDSSGG AGVPVDIKTM MANGVFAECV ICAITAQNTK GVTHLEELSP QAIVKQIDAV YDDIAPAAVK IGMVPSIEGI NAVADGLQAN KATNIVVDPV MVATSGAKLI NDDAIATLTS RLFPMATLIT PNLPETRVLL ETIGSSIDPQ DEDGMEQAGL AIAQHFGCSV LVKGGHGLAD ANDVLVNADG TTQWFRGERI NNPNTHGTGC TLSSAIAANL AKGQTLVDAI ANAKRYITGA LRQMLELGTG SGPFDHAWMW R // ID D1P0A1_9ENTR Unreviewed; 217 AA. AC D1P0A1; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PROVRUST_05611; OS Providencia rustigianii DSM 4541. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Providencia. OX NCBI_TaxID=500637; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 4541; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXV02000016; EFB73185.1; -; Genomic_DNA. DR ProteinModelPortal; D1P0A1; -. DR EnsemblBacteria; EFB73185; EFB73185; PROVRUST_05611. DR PATRIC; 36126119; VBIProRus116159_4935. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23929 MW; F080A88A04B766F5 CRC64; MNKMLKLPNS PFPQTEQHLG LYPVVDSVEW IERLLNAGVS TLQLRIKDKA DREVRDDIQQ AISLGKQHNA RLFINDYWRL AVEFGAYGVH LGQEDLEATD LVAIHQAGLR LGISTHDHEE LAIAKSVRPS YIAMGHIFPT QTKQMPSSPQ GLETLKQMVD VTPEYPTVAI GGISIERVPA VLATGVGSVA VVSAITQADD WLAATQTLLD LVKHHTR // ID D1P8U9_9BACT Unreviewed; 226 AA. AC D1P8U9; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 13-NOV-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=PREVCOP_03530; OS Prevotella copri DSM 18205. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=537011; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18205; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACBX02000001; EFB36890.1; -; Genomic_DNA. DR ProteinModelPortal; D1P8U9; -. DR EnsemblBacteria; EFB36890; EFB36890; PREVCOP_03530. DR OrthoDB; EOG679THR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 226 AA; 26006 MW; 93D4F11175F5BD1D CRC64; MKWIVITLPD FIENESNYIN QLFKAGIDLL HLRKPESNIE ECKRLIQEID KKWHKKIVVH DHFELCQEFH LHGIHLNRRN HEIPEGFQGS ISQSCHSFKE VEQALQTISS KNKDEKSAIL KPACHYVFLS PIFDSISKKG YKHSFSNKDL EEAGINGIIN ERVVALGGVT PEYIPQLRAW NFGGAAFLGD VWNRRTDAKW TEYLAVIKQK LTPGNAKNTL NSSNIW // ID D1PAP9_9BACT Unreviewed; 229 AA. AC D1PAP9; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PREVCOP_04274; OS Prevotella copri DSM 18205. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=537011; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18205; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACBX02000009; EFB36228.1; -; Genomic_DNA. DR ProteinModelPortal; D1PAP9; -. DR EnsemblBacteria; EFB36228; EFB36228; PREVCOP_04274. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 25566 MW; 85062CE7F752C966 CRC64; MNKSLALAHF QTSFQFITHQ NERFSYLEGA YLALIGGCDW VQLRMKGATD EEVEPIARKL KLACEGAGAT FILDDRVELV KKLQIDGVHL GKNDMPVDEA RKFLGDEFII GGTANTFDDI RRLHEQGADY IGCGPFRYTT TKEKLSPVLG IEGYRQIIEQ MRENKISLPM VAIGGLTPDD IDPLAELGIG VAMSGTILNA ENPVTMTRQI HDKCFGLFIE NLNHFFENQ // ID D1PHV8_9BACT Unreviewed; 202 AA. AC D1PHV8; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Uncharacterized protein; GN ORFNames=PREVCOP_06834; OS Prevotella copri DSM 18205. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=537011; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18205; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACBX02000062; EFB33722.1; -; Genomic_DNA. DR ProteinModelPortal; D1PHV8; -. DR EnsemblBacteria; EFB33722; EFB33722; PREVCOP_06834. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23283 MW; E7A7E496FEDEA4B4 CRC64; MKLAIMTKST FFVEEDKILS SLFDEGMDNL HLFKPGSSPM YAERLLTLLP EDYLRKITVH DHYYLKQEYD LAGIHIDNPL APVPDGYKGK FSRTCTDLSM LKEMKKKSNY VFLKNIFDCI EFKDEKSSFN LQQLENAAKA GLIDKKVYAL GGMSLENLKI AKELGFGGVV ICGDLWNRFD IHNERDFKEL ILHFEKLRKA IS // ID D1PIJ6_9FIRM Unreviewed; 214 AA. AC D1PIJ6; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SUBVAR_04161; OS Subdoligranulum variabile DSM 15176. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Subdoligranulum. OX NCBI_TaxID=411471; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15176; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACBY02000011; EFB77355.1; -; Genomic_DNA. DR ProteinModelPortal; D1PIJ6; -. DR EnsemblBacteria; EFB77355; EFB77355; SUBVAR_04161. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22882 MW; 50F196BCF47CB6A5 CRC64; MNFDKDRLRL YAVTDRSWLH GQTLRAQVEA ALQGGVTCVQ LREKQLHRES FIHLGRSIGC LCQRYGVPLI INDDLEVALA CGADGVHVGQ DDLPVEEVRR RVGDKMIVGV SAHTPEEARR AYEGGADYLG AGAVFGSTTK NNVTALSHET LRAICDAVPI PVVAIGGITR ENLPRLAGTG VAGVAVVSAI FAAEDITAAS RELRALSDAM TQSH // ID D1PXD7_9BACT Unreviewed; 232 AA. AC D1PXD7; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 13-NOV-2013, entry version 18. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF0645_1622; OS Prevotella bergensis DSM 17361. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=585502; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17361; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKS01000070; EFA43904.1; -; Genomic_DNA. DR ProteinModelPortal; D1PXD7; -. DR EnsemblBacteria; EFA43904; EFA43904; HMPREF0645_1622. DR OrthoDB; EOG679THR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 232 AA; 25831 MW; 7EC0FE6F624876A7 CRC64; MNRSQPIGGF LLGATRKQIL TMKIIVITSP DFIVGEAAVI EQLLRHGVWA VHLRKPQSDS RDMARLIEEI PEICRPKIVL HDHFDLCAPY GLKGIHLNRR NPIAPEGHRG SCSKSTHSLD ELKATKPLTD YVFLSPIFDS ISKQGYRSTF SEQQLRQAHE EGVIDGRVIA LGGVSTEKLQ QVADYGFGGA AMLGDVWKHA QERNFQNYMQ QLEQWANRKG GMKGNSSGAI SL // ID D1PXD8_9BACT Unreviewed; 205 AA. AC D1PXD8; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0645_1623; OS Prevotella bergensis DSM 17361. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=585502; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17361; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKS01000070; EFA43905.1; -; Genomic_DNA. DR ProteinModelPortal; D1PXD8; -. DR EnsemblBacteria; EFA43905; EFA43905; HMPREF0645_1623. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 31 35 HMP-PP binding (By similarity). FT REGION 128 130 THZ-P binding (By similarity). FT METAL 64 64 Magnesium (By similarity). FT METAL 83 83 Magnesium (By similarity). FT BINDING 63 63 HMP-PP (By similarity). FT BINDING 102 102 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22575 MW; A22CBE910C94242C CRC64; MNVQFISHRN ARFDDLEGIR LALAGGCRWV QLRMKDATDE VVIEVAVKAR RLCDEYGATL ILDDRVHLVE PTRADGVHLG RLDMPVDLAR RLLGHNRIIG GTANTIEDIR RLAAWGADYI GCGPLRFTTT KQNLAPLLGF DGYRRLISRM RAEGIRLPLV AIGGITEKDL PRLVEVGVEG IAVSGSVLNA PNPTLAMQNL INYGQ // ID D1QA48_STAAU Unreviewed; 213 AA. AC D1QA48; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAPG_01449; OS Staphylococcus aureus A9765. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553594; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A9765; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., RA Berlin A., Bochicchio J., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., RA White J., Yandava C., Peleg A.Y., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A9765."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACSN01000014; EFB98268.1; -; Genomic_DNA. DR ProteinModelPortal; D1QA48; -. DR SMR; D1QA48; 4-209. DR PRIDE; D1QA48; -. DR EnsemblBacteria; EFB98268; EFB98268; SAPG_01449. DR PATRIC; 35714022; VBIStaAur31387_1446. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D1QL25_STAAU Unreviewed; 213 AA. AC D1QL25; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 16-APR-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAQG_02399; OS Staphylococcus aureus A10102. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553601; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A10102; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., RA Berlin A., Bochicchio J., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., RA White J., Yandava C., Peleg A.Y., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A10102."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACSO01000022; EFB94414.1; -; Genomic_DNA. DR ProteinModelPortal; D1QL25; -. DR SMR; D1QL25; 4-209. DR PRIDE; D1QL25; -. DR EnsemblBacteria; EFB94414; EFB94414; SAQG_02399. DR PATRIC; 35721818; VBIStaAur115417_2384. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D1R2G6_STAAU Unreviewed; 213 AA. AC D1R2G6; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SGAG_02082; OS Staphylococcus aureus A8117. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553574; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A8117; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Peleg A.Y., Young S.K., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., RA Lewis B., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A8117."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A8117; RX PubMed=22492855; DOI=10.1093/infdis/jis252; RA Cameron D.R., Ward D.V., Kostoulias X., Howden B.P., RA Moellering R.C.Jr., Eliopoulos G.M., Peleg A.Y.; RT "Serine/threonine phosphatase Stp1 contributes to reduced RT susceptibility to vancomycin and virulence in Staphylococcus aureus."; RL J. Infect. Dis. 205:1677-1687(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYO01000010; EFC02958.1; -; Genomic_DNA. DR ProteinModelPortal; D1R2G6; -. DR SMR; D1R2G6; 4-209. DR PRIDE; D1R2G6; -. DR EnsemblBacteria; EFC02958; EFC02958; SGAG_02082. DR PATRIC; 35911270; VBIStaAur72157_2055. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D1RGQ8_LEGLO Unreviewed; 427 AA. AC D1RGQ8; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=LLB_0792; OS Legionella longbeachae D-4968. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=638315; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D-4968; RA Kozak N.A., Buss M., Frace M., Govil D., Lucas C.E., Travis T., RA Olsen-Rasmussen M., Benson R.F., Fields B.S.; RT "The Genomic Sequence of the Soil-Dwelling Opportunistic Pathogen RT Legionella longbeachae."; RL J. Bacteriol. 0:0-0(2010). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZG01000001; EEZ95614.1; -; Genomic_DNA. DR ProteinModelPortal; D1RGQ8; -. DR EnsemblBacteria; EEZ95614; EEZ95614; LLB_0792. DR PATRIC; 35980495; VBILegLon24077_0767. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 427 AA; 48308 MW; 238FE709B3DB0CA1 CRC64; MQIVWADAEI EEDSYTFRDF GVEVHRSPFH VKSMPDAIKV NLQISLEEIY LTKSYSIPVV LDAYVLLQKV YYKRSDLIPW FSLANLLVLD THEAELILGY KIASHQSMQE AAHELLSLGN QSILLLGEQL HEAWCHDYWT NGVTSFWLTQ SRISYTKYSG LRSILSAAIT ASLALGYSLE DAIIIARMYT HQVIRRTHTG FDFGGFPEDE VDLPYLASMP LYEKPQPFKL CHHLGLYPVV DSSVWVELLL NVGVKTIQLR IKEQTETLEK EVQRSIALAK KHRATLYIND YWELALKYEA DGVHLGQSDL DAADINAIRK KGLLLGVSTH CYYEVARAHA INPSYIAIGP IYPTTSKKMP FLAQGIERLK RWQRTLNYPL VAIGGINIER MSDVVATGVS GVALISAITK AHNPRRATEQ FLSILQI // ID D1U1P8_YERPE Unreviewed; 224 AA. AC D1U1P8; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YPD27_2471; OS Yersinia pestis KIM D27. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=687916; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KIM D27; RA Varga J., Schneewind O., Durkin S., Hostetler J., Nierman W.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KIM D27; RX PubMed=21559501; DOI=10.1371/journal.pone.0019054; RA Losada L., Varga J.J., Hostetler J., Radune D., Kim M., Durkin S., RA Schneewind O., Nierman W.C.; RT "Genome sequencing and analysis of Yersina pestis KIM D27, an RT avirulent strain exempt from select agent regulation."; RL PLoS ONE 6:E19054-E19054(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADDC01000001; EFA48203.1; -; Genomic_DNA. DR ProteinModelPortal; D1U1P8; -. DR EnsemblBacteria; EFA48203; EFA48203; YPD27_2471. DR PATRIC; 36073001; VBIYerPes140705_2587. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID D1W163_9BACT Unreviewed; 202 AA. AC D1W163; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 13-NOV-2013, entry version 19. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF9019_0837; OS Prevotella timonensis CRIS 5C-B1. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=679189; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CRIS 5C-B1; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Prevotella timonensis CRIS 5C-B1."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADEF01000055; EFA96869.1; -; Genomic_DNA. DR ProteinModelPortal; D1W163; -. DR EnsemblBacteria; EFA96869; EFA96869; HMPREF9019_0837. DR PATRIC; 36347709; VBIPreTim140020_1898. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23359 MW; 2EB99F5D5F66E00A CRC64; MKLVIMTKST FFVEEDKILT ALFEEGMDSL HLHKPDSSPL YSERLLSLLP ERYHKKIIVH EHYYLKNEYN LSGIHLQQLT DPVPEGVRGR ITRSCSDIQL LRETKRKADY VFLEKIFDSI EDPTQKASFN LLQIEEAARK GLIDRHVFAV GGMHLDNIKL AKEYGFGGVV IRGDLWNHFN IHNEIDFKAL IAHFQKLKKA VG // ID D1W6R1_9BACT Unreviewed; 202 AA. AC D1W6R1; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 13-NOV-2013, entry version 19. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF0650_0087; OS Prevotella buccalis ATCC 35310. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=679190; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35310; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Prevotella buccalis ATCC 35310."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADEG01000071; EFA91774.1; -; Genomic_DNA. DR ProteinModelPortal; D1W6R1; -. DR EnsemblBacteria; EFA91774; EFA91774; HMPREF0650_0087. DR PATRIC; 36351890; VBIPreBuc139135_1552. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23376 MW; ED149F8CEAB5777D CRC64; MKLVIMTKST FFVEEDKILT ALFDEGMDNL HLHKPGSSPL YSERLLSLLP EKYHKRITVH EHYYLKNEYN LSGIHLDQLT DQPPAGYRGR ITRNCSDLSL LKETKKKADD IFLTYIFDSI EEENHKANFN MQQIEEAAKR GLIDRHVFAA GGMNIDNVKL AKDYGFGGVV IRGDLWSRFD IHNETDFKDL MAHFEKLRKV VG // ID D1WK92_STAEP Unreviewed; 199 AA. AC D1WK92; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0797_0824; OS Staphylococcus epidermidis SK135. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=596317; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK135; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Staphylococcus epidermidis SK135."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADEY01000015; EFA88394.1; -; Genomic_DNA. DR ProteinModelPortal; D1WK92; -. DR EnsemblBacteria; EFA88394; EFA88394; HMPREF0797_0824. DR PATRIC; 36361753; VBIStaEpi15895_0629. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 22752 MW; A468A47409C7D4D7 CRC64; MGGIFIFIAI TYHKQLTRDD LQHYKHIEEA IDGLLFRTSM NNEENKDMIQ SLLQLGFSKD KIIIHSDVTL LEDLHLKRIH FKENDTTAFT YKEAHPDICV SMSTHDVETV KRCYENGLDS VFFGHIFPTS SHPNVPPRSK EAIQQALNVP IPIYAIGGIN EHSLQKMPPG FKGICAISYF NNASLEEIKQ LRKEWSTHA // ID D1WP79_STAEP Unreviewed; 213 AA. AC D1WP79; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0797_0139; OS Staphylococcus epidermidis SK135. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=596317; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK135; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Staphylococcus epidermidis SK135."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADEY01000022; EFA87282.1; -; Genomic_DNA. DR ProteinModelPortal; D1WP79; -. DR EnsemblBacteria; EFA87282; EFA87282; HMPREF0797_0139. DR PATRIC; 36364728; VBIStaEpi15895_2046. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID D1XXH0_9BACT Unreviewed; 206 AA. AC D1XXH0; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0648_0964; OS Prevotella bivia JCVIHMP010. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=553171; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JCVIHMP010; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Prevotella bivia JCVIHMP010."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFO01000063; EFB93244.1; -; Genomic_DNA. DR ProteinModelPortal; D1XXH0; -. DR EnsemblBacteria; EFB93244; EFB93244; HMPREF0648_0964. DR PATRIC; 36435289; VBIPreBiv94575_0853. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22694 MW; 70C382DE3F842D08 CRC64; MTSIQYITHE NQRLSYLDGA ILALMGGCKW VQLRMKEASD EEFLVVGSQL RELCKTYSAT FILDDRVHLV KPLGADGVHL GKNDMPIDEA RRCLQSDKVI IGGTANTFDD IKRLHKQGAN YIGCGPFRYT ETKKKLAPTL GFQGYKSLVE KMKSEGITLP IFAIGGILYD DVKALLSIGI DGIAISGGVL NADNPIEKMK LLMKLT // ID D1XXH3_9BACT Unreviewed; 194 AA. AC D1XXH3; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 13-NOV-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0648_0967; OS Prevotella bivia JCVIHMP010. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=553171; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JCVIHMP010; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Prevotella bivia JCVIHMP010."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFO01000063; EFB93247.1; -; Genomic_DNA. DR ProteinModelPortal; D1XXH3; -. DR EnsemblBacteria; EFB93247; EFB93247; HMPREF0648_0967. DR PATRIC; 36435295; VBIPreBiv94575_0856. DR OrthoDB; EOG679THR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 21834 MW; D1B0D1764BEB998E CRC64; MEIIVITQPT FISNEAAIIQ QLLSLGVARV HIRKPNMCIE SCRQLIKDIP ACFHAKLSLH DNFALTREFE IGGIHLNHRN PTIPKGFKGI ISKSCHSFQE VIENKETHNY LFLSPIFNSI SKQGYLSAFT HESLTLAHKQ QIIETNVYAL GGVTLKNIHK LYNYGFGGAA ILGDIWEKVG TTDFEKHVIK LVTH // ID D1Y5Y0_9BACT Unreviewed; 213 AA. AC D1Y5Y0; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF7215_1183; OS Pyramidobacter piscolens W5455. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Pyramidobacter. OX NCBI_TaxID=352165; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=W5455; RA Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFP01000086; EFB90271.1; -; Genomic_DNA. DR ProteinModelPortal; D1Y5Y0; -. DR EnsemblBacteria; EFB90271; EFB90271; HMPREF7215_1183. DR PATRIC; 36441141; VBIPyrPis26956_1595. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22327 MW; 080387CC7642E73E CRC64; MNCPRESLRL YAVTDRHWLG AKTLAQAVEE ALRGGATMVQ LREKNLDHDR FLAEALAIKS VAKRYGAPLI INDRVEIALA CDADGVHLGQ DDADPRAARL RLGPRKIIGV SAHSAAEAVA AERDGADYLG SGALFPTDTK DNAAALPLGE LKRIAAAVSI PVVGIGGVTA DNMPQLKGTG LCGAAVVSAL FAAPDVEASA RRLRRLADEI FGA // ID D1Y933_PROAA Unreviewed; 217 AA. AC D1Y933; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9206_1068; OS Propionibacterium acnes J139. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=679194; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J139; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Propionibacterium acnes J139."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFS01000001; EFB87992.1; -; Genomic_DNA. DR ProteinModelPortal; D1Y933; -. DR EnsemblBacteria; EFB87992; EFB87992; HMPREF9206_1068. DR PATRIC; 36446302; VBIProAcn138375_0181. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22508 MW; 6BD5C5023BD76D6C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRFPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRTIMASDDP AAVVRQVVQS FDEVRVS // ID D1Y9T4_PROAA Unreviewed; 216 AA. AC D1Y9T4; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9206_2112; OS Propionibacterium acnes J139. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=679194; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J139; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Propionibacterium acnes J139."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFS01000001; EFB89003.1; -; Genomic_DNA. DR ProteinModelPortal; D1Y9T4; -. DR EnsemblBacteria; EFB89003; EFB89003; HMPREF9206_2112. DR PATRIC; 36448167; VBIProAcn138375_1090. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22548 MW; D68AAF1B366F1623 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAGMRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID D1YNB3_9FIRM Unreviewed; 505 AA. AC D1YNB3; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF1035_0164; OS Veillonella parvula ATCC 17745. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=686660; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17745; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Veillonella parvula ATCC 17745."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFU01000011; EFB86319.1; -; Genomic_DNA. DR ProteinModelPortal; D1YNB3; -. DR EnsemblBacteria; EFB86319; EFB86319; HMPREF1035_0164. DR PATRIC; 36456167; VBIVeiPar156829_0478. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 505 AA; 54444 MW; 19BAF5EE911CBA7D CRC64; MTYENPYINS STWTELNILE TLRKRNPLII CITNDVVRTF TANGLLAIGA SPVMSECSED LKDLIAHSSA LLINIGTLTP DKVSYYKDAI ALAKKHEVPI VLDPVGCHAG VYRLSVVLDL IKTDAISLLR GNQSEIKAIY DALNTNHKVN NSLSGKGVDG EQVEDSAIIT YRLARQINCP VVATGEEDYV SDGTRVFAVP HGHPIMTAVT GTGCLLGAVL AAFFSSYYPF MHNMSSGEFL AYALAYYGLA GERAVKVSGV KPGSFSVAFM DALYEFDDAM LLSGNRIRPV VVPDQLKVYF ISGTQDVGFN ERHLLDTVEA ACRGGVTCFQ FREKGTGTLE GQQKLELAQQ LKEICAMYNV LYIINDDVDL AVAVNADGVH VGQEDMRLED VRNLVGNKVV GISIHSVEEL HKTDVVYADC VGVGPMYATS SKPDAQEPCG PDRITELRAE GLTLPCVGIG GITLDNATPV LQAGASGVAV ISAIAHADDP YEAAEEFKNL VDNIK // ID D1YQV8_9FIRM Unreviewed; 215 AA. AC D1YQV8; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1035_0024; OS Veillonella parvula ATCC 17745. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=686660; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17745; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Veillonella parvula ATCC 17745."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFU01000015; EFB85567.1; -; Genomic_DNA. DR ProteinModelPortal; D1YQV8; -. DR EnsemblBacteria; EFB85567; EFB85567; HMPREF1035_0024. DR PATRIC; 36457975; VBIVeiPar156829_1357. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23852 MW; DFAAD6B64FD68A6E CRC64; MNRKDKLTAV MNACPIYGIT GGTRDVVPLV KDMLSAGIRI IQYREKGKTP ILRYQEAMIL RRLTSNYHAL LIIDDYVDLA LAVHADGVHI GQDDLPPNTV RRIVGPNMLI GWSTHSISDL KAANRYTGVI DYIGVGPIFS TQTKPNANPV GISYIYWAKQ FSKAPIVAIG GIKTTNADTV WQAHPDFICA VSEITESDNI QNTIYELMMG YSRVR // ID D1YXN6_METPS Unreviewed; 215 AA. AC D1YXN6; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 14-MAY-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MCP_1136; OS Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 / OS SANAE). OC Archaea; Euryarchaeota; Methanomicrobia; Methanocellales; OC Methanocellaceae; Methanocella. OX NCBI_TaxID=304371; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE; RX PubMed=21829548; DOI=10.1371/journal.pone.0022898; RA Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H., RA Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R., RA Mori K., Fujita N., Imachi H., Takai K.; RT "Genome sequence of a mesophilic hydrogenotrophic methanogen RT Methanocella paludicola, the first cultivated representative of the RT order Methanocellales."; RL PLoS ONE 6:E22898-E22898(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011532; BAI61208.1; -; Genomic_DNA. DR RefSeq; YP_003356191.1; NC_013665.1. DR ProteinModelPortal; D1YXN6; -. DR PRIDE; D1YXN6; -. DR EnsemblBacteria; BAI61208; BAI61208; MCP_1136. DR GeneID; 8683199; -. DR KEGG; mpd:MCP_1136; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GLGPICH; -. DR BioCyc; MPAL304371:GI7G-1159-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22348 MW; 580EFD2790391E6A CRC64; MTAYDLYVIT DEGLSKGLTH VEIARRAIAG GADVIQLRDK SMSGEELMEC AVQIRTLTKE AGVLFIVNDR LDIAIASKAD GVHLGQEDIP VKLARPLAPP GFIIGVSAGT LEEALQAERD GADYIGLGPI CHTGSKKDAG PVCGFGLITG VKKHVSIPVI VIGGIGPDNA KESISAGADG LAVISAVVSQ DDVTGAAKHL KALIKEAKRQ KVYEG // ID D2AD71_SHIF2 Unreviewed; 211 AA. AC D2AD71; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SFxv_4432; OS Shigella flexneri serotype X (strain 2002017). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=591020; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2002017; RX PubMed=19955273; DOI=10.1128/JCM.00614-09; RA Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., RA Li Z., Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., RA Luo X., Bai X., Wang Y., Wang P., Xu Q., Xu J.; RT "Emergence of a new multidrug-resistant serotype X variant in an RT epidemic clone of Shigella flexneri."; RL J. Clin. Microbiol. 48:419-426(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001383; ADA76362.1; -; Genomic_DNA. DR RefSeq; YP_005729655.1; NC_017328.1. DR ProteinModelPortal; D2AD71; -. DR SMR; D2AD71; 10-208. DR EnsemblBacteria; ADA76362; ADA76362; SFxv_4432. DR GeneID; 12317606; -. DR KEGG; sfe:SFxv_4432; -. DR PATRIC; 36750997; VBIShiFle60233_4751. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SFLE591020:GLK5-4335-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D2B6I0_STRRD Unreviewed; 213 AA. AC D2B6I0; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sros_2786; OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / OS NI 9100). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptosporangineae; Streptosporangiaceae; Streptosporangium. OX NCBI_TaxID=479432; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100; RX DOI=10.4056/sigs.631049; RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., RA Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.F., RA Chertkov O., Sims D., Meincke L., Brettin T., Han C., Detter J.C., RA Bruce D., Goodwin L., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., RA Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Streptosporangium roseum type strain (NI RT 9100T)."; RL Stand. Genomic Sci. 2:29-37(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001814; ACZ85744.1; -; Genomic_DNA. DR RefSeq; YP_003338487.1; NC_013595.1. DR ProteinModelPortal; D2B6I0; -. DR EnsemblBacteria; ACZ85744; ACZ85744; Sros_2786. DR GeneID; 8666072; -. DR KEGG; sro:Sros_2786; -. DR PATRIC; 32467539; VBIStrRos112010_2763. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SROS479432:GI0V-2808-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22967 MW; ECAF0CEE17D29E7F CRC64; MPRPSVSDAR LYLCTDGRRD RGDLADFLDA ALAGGVDIVQ LREKGLEARE ELELLEVFRA ACDRHGRLLA VNDRADIAYA ARPDVLHLGQ DDLPVPVVRD MLGDDILIGR STHADEEASA AAVEPGVDYF CCGPIWPTPT KPGRHAPGPG LLRHAASLGT DRPWFGIGGI DLANLDEVIS YGVRRVVVVR AITEADDPKA AAEEFQRRLA AAG // ID D2BHM5_DEHMV Unreviewed; 352 AA. AC D2BHM5; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=DhcVS_688; OS Dehalococcoides mccartyi (strain VS). OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales; OC Dehalococcoidaceae; Dehalococcoides. OX NCBI_TaxID=311424; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VS; RX PubMed=19893622; DOI=10.1371/journal.pgen.1000714; RA McMurdie P.J., Behrens S.F., Muller J.A., Goke J., Ritalahti K.M., RA Wagner R., Goltsman E., Lapidus A., Holmes S., Loffler F.E., RA Spormann A.M.; RT "Localized plasticity in the streamlined genomes of vinyl chloride RT respiring Dehalococcoides."; RL PLoS Genet. 5:E1000714-E1000714(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001827; ACZ61825.1; -; Genomic_DNA. DR RefSeq; YP_003330153.1; NC_013552.1. DR ProteinModelPortal; D2BHM5; -. DR EnsemblBacteria; ACZ61825; ACZ61825; DhcVS_688. DR GeneID; 8657621; -. DR KEGG; dev:DhcVS_688; -. DR PATRIC; 32058272; VBIDehSp95780_0655. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DSP311424:GJ8J-663-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 179 183 HMP-PP binding (By similarity). FT REGION 276 278 THZ-P binding (By similarity). FT REGION 326 327 THZ-P binding (By similarity). FT METAL 212 212 Magnesium (By similarity). FT METAL 231 231 Magnesium (By similarity). FT BINDING 211 211 HMP-PP (By similarity). FT BINDING 250 250 HMP-PP (By similarity). FT BINDING 279 279 HMP-PP (By similarity). FT BINDING 306 306 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 352 AA; 38569 MW; 7B00D8933034E682 CRC64; MDNLEKLWRI VDVNQNRLSE GLRVLEEIAR LYLEDEKLNS RFKNLRHSLT LQDIASNSRL LFSRQADTDI GAQLETADQS EPETLFSLVS ANAKRAEQSL RVLEEFAGLP ETGLDAALYS RGRFELYTLE KDLAARLLRT NRRDMITGLY VAIDADYLAG RDITAVTREV LEGGCRLIQL RAKTASTRKF LALAVSLKEI CLEYGALFII NDRLDIALAC GADGLHLGQI DMPLSQARHF MPPDSIIGIS ADTPEQAIWA QNEGADYVAA GAVFPTQTKQ DVLFGGLSGL QAIHQVVKIP LVAIGGINKS NFYEAMQAGA GSLCLISAVL GAPDIKKATS EFITLMEAAK ID // ID D2BR31_LACLK Unreviewed; 215 AA. AC D2BR31; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LLKF_1328; OS Lactococcus lactis subsp. lactis (strain KF147). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=684738; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KF147; RX PubMed=18039825; DOI=10.1128/AEM.01850-07; RA Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D., RA van Hylckama Vlieg J.E.; RT "Genome-scale genotype-phenotype matching of two Lactococcus lactis RT isolates from plants identifies mechanisms of adaptation to the plant RT niche."; RL Appl. Environ. Microbiol. 74:424-436(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001834; ADA65006.1; -; Genomic_DNA. DR RefSeq; YP_003353762.1; NC_013656.1. DR ProteinModelPortal; D2BR31; -. DR EnsemblBacteria; ADA65006; ADA65006; LLKF_1328. DR GeneID; 8678750; -. DR KEGG; llk:LLKF_1328; -. DR PATRIC; 32251150; VBILacLac141273_1347. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LLAC684738:GI3F-1369-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23571 MW; 763D53E3E2D766AC CRC64; MKNKILDLRA YFIAGPQDFP KLSIDDAIDK ISVIIKSGVT VYQFRDKGTI YKNNNQRLEV AKRLQGVAQK AAVSFIVNDD VELARELSAD GIHVGQDDDS VSKIRELIGQ EMWVGLSVSN DMELESAQKS GADYLGIGPI YPTNSKSDAA EPIGVDHLRK MLEHNQLPTV GIGGITENSL TELSKIGLGG VAVISLLTES ENYKNMVQKI KQNIR // ID D2C1V1_DICD5 Unreviewed; 211 AA. AC D2C1V1; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dd586_0230; OS Dickeya dadantii (strain Ech586). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Dickeya. OX NCBI_TaxID=590409; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ech586; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., RA Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Balakrishnan V., Glasner J., Perna N.T.; RT "Complete sequence of Dickeya dadantii Ech586."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001836; ACZ75127.1; -; Genomic_DNA. DR RefSeq; YP_003331832.1; NC_013592.1. DR ProteinModelPortal; D2C1V1; -. DR EnsemblBacteria; ACZ75127; ACZ75127; Dd586_0230. DR GeneID; 8659132; -. DR KEGG; ddc:Dd586_0230; -. DR PATRIC; 32067103; VBIDicDad110536_0233. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; DDAD590409:GHDW-239-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22852 MW; 4316AE82CB80FA1F CRC64; MTRAFPATDA RLGLYPVVDS VAWIERLLDA GVRTLQLRIK DQPAEQAEPD IIRAIALGRQ YQARLFINDY WQLAVRHQAY GVHLGQEDLD TADLAAIHAA GLRLGVSTHD DAELARAIAL SPSYIALGHI FPTQTKAMPS APQGLVELAR HIRALNGRFP TVAIGGISID RVPAVLETGV GSIAVVSAIT QAADWRAATA TLLRLIERRE A // ID D2EJ42_PEDAC Unreviewed; 226 AA. AC D2EJ42; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9024_00804; OS Pediococcus acidilactici 7_4. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=563194; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_4; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., RA Ambrose C., McDonald J., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Pediococcus acidilactici strain 7_4."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730085; EFA26514.1; -; Genomic_DNA. DR ProteinModelPortal; D2EJ42; -. DR EnsemblBacteria; EFA26514; EFA26514; HMPREF9024_00804. DR PATRIC; 35850841; VBIPedAci303_0849. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23919 MW; EE7032DD506AC354 CRC64; MKFNPTMLQA YFIAGTQDVA SKTDFLPTVE RIVQAGATAF QFRNKGAVKT ASRDEVVELA RACHQITQKY QIPLFIDDDV DLALTVGAEG IHVGQKDERI TSVLERVGDQ MIVGLSCNTA AQITAANQLN GVDYLGTGTV YETNSKADAG NALGVDKLRE LVQMSKFPVV AIGGITLKRV AETVATGAAG IAAISMFIQM TDPAQQIAEI KATIAQVGGA ACSPKK // ID D2EKY5_PEDAC Unreviewed; 194 AA. AC D2EKY5; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9024_01447; OS Pediococcus acidilactici 7_4. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=563194; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_4; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., RA Ambrose C., McDonald J., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Pediococcus acidilactici strain 7_4."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730087; EFA25947.1; -; Genomic_DNA. DR ProteinModelPortal; D2EKY5; -. DR EnsemblBacteria; EFA25947; EFA25947; HMPREF9024_01447. DR PATRIC; 35852239; VBIPedAci303_1532. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 194 AA; 21011 MW; 6FA2848A34567010 CRC64; MLEKPLLYLV TDRLGLNQQQ FLERIELACQ GGVDLLQLRE KEISSAEYYK LAGHVKKITD RYQIPLIIDD QVAIAQAVDA AGVHLGQADL PVAVARRILG PHKIIGATTK TVAQARRAVE EGANYLGVGA IFPTTTHVKT VHTSVVTLKR IKQEAKITVF AIGGLNAENL SVLRNTNVDG VAVVSAIMKA TQPQ // ID D2ENS0_9STRE Unreviewed; 210 AA. AC D2ENS0; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0850_01720; OS Streptococcus sp. M143. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=563037; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M143; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Sibley C.D., Field T.R., Grinwis M., RA Eshaghurshan C.S., Surette M.G., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Streptococcus sp. strain M143."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730094; EFA25147.1; -; Genomic_DNA. DR ProteinModelPortal; D2ENS0; -. DR EnsemblBacteria; EFA25147; EFA25147; HMPREF0850_01720. DR PATRIC; 35704347; VBIStrSp1245_0588. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22958 MW; 64BF68C69F8653C1 CRC64; MNREALRLYL VTNRYQDSLE NFLRKVETTC RSGVTIIQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDICLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE EGGADYLGTG AIFPTRTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLVDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDDIIS // ID D2EU45_9BACE Unreviewed; 202 AA. AC D2EU45; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0969_00667; OS Bacteroides sp. D20. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=585543; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D20; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., RA White A., Ambrose C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain D20."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730105; EFA21472.1; -; Genomic_DNA. DR ProteinModelPortal; D2EU45; -. DR EnsemblBacteria; EFA21472; EFA21472; HMPREF0969_00667. DR PATRIC; 35661917; VBIBacSp64485_1184. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23273 MW; 7B69F50F0095840E CRC64; MKLIVVTAPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHKRIITH EHFYLQEEFS LMGIHLNTRN PKEPHDYSGH ISCTCHSLDE VQNKKHFYDY LFLSPIYNCI TKSGVTSGFT AEELRQAGKS KVIDSRVMAL GGITPDNILE IKDYGFGGAV VMGDLWNKFN ACTDRDYLEV IRHFKKLKKM AD // ID D2F143_9BACE Unreviewed; 216 AA. AC D2F143; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0969_03323; OS Bacteroides sp. D20. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=585543; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D20; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., RA White A., Ambrose C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain D20."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730108; EFA18654.1; -; Genomic_DNA. DR ProteinModelPortal; D2F143; -. DR EnsemblBacteria; EFA18654; EFA18654; HMPREF0969_03323. DR PATRIC; 35667271; VBIBacSp64485_3388. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23886 MW; ED164CA052BBC3E9 CRC64; MKDERLKNGG MQFITHYTER YSYLDAARMA LEGGCRWVQL RMKDTPVETI EPVALEVQAL CRQYGATFII DDHVELARKL HADGVHLGKK DMPIADARRI LGAEYIIGGT ANTFEDVLQH YKAGADYIGC GPFRYTTTKK NLSPILGLEG YTAIIHRMQE KDIHLPIVAI GGITIADIPA VMQTGVSGIA LSGTVLHADS PADEMKRIIS LMENEK // ID D2F148_9BACE Unreviewed; 200 AA. AC D2F148; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0969_03328; OS Bacteroides sp. D20. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=585543; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D20; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., RA White A., Ambrose C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain D20."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730108; EFA18659.1; -; Genomic_DNA. DR ProteinModelPortal; D2F148; -. DR EnsemblBacteria; EFA18659; EFA18659; HMPREF0969_03328. DR PATRIC; 35667281; VBIBacSp64485_3393. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 200 AA; 22160 MW; 749F2035FA58B8B8 CRC64; MKLIVITTPQ FFEGEAEAVT SLFQNGLEML HLRKPGASAE EMGNFLQQLP MEYMPRIVTH EQFQLASVFG LKGIHLNGRN PQIPSGYKGH VSRSCHSLEE VLKHKSDCNY VFLSPIYDSI SKEGYSSAYS CDTLQKAQQA GIIDSKVMAL GGITLEHLPE IAALGFGGAV LLGDVWQQAK EAFIPHFLHL KQLSSHPFNF // ID D2F901_STAAU Unreviewed; 213 AA. AC D2F901; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SARG_02314; OS Staphylococcus aureus subsp. aureus C101. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585149; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C101; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain C101."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730136; EFB43282.1; -; Genomic_DNA. DR ProteinModelPortal; D2F901; -. DR EnsemblBacteria; EFB43282; EFB43282; SARG_02314. DR PATRIC; 35727338; VBIStaAur8803_2260. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D2FFE0_STAAU Unreviewed; 213 AA. AC D2FFE0; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SASG_02510; OS Staphylococcus aureus subsp. aureus C427. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585151; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C427; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain C427."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730155; EFB46510.1; -; Genomic_DNA. DR ProteinModelPortal; D2FFE0; -. DR EnsemblBacteria; EFB46510; EFB46510; SASG_02510. DR PATRIC; 35732025; VBIStaAur87859_1801. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D2FP04_STAAU Unreviewed; 213 AA. AC D2FP04; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SATG_02251; OS Staphylococcus aureus subsp. aureus D139. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585152; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D139; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain D139."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730180; EFB48999.1; -; Genomic_DNA. DR ProteinModelPortal; D2FP04; -. DR EnsemblBacteria; EFB48999; EFB48999; SATG_02251. DR PATRIC; 35738385; VBIStaAur75833_2064. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23271 MW; A89EF5F25D160E89 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFADKII GLSISDLGEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D2FXD2_STAAU Unreviewed; 213 AA. AC D2FXD2; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAWG_02262; OS Staphylococcus aureus subsp. aureus M899. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585159; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M899; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain M899."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730203; EFB51472.1; -; Genomic_DNA. DR ProteinModelPortal; D2FXD2; -. DR EnsemblBacteria; EFB51472; EFB51472; SAWG_02262. DR PATRIC; 35755642; VBIStaAur116352_2188. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D2G332_STAAU Unreviewed; 213 AA. AC D2G332; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAXG_02438; OS Staphylococcus aureus subsp. aureus WBG10049. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585160; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WBG10049; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain WBG10049."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730215; EFB54734.1; -; Genomic_DNA. DR ProteinModelPortal; D2G332; -. DR EnsemblBacteria; EFB54734; EFB54734; SAXG_02438. DR PATRIC; 35759855; VBIStaAur63029_1574. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D2GBJ8_STAAU Unreviewed; 213 AA. AC D2GBJ8; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAYG_02118; OS Staphylococcus aureus subsp. aureus WW2703/97. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585161; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WW2703/97; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain WW2703/97."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730248; EFB56972.1; -; Genomic_DNA. DR ProteinModelPortal; D2GBJ8; -. DR EnsemblBacteria; EFB56972; EFB56972; SAYG_02118. DR PATRIC; 35766055; VBIStaAur7570_1918. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D2GI28_STAAU Unreviewed; 213 AA. AC D2GI28; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SDAG_02470; OS Staphylococcus aureus subsp. aureus Btn1260. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585148; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Btn1260; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain Btn1260."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730266; EFB59904.1; -; Genomic_DNA. DR ProteinModelPortal; D2GI28; -. DR EnsemblBacteria; EFB59904; EFB59904; SDAG_02470. DR PATRIC; 35795102; VBIStaAur65264_1629. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D2GTL8_STAAU Unreviewed; 213 AA. AC D2GTL8; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SFAG_02347; OS Staphylococcus aureus subsp. aureus C160. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585150; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C160; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain C160."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730293; EFB99769.1; -; Genomic_DNA. DR ProteinModelPortal; D2GTL8; -. DR EnsemblBacteria; EFB99769; EFB99769; SFAG_02347. DR PATRIC; 35802873; VBIStaAur65896_2716. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D2MTF3_CAMJU Unreviewed; 201 AA. AC D2MTF3; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 22-JAN-2014, entry version 20. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=C1336_000250213; OS Campylobacter jejuni subsp. jejuni 1336. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=683082; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1336; RX PubMed=21418497; DOI=10.1111/j.1462-2920.2011.02461.x; RA Hepworth P.J., Ashelford K.E., Hinds J., Gould K.A., Witney A.A., RA Williams N.J., Leatherbarrow H., French N.P., Birtles R.J., RA Mendonca C., Dorrell N., Wren B.W., Wigley P., Hall N., Winstanley C.; RT "Genomic variations define divergence of water/wildlife-associated RT Campylobacter jejuni niche specialists from common clonal complexes."; RL Environ. Microbiol. 13:1549-1560(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGL01000016; EFC30948.1; -; Genomic_DNA. DR ProteinModelPortal; D2MTF3; -. DR EnsemblBacteria; EFC30948; EFC30948; C1336_000250213. DR PATRIC; 36488875; VBICamJej140369_0677. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 23406 MW; 4CDEE0179287A510 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICTKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK ESKLVKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKAGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID D2MTJ2_CAMJU Unreviewed; 210 AA. AC D2MTJ2; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=C1336_000250255; OS Campylobacter jejuni subsp. jejuni 1336. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=683082; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1336; RX PubMed=21418497; DOI=10.1111/j.1462-2920.2011.02461.x; RA Hepworth P.J., Ashelford K.E., Hinds J., Gould K.A., Witney A.A., RA Williams N.J., Leatherbarrow H., French N.P., Birtles R.J., RA Mendonca C., Dorrell N., Wren B.W., Wigley P., Hall N., Winstanley C.; RT "Genomic variations define divergence of water/wildlife-associated RT Campylobacter jejuni niche specialists from common clonal complexes."; RL Environ. Microbiol. 13:1549-1560(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGL01000016; EFC30987.1; -; Genomic_DNA. DR ProteinModelPortal; D2MTJ2; -. DR EnsemblBacteria; EFC30987; EFC30987; C1336_000250255. DR PATRIC; 36488961; VBICamJej140369_0720. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22960 MW; CE192C191E85EA19 CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALI ELKGINLSGV AVVRAIMDAK DAFLAAKELK CKIYENLSLE // ID D2MYF9_CAMJU Unreviewed; 201 AA. AC D2MYF9; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 22-JAN-2014, entry version 20. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=C414_000240004; OS Campylobacter jejuni subsp. jejuni 414. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=683083; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=414; RX PubMed=21418497; DOI=10.1111/j.1462-2920.2011.02461.x; RA Hepworth P.J., Ashelford K.E., Hinds J., Gould K.A., Witney A.A., RA Williams N.J., Leatherbarrow H., French N.P., Birtles R.J., RA Mendonca C., Dorrell N., Wren B.W., Wigley P., Hall N., Winstanley C.; RT "Genomic variations define divergence of water/wildlife-associated RT Campylobacter jejuni niche specialists from common clonal complexes."; RL Environ. Microbiol. 13:1549-1560(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGM01000014; EFC32544.1; -; Genomic_DNA. DR ProteinModelPortal; D2MYF9; -. DR EnsemblBacteria; EFC32544; EFC32544; C414_000240004. DR PATRIC; 36492398; VBICamJej144577_0418. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 23321 MW; E851A11D50E05DC0 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKSK VDAIVLREKD LSEFEYYDLA KEVLGICAKQ KTTCFLHSFD KTCLKLGHRY FHAPLALLRK ESRLTKYFHV FGTSVHSKEE LLEAMSYRVN YAFVGHIFQS SCKADLEPKG LDFLKSLLRF SQIPLYAIGG INDQNIASFK GLNIAGVCMR EILMQEKDTK KYLMECKRKL Y // ID D2MYK2_CAMJU Unreviewed; 210 AA. AC D2MYK2; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=C414_000240051; OS Campylobacter jejuni subsp. jejuni 414. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=683083; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=414; RX PubMed=21418497; DOI=10.1111/j.1462-2920.2011.02461.x; RA Hepworth P.J., Ashelford K.E., Hinds J., Gould K.A., Witney A.A., RA Williams N.J., Leatherbarrow H., French N.P., Birtles R.J., RA Mendonca C., Dorrell N., Wren B.W., Wigley P., Hall N., Winstanley C.; RT "Genomic variations define divergence of water/wildlife-associated RT Campylobacter jejuni niche specialists from common clonal complexes."; RL Environ. Microbiol. 13:1549-1560(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGM01000014; EFC32587.1; -; Genomic_DNA. DR ProteinModelPortal; D2MYK2; -. DR EnsemblBacteria; EFC32587; EFC32587; C414_000240051. DR PATRIC; 36492494; VBICamJej144577_0466. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22908 MW; EEE21B2C4E558710 CRC64; MKNKLDLSLY LVASKGNKSE ECFLNSLENA IKGGVSIVQL REKELSASEF YKLGLKVQKL CKAYKIPFLI NDRIDIALAL DADGVHLGQE DLEIKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IRATPTKESS LLSLKLLAQI CDKSPIGVVA IGGIDKEVLS ELKGIKLSGV AVVRAIMDAK DVYLAAKELK CKIHENLSLK // ID D2N922_STAA5 Unreviewed; 213 AA. AC D2N922; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SAPIG2134; OS Staphylococcus aureus (strain MRSA ST398 / isolate S0385). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=523796; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MRSA ST398 / isolate S0385; RX PubMed=20546576; DOI=10.1186/1471-2164-11-376; RA Schijffelen M.J., Boel C.H., van Strijp J.A., Fluit A.C.; RT "Whole genome analysis of a livestock-associated methicillin-resistant RT Staphylococcus aureus ST398 isolate from a case of human RT endocarditis."; RL BMC Genomics 11:376-376(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM990992; CAQ50520.1; -; Genomic_DNA. DR RefSeq; YP_005734892.1; NC_017333.1. DR ProteinModelPortal; D2N922; -. DR EnsemblBacteria; CAQ50520; CAQ50520; SAPIG2134. DR GeneID; 12322161; -. DR KEGG; sug:SAPIG2134; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23278 MW; 4683C6CD4C160B2C CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLGEY AKSDLTHVDY IGVGPIYPTP SKNDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D2NEM9_ECOS5 Unreviewed; 211 AA. AC D2NEM9; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECSF_3847; OS Escherichia coli O150:H5 (strain SE15). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=431946; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SE15; RX PubMed=20008064; DOI=10.1128/JB.01543-09; RA Toh H., Oshima K., Toyoda A., Ogura Y., Ooka T., Sasamoto H., RA Park S.H., Iyoda S., Kurokawa K., Morita H., Itoh K., Taylor T.D., RA Hayashi T., Hattori M.; RT "Complete genome sequence of the wild-type commensal Escherichia coli RT strain SE15, belonging to phylogenetic group B2."; RL J. Bacteriol. 192:1165-1166(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009378; BAI57387.1; -; Genomic_DNA. DR RefSeq; YP_003351837.1; NC_013654.1. DR ProteinModelPortal; D2NEM9; -. DR EnsemblBacteria; BAI57387; BAI57387; ECSF_3847. DR GeneID; 12925831; -. DR KEGG; ese:ECSF_3847; -. DR PATRIC; 36719713; VBIEscCol158062_4004. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; ECOL431946:GIA0-3941-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23027 MW; 9C5E679AD0EA42DC CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D2NPG3_ROTMD Unreviewed; 206 AA. AC D2NPG3; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=RMDY18_16990; OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Rothia. OX NCBI_TaxID=680646; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DY-18; RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K., RA Fukushima H.; RT "Complete genome sequence of Rothia mucilaginosa DJ."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011540; BAI65531.1; -; Genomic_DNA. DR RefSeq; YP_003363351.1; NC_013715.1. DR ProteinModelPortal; D2NPG3; -. DR EnsemblBacteria; BAI65531; BAI65531; RMDY18_16990. DR GeneID; 8694987; -. DR KEGG; rmu:RMDY18_16990; -. DR PATRIC; 35273883; VBIRotMuc152186_1467. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6PZXB0; -. DR BioCyc; RMUC680646:GH63-1673-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). SQ SEQUENCE 206 AA; 22058 MW; 96EDDCDAB58D7900 CRC64; MTRETHPYTT PARPLDLNLY LVTGEHPLET VQAAKHATCI QVRSKPISAR ELYQLTEAIA GIIQPHQTLL VDDRVDVALA LRARGVRVDG VHIGQDDLPV ADARALLGAD AIIGLTTGTR QLVEESNKIA RLIDYIGTGP FRPSPTKQSN RPPLGIDGLR ELAELSAVPT VAIGDITPED CPAIRTTGVA GIAMVRAFVD NPALQA // ID D2NX58_LISM1 Unreviewed; 214 AA. AC D2NX58; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LM5578_0356; OS Listeria monocytogenes serotype 1/2a (strain 08-5578). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=653938; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=08-5578; RX PubMed=20167121; DOI=10.1186/1471-2164-11-120; RA Gilmour M.W., Graham M., Van Domselaar G., Tyler S., Kent H., RA Trout-Yakel K.M., Larios O., Allen V., Lee B., Nadon C.; RT "High-throughput genome sequencing of two Listeria monocytogenes RT clinical isolates during a large foodborne outbreak."; RL BMC Genomics 11:120-120(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001602; ADB67112.1; -; Genomic_DNA. DR RefSeq; YP_003412474.1; NC_013766.1. DR ProteinModelPortal; D2NX58; -. DR EnsemblBacteria; ADB67112; ADB67112; LM5578_0356. DR GeneID; 8747348; -. DR KEGG; lmn:LM5578_0356; -. DR PATRIC; 35275140; VBILisMon159512_0361. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; LMON653938:GJ8G-360-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22412 MW; 0B2A49D058F09153 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ KLCAKYQVPF IINDDVALAL EIGADGIHVG QTDEAIRQVI ASCSGKMKIG LSVHSVSEAK EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GITIPIVGIG GINETNSAEV LTAGADGVSV ISAITQSDDC HSVIKQLKNP GSPS // ID D2P8M7_LISM2 Unreviewed; 214 AA. AC D2P8M7; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LM5923_0355; OS Listeria monocytogenes serotype 1/2a (strain 08-5923). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=637381; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=08-5923; RX PubMed=20167121; DOI=10.1186/1471-2164-11-120; RA Gilmour M.W., Graham M., Van Domselaar G., Tyler S., Kent H., RA Trout-Yakel K.M., Larios O., Allen V., Lee B., Nadon C.; RT "High-throughput genome sequencing of two Listeria monocytogenes RT clinical isolates during a large foodborne outbreak."; RL BMC Genomics 11:120-120(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001604; ADB70201.1; -; Genomic_DNA. DR RefSeq; YP_003415563.1; NC_013768.1. DR ProteinModelPortal; D2P8M7; -. DR EnsemblBacteria; ADB70201; ADB70201; LM5923_0355. DR GeneID; 8757154; -. DR KEGG; lmy:LM5923_0355; -. DR PATRIC; 32254448; VBILisMon5116_0360. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; LMON637381:GH7Z-361-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22412 MW; 0B2A49D058F09153 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ KLCAKYQVPF IINDDVALAL EIGADGIHVG QTDEAIRQVI ASCSGKMKIG LSVHSVSEAK EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GITIPIVGIG GINETNSAEV LTAGADGVSV ISAITQSDDC HSVIKQLKNP GSPS // ID D2Q0C3_KRIFD Unreviewed; 219 AA. AC D2Q0C3; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Kfla_2850; OS Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Nocardioidaceae; Kribbella. OX NCBI_TaxID=479435; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.; RT "The complete genome of Kribbella flavida DSM 17836."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001736; ADB31915.1; -; Genomic_DNA. DR RefSeq; YP_003380714.1; NC_013729.1. DR ProteinModelPortal; D2Q0C3; -. DR EnsemblBacteria; ADB31915; ADB31915; Kfla_2850. DR GeneID; 8719455; -. DR KEGG; kfl:Kfla_2850; -. DR PATRIC; 32236130; VBIKriFla67707_2837. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; KFLA479435:GI0F-2878-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23228 MW; FA602F4320D6427C CRC64; MTEHTAPLRD RLDAARLYLC TDAREKQGDL EQFLDAALGG GVDIVQLRQK EMEAADELAA LEVFADACRR HGKLLAVNDR ADVAFTAGAD VLHLGQRDLP VPAARAITGP DVIVGRSTHT FSQVNAAVAE AGSDYFCVGP TWETPTKPGR TAAGLDLVAY AAGRPQVKPW FAIGGIDLER LDEVVEAGAT RVVVVRAITE ADDPAAAAAE FGRRLRAAG // ID D2Q5H7_BIFDB Unreviewed; 836 AA. AC D2Q5H7; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 34. DE SubName: Full=Thiamine biosynthesis protein ThiC; DE EC=2.5.1.3; GN Name=thiC; OrderedLocusNames=BDP_1598; OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / OS Bd1). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=401473; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1; RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785; RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., RA Bottacini F., Canchaya C., Claesson M.J., He F., Mantzourani M., RA Mulas L., Ferrarini A., Gao B., Delledonne M., Henrissat B., RA Coutinho P., Oggioni M., Gupta R.S., Zhang Z., Beighton D., RA Fitzgerald G.F., O'Toole P.W., van Sinderen D.; RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic RT adaptation to the human oral cavity."; RL PLoS Genet. 5:E1000785-E1000785(2009). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001750; ADB10192.1; -; Genomic_DNA. DR RefSeq; YP_003361016.1; NC_013714.1. DR ProteinModelPortal; D2Q5H7; -. DR EnsemblBacteria; ADB10192; ADB10192; BDP_1598. DR GeneID; 8692371; -. DR KEGG; bde:BDP_1598; -. DR PATRIC; 31957325; VBIBifDen66312_1516. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR OMA; INTICSA; -. DR OrthoDB; EOG6NWBM5; -. DR BioCyc; BDEN401473:GH09-1541-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Transferase; Zinc. SQ SEQUENCE 836 AA; 92330 MW; CEA2480BEBB9077E CRC64; MVGPQDCKGR PITDVVDDAL RGGATFIQLR AKNTDAKDLT LMAQDIAQII EDNGKSDAVA FVIDDRVDVV WQARNKGIKV DGVHIGQTDM EPREARALLG EEAIVGLSAE TESLVRLINE LPNGCIDYIG AGPLHVSTTK PEASVGGNDG SGNTLDEDQI NTICTASDFP VVVGGGVTAD DMEMLARSKA AGWFVVSAIA GADDPEAATR EMVTRWKAVR GETKHGFAPR VQSADTATTT DTQMTESNNG KFTNAKEAKA SSKLAKQQRV DIAARGSKQR DKAHVRKTTP VHFENRFGSY DLEVPYTEIK LSDTPGVGPN APFKDYNTEG PKCDPKEGLA PLRLDWIRDR GDVEEYEGRR RNLEDDGKRA IKRGKASKEW RGRQHKPLKA KDHPITQMWY ARHDIITPEM RYVAEREHCD VELVRSELAA GRAVMPCNIN HPEAEPMIIG SRFLTKLNAN MGNSAVTSSI DEEVEKLTWA TKWGADTVMD LSTGNDIHTT REWILRNSPV PIGTVPMYQA LEKVEDDASK LSWELFRDTV IEQCEQGVDY MTIHAGVLLR FVPLTANRMT GIVSRGGSIM AEWCLQHHQE SFLYTHFDEL CEIFAKYDVA FSLGDGLRPG SLADANDAAQ FAELMTLGEL TQRAWEHDVQ VMIEGPGHIP FDTVRMNIEM EKAICKDAPF YTLGPLTTDT APGYDHITSA IGGVEIARYG TAMLCYVTPK EHLGLPNKDD VKQGVIAYKI ACHAADIAKH HPHAIDRDNA MSKARFEFRW LDQFNLSYDP DTAIAFHDDT LPAEPAKMAH FCSMCGPKFC SMAISQNIRR KFGNAEAQEK LVADAQ // ID D2QQ70_SPILD Unreviewed; 206 AA. AC D2QQ70; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Slin_3495; OS Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Spirosoma. OX NCBI_TaxID=504472; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S., RA Goker M., Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Spirosoma linguale DSM 74."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001769; ADB39503.1; -; Genomic_DNA. DR RefSeq; YP_003388302.1; NC_013730.1. DR ProteinModelPortal; D2QQ70; -. DR EnsemblBacteria; ADB39503; ADB39503; Slin_3495. DR GeneID; 8727248; -. DR KEGG; sli:Slin_3495; -. DR PATRIC; 32436921; VBISpiLin97822_3494. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; SLIN504472:GHKB-3520-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21819 MW; C38827656A5C3707 CRC64; MNGLYLVTDS GIAQQAGHSL PFVVEEACRA GVRWVQLREK ELSTRAFVEL GVVLKRITQT YGAKLIINDR VDIALAVDAD GVHVGQDDMP YELVRSLIGP DKIIGLSINN MAELEAVEGA DLDYLGIATI FPTGTKTDTS SLLGLDGLRA ICQQTSLPTF AIGGINVTNI QSVLQAGASG AAVVSAICGQ PSPYEASREL IHLTNP // ID D2QUP8_SPILD Unreviewed; 212 AA. AC D2QUP8; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Slin_6573; OS Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Spirosoma. OX NCBI_TaxID=504472; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S., RA Goker M., Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Spirosoma linguale DSM 74."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001769; ADB42530.1; -; Genomic_DNA. DR RefSeq; YP_003391329.1; NC_013730.1. DR ProteinModelPortal; D2QUP8; -. DR EnsemblBacteria; ADB42530; ADB42530; Slin_6573. DR GeneID; 8730359; -. DR KEGG; sli:Slin_6573; -. DR PATRIC; 32443085; VBISpiLin97822_6542. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CVGPVHA; -. DR BioCyc; SLIN504472:GHKB-6632-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 31 35 HMP-PP binding (By similarity). FT REGION 128 130 THZ-P binding (By similarity). FT METAL 64 64 Magnesium (By similarity). FT METAL 83 83 Magnesium (By similarity). FT BINDING 63 63 HMP-PP (By similarity). FT BINDING 102 102 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22624 MW; A2632179EE053EF8 CRC64; MSQYMISPLQ YITTRPEQAD AACHAGANWI QLRLKNLAYA DWKAIALETL AVCRQYNATL ILNDNPKLAA DIGADGVHLG QEDMPVAEAR ALLGDRFIIG GTANTLETIL AHHRDGVNYV GLGPFRFTTT KEKLSPILGL DGYARILSAL PQRQISLPVI AIGGITLADV PALLATGVYG VAVSSAITGA SDPAAQTRLF LSQLTTSTSF FE // ID D2QUQ2_SPILD Unreviewed; 201 AA. AC D2QUQ2; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 16-OCT-2013, entry version 26. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Slin_6577; OS Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Spirosoma. OX NCBI_TaxID=504472; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S., RA Goker M., Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Spirosoma linguale DSM 74."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001769; ADB42534.1; -; Genomic_DNA. DR RefSeq; YP_003391333.1; NC_013730.1. DR ProteinModelPortal; D2QUQ2; -. DR EnsemblBacteria; ADB42534; ADB42534; Slin_6577. DR GeneID; 8730363; -. DR KEGG; sli:Slin_6577; -. DR PATRIC; 32443093; VBISpiLin97822_6546. DR KO; K00788; -. DR BioCyc; SLIN504472:GHKB-6636-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 21412 MW; A412D0FBA96E43CB CRC64; MNKNPFLLLG ITDGSPQSLA IPTIQALLTG GLDFMYWRTS ADNAGLTQLS AGFKPSVLLS ATKGSAVPAS FRWHLKDADR QVANFADGLP FSTSIHSLSE WPRLAGQVEL VFYSPLFPSI SKPGYGPLSS LAVIEQQISA IRQQHTALPR LIGLGGIQAE NVALVREAGF DGAALMGALW QAPDAVDALQ QIREVLSVKD G // ID D2QZS3_PIRSD Unreviewed; 380 AA. AC D2QZS3; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Psta_1882; OS Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella OS staleyi). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Pirellula. OX NCBI_TaxID=530564; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128; RX PubMed=21304671; DOI=10.4056/sigs.51657; RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., RA Lucas S., Glavina T., Del Rio., Nolan M., Chen F., Tice H., RA Pitluck S., Cheng J.F., Chertkov O., Brettin T., Han C., Detter J.C., RA Kuske C., Bruce D., Goodwin L., Ovchinikova G., Pati A., RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Chain P., Rohde M., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Complete genome sequence of Pirellula staleyi type strain (ATCC RT 27377)."; RL Stand. Genomic Sci. 1:308-316(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001848; ADB16556.1; -; Genomic_DNA. DR RefSeq; YP_003370416.1; NC_013720.1. DR ProteinModelPortal; D2QZS3; -. DR EnsemblBacteria; ADB16556; ADB16556; Psta_1882. DR GeneID; 8705811; -. DR KEGG; psl:Psta_1882; -. DR PATRIC; 32287464; VBIPirSta4342_1964. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR BioCyc; PSTA530564:GHPR-1896-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 380 AA; 41201 MW; 15423EBDD672E02B CRC64; MTYDKNSGDD HRPNLPPSSG EQLAALRILD ANFNRVSEGL RVVEEYCRFA LEDRHLAQNA KEIRHDIGHL AAGISPETLA KARETLRDVG TGVTLGSEKT RAGILDVVIA STKRVEQSLR AIEEYAKLGY PQLSAAAKQL RYRAYTLARA MLLTDHHRQQ MAKRLLYVLI DGRASDAEFA SLVRMLVEAR VDVLQLRDKR LTDRQLLEKA QLLKSLVEQF APAGAEETAE RPLLVMNDRP DLALLARLDG VHVGQDELPV DAVRKIVGPE MLVGVSTHSI EQARQAVLDG ASYIGCGPVF PSNTKQFGSF VGTEFLAQVA AEIQLPAFAI GGITLENLPQ VTAAGFSRVA VSAAVSSAAD PATAARLLKT ELLAAAARQA // ID D2RBC2_GARV4 Unreviewed; 885 AA. AC D2RBC2; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 33. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; OrderedLocusNames=HMPREF0424_0892; OS Gardnerella vaginalis (strain 409-05). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=553190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=409-05; RX PubMed=20865041; DOI=10.1371/journal.pone.0012411; RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., RA Sutton G., Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., RA Gibbs R.A., Leigh S.R., Stumpf R., White B.A., Highlander S.K., RA Nelson K.E., Wilson B.A.; RT "Comparative genomics of Gardnerella vaginalis strains reveals RT substantial differences in metabolic and virulence potential."; RL PLoS ONE 5:E12411-E12411(2010). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001849; ADB14321.1; -; Genomic_DNA. DR RefSeq; YP_003374107.1; NC_013721.1. DR ProteinModelPortal; D2RBC2; -. DR EnsemblBacteria; ADB14321; ADB14321; HMPREF0424_0892. DR GeneID; 8709229; -. DR KEGG; gva:HMPREF0424_0892; -. DR PATRIC; 32147632; VBIGarVag136958_0780. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR OMA; INTICSA; -. DR OrthoDB; EOG6NWBM5; -. DR BioCyc; GVAG553190:GJPT-889-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 885 AA; 98705 MW; 21C6DA1164519CE7 CRC64; MTSNYPYASM RNQFNLSACF IADPQACNNR PLTDIVDDAL RAGATFIRLH CNNENAKEIT TIARDIAQII EDNNKCDSVT FVIDERVDVV WQARNQSIKV DGVHLAQSDM EPREARALLG EDAVIGLSVE TESLVKVINE LPDGCIDYIC VTAMRNPEEG CESTTAAYEL EANHTTLDEA KINTICSASD FPVLVGGRTA LDDIDTIAHT KAAGWFVSEA LYSSETPEST MREFVEHWKA VRGEEKHGYA KRVIVAENSE SKSSETQEKK PTFINAKEAK DAAKLAKQQR VDIAARGCTQ RDKAHIRKTT PIHFEYEYGS YDLEVPYTEI KLSDTPGVGP NPPFKDYNTE GPKCDPKEGL APLRLDWIRD RGDVVEYEGR RRNLQDDGKR AIKRGKASKE WRGRTHKPMK GADHPITQMW YARHGITTPE MQYVATRENC DVELVREEVA AGRAVIPCNI NHPEAEPMII GSRFLTKLNA NMGNSAVTSS IDEEVEKLTW ATKWGADTVM DLSTGNDIHT TREWILRNSP VPIGTVPMYQ ALEKVEDDAS KLSWELFRDT VIEQCEQGVD YMTIHAGVLL RYVPLTANRV TGIVSRGGSI MAEWCLQHHQ ESFLYTHFEE LCEIFAKYDV AFSLGDGLRP GSLADANDAA QLSELMTLGE LTKIAWKHDV QVMIEGPGHV PFDTVRMNIE MEKAICQNAP FYTLGPLTTD TAPGYDHITS AIGGVEIARY GTAMLCYVTP KEHLGLPNKD DVKQGVIAYK IACHAADLAK HHPHAMDRDN AISKARFEFR WLDQFNLSYD PDTAIAFHDE TLPAEPAKMA HFCSMCGPKF CSMAISQNIR KRFGGAAQQE QLVEEARSQA IADGMKEMSK KFQESGSSLY QSVKA // ID D2RC21_GARV4 Unreviewed; 525 AA. AC D2RC21; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 28. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=HMPREF0424_1158; OS Gardnerella vaginalis (strain 409-05). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=553190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=409-05; RX PubMed=20865041; DOI=10.1371/journal.pone.0012411; RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., RA Sutton G., Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., RA Gibbs R.A., Leigh S.R., Stumpf R., White B.A., Highlander S.K., RA Nelson K.E., Wilson B.A.; RT "Comparative genomics of Gardnerella vaginalis strains reveals RT substantial differences in metabolic and virulence potential."; RL PLoS ONE 5:E12411-E12411(2010). CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001849; ADB13533.1; -; Genomic_DNA. DR RefSeq; YP_003374356.1; NC_013721.1. DR ProteinModelPortal; D2RC21; -. DR EnsemblBacteria; ADB13533; ADB13533; HMPREF0424_1158. DR GeneID; 8709453; -. DR KEGG; gva:HMPREF0424_1158; -. DR PATRIC; 32148120; VBIGarVag136958_1017. DR HOGENOM; HOG000106869; -. DR KO; K00878; -. DR OMA; RECKEND; -. DR OrthoDB; EOG628F8M; -. DR BioCyc; GVAG553190:GJPT-1152-MONOMER; -. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Thiamine biosynthesis; Transferase. SQ SEQUENCE 525 AA; 56230 MW; 8110078BD7645FB7 CRC64; MTTCNTEKTT NCNEANEYCT SSTTQVDTCF SVRARRRMFL NDVRQCIERV RTQQPLTHCI TNVIVQDITA NALLAAGASP IMVTDPEEAH ALAQIATGVL INVGTFHQPE TSEYMRAAVE GCEKADTPWV LDPVGIGVPA LAPRARFIHE IIKHHPTVIR ANASEIMALA GKESNGKGVD SHDNVNDALQ AARELAKKYG SVVAISGEKD AIYAHGCLAR VTGGHKTMTK VVGTGCALGA LVAAYVGANP ERPLAATVAA HVHAAAAGTW AARQTTAPGT FRTLWMDALS TLSVNDMFSL TNIEFTVEPV DWTLYLVTDP RMGNRPEEEV AVESVEGGVT VVQLRDKYSD DAEISAKAKK LRHALIDSGH GDVPVFIDDH VDCAAQLGFN LHVGQKDTPF VEARKAMPAE WMVGLSCARP DLMEKAYREC KENDVPLPDV IGIGAAFETH TKAHDVPPLG VDGVNEVAKV AHSMGVKTLA IGGIHENTVF PIRGLELDGV CTVSALMCAE DAGKVARELK SVITE // ID D2RHU1_ARCPA Unreviewed; 204 AA. AC D2RHU1; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Arcpr_0803; OS Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / OS Av18). OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; OC Archaeoglobaceae; Archaeoglobus. OX NCBI_TaxID=572546; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5631 / JCM 9629 / NBRC 100127 / Av18; RX DOI=10.4056/sigs.942153; RA von Jan M., Lapidus A., Glavina del Rio T., Copeland A., Tice H., RA Cheng J.-F., Lucas S., Chen F., Nolan M., Goodwin L., Han C., RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., RA Chertkov O., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.-J., Jeffries C.D., Saunders E., Brettin T., Detter J.C., RA Chain P., Eichinger K., Huber H., Spring S., Rohde M., Goker M., RA Wirth R., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N., Klenk H.-P.; RT "Complete genome sequence of Archaeoglobus profundus type strain RT (AV18)."; RL Stand. Genomic Sci. 2:327-346(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001857; ADB57866.1; -; Genomic_DNA. DR RefSeq; YP_003400539.1; NC_013741.1. DR ProteinModelPortal; D2RHU1; -. DR EnsemblBacteria; ADB57866; ADB57866; Arcpr_0803. DR GeneID; 8739464; -. DR KEGG; apo:Arcpr_0803; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; APRO572546:GJI1-821-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 127 129 THZ-P binding (By similarity). FT REGION 178 179 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 102 102 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 158 158 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22669 MW; C21304E2FC39B44F CRC64; MKIGLYFITS SEFSRTHEEL AEAVLRVGVR FIQFREKNMS ARQMFSVAKN LRKLTWEYSA TLIVNDRVDL ALAVEADGVH LGQDDLPFEV VKDIFDGIVG VSTHSVDEAK KAERYIDYIS AGPVFRTTTK KNAKEPIGLE GLRRIVSSVK KPVVAIGGIN KFNIEDVLKT GVKGVAVISA IANSQNPEKS AKELLEIVKR YLDD // ID D2RIG4_ACIFV Unreviewed; 210 AA. AC D2RIG4; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Acfer_0463; OS Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=591001; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25085 / DSM 20731 / VR4; RX DOI=10.4056/sigs.1002553; RA Chang Y., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J., Ha C., RA Detter J., Bruce D., Goodwin L., Pitluck S., Mikhailova N., RA Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Jeffries C., Brettin T., Rohde M., RA Goker M., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H.; RT "Complete genome sequence of Acidaminococcus fermentans type strain RT (VR4)."; RL Stand. Genomic Sci. 3:1-14(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001859; ADB46866.1; -; Genomic_DNA. DR RefSeq; YP_003398181.1; NC_013740.1. DR ProteinModelPortal; D2RIG4; -. DR EnsemblBacteria; ADB46866; ADB46866; Acfer_0463. DR GeneID; 8736920; -. DR KEGG; afn:Acfer_0463; -. DR PATRIC; 31907507; VBIAciFer109666_0491. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; AFER591001:GHUL-490-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22674 MW; 20E64A3EB955AC78 CRC64; MKKFDLSLYL VTDRHCLRGR DFYEAVEEAL RAGVTLLQLR EKDMGLEELV AEGRKVRKLC RKYQVPFLVD DNVEAARILE ADGVHLGQED DAIEKARSVL GPEAIIGISA HNLEEALKAQ ASGADYLGVG ALYPTGSKKD ASLLAPGMLE KIVQAVKIPV VGIGGIHEAQ LDQVLDQGAA GCAMISAILG AEDIGAAVER MKARIRAREK // ID D2RKF9_ACIFV Unreviewed; 189 AA. AC D2RKF9; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Acfer_1200; OS Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=591001; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25085 / DSM 20731 / VR4; RX DOI=10.4056/sigs.1002553; RA Chang Y., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J., Ha C., RA Detter J., Bruce D., Goodwin L., Pitluck S., Mikhailova N., RA Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Jeffries C., Brettin T., Rohde M., RA Goker M., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H.; RT "Complete genome sequence of Acidaminococcus fermentans type strain RT (VR4)."; RL Stand. Genomic Sci. 3:1-14(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001859; ADB47561.1; -; Genomic_DNA. DR RefSeq; YP_003398876.1; NC_013740.1. DR ProteinModelPortal; D2RKF9; -. DR EnsemblBacteria; ADB47561; ADB47561; Acfer_1200. DR GeneID; 8737684; -. DR KEGG; afn:Acfer_1200; -. DR PATRIC; 31908923; VBIAciFer109666_1173. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CIREALY; -. DR BioCyc; AFER591001:GHUL-1254-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 189 AA; 20882 MW; 506C9CEB4A080EEC CRC64; MSFPLYCITN RHLYALPFLE QLDRILALRP AGVILREKDL SLEEYLALGR QVLEKCRRAG VPCWFHTFLE AAVELRPDGI QLPMPVLREL PAGWRQGFPG RVGASCHSLD EVQEAARLGA DCCTFSHVYP TQCKPGLPPR GLEALRQVCA QSPVPVYALG GVTPEKIPEL EKAGAAGAVM MGWWKTVDC // ID D2RU78_HALTV Unreviewed; 222 AA. AC D2RU78; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Htur_0246; OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / NCIMB 13204 / OS VKM B-1734) (Halococcus turkmenicus). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Haloterrigena. OX NCBI_TaxID=543526; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51198 / DSM 5511 / NCIMB 13204 / VKM B-1734; RX PubMed=21304683; DOI=10.4056/sigs.681272; RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A., RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., RA Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., RA Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M., RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Rohde M., Goker M., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., RA Kyrpides N.C.; RT "Complete genome sequence of Haloterrigena turkmenica type strain RT (4k)."; RL Stand. Genomic Sci. 2:107-116(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001860; ADB59147.1; -; Genomic_DNA. DR RefSeq; YP_003401820.1; NC_013743.1. DR ProteinModelPortal; D2RU78; -. DR EnsemblBacteria; ADB59147; ADB59147; Htur_0246. DR GeneID; 8740809; -. DR KEGG; htu:Htur_0246; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; HTUR543526:GH7B-246-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 22711 MW; A42BBCB45EC5A42E CRC64; MDPSEYGTYL VTQQSISGDR STVDVVRDAI AGGVDVVQLR EKDTDARWRY ELGLELRELT AEADVDLIVN DRVDVAEAID ADGVHVGQSD LPVGVARDLL GPEAIVGCST ATVEEALEAE AAGADYLGVG TVYGTTSKEV DRYKDGVGPE RIAEIVDAVS IPVVGIGGIT ADNAGPVVEA GATGVAVISE ITAADEPRAA TAALADAVET AKGVGDGSVA DE // ID D2S7Z7_GEOOG Unreviewed; 219 AA. AC D2S7Z7; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Gobs_5050; OS Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / OS G-20). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Geodermatophilaceae; Geodermatophilus. OX NCBI_TaxID=526225; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / G-20; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Geodermatophilus obscurus DSM 43160."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001867; ADB77577.1; -; Genomic_DNA. DR RefSeq; YP_003411948.1; NC_013757.1. DR ProteinModelPortal; D2S7Z7; -. DR EnsemblBacteria; ADB77577; ADB77577; Gobs_5050. DR GeneID; 8756752; -. DR KEGG; gob:Gobs_5050; -. DR PATRIC; 32179325; VBIGeoObs49253_5047. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; GOBS526225:GI00-5110-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22083 MW; 1E552757CB59EFF0 CRC64; MSRPFDPTLY LVTDTALARP RPVADVVRAA VAGGVTTVQV RDKTASRREL LELTRTVQAA LADRPDVALW VDDAVDVALL AGADGVHVGQ DDLPPAEVRA LLGPGRLLGF SVSSVAELDV ARALPAGTVD LVGIGPVWTT PTKPDAGSAL GPGGVRTLAD AARAAGFTTV AIGGIDATRA AEVAATGVDG VCVVSAVCTA PDPAAAARAL RAEIEGVRV // ID D2SGL8_GEOOG Unreviewed; 199 AA. AC D2SGL8; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 29. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Gobs_0091; OS Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / OS G-20). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Geodermatophilaceae; Geodermatophilus. OX NCBI_TaxID=526225; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / G-20; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Geodermatophilus obscurus DSM 43160."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001867; ADB72900.1; -; Genomic_DNA. DR RefSeq; YP_003407271.1; NC_013757.1. DR ProteinModelPortal; D2SGL8; -. DR EnsemblBacteria; ADB72900; ADB72900; Gobs_0091. DR GeneID; 8751737; -. DR KEGG; gob:Gobs_0091; -. DR PATRIC; 32169309; VBIGeoObs49253_0091. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VMRAEDP; -. DR BioCyc; GOBS526225:GI00-94-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 199 AA; 20145 MW; 0A31CF1664CDDA6F CRC64; MSELASSTDD TARLPRLLVV TDRTQAAGPL ADVVAAAVDA GARAVLLRDR DLPDDERAAL AAELRTVLTP VGGLLVTAGV GGDGAVHLAA AEPFPDPRPA LVGRSCHSAA ELLQARAEGC DWAFLSPVHP TASKPGYGPA LGVEGFARLR PLGPPTYALG GVGPDDVPAL LTAGAHGVAV MGPVMRDPAV VRDYLAALA // ID D2TCX5_ERWP6 Unreviewed; 214 AA. AC D2TCX5; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EPYR_00271; OS Erwinia pyrifoliae (strain DSM 12163 / CIP 106111 / Ep16/96). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=644651; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12163 / CIP 106111 / Ep16/96; RX PubMed=20047678; DOI=10.1186/1471-2164-11-2; RA Smits T.H., Jaenicke S., Rezzonico F., Kamber T., Goesmann A., RA Frey J.E., Duffy B.; RT "Complete genome sequence of the fire blight pathogen Erwinia RT pyrifoliae DSM 12163T and comparative genomic insights into plant RT pathogenicity."; RL BMC Genomics 11:2-2(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN392235; CAY72570.1; -; Genomic_DNA. DR RefSeq; YP_005801022.1; NC_017390.1. DR ProteinModelPortal; D2TCX5; -. DR EnsemblBacteria; CAY72570; CAY72570; EPYR_00271. DR GeneID; 12934839; -. DR KEGG; epr:EPYR_00271; -. DR PATRIC; 36674338; VBIErwPyr40668_0253. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; EPYR644651:GLCX-294-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23269 MW; ED72E41EC054E8D6 CRC64; MSRGAFPTTA ARLGLYPVVD NVQWIARLLD TGVRTLQLRI KDRAEQQVEQ QVAEAIALGK RYQARLFIND YWRLAVKHQA YGVHLGQQDL DIADLDSIHA AGLRLGLSTH DDAELDRALV ERPSYIALGH VFPTQTKYMP SEPQGLAALT RYVKRLSGIP TVAIGGISLA RAPAVLATGV GSIAVVSAIT QASDWQAATR QLLALAEAQR PARV // ID D2TTG5_CITRI Unreviewed; 214 AA. AC D2TTG5; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ROD_37591; OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype OS 4280). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=637910; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ICC168; RX PubMed=19897651; DOI=10.1128/JB.01144-09; RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., RA Schroeder G.N., Quail M.A., Lennard N., Corton C., Barron A., RA Clark L., Toribio A.L., Parkhill J., Dougan G., Frankel G., RA Thomson N.R.; RT "The Citrobacter rodentium genome sequence reveals convergent RT evolution with human pathogenic Escherichia coli."; RL J. Bacteriol. 192:525-538(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN543502; CBG90464.1; -; Genomic_DNA. DR RefSeq; YP_003367199.1; NC_013716.1. DR ProteinModelPortal; D2TTG5; -. DR EnsemblBacteria; CBG90464; CBG90464; ROD_37591. DR GeneID; 8714891; -. DR KEGG; cro:ROD_37591; -. DR PATRIC; 32031192; VBICitRod33214_3577. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; CROD637910:GJIG-3783-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23503 MW; E3499EBB42B6D1AD CRC64; MMYQPDFPSV PFRLGLYPVV DSVAWIERLL EAGVRTIQLR IKDKRDEEVE ADVVAAIELG RRYDARLFIN DYWRLAIRHC AYGIHLGQED LQSTDLKAIQ AAGLRLGVST HDDMEIDVAL AARPSYIALG HVFPTQTKQM PSAPQGLEQL ARHIERLADY PTVAIGGISL ERAPAVLSTG VGSIAVVSAI TRVADWRTAT AQLLDLAGAG DERS // ID D2U3P7_9ENTR Unreviewed; 244 AA. AC D2U3P7; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ARN_32800; OS Arsenophonus nasoniae (son-killer infecting Nasonia vitripennis). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Arsenophonus. OX NCBI_TaxID=638; RN [1] RP NUCLEOTIDE SEQUENCE. RA Wilkes T., Darby A.C., Choi J., Colborne J.K., Werren J.H., RA Hurst G.D.D.; RT "The draft genome sequence of Arsenophonus nasoniae, son-killer RT bacterium of Nasonia vitripennis, reveals genes associated with RT virulence and symbiosis."; RL Insect Mol. Biol. 19:59-73(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN545258; CBA76015.1; -; Genomic_DNA. DR ProteinModelPortal; D2U3P7; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 67 71 HMP-PP binding (By similarity). FT REGION 164 166 THZ-P binding (By similarity). FT REGION 216 217 THZ-P binding (By similarity). FT METAL 100 100 Magnesium (By similarity). FT METAL 119 119 Magnesium (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 HMP-PP (By similarity). FT BINDING 196 196 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 244 AA; 27452 MW; D70623C3E80EDB69 CRC64; MPHKWHTYRQ HFAPRAVSYT TAWRRFPMTK WSEHAFASTE QKLGLYPVVD SVEWIKRLLN VGVTTVQLRI KDPLANNLEA DIKQAIMLSQ RYQARLFIND YWQLAIKYGA YGVHLGQEDI NFADLNRLKK AGLRLGISTH NQQELARAKQ LRPSYIALGH IFPTRTKLMS SSPQGLISLK QQVNATPDYP TIAIGGISLA RVPAVLATGV GGIAMVSAIT KSPSWYKVVT QLLHLIEGKE IIHA // ID D2UC39_XANAP Unreviewed; 207 AA. AC D2UC39; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=XALC_0778; OS Xanthomonas albilineans (strain GPE PC73 / CFBP 7063). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=380358; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GPE PC73 / CFBP 7063; RA Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., RA Cociancich S., Couloux A., Darrasse A., Gouzy J., Jacques M.A., RA Lauber E., Manceau C., Mangenot S., Poussier S., Segurens B., RA Szurek B., Verdier V., Arlat M., Rott P.; RT "The complete genome sequence of Xanthomonas albilineans provides new RT insights into the reductive genome evolution of the xylem-limited RT Xanthomonadaceae."; RL BMC Genomics 10:616-616(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP565176; CBA15296.1; -; Genomic_DNA. DR RefSeq; YP_003375284.1; NC_013722.1. DR ProteinModelPortal; D2UC39; -. DR GeneID; 8702709; -. DR KEGG; xal:XALc_0778; -. DR PATRIC; 32544051; VBIXanAlb89132_0777. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; XALB29447:GJN1-777-MONOMER; -. DR BioCyc; XALB380358:GLMQ-777-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21594 MW; 0A009AAFE2FF20B4 CRC64; MNASTTPRGV YLITPDETDG TRLLERVAPL LEQGVTWLQY RNKRADAAQR LAQASALHAM CLRAGVPLIV NDDVTLAQTV GAAGVHLGED DGDLSRARAT LGPHALIGAS CYDDLQRARA AAMAGASYVA FGAFFPSRSK VATRRADPGL LRDAAALRLP RVAIGGLTPD NARAVVAAGA DLLAVISGVF DADNPRAALA AYRACFA // ID D2UFW9_XANAP Unreviewed; 320 AA. AC D2UFW9; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 11-DEC-2013, entry version 29. DE SubName: Full=Putative nudix hydrolase protein; DE EC=3.6.1.-; GN OrderedLocusNames=XALC_2803; OS Xanthomonas albilineans (strain GPE PC73 / CFBP 7063). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=380358; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GPE PC73 / CFBP 7063; RA Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., RA Cociancich S., Couloux A., Darrasse A., Gouzy J., Jacques M.A., RA Lauber E., Manceau C., Mangenot S., Poussier S., Segurens B., RA Szurek B., Verdier V., Arlat M., Rott P.; RT "The complete genome sequence of Xanthomonas albilineans provides new RT insights into the reductive genome evolution of the xylem-limited RT Xanthomonadaceae."; RL BMC Genomics 10:616-616(2009). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP565176; CBA17280.1; -; Genomic_DNA. DR RefSeq; YP_003377274.1; NC_013722.1. DR ProteinModelPortal; D2UFW9; -. DR GeneID; 8702809; -. DR KEGG; xal:XALc_2803; -. DR PATRIC; 32548073; VBIXanAlb89132_2761. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR BioCyc; XALB29447:GJN1-2795-MONOMER; -. DR BioCyc; XALB380358:GLMQ-2795-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 320 AA; 34631 MW; A2F1460BA96E619C CRC64; MSEPLRSIHV VAAVITDARG RILLSRRTGG SDLAGLWEFP GGKREPGETS EQALVRELQE ELGIDAVVGA WLMEVPQRYP DKRLRLEVRQ VQSWKGTARG REGQPLMWVM PDKLGRYAMP PADQPVVAML RQPDRYLVTP EPADPALWLA ALERALDSGV RCVQLRARSL PHAHWWPLAR AAAALCAAHG AQVLVNRDLA LAQELGVGVH LGAEQLAQYQ ARPLPSAQVV AASCHTVEEL QAAQRLGCDF AVVGPLAATA SHPGATPLGW EAFERLREQV ALPLYPIGGL LPSQVAEARR HGGQGIAAIR GLWPLTADVA // ID D2UPA6_STAAU Unreviewed; 213 AA. AC D2UPA6; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAUG_02507; OS Staphylococcus aureus subsp. aureus H19. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585155; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H19; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain H19."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG730345; EFC06557.1; -; Genomic_DNA. DR ProteinModelPortal; D2UPA6; -. DR EnsemblBacteria; EFC06557; EFC06557; SAUG_02507. DR PATRIC; 35745409; VBIStaAur72956_2708. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23271 MW; A89EF5F25D160E89 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFADKII GLSISDLGEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D2UU21_STAAU Unreviewed; 213 AA. AC D2UU21; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SHAG_02531; OS Staphylococcus aureus subsp. aureus A017934/97. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585147; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A017934/97; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain A017934/97."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG731509; EFC28412.1; -; Genomic_DNA. DR ProteinModelPortal; D2UU21; -. DR EnsemblBacteria; EFC28412; EFC28412; SHAG_02531. DR PATRIC; 35915863; VBIStaAur33461_1641. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D2V0B2_NAEGR Unreviewed; 497 AA. AC D2V0B2; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 16-APR-2014, entry version 27. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=NAEGRDRAFT_78019; OS Naegleria gruberi (Amoeba). OC Eukaryota; Heterolobosea; Schizopyrenida; Vahlkampfiidae; Naegleria. OX NCBI_TaxID=5762; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NEG-M; RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032; RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., RA Carpenter M.L., Field M.C., Kuo A., Paredez A., Chapman J., Pham J., RA Shu S., Neupane R., Cipriano M., Mancuso J., Tu H., Salamov A., RA Lindquist E., Shapiro H., Lucas S., Grigoriev I.V., Cande W.Z., RA Fulton C., Rokhsar D.S., Dawson S.C.; RT "The genome of Naegleria gruberi illuminates early eukaryotic RT versatility."; RL Cell 140:631-642(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG738847; EFC49686.1; -; Genomic_DNA. DR ProteinModelPortal; D2V0B2; -. DR KEGG; ngr:NAEGRDRAFT_78019; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 497 AA; 53816 MW; 97BFCA66D942C8D4 CRC64; MGKRSLEETV EQSIEGGSSI IQYREKRYPQ QLTTRQMLEQ AKSLQKICRR HGVPFLIDDR VDLAVAIDAD GVHVGQKDLP PQYVRKLIGN SKILGLTVGT FDQVDEALSH NVRADYLGTN AIFPTLTKKD AGQAVGLDGL KELVSYVRHT TRNGKHVGLV AIGGIGKENI SQVMECGVDG VAVVSSVVGA ESALQASREL RSTINYYQMN QSNDKARVRE EMVQALLDIK KTRPLIHNLT NNVVTTQTAN SLLAIGASPV MSQYHEEISD MVGIASGVLI NIGTLDEYSI KAMHLAAKRA NELGKPVILD PVGYGATKAR EATVLELLLN HKITILKGNY GEIGRIHGNA GFAKLKGVDS ESNSSNLPEM DKVVSELAQK FGCVVCMTGP VDVISDGSDI IHVYHNEPNL QHLTGVGCMT GAIQAAFASV CSNPLIAASA GCSYVALSGE LAMSRMNLKD GELPPLGDFR SELFNSFSTL TPTNYRQYLN FVYQKSE // ID D2YGR7_VIBMI Unreviewed; 420 AA. AC D2YGR7; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-MAR-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VMB_27140; OS Vibrio mimicus VM603. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=671074; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VM603; RX PubMed=19860885; DOI=10.1186/1471-2148-9-258; RA Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T., RA Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.; RT "Genomic taxonomy of Vibrios."; RL BMC Evol. Biol. 9:258-258(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYU01000137; EEW06006.1; -; Genomic_DNA. DR EnsemblBacteria; EEW06006; EEW06006; VMB_27140. DR PATRIC; 28329201; VBIVibMim145354_2830. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 420 AA; 47236 MW; 41960A6B668AAFC6 CRC64; MTRLVFPRSS VELIGRVQYV LLQAKEQGFD IQNISLDVAT SDCFVLETES TLRIGCDLCP CEGTSELLDY YLQYLPEHRD IEARCKVKIG LRSHCDLGVD EWQVEENSCQ RITYPYPSLI SNYQLDQHVA WVLAMLALGF PIEDSLCVAR AAVSQKREVS RETWPINLEF FPSVHSESEL QPTKGFPAID KSQFTLYPVV DDVNWIELLL KLGVKTVQLR IKDPMQVDLE EQIVRSIDLG REYNAQVFIN DYWQLAIKHK AYGVHLGQED LTTANLTELA QAGLRLGLST HGYYELLNVA CLQPSYIALG HIFPTTTKQM PSKPQGLVRL AAYQGLANQL SYHGQKGMPT VAIGGIDHSN IEEVLRRGVT SAAVVRAITQ SANPALAVHQ LMFAFSGQKE SELRKQAKSY NMEWEASNVE // ID D2YTR8_VIBMI Unreviewed; 420 AA. AC D2YTR8; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 19-MAR-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VMD_31520; OS Vibrio mimicus VM573. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=671076; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VM573; RX PubMed=19860885; DOI=10.1186/1471-2148-9-258; RA Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T., RA Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.; RT "Genomic taxonomy of Vibrios."; RL BMC Evol. Biol. 9:258-258(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYV01000030; EEW09314.1; -; Genomic_DNA. DR EnsemblBacteria; EEW09314; EEW09314; VMD_31520. DR PATRIC; 30118239; VBIVibMim144731_3420. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 420 AA; 46841 MW; 4041B19C6BEF0DC1 CRC64; MTRLVFPCSS VELIGRVQYV LLQAKEQGFD IQNISLDVAT SDCFVLEAES TLRIACDLCL CEDTSELLDY YLQYLPEHRD IEARCKVKIG LRSHSDLGVD EWQVEENSSQ RITYPYPSLI SNCQLDQHVA WVLAMLALGF PIADALCVAR AAMSQKQDVS RETWPINLES FPSVHSGSEL QATKGFPAID KSQFTLYPVV DDVSWIELLL KLGVKTVQLR IKDPMQVDLE EQIVRAIDLG REYNAQVFIN DYWQIAIKHK AYGVHLGQED LTTANLTELA QAGLRLGLST HGYYELLNVA CLQPSYIALG HIFPTTTKQM PSKPQGLVRL AAYQGLANQL SYHGQKGMPT VAIGGIDHSN IEEVLRCGVT SAAVVRAITQ SANPALAVHQ LMFAFSGQKE SELRKQAKSY NMEWETSNVE // ID D2Z7V1_9BACT Unreviewed; 208 AA. AC D2Z7V1; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Dpep_1522; OS Dethiosulfovibrio peptidovorans DSM 11002. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Dethiosulfovibrio. OX NCBI_TaxID=469381; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 11002; RX PubMed=21304695; RA Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., RA Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., RA Mavromatis K., Mikhailova N., Pati A., Goodwin L., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Rohde M., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans RT type strain (SEBR 4207)."; RL Stand. Genomic Sci. 3:85-92(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABTR02000001; EFC91548.1; -; Genomic_DNA. DR ProteinModelPortal; D2Z7V1; -. DR EnsemblBacteria; EFC91548; EFC91548; Dpep_1522. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21563 MW; 76B31DBAE13DE51A CRC64; MDPKILTLYV IPDRRQGAPR SILEQTAAAL EGGATAIQLR DKELSARELT DLASRMTEMC RKKGAKLFVN DRLDVALAAG ADGCHLGQSD LPLAAARKLA PRPFLLGRSA RTVEQARVAL EEGADYLGVG AVYPTGTKDD ASVIGVEGLK AVVEFTSLPV VAIGGIGSSS VREVMATGAS GVAVVSAVVG TPDPTASAVE LLKLMIKP // ID D2ZFN0_9ENTR Unreviewed; 211 AA. AC D2ZFN0; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ENTCAN_07289; OS Enterobacter cancerogenus ATCC 35316. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=500639; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35316; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWM02000013; EFC55898.1; -; Genomic_DNA. DR ProteinModelPortal; D2ZFN0; -. DR EnsemblBacteria; EFC55898; EFC55898; ENTCAN_07289. DR PATRIC; 29279297; VBIEntCan670_2775. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23030 MW; 9BF8A73350EB1F17 CRC64; MYQPDFPSVP FRLGLYPVVD SVEWIARLLE AGVRTIQLRI KDKRDDEVEA DVVAAIALGR RYQARLFIND YWQLAVKHQA YGVHLGQEDL ETTDLSAIRD AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLAQLA DHVKRLAEYP TVAIGGISLE RAASVLETGV GSIAVVSAIT QANDWRDATA QLLRLAGAGD E // ID D2ZPW3_METSM Unreviewed; 209 AA. AC D2ZPW3; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=METSMIF1_02881; OS Methanobrevibacter smithii DSM 2374. OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanobrevibacter. OX NCBI_TaxID=521002; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2374; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYV02000006; EFC93310.1; -; Genomic_DNA. DR ProteinModelPortal; D2ZPW3; -. DR EnsemblBacteria; EFC93310; EFC93310; METSMIF1_02881. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22698 MW; 5A8B045BD643F396 CRC64; MNNLDLSLYL VTNNSEDEEK FLNIIEESLK GGVSVVQLRE KKAETLDFYN LALKVKEITQ KYNVPLIIND RIDIALAIDA DGVHVGQSDM PAKTARSMIG EDKILGVSAA NIKEAKKAQR DSADYIGVGA VYPTNTKDDA TSVPKKELKE IVKSVDIPVV AIGGITQENA HELNDCGIDG LSVVSAIMEA KNPKIASKNL LKEFKAKNS // ID D2ZX17_NEIMU Unreviewed; 205 AA. AC D2ZX17; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NEIMUCOT_05165; OS Neisseria mucosa ATCC 25996. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=546266; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25996; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDX02000008; EFC88493.1; -; Genomic_DNA. DR ProteinModelPortal; D2ZX17; -. DR EnsemblBacteria; EFC88493; EFC88493; NEIMUCOT_05165. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21890 MW; 2B91849BBB49DD99 CRC64; MTFPPLKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKTL HGDELKREIT RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDAA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AVVRAVIEAE NPEAVVKAFQ ALWNE // ID D3A1X1_NEISU Unreviewed; 205 AA. AC D3A1X1; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NEISUBOT_03210; OS Neisseria subflava NJ9703. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=546268; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NJ9703; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEO02000001; EFC53209.1; -; Genomic_DNA. DR ProteinModelPortal; D3A1X1; -. DR EnsemblBacteria; EFC53209; EFC53209; NEISUBOT_03210. DR PATRIC; 25464376; VBINeiSub99872_0184. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006162; PPantetheine_attach_site. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22082 MW; 112A66091B450787 CRC64; MTFPPLKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKIL HGDELKREIE RCVVACQNSA TQLFINDHWR EAIAAGAYGV HLGQEDMDTA DLAAIEAAGL RLGLSTHSVA ELDRALSVQP SYVASGAIFP TTTKQMPTAP QGLEKLREYV KQARGIPVVA IGGIDLNNAE DVLATGVSSL AVVRAVTEAE NPEAVVKAFQ ALWDE // ID D3AHE5_9CLOT Unreviewed; 218 AA. AC D3AHE5; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLOSTHATH_03033; OS Clostridium hathewayi DSM 13479. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=566550; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13479; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIO01000238; EFC98777.1; -; Genomic_DNA. DR ProteinModelPortal; D3AHE5; -. DR EnsemblBacteria; EFC98777; EFC98777; CLOSTHATH_03033. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 22998 MW; 3DF0A2F748231FD9 CRC64; MKLDKKSLLL YAVTDRSWLG EETLYSQVER ALKGGATMIQ LREKEMTEEA FIAEAQSIKE LCGRYGVPFI INDSTAVAVA VDADGVHVGQ SDMEAGDVRR RLGKNKIIGV SAQTVEQALL AEKQGADYLG VGAVFHTGTK KDASDVSFQT LKAICGAVQI PVVAIGGITA DNMKHLAGSG ICGVAVVSAI FAEADIEAAA RKLKRAAAET ADAEKEAD // ID D3DCC9_9ACTO Unreviewed; 234 AA. AC D3DCC9; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FrEUN1fDRAFT_7451; OS Frankia sp. EUN1f. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=102897; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EUN1f; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L., RA Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A., RA Fernandez M., Tisa L.; RT "The draft genome of Frankia sp. EUN1f."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGX01000230; EFC79430.1; -; Genomic_DNA. DR ProteinModelPortal; D3DCC9; -. DR EnsemblBacteria; EFC79430; EFC79430; FrEUN1fDRAFT_7451. DR PATRIC; 35522269; VBIFraSp73591_7183. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 57 61 HMP-PP binding (By similarity). FT REGION 155 157 THZ-P binding (By similarity). FT METAL 90 90 Magnesium (By similarity). FT METAL 109 109 Magnesium (By similarity). FT BINDING 89 89 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 158 158 HMP-PP (By similarity). FT BINDING 191 191 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 234 AA; 24603 MW; C780C9E9865E388D CRC64; MPLSENVPAS ASAPRARRLA RLLDARLYLC TPRHQADAAF YEKVLGDGRV PGVDLIQLRE KGLEWRDELA GLAAMAVAAV PSGALVSAND RADVARFAGV DILHVGQDDI PPRLARDLLG PDVLIGQSTH DPDQFLTALA DPDVDYVCVG PVHATPTKEG RAPVGLELPR LAARHAPPFE PGAKPWFVTG GVAPHTLDAI LDTGARRVVV VRGITQAADP GAAAAALAGR LREA // ID D3DHF3_HYDTT Unreviewed; 216 AA. AC D3DHF3; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; OrderedLocusNames=HTH_0795, Hydth_0795; OS Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobacter. OX NCBI_TaxID=608538; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6534 / IAM 12695 / TK-6 [Tokyo], and TK-6; RX PubMed=20348262; DOI=10.1128/JB.00158-10; RA Arai H., Kanbe H., Ishii M., Igarashi Y.; RT "Complete genome sequence of the thermophilic, obligately RT chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter RT thermophilus TK-6."; RL J. Bacteriol. 192:2651-2652(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6534 / IAM 12695 / TK-6 [JGI], and TK-6; RX DOI=10.4056/sigs.1463589; RG US DOE Joint Genome Institute (JGI-PGF); RA Zeytun A., Sikorski J., Nolan M., Lapidus A., Lucas S., Han J., RA Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., RA Chen A., Palaniappan K., Ngatchou O., Land M., Hauser L., Chang Y., RA Jeffries C., Han C., Detter J., Ubler S., Rohde M., Tindall B., RA Wirth R., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Klenk H., Kyrpides N.; RT "Complete genome sequence of Hydrogenobacter thermophilus type strain RT (TK-6)."; RL Stand. Genomic Sci. 4:131-143(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002221; ADO45192.1; -; Genomic_DNA. DR EMBL; AP011112; BAI69255.1; -; Genomic_DNA. DR RefSeq; YP_003432456.1; NC_013799.1. DR RefSeq; YP_005511485.1; NC_017161.1. DR EnsemblBacteria; ADO45192; ADO45192; Hydth_0795. DR EnsemblBacteria; BAI69255; BAI69255; HTH_0795. DR GeneID; 12100936; -. DR GeneID; 8772478; -. DR KEGG; hte:Hydth_0795; -. DR KEGG; hth:HTH_0795; -. DR PATRIC; 32210489; VBIHydThe36152_0804. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTLLQYR; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 24047 MW; 3FB3DA8D8ACAAA5D CRC64; MGRMNLSLYL VTDDKYFVGR DLVDTIEKAL QGGVTALQYR FKNKSTRQMY EELLVLRELT RRYGADLVVN DRVDLAMAVG ADGVHVGKED LPPDVVRKIV GESMYIGYSV NSVEDLREVN HLPIDYIGFG SVYETTTKEN YKLVGIEGLR QAVKLTSKPV VAIGGITSYR MKEVLQTGVK GVAVVSAILG FEDVEKAART LAQIYKSTVK EKFLMP // ID D3DHH6_HYDTT Unreviewed; 185 AA. AC D3DHH6; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; OrderedLocusNames=HTH_0818, Hydth_0818; OS Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobacter. OX NCBI_TaxID=608538; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6534 / IAM 12695 / TK-6 [Tokyo], and TK-6; RX PubMed=20348262; DOI=10.1128/JB.00158-10; RA Arai H., Kanbe H., Ishii M., Igarashi Y.; RT "Complete genome sequence of the thermophilic, obligately RT chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter RT thermophilus TK-6."; RL J. Bacteriol. 192:2651-2652(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6534 / IAM 12695 / TK-6 [JGI], and TK-6; RX DOI=10.4056/sigs.1463589; RG US DOE Joint Genome Institute (JGI-PGF); RA Zeytun A., Sikorski J., Nolan M., Lapidus A., Lucas S., Han J., RA Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., RA Chen A., Palaniappan K., Ngatchou O., Land M., Hauser L., Chang Y., RA Jeffries C., Han C., Detter J., Ubler S., Rohde M., Tindall B., RA Wirth R., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Klenk H., Kyrpides N.; RT "Complete genome sequence of Hydrogenobacter thermophilus type strain RT (TK-6)."; RL Stand. Genomic Sci. 4:131-143(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002221; ADO45215.1; -; Genomic_DNA. DR EMBL; AP011112; BAI69278.1; -; Genomic_DNA. DR RefSeq; YP_003432479.1; NC_013799.1. DR RefSeq; YP_005511508.1; NC_017161.1. DR EnsemblBacteria; ADO45215; ADO45215; Hydth_0818. DR EnsemblBacteria; BAI69278; BAI69278; HTH_0818. DR GeneID; 12100959; -. DR GeneID; 8773899; -. DR KEGG; hte:Hydth_0818; -. DR KEGG; hth:HTH_0818; -. DR PATRIC; 32210537; VBIHydThe36152_0828. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 185 AA; 20825 MW; AC4446C3D3365BDF CRC64; MLPRLYAITD SQRYGEDFWE SLRRVLERGV RMVQLREKAL SAKEYYQKAL EAREITREYS ALLLINERVD IALAVGADGV HLPQEGLPPS CVRKIKKDLI VGFSAHDLKS ALYAQEEGAD FITLSPIFKT SSHPEREPLG LEVLKDISKR VSIPVYALGG ITWEKIKLCY KNGAYGIAGV SLFLK // ID D3DZJ2_METRM Unreviewed; 219 AA. AC D3DZJ2; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=mru_1820; OS Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM OS 13430 / M1) (Methanobacterium ruminantium). OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanobrevibacter. OX NCBI_TaxID=634498; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / M1; RX PubMed=20126622; DOI=10.1371/journal.pone.0008926; RA Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J., RA Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C., RA Janssen P.H., Dey D., Attwood G.T.; RT "The genome sequence of the rumen methanogen Methanobrevibacter RT ruminantium reveals new possibilities for controlling ruminant methane RT emissions."; RL PLoS ONE 5:E8926-E8926(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001719; ADC47670.1; -; Genomic_DNA. DR RefSeq; YP_003424562.1; NC_013790.1. DR ProteinModelPortal; D3DZJ2; -. DR EnsemblBacteria; ADC47670; ADC47670; mru_1820. DR GeneID; 8771490; -. DR KEGG; mru:mru_1820; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; MRUM634498:GHDG-1873-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23791 MW; D00C983A28AF435D CRC64; MFKAMKKEDK MNKSSIDYSV YLVTDHRGKT DEEILNIIEQ AIKGGTSVVQ IREKTASTKD FYNLALKAKE ITEKYNVPLI VNDRIDIALA VKSDGVHIGQ DDMPAKVARE IIGEEMILGV SASTVEEAMK AESDGADYIG SGAVFPTATK DDADSVSKEE LKEIVNSTSI PVVAIGGITI ENAESLKDAE IDGFSVVSAI MNADDPKKAS EILKEIYNR // ID D3EGR1_GEOS4 Unreviewed; 224 AA. AC D3EGR1; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GYMC10_1139; OS Geobacillus sp. (strain Y412MC10). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=481743; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y412MC10; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Brumm P., Mead D.; RT "Complete sequence of Geobacillus sp. Y412MC10."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001793; ACX63429.1; -; Genomic_DNA. DR RefSeq; YP_003241236.1; NC_013406.1. DR ProteinModelPortal; D3EGR1; -. DR EnsemblBacteria; ACX63429; ACX63429; GYMC10_1139. DR GeneID; 8515303; -. DR KEGG; gym:GYMC10_1139; -. DR PATRIC; 32150823; VBIGeoSp56627_1143. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PSP481743:GH8K-1166-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23907 MW; 5CE54324B278AFA3 CRC64; MTGRVAPEIM RRHLRMYLVL GSVNCSVEPS LVVQEALAGG ATMVQFREKG QAALAGEPMI RLARRIQAEC HLAGVPFIVN DDVELALKLD ADGVHVGQDD ESAASVRERI GNRILGVSAH TVEEARRAIL HGADYLGIGP IYPTRSKDDA RTAQGPAIFR ELREAGIHLP IVGIGGITVE RVEEVIGAGA DGVAVISAVT GAESAREVVE AFIDKIRCTT ERIS // ID D3ENA9_ATETH Unreviewed; 338 AA. AC D3ENA9; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 16-APR-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=UCYN_02100; OS Atelocyanobacterium thalassa (isolate ALOHA). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Candidatus Atelocyanobacterium. OX NCBI_TaxID=713887; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20173737; DOI=10.1038/nature08786; RA Tripp H.J., Bench S.R., Turk K.A., Foster R.A., Desany B.A., Niazi F., RA Affourtit J.P., Zehr J.P.; RT "Metabolic streamlining in an open-ocean nitrogen-fixing RT cyanobacterium."; RL Nature 464:90-94(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001842; ADB94959.1; -; Genomic_DNA. DR RefSeq; YP_003421317.1; NC_013771.1. DR ProteinModelPortal; D3ENA9; -. DR EnsemblBacteria; ADB94959; ADB94959; UCYN_02100. DR GeneID; 8750578; -. DR KEGG; cyu:UCYN_02100; -. DR PATRIC; 35281200; VBICyaUCY151080_0194. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR BioCyc; CUCY713887:GI71-199-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 121 Unknown (By similarity). FT REGION 122 338 Thiamine-phosphate synthase (By FT similarity). FT REGION 169 173 HMP-PP binding (By similarity). FT METAL 202 202 Magnesium (By similarity). FT METAL 221 221 Magnesium (By similarity). FT BINDING 201 201 HMP-PP (By similarity). FT BINDING 240 240 HMP-PP (By similarity). FT BINDING 269 269 HMP-PP (By similarity). FT BINDING 296 296 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 338 AA; 38630 MW; 5AF6C2A4B851208C CRC64; MNNNFLISQI LDANLDRARE GIRVIEEWCR FGIKKGHLAK TCKDIRQELA LWHTYELRLS RNTENDPGID LSHPKEEVKN NVEELLQANL CRVQEALRVL EEYGKLYDSK MGKSFKKIRY EVYILESSLI RYSNHKQLCK ASIYLITSPI KNLFSVVESS LKGGLQILQY REKNISDSSY IKVARKLCEL CHQYDALFIM NDRVDIALAI NADGVHIGQE DISIKIAREI IGPQKIIGCS TTNPLEMEKA IEEGADYIGV GPIYPTPNKP EKETIQSDYL DYVINKCTIP WFAIGGINID NIKNITDLGV KQVAVIRLIM EADNPEEMTK FLLKNYLS // ID D3EYC0_STAA4 Unreviewed; 213 AA. AC D3EYC0; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SA2981_2032; OS Staphylococcus aureus (strain 04-02981). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=703339; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=04-02981; RA Nuebel U., Dordel J., Kurt K., Strommenger B., Westh H., Shukla S.K., RA Zemlickova H., Leblois R., Wirth T., Jombart T., Balloux F., Witte W.; RT "A timescale for evolution, population expansion, and spatial spread RT of an emerging clone of methicillin-resistant Staphlococcus aureus."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001844; ADC38243.1; -; Genomic_DNA. DR RefSeq; YP_005742781.1; NC_017340.1. DR ProteinModelPortal; D3EYC0; -. DR SMR; D3EYC0; 4-209. DR PRIDE; D3EYC0; -. DR EnsemblBacteria; ADC38243; ADC38243; SA2981_2032. DR GeneID; 12865717; -. DR KEGG; suy:SA2981_2032; -. DR PATRIC; 36808454; VBIStaAur158479_2071. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SAUR703339:GLKF-2102-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D3FAD4_CONWI Unreviewed; 227 AA. AC D3FAD4; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Precursor; GN Name=thiE; OrderedLocusNames=Cwoe_0770; OS Conexibacter woesei (strain DSM 14684 / JCM 11494 / NBRC 100937 / OS ID131577). OC Bacteria; Actinobacteria; Rubrobacteridae; Solirubrobacterales; OC Conexibacteraceae; Conexibacter. OX NCBI_TaxID=469383; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14684 / JCM 11494 / NBRC 100937 / ID131577; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Chertkov O., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K., RA Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Conexibacter woesei DSM 14684."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001854; ADB49203.1; -; Genomic_DNA. DR RefSeq; YP_003392578.1; NC_013739.1. DR ProteinModelPortal; D3FAD4; -. DR EnsemblBacteria; ADB49203; ADB49203; Cwoe_0770. DR GeneID; 8731200; -. DR KEGG; cwo:Cwoe_0770; -. DR PATRIC; 32043496; VBIConWoe21639_0771. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; CWOE469383:GH82-772-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 51 55 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 23247 MW; 448B841B501FD699 CRC64; MGFQMSLTTG TERRARLAAA HLYLVCDATG DGRDLAAFLD AALRGGADLV QLRDKDGDDA TILRAAPVFR AAADAHGALF ILNDRPDLVA ATGADGVHVG QDDLPVAQTR AAVGPDRIVG LSTHTPAQVD AADARDEVDY FAVGPVHATP TKPGRPAVGI ELIEHAARTP RRAPWFAIGG IDASTVGPVA AAGATRAVVV RALTAAADPE ASARALRATL EARVGAA // ID D3FMP9_CAMJI Unreviewed; 201 AA. AC D3FMP9; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=CJSA_0986; OS Campylobacter jejuni subsp. jejuni (strain IA3902). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=567106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IA3902; RA Sahin O., Zhang Q.; RT "Complete genome sequence of a highy virulent Campylobacter jejuni RT strain associated with sheep abortion in the United States."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001876; ADC28625.1; -; Genomic_DNA. DR RefSeq; YP_005656343.1; NC_017279.1. DR ProteinModelPortal; D3FMP9; -. DR EnsemblBacteria; ADC28625; ADC28625; CJSA_0986. DR GeneID; 12249862; -. DR KEGG; cji:CJSA_0986; -. DR PATRIC; 36811887; VBICamJej152966_1027. DR KO; K00788; -. DR OMA; AGHIFET; -. DR BioCyc; CJEJ567106:GLA7-1021-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 201 AA; 23321 MW; 0411D704EF1099AC CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICTKQ KVTCFLHSFD KVCLKLGHHY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID D3FMT6_CAMJI Unreviewed; 210 AA. AC D3FMT6; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CJSA_1023; OS Campylobacter jejuni subsp. jejuni (strain IA3902). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=567106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IA3902; RA Sahin O., Zhang Q.; RT "Complete genome sequence of a highy virulent Campylobacter jejuni RT strain associated with sheep abortion in the United States."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001876; ADC28662.1; -; Genomic_DNA. DR RefSeq; YP_005656380.1; NC_017279.1. DR ProteinModelPortal; D3FMT6; -. DR EnsemblBacteria; ADC28662; ADC28662; CJSA_1023. DR GeneID; 12249899; -. DR KEGG; cji:CJSA_1023; -. DR PATRIC; 36811961; VBICamJej152966_1064. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; CJEJ567106:GLA7-1058-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID D3FYK4_BACPE Unreviewed; 205 AA. AC D3FYK4; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BpOF4_14025; OS Bacillus pseudofirmus (strain OF4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=398511; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OF4; RX PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x; RA Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., RA Fackelmayer O.J., Smith T.A., Earl J., Elbourne L.D., Hassan K., RA Paulsen I.T., Kolsto A.B., Tourasse N.J., Ehrlich G.D., Boissy R., RA Ivey D.M., Li G., Xue Y., Ma Y., Hu F.Z., Krulwich T.A.; RT "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations RT that support the ability to grow in an external pH range from 7.5 to RT 11.4."; RL Environ. Microbiol. 13:3289-3309(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001878; ADC50856.1; -; Genomic_DNA. DR RefSeq; YP_003427748.1; NC_013791.2. DR ProteinModelPortal; D3FYK4; -. DR EnsemblBacteria; ADC50856; ADC50856; BpOF4_14025. DR GeneID; 8767856; -. DR KEGG; bpf:BpOF4_14025; -. DR PATRIC; 31948144; VBIBacPse80461_2737. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; BPSE398511:GJI9-1277-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22383 MW; 37C8FED48C8F9221 CRC64; MKDFKLYAIT GEEFHQGRDL IEVMEEAILG GVDIIQLRDK KSKKIDVLKK AQALRELTKK HDVTFIVNDH IDVALAVDAD GIHVGQDDLP LAEARKVMGP DKIIGISTHK IEEARAAEAG GADYIGVGPI FETKSKEDVV DPVTTQYIQQ VANEIKIPFV AIGGIKLHNV DQVLAAGATR VCMISEIVGA EDVKGTCEKF IKILK // ID D3GSX2_ECO44 Unreviewed; 211 AA. AC D3GSX2; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EC042_4360; OS Escherichia coli O44:H18 (strain 042 / EAEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=216592; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=042 / EAEC; RX PubMed=20098708; DOI=10.1371/journal.pone.0008801; RA Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L., RA Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R., RA Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., RA Rasko D.A., Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., RA Henderson I.R.; RT "Complete genome sequence and comparative metabolic profiling of the RT prototypical enteroaggregative Escherichia coli strain 042."; RL PLoS ONE 5:E8801-E8801(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN554766; CBG37184.1; -; Genomic_DNA. DR RefSeq; YP_006098641.1; NC_017626.1. DR ProteinModelPortal; D3GSX2; -. DR GeneID; 12885279; -. DR KEGG; elo:EC042_4360; -. DR PATRIC; 36690511; VBIEscCol52250_4524. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; ECOL216592:GCV7-4426-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23087 MW; C69F22E5371F9A56 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QSTDLDAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVKRLADYP TVAIGGISLA RSPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D3HDR0_STRG3 Unreviewed; 210 AA. AC D3HDR0; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GALLO_1178; OS Streptococcus gallolyticus (strain UCN34). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=637909; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCN34; RX PubMed=20139183; DOI=10.1128/JB.01659-09; RA Rusniok C., Couve E., Da Cunha V., El Gana R., Zidane N., Bouchier C., RA Poyart C., Leclercq R., Trieu-Cuot P., Glaser P.; RT "Genome sequence of Streptococcus gallolyticus: insights into its RT adaptation to the bovine rumen and its ability to cause RT endocarditis."; RL J. Bacteriol. 192:2266-2276(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN597254; CBI13670.1; -; Genomic_DNA. DR RefSeq; YP_003430601.1; NC_013798.1. DR ProteinModelPortal; D3HDR0; -. DR EnsemblBacteria; CBI13670; CBI13670; GALLO_1178. DR GeneID; 8775976; -. DR KEGG; sga:GALLO_1178; -. DR PATRIC; 35285795; VBIStrGal150982_1174. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SGAL637909:GJOV-1901-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22695 MW; B32CAC167AC003AB CRC64; MDKEILQVYF ICGTANCPEG KFLEILEAAF KSGVTCFQFR EKGANALKGG EKVVLARKVK ELCRKYQIPL IINDDVDLAL ELDADGIHLG QDDLPITKAR QLFPNKIIGL SVGSTIEYQR SAVELVDYIG VGPIFPTSSK NDAGEVIGLK GLNDVRDYDK EIPIVAIGGI TFGDVAAIKQ SGADGVAVIS AIAQSKQVEV DTQRLSSFFD // ID D3HQV1_LEGLN Unreviewed; 427 AA. AC D3HQV1; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiDE; OrderedLocusNames=LLO_0924; OS Legionella longbeachae serogroup 1 (strain NSW150). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=661367; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NSW150; RX PubMed=20174605; DOI=10.1371/journal.pgen.1000851; RA Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D., RA Newton H.J., Sansom F.M., Jarraud S., Zidane N., Ma L., Bouchier C., RA Etienne J., Hartland E.L., Buchrieser C.; RT "Analysis of the Legionella longbeachae genome and transcriptome RT uncovers unique strategies to cause Legionnaires' disease."; RL PLoS Genet. 6:E1000851-E1000851(2010). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN650140; CBJ11271.1; -; Genomic_DNA. DR RefSeq; YP_003454408.1; NC_013861.1. DR ProteinModelPortal; D3HQV1; -. DR EnsemblBacteria; CBJ11271; CBJ11271; LLO_0924. DR GeneID; 8802976; -. DR KEGG; llo:LLO_0924; -. DR PATRIC; 35289913; VBILegLon159544_0954. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR BioCyc; LLON661367:GJAR-984-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 427 AA; 48308 MW; 238FE709B3DB0CA1 CRC64; MQIVWADAEI EEDSYTFRDF GVEVHRSPFH VKSMPDAIKV NLQISLEEIY LTKSYSIPVV LDAYVLLQKV YYKRSDLIPW FSLANLLVLD THEAELILGY KIASHQSMQE AAHELLSLGN QSILLLGEQL HEAWCHDYWT NGVTSFWLTQ SRISYTKYSG LRSILSAAIT ASLALGYSLE DAIIIARMYT HQVIRRTHTG FDFGGFPEDE VDLPYLASMP LYEKPQPFKL CHHLGLYPVV DSSVWVELLL NVGVKTIQLR IKEQTETLEK EVQRSIALAK KHRATLYIND YWELALKYEA DGVHLGQSDL DAADINAIRK KGLLLGVSTH CYYEVARAHA INPSYIAIGP IYPTTSKKMP FLAQGIERLK RWQRTLNYPL VAIGGINIER MSDVVATGVS GVALISAITK AHNPRRATEQ FLSILQI // ID D3HW48_9BACT Unreviewed; 202 AA. AC D3HW48; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 13-NOV-2013, entry version 19. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF0649_00480; OS Prevotella buccae D17. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=575611; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D17; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Sibley C.D., White A., Allen-Vercoe E., RA Strauss J., Crowley S., Surette M.G., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella buccae Oral Taxon 560 strain D17."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG739927; EFC76573.1; -; Genomic_DNA. DR ProteinModelPortal; D3HW48; -. DR EnsemblBacteria; EFC76573; EFC76573; HMPREF0649_00480. DR PATRIC; 35698595; VBIPreBuc31492_0551. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23349 MW; 70657E3A25EDDA55 CRC64; MKLVIMTKST FFVEEDKILA TLFEEGMDNL HLNKPDSSPM YSERLLSLLP EETYRKITVH DHFYLKNEYG LAGIHLDDAF QEVPKGYKGK MSATCTETER LKEAKRKFNY VFLKNIFDCI EYPSEKSSFN LNELEDAAHR GLIDKHVYAL GGMSLENVKL AKQLGFGGVV VCGDLWNRFD IHNETDYLQL INHFNKLRKA VE // ID D3I0T0_9BACT Unreviewed; 194 AA. AC D3I0T0; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 13-NOV-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0649_02112; OS Prevotella buccae D17. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=575611; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D17; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Sibley C.D., White A., Allen-Vercoe E., RA Strauss J., Crowley S., Surette M.G., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella buccae Oral Taxon 560 strain D17."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG739950; EFC74912.1; -; Genomic_DNA. DR ProteinModelPortal; D3I0T0; -. DR EnsemblBacteria; EFC74912; EFC74912; HMPREF0649_02112. DR PATRIC; 35702027; VBIPreBuc31492_2182. DR OrthoDB; EOG679THR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 21267 MW; E57178A6C6127755 CRC64; MKTIVITSPD HWPGEETVIP RLLEAGVDFV HLRKPAWSEA DCARLLSLVP AWCHGRIVVH DHFALCRRFA LRGIHLNGRC PEIPVGFEGV VSRSCHSLCE VEEGKPLSSY VFLSPVFDSI SKPGYRAAFT PAELQSAARR GIIDRRVVAL GGVSVDNVAL LRTCGFGGVA LLGEVWRQAA GAHFDDYLRR LAAL // ID D3I7X4_9BACT Unreviewed; 195 AA. AC D3I7X4; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 13-NOV-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0660_01989; OS Prevotella melaninogenica D18. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=575612; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D18; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Sibley C.D., White A., Allen-Vercoe E., RA Strauss J., Crowley S., Surette M.G., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella melaninogenica Oral Taxon 469 RT strain D18."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG740021; EFC72420.1; -; Genomic_DNA. DR ProteinModelPortal; D3I7X4; -. DR EnsemblBacteria; EFC72420; EFC72420; HMPREF0660_01989. DR PATRIC; 35833927; VBIPreMel53552_1966. DR OrthoDB; EOG679THR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 195 AA; 22209 MW; E5F994E6CBDDA6F3 CRC64; MKWITITSPE FLSGEATFIS KLFSQGLDLL HLRKPEASLE AYKQLLLQIP EQWHSRIVLH EHFELAEEYK LHGIHLNRRY SVAPNAYHGS ISCSCHTIEE VITQKDSKDY VFLSPIFDSI SKVGYHAAFS PTLLKQAAIE NVIDEKVIAL GGITANNIPL VKEWHFGGVA LLGDIWKRMS DPQVDEYLMH IRTLL // ID D3IAX6_9BACT Unreviewed; 202 AA. AC D3IAX6; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF0669_00580; OS Prevotella sp. oral taxon 299 str. F0039. OG Plasmid unnamed. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=575614; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0039; PLASMID=unnamed; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Izard J., Baranova O.V., Blanton J.M., RA Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0039; PLASMID=unnamed; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V., RA Blanton J.M., Tanner A.C., Dewhirst F.E., Walker B., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., RA McCowan C., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella sp. Oral Taxon 299 strain F0039."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003667; EFC71908.1; -; Genomic_DNA. DR RefSeq; YP_008444692.1; NC_022111.1. DR ProteinModelPortal; D3IAX6; -. DR EnsemblBacteria; EFC71908; EFC71908; HMPREF0669_00580. DR GeneID; 16638201; -. DR KEGG; pro:HMPREF0669_00580; -. DR PATRIC; 35836068; VBIPreSp104905_0565. DR KO; K00788; -. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Plasmid. SQ SEQUENCE 202 AA; 23197 MW; 9AD991D27290E602 CRC64; MKLAVMTHST FFVEEDKILT TLFNEGMENL HLYKREASPI YSERLLSLLN EENRKRTIVH DNFYLKNEFE LGGIHLDTID TPIPEGYKGK VSRTCGDLSL LKDIVKVSKY VFLSNFLLPK QEKSDTKTYS LDLLEKAAKS GYINKNVYAM GNINLETIPV AKALGFGGVV LCEDLWSRFD IQNQTDYRDL IHHFQKIKRA IG // ID D3IG65_9BACT Unreviewed; 202 AA. AC D3IG65; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 13-NOV-2013, entry version 20. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF0670_00334; OS Prevotella sp. oral taxon 317 str. F0108. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=575615; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0108; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Izard J., Baranova O.V., Blanton J.M., RA Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella sp. Oral Taxon 317 strain F0108."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG740072; EFC69011.1; -; Genomic_DNA. DR ProteinModelPortal; D3IG65; -. DR EnsemblBacteria; EFC69011; EFC69011; HMPREF0670_00334. DR PATRIC; 35692058; VBIPreSp57183_0229. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23010 MW; 844177B6D20BAD46 CRC64; MKLVIMTKST YFVEEDKILT ALFDEGMDKL HLYKPGSQLV FSERLLSLIP EGYHDKIVVH EHFRLKNEYD LAGIHLNKPT EIVPNGIKGK ISRTCEDLDL LKDMKKNSNY VFLRRIFSCA GNADKPSSFS VKQLEDAADK GLIDKRVYAL GGIDVDNVRM AKELGFGGVV VCSDLWKRFD IHNGTDFRDL LAHFRNFQKI VG // ID D3KKJ9_LISMN Unreviewed; 214 AA. AC D3KKJ9; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMFG_00777; OS Listeria monocytogenes FSL J2-071. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393121; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL J2-071; RG The Broad Institute Genome Sequencing Platform; RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Borowsky M., RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., RA Mauceli E., Brockman W., MacCallum I.A., Rounsley S., Young S., RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., RA White J., Yandava C., Kodira C., Zeng Q., Alvarado L., O'Leary S., RA Wiedmann M., Lauer P.; RT "The Genome Sequence of Listeria monocytogenes FSL J2-071."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AARN04000005; EFD91362.1; -; Genomic_DNA. DR ProteinModelPortal; D3KKJ9; -. DR EnsemblBacteria; EFD91362; EFD91362; LMFG_00777. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22470 MW; 5F2E09945CB49154 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ KLCAKYQVPF IINDDVALAL EIGADGIHVG QTDEAIRQVI ASCSGKMKIG LSVHSVSEAK EAERLGEVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GITIPIVGIG GINETNSAEV LTAGADGVSV ISAITQSDDC HSVIKQLKNP GSPS // ID D3KZR1_9BACT Unreviewed; 210 AA. AC D3KZR1; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1705_00095; OS Anaerobaculum hydrogeniformans ATCC BAA-1850. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Anaerobaculum. OX NCBI_TaxID=592015; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1850; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJX02000004; EFD25197.1; -; Genomic_DNA. DR ProteinModelPortal; D3KZR1; -. DR EnsemblBacteria; EFD25197; EFD25197; HMPREF1705_00095. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22251 MW; BC1B5436EC08DC09 CRC64; MKLLDLKDRL KLYVILDRRL GRGVPLCDQA RLAIQGGATA IQLRDKRMQG RDFYRAALAI KEICKEKGVL FIVNDRLDVA LTAGADGVHL GQEDLPLEAA EKIAPEGFII GISVRTPDQA IEAERKGADY LGVGDVFGTS SKPDAKTIGI EGLKEVCVNT KLPCVAIGGI GVHNVKQALQ AGAVGVAVIS AVISQKDIAG AARTLRSLVS // ID D3LQM7_MICLU Unreviewed; 245 AA. AC D3LQM7; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0569_1314; OS Micrococcus luteus SK58. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Micrococcus. OX NCBI_TaxID=596312; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK58; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADCD01000080; EFD50208.1; -; Genomic_DNA. DR ProteinModelPortal; D3LQM7; -. DR EnsemblBacteria; EFD50208; EFD50208; HMPREF0569_1314. DR PATRIC; 36261433; VBIMicLut15202_1745. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 69 73 HMP-PP binding (By similarity). FT REGION 167 169 THZ-P binding (By similarity). FT METAL 102 102 Magnesium (By similarity). FT METAL 121 121 Magnesium (By similarity). FT BINDING 101 101 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 170 170 HMP-PP (By similarity). FT BINDING 203 203 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 245 AA; 25550 MW; A51E1D65B71E1387 CRC64; MHSPDPLLMA AADHDDGDTG AGRRARLAAS RLYVCTDLQR FLRPDGTLDT AAFAHFCAAA FRGGVDLIQV RDKAVDVAVE LAAFAVLVPL AREHGALSAA NDRADVAALA GVDVFHTGQT DLTTAQCRAL LGPDTVLGRS CHTEAQVRAA RAEDGLDYFC TGPVWATPTK PGRAAVGLEL PSLAARLDAE DPAGARPWFA IGGVDADRLP EVRAAGAERI VVVRAVTQAE DPEAAARTLR AGLPG // ID D3LSX6_9FIRM Unreviewed; 202 AA. AC D3LSX6; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 13-NOV-2013, entry version 19. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF0889_1499; OS Megasphaera genomosp. type_1 str. 28L. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=699218; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=28L; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGP01000005; EFD94760.1; -; Genomic_DNA. DR ProteinModelPortal; D3LSX6; -. DR EnsemblBacteria; EFD94760; EFD94760; HMPREF0889_1499. DR PATRIC; 36494357; VBIMegGen154667_0129. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 22522 MW; 54A069CD474A9285 CRC64; MVLKIIAITN HDLVSTNYWE RLEQIATAPI DAVVLREKNL TEDEYAEYAR RMLKLCNLHD QTCILHNFGK AAVRLHVPRF QCSLKYLEDH SSLLYYMTTL GVSVHTVKEA VRAEELGATY IIAGHIFPTA CKKTEPPVGV DILKEICQAV SVPVYALGGV NTTTITQLRN IPIAGIALMS GIMTCKNVTD YIAELKNKYV GK // ID D3LUC5_9FIRM Unreviewed; 215 AA. AC D3LUC5; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0889_1319; OS Megasphaera genomosp. type_1 str. 28L. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=699218; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=28L; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGP01000017; EFD94199.1; -; Genomic_DNA. DR ProteinModelPortal; D3LUC5; -. DR EnsemblBacteria; EFD94199; EFD94199; HMPREF0889_1319. DR PATRIC; 36495411; VBIMegGen154667_0627. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23523 MW; AD411556866CA726 CRC64; MTKEQHLQRL RDDPLYVILG EALSCGRTNV QTAADVLAAG VRIIQYREKH KTWREKYAEA KEIRRLCRKY DATFIMNDAV DLAVACEADG IHVGQDDAPV SFVRQWAGPQ MLIGVSTHTE EEMTEAVRDG ADYVGLGPFY PTQSKRDVHA PVTPKVRQFA LQLSIPVVAI GGIGKANIGA LYAEGFRSFA MISAVVGQVQ IAAAVQALRQ AVAVD // ID D3MC86_PROAA Unreviewed; 216 AA. AC D3MC86; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9207_0380; OS Propionibacterium acnes J165. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=679195; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J165; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Propionibacterium acnes J165."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADJL01000026; EFD07710.1; -; Genomic_DNA. DR ProteinModelPortal; D3MC86; -. DR EnsemblBacteria; EFD07710; EFD07710; HMPREF9207_0380. DR PATRIC; 36552457; VBIProAcn141457_0542. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID D3MDC5_PROAA Unreviewed; 217 AA. AC D3MDC5; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9207_2010; OS Propionibacterium acnes J165. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=679195; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J165; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Propionibacterium acnes J165."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADJL01000029; EFD07502.1; -; Genomic_DNA. DR ProteinModelPortal; D3MDC5; -. DR EnsemblBacteria; EFD07502; EFD07502; HMPREF9207_2010. DR PATRIC; 36553222; VBIProAcn141457_0920. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID D3MIU1_PROAA Unreviewed; 217 AA. AC D3MIU1; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1034_1761; OS Propionibacterium acnes SK187. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=686659; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK187; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Propionibacterium acnes SK187."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADJM01000001; EFD04144.1; -; Genomic_DNA. DR ProteinModelPortal; D3MIU1; -. DR EnsemblBacteria; EFD04144; EFD04144; HMPREF1034_1761. DR PATRIC; 36556602; VBIProAcn157577_0176. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID D3MK58_PROAA Unreviewed; 216 AA. AC D3MK58; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1034_0036; OS Propionibacterium acnes SK187. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=686659; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK187; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Propionibacterium acnes SK187."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADJM01000007; EFD03230.1; -; Genomic_DNA. DR ProteinModelPortal; D3MK58; -. DR EnsemblBacteria; EFD03230; EFD03230; HMPREF1034_0036. DR PATRIC; 36557962; VBIProAcn157577_0839. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID D3MQ59_9FIRM Unreviewed; 223 AA. AC D3MQ59; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 13-NOV-2013, entry version 18. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF0631_1660; OS Peptostreptococcus anaerobius 653-L. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptostreptococcus. OX NCBI_TaxID=596329; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=653-L; RA Dodson R., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADJN01000015; EFD05697.1; -; Genomic_DNA. DR EnsemblBacteria; EFD05697; EFD05697; HMPREF0631_1660. DR PATRIC; 36561551; VBIPepAna70759_0402. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 223 AA; 25757 MW; BEAAA5B51122C9FE CRC64; MENSPNDITY DRNSPIRLKV ITNRKLCEGQ DLVYRLGRVI DDYMDCKYLE GYILDSIILR EKDMDQSDYI KLYQNIYDLV DRFNRDKRLV VNNLPRIGLY SHYFMEKSVE NGIKNIHLPL HILKNNKKLV DKFDSIGVSC HSLEEAREAR ELGASYITFS HIFITDCKKG LEPRGLDELN YVVKNIDIPV YALGGINHTN ARECIDSGAS GVVMMSNIMK NKI // ID D3MSX2_9FIRM Unreviewed; 209 AA. AC D3MSX2; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0631_0522; OS Peptostreptococcus anaerobius 653-L. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptostreptococcus. OX NCBI_TaxID=596329; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=653-L; RA Dodson R., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADJN01000056; EFD04782.1; -; Genomic_DNA. DR ProteinModelPortal; D3MSX2; -. DR EnsemblBacteria; EFD04782; EFD04782; HMPREF0631_0522. DR PATRIC; 36563310; VBIPepAna70759_1228. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22988 MW; 6345A1267194682A CRC64; MANIGDKILY LVTDEAACRG KDFFESVEAA IRGGVSIVQL REKNLSTRDF YQKGLKLKKL CQDYGVTLLV NDRLDIAQAI GADGVHLGQT DMPIEVAKEI LGPDKIIGIT AKTIYQALDA QEAGADYIGV GAFFPTPSKK DAVLLDRSQL DMILERVRIK KYAIGGLGLD NVDKIRSYDM DGVCIISDIL ASDDCEARSR QIFDKINNR // ID D3NT73_AZOS1 Unreviewed; 216 AA. AC D3NT73; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AZL_009640; OS Azospirillum sp. (strain B510). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=137722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B510; RX PubMed=20047946; DOI=10.1093/dnares/dsp026; RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H., RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., RA Katoh M., Nakazaki N., Nakayama S., Yamada M., Tabata S., Sato S.; RT "Complete genomic structure of the cultivated rice endophyte RT Azospirillum sp. B510."; RL DNA Res. 17:37-50(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010946; BAI71602.1; -; Genomic_DNA. DR RefSeq; YP_003448146.1; NC_013854.1. DR ProteinModelPortal; D3NT73; -. DR EnsemblBacteria; BAI71602; BAI71602; AZL_009640. DR GeneID; 8789300; -. DR KEGG; azl:AZL_009640; -. DR PATRIC; 31930839; VBIAzoSp82869_1059. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; ASP137722:GBYD-981-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22805 MW; 643DA69520D0368C CRC64; MESAACRLYL VTPPALEPAA FAPLLAEALD AGDVACVQLR LKDRPEDDIR RACDLLRPIA QERDVAFILN DHPRLAREAG CDGVHVGQTD TPYRDARKIM GNDAIVGVTC HDSRHLAMIA GEEGADYVAF GAFFPTTTKT AEYKAEPELL SWWSELMEVP CVAIGGITAD NCAPLVAAGA DFLAVVNAVW GHPQGPGAGV RALNAAIDAV LVGSAG // ID D3NZN0_AZOS1 Unreviewed; 206 AA. AC D3NZN0; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 13-NOV-2013, entry version 26. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=AZL_a03280; OS Azospirillum sp. (strain B510). OG Plasmid pAB510a. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=137722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B510; PLASMID=pAB510a; RX PubMed=20047946; DOI=10.1093/dnares/dsp026; RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H., RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., RA Katoh M., Nakazaki N., Nakayama S., Yamada M., Tabata S., Sato S.; RT "Complete genomic structure of the cultivated rice endophyte RT Azospirillum sp. B510."; RL DNA Res. 17:37-50(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010947; BAI73859.1; -; Genomic_DNA. DR RefSeq; YP_003450403.1; NC_013855.1. DR ProteinModelPortal; D3NZN0; -. DR EnsemblBacteria; BAI73859; BAI73859; AZL_a03280. DR GeneID; 8792637; -. DR KEGG; azl:AZL_a03280; -. DR PATRIC; 31935812; VBIAzoSp82869_3506. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; ASP137722:GBYD-3281-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Transferase. SQ SEQUENCE 206 AA; 20903 MW; AA0223A0A4FC6081 CRC64; MPVPYPPLLV ITDRRQADQP LPELVERLFL AGVRWLSLRD KDLPDAERVE LARALMVLAR LWGACVTLHG DPALAVAAGA DGVHLTSGGD PAAARALLGA GALIGLSLHD SDGPAALERV AGQADYVTLS PVFPSGSKPG YGPCLGEAGL RRWTGTGVPV IGLGGIDNAE SVVACRAAGA AGVAVMGLAM RDVPALAPLL GALGAE // ID D3P8N4_DEFDS Unreviewed; 213 AA. AC D3P8N4; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=DEFDS_1616; OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC OS 101012 / SSM1). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Deferribacter. OX NCBI_TaxID=639282; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1; RX PubMed=20189949; DOI=10.1093/dnares/dsq005; RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., RA Ankai A., Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., RA Takami H., Takai K.; RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed RT by the genome sequence of the thermophilic bacterium Deferribacter RT desulfuricans SSM1."; RL DNA Res. 17:123-137(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011529; BAI81074.1; -; Genomic_DNA. DR RefSeq; YP_003496830.1; NC_013939.1. DR ProteinModelPortal; D3P8N4; -. DR EnsemblBacteria; BAI81074; BAI81074; DEFDS_1616. DR GeneID; 8868614; -. DR KEGG; ddf:DEFDS_1616; -. DR PATRIC; 35337191; VBIDefDes107323_1617. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; DDES639282:GJ90-1605-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 24052 MW; 87DB47CED0E1B0A6 CRC64; MRSKDRSKIA DYLKCYIILE TDLIKLPLEE FLNQCIEAGA KMFQLRNKHK TARENFHIGE SIKKILDGKD VFFIINDRVD LALCLDADGV HLGEKDLPAD IVKRKYKDLI IGYSCNNLSD INYANQTNVD YIGIGPAFPT KTKEDHRTVL SKEDYNKLLS HTNLPAVAIG GITPKNISKF HDIPISGFAV SSYICASENP FEAVKNILSF FHE // ID D3PA42_DEFDS Unreviewed; 188 AA. AC D3PA42; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 16-OCT-2013, entry version 25. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=DEFDS_2135; OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC OS 101012 / SSM1). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Deferribacter. OX NCBI_TaxID=639282; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1; RX PubMed=20189949; DOI=10.1093/dnares/dsq005; RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., RA Ankai A., Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., RA Takami H., Takai K.; RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed RT by the genome sequence of the thermophilic bacterium Deferribacter RT desulfuricans SSM1."; RL DNA Res. 17:123-137(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011529; BAI81582.1; -; Genomic_DNA. DR RefSeq; YP_003497338.1; NC_013939.1. DR ProteinModelPortal; D3PA42; -. DR EnsemblBacteria; BAI81582; BAI81582; DEFDS_2135. DR GeneID; 8868283; -. DR KEGG; ddf:DEFDS_2135; -. DR PATRIC; 35338271; VBIDefDes107323_2144. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; YTLSPIF; -. DR BioCyc; DDES639282:GJ90-2131-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 188 AA; 21885 MW; 239E5A9750F22A88 CRC64; MLKILQILDF DTFGDKIFDI AVRVDKFVDF FWLRIKNQNT RFIFDTAKNL TNYIDREKII ISEHCDIASI LTLHGAHLNK NSIPTNFIKY TFPNLTIGYS AHSIEEIQTI EADYYTLSPI FNTKKSYPVK PLGLDFKLPK NKKIFALGGI NKNNINFIIN KGFHGIAGIR FFNELKEMRM LLNRLTCR // ID D3PTL3_MEIRD Unreviewed; 208 AA. AC D3PTL3; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mrub_2041; ORFNames=K649_12335; OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) OS (Thermus ruber). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Meiothermus. OX NCBI_TaxID=504728; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21; RX PubMed=21304689; DOI=10.4056/sigs.1032748; RA Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A., RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., RA Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Complete genome sequence of Meiothermus ruber type strain (21)."; RL Stand. Genomic Sci. 3:26-36(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1279; RA Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J., RA Eichler E., Turner S.W.; RT "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT RT Sequencing Data."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1279; RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001743; ADD28796.1; -; Genomic_DNA. DR EMBL; CP005385; AGK05755.1; -; Genomic_DNA. DR RefSeq; YP_003507816.1; NC_013946.1. DR RefSeq; YP_007881252.1; NC_021081.1. DR EnsemblBacteria; ADD28796; ADD28796; Mrub_2041. DR EnsemblBacteria; AGK05755; AGK05755; K649_12335. DR GeneID; 15337065; -. DR GeneID; 8880150; -. DR KEGG; mrb:Mrub_2041; -. DR KEGG; mre:K649_12335; -. DR PATRIC; 35360271; VBIMeiRub128672_2051. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; MRUB504728:GI6U-2085-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22772 MW; 628BD72B62C55D0A CRC64; MHGKLYLVAT PRPGQAEAEL MRRLEAALEG GVDLLQLRAK NLEAQAILAL GENLRALCAR YRVPLIINDR PDLAALLEAH GVHLGQGDLN VAQARRFFSG WIGRSTHEPE QALREQAALE GGPGYLSVGP VWETPTKPGR PAAGLAYVRW AAQNLRVPWF AIGGIDEHTL PQVLEAGARR VAVVRSILDA PDPEKAARHM RRWLDGLD // ID D3Q913_STANL Unreviewed; 218 AA. AC D3Q913; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Snas_0911; OS Stackebrandtia nassauensis (strain DSM 44728 / NRRL B-16338 / NBRC OS 102104 / LLR-40K-21). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Glycomycineae; Glycomycetaceae; Stackebrandtia. OX NCBI_TaxID=446470; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44728 / NRRL B-16338 / NBRC 102104 / LLR-40K-21; RX PubMed=21304662; DOI=10.4056/sigs.47643; RA Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S., RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F., RA Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., RA Goker M., Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Stackebrandtia nassauensis type strain RT (LLR-40K-21)."; RL Stand. Genomic Sci. 1:292-299(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001778; ADD40622.1; -; Genomic_DNA. DR RefSeq; YP_003509715.1; NC_013947.1. DR ProteinModelPortal; D3Q913; -. DR EnsemblBacteria; ADD40622; ADD40622; Snas_0911. DR GeneID; 8882095; -. DR KEGG; sna:Snas_0911; -. DR PATRIC; 35364142; VBIStaNas43420_0894. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; SNAS446470:GHHC-922-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 22090 MW; 65C212508D9B6ACC CRC64; MDSSLPLGRL HVITDTRPGA DPVRVARAAL AAGAPVLQVR VADHHTDREA FDLTLTLVEL CREYGATCLV NDRLHVALAV GADGGHVGAH DLPVHAARVV LGGTAVIGGT CRNPEAARAL RRAGASYLGA GPAFATTTKD GLPEPIGPGA IGRIAAAVDI PVIGIGGVTA ATAGELIEAG AHGVAVVGAI SLAPDPYAAT RELLDVVERA ARQRGRSR // ID D3QC03_STANL Unreviewed; 192 AA. AC D3QC03; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 30. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Snas_5258; OS Stackebrandtia nassauensis (strain DSM 44728 / NRRL B-16338 / NBRC OS 102104 / LLR-40K-21). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Glycomycineae; Glycomycetaceae; Stackebrandtia. OX NCBI_TaxID=446470; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44728 / NRRL B-16338 / NBRC 102104 / LLR-40K-21; RX PubMed=21304662; DOI=10.4056/sigs.47643; RA Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S., RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F., RA Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., RA Goker M., Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Stackebrandtia nassauensis type strain RT (LLR-40K-21)."; RL Stand. Genomic Sci. 1:292-299(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001778; ADD44892.1; -; Genomic_DNA. DR RefSeq; YP_003513985.1; NC_013947.1. DR ProteinModelPortal; D3QC03; -. DR EnsemblBacteria; ADD44892; ADD44892; Snas_5258. DR GeneID; 8886467; -. DR KEGG; sna:Snas_5258; -. DR PATRIC; 35372831; VBIStaNas43420_5215. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VMRAEDP; -. DR BioCyc; SNAS446470:GHHC-5294-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 192 AA; 20176 MW; 6A4D64576BE04BC1 CRC64; MIHTLPRLLI LTDASACPRP LPEQIALALD AGARAFVLRE KGLPPARRRA LAQRLEPPLT EAGAKLIISD PTWTVDACHL SALARAPRPR PDLVGRSAHT GQSDDPNADY VTFSPIYPTA SKPGYGPALG PEGLAEYCAS SRVPVYALGG VETGERAAEC RAAGAHGVAV MGAVMRAEDP ATVVRELLDG LD // ID D3QHD0_STALH Unreviewed; 196 AA. AC D3QHD0; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=SLGD_00498; OS Staphylococcus lugdunensis (strain HKU09-01). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=698737; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HKU09-01; RX PubMed=20047907; DOI=10.1128/JB.01627-09; RA Tse H., Tsoi H.W., Leung S.P., Lau S.K., Woo P.C., Yuen K.Y.; RT "Complete genome sequence of Staphylococcus lugdunensis strain HKU09- RT 01."; RL J. Bacteriol. 192:1471-1472(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001837; ADC86646.1; -; Genomic_DNA. DR RefSeq; YP_003470773.1; NC_013893.1. DR ProteinModelPortal; D3QHD0; -. DR EnsemblBacteria; ADC86646; ADC86646; SLGD_00498. DR GeneID; 8818204; -. DR KEGG; slg:SLGD_00498; -. DR PATRIC; 35304352; VBIStaLug155172_0489. DR HOGENOM; HOG000090085; -. DR KO; K10810; -. DR OMA; FAGICAI; -. DR BioCyc; SLUG698737:GHG4-498-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 196 AA; 22570 MW; 8D0598C59E1D47A5 CRC64; MFIFIAITEY KFLDNNDLQH FLTIEQDIDF LLFRTSMSQK ELQHFIQQLI YQGFPKSKMM IHSDVKLLNT LGLQNIHFRE NDAQAFHLKS KYPDIHVSMS THHLSSVIRA YEAGLDAVFF GHIFPTPSKP NLPPRSQVEI DSVLEVPIPV YAIGGITTDT IRKLSPKFAG ICAISFFMKS SASVIHQFRK EWHHHA // ID D3QIK6_STALH Unreviewed; 212 AA. AC D3QIK6; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SLGD_00931; OS Staphylococcus lugdunensis (strain HKU09-01). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=698737; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HKU09-01; RX PubMed=20047907; DOI=10.1128/JB.01627-09; RA Tse H., Tsoi H.W., Leung S.P., Lau S.K., Woo P.C., Yuen K.Y.; RT "Complete genome sequence of Staphylococcus lugdunensis strain HKU09- RT 01."; RL J. Bacteriol. 192:1471-1472(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001837; ADC87069.1; -; Genomic_DNA. DR RefSeq; YP_003471196.1; NC_013893.1. DR ProteinModelPortal; D3QIK6; -. DR EnsemblBacteria; ADC87069; ADC87069; SLGD_00931. DR GeneID; 8818636; -. DR KEGG; slg:SLGD_00931; -. DR PATRIC; 35305218; VBIStaLug155172_0913. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR BioCyc; SLUG698737:GHG4-930-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23242 MW; 9479E06EB38F9005 CRC64; MFKSTDLKVY FICGTQDIPE GKSLEQVVTQ ALESGVTMFQ FREKGSKVSQ DKKIEQLALK LKELCHNYQV PFIVNDNVAL ALKVQADGIH VGQDDAKVED FFEQFHDKII GLSVSNLDEL KRSDLTHVDY IGVGPIYQTP SKSDASTPVG PEMILTLRKE IGDFPIVAIG GVTENNAQAV VDAGADGISV ISAIARSQNI DSTVNKFLSY YN // ID D3QYJ3_ECOCB Unreviewed; 211 AA. AC D3QYJ3; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=G2583_4811; OS Escherichia coli O55:H7 (strain CB9615 / EPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=701177; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CB9615 / EPEC; RX PubMed=20090843; DOI=10.1371/journal.pone.0008700; RA Zhou Z., Li X., Liu B., Beutin L., Xu J., Ren Y., Feng L., Lan R., RA Reeves P.R., Wang L.; RT "Derivation of Escherichia coli O157:H7 from its O55:H7 precursor."; RL PLoS ONE 5:E8700-E8700(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001846; ADD59242.1; -; Genomic_DNA. DR RefSeq; YP_003502226.1; NC_013941.1. DR ProteinModelPortal; D3QYJ3; -. DR SMR; D3QYJ3; 10-209. DR EnsemblBacteria; ADD59242; ADD59242; G2583_4811. DR GeneID; 8873773; -. DR KEGG; eok:G2583_4811; -. DR PATRIC; 35348795; VBIEscCol154499_4809. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; ECOL701177:GI1N-4812-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D3QYY4_CLOB3 Unreviewed; 211 AA. AC D3QYY4; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HMPREF0868_1412; OS Clostridiales genomosp. BVAB3 (strain UPII9-5). OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=699246; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UPII9-5; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001850; ADC90797.1; -; Genomic_DNA. DR RefSeq; YP_003475667.1; NC_013895.2. DR ProteinModelPortal; D3QYY4; -. DR EnsemblBacteria; ADC90797; ADC90797; HMPREF0868_1412. DR GeneID; 8810585; -. DR KEGG; clo:HMPREF0868_1412; -. DR PATRIC; 35311318; VBICloGen152872_1358. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; CGEN699246:GI5D-321-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22911 MW; 8F45040E3C82B36F CRC64; MRIKKTKELY FITDNSYGDR TSFIHTIEEV LRAGVGLIQL REKNTEGREL LALARRVKSL CDQYNVPLII DDRLDVALLA GCGVHLGQSD LPIAEARRVL PPDTIIGATT KTVPQALEAA AAGADYLGVG AIYQTKTKVK TIFTSVDTLK EICEQVNIPV FAIGGLNETN LDILRPASAI QGICVVSAIM QAADPYAKTL AIKQALKDLF D // ID D3R689_BIFAB Unreviewed; 564 AA. AC D3R689; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 29. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.1.49; DE EC=2.7.4.7; GN OrderedLocusNames=BIF_02010; OS Bifidobacterium animalis subsp. lactis (strain BB-12). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=552531; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BB-12; RX PubMed=20190051; DOI=10.1128/JB.00109-10; RA Garrigues C., Johansen E., Pedersen M.B.; RT "Complete genome sequence of Bifidobacterium animalis subsp. lactis RT BB-12, a widely consumed probiotic strain."; RL J. Bacteriol. 192:2467-2468(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001853; ADC84621.1; -; Genomic_DNA. DR RefSeq; YP_005575631.1; NC_017214.1. DR ProteinModelPortal; D3R689; -. DR EnsemblBacteria; ADC84621; ADC84621; BIF_02010. DR GeneID; 12175815; -. DR KEGG; bbb:BIF_02010; -. DR PATRIC; 36801048; VBIBifAni31632_0112. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OMA; YLAQGEP; -. DR BioCyc; BANI552531:GL90-115-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 564 AA; 59777 MW; C0D07895B7146A86 CRC64; MGRDRSKPRS STLCGTLRRR KSPPHRSIWP RICHGTACRH TTNESGDTMN SFPYPSMRDR FDLRFYFVVG PDDCGNRPIL DVVAKALDGG ASFIQLRAKT QDVAEIVSLA NDIAEEIAGH HVEHSVAFVV DDRVDAALEA RAKGIKVDGV HIGQDDLDPV VARKLLGPDA IIGLSAKTVD EVREANHLPE GTIDYIGAGP LHMTATKPES MIVDENGDIT TLNVSSIDEM RTMSKYPLIV GGGVKADDIP MLAKTKADGW FVVSAIAGAT DPEQATRRLV DDWTAIRGDE KPRYTGRKPA ATKLPAVLTI ATTDSSGGAG IPADLKTMLA NDVFGECVVA GITAQNTTGV QAIAAVDPSI VGAQIDSVFD DIRPTAVKIG VIVGVESVKT VARKLRDHQA TNIVVDPVMV ATSGSSLAAD DTIAEEISSL FPIATVITPN IPEAQVLAQM PIGNQADMET AAVQLAKDYG TCVLVKGGHG VKDADDVLAF PTGAVTWFEG ERIANDNTHG TGCTLSSAIA SYLAQGEDLE DAVRDAKAYL SGALRANLNL GKGHGPMDHA WAMH // ID D3RGB1_KLEVT Unreviewed; 211 AA. AC D3RGB1; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Kvar_4867; OS Klebsiella variicola (strain At-22). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=640131; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=At-22; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Pinto A., RA Currie C., Woyke T.; RT "Complete sequence of Klebsiella variicola At-22."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001891; ADC60738.1; -; Genomic_DNA. DR RefSeq; YP_003441770.1; NC_013850.1. DR ProteinModelPortal; D3RGB1; -. DR EnsemblBacteria; ADC60738; ADC60738; Kvar_4867. DR GeneID; 8785068; -. DR KEGG; kva:Kvar_4867; -. DR PATRIC; 32229880; VBIKleVar54872_4835. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; KVAR640131:GHXG-4956-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22973 MW; 50107BF2974F876F CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIERLLE AGVRTLQLRI KDQRDSDVED DVIAAIALGR RYHARLFIND YWQLAIKHQA YGVHLGQEDL ETTDLSAIRK AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLDQLA RHIQRLADYP TVAIGGISLE KAPAVLATGV GSIAVVSAIT QAADWRAATD QLLALAGAGD E // ID D3RVE6_ALLVD Unreviewed; 212 AA. AC D3RVE6; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Alvin_0104; OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) OS (Chromatium vinosum). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Allochromatium. OX NCBI_TaxID=572477; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / D; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., RA Land M., Hauser L., Kyrpides N., Ivanova N., Zigann R., Dahl C., RA Woyke T.; RT "Complete sequence of chromosome of Allochromatium vinosum DSM 180."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001896; ADC61073.1; -; Genomic_DNA. DR RefSeq; YP_003442105.1; NC_013851.1. DR ProteinModelPortal; D3RVE6; -. DR EnsemblBacteria; ADC61073; ADC61073; Alvin_0104. DR GeneID; 8785431; -. DR KEGG; alv:Alvin_0104; -. DR PATRIC; 31919947; VBIAllVin64954_0105. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; AVIN572477:GCJK-104-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22347 MW; ECE3A50BCE913C8A CRC64; MSNTSLRGLY AITPDAPLTI ATLVDQVDAA IDGGARVIQY RDKTYERDER RRRAAALLAR CRAAGVPLII NDDLDLAVEL GADGVHLGRD DPDPRAARER LSETAIIGVS CYDQLALAEA AAANGASYVA FGSFFPSTTK PKAVRPDPGL LTEARRRVTL PLVAIGGITP HNGGPLIAAG ADMLAVVTGV FAQADITAAA RAYTNLFPKE TH // ID D3RVI7_ALLVD Unreviewed; 315 AA. AC D3RVI7; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 16-OCT-2013, entry version 30. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=Alvin_0145; OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) OS (Chromatium vinosum). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Allochromatium. OX NCBI_TaxID=572477; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / D; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., RA Land M., Hauser L., Kyrpides N., Ivanova N., Zigann R., Dahl C., RA Woyke T.; RT "Complete sequence of chromosome of Allochromatium vinosum DSM 180."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001896; ADC61114.1; -; Genomic_DNA. DR RefSeq; YP_003442146.1; NC_013851.1. DR ProteinModelPortal; D3RVI7; -. DR EnsemblBacteria; ADC61114; ADC61114; Alvin_0145. DR GeneID; 8785478; -. DR KEGG; alv:Alvin_0145; -. DR PATRIC; 31920039; VBIAllVin64954_0146. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR BioCyc; AVIN572477:GCJK-151-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34106 MW; 6E2F5C965A55E4B6 CRC64; MPEIIHVMAG AIADASGRIL VGKRPDHVHQ GGLWEFPGGK LEPGESPEAG LARELAEELG IQVRASRPLI RVHHDYGDRH ILLDVHRVDD YAGVPHGREG QPLDWLAPEE MDPAAFPAAD RPIITSLRLP PLMLITGEEP DRPDAFLARL GRALETGARL VQLRAHQLSA NDYVHLAQAA CDLCDRTGAK LLLNRDPAEV ASVPRHGLHL NSQVLMTLRE RPGRSSELVG ASCHDPVQLA RAVDLGLDYA LLSPVKPTAS HPETSPLGWN TFAAWVDLVP LPVYALGGLT TDDLDDAFQH GAQGIAAIRG LWPAR // ID D3S1W5_FERPA Unreviewed; 207 AA. AC D3S1W5; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ferp_0240; OS Ferroglobus placidus (strain DSM 10642 / AEDII12DO). OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; OC Archaeoglobaceae; Ferroglobus. OX NCBI_TaxID=589924; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10642 / AEDII12DO; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D., RA Lovley D., Kyrpides N., Anderson I.J., Woyke T.; RT "Complete sequence of Ferroglobus placidus DSM 10642."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001899; ADC64422.1; -; Genomic_DNA. DR RefSeq; YP_003434697.1; NC_013849.1. DR ProteinModelPortal; D3S1W5; -. DR EnsemblBacteria; ADC64422; ADC64422; Ferp_0240. DR GeneID; 8777735; -. DR KEGG; fpl:Ferp_0240; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; FPLA589924:GHX0-245-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22784 MW; 88D86CACBFE8D01C CRC64; MFSVKIRGLY VITSADFGWK HEEIAEMALK AGARIIQLRE KRMPARKIYE VARKIRKLCD EYDAIFIVND RLDIAMLSDA DGVHVGKEDP PADKIKEIFD GIVGVSVDNV EEAKEAESYA DYVGVGPVFK TTTKPDAGEV IGLEGLKKVK EVVKIPVVAI GGINKDNVRE VIRIADAVAV VSAIASSKDP YKATKELLEI IENETQL // ID D3SD80_THISK Unreviewed; 315 AA. AC D3SD80; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 16-OCT-2013, entry version 29. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=TK90_2189; OS Thioalkalivibrio sp. (strain K90mix). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thioalkalivibrio. OX NCBI_TaxID=396595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K90mix; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L., RA Kyrpides N., Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.; RT "Complete sequence of chromosome of Thioalkalivibrio sp. K90mix."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001905; ADC72679.1; -; Genomic_DNA. DR RefSeq; YP_003461415.1; NC_013889.1. DR ProteinModelPortal; D3SD80; -. DR EnsemblBacteria; ADC72679; ADC72679; TK90_2189. DR GeneID; 8807968; -. DR KEGG; tkm:TK90_2189; -. DR PATRIC; 32527970; VBIThiSp13812_2177. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR BioCyc; TSP396595:GH8D-2240-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 33747 MW; 2302895564EF97BB CRC64; MGLVLDAEGR VLVSRRLAGR HLAGYWEFPG GKIDAGESAF AGLVRELHEE LGIVVRAGVQ CLTVRHDFAE CSVALRVFRV TEWSGTVHGR EGQEWAWRDP ATLDPADFPA ANHPMFQALV LPQRYVITPS PAVRAEIPAV VEQVQAALVA MDDAMLQVRA PSLGRKDYRA LVEPLHGFAR GRGIPLLANA PWEWVADLSG IGWHLPERRW RALDERPPVS GLVAASVHDA EGLTAAARLG LDFAVLSPVC STVSHPGVPG MGWAQFAAQV REAGVPVYAL GGMRASDLEQ ARTCGAQGIA AIRGLLGMEA GETAV // ID D3SDT7_THISK Unreviewed; 214 AA. AC D3SDT7; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TK90_0392; OS Thioalkalivibrio sp. (strain K90mix). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thioalkalivibrio. OX NCBI_TaxID=396595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K90mix; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L., RA Kyrpides N., Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.; RT "Complete sequence of chromosome of Thioalkalivibrio sp. K90mix."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001905; ADC70907.1; -; Genomic_DNA. DR RefSeq; YP_003459643.1; NC_013889.1. DR ProteinModelPortal; D3SDT7; -. DR EnsemblBacteria; ADC70907; ADC70907; TK90_0392. DR GeneID; 8806127; -. DR KEGG; tkm:TK90_0392; -. DR PATRIC; 32524308; VBIThiSp13812_0387. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; TSP396595:GH8D-398-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 21990 MW; C4FE734723B8C48C CRC64; MTTDSRAPLR GLYFITPAVP EGVDPRATHL AHAEAALRGG ASLIQFRDKE LQGDAREAIA RELVALAHTH GARCIINDDT ELAARIQADG VHLGRDDPDP AAARALLGPD AVIGVSCYNE LARAEAAARA GASYVAFGTM FASPTKPEAA FAGPALVRRA RAALDLPICG IGGITPDNAA EVVAAGADLV AVIQGISAAP DPEAAARRIS ALFD // ID D3SIM8_DEHMG Unreviewed; 352 AA. AC D3SIM8; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 32. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=DehalGT_0669; OS Dehalococcoides mccartyi (strain GT). OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales; OC Dehalococcoidaceae; Dehalococcoides. OX NCBI_TaxID=633145; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GT; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Misra M., Chertkov O., Detter J.C., Han C., Tapia R., RA Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Ritalahti K.M., Fletcher K.E., Sung Y., Wagner D., RA Konstantinidis K.T., Loeffler F.E., Woyke T.; RT "Complete sequence of Dehalococcoides sp. GT."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001924; ADC74035.1; -; Genomic_DNA. DR RefSeq; YP_003462491.1; NC_013890.1. DR ProteinModelPortal; D3SIM8; -. DR EnsemblBacteria; ADC74035; ADC74035; DehalGT_0669. DR GeneID; 8809118; -. DR KEGG; deg:DehalGT_0669; -. DR PATRIC; 32055306; VBIDehSp13473_0643. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR BioCyc; DSP633145:GHAK-686-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 179 183 HMP-PP binding (By similarity). FT REGION 276 278 THZ-P binding (By similarity). FT REGION 326 327 THZ-P binding (By similarity). FT METAL 212 212 Magnesium (By similarity). FT METAL 231 231 Magnesium (By similarity). FT BINDING 211 211 HMP-PP (By similarity). FT BINDING 250 250 HMP-PP (By similarity). FT BINDING 279 279 HMP-PP (By similarity). FT BINDING 306 306 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 352 AA; 38380 MW; DB76FB22E5595F25 CRC64; MDNLEKLWRI VDVNQNRLSE GLRILEEIAR LYLENETLTL RLKNLRHALT LQDTASNCHL LFSRQADTDI GAHLKTVDQS KPETLFSLIS ANAKRAEQSL RVLEEFAGLL ELGLDTSIYS RGRFELYTLE KDLAAILLRK NRRDMIKGLY VAIDVDYLAG RDIPRVTKEV LEGGCRLVQL RAKTASARQF LSLALSLKEL CIEYGAVFIV NDRLDIALAC GADGLHLGQT DLPLSQARRL MPAGSIIGIS ADSPEDAASA QAGDADYVAA GAVFPTQTKL DVLYGGLSGL KAIRQVVNIP LVAIGGINKS NYNEALQAGA DSLCLISAVL GAPDIKKATS EFMTLVEAEK ND // ID D3SLF6_THEAH Unreviewed; 217 AA. AC D3SLF6; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Thal_0954; OS Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Thermocrinis. OX NCBI_TaxID=638303; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14484 / JCM 11386 / HI 11/12; RA Wirth R., Sikorski J., Brambilla E., Misra M., Lapidus A., RA Copeland A., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Han C., RA Detter J.C., Tapia R., Bruce D., Goodwin L., Pitluck S., Pati A., RA Anderson I., Ivanova N., Mavromatis K., Mikhailova N., Chen A., RA Palaniappan K., Bilek Y., Hader T., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Tindall B.J., Rohde M., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Thermocrinis albus type strain (HI RT 11/12T)."; RL Stand. Genomic Sci. 2:194-202(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001931; ADC89586.1; -; Genomic_DNA. DR RefSeq; YP_003473713.1; NC_013894.1. DR ProteinModelPortal; D3SLF6; -. DR EnsemblBacteria; ADC89586; ADC89586; Thal_0954. DR GeneID; 8814469; -. DR KEGG; tal:Thal_0954; -. DR PATRIC; 32508178; VBITheAlb52854_0949. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTLLQYR; -. DR BioCyc; TALB638303:GHKY-988-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 24290 MW; A3FAE428E8148F57 CRC64; MKGRMNLSIY LVTDDRYFQD RDLVDTIEKA IQGGVTAVQY RFKNKSTRQM YEELLVLREL TKRYGVDLVV NDRVDLALAV EADGVHVGET DLPPDVVRKL VGDKMYIGYS VNSLEKLREV EHLPIDYIGF GSVYETTTKE NYKLVGIEAL KQAVKMTSKP VIAIGGITHY RVPEVLATGV KGIAVVSAIL GFEDVKKAAE SLLQACRQAM RQKLFMG // ID D3SNR5_THEAH Unreviewed; 188 AA. AC D3SNR5; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Thal_0166; OS Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Thermocrinis. OX NCBI_TaxID=638303; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14484 / JCM 11386 / HI 11/12; RA Wirth R., Sikorski J., Brambilla E., Misra M., Lapidus A., RA Copeland A., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Han C., RA Detter J.C., Tapia R., Bruce D., Goodwin L., Pitluck S., Pati A., RA Anderson I., Ivanova N., Mavromatis K., Mikhailova N., Chen A., RA Palaniappan K., Bilek Y., Hader T., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Tindall B.J., Rohde M., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Thermocrinis albus type strain (HI RT 11/12T)."; RL Stand. Genomic Sci. 2:194-202(2010). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001931; ADC88802.1; -; Genomic_DNA. DR RefSeq; YP_003472929.1; NC_013894.1. DR ProteinModelPortal; D3SNR5; -. DR EnsemblBacteria; ADC88802; ADC88802; Thal_0166. DR GeneID; 8813653; -. DR KEGG; tal:Thal_0166; -. DR PATRIC; 32506538; VBITheAlb52854_0157. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INERSDI; -. DR BioCyc; TALB638303:GHKY-171-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 188 AA; 20862 MW; DF3CAE6E2271892A CRC64; MAQLPRLYAI TDSKLYGDRW EEILLRLMER GVRMIQLREK DISASQYYQK ALKVREITAR YGALLFINDR VDIAMAVEAD GVHLPSSGLP PSVVKKLSPK LLVGFSAHNM EEALQAEREG ADFITLSPIF PTRSHPNAEP VGLKTLAEVS RAVSIPVYAL GGVTWDKLKL CYKNGAYGVA GISLFLEE // ID D3SUX7_NATMM Unreviewed; 221 AA. AC D3SUX7; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Nmag_1811; ORFNames=C500_11295; OS Natrialba magadii (strain ATCC 43099 / DSM 3394 / NCIMB 2190 / MS3) OS (Natronobacterium magadii). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Natrialba. OX NCBI_TaxID=547559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43099 / DSM 3394 / NCIMB 2190 / MS3; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E., RA Maupin-Furlow J.A., Woyke T.; RT "Complete sequence of chromosome of Natrialba magadii ATCC 43099."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43099; RX PubMed=22559199; DOI=10.1186/1471-2164-13-165; RA Siddaramappa S., Challacombe J.F., Decastro R.E., Pfeiffer F., RA Sastre D.E., Gimenez M.I., Paggi R.A., Detter J.C., Davenport K.W., RA Goodwin L.A., Kyrpides N., Tapia R., Pitluck S., Lucas S., Woyke T., RA Maupin-Furlow J.A.; RT "A comparative genomics perspective on the genetic content of the RT alkaliphilic haloarchaeon Natrialba magadii ATCC 43099T."; RL BMC Genomics 13:165-165(2012). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS-3; RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., RA Darling A., Eisen J.A., Facciotti M.T.; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001932; ADD05385.1; -; Genomic_DNA. DR EMBL; AOHS01000037; ELY29299.1; -; Genomic_DNA. DR RefSeq; YP_003479947.1; NC_013922.1. DR EnsemblBacteria; ADD05385; ADD05385; Nmag_1811. DR EnsemblBacteria; ELY29299; ELY29299; C500_11295. DR GeneID; 8824652; -. DR KEGG; nmg:Nmag_1811; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; NMAG547559:GJAP-1838-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 22405 MW; C88D28F07833039A CRC64; MDPSNWQTYL VTQESVSAGR STLEIVEAAI AGGVDVVQLR EKDTDTRFRY ELGRELRELT AEAGVGLIVN DRVDIAQAID ADGVHVGQSD LPVSVARDLL GPDSIVGCST GTVDAAEQAE ADGADYVGVG TIYGTTSKDV AKHKDGVGPE RVADVTDAIS IPAVGIGGIT AGNAGPVVEA GAVGVAVISA ITAADDPRAA TAALASTVET TKHVEHGGAT E // ID D3T7H0_THEIA Unreviewed; 209 AA. AC D3T7H0; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-MAY-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Thit_0601; OS Thermoanaerobacter italicus (strain DSM 9252 / Ab9). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=580331; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9252 / Ab9; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Hemme C.L., Woyke T.; RT "Complete sequence of Thermoanaerobacter italicus Ab9."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001936; ADD01902.1; -; Genomic_DNA. DR RefSeq; YP_003476464.1; NC_013921.1. DR ProteinModelPortal; D3T7H0; -. DR EnsemblBacteria; ADD01902; ADD01902; Thit_0601. DR GeneID; 8820922; -. DR KEGG; tit:Thit_0601; -. DR PATRIC; 32496188; VBITheIta22270_0616. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR BioCyc; TITA580331:GHTM-629-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22464 MW; 250058A709114E30 CRC64; MDLTLYAITD RSYIKNMDIA DAVELAIKGG ATVIQLREKD ISSREFYEIA LKVKEVAKRN KIPFIINDRV DIALAVDADG VHVGQEDLPA DVVRRMIGPH KIVGVSASTV EEALKAQKDG ADYLGVGAVF KTPTKPEAEA IGIEGLKKIK EAVSIPVVAI GGITKDNAYE VMLKSGVDGI SSVSAVFYGD IENNTRKLLE VIAKAIKAL // ID D3V662_XENBS Unreviewed; 224 AA. AC D3V662; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=XBJ1_4029; OS Xenorhabdus bovienii (strain SS-2004). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Xenorhabdus. OX NCBI_TaxID=406818; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SS-2004; RA Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S., RA Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P., RA Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S., RA Suen G.; RT "Complete genome sequence of Xenorhabdus nematophila (strain ATCC RT 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6)."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN667741; CBJ83141.1; -; Genomic_DNA. DR RefSeq; YP_003469903.1; NC_013892.1. DR ProteinModelPortal; D3V662; -. DR EnsemblBacteria; CBJ83141; CBJ83141; XBJ1_4029. DR GeneID; 8833652; -. DR KEGG; xbo:XBJ1_4029; -. DR PATRIC; 35302647; VBIXenBov95754_3637. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; XBOV406818:GHLH-4023-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24858 MW; CF822891D0228D93 CRC64; MKNQPEASSI PQAPFAPTVH RLGLYPVVDS LTWIERLLKA GIRTLQLRIK DLPEDQVEED IQSAIVLGRQ YNARLFINDY WDLAIKHRAY GVHLGQEDLD IADLNAIRQA GLRLGISTHD EYELARTKAL RPSYIALGHI FPTTTKEMPS KPQGLSALKH QVEITPEYPT VAIGGISLDR VPDVVATGVG GVALVSAITK AKDWRQVTDQ LLHLIEGSDR ELLC // ID D3VJA3_XENNA Unreviewed; 224 AA. AC D3VJA3; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=XNC1_0585; OS Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 / OS NCIB 9965 / AN6). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Xenorhabdus. OX NCBI_TaxID=406817; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6; RA Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S., RA Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P., RA Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S., RA Suen G.; RT "Complete genome sequence of Xenorhabdus nematophila (strain ATCC RT 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6)."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN667742; CBJ88659.1; -; Genomic_DNA. DR RefSeq; YP_003710891.1; NC_014228.1. DR ProteinModelPortal; D3VJA3; -. DR EnsemblBacteria; CBJ88659; CBJ88659; XNC1_0585. DR GeneID; 9433614; -. DR KEGG; xne:XNC1_0585; -. DR PATRIC; 42461080; VBIXenNem38452_0535. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; XNEM406817:GHY4-591-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24745 MW; 2A5CEB40F699D448 CRC64; MKNTSDTFTL PSAPFAPTAH RLGLYPVVDS LIWIERLLEA GVRTLQLRIK DQPEEQAEKD IQSAIALGRQ YYARLFINDY WRLAIKHHAY GVHLGQEDLD VADLNAIQQA GLRLGISTHD QQELVRAKAL RPSYIALGHI FPTSTKEMPS SPQGLEALKH QVEITPEYPT VAIGGISLER VPDVVATGVG GVALVSAITK AQDWRQATAR LLHLVESQDR GLLC // ID D4AKP9_ARTBC Unreviewed; 559 AA. AC D4AKP9; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 16-APR-2014, entry version 21. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=ARB_04892; OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OS (Trichophyton mentagrophytes). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Arthroderma. OX NCBI_TaxID=663331; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4681 / CBS 112371; RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7; RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S., RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., RA Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., RA Kniemeyer O., Schroeckh V., Hertweck C., Hube B., White T.C., RA Platzer M., Guthke R., Heitman J., Woestemeyer J., Zipfel P.F., RA Monod M., Brakhage A.A.; RT "Comparative and functional genomics provide insights into the RT pathogenicity of dermatophytic fungi."; RL Genome Biol. 12:R7.1-R7.16(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABSU01000002; EFE35958.1; -; Genomic_DNA. DR RefSeq; XP_003016603.1; XM_003016557.1. DR GeneID; 9522085; -. DR KEGG; abe:ARB_04892; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 2. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 559 AA; 59336 MW; 40B0BC7C29FCCE7E CRC64; MPVNLSLYLV TDSTPKILGD RDLCSVVEQA VQGGVTIVQY RDKHSDTKEL IKTAAKLHDI TLNHGIPLII NDRVDVALAV GAEGVHLGQD DMSKIFLYSL SFNCIFMLMN LVDIAVARKM LPKGTIIGVT VSSVEEAQAA VESGADYLGI GTVYATPTEA KDSDSKTNTK SIIGTAGVKR ILSCVASLNP RVGTVAIGGI NLDNVQRIIY QSQDTKKGLE GVAIVSAIMA AENPRATAAL FLDKVSKNPA FATIPISPRE NEEELLLGKV DGLVRKVATA HPLCHNMINY VVANFAANVA LAIGASPIMS GYGLEAPDLA KNKGSLLINM GTLNSESLDN YMQAIRAYNE AGNPVVLDPV GAAATQLRRQ SVKTLMQGGY FDLIKGNESE IGHIYGHTGN QIGVDSGPST LDIKEKAMLV RDLALREILL CQQANNLFTG CIVLLTGPTD YLSDGARTIA IHNGHPLLGQ VTGTGCVIGT VTSAFLAVER QDKLLAVLSA LLMFEVAAER AVVSGVKGPG SFVPALLDEL YSLRTQATES KSASIDTLKK AAKVNFIHF // ID D4BL13_9ENTR Unreviewed; 211 AA. AC D4BL13; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CIT292_11253; OS Citrobacter youngae ATCC 29220. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex. OX NCBI_TaxID=500640; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29220; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWL02000041; EFE05390.1; -; Genomic_DNA. DR ProteinModelPortal; D4BL13; -. DR EnsemblBacteria; EFE05390; EFE05390; CIT292_11253. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22903 MW; 4DC909F3514F4AD8 CRC64; MYQPDFPTVP LRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLQAIQA AGLRLGVSTH DDMEIDVALS ARPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIKRLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID D4BRL3_BIFBR Unreviewed; 917 AA. AC D4BRL3; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; ORFNames=BIFBRE_04749; OS Bifidobacterium breve DSM 20213 = JCM 1192. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=518634; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20213; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCG02000012; EFE88858.1; -; Genomic_DNA. DR ProteinModelPortal; D4BRL3; -. DR EnsemblBacteria; EFE88858; EFE88858; BIFBRE_04749. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100186 MW; C187FAE9EFA32E98 CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVQLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLAGTKA AGWFAVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVAHTPAADT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCKGAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGVDSEA LAKAKANVDN DVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID D4C489_PRORE Unreviewed; 235 AA. AC D4C489; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PROVRETT_09435; OS Providencia rettgeri DSM 1131. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Providencia. OX NCBI_TaxID=521000; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1131; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCI02000091; EFE51919.1; -; Genomic_DNA. DR ProteinModelPortal; D4C489; -. DR EnsemblBacteria; EFE51919; EFE51919; PROVRETT_09435. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 157 159 THZ-P binding (By similarity). FT REGION 209 210 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 160 160 HMP-PP (By similarity). FT BINDING 189 189 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 235 AA; 25474 MW; 7391AA4DECF078AB CRC64; MKMPKLPSAI SIPNTISIPN TISIPNSPFP ATEQRLGLYP VVDSVEWIER LLNAGVSTIQ LRIKDKPDAD VRDDIQQAIA LGKKHNARLF INDYWRLAVE LGAYGVHLGQ EDLETTDLLA IHQAGLRLGI STHDEHELAI AKSVRPSYIA MGHIFPTQTK EMPSSPQGLE TLKAMVEATP DYPTVAIGGI SIDKVPAVLA TGVGSVALVS AITKADDWRA ATETLLDLIE RNTAN // ID D4C7U8_9CLOT Unreviewed; 219 AA. AC D4C7U8; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLOM621_05467; OS Clostridium sp. M62/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411486; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M62/1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFX02000003; EFE14636.1; -; Genomic_DNA. DR ProteinModelPortal; D4C7U8; -. DR EnsemblBacteria; EFE14636; EFE14636; CLOM621_05467. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23568 MW; 9D1A1BD359E176E0 CRC64; MKFSRDEIRR AMLLYAVTDR SWLREGESLS GVCREVLKGG ATFLQIREKD LDEASFEAEA RELKELCAEY RVPFVVNDSV EIALKIQADG VHVGQSDIKG RDIRAMIGPD RILGISAGTP EEAAVAEKVG ADYIGVGAVF GTSTKKDARN LSVDALREIR NSVSIPIVAI GGIQPSNLME LAGTGVDGVA VVSAIFAAER PGEAAENLRK LAEEMVRHG // ID D4CSJ6_9FUSO Unreviewed; 205 AA. AC D4CSJ6; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=FUSPEROL_00355; OS Fusobacterium periodonticum ATCC 33693. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=546275; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33693; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJY01000028; EFE87632.1; -; Genomic_DNA. DR ProteinModelPortal; D4CSJ6; -. DR EnsemblBacteria; EFE87632; EFE87632; FUSPEROL_00355. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 205 AA; 23616 MW; 7F5A2A175EA5EB79 CRC64; MLDKIKLNII SNRKLCENEN LEKQIEKIFS AYEKKIILEN FEIVSLTLRE KDLDKNEYLN LVEKIYPICK KYKINLILHQ NYDLNLDDKY KIDGIHLSYN IFKSLNENIK AELIKKYKRI GVSIHSLEEA KDVESLGASY VIAGHIFKTD CKKGLEPRGL KFIEDLSSAL SIPIFAIGGI DEKNSQSVID RGAFSVCMMS SIMKY // ID D4CSK2_9FUSO Unreviewed; 206 AA. AC D4CSK2; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FUSPEROL_00361; OS Fusobacterium periodonticum ATCC 33693. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=546275; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33693; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJY01000028; EFE87638.1; -; Genomic_DNA. DR ProteinModelPortal; D4CSK2; -. DR EnsemblBacteria; EFE87638; EFE87638; FUSPEROL_00361. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22360 MW; CB3F2BCE00D93158 CRC64; MNLKTCKIYL VTDEKACLGK DFYACIEEAI KGGAGIVQLR EKNISTKDLY EKALKVKEIC KNYGALFIIN DRFDIAQAVG ADGVHLGQSD MPIEKAREIL KDKFLIGATA RNVEEAKKAE LLGADYIGSG AIFGTNTKDN AKKLEMEELK KIVASVKIPV FAIGGININN VGSLKNIGLQ GICAVSGILS EKDCKKAVDI MLKNFN // ID D4DIR6_TRIVH Unreviewed; 605 AA. AC D4DIR6; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 16-APR-2014, entry version 19. DE SubName: Full=Putative uncharacterized protein; DE Flags: Fragment; GN ORFNames=TRV_07077; OS Trichophyton verrucosum (strain HKI 0517). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; OC mitosporic Arthrodermataceae; Trichophyton. OX NCBI_TaxID=663202; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HKI 0517; RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7; RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S., RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., RA Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., RA Kniemeyer O., Schroeckh V., Hertweck C., Hube B., White T.C., RA Platzer M., Guthke R., Heitman J., Woestemeyer J., Zipfel P.F., RA Monod M., Brakhage A.A.; RT "Comparative and functional genomics provide insights into the RT pathogenicity of dermatophytic fungi."; RL Genome Biol. 12:R7.1-R7.16(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYE01000410; EFE38263.1; -; Genomic_DNA. DR RefSeq; XP_003018908.1; XM_003018862.1. DR GeneID; 9582065; -. DR KEGG; tve:TRV_07077; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 2. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome. FT NON_TER 1 1 SQ SEQUENCE 605 AA; 64651 MW; 625DE53111A60619 CRC64; SIRISGYIFF SQIFPPPPPF HAYIHTLDPS FRYLTGFTLL PGNILKMPVN LSLYLVTDST PKILGDRDLC SVVEQAVQGG VTIVQYRDKH SDTKELIKTA AKLHDITLNH GIPLIINDRV DVALAVGAEG VHLGQDDMSR IFLYSPSFNC VFMLMNLVDI AVARKMLPKG TIIGVTVSSV EEAQAAVESG ADYLGIGTVY ATPTEAKDSD SKTNTKSIIG TAGVKRILNC VASLNPRVGT VAIGGINLDN VQRIIYQSQD TKKGLEGVAI VSAIMAAENP RATAALFLDK VSKNPAFATI PISPRENEEE LLLGKVDGLV RKVATVHPLC HNMINYVVAN FAANVALAIG ASPIMSGYGL EAPDLAKNKG SLLINMGTLN SESLDNYMQA IRAYNEAGNP VVLDPVGAAA TQLRRQSVKT LMQGGYFDLI KGNESEIGYI YGHTGNQIGV DSGPSTLDIK EKAMLVRDLA LREILLCQQA NNLFTGCIVL LTGPTDYLSD GARTIAIHNG HPLLGQVTGT GCVIGTVTSA FLAVERQDKL LAVLSALLMF EVAAERAVVS GVKGPGSFVP ALLDELYSLK TQATESKSAS IDTLKKAAKV NFIHF // ID D4DMG1_NEIEG Unreviewed; 205 AA. AC D4DMG1; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NEIELOOT_00229; OS Neisseria elongata subsp. glycolytica ATCC 29315. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=546263; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29315; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADBF01000006; EFE50878.1; -; Genomic_DNA. DR ProteinModelPortal; D4DMG1; -. DR EnsemblBacteria; EFE50878; EFE50878; NEIELOOT_00229. DR PATRIC; 36185418; VBINeiElo48274_0199. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21904 MW; DFC9C8D6067DF233 CRC64; MTFPPLKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKTL YGDELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLRKYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AVVRAVTEAE NPEAVVKAFQ ALWDE // ID D4E0G9_SEROD Unreviewed; 212 AA. AC D4E0G9; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0758_1669; OS Serratia odorifera DSM 4582. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=667129; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 4582; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADBY01000028; EFE96694.1; -; Genomic_DNA. DR ProteinModelPortal; D4E0G9; -. DR EnsemblBacteria; EFE96694; EFE96694; HMPREF0758_1669. DR PATRIC; 36061200; VBISerOdo144996_0929. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22813 MW; 6314CB86F798C0A5 CRC64; MADITTPFPA TPHRLGLYPV VDSVVWIERL LAAGVTTIQL RIKDLPEEQV EADIATAIAL GKRYQARVFI NDYWRLAIKH RAYGVHLGQE DLDDSDLAAI HQAGLRLGVS THDDAELARA KAVKPSYIAL GHIFPTQTKD MPSAPQGLTE LKRHVAGLAD YPTVAIGGIG IDRVPAVLAC GVGSIAVVSA ITQAADWRAA TAELLRLIEG KE // ID D4ELP9_ENTFL Unreviewed; 211 AA. AC D4ELP9; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9376_01570; OS Enterococcus faecalis S613. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=699185; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S613; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADDP01000063; EFE19412.1; -; Genomic_DNA. DR ProteinModelPortal; D4ELP9; -. DR EnsemblBacteria; EFE19412; EFE19412; HMPREF9376_01570. DR PATRIC; 36331932; VBIEntFae153134_1466. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22881 MW; E4C24F8F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID D4EXG5_ENTFL Unreviewed; 211 AA. AC D4EXG5; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9377_02240; OS Enterococcus faecalis R712. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=699186; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R712; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADDQ01000062; EFE15646.1; -; Genomic_DNA. DR ProteinModelPortal; D4EXG5; -. DR EnsemblBacteria; EFE15646; EFE15646; HMPREF9377_02240. DR PATRIC; 36338973; VBIEntFae154991_1991. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22881 MW; E4C24F8F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID D4F2R0_EDWTA Unreviewed; 211 AA. AC D4F2R0; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EDWATA_01011; OS Edwardsiella tarda ATCC 23685. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Edwardsiella. OX NCBI_TaxID=500638; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23685; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGK01000045; EFE23906.1; -; Genomic_DNA. DR ProteinModelPortal; D4F2R0; -. DR EnsemblBacteria; EFE23906; EFE23906; EDWATA_01011. DR PATRIC; 36079701; VBIEdwTar109008_1006. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22798 MW; 3657C6F56CA1EFD7 CRC64; MYQPDFPPVP FRLGAYPVVD SVEWIARLLE AGVRTLQLRI KDRDDEQLEE AVKAAIELGR RYQARLFIND YWRLAIKHQA YGVHLGQEDL AATDLAAIRA AGLRLGVSTH DDMEIEVALA ARPSYIALGQ VFPTQSKQMP SAPQGIAQLA RHIQRLGDYP TVAIGGITLA RVPAVLATGV GSVAVISAIT QAADWREATA HLLALAGAGG E // ID D4FHI8_STAEP Unreviewed; 215 AA. AC D4FHI8; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0794_0026; OS Staphylococcus epidermidis M23864:W2(grey). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525375; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23864:W2; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMU01000002; EFE60137.1; -; Genomic_DNA. DR ProteinModelPortal; D4FHI8; -. DR EnsemblBacteria; EFE60137; EFE60137; HMPREF0794_0026. DR PATRIC; 36662472; VBIStaEpi43789_2313. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 24056 MW; 87DE668162513994 CRC64; MNMMFDSKQL SVYFICGTQD IPKNKSIEQV LKEALEAGIT LYQFREKGPN ALKGEKKKQL ALKLKQLCHS YHVPMIVNDD VQLAQEINAD GIHVGQDDME IQQFASQFKN KIIGLSVGNL KEYQQSDLSK VDYIGVGPMY TTSSKDDASK PVDPSMISQL RLYIHDFPIV AIGGINETNV QPIVDEGADG ISVISAITRS TNIDKTVKYF LRYFT // ID D4FKP7_STAEP Unreviewed; 160 AA. AC D4FKP7; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0794_1135; OS Staphylococcus epidermidis M23864:W2(grey). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525375; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23864:W2; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMU01000019; EFE59118.1; -; Genomic_DNA. DR ProteinModelPortal; D4FKP7; -. DR EnsemblBacteria; EFE59118; EFE59118; HMPREF0794_1135. DR PATRIC; 36659814; VBIStaEpi43789_0776. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID D4FRV4_STROR Unreviewed; 217 AA. AC D4FRV4; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF8579_0885; OS Streptococcus oralis ATCC 35037. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=655813; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35037; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMV01000012; EFE56925.1; -; Genomic_DNA. DR ProteinModelPortal; D4FRV4; -. DR EnsemblBacteria; EFE56925; EFE56925; HMPREF8579_0885. DR PATRIC; 36663293; VBIStrOra19579_0334. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23657 MW; ABB0214B4FE48A52 CRC64; MLSKETFMNR EALRLYLVTN RYQDSLENFL EKVETACRSG VTIIQLREKN LTTNQYYQLA KQVKEITDAY QVPLIIDDRL DVCLAVDAAG LHIGDDELPV SVARKVLGPE KILGVTAKTV KRALEAETSG ADYLGTGAIF PTTTKENAPI TLISTLKTIC QTVAIPVVAI GGLTSENIDQ LAETGIAGVA VVRDLMQAED IEAKTQAFLT KLDDIIS // ID D4FV40_BACNB Unreviewed; 205 AA. AC D4FV40; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Transcriptional regulator TenI; GN Name=tenI; ORFNames=BSNT_01949; OS Bacillus subtilis subsp. natto (strain BEST195). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=645657; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BEST195; RX PubMed=20398357; DOI=10.1186/1471-2164-11-243; RA Nishito Y., Osana Y., Hachiya T., Popendorf K., Toyoda A., RA Fujiyama A., Itaya M., Sakakibara Y.; RT "Whole genome assembly of a natto production strain Bacillus subtilis RT natto from very short read data."; RL BMC Genomics 11:243-243(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011541; BAI84721.1; -; Genomic_DNA. DR RefSeq; YP_005560424.1; NC_017196.1. DR ProteinModelPortal; D4FV40; -. DR EnsemblBacteria; BAI84721; BAI84721; BSNT_01949. DR GeneID; 14101818; -. DR KEGG; bso:BSNT_01949; -. DR PATRIC; 42729921; VBIBacSub97792_2138. DR KO; K10810; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 22888 MW; 725BA0A76AB25D1A CRC64; MELHAITDDS KPVEELARTI ISIQNEVDFI HIRERSKSAA DILKLLELIF EGGIDKRKLV MNGRVDIALF STIHRVQLPS GSFSPKQVRA RFPHLHIGRS VHSLEEAVQA EKEDADYVLF GHVFETDCKK GLEGRGVSLL STIKQRISIP VIAIGGMTPD RLRDVKQAGA DGIAVMSGIF SSAEPLEAAR RYSRKLKEMR YEKAL // ID D4G316_BACNB Unreviewed; 222 AA. AC D4G316; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSNT_05856; OS Bacillus subtilis subsp. natto (strain BEST195). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=645657; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BEST195; RX PubMed=20398357; DOI=10.1186/1471-2164-11-243; RA Nishito Y., Osana Y., Hachiya T., Popendorf K., Toyoda A., RA Fujiyama A., Itaya M., Sakakibara Y.; RT "Whole genome assembly of a natto production strain Bacillus subtilis RT natto from very short read data."; RL BMC Genomics 11:243-243(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011541; BAI87497.1; -; Genomic_DNA. DR RefSeq; YP_005563200.1; NC_017196.1. DR ProteinModelPortal; D4G316; -. DR EnsemblBacteria; BAI87497; BAI87497; BSNT_05856. DR GeneID; 14104036; -. DR KEGG; bso:BSNT_05856; -. DR PATRIC; 42735500; VBIBacSub97792_0715. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23740 MW; CC3E148BB2D91508 CRC64; MTRISREMMK ELLSVYFIMG SNNTKADPVT VVQKALKGGA TLYQFREKGG DALTGEARIE FAEKVQAACR EAGVPFIVND DVELALKLKA DGIHIGQEDA NAKEVRASIG DMILGVSAHT MSEVKQAEED GADYVGLGPI YPTETKKDTR AVQGVSLIEA VRRQGISIPI VGIGGITIDN AAPVIQAGAD GVSMISAISQ AEDPESAARK FREEIQTYKT GR // ID D4GH70_PANAM Unreviewed; 210 AA. AC D4GH70; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PANA_0218; OS Pantoea ananatis (strain LMG 20103). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=706191; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 20103; RX PubMed=20348253; DOI=10.1128/JB.00060-10; RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., RA Joubert F., Coutinho T.A.; RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of RT Eucalyptus blight and dieback."; RL J. Bacteriol. 192:2936-2937(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001875; ADD75385.1; -; Genomic_DNA. DR RefSeq; YP_003518513.1; NC_013956.2. DR ProteinModelPortal; D4GH70; -. DR EnsemblBacteria; ADD75385; ADD75385; PANA_0218. DR GeneID; 8894042; -. DR KEGG; pam:PANA_0218; -. DR PATRIC; 35381199; VBIPanAna151616_0231. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; PANA706191:GJNK-233-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23041 MW; 58C94673C26E3547 CRC64; MDAFPATASR LGLYPVVDSV EWIERLLEAG VRTLQLRIKD QPDEVVEPMI IRAIAAGKRY QARLFINDYW QLAIKHQAYG VHLGQEDLEV ANLQQILHAG LRLGLSTHDD AELDRALALR PSYVALGHIF PTQTKAMPSS PQGVAELKRH LARLHGISTV AIGGISIDRA PEVLATGVGS IAVVSAITQA EDWQEATRVL LRLAEPETAY // ID D4GV42_HALVD Unreviewed; 214 AA. AC D4GV42; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HVO_2668; OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC OS 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Haloferax. OX NCBI_TaxID=309800; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / RC VKM B-1768 / DS2; RX PubMed=20333302; DOI=10.1371/journal.pone.0009605; RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., RA Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M., RA Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T., RA Eisen J.A.; RT "The complete genome sequence of Haloferax volcanii DS2, a model RT archaeon."; RL PLoS ONE 5:E9605-E9605(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001956; ADE03846.1; -; Genomic_DNA. DR RefSeq; YP_003536684.1; NC_013967.1. DR ProteinModelPortal; D4GV42; -. DR EnsemblBacteria; ADE03846; ADE03846; HVO_2668. DR GeneID; 8926418; -. DR KEGG; hvo:HVO_2668; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; HVOL309800:GCOK-2672-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 21688 MW; B3B2833638BFA067 CRC64; MNTSMGTYLV TQSDRSGGRS TPDVVRAAVD GGIDVVQLRE KHASARDRYE VGRELRAVTA DAGVPLVVND RVDIAAAIDA DGVHLGDDDV PVSVAREQLG EGAIVGRSVS TVAGARAAEE AGADYLGVGA VFATDTKETN PEQSEIGTER VSAIAEAVSI PFVGIGGVTP DNAADVVAAG ADGVAVVSAI TAADDPADAT RHLADSVAAG RNRR // ID D4H5S9_DENA2 Unreviewed; 181 AA. AC D4H5S9; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Dacet_2766; OS Denitrovibrio acetiphilus (strain DSM 12809 / N2460). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Denitrovibrio. OX NCBI_TaxID=522772; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12809 / N2460; RX DOI=10.4056/sigs.892105; RA Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., RA Glavina Del Rio T., Chen F., Lucas S., Tice H., Cheng J., Han C., RA Goodwin L., Pitluck S., Liolios K., Pati A., Ivanova N., RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y., RA Jeffries C., Detter J., Brettin T., Spring S., Rohde M., Goker M., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H.; RT "Complete genome sequence of Denitrovibrio acetiphilus type strain RT (N2460)."; RL Stand. Genomic Sci. 2:270-279(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001968; ADD69520.1; -; Genomic_DNA. DR RefSeq; YP_003505476.1; NC_013943.1. DR ProteinModelPortal; D4H5S9; -. DR EnsemblBacteria; ADD69520; ADD69520; Dacet_2766. DR GeneID; 8877144; -. DR KEGG; dap:Dacet_2766; -. DR PATRIC; 35355555; VBIDenAce54242_2768. DR HOGENOM; HOG000155781; -. DR BioCyc; DACE522772:GHC2-2809-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 181 AA; 20470 MW; 0E71107C612DDBC3 CRC64; MKIMQILDYE TFGERFIDIA GQCAPYADVI WFRIKERALV DEKAGRLREA LPDTFLSLSL DAQTASKYGY DAVQLGKDSY IESVRRDFPK LRIGYSAHSM DELESKGVDY FTLSPIFFTK KNYEVKPLGT VDVSHIDSEI YALGGISSEN INRLKGKGFA GVAGISFYRE IKLLRSQCLL K // ID D4H738_DENA2 Unreviewed; 205 AA. AC D4H738; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dacet_2992; OS Denitrovibrio acetiphilus (strain DSM 12809 / N2460). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Denitrovibrio. OX NCBI_TaxID=522772; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12809 / N2460; RX DOI=10.4056/sigs.892105; RA Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., RA Glavina Del Rio T., Chen F., Lucas S., Tice H., Cheng J., Han C., RA Goodwin L., Pitluck S., Liolios K., Pati A., Ivanova N., RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y., RA Jeffries C., Detter J., Brettin T., Spring S., Rohde M., Goker M., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H.; RT "Complete genome sequence of Denitrovibrio acetiphilus type strain RT (N2460)."; RL Stand. Genomic Sci. 2:270-279(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001968; ADD69742.1; -; Genomic_DNA. DR RefSeq; YP_003505698.1; NC_013943.1. DR ProteinModelPortal; D4H738; -. DR EnsemblBacteria; ADD69742; ADD69742; Dacet_2992. DR GeneID; 8877374; -. DR KEGG; dap:Dacet_2992; -. DR PATRIC; 35356025; VBIDenAce54242_2999. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; DACE522772:GHC2-3040-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21637 MW; 685378E85DCAB051 CRC64; MIAEYLKLYL ILETSMLKMP LEQFIPAVIN GGVTSIQLRD KGATSAEMYA TGKKVMELIN GRDVLFVVND RLDIALMLGA KAVHLGVKDI PVSNVRAKYP ELILGYSCND MDDVRAAGVA DYIGSGPAFP TSTKADLRGL IGPSGIKELV AAAGKPSVAI GGITGENVDQ LSNSGVSGVA VSSAICAAED PYMAAKMLRD KLEKF // ID D4HD47_PROAS Unreviewed; 216 AA. AC D4HD47; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HMPREF0675_3944; OS Propionibacterium acnes (strain SK137). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=553199; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK137; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RT "The complete genome of Propionibacterium acnes SK137."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001977; ADE00594.1; -; Genomic_DNA. DR RefSeq; YP_003581111.1; NC_014039.1. DR ProteinModelPortal; D4HD47; -. DR EnsemblBacteria; ADE00594; ADE00594; HMPREF0675_3944. DR GeneID; 9075374; -. DR KEGG; pak:HMPREF0675_3944; -. DR PATRIC; 37226506; VBIProAcn10541_0931. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; PACN553199:GHRZ-935-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID D4HF54_PROAS Unreviewed; 217 AA. AC D4HF54; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HMPREF0675_3116; OS Propionibacterium acnes (strain SK137). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=553199; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK137; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RT "The complete genome of Propionibacterium acnes SK137."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001977; ADE01173.1; -; Genomic_DNA. DR RefSeq; YP_003580306.1; NC_014039.1. DR ProteinModelPortal; D4HF54; -. DR EnsemblBacteria; ADE01173; ADE01173; HMPREF0675_3116. DR GeneID; 9074536; -. DR KEGG; pak:HMPREF0675_3116; -. DR PATRIC; 37224848; VBIProAcn10541_0115. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; PACN553199:GHRZ-115-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID D4HUS0_ERWAC Unreviewed; 214 AA. AC D4HUS0; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EAMY_0251; OS Erwinia amylovora (strain CFBP1430). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=665029; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFBP1430; RX PubMed=20192826; DOI=10.1094/MPMI-23-4-0384; RA Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E., RA Duffy B.; RT "Complete genome sequence of the fire blight pathogen Erwinia RT amylovora CFBP 1430 and comparison to other Erwinia spp."; RL Mol. Plant Microbe Interact. 23:384-393(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN434113; CBA19193.1; -; Genomic_DNA. DR RefSeq; YP_003529609.1; NC_013961.1. DR ProteinModelPortal; D4HUS0; -. DR EnsemblBacteria; CBA19193; CBA19193; EAMY_0251. DR GeneID; 8911229; -. DR KEGG; eam:EAMY_0251; -. DR PATRIC; 35404686; VBIErwAmy142366_0276. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; EAMY665029:GCM3-271-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23235 MW; 599283DC58CED601 CRC64; MSRGAFPATA ARLGLYPVVD NVQWIARLLE AGVRTIQLRI KDRTEQEVET QVAGAIALGK RYQARLFIND YWRLAVKHQA YGVHLGQEDL NIADLDSIYA AGLRLGLSTH DDDELDRALA EKPSYIALGH VFPTRTKDMP SAPQGLEALS RYIKRLPGIS TVAIGGISLE RAPAVLATGV GSIAVVSAIT QASDWQAATR QLLALAETQR PPRA // ID D4ID70_ERWAE Unreviewed; 214 AA. AC D4ID70; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EAM_0239; OS Erwinia amylovora (strain ATCC 49946 / CCPPB 0273 / Ea273 / 27-3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=716540; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49946 / CCPPB 0273 / Ea273 / 27-3; RX PubMed=20118253; DOI=10.1128/JB.00022-10; RA Sebaihia M., Bocsanczy A.M., Biehl B.S., Quail M.A., Perna N.T., RA Glasner J.D., DeClerck G.A., Cartinhour S., Schneider D.J., RA Bentley S.D., Parkhill J., Beer S.V.; RT "Complete genome sequence of the plant pathogen Erwinia amylovora RT strain ATCC 49946."; RL J. Bacteriol. 192:2020-2021(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN666575; CBJ44914.1; -; Genomic_DNA. DR RefSeq; YP_003537340.1; NC_013971.1. DR ProteinModelPortal; D4ID70; -. DR EnsemblBacteria; CBJ44914; CBJ44914; EAM_0239. DR GeneID; 8948838; -. DR KEGG; eay:EAM_0239; -. DR PATRIC; 35411927; VBIErwAmy154257_0245. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; EAMY716540:GJAV-263-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23235 MW; 599283DC58CED601 CRC64; MSRGAFPATA ARLGLYPVVD NVQWIARLLE AGVRTIQLRI KDRTEQEVET QVAGAIALGK RYQARLFIND YWRLAVKHQA YGVHLGQEDL NIADLDSIYA AGLRLGLSTH DDDELDRALA EKPSYIALGH VFPTRTKDMP SAPQGLEALS RYIKRLPGIS TVAIGGISLE RAPAVLATGV GSIAVVSAIT QASDWQAATR QLLALAETQR PPRA // ID D4IWA2_BUTFI Unreviewed; 209 AA. AC D4IWA2; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CIY_24060; OS Butyrivibrio fibrisolvens 16/4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=657324; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=16/4; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Butyrivibrio fibrisolvens 16/4."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929036; CBK75045.1; -; Genomic_DNA. DR RefSeq; YP_007820111.1; NC_021031.1. DR ProteinModelPortal; D4IWA2; -. DR EnsemblBacteria; CBK75045; CBK75045; CIY_24060. DR GeneID; 15214916; -. DR KEGG; bfi:CIY_24060; -. DR PATRIC; 42804675; VBIButFib8520_2191. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22660 MW; 9ABF5CF3E8D7FC86 CRC64; MEFNTELYFI TDSTPYDRKE FLFRVEEALK GGVTLMQLRE KNRTTREYIE LAEAVHEISK KYNVPLIIDD RVDVMLAVDA EGVHVGAEDM PLALARKIIG PNKILGATAK TVEVAKAAYE AGADYLGVGA IYPTTTKVKT IITSTETLDK ICQAVPIPVN AIGGLNPSNM DVLAGIPIAG VCAVSAIMKA DSPMVAATEM KKKFVELRA // ID D4JB31_9FIRM Unreviewed; 193 AA. AC D4JB31; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 22-JAN-2014, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN ORFNames=CC1_29720; OS Coprococcus catus GD/7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=717962; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GD/7; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Coprococcus catus GD/7."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929038; CBK81552.1; -; Genomic_DNA. DR RefSeq; YP_007770961.1; NC_021009.1. DR ProteinModelPortal; D4JB31; -. DR EnsemblBacteria; CBK81552; CBK81552; CC1_29720. DR GeneID; 15173015; -. DR KEGG; cct:CC1_29720; -. DR PATRIC; 42887456; VBICopCat158046_2855. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 193 AA; 21380 MW; D63F3B9BA8EDB0C1 CRC64; MSSRSYAHMM AVTNRHLCDR DFLEQIEFLA STDIDAIILR EKDMTPDEYE HLAKDVLMIC HEHHKKCILH SFAEVAAKLN CENIHLPLPV LMELSEKDAL EGFKHIGTSV HSVEDALAAE KAGATCLTAG HIFDTDCKKG LPGRGLTFLE NVCHRTKLPV YAIGGITPEN LEVVRHAGAV GGCMMSLSMK IRE // ID D4JBB6_9FIRM Unreviewed; 211 AA. AC D4JBB6; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CC1_30740; OS Coprococcus catus GD/7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=717962; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GD/7; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Coprococcus catus GD/7."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929038; CBK81637.1; -; Genomic_DNA. DR RefSeq; YP_007771046.1; NC_021009.1. DR ProteinModelPortal; D4JBB6; -. DR EnsemblBacteria; CBK81637; CBK81637; CC1_30740. DR GeneID; 15173100; -. DR KEGG; cct:CC1_30740; -. DR PATRIC; 42887643; VBICopCat158046_2948. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22573 MW; 2889C37432DB4EE4 CRC64; MKCAKEDLLL YAVTDRHWLN GRTLYEVVKE SLDGGVTFLQ LREKTLDEAH FLEEAKELQK LCKEYKVPFI INDNVDIAVA MNADGVHVGQ SDMEAGDVRA KLGPDKIIGV STQTVEQAIL AEKHGADYLG VGAVFPTTSK DDAAEVSYDT LKAICEAVSI PVVAIGGITQ GNVVKLAGSG IDGVAVISAI YAQKDIKKAT ADLKEAVKAI V // ID D4JGP9_9FIRM Unreviewed; 240 AA. AC D4JGP9; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 22-JAN-2014, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN ORFNames=ERE_04330; OS Eubacterium rectale M104/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=657317; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M104/1; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Eubacterium rectale M104/1."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929043; CBK92533.1; -; Genomic_DNA. DR RefSeq; YP_007841343.1; NC_021044.1. DR ProteinModelPortal; D4JGP9; -. DR EnsemblBacteria; CBK92533; CBK92533; ERE_04330. DR GeneID; 15227157; -. DR KEGG; era:ERE_04330; -. DR PATRIC; 42987890; VBIEubRec155814_1077. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 240 AA; 26579 MW; 69F2E05B5F5A76B2 CRC64; MNKEKLLYEN SKYALQSDNI IAITNRHLCS RPFMEQLERV CKLHPHAIVL REKDMPEAEY LSLARDVIAL CKKYDVQCML HSFINVAMEL EHPYIHLPLP ILEAYVKKGL SDNISTDMSK STDNYQQFFK VIGTSVHSVE DAIKAEQLGA TYMTAGHIFA TDCKKGLPPR GLDFLKNVCD AVEIPVYAIG GINIASSDDS TASNAPSTYD AMPDINVPRL ADVMECGAAG GCIMSGMMRV // ID D4JM26_9FIRM Unreviewed; 216 AA. AC D4JM26; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ERE_08030; OS Eubacterium rectale M104/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=657317; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M104/1; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Eubacterium rectale M104/1."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929043; CBK92861.1; -; Genomic_DNA. DR RefSeq; YP_007841671.1; NC_021044.1. DR ProteinModelPortal; D4JM26; -. DR EnsemblBacteria; CBK92861; CBK92861; ERE_08030. DR GeneID; 15227485; -. DR KEGG; era:ERE_08030; -. DR PATRIC; 42988614; VBIEubRec155814_1462. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23069 MW; 457390AFA22F1694 CRC64; MNKTDLKLYA ITDRQWLHGA RLSEHVKLAI EGGATMIQIR DKDILSTDSD AGLKDEYNEA LEIKRICHEH KVPLIINDNV QFAIDIDADG VHLGQDDMNP AEARKLLGTD KIIGVTAKTV EQAKKAEADG ADYLGSGAVF GSTTKLNAKP MTKELLREIT EAVDIPVVAI GGINADNAVT LKGTGIAGIA VVGAIFASAD IRAAARELAE ICDKIL // ID D4JUJ8_9FIRM Unreviewed; 217 AA. AC D4JUJ8; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUS_16690; OS Eubacterium siraeum 70/3. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=657319; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=70/3; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Eubacterium siraeum 70/3."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929044; CBK96767.1; -; Genomic_DNA. DR RefSeq; YP_007775669.1; NC_021011.1. DR ProteinModelPortal; D4JUJ8; -. DR EnsemblBacteria; CBK96767; CBK96767; EUS_16690. DR GeneID; 15177828; -. DR KEGG; esu:EUS_16690; -. DR PATRIC; 42997303; VBIEubSir135646_1984. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23254 MW; 0C5080A7F46955BA CRC64; MNITPKQMLL YAVSDRAWSN SDEEFLSQAK QAIKSGITIF QLREKHTEYE HFREIALKLK PICKQYNVPL IINDNVKLAK EIDADGVHLG QDDLDIKAAR EYLGADKIIG VSAHNVKEAL EAENGGADYL GSGAAFVTST KTDAGAIDHK VLSDVAHSVK IPVVAIGGIN KDNISQLEGL GLDGVAVVSA IFAADDISSA VIDLKAKAEK VAESSVK // ID D4K0Y4_9FIRM Unreviewed; 217 AA. AC D4K0Y4; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FP2_26250; OS Faecalibacterium prausnitzii L2-6. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=718252; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2/6; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Faecalibacterium prausnitzii L2/6."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929045; CBK99933.1; -; Genomic_DNA. DR RefSeq; YP_007838217.1; NC_021042.1. DR ProteinModelPortal; D4K0Y4; -. DR EnsemblBacteria; CBK99933; CBK99933; FP2_26250. DR GeneID; 15243665; -. DR KEGG; fpr:FP2_26250; -. DR PATRIC; 43010005; VBIFaePra154692_0815. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23239 MW; C73EFCFD64F0858F CRC64; MKCDKHTMLL YAVTDRAWTG RETLRQQVED ALKGGVTCVQ LREKELDDAA FLQEAMELSA LCRSYGVPFI INDNVEIAIK CHADGIHVGQ EDMAAADVRA KVGPDMIIGV SAHSVEEAQL AVAHGADYLG VGAAFSTHTK TDVDVLPEGR LKEICDSVDV PVVAIGGIHK DNILKLKGSG ADGVALVSAI FSAEDIEAEC KELKALAEQI IYSNSTF // ID D4K813_9FIRM Unreviewed; 212 AA. AC D4K813; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FPR_05870; OS Faecalibacterium prausnitzii SL3/3. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=657322; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SL3/3; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Faecalibacterium prausnitzii SL3/3."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929046; CBL00976.1; -; Genomic_DNA. DR RefSeq; YP_007799369.1; NC_021020.1. DR ProteinModelPortal; D4K813; -. DR EnsemblBacteria; CBL00976; CBL00976; FPR_05870. DR GeneID; 15199168; -. DR KEGG; fpa:FPR_05870; -. DR PATRIC; 43012394; VBIFaePra148460_0268. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22788 MW; CA8598C89546D27A CRC64; MKCDKHTMLL YAVTDRAWVG EQTLYQQVES ALKGGATCVQ LREKQLGDAD FLQEAIQIHA LCQQYGVPLF INDNVEVALQ CHAEGIHVGQ DDMAAAQVRQ RVGDGVMIGV SAHTVQEALD AVAHGADYLG VGAVFATHTK TDVSEMPRQT LLDICNAVDV PVVAIGGIHK ENILQLKGTG VDGVALVSAI FAAKDIEAEC RELRALSEQI IK // ID D4KEK8_9FIRM Unreviewed; 216 AA. AC D4KEK8; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MHY_21370; OS Megamonas hypermegale ART12/1. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megamonas. OX NCBI_TaxID=657316; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ART12/1; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Megamonas hypermegale ART12/1."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929048; CBL06805.1; -; Genomic_DNA. DR RefSeq; YP_007835442.1; NC_021041.1. DR ProteinModelPortal; D4KEK8; -. DR EnsemblBacteria; CBL06805; CBL06805; MHY_21370. DR GeneID; 15223912; -. DR KEGG; mhg:MHY_21370; -. DR PATRIC; 43125088; VBIMegHyp147215_2024. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23881 MW; 9848DC3237157462 CRC64; MRKGMEHFIN NPIYTITAEA MSNGRNNIEV VGKMLKAGIK FIQYREKEKP ALERYQECMQ LVKMTKEAGA IFIIDDFVDL AMAVNADGVH IGQTDLPPQV VRQLIGEDKI LGLSTHEEAQ LQKANELGDI IDYIGVGPVY ATQTKKDAVP VGFSYVDYAS KYAKHPFVAI GGIKEHNICE VASHGAKTFA IVSEIVSADD IVNKIKSIEK TLQNKL // ID D4KNT2_9FIRM Unreviewed; 212 AA. AC D4KNT2; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ROI_13870; OS Roseburia intestinalis M50/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=657315; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M50/1; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Roseburia intestinalis M50/1."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929049; CBL08534.1; -; Genomic_DNA. DR RefSeq; YP_007831575.1; NC_021040.1. DR ProteinModelPortal; D4KNT2; -. DR EnsemblBacteria; CBL08534; CBL08534; ROI_13870. DR GeneID; 15219988; -. DR KEGG; rim:ROI_13870; -. DR PATRIC; 43141135; VBIRosInt153491_2470. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23258 MW; 3DBDC4E387FB1C15 CRC64; MRFDRKQLLL YGVTDRSWLN GQTLYEQVRQ ALEGGVSFLQ LREKNLSEQA FLEEAKEIQK LCREYKVPFI INDNVDLALE IDADGVHVGQ DDMEAGEVRK RLGEDKIIGV SAHSVEEALR AEKCGATYLG SGAVFGSGTK KDVGTLDHEV LKEICAAVQI PVVAIGGISR DNILQLKGTG IDGVAVISAI FAQKDIRAAA QELRKLSEEV CR // ID D4KRE9_9FIRM Unreviewed; 214 AA. AC D4KRE9; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 22-JAN-2014, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN ORFNames=ROI_24880; OS Roseburia intestinalis M50/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=657315; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M50/1; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Roseburia intestinalis M50/1."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929049; CBL09451.1; -; Genomic_DNA. DR RefSeq; YP_007832492.1; NC_021040.1. DR ProteinModelPortal; D4KRE9; -. DR EnsemblBacteria; CBL09451; CBL09451; ROI_24880. DR GeneID; 15220905; -. DR KEGG; rim:ROI_24880; -. DR PATRIC; 43143286; VBIRosInt153491_3615. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 214 AA; 23826 MW; 8540E76FB974DA77 CRC64; MCKKENPIPG KIIAVTNRSL CERPFLEQIK RVCETKPAAL ILREKDLPET EYEEMARQVL AICEEYGVIC ILHSYIETAK RLERQYVHLP LPLLRTCMQK TENEEKQIKF MSGNLSMDQK NKNKLILGCS VHSVEDAIEA EKLGASYLTA GHIFATDCKR GLPPRGMEFL KQVCETVNIP VYAIGGIGLN DGKIDSVCEC GAAGACIMSA FMAI // ID D4KUK4_9FIRM Unreviewed; 212 AA. AC D4KUK4; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RO1_02400; OS Roseburia intestinalis XB6B4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=718255; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XB6B4; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Bernalier A.; RT "The genome sequence of Roseburia intestinalis XB6B4."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929050; CBL11044.1; -; Genomic_DNA. DR RefSeq; YP_007776821.1; NC_021012.1. DR ProteinModelPortal; D4KUK4; -. DR EnsemblBacteria; CBL11044; CBL11044; RO1_02400. DR GeneID; 15179033; -. DR KEGG; rix:RO1_02400; -. DR PATRIC; 43146936; VBIRosInt152332_0155. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23258 MW; 92482B1987E117C3 CRC64; MRFDRKQLLL YGVTDRSWLN GQTLYEQVRK ALEGGVSFLQ LREKNLSEQA FLEEAKEIQK LCREYKVPFI INDNVDLALE IDADGVHVGQ DDMEAGEVRK RLGEDKIIGV SAHSVEEALR AEKCGATYLG SGAVFGSGTK KDVGTLDHEV LKEICAAVQI PVVAIGGISR DNILQLKGTG IDGVAVISAI FAQKDIRAAA QELRKLSEEV CR // ID D4KX11_9FIRM Unreviewed; 214 AA. AC D4KX11; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 22-JAN-2014, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN ORFNames=RO1_12680; OS Roseburia intestinalis XB6B4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=718255; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XB6B4; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Bernalier A.; RT "The genome sequence of Roseburia intestinalis XB6B4."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929050; CBL11901.1; -; Genomic_DNA. DR RefSeq; YP_007777678.1; NC_021012.1. DR ProteinModelPortal; D4KX11; -. DR EnsemblBacteria; CBL11901; CBL11901; RO1_12680. DR GeneID; 15179890; -. DR KEGG; rix:RO1_12680; -. DR PATRIC; 43148905; VBIRosInt152332_2465. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 214 AA; 23826 MW; 8540E76FB974DA77 CRC64; MCKKENPIPG KIIAVTNRSL CERPFLEQIK RVCETKPAAL ILREKDLPET EYEEMARQVL AICEEYGVIC ILHSYIETAK RLERQYVHLP LPLLRTCMQK TENEEKQIKF MSGNLSMDQK NKNKLILGCS VHSVEDAIEA EKLGASYLTA GHIFATDCKR GLPPRGMEFL KQVCETVNIP VYAIGGIGLN DGKIDSVCEC GAAGACIMSA FMAI // ID D4L4X0_9FIRM Unreviewed; 214 AA. AC D4L4X0; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RBR_02320; OS Ruminococcus bromii L2-63. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=657321; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-63; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Ruminococcus bromii L2-63."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929051; CBL14665.1; -; Genomic_DNA. DR RefSeq; YP_007780442.1; NC_021013.1. DR ProteinModelPortal; D4L4X0; -. DR EnsemblBacteria; CBL14665; CBL14665; RBR_02320. DR GeneID; 15182724; -. DR KEGG; rbr:RBR_02320; -. DR PATRIC; 43155162; VBIRumBro49525_1141. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23074 MW; 1CDEFDE03A83A27A CRC64; MNCDKKDLLL YAVTDRAWLN GETLCSQVEK AIKGGATFIQ LREKNLDQKH FLEEALEIQK LCKKYNVPFV INDNVEIAKK IDADGVHVGQ SDMEAGNVRK ILGDDKIIGV SAQTVEQALL AQKHGADYLG VGAVFKTGSK DDADDVSHDE LQKICEAVDI PVIAIGGISS KNVTELKGRG IVGIAVISAI FAQPDITKAT AELKALTEKT VAND // ID D4LD34_RUMC1 Unreviewed; 216 AA. AC D4LD34; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=RUM_14190; OS Ruminococcus champanellensis (strain DSM 18848 / JCM 17042 / 18P13). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=213810; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18848 / JCM 17042 / 18P13; RA Pajon A., Turner K., Parkhill J., Bernalier A.; RT "The genome sequence of Ruminococcus sp. 18P13."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929052; CBL17529.1; -; Genomic_DNA. DR RefSeq; YP_007829537.1; NC_021039.1. DR ProteinModelPortal; D4LD34; -. DR EnsemblBacteria; CBL17529; CBL17529; RUM_14190. DR GeneID; 15240532; -. DR KEGG; rch:RUM_14190; -. DR PATRIC; 43169139; VBIRumSp55702_1316. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23305 MW; 908AC3387563A583 CRC64; MKFDPTLYLV TDSSLYEEDA FLSVIDGVCS AGITLLQLRE KERSTREYLR LARVVRQITD RYGIPLILDD RADVAAACGC AGVHVGQEDL PVEDARRILG ADKIVGATAK TLEQARIAYA QGADYLGCGA VYPTTTKVRT VLTPVETIRQ ICESVPIPVN AIGGLNRGNL EILRGVPIRG VCVVSAIMKA ADPALETRLL KEAVRTLLED APCAAH // ID D4LKV6_9FIRM Unreviewed; 213 AA. AC D4LKV6; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CK1_25280; OS Ruminococcus sp. SR1/5. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=657323; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SR1/5; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Ruminococcus sp. SR1/5."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929053; CBL20467.1; -; Genomic_DNA. DR RefSeq; YP_007784130.1; NC_021014.1. DR ProteinModelPortal; D4LKV6; -. DR EnsemblBacteria; CBL20467; CBL20467; CK1_25280. DR GeneID; 15186454; -. DR KEGG; rum:CK1_25280; -. DR PATRIC; 43176042; VBIRumSp156992_2138. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22637 MW; 09E74F0DCF7B6090 CRC64; MDRKDLDVTL YLVTDSSYHT EESLLRTVEE ACKGGVTLVQ LREKNKGGRE YLDKAFKVKE ITDRYNVPLI IDDRVDVALA CDAAGVHVGA SDIPVAVARK LMGPDKIVGA TAKTVEAAVK AYEDGADYLG VGAIYPTTTK VVTILTKVST LKDICEAVPI PAVAIGGLNA GNMDVLEGAG MSGMAVVSAI MKAEDPKKNA RELKEKIVAL MGK // ID D4LQS7_9FIRM Unreviewed; 211 AA. AC D4LQS7; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CK5_17320; OS Ruminococcus obeum A2-162. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=657314; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A2-162; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Ruminococcus obeum A2-162."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929054; CBL23135.1; -; Genomic_DNA. DR RefSeq; YP_007805117.1; NC_021022.1. DR ProteinModelPortal; D4LQS7; -. DR EnsemblBacteria; CBL23135; CBL23135; CK5_17320. DR GeneID; 15205038; -. DR KEGG; rob:CK5_17320; -. DR PATRIC; 43162514; VBIRumObe156199_1588. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22277 MW; 686F27955786E593 CRC64; MKINARQLNL YAVTDRSWLE PGETLVTVTE ELLKAGVTCV QLREKHMSDE EILKEASLLK DLCDRYQVPL IINDRPDLAK KVGASGVHVG LSDMGIQKAR KLLGEDFIIG GSAHNVEEAL AAEAAGADYL GCGAVFGSTT KTNVTQLPVE TLKAICKAVK IPVVAIGGVN SDNLPLLAGS GIAGAAVVSG LFKPTDKAAA VRRFLSQLKA I // ID D4LWA5_9FIRM Unreviewed; 197 AA. AC D4LWA5; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN ORFNames=CK5_02850; OS Ruminococcus obeum A2-162. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=657314; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A2-162; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Ruminococcus obeum A2-162."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929054; CBL21908.1; -; Genomic_DNA. DR RefSeq; YP_007803890.1; NC_021022.1. DR ProteinModelPortal; D4LWA5; -. DR EnsemblBacteria; CBL21908; CBL21908; CK5_02850. DR GeneID; 15203811; -. DR KEGG; rob:CK5_02850; -. DR PATRIC; 43159692; VBIRumObe156199_0994. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 197 AA; 22337 MW; D0A2A5A083B25B9D CRC64; MIISMYKEYE HTIVITNRAL VQGDFFEQMQ KVICLHPHAV ILREKDLVDE EYKMLAEKVL DMCREEDVNC FLHSRISIAK SLGCGRIHLS IPVLESMKEE ERRNLRKDFQ EISVSCHSME DMKAAVKNGA THIILGTIFE TECKKGLRGK GLEFVREICK ACPVPVYAIG GINMERLPHV MDAGAAGGCR MSGFMKM // ID D4LYZ2_9FIRM Unreviewed; 198 AA. AC D4LYZ2; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN ORFNames=RTO_25310; OS Ruminococcus torques L2-14. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=657313; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-14; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Ruminococcus torques L2-14."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929055; CBL27002.1; -; Genomic_DNA. DR RefSeq; YP_007787510.1; NC_021015.1. DR ProteinModelPortal; D4LYZ2; -. DR EnsemblBacteria; CBL27002; CBL27002; RTO_25310. DR GeneID; 15189888; -. DR KEGG; rto:RTO_25310; -. DR PATRIC; 43183912; VBIRumTor148568_2413. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 198 AA; 22472 MW; 822BC7272D973503 CRC64; MCKMKCDLSE IDLKIIAVSN RKLCERPFLE QIERVCQMKP QAIILREKDM SEEEYRILSE EVLSVCKKYE IPCILHKFWK TALELECTSV HLPLPELRKL PEGVKEQFQR IGTSVHSVED AKEAERLGVS YMTAGHIYVT DCKKGLAPRG LGFLKDVCST VNVPVYAIGG IKFDEKQWEE LKQNGASGGC IMSGMMEL // ID D4M0X0_9FIRM Unreviewed; 215 AA. AC D4M0X0; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RTO_00770; OS Ruminococcus torques L2-14. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=657313; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-14; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Ruminococcus torques L2-14."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929055; CBL24882.1; -; Genomic_DNA. DR RefSeq; YP_007785390.1; NC_021015.1. DR ProteinModelPortal; D4M0X0; -. DR EnsemblBacteria; CBL24882; CBL24882; RTO_00770. DR GeneID; 15190554; -. DR KEGG; rto:RTO_00770; -. DR PATRIC; 43179076; VBIRumTor148568_0856. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23689 MW; 1CC51081E90FA013 CRC64; MSFTKEQLRE QMLLYAVTDR HWLKGQTLYE QVEEALKGGA TFIQLREKDL TEEEFLEEAK KIQQLCKKYR VPFIINDNVK LAKEIDADGV HVGQSDMEAL DVRAQLGEDK IIGVSARTVE QALLAEKHGA DYLGVGAVFQ TGTKTDAREV EHSVLKEICT KVDIPVVAIG GITQDNVKEL SGSGINGVAV ISAIFAQKDI ETATAKLKSC VEQIV // ID D4MDF1_9ENTE Unreviewed; 211 AA. AC D4MDF1; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ENT_19410; OS Enterococcus sp. 7L76. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=657310; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7L76; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Bernalier A.; RT "The genome sequence of Enterococcus sp. 7L76."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929058; CBL32345.1; -; Genomic_DNA. DR RefSeq; YP_007808206.1; NC_021023.1. DR ProteinModelPortal; D4MDF1; -. DR EnsemblBacteria; CBL32345; CBL32345; ENT_19410. DR GeneID; 15208183; -. DR KEGG; ene:ENT_19410; -. DR PATRIC; 42934348; VBIEntSp14464_1085. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22863 MW; E0820B8F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIILAE QITEKVQGLM RVTERMLEAR K // ID D4MMV2_9FIRM Unreviewed; 217 AA. AC D4MMV2; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ES1_22410; OS Eubacterium siraeum V10Sc8a. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=717961; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=V10Sc8a; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Eubacterium siraeum V10Sc8a."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929059; CBL35085.1; -; Genomic_DNA. DR RefSeq; YP_007840614.1; NC_021043.1. DR ProteinModelPortal; D4MMV2; -. DR EnsemblBacteria; CBL35085; CBL35085; ES1_22410. DR GeneID; 15226383; -. DR KEGG; esr:ES1_22410; -. DR PATRIC; 43003838; VBIEubSir152769_2377. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23158 MW; 7ABF56288F8D010D CRC64; MNITPKQMLL YAVSDRAWSN SDEEFLSQAK QAIKSGVTIF QLREKHTSYE HFREIALKLK PICKQYNVPL IINDNVKLAK EIDADGVHLG QDDLDIKAAR EYLGADKIIG VSAHNVKEAL EAENGGADYL GSGAAFVTST KTDAGAIDHK VLSDVAHSVK IPVVAIGGIN KDNISQLEGL GLDGVAVVSA IFAADDISSA VIDLKAKAEK AAESSSK // ID D4MP75_9FIRM Unreviewed; 208 AA. AC D4MP75; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CL3_02560; OS butyrate-producing bacterium SM4/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=245012; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SM4/1; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Clostridiales sp. SM4/1."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929060; CBL35561.1; -; Genomic_DNA. DR ProteinModelPortal; D4MP75; -. DR EnsemblBacteria; CBL35561; CBL35561; CL3_02560. DR KEGG; bprm:CL3_02560; -. DR PATRIC; 42781821; VBIButBac39087_2013. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22121 MW; 464DA7F7D09B94A1 CRC64; MLLYAVTDRS WLREGESLSG VCREVLKGGA TFLQIREKDL DEASFEAEAR ELKELCAEYR VPFVVNDSVE IALKIQADGV HVGQSDIKGR DIRAMIGPDR ILGISAGTPE EAAAAEKAGA DYIGVGAVFG TSTKKDARNL SVDALREIRN SVSIPIVAIG GIQPSNLMEL AGTGVDGVAV VSAIFAAERP GEAAENLRKL AEEMVRHG // ID D4MZM6_9FIRM Unreviewed; 223 AA. AC D4MZM6; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CL2_10760; OS butyrate-producing bacterium SSC/2. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=245018; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SSC/2; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Clostridiales sp. SSC/2."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929061; CBL38071.1; -; Genomic_DNA. DR RefSeq; YP_007789066.1; NC_021016.1. DR ProteinModelPortal; D4MZM6; -. DR EnsemblBacteria; CBL38071; CBL38071; CL2_10760. DR GeneID; 15231162; -. DR KEGG; bprl:CL2_10760; -. DR PATRIC; 42796010; VBIButBac135163_1316. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24481 MW; 2DFEAAB7FCF49305 CRC64; MQNGWKGAVK LRVNADAMTL YAVTDRTWVK DTTLMDQVKE ALEGGITFLQ LREKHLSKEE FIKEAREMKE LSKEYKVPFV INDNIEVALA VDADGVHIGQ DDMSVEEARK LLGEDKIIGV SAHNVEEAIK AQKGGADYLG VGAVCATSTK KDANVVSKEE IKKICHTVEI PVVAIGGIKK ENIKTLEGTD VDGVAVVSAI FAAKDIKKDT KQLRSLVEEM KQK // ID D4N1F0_9FIRM Unreviewed; 185 AA. AC D4N1F0; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 22-JAN-2014, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN ORFNames=CL2_17850; OS butyrate-producing bacterium SSC/2. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=245018; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SSC/2; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Clostridiales sp. SSC/2."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929061; CBL38695.1; -; Genomic_DNA. DR RefSeq; YP_007789690.1; NC_021016.1. DR ProteinModelPortal; D4N1F0; -. DR EnsemblBacteria; CBL38695; CBL38695; CL2_17850. DR GeneID; 15231786; -. DR KEGG; bprl:CL2_17850; -. DR PATRIC; 42797350; VBIButBac135163_2075. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 185 AA; 20647 MW; 1D5C6D2212CD670D CRC64; MNKPCFIAVT NRNLCKRPFF DVIEDLSKKD VKTIVLREKD LSEEEYYEIA EKCKEICDRN GASLTIHNFI DVARRLGIKK IHLPYPVFLK EAGNLSDFES VSTSIHKPEE AIKAQKLGVD FVFAGHVFVT DCKKGLPPRG LEFLTDVVNA VKIPVYGIGG INEENITKIM ECGAAGGCMM SGFMK // ID D4PNG6_LISMN Unreviewed; 214 AA. AC D4PNG6; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMBG_02156; OS Listeria monocytogenes FSL J1-194. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393117; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL J1-194; RG The Broad Institute Genome Sequencing Platform; RA Borowsky M., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Wiedmann M., RA Swaminathan B., Lauer P., Portnoy D., Cossart P., Buchrieser C., RA Higgins D., Lander E., Galagan J., Nusbaum C., Birren B.; RT "The genome sequence of Listeria monocytogenes strain FSL J1-194."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AARJ02000007; EFG02638.1; -; Genomic_DNA. DR ProteinModelPortal; D4PNG6; -. DR EnsemblBacteria; EFG02638; EFG02638; LMBG_02156. DR PATRIC; 27495145; VBILisMon90678_2152. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22625 MW; 9AC5E8FD16A53B4D CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCTKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAE EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GYPS // ID D4PY18_LISMN Unreviewed; 214 AA. AC D4PY18; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMPG_02495; OS Listeria monocytogenes J2818. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393131; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J2818; RG The Broad Institute Genome Sequencing Platform; RA Borowsky M., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Wiedmann M., RA Swaminathan B., Lauer P., Portnoy D., Cossart P., Buchrieser C., RA Higgins D., Lander E., Galagan J., Nusbaum C., Birren B.; RT "The genome sequence of Listeria monocytogenes strain J2818."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AARX02000005; EFF99894.1; -; Genomic_DNA. DR ProteinModelPortal; D4PY18; -. DR EnsemblBacteria; EFF99894; EFF99894; LMPG_02495. DR PATRIC; 30229587; VBILisMon8847_2434. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22392 MW; 67844F688FC140A4 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALKCQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAA EAELLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GITIPIVGIG GINETNLAEV LTAGADGVSV ISAITQSDDC HSVIKQLKNP GSPS // ID D4Q4U2_LISMN Unreviewed; 208 AA. AC D4Q4U2; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMSG_03074; OS Listeria monocytogenes HPB2262. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=401650; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HPB2262; RA Aureli P.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HPB2262; RG The Broad Institute Genome Sequencing Platform; RA Borowsky M., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Wiedmann M., RA Swaminathan B., Lauer P., Portnoy D., Cossart P., Buchrieser C., RA Higgins D., Lander E., Galagan J., Nusbaum C., Birren B.; RT "The genome sequence of Listeria monocytogenes strain HPB2262."; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HPB2262; RG The Broad Institute Genome Sequencing Platform; RA Borowsky M., Young S., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A.M., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., RA Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C., RA Borodovsky M., Wiedmann M., Swaminathan B., Lauer P., Portnoy D., RA Cossart P., Buchrieser C., Higgins D., Galagan J., Nusbaum C., RA Birren B.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATL02000009; EFF96133.1; -; Genomic_DNA. DR ProteinModelPortal; D4Q4U2; -. DR EnsemblBacteria; EFF96133; EFF96133; LMSG_03074. DR PATRIC; 30215896; VBILisMon51148_1764. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21913 MW; 91665D070EBAFD9D CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAE EAERLGAVDY IGVGPIFPTI SKADAEPVSG TTILKEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC QLVIANLI // ID D4RYU8_9FIRM Unreviewed; 208 AA. AC D4RYU8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BUTYVIB_01012; OS Butyrivibrio crossotus DSM 2876. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=511680; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2876; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWN01000023; EFF68922.1; -; Genomic_DNA. DR ProteinModelPortal; D4RYU8; -. DR EnsemblBacteria; EFF68922; EFF68922; BUTYVIB_01012. DR PATRIC; 30454083; VBIButCro39456_0951. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22567 MW; F92C55BFE0B82982 CRC64; MNRNNLLLYL ITDREAAGGR NLCECVKAAL DGGVTMVQLR EKNMEYEELK KEAFEIKKLC HEYKVPFIIN DNVRLALETD ADGVHLGQSD MGIEEARRIL GKNKIIGATA KTVEQAKAAM EQGADYLGSG AVFGSSTKKD AVTMSFDMLK NICRSVAIPV VAIGGINLSN VSKLAKTGIK GVAVISGILT ETDICGTSEK FRRILKNI // ID D4S7U6_9FIRM Unreviewed; 228 AA. AC D4S7U6; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiEC; Synonyms=thiE; ORFNames=HMPREF7545_1611; OS Selenomonas noxia ATCC 43541. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=585503; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43541; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKT01000034; EFF65646.1; -; Genomic_DNA. DR ProteinModelPortal; D4S7U6; -. DR EnsemblBacteria; EFF65646; EFF65646; HMPREF7545_1611. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 206 207 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 186 186 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 24311 MW; 8B88CA152C6160B7 CRC64; MRHQFDLSSY LVIGPENTNG RPVAHIIAEA LRAGFTFAQI RAKHAEAAEI IRLARAAADA IAGQKKSDEV ALVINDRLDV VLAARELRIK VDGVHVGQED IPPAVCRKYL GVNAVIGLSA RTSDLINYVE SCDTSCIDYF GAGPLHATAT KPDAGMDQNG KIVTRSLDEL RALHRVSPLP VVVGGGVKAD DLPALRATGV DGFFVVSAVA GAEHPYTAAK ELVRCWHS // ID D4SYN3_9XANT Unreviewed; 233 AA. AC D4SYN3; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-MAR-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=XAUB_32100; OS Xanthomonas fuscans subsp. aurantifolii str. ICPB 11122. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=427081; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ICPB 11122; RX PubMed=20388224; DOI=10.1186/1471-2164-11-238; RA Moreira L.M., Almeida N.F.Jr., Potnis N., Digiampietri L.A., Adi S.S., RA Bortolossi J.C., da Silva A.C., da Silva A.M., de Moraes F.E., RA de Oliveira J.C., de Souza R.F., Fancincani A.P., Ferraz A.L., RA Ferro M.I., Furlan L.R., Gimenez D.F., Jones J.B., Kitajima E.W., RA Laia M.L., Leite R.P.Jr., Nishiyama M.Y., Rodrigues Neto J., RA Nociti L.A., Norman D.J., Ostroski E.H., Pereira H.A.Jr., RA Staskawicz B.J., Tezza R.I., Ferro J.A., Vinatzer B.A., Setubal J.C.; RT "Novel insights into the genomic basis of citrus canker based on the RT genome sequences of two strains of Xanthomonas fuscans subsp. RT aurantifolii."; RL BMC Genomics 11:238-238(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACPX01000211; EFF42713.1; -; Genomic_DNA. DR ProteinModelPortal; D4SYN3; -. DR EnsemblBacteria; EFF42713; EFF42713; XAUB_32100. DR PATRIC; 35675114; VBIXanFus92710_3438. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 66 70 HMP-PP binding (By similarity). FT REGION 164 166 THZ-P binding (By similarity). FT REGION 213 214 THZ-P binding (By similarity). FT METAL 99 99 Magnesium (By similarity). FT METAL 118 118 Magnesium (By similarity). FT BINDING 98 98 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 167 167 HMP-PP (By similarity). FT BINDING 193 193 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 24216 MW; 1097CEFCC0921D95 CRC64; MSRSSDNRGH ATVGLHCPIP STAFGSVAMP NRLNVRGVYL ITPDEPNTQR LLLRTAPLLG SITWLQYRNK QADAALRLRQ ASALREACVA HGVPLIINDD AQLAAQVGAQ GVHLGEDDGD VAAARALLGR QAIIGVSCYD DIERARAAAK AGASYVAFGA FFPTTTKQTT RRATPALLQQ AAGLDLPRVA IGGIAPAQVP ALASAGADLI AVVSGVYAAP DPVAAVQAYR DGF // ID D4T0D0_9XANT Unreviewed; 315 AA. AC D4T0D0; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-MAR-2014, entry version 22. DE SubName: Full=Uncharacterized protein; GN ORFNames=XAUB_39370; OS Xanthomonas fuscans subsp. aurantifolii str. ICPB 11122. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=427081; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ICPB 11122; RX PubMed=20388224; DOI=10.1186/1471-2164-11-238; RA Moreira L.M., Almeida N.F.Jr., Potnis N., Digiampietri L.A., Adi S.S., RA Bortolossi J.C., da Silva A.C., da Silva A.M., de Moraes F.E., RA de Oliveira J.C., de Souza R.F., Fancincani A.P., Ferraz A.L., RA Ferro M.I., Furlan L.R., Gimenez D.F., Jones J.B., Kitajima E.W., RA Laia M.L., Leite R.P.Jr., Nishiyama M.Y., Rodrigues Neto J., RA Nociti L.A., Norman D.J., Ostroski E.H., Pereira H.A.Jr., RA Staskawicz B.J., Tezza R.I., Ferro J.A., Vinatzer B.A., Setubal J.C.; RT "Novel insights into the genomic basis of citrus canker based on the RT genome sequences of two strains of Xanthomonas fuscans subsp. RT aurantifolii."; RL BMC Genomics 11:238-238(2010). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACPX01000217; EFF42241.1; -; Genomic_DNA. DR ProteinModelPortal; D4T0D0; -. DR EnsemblBacteria; EFF42241; EFF42241; XAUB_39370. DR PATRIC; 35676491; VBIXanFus92710_4119. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34856 MW; 1AB8D2D6F86E4455 CRC64; MPDSLRSIHV VAGVITDPRG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIEAQVGD WVMDVPQLYP DKRLRLEVRR ITSWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGAL RQPDRYLITP EPEDDARWLE GLELALHNGI TRIQLRARQL APARWQALLQ QAMRLRGRAR AQLLLNRDIA QAADLGIGVH LGSEQLAGLQ ERPLPAEQLV AASCHGLDDL RHAQRIGCDF AVLGPVQATA SHPGATPIGW DGFETLREQV SLPIYALGGM QIEDVRKARS HGGQGIAAIR ALWPQ // ID D4T7W5_9XANT Unreviewed; 315 AA. AC D4T7W5; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-MAR-2014, entry version 22. DE SubName: Full=Uncharacterized protein; GN ORFNames=XAUC_24230; OS Xanthomonas fuscans subsp. aurantifolii str. ICPB 10535. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=427082; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ICPB 10535; RX PubMed=20388224; DOI=10.1186/1471-2164-11-238; RA Moreira L.M., Almeida N.F.Jr., Potnis N., Digiampietri L.A., Adi S.S., RA Bortolossi J.C., da Silva A.C., da Silva A.M., de Moraes F.E., RA de Oliveira J.C., de Souza R.F., Fancincani A.P., Ferraz A.L., RA Ferro M.I., Furlan L.R., Gimenez D.F., Jones J.B., Kitajima E.W., RA Laia M.L., Leite R.P.Jr., Nishiyama M.Y., Rodrigues Neto J., RA Nociti L.A., Norman D.J., Ostroski E.H., Pereira H.A.Jr., RA Staskawicz B.J., Tezza R.I., Ferro J.A., Vinatzer B.A., Setubal J.C.; RT "Novel insights into the genomic basis of citrus canker based on the RT genome sequences of two strains of Xanthomonas fuscans subsp. RT aurantifolii."; RL BMC Genomics 11:238-238(2010). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACPY01000217; EFF47205.1; -; Genomic_DNA. DR ProteinModelPortal; D4T7W5; -. DR EnsemblBacteria; EFF47205; EFF47205; XAUC_24230. DR PATRIC; 35682803; VBIXanFus21887_2710. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34837 MW; 4A3FB60A1F031280 CRC64; MPDSLRSIHV VAGVITDPRG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIEAQVGD WVMDVPQLYP DKRLRLEVRH ITSWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGAL RQPDRYLITP EPEDDARWLE GLELALHNGI TRIQLRARQL APARWQALLQ QAMRLRGRAR AQLLLNRDIA QAADLGIGVH LGSEQLAGLQ ERPLPAEQLV AASCHGLDDL RHAQRIGCDF AVLGPVQATA SHPGATPIGW DGFETLREQV SLPIYALGGM QIEDVRKARS HGGQGIAAIR ALWPQ // ID D4TAL4_9XANT Unreviewed; 233 AA. AC D4TAL4; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-MAR-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=XAUC_33740; OS Xanthomonas fuscans subsp. aurantifolii str. ICPB 10535. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=427082; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ICPB 10535; RX PubMed=20388224; DOI=10.1186/1471-2164-11-238; RA Moreira L.M., Almeida N.F.Jr., Potnis N., Digiampietri L.A., Adi S.S., RA Bortolossi J.C., da Silva A.C., da Silva A.M., de Moraes F.E., RA de Oliveira J.C., de Souza R.F., Fancincani A.P., Ferraz A.L., RA Ferro M.I., Furlan L.R., Gimenez D.F., Jones J.B., Kitajima E.W., RA Laia M.L., Leite R.P.Jr., Nishiyama M.Y., Rodrigues Neto J., RA Nociti L.A., Norman D.J., Ostroski E.H., Pereira H.A.Jr., RA Staskawicz B.J., Tezza R.I., Ferro J.A., Vinatzer B.A., Setubal J.C.; RT "Novel insights into the genomic basis of citrus canker based on the RT genome sequences of two strains of Xanthomonas fuscans subsp. RT aurantifolii."; RL BMC Genomics 11:238-238(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACPY01000243; EFF46278.1; -; Genomic_DNA. DR ProteinModelPortal; D4TAL4; -. DR EnsemblBacteria; EFF46278; EFF46278; XAUC_33740. DR PATRIC; 35685136; VBIXanFus21887_3849. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 66 70 HMP-PP binding (By similarity). FT REGION 164 166 THZ-P binding (By similarity). FT REGION 213 214 THZ-P binding (By similarity). FT METAL 99 99 Magnesium (By similarity). FT METAL 118 118 Magnesium (By similarity). FT BINDING 98 98 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 167 167 HMP-PP (By similarity). FT BINDING 193 193 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 24216 MW; 1097CEFCC0921D95 CRC64; MSRSSDNRGH ATVGLHCPIP STAFGSVAMP NRLNVRGVYL ITPDEPNTQR LLLRTAPLLG SITWLQYRNK QADAALRLRQ ASALREACVA HGVPLIINDD AQLAAQVGAQ GVHLGEDDGD VAAARALLGR QAIIGVSCYD DIERARAAAK AGASYVAFGA FFPTTTKQTT RRATPALLQQ AAGLDLPRVA IGGIAPAQVP ALASAGADLI AVVSGVYAAP DPVAAVQAYR DGF // ID D4TJA5_9NOST Unreviewed; 334 AA. AC D4TJA5; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-MAR-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CRC_02459; OS Cylindrospermopsis raciborskii CS-505. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Cylindrospermopsis. OX NCBI_TaxID=533240; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CS-505; RX PubMed=20169071; DOI=10.1371/journal.pone.0009235; RA Stucken K., John U., Cembella A., Murillo A.A., Soto-Liebe K., RA Fuentes-Valdes J.J., Friedel M., Plominsky A.M., Vasquez M., RA Glockner G.; RT "The smallest known genomes of multicellular and toxic cyanobacteria: RT comparison, minimal gene sets for linked traits and the evolutionary RT implications."; RL PLoS ONE 5:E9235-E9235(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYA01000056; EFA69098.1; -; Genomic_DNA. DR ProteinModelPortal; D4TJA5; -. DR EnsemblBacteria; EFA69098; EFA69098; CRC_02459. DR PATRIC; 35898229; VBICylRac118657_2679. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 116 Unknown (By similarity). FT REGION 117 334 Thiamine-phosphate synthase (By FT similarity). FT REGION 164 168 HMP-PP binding (By similarity). FT REGION 261 263 THZ-P binding (By similarity). FT METAL 197 197 Magnesium (By similarity). FT METAL 216 216 Magnesium (By similarity). FT BINDING 196 196 HMP-PP (By similarity). FT BINDING 235 235 HMP-PP (By similarity). FT BINDING 264 264 HMP-PP (By similarity). FT BINDING 291 291 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 334 AA; 37684 MW; 3F9DFFD4CDC19C02 CRC64; MVYRILDANL NRSREGLRII EEWCRFGLND ASLAETCKNL RQEVARWHTP QIRAARDTVG DPGTVLSHPQ EEQRSSITSL LQANFCRIQE AFRVLEEYGK LHHEEMGKTF KQMRYQVYTL ESTLMGHQRH HLLWQSRLYL VTSPADNLLA IVESCLQGGL TILQYREKTA DDMVRWDRAK KLRELCRTYG ALFIVNDRID LALAVDADGI HLGQQDLPVA VARELLGSQR ILGRSTTNPQ EMQAAITEGA DYIGVGPVYE TPTKPGKAAA GFDYVSYAAR NCPIPWFAIG GVDMGNIHDV IKAGAQRVAV VRSLMEAEQP TLATQYFISQ LLRK // ID D4TV32_9NOST Unreviewed; 334 AA. AC D4TV32; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-MAR-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CRD_02842; OS Raphidiopsis brookii D9. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Raphidiopsis. OX NCBI_TaxID=533247; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D9; RX PubMed=20169071; DOI=10.1371/journal.pone.0009235; RA Stucken K., John U., Cembella A., Murillo A.A., Soto-Liebe K., RA Fuentes-Valdes J.J., Friedel M., Plominsky A.M., Vasquez M., RA Glockner G.; RT "The smallest known genomes of multicellular and toxic cyanobacteria: RT comparison, minimal gene sets for linked traits and the evolutionary RT implications."; RL PLoS ONE 5:E9235-E9235(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYB01000046; EFA71742.1; -; Genomic_DNA. DR ProteinModelPortal; D4TV32; -. DR EnsemblBacteria; EFA71742; EFA71742; CRD_02842. DR PATRIC; 35906652; VBIRapBro106515_3005. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 116 Unknown (By similarity). FT REGION 117 334 Thiamine-phosphate synthase (By FT similarity). FT REGION 164 168 HMP-PP binding (By similarity). FT REGION 261 263 THZ-P binding (By similarity). FT METAL 197 197 Magnesium (By similarity). FT METAL 216 216 Magnesium (By similarity). FT BINDING 196 196 HMP-PP (By similarity). FT BINDING 235 235 HMP-PP (By similarity). FT BINDING 264 264 HMP-PP (By similarity). FT BINDING 291 291 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 334 AA; 37755 MW; 30BE75FD64CDEB94 CRC64; MVYRILDANL NRSREGLRII EEWCRFGLND ASLAETCKNL RQEVARWHTP QIRSSRDTVG DTGTILSHPQ EEHRNSITSL LQANFCRIQE AFRVLEEYGK LHHEEMGKTF KQMRYQVYTL ESSLMGHQRH HLLWQSRLYL VTSPADSLLT IVESCLQGGL TIVQYREKTA DDMVRLDRAK KLRELCRSYG ALFIINDRVD LALAVDADGV HLGQQDLPVP VARELLGPQR ILGRSTTNPQ EMQAAITEGA DYVGVGPVYE TPTKPGKPAA GFDYVNYASR NCPIPWFAIG GVDMGNIHDT IKAGAQRVAV VRSLMEAEQP TLATQYFMSQ LLRK // ID D4U8J0_STAAU Unreviewed; 213 AA. AC D4U8J0; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SKAG_02152; OS Staphylococcus aureus A9754. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553590; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A9754; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Peleg A.Y., Young S., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Neiman D., Park D., Pearson M., RA Richards J., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., RA Stolte C., Sykes S.N., Walk T., White J., Yandava C., Haas B., RA Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus A9754."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADJI01000011; EFG39443.1; -; Genomic_DNA. DR ProteinModelPortal; D4U8J0; -. DR SMR; D4U8J0; 4-209. DR PRIDE; D4U8J0; -. DR EnsemblBacteria; EFG39443; EFG39443; SKAG_02152. DR PATRIC; 36549615; VBIStaAur15630_2120. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D4UGT8_STAAU Unreviewed; 213 AA. AC D4UGT8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-APR-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SMAG_02197; OS Staphylococcus aureus A8819. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553580; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A8819; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Peleg A.Y., Young S., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Neiman D., Park D., Pearson M., RA Richards J., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., RA Stolte C., Sykes S.N., Walk T., White J., Yandava C., Haas B., RA Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus A8819."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADJK01000010; EFG44074.1; -; Genomic_DNA. DR ProteinModelPortal; D4UGT8; -. DR SMR; D4UGT8; 4-209. DR PRIDE; D4UGT8; -. DR EnsemblBacteria; EFG44074; EFG44074; SMAG_02197. DR PATRIC; 37106160; VBIStaAur108636_2166. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D4UXM8_ENTFL Unreviewed; 211 AA. AC D4UXM8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CUI_1868; OS Enterococcus faecalis PC1.1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=791166; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PC1.1; RX PubMed=23469340; RA O Cuiv P., Klaassens E.S., Smith W.J., Mondot S., Durkin A.S., RA Harkins D.M., Foster L., McCorrison J., Torralba M., Nelson K.E., RA Morrison M.; RT "Draft Genome Sequence of Enterococcus faecalis PC1.1, a Candidate RT Probiotic Strain Isolated from Human Feces."; RL Genome Announc. 1:E00160-12(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADKN01000026; EFG21607.1; -; Genomic_DNA. DR ProteinModelPortal; D4UXM8; -. DR EnsemblBacteria; EFG21607; EFG21607; CUI_1868. DR PATRIC; 36595951; VBIBacVul153182_0616. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22936 MW; A6E424940A930223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTRVAGV SLVSEIMLAE QIAEKVQGLM RVTERMLEAR K // ID D4VCK3_BACVU Unreviewed; 202 AA. AC D4VCK3; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=CUU_3769; OS Bacteroides vulgatus PC510. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=702446; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PC510; RX PubMed=21622758; DOI=10.1128/JB.05256-11; RA Cuiv P.O., Klaassens E.S., Durkin A.S., Harkins D.M., Foster L., RA McCorrison J., Torralba M., Nelson K.E., Morrison M.; RT "Draft Genome Sequence of Bacteroides vulgatus PC510, a Strain RT Isolated from Human Feces."; RL J. Bacteriol. 193:4025-4026(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADKO01000107; EFG16397.1; -; Genomic_DNA. DR ProteinModelPortal; D4VCK3; -. DR SMR; D4VCK3; 1-202. DR EnsemblBacteria; EFG16397; EFG16397; CUU_3769. DR PATRIC; 36606688; VBIBacVul154801_3320. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 22933 MW; 0AE478B2289391FD CRC64; MKLILITPPT YFVEEDKIIT ALFEEGLDTL HLRKPGTAPM FAERLLTLIP EQYHKRIVVH GHFYLKEEYK LKGIHLNGRN PNLPEGYKGH VSCSCHSLDE VKERKSSCDY VFLSPVFNSI SKLNYNSAYT AEELRTAAKA GIIDKKVIAL GGIDEENLLE VKDFGFGGAA ILGALWNKFD ACTDRDYRCV IEHFRKLRDL AD // ID D4VCL2_BACVU Unreviewed; 208 AA. AC D4VCL2; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CUU_3778; OS Bacteroides vulgatus PC510. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=702446; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PC510; RX PubMed=21622758; DOI=10.1128/JB.05256-11; RA Cuiv P.O., Klaassens E.S., Durkin A.S., Harkins D.M., Foster L., RA McCorrison J., Torralba M., Nelson K.E., Morrison M.; RT "Draft Genome Sequence of Bacteroides vulgatus PC510, a Strain RT Isolated from Human Feces."; RL J. Bacteriol. 193:4025-4026(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADKO01000107; EFG16406.1; -; Genomic_DNA. DR ProteinModelPortal; D4VCL2; -. DR EnsemblBacteria; EFG16406; EFG16406; CUU_3778. DR PATRIC; 36606706; VBIBacVul154801_3329. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 23078 MW; C08790A5F80A9015 CRC64; MEDKTVELQF ITHFTDTYSY YDSARMALEG GCRWIQLRMK DTPVDEVERE AIRLQGLCKD YGATFIIDDH VELVKKIHAD GVHLGKKDMP VAEARGILGK EFIIGGTANT FDDVKMHYKA GADYIGCGPF RFTTTKKDLS PVLGLEGYRS IILQMKEANI HLPIVAIGGI TLEDIPSIME TGITGIALSG TILRAKDPVA ETKRIMNL // ID D4VJ42_9BACE Unreviewed; 212 AA. AC D4VJ42; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=CW3_4070; OS Bacteroides xylanisolvens SD CC 1b. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=702447; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SD CC 1b; RA Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D., RA Montgomery R., Ziemer C., Klaassens E., Ocuiv P., Morrison M.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADKP01000069; EFG14116.1; -; Genomic_DNA. DR EnsemblBacteria; EFG14116; EFG14116; CW3_4070. DR PATRIC; 36611391; VBIBacXyl153952_1573. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 212 AA; 24781 MW; 3107C52BC6ABF26B CRC64; MLNNPILTKE MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNRFD ACQDQNYLAV IEHFKKLKKL SD // ID D4VJ47_9BACE Unreviewed; 206 AA. AC D4VJ47; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CW3_4075; OS Bacteroides xylanisolvens SD CC 1b. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=702447; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SD CC 1b; RA Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D., RA Montgomery R., Ziemer C., Klaassens E., Ocuiv P., Morrison M.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADKP01000069; EFG14121.1; -; Genomic_DNA. DR ProteinModelPortal; D4VJ47; -. DR EnsemblBacteria; EFG14121; EFG14121; CW3_4075. DR PATRIC; 36611401; VBIBacXyl153952_1578. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22655 MW; C71D2CE7B5A79C06 CRC64; MISLQFITHQ TERYSYLESA RMALEGGCKW IQLRMKDALL EEVEAVALQL KPLCKEHEAI LILDDHVELA KKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYSSILSQ MKEANIEIPV VAIGGITFED IPAILHTGVN GIALSGTILG ADNPVEETRR IIESDL // ID D4W904_9FIRM Unreviewed; 209 AA. AC D4W904; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CUW_1492; OS Turicibacter sanguinis PC909. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Turicibacter. OX NCBI_TaxID=702450; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PC909; RX PubMed=21183674; DOI=10.1128/JB.01328-10; RA Cuiv P.O., Klaassens E.S., Durkin A.S., Harkins D.M., Foster L., RA McCorrison J., Torralba M., Nelson K.E., Morrison M.; RT "Draft genome sequence of Turicibacter sanguinis PC909, isolated from RT human feces."; RL J. Bacteriol. 193:1288-1289(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMN01000120; EFF62578.1; -; Genomic_DNA. DR ProteinModelPortal; D4W904; -. DR EnsemblBacteria; EFF62578; EFF62578; CUW_1492. DR PATRIC; 36629392; VBITurSp148888_2646. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22869 MW; DFBA31C800E4F83C CRC64; MKLNKQDLSL YLVTDRHWTK DQSLVEQVEA GLKGGVTMVQ LREKNLSDEE FLLKALELKE LTTTYKVPFM INDNVWVAIQ SDADGIHIGQ DDLPADEVRK LVGEEKILGV SVQTVEQAQI AKRQGADYLG VGAVFSTDTK KDAKHVPLQV LKEICEAVNL PVVAIGGIDE DNVDELTGSG ICGVAVVSAI LASDDIMQAA KNLKRDWVL // ID D4WNP8_BACOV Unreviewed; 205 AA. AC D4WNP8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CUY_4064; OS Bacteroides ovatus SD CMC 3f. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=702443; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SD CMC 3f; RA Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D.M., RA Montgomery R., Ziemer C., Klaassens E., Ocuiv P., Morrison M., RA Nelson K.E.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMO01000151; EFF49860.1; -; Genomic_DNA. DR ProteinModelPortal; D4WNP8; -. DR EnsemblBacteria; EFF49860; EFF49860; CUY_4064. DR PATRIC; 36640346; VBIBacOva158973_5235. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22561 MW; 5396C877E01764E2 CRC64; MVSLQFITHQ TERYSYLESA RMALEGGCKW IQLRMKEAPL EEVEAVALQL KPLCKEHEAI LVLDDHVELA RKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYSSILSQ MKEANIEIPV VAIGGITYED IPAILHTGVN GIALSGTILG ADNPIEETRR ILNHA // ID D4WNQ3_BACOV Unreviewed; 202 AA. AC D4WNQ3; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=CUY_4069; OS Bacteroides ovatus SD CMC 3f. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=702443; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SD CMC 3f; RA Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D.M., RA Montgomery R., Ziemer C., Klaassens E., Ocuiv P., Morrison M., RA Nelson K.E.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMO01000151; EFF49865.1; -; Genomic_DNA. DR ProteinModelPortal; D4WNQ3; -. DR SMR; D4WNQ3; 1-202. DR EnsemblBacteria; EFF49865; EFF49865; CUY_4069. DR PATRIC; 36640356; VBIBacOva158973_5240. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23599 MW; 772F8DFC6BF5D5DD CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNKFD ACQDQNYLAV IEHFKKLKKL SD // ID D4WR70_9BACE Unreviewed; 206 AA. AC D4WR70; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CW1_3556; OS Bacteroides xylanisolvens SD CC 2a. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=702444; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SD CC 2a; RA Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D.M., RA Montgomery R., Ziemer C., Klaassens E., Ocuiv P., Morrison M., RA Nelson K.E.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMP01000041; EFF59164.1; -; Genomic_DNA. DR ProteinModelPortal; D4WR70; -. DR EnsemblBacteria; EFF59164; EFF59164; CW1_3556. DR PATRIC; 36642195; VBIBacOva147808_0641. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22655 MW; C71D2CE7B5A79C06 CRC64; MISLQFITHQ TERYSYLESA RMALEGGCKW IQLRMKDALL EEVEAVALQL KPLCKEHEAI LILDDHVELA KKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYSSILSQ MKEANIEIPV VAIGGITFED IPAILHTGVN GIALSGTILG ADNPVEETRR IIESDL // ID D4WR75_9BACE Unreviewed; 202 AA. AC D4WR75; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-APR-2014, entry version 18. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BN891_2030, CW1_3561; OS Bacteroides xylanisolvens SD CC 2a. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=702444; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SD CC 2a; RA Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D.M., RA Montgomery R., Ziemer C., Klaassens E., Ocuiv P., Morrison M., RA Nelson K.E.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RA Ramaraj T., Sundararajan A., Mudge J., Schilkey F.D., Delvecchio V., RA Donlon M., Ziemer C.; RT "Improved hybrid genome assemblies of Bacteroides xylanisolvens SD CC RT 1b and Bacteroides xylanisolvens SD CC 2a using Illumina and 454 RT Sequencing."; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBXH010000003; CDL97329.1; -; Genomic_DNA. DR EMBL; ADMP01000041; EFF59169.1; -; Genomic_DNA. DR ProteinModelPortal; D4WR75; -. DR EnsemblBacteria; EFF59169; EFF59169; CW1_3561. DR PATRIC; 36642207; VBIBacOva147808_0647. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 202 AA; 23627 MW; 6FBE04FC6BF5D5DD CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNRFD ACQDQNYLAV IEHFKKLKKL SD // ID D4X6W9_9BURK Unreviewed; 320 AA. AC D4X6W9; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=mutT; ORFNames=HMPREF0004_1216; OS Achromobacter piechaudii ATCC 43553. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=742159; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43553; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMS01000026; EFF77486.1; -; Genomic_DNA. DR ProteinModelPortal; D4X6W9; -. DR EnsemblBacteria; EFF77486; EFF77486; HMPREF0004_1216. DR PATRIC; 36775578; VBIAchPie159143_2088. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase; Transferase. SQ SEQUENCE 320 AA; 34167 MW; 46B6128B80265D43 CRC64; MSEKIVDVAA GLILRPNGML LLGQRPEGKP WSGWWELPGG KLEPGETVLQ ALARELQEEL GIRVTQSRPW VTYVHVYPHT TVRLAFCHVT AWEGEPQGLE NQRLQWVDPA NAASVGDLLP ATLPPLRWLQ LPTTYGISSI GSRAGVAAFL GRLEAALARG VKLVQFREPQ WPDGAGASSL HEVLQQVIKR CHAAGARVLV NSAHPAAWWK EADGVHLRTA DAARLHARPE LPEGALLGVS AHDNAQVVHA REIGADFAVL GPVLDTPSHP GAATLGWEGF VAGNRDAGIP VFALGGQSTQ TVSQALRHGA HGIAGIRGVI // ID D4X701_9BURK Unreviewed; 221 AA. AC D4X701; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0004_1248; OS Achromobacter piechaudii ATCC 43553. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=742159; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43553; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMS01000027; EFF77421.1; -; Genomic_DNA. DR ProteinModelPortal; D4X701; -. DR EnsemblBacteria; EFF77421; EFF77421; HMPREF0004_1248. DR PATRIC; 36775642; VBIAchPie159143_2120. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23562 MW; 4A6BB384A4260F28 CRC64; MKPLRFPSGL YGVTPEWDDT DRLLQAVRKA AEGGMRSLQL RRKNVPDAVR AEQARALAPL CRELGVVFLI NDDWRLALDV GADGAHVGRE DESLARIRAE AGPDLILGGS SYDDLNRARE LLDAGADYIA FGAMYPSTVK PDTVRAPLSV LTEARRLVDE RDAPRPAVVA IGGITPDNAP LVAQAGADAI AVITALFEAP SIRAAAAACS APYSVNPLRK P // ID D4XNW9_ACIHA Unreviewed; 203 AA. AC D4XNW9; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMP0015_1411; OS Acinetobacter haemolyticus ATCC 19194. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=707232; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19194; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMT01000133; EFF83084.1; -; Genomic_DNA. DR ProteinModelPortal; D4XNW9; -. DR EnsemblBacteria; EFF83084; EFF83084; HMP0015_1411. DR PATRIC; 36653573; VBIAciHae153512_2729. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21703 MW; E2F88A588D0EC45C CRC64; MRGLYLITND DPIQLLLEKL EVALATGKVA ILQYRRKKAT KADQPMEVEQ IKTLCEKYQV PFVINDDLAL AEQFGLGVHL GQSDGEISDA AARLPQGAII GRTCLNSLEL AEKAIADEAT YVAFGAVYAT STKPEAGNVG IEVIKQAKQK FTVPICAIGG LTVENSQVVI EAGASLCAVI SDILGRSTAE IPARVNAWAT LFD // ID D4XPS6_ACIHA Unreviewed; 303 AA. AC D4XPS6; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Mutator mutT protein; DE EC=3.6.1.-; GN ORFNames=HMP0015_1718; OS Acinetobacter haemolyticus ATCC 19194. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=707232; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19194; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMT01000154; EFF82800.1; -; Genomic_DNA. DR ProteinModelPortal; D4XPS6; -. DR EnsemblBacteria; EFF82800; EFF82800; HMP0015_1718. DR PATRIC; 36654132; VBIAciHae153512_3016. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 303 AA; 34900 MW; B4753FD17FCC13E3 CRC64; MAKSIVEVAI AILLHKSKVL VGWRQANQHQ GNKHEFPGGK VEQHETPEQA CRREIFEEVG IGLKDWHKFD VIQHEYDDLI VRLHLFHAHV PDQFLDLIHQ PWTWYSRDQL RSLNFPKANK TIIERLVWSH LIKISDLLPA LPHSNVQFYW RNEKLNIVEV QQQLSVLTDD QLNKLIINFS LWQQLDSKLQ AKIQTIHLKQ SQLMRFKNGE LIVGKRFIAA CHDAVSLKHA HDIGCDAVFL SPVNQTETHL EAKVLGWDVF SELAENSDIP VFALGGVAPK DIEQAQKHHA YGLAGIREFE SIE // ID D4YFV1_9LACT Unreviewed; 219 AA. AC D4YFV1; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0061_0740; OS Aerococcus viridans ATCC 11563. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Aerococcus. OX NCBI_TaxID=655812; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11563; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNT01000056; EFG49933.1; -; Genomic_DNA. DR ProteinModelPortal; D4YFV1; -. DR EnsemblBacteria; EFG49933; EFG49933; HMPREF0061_0740. DR PATRIC; 37121818; VBIAerVir111637_0669. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23557 MW; 41D7874DB4AAB8E6 CRC64; MVNRYQGRPT IMDYSLYLVT AGFDYQEDAF LQVVEDAVKA GVTLVQFRDK TATSRDAYAL AQKLKAITDR YDVPLIINDR VDLALAVDAA GVHIGDDELP VDVVRKLIGP DKILGVSTKT LARAEEAYQQ GADYLGVGAI FPTTTKDSSL VTVETLQTIT SQVAIPVVAI GGIHLDNIKT LSGSGIAGIS VVSEIMLADS VTQRVRDLKA EVADMLEVD // ID D4YLN4_9MICO Unreviewed; 233 AA. AC D4YLN4; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0183_0844; OS Brevibacterium mcbrellneri ATCC 49030. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Brevibacteriaceae; Brevibacterium. OX NCBI_TaxID=585530; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49030; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNU01000023; EFG47767.1; -; Genomic_DNA. DR ProteinModelPortal; D4YLN4; -. DR EnsemblBacteria; EFG47767; EFG47767; HMPREF0183_0844. DR PATRIC; 37125755; VBIBreMcb74223_0822. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 160 162 THZ-P binding (By similarity). FT REGION 211 212 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 109 109 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 163 163 HMP-PP (By similarity). FT BINDING 191 191 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 24422 MW; C9F141B810740EA5 CRC64; MTNPRLKDID GSLYFITDTK MCEQAGRTVA QTVELAVAGG AGIVQVRDKH ATDATFAELT LSVLEAVENA RSAYNITRPV PVFVNDRVDV AASLINDGHD IHVHVGQDDT SVPRVRELIG NSPLIGLSAN TPEEIEVART HGDFGNGGVD LLGVGPVWDT ATKEGAPAGL GIDTLKNLTA ISAIPVFAIG GINAERAAQL KDTSVSGVCV VSAICLAADP QAEAHKIYDA FRN // ID D4YWW4_SPHJU Unreviewed; 187 AA. AC D4YWW4; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 11-DEC-2013, entry version 23. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN OrderedLocusNames=SJA_C1-00120; OS Sphingobium japonicum (strain NBRC 101211 / UT26S). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=452662; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101211 / UT26S; RX PubMed=20817768; DOI=10.1128/JB.00961-10; RA Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A., RA Fukui S., Fujita N., Tsuda M.; RT "Complete genome sequence of the representative gamma- RT hexachlorocyclohexane-degrading bacterium Sphingobium japonicum RT UT26."; RL J. Bacteriol. 192:5852-5853(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010803; BAI94846.1; -; Genomic_DNA. DR RefSeq; YP_003543458.1; NC_014006.1. DR ProteinModelPortal; D4YWW4; -. DR EnsemblBacteria; BAI94846; BAI94846; SJA_C1-00120. DR GeneID; 8953308; -. DR KEGG; sjp:SJA_C1-00120; -. DR PATRIC; 35432455; VBISphJap147895_0049. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SJAP452662:GHEL-12-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 187 AA; 20651 MW; A9E334DFD8555664 CRC64; MAMQRRHRKK LPTIWLMTDE RVGESALLAA IDRLPKGRAG VIFRHYRTAA AERRALFDRV ARMARRRRLV LMLGGTAAQA RAWRADGWHG RDRRRDGKTL LHSRPVHDKR QMAEAARAGA DFVFLSPLFP TRSHPGSLVL GRAGFAALAR LAPMPVIALG GVRAAHRHML AGMGASGWGA IDGLSVE // ID D4Z0L7_SPHJU Unreviewed; 230 AA. AC D4Z0L7; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SJA_C1-13150; OS Sphingobium japonicum (strain NBRC 101211 / UT26S). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=452662; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101211 / UT26S; RX PubMed=20817768; DOI=10.1128/JB.00961-10; RA Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A., RA Fukui S., Fujita N., Tsuda M.; RT "Complete genome sequence of the representative gamma- RT hexachlorocyclohexane-degrading bacterium Sphingobium japonicum RT UT26."; RL J. Bacteriol. 192:5852-5853(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010803; BAI96149.1; -; Genomic_DNA. DR RefSeq; YP_003544761.1; NC_014006.1. DR ProteinModelPortal; D4Z0L7; -. DR EnsemblBacteria; BAI96149; BAI96149; SJA_C1-13150. DR GeneID; 8954157; -. DR KEGG; sjp:SJA_C1-13150; -. DR PATRIC; 35434885; VBISphJap147895_1247. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SJAP452662:GHEL-1335-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 58 62 HMP-PP binding (By similarity). FT REGION 156 158 THZ-P binding (By similarity). FT METAL 91 91 Magnesium (By similarity). FT METAL 110 110 Magnesium (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 159 159 HMP-PP (By similarity). FT BINDING 186 186 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 24244 MW; 5C9FA81B0F62C7AD CRC64; MTDFTDEELA LDPNFADRFE QGFRPACQLY LISPPAIGAD FADSLAAAFD GGGVAAFQLR LKGLDEDAVA RAAEPLQKLC AERDVAFIVN DSMALAKRLG ADGVHLGQGD GDPKEARRLL GPSVQIGVTC HDSRHLAMEA GEAGADYVAF GAFYPTTTKE THYRPDPSIL GWWTALFELP CVAIGGITAD NAAPLVKAGA DFLAVSGAVW SHPEGPRAGV AAFEAVLARK // ID D4ZKZ2_SHEVD Unreviewed; 525 AA. AC D4ZKZ2; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiDE; OrderedLocusNames=SVI_2370; OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / OS DSS12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=637905; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12; RX PubMed=20458400; DOI=10.1039/c000396d; RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., RA Toyonaga H., Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., RA Kato C., Oshima T., Nakasone K., Mori H.; RT "Complete genome sequence and comparative analysis of Shewanella RT violacea, a psychrophilic and piezophilic bacterium from deep sea RT floor sediments."; RL Mol. Biosyst. 6:1216-1226(2010). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011177; BAJ02341.1; -; Genomic_DNA. DR RefSeq; YP_003557119.1; NC_014012.1. DR ProteinModelPortal; D4ZKZ2; -. DR EnsemblBacteria; BAJ02341; BAJ02341; SVI_2370. DR GeneID; 8966580; -. DR KEGG; svo:SVI_2370; -. DR PATRIC; 35460985; VBISheVio92117_2290. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR BioCyc; SVIO637905:GCRO-2470-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 525 AA; 56390 MW; 75B94C94F854345A CRC64; MANLEPTSSA LKPVVWSIAG SDSGGGAGIQ ADLATMNDLA CHACTVITTL TAQSSVAVNL VEPVSDEMLL AQLDTLLQDL PPKAIKIGLL ANQRQIDLLS RWLALDLPDH NKRNGTEVAV ILDPVMIASC GDRLDGDDTR LDFTPFKGLL TLITPNALEL GELVGQTLTD MSQYHQAAKD LSLSLDTNVL AKGGDKGPAW RSDLAQDIFV CTRAAACSEI HQQASFLLSS QRIASNNNHG TGCTLSSAIA SVMASGFVLH DAIVVAKAYV SAGIKHSYRV GDGPGPLART GWPKELSAFP KISSLDDGPS LPRGIKFKAI DERLGLYPVV SELSLLETLL RAGAKTIQLR IKDENDPHLE DKIAQAIVLG RDYQAKVFIN DYWELALKHN AYGVHLGQED LYDADLKRIA DAQMALGISS HSYFELLLAS QITPSYIALG HIFPTTTKEM PSAPQGLMKL QHYVDLFKGH YPLVAIGGIN ASRIPKVKTT GVDDIAVVRA LSESEQPGAT YRALSSAWEQ ANVVE // ID D5A643_ARTPN Unreviewed; 365 AA. AC D5A643; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NIES39_O04290; OS Arthrospira platensis (strain NIES-39 / IAM M-135) (Spirulina OS platensis). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Arthrospira. OX NCBI_TaxID=696747; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-39 / IAM M-135; RX PubMed=20203057; DOI=10.1093/dnares/dsq004; RA Fujisawa T., Narikawa R., Okamoto S., Ehira S., Yoshimura H., RA Suzuki I., Masuda T., Mochimaru M., Takaichi S., Awai K., Sekine M., RA Horikawa H., Yashiro I., Omata S., Takarada H., Katano Y., Kosugi H., RA Tanikawa S., Ohmori K., Sato N., Ikeuchi M., Fujita N., Ohmori M.; RT "Genomic structure of an economically important cyanobacterium, RT Arthrospira (Spirulina) platensis NIES-39."; RL DNA Res. 17:85-103(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011615; BAI93676.1; -; Genomic_DNA. DR RefSeq; YP_005072214.1; NC_016640.1. DR ProteinModelPortal; D5A643; -. DR EnsemblBacteria; BAI93676; BAI93676; NIES39_O04290. DR GeneID; 15165692; -. DR KEGG; arp:NIES39_O04290; -. DR PATRIC; 42725435; VBIArtPla153080_3929. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 129 Unknown (By similarity). FT REGION 130 365 Thiamine-phosphate synthase (By FT similarity). FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 365 AA; 41263 MW; 97EFB4057AAA7A23 CRC64; MGDLNHKTKL GQPALYRILD ANLDRAREGI RTIEEWFRFG LDNSEMAAEC KNLRQQLAQW HSNELRMSRD TTTDVGTQLS HPSEENRESL EQVIQVNFCR VEEALRVLEE YGKVYHPNMG AAVKQMRYRV YTLESNLLAY GRHQTLQRAN LYLVTSPSER LMSVVEAALQ GGLKVVQYRD KDTDDHQRWK NARQLCQLCH RYNALFLVND RVDIAIAVNA DGVHLGQQDL PIAVAKQLLG PQKIVGKSTT NPEEMKLAIA EGADYIGVGP VYATPTKPDK QAAGLEYVRH ATRHASVPWF AIGGINMNNF DDVLMAGATR VAVVRSLMQA EQPTLVTQYF LSQFTRVQTL RDRQILPENA PADFS // ID D5AH67_STRGZ Unreviewed; 245 AA. AC D5AH67; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SSGZ1_0725; OS Streptococcus suis (strain GZ1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=423211; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GZ1; RX PubMed=19016627; DOI=10.1086/594370; RA Ye C., Zheng H., Zhang J., Jing H., Wang L., Xiong Y., Wang W., RA Zhou Z., Sun Q., Luo X., Du H., Gottschalk M., Xu J.; RT "Clinical, experimental, and genomic differences between RT intermediately pathogenic, highly pathogenic, and epidemic RT Streptococcus suis."; RL J. Infect. Dis. 199:97-107(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000837; ADE31182.1; -; Genomic_DNA. DR RefSeq; YP_006074124.1; NC_017617.1. DR ProteinModelPortal; D5AH67; -. DR EnsemblBacteria; ADE31182; ADE31182; SSGZ1_0725. DR GeneID; 12724124; -. DR KEGG; ssw:SSGZ1_0725; -. DR PATRIC; 36796061; VBIStrSui127079_0714. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SSUI423211:GLLL-773-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 153 155 THZ-P binding (By similarity). FT REGION 205 206 THZ-P binding (By similarity). FT METAL 90 90 Magnesium (By similarity). FT METAL 109 109 Magnesium (By similarity). FT BINDING 89 89 HMP-PP (By similarity). FT BINDING 127 127 HMP-PP (By similarity). FT BINDING 156 156 HMP-PP (By similarity). FT BINDING 185 185 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 245 AA; 26853 MW; 707A55F68C7C6311 CRC64; MQSNQKRLKK IKRSFIMNRK MLQVYFICGT SDCPKGKFLD VLEKALQAGI TCFQFREKGE QGLTGADKLL LAKQVQHLCH RYQVPLIIND DVELARAIDA DGIHLGQEDL SVVEARQLFP GKIIGLSVGT KEEYLNSPID LVDYIGSGPV FPTLSKDDAS PAIGMDGLKQ LRKLNSDIPM VAIGGLSAKD CKEVLQAGAD GIAVISAISH AEDPYKATKI LVDGMQAMIL KFNQVESNKQ ILKNP // ID D5APL1_RHOCB Unreviewed; 203 AA. AC D5APL1; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=RCAP_rcc02851; OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=272942; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SB1003; RA Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N., RA Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R., RA Kyrpides N., Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V., RA Los T., Lykidis A., Mikhailova N., Reznik G., Vasieva O., Fonstein M., RA Paces V., Haselkorn R.; RT "Complete genome sequence of Rhodobacter capsulatus SB1003."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; RX PubMed=20418398; DOI=10.1128/JB.00366-10; RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., RA Haselkorn R.; RT "Complete genome sequence of the photosynthetic purple nonsulfur RT bacterium Rhodobacter capsulatus SB 1003."; RL J. Bacteriol. 192:3545-3546(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001312; ADE86580.1; -; Genomic_DNA. DR RefSeq; YP_003578987.1; NC_014034.1. DR ProteinModelPortal; D5APL1; -. DR EnsemblBacteria; ADE86580; ADE86580; RCAP_rcc02851. DR GeneID; 9005670; -. DR KEGG; rcp:RCAP_rcc02851; -. DR PATRIC; 35505918; VBIRhoCap134200_2900. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VTDRTLC; -. DR BioCyc; RCAP272942:GJIY-2891-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 20619 MW; D5F1C68FADB1E7D6 CRC64; MIGPVYVITD PGAALSVPDQ ARAAARGGAR AVQLRDKTAS DADLLALARQ LLPEMRAHGV KLFLNDRIEV AIAAGADGLH IGQGDGDPVA IRARIGAGML LGLSIETEAQ ASRLPGCVDY IGAGPVRATA TKPDAAAPIG FDGLARIARL VAVPTLAIGG LTRADIPALK AAGVAGMAVV SAVTRAPDAE AACRALVQDW RPR // ID D5ATR1_RHOCB Unreviewed; 205 AA. AC D5ATR1; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-OCT-2013, entry version 25. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN OrderedLocusNames=RCAP_rcc01605; OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=272942; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SB1003; RA Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N., RA Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R., RA Kyrpides N., Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V., RA Los T., Lykidis A., Mikhailova N., Reznik G., Vasieva O., Fonstein M., RA Paces V., Haselkorn R.; RT "Complete genome sequence of Rhodobacter capsulatus SB1003."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; RX PubMed=20418398; DOI=10.1128/JB.00366-10; RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., RA Haselkorn R.; RT "Complete genome sequence of the photosynthetic purple nonsulfur RT bacterium Rhodobacter capsulatus SB 1003."; RL J. Bacteriol. 192:3545-3546(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001312; ADE85350.1; -; Genomic_DNA. DR RefSeq; YP_003577757.1; NC_014034.1. DR ProteinModelPortal; D5ATR1; -. DR EnsemblBacteria; ADE85350; ADE85350; RCAP_rcc01605. DR GeneID; 9004428; -. DR KEGG; rcp:RCAP_rcc01605; -. DR PATRIC; 35503336; VBIRhoCap134200_1627. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR BioCyc; RCAP272942:GJIY-1629-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 205 AA; 22021 MW; 1039BE39D6126598 CRC64; MSEDRPQLYL ATPPSFDLDV FPQLLARVLG AQEVACIRLG LATKDEDKVM RAADAVRQVA HEFDVALVIE NHIALVERHG LDGVHLTDGA RTVRYARKEL GQDAIVGAFC AASQHDGMTA GEAGADYVCF GPVGETGLGT GARAERDLFQ WWSEVIEVPV VAEGALTEDL VRDFAPVTDF FAVGEEIWTA EDPVAALGRL VAAMG // ID D5B4K2_YERPZ Unreviewed; 224 AA. AC D5B4K2; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=YPZ3_3300; OS Yersinia pestis (strain Z176003). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=637386; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Z176003; RA Hai R., Yu D., Xia L., Zhu X., Liang Y., Shen X., Zhang E., Zhang H.; RT "Complete genome sequence of Yersinia pestis from new plague natural RT foci in China."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Z176003; RX PubMed=20453098; DOI=10.1128/JB.00340-10; RA Shen X., Wang Q., Xia L., Zhu X., Zhang Z., Liang Y., Cai H., RA Zhang E., Wei J., Chen C., Song Z., Zhang H., Yu D., Hai R.; RT "Complete genome sequences of Yersinia pestis from natural foci in RT China."; RL J. Bacteriol. 192:3551-3552(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001593; ADE66209.1; -; Genomic_DNA. DR RefSeq; YP_003569471.1; NC_014029.1. DR ProteinModelPortal; D5B4K2; -. DR EnsemblBacteria; ADE66209; ADE66209; YPZ3_3300. DR GeneID; 8993259; -. DR KEGG; ypz:YPZ3_3300; -. DR PATRIC; 35475743; VBIYerPes97410_4539. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; YPES637386:GKE8-3371-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID D5BA02_ZUNPS Unreviewed; 215 AA. AC D5BA02; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ZPR_1975; OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Zunongwangia. OX NCBI_TaxID=655815; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87; RX PubMed=20398413; DOI=10.1186/1471-2164-11-247; RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., RA Dang H.Y., Zhou B.C., Yu J., Zhang Y.Z.; RT "The complete genome of Zunongwangia profunda SM-A87 reveals its RT adaptation to the deep-sea environment and ecological role in RT sedimentary organic nitrogen degradation."; RL BMC Genomics 11:247-247(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001650; ADF52300.1; -; Genomic_DNA. DR RefSeq; YP_003584496.1; NC_014041.1. DR ProteinModelPortal; D5BA02; -. DR EnsemblBacteria; ADF52300; ADF52300; ZPR_1975. DR GeneID; 9077847; -. DR KEGG; zpr:ZPR_1975; -. DR PATRIC; 37233349; VBIZunPro130839_1892. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; ZPRO655815:GI6J-1971-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). SQ SEQUENCE 215 AA; 23890 MW; 168AF634843C740F CRC64; MHPDFPYQLY LVIAEESCVH YPLLQVAKMA IEGGVDIIQL REKNLSTSVF IKKAEALKQL TDQYKIPLII NDNLEVAKAV DAFGIHVGNN DIPPTQIKQQ WDKHKAIGYS IEYLEQLKNE QTEVANHLGI SPVYSTATKT DTVTEWGIEG IKKIRTLTTK PLIAIGRMDA GNAGEIIKAG ADCIAVVSAI CASKYPEKTA KNIKTQIHKH RNENI // ID D5BCI8_ZUNPS Unreviewed; 198 AA. AC D5BCI8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase; GN OrderedLocusNames=ZPR_0138; OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Zunongwangia. OX NCBI_TaxID=655815; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87; RX PubMed=20398413; DOI=10.1186/1471-2164-11-247; RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., RA Dang H.Y., Zhou B.C., Yu J., Zhang Y.Z.; RT "The complete genome of Zunongwangia profunda SM-A87 reveals its RT adaptation to the deep-sea environment and ecological role in RT sedimentary organic nitrogen degradation."; RL BMC Genomics 11:247-247(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001650; ADF50501.1; -; Genomic_DNA. DR RefSeq; YP_003582697.1; NC_014041.1. DR ProteinModelPortal; D5BCI8; -. DR EnsemblBacteria; ADF50501; ADF50501; ZPR_0138. DR GeneID; 9076014; -. DR KEGG; zpr:ZPR_0138; -. DR PATRIC; 37229771; VBIZunPro130839_0135. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR BioCyc; ZPRO655815:GI6J-138-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 198 AA; 22858 MW; CE91C7EC4817AFA6 CRC64; MLIVISAEKL IENEESQLKS MFDAGLETLH IRKPEVSFEE LKTWLENFEP GYRSKMVLHQ HHELAREFGL KGVHLPEYFR TSLKETLEDY VNTFQHLKFT VSTSFHQKEE ISRTSIFDYC FLSPIFNSIS KTGYVGKTFQ VLDIQQKVIA LGGIDAAKIP LAYNMGFYGV AVLGAVWLQE DPIHSFIKIQ QQYESVFN // ID D5BCI9_ZUNPS Unreviewed; 215 AA. AC D5BCI9; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ZPR_0139; OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Zunongwangia. OX NCBI_TaxID=655815; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87; RX PubMed=20398413; DOI=10.1186/1471-2164-11-247; RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., RA Dang H.Y., Zhou B.C., Yu J., Zhang Y.Z.; RT "The complete genome of Zunongwangia profunda SM-A87 reveals its RT adaptation to the deep-sea environment and ecological role in RT sedimentary organic nitrogen degradation."; RL BMC Genomics 11:247-247(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001650; ADF50502.1; -; Genomic_DNA. DR RefSeq; YP_003582698.1; NC_014041.1. DR ProteinModelPortal; D5BCI9; -. DR EnsemblBacteria; ADF50502; ADF50502; ZPR_0139. DR GeneID; 9076015; -. DR KEGG; zpr:ZPR_0139; -. DR PATRIC; 37229773; VBIZunPro130839_0136. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; ZPRO655815:GI6J-139-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23942 MW; 8206E4DC33F210E3 CRC64; MNLPKEISCL HYISQGKDRE EHLANITRVL KAGANWIQLR IKEMPQKEIL KTAILARELC AKYKAKLIVN DHVKVAKTCN ADGVHLGQED TDVLEARKIL GKDKIIGGTA NTLQHCLEHL ENGVDYIGLG PLRFTSTKKE LSPVLGFSGY QELIEKYSQQ ENTVPIIAIG GIKVNDIEEL RKIGLSGVAI SSLLTHSKDP KNEIQQILDR FAVRV // ID D5BN23_PUNMI Unreviewed; 198 AA. AC D5BN23; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 14-MAY-2014, entry version 31. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=SAR116_1973; OS Puniceispirillum marinum (strain IMCC1322). OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR116 cluster; OC Candidatus Puniceispirillum. OX NCBI_TaxID=488538; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC1322; RX PubMed=20382761; DOI=10.1128/JB.00347-10; RA Oh H.M., Kwon K.K., Kang I., Kang S.G., Lee J.H., Kim S.J., Cho J.C.; RT "Complete genome sequence of "Candidatus Puniceispirillum marinum" RT IMCC1322, a representative of the SAR116 clade in the RT Alphaproteobacteria."; RL J. Bacteriol. 192:3240-3241(2010). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001751; ADE40216.1; -; Genomic_DNA. DR RefSeq; YP_003552300.1; NC_014010.1. DR ProteinModelPortal; D5BN23; -. DR EnsemblBacteria; ADE40216; ADE40216; SAR116_1973. DR GeneID; 8962317; -. DR KEGG; apb:SAR116_1973; -. DR PATRIC; 35450937; VBIAlpPro78664_1996. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; PMAR488538:GI1I-2002-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 198 AA; 22253 MW; DCD492C0126ED440 CRC64; MTLDRFYPIF DSCDWLRRML PLGVKLVQLR IKDAPLDIVR REIVEAKALC DAHGAVLVVN DYWHIAIDAG CDWVHLGQED MDNADLNAIR RAGIRLGFST HDDDELERAL GFAPDYLALG PVYPTILKKM KWHQQGLPRV TEWKARIGAI PLVGIGGMRV DRAAGVFESG ADIISVVTDI TLHDDPEARV KSWLEVTR // ID D5C2V5_NITHN Unreviewed; 217 AA. AC D5C2V5; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Nhal_3764; OS Nitrosococcus halophilus (strain Nc4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=472759; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nc4; RG US DOE Joint Genome Institute; RA Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., RA Ward B.B., Klotz M.G.; RT "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt- RT adapted, aerobic obligate ammonia-oxidizing sulfur purple bacterium."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001798; ADE16780.1; -; Genomic_DNA. DR RefSeq; YP_003529167.1; NC_013960.1. DR ProteinModelPortal; D5C2V5; -. DR EnsemblBacteria; ADE16780; ADE16780; Nhal_3764. DR GeneID; 8918780; -. DR KEGG; nhl:Nhal_3764; -. DR PATRIC; 35397673; VBINitHal115488_3944. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR BioCyc; NHAL472759:GHH2-3816-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23386 MW; 7AF7E4916DD6C02E CRC64; MNELIRGLYA IADTHLLPHQ DLGNAVALAL LGGASLIQYR DKSQEEKRRY QEAKSLQQIC RQHQVPLIIN DDTLLAAEIG ADGVHLGRDD LAPSSARQIL GADAIIGVSC YNELARAIAA EQAGADYVAF GRFFPSRTKP EAIQASLELL REARKKLKLP IVAIGGITTE NAPQVIEAGA NAVAIIGGLF KSQDIRATAA AYQQQFLSQH LPAPHSF // ID D5C3F8_NITHN Unreviewed; 318 AA. AC D5C3F8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=Nhal_3853; OS Nitrosococcus halophilus (strain Nc4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=472759; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nc4; RG US DOE Joint Genome Institute; RA Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., RA Ward B.B., Klotz M.G.; RT "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt- RT adapted, aerobic obligate ammonia-oxidizing sulfur purple bacterium."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001798; ADE16865.1; -; Genomic_DNA. DR RefSeq; YP_003529252.1; NC_013960.1. DR ProteinModelPortal; D5C3F8; -. DR EnsemblBacteria; ADE16865; ADE16865; Nhal_3853. DR GeneID; 8918869; -. DR KEGG; nhl:Nhal_3853; -. DR PATRIC; 35397853; VBINitHal115488_4034. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; NHAL472759:GHH2-3905-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 318 AA; 34873 MW; F3C591EDE8F2BB87 CRC64; MILQVAAGAI FNGQGQVLLS KRPPHVHQGN LWEFPGGKLN PGESVAQALS RELWEELGIR VLQARPLLQV HHDYPDRSVR LHTWRVDRFS GEARGQEGQP VEWVWPADLS SYPFPAANQP IVAAVRLPPT YLITGEPIGD PAVFLDRLLQ SLRAGVRLVQ LRAKNLSPLH YQTLARAARR LCLEHGAILL LNTSPAQAVE LGADGVHLTS DRLMCLSRRP LAADRWVAAS CHNPDQLAHA ARIGVDFAVL GPVLETLSHP QASPLGWERF QTLVAQVPFP VYALGGMGLE HLEEAWYCGA QGIAAIRGLW SPPLRVSS // ID D5CBM3_ENTCC Unreviewed; 211 AA. AC D5CBM3; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECL_00254; OS Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / OS NBRC 13535 / NCDC 279-56). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=716541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56; RX PubMed=20207761; DOI=10.1128/JB.00067-10; RA Ren Y., Ren Y., Zhou Z., Guo X., Li Y., Feng L., Wang L.; RT "Complete genome sequence of Enterobacter cloacae subsp. cloacae type RT strain ATCC 13047."; RL J. Bacteriol. 192:2463-2464(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001918; ADF59821.1; -; Genomic_DNA. DR RefSeq; YP_003610770.1; NC_014121.1. DR ProteinModelPortal; D5CBM3; -. DR EnsemblBacteria; ADF59821; ADF59821; ECL_00254. DR GeneID; 9122764; -. DR KEGG; enc:ECL_00254; -. DR PATRIC; 38451538; VBIEntClo148801_0542. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; ECLO716541:GH13-259-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22860 MW; A54A8514D8785F48 CRC64; MYQPDFPCVP FRLGLYPVVD SVAWIERLLA CGVRTIQLRI KDKRDDEVEA DVVAAIALGR RYDARLFIND YWRLAVKHQA YGVHLGQEDL ETTDLSAIRD AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLTQLA AHVKRLADYP TVAIGGISLE RAPAVLDTGV GSIAVVSAIT QAADWQAATA QLLKLAGAGD E // ID D5CP08_SIDLE Unreviewed; 312 AA. AC D5CP08; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Slit_2704; OS Sideroxydans lithotrophicus (strain ES-1). OC Bacteria; Proteobacteria; Betaproteobacteria; Gallionellales; OC Gallionellaceae; Sideroxydans. OX NCBI_TaxID=580332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ES-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., RA Land M., Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.; RT "Complete sequence of Sideroxydans lithotrophicus ES-1."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001965; ADE12929.1; -; Genomic_DNA. DR RefSeq; YP_003525316.1; NC_013959.1. DR ProteinModelPortal; D5CP08; -. DR EnsemblBacteria; ADE12929; ADE12929; Slit_2704. DR GeneID; 8893410; -. DR KEGG; slt:Slit_2704; -. DR PATRIC; 35403526; VBISidLit69165_2673. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR BioCyc; SLIT580332:GH9F-2756-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 312 AA; 34246 MW; 3A1C2D15223802E4 CRC64; MPENKCIEVS AAVLQRPDGS FLLAQRPPGK IWAGYWEFPG GKIEPGETAH DALVRELHEE LGITVQTAYP WLTRVFTYPH ATVHLNFFRV TTWTGELHPH EGQQFSWQHP AGVLVDPVLP ANTPILRALT LPALYAISNA AELGTEQFLL KLEARLDDGL QLIQVREKDL SRDRLRELAL KVVALAHARG ARVLLNGDIE MAREVGADGV QLTSSQLAAL KLRPAIDWCA ASCHNAEELR RAEALGCDFA LLSPVLPTRS HLGASYLGWE RFAALAGGST IPVYALGGLS QADMQMAWQH GAHGISLLRQ AW // ID D5CTH6_SIDLE Unreviewed; 210 AA. AC D5CTH6; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Slit_0040; OS Sideroxydans lithotrophicus (strain ES-1). OC Bacteria; Proteobacteria; Betaproteobacteria; Gallionellales; OC Gallionellaceae; Sideroxydans. OX NCBI_TaxID=580332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ES-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., RA Land M., Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.; RT "Complete sequence of Sideroxydans lithotrophicus ES-1."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001965; ADE10282.1; -; Genomic_DNA. DR RefSeq; YP_003522669.1; NC_013959.1. DR ProteinModelPortal; D5CTH6; -. DR EnsemblBacteria; ADE10282; ADE10282; Slit_0040. DR GeneID; 8890695; -. DR KEGG; slt:Slit_0040; -. DR PATRIC; 35398160; VBISidLit69165_0040. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SLIT580332:GH9F-40-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22167 MW; 163B7DBBEAE0BFFB CRC64; MKQHQHITGL YAITPDILDT DELLRSVRLA LRGGAHVLQY RNKAADTALK LAQAHALRQL TREFGAIFIV NDDAGLAAQV DADGVHLGGE DGSVVAARAL LGDSRIVGVS CYNRFPLAHE AVRLGADYVA FGAFFSSSVK PEAVQADVAL LRSARKELNV PIVAIGGITQ QNAATLIEAG ADAVAVISAL WNAPDIEASA HGFSTLFSRT // ID D5D6I6_ECOKI Unreviewed; 211 AA. AC D5D6I6; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECOK1_4469; OS Escherichia coli O18:K1:H7 (strain IHE3034 / ExPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=714962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IHE3034 / ExPEC; RX PubMed=20439758; DOI=10.1073/pnas.0915077107; RA Moriel D.G., Bertoldi I., Spagnuolo A., Marchi S., Rosini R., RA Nesta B., Pastorello I., Corea V.A., Torricelli G., Cartocci E., RA Savino S., Scarselli M., Dobrindt U., Hacker J., Tettelin H., RA Tallon L.J., Sullivan S., Wieler L.H., Ewers C., Pickard D., RA Dougan G., Fontana M.R., Rappuoli R., Pizza M., Serino L.; RT "Identification of protective and broadly conserved vaccine antigens RT from the genome of extraintestinal pathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 107:9072-9077(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IHE3034; RA Moriel D.G., Bertoldi I., Spagnuolo A., Marchi S., Rosini R., RA Nesta B., Pastorello I., Mariani Corea V.A., Torricelli G., RA Cartocci E., Savino S., Scarselli M., Dobrindt U., Hacker J., RA Tettelin H., Wieler L.H., Ewers C., Picard D., Dougan G., RA Fontana M.R., Rappuoli R., Pizza M., Serino L.; RT "Identification of protective and broadly conserved vaccine antigens RT from the genome of Extraintestinal Pathogenic Escherichia coli RT (ExPEC)."; RL Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001969; ADE89397.1; -; Genomic_DNA. DR RefSeq; YP_006103535.1; NC_017628.1. DR ProteinModelPortal; D5D6I6; -. DR SMR; D5D6I6; 9-208. DR EnsemblBacteria; ADE89397; ADE89397; ECOK1_4469. DR GeneID; 12693035; -. DR KEGG; eih:ECOK1_4469; -. DR PATRIC; 36710483; VBIEscCol148715_4499. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; ECOL714962:GI9T-4467-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D5DAP5_BACMD Unreviewed; 207 AA. AC D5DAP5; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=BMD_0551; OS Bacillus megaterium (strain DSM 319). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=592022; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 319; RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., RA Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., RA Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., RA Vary P.S.; RT "Genome sequences of the industrial vitamin B12-producers B. RT megaterium QM B1551 and DSM319 reveal new insights into the Bacillus RT genome evolution and pan-genome structure."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001982; ADF37437.1; -; Genomic_DNA. DR RefSeq; YP_003595787.1; NC_014103.1. DR ProteinModelPortal; D5DAP5; -. DR EnsemblBacteria; ADF37437; ADF37437; BMD_0551. DR GeneID; 9115942; -. DR KEGG; bmd:BMD_0551; -. DR PATRIC; 37251061; VBIBacMeg104484_0480. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR BioCyc; BMEG592022:GIVX-551-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 207 AA; 22256 MW; 46CC810023831E96 CRC64; MDIPKFHVIT TDKQPIEELQ KVLTAIAPFA GAVHIREKEK TAKQIQCLLE SLPFCRSKII VNDRVDVAHA LKAKGVQLAY HSLDVSVVID AFPSLIVGKS VHSVEEALEA EKDGAHYILY GHIYSTHSKK GLKSRGVAAL KEVVDAVQIP VIAIGGITPV NAKEVLQTGA HGIAVMSGVM LAQDPLKAIK QYSHIWTSGG GENEAAL // ID D5DFG9_BACMD Unreviewed; 214 AA. AC D5DFG9; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BMD_2116; OS Bacillus megaterium (strain DSM 319). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=592022; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 319; RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., RA Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., RA Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., RA Vary P.S.; RT "Genome sequences of the industrial vitamin B12-producers B. RT megaterium QM B1551 and DSM319 reveal new insights into the Bacillus RT genome evolution and pan-genome structure."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001982; ADF38969.1; -; Genomic_DNA. DR RefSeq; YP_003597319.1; NC_014103.1. DR ProteinModelPortal; D5DFG9; -. DR EnsemblBacteria; ADF38969; ADF38969; BMD_2116. DR GeneID; 9117507; -. DR KEGG; bmd:BMD_2116; -. DR PATRIC; 37254281; VBIBacMeg104484_2066. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; BMEG592022:GIVX-2116-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23045 MW; FF96DCE3FA77BE1F CRC64; MTNEEIKKLL QVYFIMGSNN CTKDPKEVLK EAIEGGVTVF QFREKGEGAL TGEAKYQLAK ELQQICQQHS VPFVVNDDLD LAIRLQADGV HIGQEDEKAH IVREKIGKGI VGVSVHNVQE LQQAIKDGAD YVGMGPVFPT STKKDAKAVQ GTKLIEEVRN QNIDFPIVGI GGITPENAKQ VVEAGADGVS IITAISLAAS PKEKAAQLKE AVGK // ID D5DR38_BACMQ Unreviewed; 214 AA. AC D5DR38; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BMQ_2159; OS Bacillus megaterium (strain ATCC 12872 / QMB1551). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=545693; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12872 / QMB1551; RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., RA Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., RA Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., RA Vary P.S.; RT "Genome sequences of the industrial vitamin B12-producers B. RT megaterium QM B1551 and DSM319 reveal new insights into the Bacillus RT genome evolution and pan-genome structure."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001983; ADE69188.1; -; Genomic_DNA. DR RefSeq; YP_003562622.1; NC_014019.1. DR ProteinModelPortal; D5DR38; -. DR EnsemblBacteria; ADE69188; ADE69188; BMQ_2159. DR GeneID; 8986597; -. DR KEGG; bmq:BMQ_2159; -. DR PATRIC; 35481028; VBIBacMeg35839_2188. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; BMEG545693:GHSY-2159-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23072 MW; 36B746C853562E0D CRC64; MTNEEIKKLL QVYFIMGSNN CKKDPKEVLK EAIEGGVTVF QFREKGEGAL TGEAKYQLAK ELQQICQQHS VPFVVNDDLD LAIRLQADGV HIGQEDEKAH IVREKIGKGI VGVSVHNVQE LQQAIKDGAD YVGMGPVFPT STKKDAKAVQ GTKLIEEVRN QNIDFPIVGI GGITPENAKQ VVEAGADGVS IITAISLAAS PKEKAAQLKE AVGK // ID D5DYW3_BACMQ Unreviewed; 207 AA. AC D5DYW3; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=BMQ_0548; OS Bacillus megaterium (strain ATCC 12872 / QMB1551). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=545693; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12872 / QMB1551; RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., RA Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., RA Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., RA Vary P.S.; RT "Genome sequences of the industrial vitamin B12-producers B. RT megaterium QM B1551 and DSM319 reveal new insights into the Bacillus RT genome evolution and pan-genome structure."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001983; ADE67605.1; -; Genomic_DNA. DR RefSeq; YP_003561039.1; NC_014019.1. DR ProteinModelPortal; D5DYW3; -. DR EnsemblBacteria; ADE67605; ADE67605; BMQ_0548. DR GeneID; 8984986; -. DR KEGG; bmq:BMQ_0548; -. DR PATRIC; 35477717; VBIBacMeg35839_0556. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR BioCyc; BMEG545693:GHSY-548-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 207 AA; 22298 MW; 8CE804D56BC4E314 CRC64; MDIPKFHVIT TDKQPIEELQ KILTAIAPFA GAVHIREKEK TAKQIQCLLE SLPFCRSKII LNDRVDVAHA LKAKGVQLAY HSLDVSVVID AFPSLIVGKS VHSVEEALEA EKDGAHYILY GHIYSTHSKK GLKSRGIAAL KEVVDAVQIP VIAIGGITPV NAKEVLQTGA HGIAVMSGVM LAQDPLKAIK QYSHIWTSGG GENEAAL // ID D5EBA6_METMS Unreviewed; 220 AA. AC D5EBA6; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mmah_0937; OS Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanohalophilus. OX NCBI_TaxID=547558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35705 / DSM 5219 / SLP; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Spring S., Schneider S., Schroeder M., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of Methanohalophilus mahii DSM 5219."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001994; ADE36457.1; -; Genomic_DNA. DR RefSeq; YP_003542102.1; NC_014002.1. DR ProteinModelPortal; D5EBA6; -. DR EnsemblBacteria; ADE36457; ADE36457; Mmah_0937. DR GeneID; 8983102; -. DR KEGG; mmh:Mmah_0937; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HRFYFIT; -. DR BioCyc; MMAH547558:GHP5-972-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24156 MW; B4E4DB42BCB661A4 CRC64; MAFWKSLLKD IDFYLVTDSG LSRKGTLSDV KCAVAAGCKI VQYREKDKTT KEMIEEAILI RKICGENAIF LVNDRIDVAL AAGADGVHIG QDDMPIDSAR RILGENKIIG LTVHDTDEAI EAERKGADYV GFSPVFDTTT KKDAGMGVGP ERIQAVRKTI NIPIVAIGGI NKDNCISVIE KGVDSLVAIS AIVCSDDVRR ETEYFIETIR KTKQKYIQQS // ID D5ECX0_AMICL Unreviewed; 207 AA. AC D5ECX0; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Amico_0257; OS Aminobacterium colombiense (strain DSM 12261 / ALA-1). OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Aminobacterium. OX NCBI_TaxID=572547; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12261 / ALA-1; RX DOI=10.4056/sigs.902116; RA Chertkov O., Sikorski J., Brambilla E., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J., Han C., RA Detter J., Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Spring S., RA Rohde M., Goker M., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H.; RT "Complete genome sequence of Aminobacterium colombiense type strain RT (ALA-1)."; RL Stand. Genomic Sci. 2:280-289(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001997; ADE56402.1; -; Genomic_DNA. DR RefSeq; YP_003553126.1; NC_014011.1. DR ProteinModelPortal; D5ECX0; -. DR EnsemblBacteria; ADE56402; ADE56402; Amico_0257. DR GeneID; 8963155; -. DR KEGG; aco:Amico_0257; -. DR PATRIC; 35452652; VBIAmiCol31354_0268. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; ACOL572547:GHQ0-257-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22125 MW; 0F65C0CF547308E6 CRC64; MNIRHMLKLY VIPDRQIGAP RTLLEQTEEV LKGGATVIQL RDKQSGGREL LETALAMKRL CYDYNVPLII NDRLDVALAA QADGVHLGQK DLPLEAVRPF LPRGFIVGVS AHTVDQARIA LKSGASYIGI GAAFPTGSKE DAHVVGLSRI REIMEAVPIP AVAIGGINEE NVAEAMKTGV NGVAVISAIV GAPHIKKAAR HFLSLIS // ID D5EPX6_CORAD Unreviewed; 197 AA. AC D5EPX6; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-APR-2014, entry version 24. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Caka_2694; OS Coraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 OS / KCTC 12865). OC Bacteria; Verrucomicrobia; Opitutae; Puniceicoccales; OC Puniceicoccaceae; Coraliomargarita. OX NCBI_TaxID=583355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865; RX PubMed=21304713; DOI=10.4056/sigs.952166; RA Mavromatis K., Abt B., Brambilla E., Lapidus A., Copeland A., RA Deshpande S., Nolan M., Lucas S., Tice H., Cheng J.F., Han C., RA Detter J.C., Woyke T., Goodwin L., Pitluck S., Held B., Brettin T., RA Tapia R., Ivanova N., Mikhailova N., Pati A., Liolios K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Coraliomargarita akajimensis type strain RT (04OKA010-24)."; RL Stand. Genomic Sci. 2:290-299(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001998; ADE55709.1; -; Genomic_DNA. DR RefSeq; YP_003549879.1; NC_014008.1. DR ProteinModelPortal; D5EPX6; -. DR EnsemblBacteria; ADE55709; ADE55709; Caka_2694. DR GeneID; 8959854; -. DR KEGG; caa:Caka_2694; -. DR PATRIC; 35446052; VBICorAka2911_2675. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR BioCyc; CAKA583355:GI4D-2742-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 197 AA; 21923 MW; F2EE290763E8190D CRC64; MMHLLAVSPE SEYADEPALV VRLFDAGLAR YHLRKPDWSR EQCAEWLQAI PMGLHALISV HQHHDLAKEF GVGLHFRDDG QRLDHEARFG VGPLVRSRSL HELERLSERV EGMAYTFLSP IFASISKQGY KPDWTEAELR AALAGPRSSK LYALGGITAE NLAQVGELGF DGAVLHGCLW QANDPIAAFD VVRKEAL // ID D5EPX7_CORAD Unreviewed; 209 AA. AC D5EPX7; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Caka_2695; OS Coraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 OS / KCTC 12865). OC Bacteria; Verrucomicrobia; Opitutae; Puniceicoccales; OC Puniceicoccaceae; Coraliomargarita. OX NCBI_TaxID=583355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865; RX PubMed=21304713; DOI=10.4056/sigs.952166; RA Mavromatis K., Abt B., Brambilla E., Lapidus A., Copeland A., RA Deshpande S., Nolan M., Lucas S., Tice H., Cheng J.F., Han C., RA Detter J.C., Woyke T., Goodwin L., Pitluck S., Held B., Brettin T., RA Tapia R., Ivanova N., Mikhailova N., Pati A., Liolios K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Coraliomargarita akajimensis type strain RT (04OKA010-24)."; RL Stand. Genomic Sci. 2:290-299(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001998; ADE55710.1; -; Genomic_DNA. DR RefSeq; YP_003549880.1; NC_014008.1. DR ProteinModelPortal; D5EPX7; -. DR EnsemblBacteria; ADE55710; ADE55710; Caka_2695. DR GeneID; 8959855; -. DR KEGG; caa:Caka_2695; -. DR PATRIC; 35446054; VBICorAka2911_2676. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IGISCHT; -. DR BioCyc; CAKA583355:GI4D-2743-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22587 MW; FCD5812C4A6D7CD4 CRC64; MNWPKLMCLT TDGVSLSHSE QVQALCSAGV DWIQLRSKEL SDAELEPIAF ECLIRCREVG ATFVLNDRVE LALNIGADGV HIGKQDMAWR EARKLAGADF IIGGTVNSID DAQSAIESDV LDYVGVGPFK FTQTKQNLAP VLSDPEWVAI VQTLGELPSY AIGGIEARDL ERVNQLGVNG AAVCSVLYRD GTVMENYKAL LEGMNVGVS // ID D5EX07_PRER2 Unreviewed; 212 AA. AC D5EX07; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PRU_0400; OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=264731; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19189 / JCM 8958 / 23; RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8; RG North American Consortium for Rumen Bacteria; RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I., RA Coutinho P.M., Henrissat B., Nelson K.E.; RT "Comparative genome analysis of Prevotella ruminicola and Prevotella RT bryantii: insights into their environmental niche."; RL Microb. Ecol. 60:721-729(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002006; ADE83723.1; -; Genomic_DNA. DR RefSeq; YP_003573776.1; NC_014033.1. DR ProteinModelPortal; D5EX07; -. DR EnsemblBacteria; ADE83723; ADE83723; PRU_0400. DR GeneID; 9000528; -. DR KEGG; pru:PRU_0400; -. DR PATRIC; 35494961; VBIPreRum14515_0385. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; PRUM264731:GHX6-385-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23361 MW; 76C4DC1AAF3DE1DA CRC64; MRGVRAMLQF ISHYTDKYSY LDSIRLALQG GCRWIQLRMK DATDDEVRPV AIEAQKLCKQ YGATFIIDDR VALVKELQAD GVHLGKNDMP ISEARRQLGP DYIIGGTANT IWDVKAHYAA GADYIGCGPF RFTTTKQKLS PVLGLDGYRR IIIEMRAAHI DIPIVAIGGI TKDDIPAILA TGITGIALSG TVLRAANPID EMKHLTNIVN HE // ID D5EX12_PRER2 Unreviewed; 178 AA. AC D5EX12; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=PRU_0405; OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=264731; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19189 / JCM 8958 / 23; RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8; RG North American Consortium for Rumen Bacteria; RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I., RA Coutinho P.M., Henrissat B., Nelson K.E.; RT "Comparative genome analysis of Prevotella ruminicola and Prevotella RT bryantii: insights into their environmental niche."; RL Microb. Ecol. 60:721-729(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002006; ADE83012.1; -; Genomic_DNA. DR RefSeq; YP_003573781.1; NC_014033.1. DR ProteinModelPortal; D5EX12; -. DR EnsemblBacteria; ADE83012; ADE83012; PRU_0405. DR GeneID; 9002571; -. DR KEGG; pru:PRU_0405; -. DR PATRIC; 35494971; VBIPreRum14515_0390. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR BioCyc; PRUM264731:GHX6-390-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 178 AA; 19703 MW; 66E76BDE0347ED48 CRC64; MIIVITRPDF FEGEAAKIAQ LLQSGRADLV HIRKPRASQS EVEQLLFSIP TELYSRLVLH DHHSLAIKYG LRGVHLNSRN PEPPAGWSGA VSISCHTLSE LSECRRKPYA YMSLSPIFDS ISKRGYRSAF SADDIAAARS QGLIDERVMA LGGITFDKIT EIKEMGFGGA MILGDAWR // ID D5EYI5_PRER2 Unreviewed; 202 AA. AC D5EYI5; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE SubName: Full=Thiamine-phosphate pyrophosphorylase-like protein; GN OrderedLocusNames=PRU_0674; OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=264731; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19189 / JCM 8958 / 23; RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8; RG North American Consortium for Rumen Bacteria; RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I., RA Coutinho P.M., Henrissat B., Nelson K.E.; RT "Comparative genome analysis of Prevotella ruminicola and Prevotella RT bryantii: insights into their environmental niche."; RL Microb. Ecol. 60:721-729(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002006; ADE81422.1; -; Genomic_DNA. DR RefSeq; YP_003574034.1; NC_014033.1. DR ProteinModelPortal; D5EYI5; -. DR EnsemblBacteria; ADE81422; ADE81422; PRU_0674. DR GeneID; 9000202; -. DR KEGG; pru:PRU_0674; -. DR PATRIC; 35495495; VBIPreRum14515_0644. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR BioCyc; PRUM264731:GHX6-651-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 23364 MW; AC182D73668D14F6 CRC64; MKLIVMTKPT FFVEEDKILV NLFEEGLDNL HLYKPGASPM YSERLLTLLG DDYHNRITVH GHFYLKEEYR LRGIHIDDAF TEAPVGYKGN ISRTCHAISE LKETKKKSNY VFLHSIFDSQ TNADEKQSFT MDELRAASKQ GLIDKKVYAL GGMNLDRVKE IKDLGFGGMV ICGDLWNRFN IHNEIDYKAL LNHFEKLRKT ID // ID D5G605_TUBMM Unreviewed; 540 AA. AC D5G605; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-APR-2014, entry version 22. DE SubName: Full=Whole genome shotgun sequence assembly, scaffold_116, strain Mel28; GN ORFNames=GSTUM_00001710001; OS Tuber melanosporum (strain Mel28) (Perigord black truffle). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes; OC Pezizales; Tuberaceae; Tuber. OX NCBI_TaxID=656061; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mel28; RX PubMed=20348908; DOI=10.1038/nature08867; RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., RA Jaillon O., Montanini B., Morin E., Noel B., Percudani R., Porcel B., RA Rubini A., Amicucci A., Amselem J., Anthouard V., Arcioni S., RA Artiguenave F., Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., RA Buee M., Cantarel B., Chevalier G., Couloux A., Da Silva C., RA Denoeud F., Duplessis S., Ghignone S., Hilselberger B., Iotti M., RA Marcais B., Mello A., Miranda M., Pacioni G., Quesneville H., RA Riccioni C., Ruotolo R., Splivallo R., Stocchi V., Tisserant E., RA Viscomi A.R., Zambonelli A., Zampieri E., Henrissat B., Lebrun M.H., RA Paolocci F., Bonfante P., Ottonello S., Wincker P.; RT "Perigord black truffle genome uncovers evolutionary origins and RT mechanisms of symbiosis."; RL Nature 464:1033-1038(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN430005; CAZ79948.1; -; Genomic_DNA. DR RefSeq; XP_002835791.1; XM_002835745.1. DR ProteinModelPortal; D5G605; -. DR EnsemblFungi; CAZ79948; CAZ79948; GSTUM_00001710001. DR GeneID; 9187626; -. DR KEGG; tml:GSTUM_00001710001; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 540 AA; 57496 MW; F9693E232125F979 CRC64; MPPPRPNLEL YLVTDSVNLP FNSTVYSQVE ACLSAKHPPT IVQLREKHLS TAKFIELARD IYALTSKNGV PLLINDRVDV ALAVGCEGVH LGWDDIDVPT ARKLLGPEKI IGLSVSNHEQ LEKALGLDPT YLGIGPVFST PTKPDHNPPL GTSGVRSLLS AIPITMQAVA IGGINHGNVQ RVLFQSKDIS GRRLDGVAVV SAIMASPLPV GACNLLHETV NWPPLFVPTD YSLRTEDFPI YRDNIHKHKP LVHHITNNVV KSISANISLA IGASPIMSEN PAEFADLAAL PNVGCVLNMG TFASSKESQD LFLGALREHN VRGNPVIFDP VGAGATNARR EFAQMIVGAG YCTVIKGNEG EIRSLAGLET AKMRGVDGAG EGGSEEELAK VVHDLASLEN NIVLMTGPKD YISNGARTFC LTNGSAYQSR VTGVGCALGS VIAAFCAAAP VDESLIGPVI SAIGMYNIAA ERAEKLMESG DQPGKWAAAF VDCLAVMAMS DENLTELISV HEVKELANLE KWGRPTGREG LKQGEDLTEA // ID D5H8J3_SALRM Unreviewed; 212 AA. AC D5H8J3; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=SRM_01427; OS Salinibacter ruber (strain M8). OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Salinibacter. OX NCBI_TaxID=761659; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M8; RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P., RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I., RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R., RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.; RT "Fine-scale evolution: genomic, phenotypic and ecological RT differentiation in two coexisting Salinibacter ruber strains."; RL ISME J. -:0-0(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M8; RG Genoscope; RT "Genome sequence of Salinibacter ruber M8."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP565814; CBH24348.1; -; Genomic_DNA. DR RefSeq; YP_003571300.1; NC_014032.1. DR ProteinModelPortal; D5H8J3; -. DR EnsemblBacteria; CBH24348; CBH24348; SRM_01427. DR GeneID; 8996669; -. DR KEGG; srm:SRM_01427; -. DR PATRIC; 35490670; VBISalRub49863_1333. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SRUB761659:GHC6-1443-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 212 AA; 22449 MW; A7EA8EC8E6E83929 CRC64; MLMAALPYPR LALIADGFTN DARADRGVEA VRAGVRWVHL RDHEASPEAF ATAAHALADR LQTAADDVTI TVNTRVDVAD ALGSGAHIGW RGPSVGETRE RLGPEALIGY SAHEHVEAEG DRTQGVDYYF FSPVFPTTSK PDRPPTGIGP LRAFCRVAAP VPVLALGGIT PERVSVCREA GAHGVAVLSG IMNVDTPRAA ARAYLRALAE HA // ID D5H9G6_SALRM Unreviewed; 252 AA. AC D5H9G6; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SRM_01750; OS Salinibacter ruber (strain M8). OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Salinibacter. OX NCBI_TaxID=761659; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M8; RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P., RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I., RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R., RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.; RT "Fine-scale evolution: genomic, phenotypic and ecological RT differentiation in two coexisting Salinibacter ruber strains."; RL ISME J. -:0-0(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M8; RG Genoscope; RT "Genome sequence of Salinibacter ruber M8."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP565814; CBH24671.1; -; Genomic_DNA. DR RefSeq; YP_003571623.1; NC_014032.1. DR ProteinModelPortal; D5H9G6; -. DR EnsemblBacteria; CBH24671; CBH24671; SRM_01750. DR GeneID; 8994755; -. DR KEGG; srm:SRM_01750; -. DR PATRIC; 35491310; VBISalRub49863_1649. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SRUB761659:GHC6-1770-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 75 79 HMP-PP binding (By similarity). FT REGION 172 174 THZ-P binding (By similarity). FT REGION 223 224 THZ-P binding (By similarity). FT METAL 108 108 Magnesium (By similarity). FT METAL 127 127 Magnesium (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 HMP-PP (By similarity). FT BINDING 203 203 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 252 AA; 26592 MW; B1B559CB23BA6A25 CRC64; MPSGTAAKLR SEGTVRYRRD APTSVMENTS TNGEPTRAEK SIGRLHVLTD FHLQQDRSHA ELARLAIRGG ADTVQFRQKH GGIQNKLLEA RKVATVCADA STPLLIDDHL DIAQATDADG VHLGRDDFPI DAARSVLGPS PIIGGTASKP HEAAEAYEQG ADYIGFGPVF PTTSKRNPKS VKGPDGLADA CEAVPIPVIA IGGITHDRVR SVLEAGAHGV AVLSAVDTAR NPEQATARFR AAIDGVLREA DS // ID D5HHG8_9FIRM Unreviewed; 215 AA. AC D5HHG8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CCU_03370; OS Coprococcus sp. ART55/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=751585; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ART55/1; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Coprococcus sp. ART55/1."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929039; CBK82223.1; -; Genomic_DNA. DR RefSeq; YP_007795554.1; NC_021018.1. DR ProteinModelPortal; D5HHG8; -. DR EnsemblBacteria; CBK82223; CBK82223; CCU_03370. DR GeneID; 15195272; -. DR KEGG; coo:CCU_03370; -. DR PATRIC; 42889008; VBICopSp152499_1844. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23284 MW; C8588B60BACB94C7 CRC64; MYTFDPTLYF ITDSTGLSEE EFLYRVECAL DGGATLMQLR EKERTTREYI HLADKVHSIA RRYNVPLIID DRVDVALAAD SEGVHVGQTD MPVSIARKLM GSDRIVGATT KTVPQAVEAY EQGADYLGVG AIYPTTTKVK TVLTSTDTLR DICKAVPIPV NAIGGLNPTN LDVLSGIPIA GICVVSAIMK ADNPKDAASR LLALSRQLQS KISLK // ID D5MFD0_9BACT Unreviewed; 214 AA. AC D5MFD0; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DAMO_1399; OS Candidatus Methylomirabilis oxyfera. OC Bacteria; candidate division NC10; Candidatus Methylomirabilis. OX NCBI_TaxID=671143; RN [1] RP NUCLEOTIDE SEQUENCE. RA Genoscope - CEA; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RX DOI=10.1038/nature08883; RA Ettwig K.F., Butler M.K., Le Paslier D., Pelletier E., Mangenot S., RA Kuypers M.M.M., Schreiber F., Dutilh B.E., Zedelius J., de Beer D., RA Gloerich J., Wessels H.J.C.T., van Allen T., Luesken F., Wu M., RA van de Pas-Schoonen K.T., Op den Camp H.J.M., Janssen-Megens E.M., RA Francoijs K-J., Stunnenberg H., Weissenbach J., Jetten M.S.M., RA Strous M.; RT "Nitrite-driven anaerobic methane oxidation by oxygenic bacteria."; RL Nature 464:543-548(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP565575; CBE68459.1; -; Genomic_DNA. DR RefSeq; YP_003206294.1; NC_013260.1. DR ProteinModelPortal; D5MFD0; -. DR GeneID; 13098905; -. DR KEGG; mox:DAMO_1399; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22298 MW; AA49B9397655E698 CRC64; MIAPQACRLC VITNRQLGHG LSHFDIAARA IDGGATMIQL RDKAAGPRQL LSDARRIARL CRERGVRFIV NDRLDLALAA DADGVHLGQD DLPPHAARAV LGTNKVLGVS THSLEQALEA AEQGADYLGI GPIFATGTKA TGYEPRGCDI IRQLRARIDL PLIAIGGIAL SNVGEAMAAG ATGVAVISAI VGADDITAAT QAFATAIRQV EGKH // ID D5MJQ2_9BACT Unreviewed; 189 AA. AC D5MJQ2; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DAMO_2564; OS Candidatus Methylomirabilis oxyfera. OC Bacteria; candidate division NC10; Candidatus Methylomirabilis. OX NCBI_TaxID=671143; RN [1] RP NUCLEOTIDE SEQUENCE. RA Genoscope - CEA; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RX DOI=10.1038/nature08883; RA Ettwig K.F., Butler M.K., Le Paslier D., Pelletier E., Mangenot S., RA Kuypers M.M.M., Schreiber F., Dutilh B.E., Zedelius J., de Beer D., RA Gloerich J., Wessels H.J.C.T., van Allen T., Luesken F., Wu M., RA van de Pas-Schoonen K.T., Op den Camp H.J.M., Janssen-Megens E.M., RA Francoijs K-J., Stunnenberg H., Weissenbach J., Jetten M.S.M., RA Strous M.; RT "Nitrite-driven anaerobic methane oxidation by oxygenic bacteria."; RL Nature 464:543-548(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP565575; CBE69637.1; -; Genomic_DNA. DR RefSeq; YP_003207438.1; NC_013260.1. DR ProteinModelPortal; D5MJQ2; -. DR GeneID; 13097681; -. DR KEGG; mox:DAMO_2564; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 15 19 HMP-PP binding (By similarity). FT REGION 112 114 THZ-P binding (By similarity). FT REGION 163 164 THZ-P binding (By similarity). FT BINDING 47 47 HMP-PP (By similarity). FT BINDING 86 86 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 143 143 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 189 AA; 19518 MW; 1AEBF69B372EFE1B CRC64; MVIEAALAGG AKAIQLREKD LSTRDLYQLV ERLLPIVRGR GASLLINDRV DLTLALPIDG VHLSRTSLPP AEARALLGPA RLVGVSCHSL EEVIEAERGG ADFIVFGPLF PTPSKAAYGP PVGLMRLSEV RRQVRLPILG IGGVTVVNVA SVVAAGADGA AMISAVMTAD DPADAVSSLL QVVRSAAGG // ID D5N0J8_BACPN Unreviewed; 220 AA. AC D5N0J8; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-MAR-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSU6633_10231; OS Bacillus subtilis subsp. spizizenii ATCC 6633. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=703612; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 6633; RA Metcalf W.W., Zhang J.K., Borisova S.A.; RT "The complete genome sequence of the gram-positive bacterium Bacillus RT subtilis ATCC 6633."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGS01000016; EFG92464.1; -; Genomic_DNA. DR ProteinModelPortal; D5N0J8; -. DR EnsemblBacteria; EFG92464; EFG92464; BSU6633_10231. DR PATRIC; 37935447; VBIBacSub155824_2022. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23652 MW; 31370F7877001EA7 CRC64; MTRISREMMK ELLSVYFIMG SNNTKADPVT VVQKALKGGA TLYQFREKGG DALTGEARIE FAKKVQEACR EAGIPFIVND DVELALKLKA DGIHIGQEDA NAKEVRDAIG DMILGVSTHT MSEVKQAEED GADYVGLGPI YPTETKKDTR AVQGVSLIEA VRRQGIDIPI VGIGGITIEN AAPVIQAGAD GVSMISAISQ AEDPEGAARK FHEEVQTPRR // ID D5N3B2_BACPN Unreviewed; 163 AA. AC D5N3B2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-MAR-2014, entry version 19. DE SubName: Full=Transcriptional regulator TenI; GN ORFNames=BSU6633_15842; OS Bacillus subtilis subsp. spizizenii ATCC 6633. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=703612; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 6633; RA Metcalf W.W., Zhang J.K., Borisova S.A.; RT "The complete genome sequence of the gram-positive bacterium Bacillus RT subtilis ATCC 6633."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGS01000027; EFG91394.1; -; Genomic_DNA. DR ProteinModelPortal; D5N3B2; -. DR EnsemblBacteria; EFG91394; EFG91394; BSU6633_15842. DR PATRIC; 37937762; VBIBacSub155824_3147. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 163 AA; 18058 MW; 994ED94B726B43C4 CRC64; MKLLGLISEG GVDKRKLIMN GRVDIALFST IHRVQLPSSS FSPKQVRARF PHLHIGRSVH SLEEAVQAEK EDADYVLFGH VFETDCKKGL EGRGVSLLSD IKQRISVPVI AIGGMTPDRL RDVKRAGAEG IAVMSGIFSS ADPLEAARRY SRKLKEMRYE KAL // ID D5NX49_CORAM Unreviewed; 218 AA. AC D5NX49; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0281_01162; OS Corynebacterium ammoniagenes DSM 20306. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=649754; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20306; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Wollam A., Pepin K.H., Johnson M., Bhonagiri V., RA Zhang X., Suruliraj S., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNS01000008; EFG81605.1; -; Genomic_DNA. DR ProteinModelPortal; D5NX49; -. DR EnsemblBacteria; EFG81605; EFG81605; HMPREF0281_01162. DR PATRIC; 37975327; VBICorAmm25238_1098. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23107 MW; A183778C84AFBFF0 CRC64; MNELHDYGIY FITDRELCGE RGVKETVRAA VDGGVRTVQL RDKHSSFDQQ LQQLEELAEV IDGRAALVIN DRVDVAVEAY RRGIAIDGVH VGQGDAAVVQ AREELGPDAI VGLTANTEEH LQAVAALPEG TVDYLGVGVI RPTSTKPDHP PALGIDGFRH LNSVSPVPTV AIGGVREEDI SPLRAAGAAG ICFVSALCAA PDAEATARRF VAQWHGAS // ID D5P108_CORAM Unreviewed; 225 AA. AC D5P108; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0281_02297; OS Corynebacterium ammoniagenes DSM 20306. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=649754; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20306; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Wollam A., Pepin K.H., Johnson M., Bhonagiri V., RA Zhang X., Suruliraj S., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNS01000031; EFG80205.1; -; Genomic_DNA. DR ProteinModelPortal; D5P108; -. DR EnsemblBacteria; EFG80205; EFG80205; HMPREF0281_02297. DR PATRIC; 37977445; VBICorAmm25238_2116. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). SQ SEQUENCE 225 AA; 23353 MW; C454D3B01941091D CRC64; MPHHAQLDLR CYVVTGNGSI DEIVDTAQQA AAGGAGVIQV RSKPIEAGQL LQLAEQVALA VADTNPATKV LIDDRVDIAA ILMRRGLPVH GVHVGQSDIP VTAVRELLGP DAIIGLTTGT AELIHQANEY AGIIDYVGAG PFRPTPTKDS GRRPIDLEGY PHLVELSKLP IVAIGDVQPG DVAELAATGI AGVAMVRAFR DAPSATELAQ KVIADFSAGQ NRAGA // ID D5PBF2_9MYCO Unreviewed; 223 AA. AC D5PBF2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0591_3496; OS Mycobacterium parascrofulaceum ATCC BAA-614. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=525368; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-614; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNV01000255; EFG76620.1; -; Genomic_DNA. DR ProteinModelPortal; D5PBF2; -. DR EnsemblBacteria; EFG76620; EFG76620; HMPREF0591_3496. DR PATRIC; 37980589; VBIMycPar21360_1057. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23243 MW; F3A6CD069587C125 CRC64; MHQRVTRLAA ARLYLCTDAR RERGDLAEFA DAALAGGVDI IQLRDKGSAG ERRFGPLEAR DELAACEILA DAARRHGALF AVNDRADIAR AAGADVLHLG QGDLPLDVAR GIVGPDTLLG LSSHDRDQAV AASASEADYF CVGPCWPTPT KPGREAPGLP LVRAAAGFGG AKPWFAIGGI DEARLPEVLA AGARRIVVVR AITAAADPRA AARRLRSALA AAC // ID D5Q6S1_CLODI Unreviewed; 210 AA. AC D5Q6S1; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0220_2603; OS Peptoclostridium difficile NAP08. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=525259; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAP08; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNX01000058; EFH06403.1; -; Genomic_DNA. DR ProteinModelPortal; D5Q6S1; -. DR EnsemblBacteria; EFH06403; EFH06403; HMPREF0220_2603. DR PATRIC; 37996197; VBICloDif41119_3004. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23490 MW; FE1F8BAE0A927BD0 CRC64; MIDKESLKKC LRLYLITDSE MLEGRDFYKC IEDAISSGIT TVQLREKNTC GREFLRKAMK LREITKRYGV KFIINDRVDI ALICDADGVH VGQSDIDVRE VRKLIGNDKI LGVSARTLEE AICAKNDGAD YLGIGSIFST STKLDAKSAS FETVKEIKEK VDMPFVLIGG INLDNIDKLK CLDSDGYAII SAILKAEDIS KEVEKWTLKI // ID D5Q727_CLODI Unreviewed; 229 AA. AC D5Q727; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 21. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF0220_2709; OS Peptoclostridium difficile NAP08. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=525259; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAP08; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNX01000061; EFH06298.1; -; Genomic_DNA. DR EnsemblBacteria; EFH06298; EFH06298; HMPREF0220_2709. DR PATRIC; 37996404; VBICloDif41119_2486. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 229 AA; 26804 MW; AB1FE25F95481499 CRC64; MYLITNRKLC SEERYLEVIK ESILSGVENI IIREKDLEYQ ELKNLYMKIK TKINCIDFQE QISDESLKTN INQKGCGNKF KVNFIINSNI EFFEKMDCQG IHLPFKLFLN LIENKYNFNE NKILGLSLHK VDEVEYLEKL IRKQNIKIDY ITLSHIYETK CKEGLNPKGI ELLKEAKKIT DIKIIALGGI LPSNVKETLK YCDDFAVMST IMKSKDIKKT ISNYNEKLN // ID D5QBG3_KOMHA Unreviewed; 213 AA. AC D5QBG3; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GXY_02281; OS Gluconacetobacter hansenii ATCC 23769. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Komagataeibacter. OX NCBI_TaxID=714995; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23769; RX PubMed=20543071; DOI=10.1128/JB.00588-10; RA Iyer P.R., Geib S.M., Catchmark J., Kao T.H., Tien M.; RT "Genome sequence of a cellulose-producing bacterium, Gluconacetobacter RT hansenii ATCC 23769."; RL J. Bacteriol. 192:4256-4257(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTV01000004; EFG85649.1; -; Genomic_DNA. DR ProteinModelPortal; D5QBG3; -. DR EnsemblBacteria; EFG85649; EFG85649; GXY_02281. DR PATRIC; 37998679; VBIGluHan153203_1543. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22755 MW; D69518352C051AF9 CRC64; MTDCQLYLVT PESLDPTQFA PLLARALDAG PVAAVQLRLK DVPDDTIRRA IDVLRPTAHE RDVAFILNDR PDLARDTGCD GAHVGMDDMS VEEARRMLGD DLQLGVSCYD SRDMAMHAGE GGADYIAFGA FFPSPSKETS VRAGTDLLAW WSTMMELPVV AIGGITPENC GPLVHAGADF LAVISAVWSH PDGPDAGVRA MNAAMDRASD AID // ID D5QDC3_KOMHA Unreviewed; 210 AA. AC D5QDC3; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 21. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=GXY_05646; OS Gluconacetobacter hansenii ATCC 23769. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Komagataeibacter. OX NCBI_TaxID=714995; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23769; RX PubMed=20543071; DOI=10.1128/JB.00588-10; RA Iyer P.R., Geib S.M., Catchmark J., Kao T.H., Tien M.; RT "Genome sequence of a cellulose-producing bacterium, Gluconacetobacter RT hansenii ATCC 23769."; RL J. Bacteriol. 192:4256-4257(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTV01000016; EFG85078.1; -; Genomic_DNA. DR ProteinModelPortal; D5QDC3; -. DR EnsemblBacteria; EFG85078; EFG85078; GXY_05646. DR PATRIC; 37999995; VBIGluHan153203_0319. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 210 AA; 23098 MW; 0A3DDB4971113167 CRC64; MRALPSRIYP VVDRADWIAT LGQAGAKLIQ LRLKDMAEDA LRLEIRRGVA LAHLHGVCLV LNDYWRLAIE EGIDFIHLGQ EDLDEADLPA IRRAGLRLGV STHSHDELQR ALDVRPDYVA LGPVWPTKLK KMPWGPQGVD RLREWKRLVG DLPLVAIGGI TLARAPSCIA AGADCVSAVS DFIRMPDPAA QVRAWLHATQ VSQQGDDGTV // ID D5RFP3_FUSNC Unreviewed; 206 AA. AC D5RFP3; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN ORFNames=HMPREF0397_2028; OS Fusobacterium nucleatum subsp. nucleatum ATCC 23726. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=525283; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23726; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVK01000055; EFG94507.1; -; Genomic_DNA. DR ProteinModelPortal; D5RFP3; -. DR EnsemblBacteria; EFG94507; EFG94507; HMPREF0397_2028. DR PATRIC; 38049210; VBIFusNuc129935_2019. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 206 AA; 23968 MW; 9DC7B63693E14DE5 CRC64; MIENKIKLNI ITNRKLCENE NLEKQIEKIF SAYKRKIILE DFEIVALTLR EKDLDKNEYL KLVEKIYPIC QKYRIDLILH QNYDLNLDEK YNIGGIHLSY EIFKSLNKNI REELIKKYKK IGVSIHSIDE AKEVEMLGAT YIVAGHIFET DCKKDLEPRG LKFIQELSST LTIPIFVIGG INQENSNLVI NSGAFGVCMM SSLMRY // ID D5RFP9_FUSNC Unreviewed; 206 AA. AC D5RFP9; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0397_2034; OS Fusobacterium nucleatum subsp. nucleatum ATCC 23726. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=525283; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23726; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVK01000055; EFG94513.1; -; Genomic_DNA. DR ProteinModelPortal; D5RFP9; -. DR EnsemblBacteria; EFG94513; EFG94513; HMPREF0397_2034. DR PATRIC; 38049222; VBIFusNuc129935_2025. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22966 MW; 0BB82B5F632778CA CRC64; MDLKDCKIYL VTDEKACNGK DFYKCIEESI KGGVKIVQLR EKNISTKDFY KKALKVKEIC KNYEVLFIIN DRLDITQAVE ADGVHLGQSD MPIEKAREIL KDKFLIGATA RNIEEAEKAQ LLGADYIGSG AIFGTSTKDN AKRLEMEDLK KIVNSVKIPV FAIGGININN VWMLKNIGLQ GVCSVSGILS EKDCKKAVEN ILKNFN // ID D5RUA1_9PROT Unreviewed; 223 AA. AC D5RUA1; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0731_4663; OS Roseomonas cervicalis ATCC 49957. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Roseomonas. OX NCBI_TaxID=525371; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49957; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVL01000958; EFH09117.1; -; Genomic_DNA. DR ProteinModelPortal; D5RUA1; -. DR EnsemblBacteria; EFH09117; EFH09117; HMPREF0731_4663. DR PATRIC; 38057203; VBIRosCer132485_3751. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 51 55 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23360 MW; 7247F8FEB4027102 CRC64; MAGSAPAEET RGGGGETRCR LYLITPPALD PAAFAETLAR ALDAGDVAAL QLRLKDVDDD ALRRAIDLLR PVAQSRDVAF LLNDRADLAV QTGCDGAHLG QSDGDHARAR KLLGPDRMLG ITCHGSRHLA MEAGEIGADY VAFGAFFPTT TKNAEHRAEP DLLQWWTEMF ELPSVAIGGI TAANCAPLVR AGADFLAVVG AVWNHPEGPA AGVRAMNAAI AAA // ID D5RYL2_CLODI Unreviewed; 210 AA. AC D5RYL2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0219_1393; OS Peptoclostridium difficile NAP07. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=525258; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAP07; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVM01000034; EFH15989.1; -; Genomic_DNA. DR ProteinModelPortal; D5RYL2; -. DR EnsemblBacteria; EFH15989; EFH15989; HMPREF0219_1393. DR PATRIC; 38062604; VBICloDif89320_2248. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23490 MW; FE1F8BAE0A927BD0 CRC64; MIDKESLKKC LRLYLITDSE MLEGRDFYKC IEDAISSGIT TVQLREKNTC GREFLRKAMK LREITKRYGV KFIINDRVDI ALICDADGVH VGQSDIDVRE VRKLIGNDKI LGVSARTLEE AICAKNDGAD YLGIGSIFST STKLDAKSAS FETVKEIKEK VDMPFVLIGG INLDNIDKLK CLDSDGYAII SAILKAEDIS KEVEKWTLKI // ID D5RYW7_CLODI Unreviewed; 229 AA. AC D5RYW7; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 21. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF0219_1498; OS Peptoclostridium difficile NAP07. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=525258; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAP07; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVM01000036; EFH15853.1; -; Genomic_DNA. DR EnsemblBacteria; EFH15853; EFH15853; HMPREF0219_1498. DR PATRIC; 38062808; VBICloDif89320_2349. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 229 AA; 26804 MW; AB1FE25F95481499 CRC64; MYLITNRKLC SEERYLEVIK ESILSGVENI IIREKDLEYQ ELKNLYMKIK TKINCIDFQE QISDESLKTN INQKGCGNKF KVNFIINSNI EFFEKMDCQG IHLPFKLFLN LIENKYNFNE NKILGLSLHK VDEVEYLEKL IRKQNIKIDY ITLSHIYETK CKEGLNPKGI ELLKEAKKIT DIKIIALGGI LPSNVKETLK YCDDFAVMST IMKSKDIKKT ISNYNEKLN // ID D5SQY4_PLAL2 Unreviewed; 536 AA. AC D5SQY4; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Plim_0604; OS Planctomyces limnophilus (strain ATCC 43296 / DSM 3776 / IFAM 1008 / OS 290). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Planctomyces. OX NCBI_TaxID=521674; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290; RX PubMed=21304691; DOI=10.4056/sigs.1052813; RA Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Complete genome sequence of Planctomyces limnophilus type strain (Mu RT 290)."; RL Stand. Genomic Sci. 3:47-56(2010). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001744; ADG66452.1; -; Genomic_DNA. DR RefSeq; YP_003628651.1; NC_014148.1. DR ProteinModelPortal; D5SQY4; -. DR EnsemblBacteria; ADG66452; ADG66452; Plim_0604. DR GeneID; 9137283; -. DR KEGG; plm:Plim_0604; -. DR PATRIC; 38236960; VBIPlaLim6916_0746. DR KO; K00788; -. DR OMA; NFNRARE; -. DR BioCyc; PLIM521674:GKE7-630-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.1780.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR023150; Dbl_Clp-N. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 536 AA; 59048 MW; FB8E0CBB26096867 CRC64; MEHFLTAAAL RVIEAARGLT DATVMAPVMP EVFSPHASAT RLNSMARLNS DQVVEAALFW ALLEEESVAH LRMIEQGLEI DDLRQRMERF LPSMSSSVGD ETDLQSSLST AFDRMIRQAR HEAHKVSRSE VGTEHLLRAL FEANGWLTAW LAQEQIALAK PVEEISGPAT SASGPPLEHE QILLPETAPP ENLTAVYRLL DASGNRAREG LRVIEDAVRM VRNDGWFSRE LKELRHRLTT ALRMLPEEAL LASRDTPNDV GTQITTMSET MRGSANDVIA AAFKRLQESL RSLEEYGKII NGYFASRIEA IRYQSYTLEK AVRIGQFSQK TLEGRVLYLL LTEKLCHRPV GQTLREALRA GVGIVQIREK SMSDRRLLDH TRLVLDLAHE YDALVIMNDR PDLAALTQAD GIHVGQEELT IAQVRQITGP RPLVGLSTHS LQQAEAAVIE GASYIGVGPT FPTTTKEFAE YAGLEYVREV AREIALPAYA IGGITTENAA DVVAAGATRL AVSSAICSAN EPYDAARHLM EILNGA // ID D5T244_LEUKI Unreviewed; 211 AA. AC D5T244; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LKI_04005; OS Leuconostoc kimchii (strain IMSNU 11154 / KCTC 2386 / IH25). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=762051; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMSNU 11154 / KCTC 2386 / IH25; RX PubMed=20494991; DOI=10.1128/JB.00508-10; RA Oh H.M., Cho Y.J., Kim B.K., Roe J.H., Kang S.O., Nahm B.H., Jeong G., RA Han H.U., Chun J.; RT "Complete genome sequence analysis of Leuconostoc kimchii IMSNU RT 11154."; RL J. Bacteriol. 192:3844-3845(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001758; ADG40343.1; -; Genomic_DNA. DR RefSeq; YP_003621312.1; NC_014136.1. DR ProteinModelPortal; D5T244; -. DR EnsemblBacteria; ADG40343; ADG40343; LKI_04005. DR GeneID; 9133321; -. DR KEGG; lki:LKI_04005; -. DR PATRIC; 38186163; VBILeuKim161478_0805. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; LKIM762051:GJOL-809-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23414 MW; 038405A9E44DDA9E CRC64; MADKNIDYTL YLITNRYDYS DEQFLNIVFE ACDSGVTLVQ LREKDVTTKR YFDLAVAVKK ITDKFKVPLI IDDRVDICLA VNAAGVHIGD NELPVKRVRQ LIGKDKILGV SVKDVQRAKE AEAQGADYFG VGAIYPTKTK VITKHTTIET LKDIVSCVDI PVNAIGGIKE NNILSLKNTG ISGVCMVSEI MQAEDVRTKV TNCLKNVEQL M // ID D5T2R3_LEUKI Unreviewed; 212 AA. AC D5T2R3; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LKI_05105; OS Leuconostoc kimchii (strain IMSNU 11154 / KCTC 2386 / IH25). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=762051; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMSNU 11154 / KCTC 2386 / IH25; RX PubMed=20494991; DOI=10.1128/JB.00508-10; RA Oh H.M., Cho Y.J., Kim B.K., Roe J.H., Kang S.O., Nahm B.H., Jeong G., RA Han H.U., Chun J.; RT "Complete genome sequence analysis of Leuconostoc kimchii IMSNU RT 11154."; RL J. Bacteriol. 192:3844-3845(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001758; ADG40562.1; -; Genomic_DNA. DR RefSeq; YP_003621531.1; NC_014136.1. DR ProteinModelPortal; D5T2R3; -. DR EnsemblBacteria; ADG40562; ADG40562; LKI_05105. DR GeneID; 9133555; -. DR KEGG; lki:LKI_05105; -. DR PATRIC; 38186613; VBILeuKim161478_1015. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; LKIM762051:GJOL-1043-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22600 MW; 0A22959297DBE904 CRC64; MIFKQAMLAR YFILGTQNVA SEAVFFDVLT QALAHGITLF QYREKGPGAL TGSEKRRVAQ RVRELTTQYQ VPLVIDDDID LAHAIKADGV HFGQGDGDIK KNIQASQPLF VGVSVSTQEE YDRIAGLSGI DNVGIGPVFA TMSKADAKPA IGISGLQGLV RQSQWPAIAI GGISQANLPD VLKTGVAGAS VISMISASEN IAKTLAFWKQ LS // ID D5TDG6_LEGP2 Unreviewed; 488 AA. AC D5TDG6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiD; OrderedLocusNames=lpa_02278; OS Legionella pneumophila serogroup 1 (strain 2300/99 Alcoy). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=423212; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2300/99 Alcoy; RX PubMed=20236513; DOI=10.1186/1471-2164-11-181; RA D'Auria G., Jimenez-Hernandez N., Peris-Bondia F., Moya A., RA Latorre A.; RT "Legionella pneumophila pangenome reveals strain-specific virulence RT factors."; RL BMC Genomics 11:181-181(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001828; ADG24900.1; -; Genomic_DNA. DR RefSeq; YP_003618852.1; NC_014125.1. DR ProteinModelPortal; D5TDG6; -. DR EnsemblBacteria; ADG24900; ADG24900; lpa_02278. DR GeneID; 9129433; -. DR KEGG; lpa:lpa_02278; -. DR PATRIC; 38181253; VBILegPne70474_1737. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR BioCyc; LPNE423212:GHRR-1679-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 488 AA; 54145 MW; 713B18338FEA67E8 CRC64; MKKPIVWTIA GVDSSGLAGV HADMETFSRL NVRACSVITA VTAQNAHSII AVEAISRDQV AAQCRALELN LKPDAIKIGM LCSTPICEEI AYFLKGYEGF VVLDPIITSS SGTNLFFPDL QQHKENLIQL FPYVTIITPN RIEAEIILNR SISSYQDIIN AASDLLSLGA KQVLLKGGHV KDNSFSQDYW TDGKESFWIA NRRFPETNYR GTGCVLSSAL TACLALGYSI KDAIVIAKMY VNRGIRQSIE LDKDASQLYH DGWPEDEADL PYLSPTPFIK PVPSFKKCSM GFYPIVDSSH WLEMLLPLGI KCIQLRIKEA SKERLEEEIK RSVHLANQYN AALFINDYWE LAIHYGAAGV HLGQEDLEKA DVDRINRSGL FLGISTHCYY EVARAHALNP SYVACGPIYE TTSKIMPFQA QGIARLERWR KTLHYPLVAI GGITLKNLSD VLKTKIDGVS VISAITKASA PLVAAKQFLT QMNESHNE // ID D5TI63_BIFAV Unreviewed; 516 AA. AC D5TI63; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE SubName: Full=Phosphomethylpyrimidine kinase; GN OrderedLocusNames=BalV_1201; OS Bifidobacterium animalis subsp. lactis (strain V9). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=573236; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=V9; RX PubMed=20511504; DOI=10.1128/JB.00369-10; RA Sun Z., Chen X., Wang J., Gao P., Zhou Z., Ren Y., Sun T., Wang L., RA Meng H., Chen W., Zhang H.; RT "Complete genome sequence of probiotic Bifidobacterium animalis subsp. RT lactis strain V9."; RL J. Bacteriol. 192:4080-4081(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001892; ADG33789.1; -; Genomic_DNA. DR RefSeq; YP_005581568.1; NC_017217.1. DR ProteinModelPortal; D5TI63; -. DR EnsemblBacteria; ADG33789; ADG33789; BalV_1201. DR GeneID; 12171786; -. DR KEGG; blv:BalV_1201; -. DR PATRIC; 42764820; VBIBifAni108068_1237. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OMA; YLAQGEP; -. DR BioCyc; BANI573236:GL92-1243-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 516 AA; 54334 MW; BA2BECA74309264A CRC64; MNSFPYPSMR DRFDLRFYFV VGPDDCGNRP ILDVVAKALD GGASFIQLRA KTQDVAEIVS LANDIAEEIA GHHVEHSVAF VVDDRVDAAL EARAKGIKVD GVHIGQDDLD PVVARKLLGP DAIIGLSAKT VDEVREANHL PEGTIDYIGA GPLHMTATKP ESMIVDENGD ITTLNVSSID EMRTMSKYPL IVGGGVKADD IPMLAKTKAD GWFVVSAIAG ATDPEQATRR LVDDWTAIRG DEKPRYTGRK PAATKLPAVL TIATTDSSGG AGIPADLKTM LANDVFGECV VAGITAQNTT GVQAIAAVDP SIVGAQIDSV FDDIRPTAVK IGVIVGVESV KTVARKLRDH QATNIVVDPV MVATSGSSLA ADDTIAEEIS SLFPIATVIT PNIPEAQVLA QMPIGNQADM ETAAVQLAKD YGTCVLVKGG HGVKDADDVL AFPTGAVTWF EGERIANDNT HGTGCTLSSA IASYLAQGED LEDAVRDAKA YLSGALRANL NLGKGHGPMD HAWAMH // ID D5TMI6_BACT1 Unreviewed; 201 AA. AC D5TMI6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BMB171_C0361; OS Bacillus thuringiensis (strain BMB171). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=714359; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BMB171; RX PubMed=20525827; DOI=10.1128/JB.00562-10; RA He J., Shao X., Zheng H., Li M., Wang J., Zhang Q., Li L., Liu Z., RA Sun M., Wang S., Yu Z.; RT "Complete genome sequence of Bacillus thuringiensis mutant strain RT BMB171."; RL J. Bacteriol. 192:4074-4075(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001903; ADH05179.1; -; Genomic_DNA. DR RefSeq; YP_003662899.1; NC_014171.1. DR ProteinModelPortal; D5TMI6; -. DR EnsemblBacteria; ADH05179; ADH05179; BMB171_C0361. DR GeneID; 9191402; -. DR KEGG; btb:BMB171_C0361; -. DR PATRIC; 38127105; VBIBacThu148000_0386. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; BTHU714359:GJBQ-431-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 26 30 HMP-PP binding (By similarity). FT REGION 125 127 THZ-P binding (By similarity). FT REGION 177 178 THZ-P binding (By similarity). FT METAL 62 62 Magnesium (By similarity). FT METAL 81 81 Magnesium (By similarity). FT BINDING 61 61 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 201 AA; 21406 MW; EA6EE0B7E11477DF CRC64; MGSNNCTRDP LAVLKEALDG GVTIFQFREK GEGSLIGEDR VRFAKELQTL CNEYSVPFIV NDDVELAIEL DADGVHVGQD DEGITSVREK MGDKIIGVSA HTIEEARFAI ENGADYLGVG PIFPTSTKKD TKAVQGTKGL AYFREQGITV PIVGIGGITI ENTAAVIEAG ADGVSVISAI SLAESAYEST RKLAEEVKRS L // ID D5TQN0_BACT1 Unreviewed; 206 AA. AC D5TQN0; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Transcriptional regulator TenI; GN Name=tenI; OrderedLocusNames=BMB171_C0639; OS Bacillus thuringiensis (strain BMB171). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=714359; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BMB171; RX PubMed=20525827; DOI=10.1128/JB.00562-10; RA He J., Shao X., Zheng H., Li M., Wang J., Zhang Q., Li L., Liu Z., RA Sun M., Wang S., Yu Z.; RT "Complete genome sequence of Bacillus thuringiensis mutant strain RT BMB171."; RL J. Bacteriol. 192:4074-4075(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001903; ADH05457.1; -; Genomic_DNA. DR RefSeq; YP_003663177.1; NC_014171.1. DR EnsemblBacteria; ADH05457; ADH05457; BMB171_C0639. DR GeneID; 9191680; -. DR KEGG; btb:BMB171_C0639; -. DR PATRIC; 38127767; VBIBacThu148000_0673. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR BioCyc; BTHU714359:GJBQ-751-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22791 MW; F39BD4067A87BD08 CRC64; MKNELHVISN GHMPFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLMEGFPASK IVINDRIDIA ILLNIPRVQL GYRSTDVKSV KEKFSYLHVG YSVHSLDEAI VAFKNGADSL VYGHVFPTDC KKGVPARGLE EISDIARCLS IPITAIGGIT PENTVDVLTN GVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID D5U1P9_THEAM Unreviewed; 218 AA. AC D5U1P9; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tagg_0776; OS Thermosphaera aggregans (strain DSM 11486 / M11TL). OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Thermosphaera. OX NCBI_TaxID=633148; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11486 / M11TL; RX DOI=10.4056/sigs.821804; RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A., RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., RA Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J., RA Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., Heimerl T., RA Weikl F., Brambilla E., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Thermosphaera aggregans type strain RT (M11TLT)."; RL Stand. Genomic Sci. 2:245-259(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 11486; RG US DOE Joint Genome Institute (JGI-PGF); RA Spring S., Lapidus A., Munk C., Schroeder M., Glavina Del Rio T., RA Tice H., Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., RA Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.-J., Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., RA Chain P., Heimerl T., Weik F., Goker M., Rachel R., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Thermosphaera aggregans type strain RT (M11TL)."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001939; ADG91049.1; -; Genomic_DNA. DR RefSeq; YP_003650001.1; NC_014160.1. DR ProteinModelPortal; D5U1P9; -. DR EnsemblBacteria; ADG91049; ADG91049; Tagg_0776. DR GeneID; 9165791; -. DR KEGG; tag:Tagg_0776; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HRFYFIT; -. DR BioCyc; TAGG633148:GHBI-787-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23148 MW; 2A4B61B96D36E8DF CRC64; MRLENHLRLL VLTEPKLRPD VAESVREALE GGATSIQLRM KEASTRQMIE VGLEIRRLTR EYGALYFVDD RVDVALACKA DGVQLGPDDM PVETAREVVP NLLIGASVYS LEEALKAEKA GADFLGAGSV YPSPTKQGVP VIGLDGLRLI VNAVKIPVVA IGGVNESNAL EVLETGVAGI AVVSAVMGAP SAKEATSRLR SIVDKALAAR QKASSRHK // ID D5UAG5_BRAM5 Unreviewed; 234 AA. AC D5UAG5; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-MAR-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Bmur_1601; OS Brachyspira murdochii (strain ATCC 51284 / DSM 12563 / 56-150) OS (Serpulina murdochii). OC Bacteria; Spirochaetes; Spirochaetales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=526224; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51284 / DSM 12563 / 56-150; RX PubMed=21304710; DOI=10.4056/sigs.831993; RA Pati A., Sikorski J., Gronow S., Munk C., Lapidus A., Copeland A., RA Glavina Del Tio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., RA Han C., Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Spring S., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Brachyspira murdochii type strain (56- RT 150)."; RL Stand. Genomic Sci. 2:260-269(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001959; ADG71688.1; -; Genomic_DNA. DR RefSeq; YP_003633887.1; NC_014150.1. DR ProteinModelPortal; D5UAG5; -. DR EnsemblBacteria; ADG71688; ADG71688; Bmur_1601. DR GeneID; 9142594; -. DR KEGG; brm:Bmur_1601; -. DR PATRIC; 38145382; VBIBraMur21074_1614. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; BMUR526224:GHIV-1627-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 160 162 THZ-P binding (By similarity). FT REGION 211 212 THZ-P binding (By similarity). FT METAL 96 96 Magnesium (By similarity). FT METAL 115 115 Magnesium (By similarity). FT BINDING 95 95 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 HMP-PP (By similarity). FT BINDING 191 191 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 234 AA; 26598 MW; 2A9239C3F39A9CED CRC64; MISFMKYFKT IKNKKDKREF LKQKYFNSSI YCVTAEDFSN GRSNIEVVKS MLEAGIKIIQ YREKDNPNKY MREKYNECLE IRELTNKYEA LFLIDDYADL ALAVEADGVH IGQKDMPIEA VRKVVGDDLI IGLSTTNKNE ALSAVNTSCN YIGIGPIFST QTKPDANTAT GIDYLDYVVK NIDIPFVCIG GIKLNNMDIL IEHKAMSLCM LTEIVSSEDI KAKCELLIKK MKRL // ID D5UDX5_CELFN Unreviewed; 221 AA. AC D5UDX5; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cfla_1635; OS Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / NCIB 8073 / NRS OS 134). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Cellulomonadaceae; Cellulomonas. OX NCBI_TaxID=446466; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 482 / DSM 20109 / NCIB 8073 / NRS 134; RX DOI=10.4056/sigs.1012662; RA Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S., RA Glavina Del Rio T., Nolan M., Tice H., Cheng J., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., RA Goodwin L., Chen A., Palaniappan K., Land M., Hause L., Chang Y., RA Jeffries C., Rohde M., Goker M., Woyke T., Bristow J., Eisen J., RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H.; RT "Complete genome sequence of Cellulomonas flavigena type strain RT (134)."; RL Stand. Genomic Sci. 3:15-25(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001964; ADG74533.1; -; Genomic_DNA. DR RefSeq; YP_003636732.1; NC_014151.1. DR ProteinModelPortal; D5UDX5; -. DR EnsemblBacteria; ADG74533; ADG74533; Cfla_1635. DR GeneID; 9145521; -. DR KEGG; cfl:Cfla_1635; -. DR PATRIC; 38151239; VBICelFla99035_1637. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; CFLA446466:GHDJ-1659-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 21631 MW; E32AB158B9BC64BF CRC64; MSALPCGIYL VLDADVCTRA GHDPAGVAVA AVRAGVGTVQ VRAKRAGVRD LVALTVAVAD ALRGSPPAAL VVDDRVDVAL AARARGARVD GVHVGRHDLE TADARALLGP DALVGVSAAR PEHMAAAVGA DHVGSGPVRL TPTKPEAGPA IGFDGLRAAV VAADGRPVVA IGGLGAADAP ALRAAGVHAM AVVSAVCAAP DPGGAAARLV AAWQQVPAVA R // ID D5UHY6_CELFN Unreviewed; 220 AA. AC D5UHY6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cfla_0496; OS Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / NCIB 8073 / NRS OS 134). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Cellulomonadaceae; Cellulomonas. OX NCBI_TaxID=446466; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 482 / DSM 20109 / NCIB 8073 / NRS 134; RX DOI=10.4056/sigs.1012662; RA Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S., RA Glavina Del Rio T., Nolan M., Tice H., Cheng J., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., RA Goodwin L., Chen A., Palaniappan K., Land M., Hause L., Chang Y., RA Jeffries C., Rohde M., Goker M., Woyke T., Bristow J., Eisen J., RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H.; RT "Complete genome sequence of Cellulomonas flavigena type strain RT (134)."; RL Stand. Genomic Sci. 3:15-25(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001964; ADG73410.1; -; Genomic_DNA. DR RefSeq; YP_003635609.1; NC_014151.1. DR ProteinModelPortal; D5UHY6; -. DR EnsemblBacteria; ADG73410; ADG73410; Cfla_0496. DR GeneID; 9144363; -. DR KEGG; cfl:Cfla_0496; -. DR PATRIC; 38148927; VBICelFla99035_0499. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR BioCyc; CFLA446466:GHDJ-501-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 147 149 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23076 MW; 73BAF90D4D419009 CRC64; MPDALEVHAR RRARLDDARL YLCTDARRAT GDLEEFLHAV LASGVDVVQL RDRSLDVLDE LELGALVRDV AHEHGALFAV NDRADLALAL RADVLHTGQR DLPVAQAREI VGPGVLLGRS SGGGAAAAEA DADPDVDYFC VGPLVATPTK PGREPVGLDA VRAVAATAPR TPWFAIGGVD EALLPEVVAA GARRVVVVRA LTAAADPRGA AQRLRRGTVG // ID D5UYM4_TSUPD Unreviewed; 222 AA. AC D5UYM4; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tpau_3749; OS Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 / OS NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Tsukamurellaceae; Tsukamurella. OX NCBI_TaxID=521096; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C., RA Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Tsukamurella paurometabola DSM 20162."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001966; ADG80327.1; -; Genomic_DNA. DR RefSeq; YP_003648666.1; NC_014158.1. DR ProteinModelPortal; D5UYM4; -. DR EnsemblBacteria; ADG80327; ADG80327; Tpau_3749. DR GeneID; 9157929; -. DR KEGG; tpr:Tpau_3749; -. DR PATRIC; 38310855; VBITsuPau718_3756. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; TPAU521096:GI2W-3790-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23324 MW; 92D3CE706808A265 CRC64; MVSPRDRLDS ARLYLCTDAR RERGDLAEFV AAALRGGVDI VQLRDKGSAG EREYGPLEAK QEIELVSQLR EIAHAHDALV AVNDRADIAF AARADVLHLG QDDLPVAVAR RIVGDEVVIG RSTHDADQAT AAATETGVDY FCTGPCWPTP TKPGRTAPGL DLVRATATAA PARKWFAIGG IDLDRVPEVS AAGADAIVVV RAITAAADPE AAARALRAAV SG // ID D5UZE1_ARCNC Unreviewed; 186 AA. AC D5UZE1; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Arnit_0513; OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / LMG 7604 / OS NCTC 12251 / CI) (Campylobacter nitrofigilis). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=572480; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33309 / DSM 7299 / LMG 7604 / NCTC 12251 / CI; RX PubMed=21304714; DOI=10.4056/sigs.912121; RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., RA Nolan M., Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., RA Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K., Ivanova N., RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Detter J.C., Rohde M., Goker M., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., RA Kyrpides N.C.; RT "Complete genome sequence of Arcobacter nitrofigilis type strain RT (CI)."; RL Stand. Genomic Sci. 2:300-308(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001999; ADG92178.1; -; Genomic_DNA. DR RefSeq; YP_003654684.1; NC_014166.1. DR EnsemblBacteria; ADG92178; ADG92178; Arnit_0513. DR GeneID; 9170660; -. DR KEGG; ant:Arnit_0513; -. DR PATRIC; 38113642; VBIArcNit33843_0509. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FATPNKG; -. DR BioCyc; ANIT572480:GJ62-528-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 186 AA; 21714 MW; E172149C2ECF1308 CRC64; MNQTFNYYLI TDPQYYTNDK NTFKEKLEDI LTNKRVDMAC FRDKESANYE ELANIFINTC KKFNIKQIIL NRNLELAINL NCGIHLTSQQ FDKIKIAKEK NIYTIISCHN EKDIEKAIKE KADAITYSPI FYTPNKGQEK GIKALEDMQK KYQIKIIALG GIIADLQIKQ IQDCQVFGFA SIRYFI // ID D5V2D5_ARCNC Unreviewed; 203 AA. AC D5V2D5; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Arnit_0703; OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / LMG 7604 / OS NCTC 12251 / CI) (Campylobacter nitrofigilis). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=572480; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33309 / DSM 7299 / LMG 7604 / NCTC 12251 / CI; RX PubMed=21304714; DOI=10.4056/sigs.912121; RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., RA Nolan M., Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., RA Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K., Ivanova N., RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Detter J.C., Rohde M., Goker M., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., RA Kyrpides N.C.; RT "Complete genome sequence of Arcobacter nitrofigilis type strain RT (CI)."; RL Stand. Genomic Sci. 2:300-308(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001999; ADG92368.1; -; Genomic_DNA. DR RefSeq; YP_003654874.1; NC_014166.1. DR EnsemblBacteria; ADG92368; ADG92368; Arnit_0703. DR GeneID; 9170851; -. DR KEGG; ant:Arnit_0703; -. DR PATRIC; 38114022; VBIArcNit33843_0698. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NADIAFI; -. DR BioCyc; ANIT572480:GJ62-719-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 203 AA; 23104 MW; FA86F7339A3CF84B CRC64; MNKNRFEELL GFNPKSSSNE LYALCDFQTL KNKNISFERF LELCEKFDAK IIQYRDKLSN YETKKENLFY LRSKTNIPII INDEIDLVQY CDGLHLGQED FDKINSNKQL VVKLIRKKIG NKLLGLSTHN EKEILEANNL DLDMIGLGAY RTTTTKDVSV MLGNKISYLA KISKHPVCAI GGVKIAEPIA NISFNVVGSS LYD // ID D5VC45_MORCR Unreviewed; 220 AA. AC D5VC45; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-MAR-2014, entry version 28. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=MCR_0983; ORFNames=MCRH_1055; OS Moraxella catarrhalis (strain RH4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=749219; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BBH18, and RH4; RX PubMed=20453089; DOI=10.1128/JB.00121-10; RA de Vries S.P., van Hijum S.A., Schueler W., Riesbeck K., Hays J.P., RA Hermans P.W., Bootsma H.J.; RT "Genome analysis of Moraxella catarrhalis strain RH4, a human RT respiratory tract pathogen."; RL J. Bacteriol. 192:3574-3583(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BBH18, and RH4; RA de Vries S.P.W., van Hijum S.A.F.T., Schueler W., Riesbeck K., RA Hays J.P., Hermans P.W.M., Bootsma H.J.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RH4; RX PubMed=23209224; DOI=10.1128/JB.01833-12; RA Zomer A., de Vries S.P., Riesbeck K., Meinke A.L., Hermans P.W., RA Bootsma H.J.; RT "Genome Sequence of Moraxella catarrhalis RH4, an Isolate of RT Seroresistant Lineage."; RL J. Bacteriol. 194:6969-6969(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002005; ADG61248.1; -; Genomic_DNA. DR EMBL; AMSO01000006; EKF83594.1; -; Genomic_DNA. DR RefSeq; YP_003627141.1; NC_014147.1. DR EnsemblBacteria; ADG61248; ADG61248; MCR_0983. DR EnsemblBacteria; EKF83594; EKF83594; MCRH_1055. DR GeneID; 9135693; -. DR KEGG; mct:MCR_0983; -. DR PATRIC; 38207821; VBIMorCat148474_0981. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IGRTCHG; -. DR BioCyc; MCAT749219:GHBK-1007-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 220 AA; 24377 MW; 6B76374C2FC8B34D CRC64; MTLQSIDKVP KLYLLTNDDE LTTLLDKLER VFDTGAVSLL QVRRKSTLKL YDLATVYREA EMIVSLANDY DIKVVMNDSL ELASHFGTGL HLGQRDGSVR VAREILGDHV VIGRTCHTDL ALFKEAKREG ATYGAMGTAF ASITKPRAKI ISKDILKKAC ELDFPLCVIG GITLENIHQL RDKLNGAAID YIAVTADIMG HSVDTIADKC LAWQQKLNTW // ID D5VCT3_MORCR Unreviewed; 315 AA. AC D5VCT3; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-MAR-2014, entry version 27. DE SubName: Full=NUDIX hydrolase; DE EC=2.5.1.3; GN OrderedLocusNames=MCR_1223; ORFNames=MCRH_1292; OS Moraxella catarrhalis (strain RH4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=749219; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BBH18, and RH4; RX PubMed=20453089; DOI=10.1128/JB.00121-10; RA de Vries S.P., van Hijum S.A., Schueler W., Riesbeck K., Hays J.P., RA Hermans P.W., Bootsma H.J.; RT "Genome analysis of Moraxella catarrhalis strain RH4, a human RT respiratory tract pathogen."; RL J. Bacteriol. 192:3574-3583(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BBH18, and RH4; RA de Vries S.P.W., van Hijum S.A.F.T., Schueler W., Riesbeck K., RA Hays J.P., Hermans P.W.M., Bootsma H.J.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RH4; RX PubMed=23209224; DOI=10.1128/JB.01833-12; RA Zomer A., de Vries S.P., Riesbeck K., Meinke A.L., Hermans P.W., RA Bootsma H.J.; RT "Genome Sequence of Moraxella catarrhalis RH4, an Isolate of RT Seroresistant Lineage."; RL J. Bacteriol. 194:6969-6969(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002005; ADG61486.1; -; Genomic_DNA. DR EMBL; AMSO01000007; EKF83184.1; -; Genomic_DNA. DR RefSeq; YP_003627379.1; NC_014147.1. DR EnsemblBacteria; ADG61486; ADG61486; MCR_1223. DR EnsemblBacteria; EKF83184; EKF83184; MCRH_1292. DR GeneID; 9135936; -. DR KEGG; mct:MCR_1223; -. DR PATRIC; 38208297; VBIMorCat148474_1216. DR KO; K03574; -. DR OMA; VAVIHYQ; -. DR BioCyc; MCAT749219:GHBK-1250-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Transferase. SQ SEQUENCE 315 AA; 35857 MW; 976C848E5AC2CAEB CRC64; MHQHQGGKWE FIGGKIDANE SAKQALMREV NEEIGLSLNT DQLVFMGKVY HDYQDKKVYL YTYEVYLTKK QYHDFLYCQK GLENQALRWL DMDEMIAKVN QFPVANARIM DWIGLPNLLY ISHAVDYFGD FDGFVNYYSN QLPKSAYFYC RPCVGTDDAI RLLTLLKSKR PDINFVVSWS VCQAAQDMMK VLGGVMVKLT CDELEYFSAN FDKLPTDLPL WVGVHDKKEA MMANQLAKSH RIVAALISPV HKTKTHPKAH ALGWQGFESL AKLCDMPSMA LGGMTYFDMN CAKNHGAKGI AGIRGLILSH NSQHY // ID D5VEM4_CAUST Unreviewed; 222 AA. AC D5VEM4; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cseg_0655; OS Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC OS 15250 / LMG 17158 / TK0059) (Mycoplana segnis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=509190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 / RC TK0059; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002008; ADG09167.1; -; Genomic_DNA. DR RefSeq; YP_003591785.1; NC_014100.1. DR ProteinModelPortal; D5VEM4; -. DR EnsemblBacteria; ADG09167; ADG09167; Cseg_0655. DR GeneID; 9102139; -. DR KEGG; cse:Cseg_0655; -. DR PATRIC; 37201285; VBICauSeg118057_0668. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR BioCyc; CSEG509190:GHVG-666-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 22998 MW; B536CE0EFE377103 CRC64; MTLDCRLYLI TPPALSDLAG FGRTLAQALE GGDVAALQIR LKDAPDEVVA AAVDVLAPIA QARDVAVILN DRPDLAARLA VDGVHIGQSD MPYKDARKLM GQRMIGVTCH DSRHLAMEAS EAGADYVAFG AFFPTTTKDA PTTADPEILT IWQETMETPC VAIGGITADN ATGLAAAGAD FLAVSAGVWA HPEGPAAAVA ALNAAIADGL AARREARQQS PK // ID D5VQ76_CAUST Unreviewed; 185 AA. AC D5VQ76; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Cseg_4242; OS Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC OS 15250 / LMG 17158 / TK0059) (Mycoplana segnis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=509190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 / RC TK0059; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002008; ADG12649.1; -; Genomic_DNA. DR RefSeq; YP_003595267.1; NC_014100.1. DR ProteinModelPortal; D5VQ76; -. DR EnsemblBacteria; ADG12649; ADG12649; Cseg_4242. DR GeneID; 9105773; -. DR KEGG; cse:Cseg_4242; -. DR PATRIC; 37208706; VBICauSeg118057_4328. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INERSDI; -. DR BioCyc; CSEG509190:GHVG-4301-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 185 AA; 18876 MW; AE18080F99E15A6A CRC64; MRDRVLPNLL FFTDPARVAS PEAIAERLPR GAGIVFRAFS AENAVEQGRR LRAIADARGL ILLAGAHPGL AEGIGADGLH MPERLAGEIP KLRAEHARYL ITVAAHDLKA VQAAERAGAD AVIVSPVFPS NSPSAGQPLG VDGLKALVSA TTLPVYALGG VRADTVAQLA GSGVAGIAAV EALAG // ID D5W365_CLOB2 Unreviewed; 205 AA. AC D5W365; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CBF_0502; OS Clostridium botulinum (strain 230613 / Type F). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=758678; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=230613 / Type F; RA Tian R., Li T.; RT "The complete genome sequence of a type F Clostridium botulinum RT strain."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002011; ADF98284.1; -; Genomic_DNA. DR RefSeq; YP_005673485.1; NC_017297.1. DR ProteinModelPortal; D5W365; -. DR EnsemblBacteria; ADF98284; ADF98284; CBF_0502. DR GeneID; 12229022; -. DR KEGG; cbm:CBF_0502; -. DR PATRIC; 36785540; VBICloBot152196_0487. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; CBOT758678:GLBH-502-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22407 MW; 33B89532CE505327 CRC64; MEINYELYLI TDRRFLKGRQ LKKVVEDAIL GGVTIVQVRE KDVSTREFYN VAKEVKEVTD YYKVPIIIND RLDIAQAIDA SGVHLGQKDM HLNIAREILG KDKIIGISVG NVKEALEAQN NGADYLGIGT IFPTGSKKDV DAIIGIDGLS KIKDSISIPS VAIGGINKTN FKDVLKTGIE GISVISAILD EDDIKLAANN LLINK // ID D5W560_BURSC Unreviewed; 367 AA. AC D5W560; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=BC1002_2830; OS Burkholderia sp. (strain CCGE1002). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=640511; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCGE1002; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ovchinnikova G., Martinez-Romero E., RA Hernandez M.A.R., Tiedje J.M., Woyke T.; RT "Complete sequence of chromosome 1 of Burkholderia sp. CCGE1002."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002013; ADG16878.1; -; Genomic_DNA. DR RefSeq; YP_003606389.1; NC_014117.1. DR ProteinModelPortal; D5W560; -. DR EnsemblBacteria; ADG16878; ADG16878; BC1002_2830. DR GeneID; 9090550; -. DR KEGG; bge:BC1002_2830; -. DR PATRIC; 37214681; VBIBurSp41388_2907. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; BSP640511:GJ7J-2890-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 367 AA; 39649 MW; AC494DB7040F0C6D CRC64; MTQSLTLKDR DLFWPTADEL IEAAERIRAR LGDWPPTHAP WRICLTAPDE PNGGDLIVIA DAQPHGEQIA RWLTRGAGVI VAAENRATLH LGGEKYGLEG RLAEDWIAAL AAFLDCGFDP HDALVLALAW RDGDETRADD AFPSDLGRFP RLTDLPPAPA RAFARCPERL GLYPVLPTAD WVERVVGFGV KTVQLRRKSA EPADELKREI ARCVAAGRAH DAQVFINDHW QAALEAGAYG VHLGQEDVHT ADLSTLANAG IRLGLSTHGF YEMLKALHFR PSYIALGAVF PTTTKVMPTA PQGLRRLARY VRLLDGVVPL VAIGGIDLQV LPDVLATGVG CAAVVRAVTE AADPAAAVSA LQHTFTQ // ID D5WQ99_KYRT2 Unreviewed; 217 AA. AC D5WQ99; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Btus_1808; OS Kyrpidia tusciae (strain DSM 2912 / NBRC 15312 / T2) (Bacillus OS tusciae). OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Kyrpidia. OX NCBI_TaxID=562970; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2912 / NBRC 15312 / T2; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Chertkov O., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Pukall R., Schneider S., RA Wahrenburg C., Klenk H.-P., Eisen J.A.; RT "The complete genome of Bacillus tusciae DSM 2912."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002017; ADG06508.1; -; Genomic_DNA. DR RefSeq; YP_003589652.1; NC_014098.1. DR ProteinModelPortal; D5WQ99; -. DR EnsemblBacteria; ADG06508; ADG06508; Btus_1808. DR GeneID; 9109752; -. DR KEGG; bts:Btus_1808; -. DR PATRIC; 37246702; VBIBacTus29608_1884. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; KTUS562970:GHUX-1846-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23460 MW; E9ED888824A1133C CRC64; MVKQIHGLYA ITDRRFYRGR SLEEVAGDWL AGGVTCIQLR EKDLNTRELL EAGRVLRRMT RAAGALLIVN DRVDVAMALD ADGVHLGQGD LPIRAAREIL GEGRIIGVST HNVEEAREAA IQGANYIGVG PMRATTTKTD TKPVVGIAGL RRIRQAVDLP IIAIGGIRLE DAEELAAAGA DGLAVIRGLV DTEDILERAK AFVQAILRGR QRREGRG // ID D5WTU6_KYRT2 Unreviewed; 218 AA. AC D5WTU6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Btus_0498; OS Kyrpidia tusciae (strain DSM 2912 / NBRC 15312 / T2) (Bacillus OS tusciae). OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Kyrpidia. OX NCBI_TaxID=562970; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2912 / NBRC 15312 / T2; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Chertkov O., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Pukall R., Schneider S., RA Wahrenburg C., Klenk H.-P., Eisen J.A.; RT "The complete genome of Bacillus tusciae DSM 2912."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002017; ADG05266.1; -; Genomic_DNA. DR RefSeq; YP_003588410.1; NC_014098.1. DR ProteinModelPortal; D5WTU6; -. DR EnsemblBacteria; ADG05266; ADG05266; Btus_0498. DR GeneID; 9108416; -. DR KEGG; bts:Btus_0498; -. DR PATRIC; 37243928; VBIBacTus29608_0521. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; KTUS562970:GHUX-512-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 22416 MW; 34CE6893E89091FB CRC64; MGLFQIHVVT DGQKAAGELA EVVRKVAQAG ADAVQLRYKA APALELYRLA EQLLPVLDGT STRLLINDRV DVALAAGAHG VHLAAKSLPV DRVKALLPAP MVVGRSVHSL EEALEAQRSG ADYVTFGHVF TTRSKPGAPP RGPDALRRIV ESLDIPVLAI GGITPDNAAE AARTGCAGVA VIGAVMDHAN PGAALSALAS ALEASGAAPA HPFRWPAS // ID D5X0M2_THIK1 Unreviewed; 504 AA. AC D5X0M2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Tint_1280; OS Thiomonas intermedia (strain K12) (Thiobacillus intermedius). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Thiomonas. OX NCBI_TaxID=75379; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C., RA Heinhorst S., Woyke T.; RT "Complete sequence of Thiomonas intermedia K12."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002021; ADG30668.1; -; Genomic_DNA. DR RefSeq; YP_003642998.1; NC_014153.1. DR ProteinModelPortal; D5X0M2; -. DR EnsemblBacteria; ADG30668; ADG30668; Tint_1280. DR GeneID; 9152011; -. DR KEGG; tin:Tint_1280; -. DR PATRIC; 38293078; VBIThiInt85915_1302. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR BioCyc; TINT75379:GH6C-1294-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 504 AA; 53600 MW; B3451D266BF57DD8 CRC64; MTTTAYLLTI DAHDPTGGSG QTADLATWAA LGWRGTSITT ALTAQNSYGV QGVQAAEVAL LRNSLRTLLA DGEPAAVKIG MISHAAVAEE VAQFVEARQC PVVWDPQLAS ADGSEPWARA HGGGLAMRLA QRADLITANR AEASALLDLP AWEMGPPPAA WINAIRSRWL EAGAPHRAVV VKGGNAWGAH STDWYITSST VLPLVSRRLP RSAHGSGSVH ASVCAARLAE GWSVLDAAAE AQLRAHAGID QAIAAGPGRP NTRTDARADS DDLPWLPLPG QSEEAPPDFA RLSGQIGFYP VVPDADWVLR LLEWGVCTIQ LRIKELEGAE LRMQIREAVQ AAREVPGTQL FINDHWREAI EAGAYGVHLG QDDVHTADLP AIHTAGLRLG LSTHTPAEIA RAHALRPSYI ALGPVFPTTL KAMPYRPLGL ERLTQWRQWL SPRYPVVAIG GISLEQMSAV RATGVSGAAV VSAVTQAVNP RLAVREALHI WPACADEAVA QAMV // ID D5X4P5_THIK1 Unreviewed; 220 AA. AC D5X4P5; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tint_2360; OS Thiomonas intermedia (strain K12) (Thiobacillus intermedius). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Thiomonas. OX NCBI_TaxID=75379; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C., RA Heinhorst S., Woyke T.; RT "Complete sequence of Thiomonas intermedia K12."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002021; ADG31709.1; -; Genomic_DNA. DR RefSeq; YP_003644039.1; NC_014153.1. DR ProteinModelPortal; D5X4P5; -. DR EnsemblBacteria; ADG31709; ADG31709; Tint_2360. DR GeneID; 9153094; -. DR KEGG; tin:Tint_2360; -. DR PATRIC; 38295265; VBIThiInt85915_2377. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; TINT75379:GH6C-2396-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22789 MW; 1F4C76A8BF6B504E CRC64; MTEAARRWPL AALRLHLVTD AALCGPRGVE AVVAAAVRGG ATCVQLREKQ LDTRPFVERA RALKALLASL GVPLLINDRL DVALAAGADG VHVGQSDLPP EDVRRLMPHA LIGLSVENPE QVRAAADMPV DYLGVSPVFS TPSKQDTAPA LGLEGLRAMR ALTDLPLIAI GGIDLNNAAQ VLAAGADGLA VVRALCAAPD PAAAAQALRQ LTDSSTFVHS // ID D5XCG5_THEPJ Unreviewed; 492 AA. AC D5XCG5; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 27. DE SubName: Full=Phosphomethylpyrimidine kinase; GN OrderedLocusNames=TherJR_0724; OS Thermincola potens (strain JR). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Thermincola. OX NCBI_TaxID=635013; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JR; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.; RT "Complete sequence of Thermincola sp. JR."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002028; ADG81591.1; -; Genomic_DNA. DR RefSeq; YP_003639492.1; NC_014152.1. DR ProteinModelPortal; D5XCG5; -. DR EnsemblBacteria; ADG81591; ADG81591; TherJR_0724. DR GeneID; 9148395; -. DR KEGG; tjr:TherJR_0724; -. DR PATRIC; 38272903; VBITheSp141296_0766. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR BioCyc; TPOT635013:GHIM-748-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 492 AA; 52051 MW; 425EA00F4A91171A CRC64; MKKALTIAGS DSGGGAGIQA DLKTFSAFGV YGMSVITAVT SQNTLGVSGF RAMPADFVGQ QMSDVLSDIG ADATKTGMLA NADIICEVAE KIREFKHENL VVDPVMVATS GDRLMEPEAE KALKDKLLPL ALVVTPNIAE AEVLSGIRIA NREDVEKAAQ IIYGWGPKGV IIKGGHLSGE AVDYYYDGKE IYEYRSPRVD TKNTHGTGCT FSAALAACLA LGMPLKKAIP IAKDYLYLAL LNADSLGAGH GPTNHLAGYF DHLTKAIRPA KGLPAAKTES NSRKLTGRKL YVITGQEFAK GRPVTEVVSQ ALAGGAGIIQ LREKKWTTRQ LVEVGRELQR LARENNALFI VNDRIDVALA VDADGVHLGQ DDMPVRMARR VIGPDMILGI SAETVEEALT AEKEGADYIG FGPVFHTDTK PDAGTARGLE LLAQVKKAVS IPVYGIGGIK LDNAAEVLSA GVDGVAVITA VVGADDITLA AQKFIHIMEG GR // ID D5XF79_THEPJ Unreviewed; 203 AA. AC D5XF79; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TherJR_1443; OS Thermincola potens (strain JR). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Thermincola. OX NCBI_TaxID=635013; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JR; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.; RT "Complete sequence of Thermincola sp. JR."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002028; ADG82300.1; -; Genomic_DNA. DR RefSeq; YP_003640201.1; NC_014152.1. DR ProteinModelPortal; D5XF79; -. DR EnsemblBacteria; ADG82300; ADG82300; TherJR_1443. DR GeneID; 9149131; -. DR KEGG; tjr:TherJR_1443; -. DR PATRIC; 38274503; VBITheSp141296_1549. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; TPOT635013:GHIM-1484-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 131 133 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21620 MW; B043B91DA66788D4 CRC64; MAEVWLVTNR KLVKNRCLVK KVESLCRRGI DGVILREKDL PLKELYHLAR EIRAVTKQYG VKLIVNKSIE TALAVEAEGI HLGSDALPLH NARLIVPAYM KIGVSVHSAE EAKTAAAEGA DYILAGNVYA TASKPNLAGR GTAWLSRVVQ TVYPLPVLAI GGINESNAGE VLKAGAAGVA AISGLLANNN PGKLIEIIKG QRT // ID D5XQ24_MYCTX Unreviewed; 212 AA. AC D5XQ24; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 16-APR-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TBDG_01442; OS Mycobacterium tuberculosis T92. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=515617; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T92; RG The Broad Institute Genome Sequencing Platform; RA Small P., Gagneaux S., Hopewell P., Young S.K., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Nusbaum C., Galagan J., Birren B.; RT "Annotation of Mycobacterium tuberculosis strain T92."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS985117; EFD56914.2; -; Genomic_DNA. DR ProteinModelPortal; D5XQ24; -. DR EnsemblBacteria; EFD56914; EFD56914; TBDG_01442. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 30 34 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22150 MW; CCF5677F18C6CC0C CRC64; MYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID D5Y075_MYCTX Unreviewed; 204 AA. AC D5Y075; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 16-APR-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=TBEG_03287; OS Mycobacterium tuberculosis T85. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=520141; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T85; RG The Broad Institute Genome Sequencing Platform; RA Small P., Gagneaux S., Hopewell P., Young S.K., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Nusbaum C., Galagan J., Birren B.; RT "Annotation of Mycobacterium tuberculosis strain T85."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS985147; EFD76059.2; -; Genomic_DNA. DR EnsemblBacteria; EFD76059; EFD76059; TBEG_03287. DR PATRIC; 30794163; VBIMycTub21498_0041. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 204 AA; 21590 MW; CF075ECB37DD00B1 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KAVVRYRRHQ RATAAGRARC RRSPDRGGAG DHLG // ID D5YC92_MYCTX Unreviewed; 222 AA. AC D5YC92; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TBGG_03559; OS Mycobacterium tuberculosis EAS054. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=520140; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EAS054; RG The Broad Institute Genome Sequencing Platform; RA Small P., Gagneaux S., Hopewell P., Young S.K., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Nusbaum C., Galagan J., Birren B.; RT "Annotation of Mycobacterium tuberculosis strain EAS054."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS985164; EFD60459.2; -; Genomic_DNA. DR ProteinModelPortal; D5YC92; -. DR SMR; D5YC92; 1-221. DR EnsemblBacteria; EFD60459; EFD60459; TBGG_03559. DR PATRIC; 26062798; VBIMycTub137161_0488. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID D5YN44_MYCTX Unreviewed; 222 AA. AC D5YN44; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TBBG_03456; OS Mycobacterium tuberculosis 02_1987. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=515616; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=02_1987; RG The Broad Institute Genome Sequencing Platform; RA Small P., Gagneaux S., Hopewell P., Young S.K., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Nusbaum C., Galagan J., Birren B.; RT "Annotation of Mycobacterium tuberculosis strain 02_1987."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS985180; EFD52126.2; -; Genomic_DNA. DR ProteinModelPortal; D5YN44; -. DR SMR; D5YN44; 1-221. DR EnsemblBacteria; EFD52126; EFD52126; TBBG_03456. DR PATRIC; 26026065; VBIMycTub81570_0087. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID D5YZY7_MYCTX Unreviewed; 222 AA. AC D5YZY7; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TBIG_03201; OS Mycobacterium tuberculosis GM 1503. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=537209; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GM 1503; RG The Broad Institute Genome Sequencing Platform; RA Small P., Gagneaux S., Hopewell P., Young S.K., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Nusbaum C., Galagan J., Birren B.; RT "Annotation of Mycobacterium tuberculosis strain GM 1503."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS986655; EFD72052.2; -; Genomic_DNA. DR ProteinModelPortal; D5YZY7; -. DR SMR; D5YZY7; 1-221. DR EnsemblBacteria; EFD72052; EFD72052; TBIG_03201. DR PATRIC; 30737826; VBIMycTub20418_0011. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID D5ZCD1_MYCTX Unreviewed; 222 AA. AC D5ZCD1; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TBJG_03433; OS Mycobacterium tuberculosis T17. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=537210; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T17; RG The Broad Institute Genome Sequencing Platform; RA Small P., Gagneaux S., Hopewell P., Young S.K., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Nusbaum C., Galagan J., Birren B.; RT "Annotation of Mycobacterium tuberculosis strain T17."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS986674; EFD45731.2; -; Genomic_DNA. DR ProteinModelPortal; D5ZCD1; -. DR SMR; D5ZCD1; 1-221. DR EnsemblBacteria; EFD45731; EFD45731; TBJG_03433. DR PATRIC; 30776152; VBIMycTub63299_0452. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID D6ARH8_STRFL Unreviewed; 219 AA. AC D6ARH8; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSGG_01246; OS Streptomyces roseosporus NRRL 15998. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457431; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL 15998; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M., RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., RA Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M., Galagan J., RA Nusbaum C., Birren B.; RT "Annotation of Streptomyces roseosporus strain NRRL 15998."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999644; EFE73880.2; -; Genomic_DNA. DR ProteinModelPortal; D6ARH8; -. DR EnsemblBacteria; EFE73880; EFE73880; SSGG_01246. DR PATRIC; 25406460; VBIStrRos54375_6391. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23049 MW; 56C408925563001C CRC64; MSTPSTPREQ LSDARLYLCT DARKRQGDLP AFLDAVLTSG VDIVQLRDKG MEAAEELDHL AVFADACRRH GKLLAVNDRA DVAHAIGADV LHLGQGDLPV PAARAIIGDG RLIGRSTHAE AEVDAAVAQD GVDYFCTGPC WPTPTKPGRH APGLGLVRYA ASLGSPRPWF AIGGIGAGNL DQVLDAGARR VVVVRAITEA DDPAAATAEL ARRVRAHTV // ID D6AWV9_9ACTO Unreviewed; 215 AA. AC D6AWV9; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSHG_01163, XNR_4774; OS Streptomyces albus J1074. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457425; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J1074; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M., RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., RA Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M., Galagan J., RA Nusbaum C., Birren B.; RT "Annotation of Streptomyces albus strain J1074."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J1074; RX PubMed=24495463; DOI=10.1186/1471-2164-15-97; RA Zaburannyi N., Rabyk M., Ostash B., Fedorenko V., Luzhetskyy A.; RT "Insights into naturally minimised Streptomyces albus J1074 genome."; RL BMC Genomics 15:97-97(2014). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004370; AGI91096.1; -; Genomic_DNA. DR EMBL; DS999645; EFE80721.2; -; Genomic_DNA. DR RefSeq; YP_007748099.1; NC_020990.1. DR EnsemblBacteria; AGI91096; AGI91096; XNR_4774. DR EnsemblBacteria; EFE80721; EFE80721; SSHG_01163. DR GeneID; 15148598; -. DR KEGG; salb:XNR_4774; -. DR PATRIC; 29731742; VBIStrAlb121414_0356. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22703 MW; 46D477897B43A415 CRC64; MSDTARARLA DARLYLCVDA RKRQGDLPEF LDAVLAGGVD IVQLRDKSLE AAEELELLEL FADACRRHGR LLAVNDRADV AHAAKADVLH LGQGDLPVPA ARAVIGGAPL VGRSTHSEAE AAAAAAQPGV DYFCTGPCWP TPTKPGRHAP GLDLVRYAAT LTTDRPWFAI GGIDAANLDE VTEAGARRVV VVRALTEADD PKAAAAGFAR RLRAL // ID D6BI07_FUSNU Unreviewed; 206 AA. AC D6BI07; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSAG_01840; OS Fusobacterium nucleatum subsp. animalis D11. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=556264; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D11; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., RA White A., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RT "Annotation of Fusobacterium sp. D11."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999815; EFD81804.2; -; Genomic_DNA. DR ProteinModelPortal; D6BI07; -. DR EnsemblBacteria; EFD81804; EFD81804; PSAG_01840. DR PATRIC; 28736062; VBIFusSp99290_1892. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22881 MW; 96882BEF86154D2F CRC64; MDLKDCKIYL VTDEKACNGK DFYKCIEESI KGGVKIVQLR EKNISTKDFY EKALKVKEIC KNYGVLFIIN DRLDITQAVE ADGVHLGQSD MPIEKAREIL KDKFLIGATA RNIEEAKKAE LLGADYIGSG AIFGTSTKDN AKKLEMEDLK KIVNSVKIPV FAIGGININN VWMLKNIGLQ GICSVSGILS EKDCKKAVEN ILKNFN // ID D6BI13_FUSNU Unreviewed; 206 AA. AC D6BI13; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Regulatory protein TENI; GN ORFNames=PSAG_01846; OS Fusobacterium nucleatum subsp. animalis D11. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=556264; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D11; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., RA White A., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RT "Annotation of Fusobacterium sp. D11."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ999815; EFD81810.2; -; Genomic_DNA. DR EnsemblBacteria; EFD81810; EFD81810; PSAG_01846. DR PATRIC; 28736074; VBIFusSp99290_1898. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 23989 MW; 39AD0FFC39AD8651 CRC64; MIENKIKLNI ISNRKLCENE NLEKQIEKIF SAYQRKIILE NFEIVSLTLR EKDLNKNKYL KLVEKIYPIC QKYRIDLILH QNYDLRLDNK YNIKGLHLSY NTFKSLNKNI REELIRKYKK IGVSIHSINE AKEVENLGAN YVVAGHIFKT DCKKDLEPRG LKFIQELSVI LTIPIFAIGG INQENSHLVI NSGAFGVCMM SSLMKD // ID D6CLD3_THIA3 Unreviewed; 220 AA. AC D6CLD3; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=THI_2748; OS Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Thiomonas. OX NCBI_TaxID=426114; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3As; RA Genoscope - CEA; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22701 / CIP 110005 / 3As; RX PubMed=20195515; DOI=10.1371/journal.pgen.1000859; RA Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M., RA Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V., RA Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J., RA Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., RA Joulian C., Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., RA Ortet P., Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., RA Slyemi D., Talla E., Weiss S., Weissenbach J., Medigue C., RA Bertin P.N.; RT "Structure, function, and evolution of the Thiomonas spp. genome."; RL PLoS Genet. 6:E1000859-E1000859(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP475956; CAZ89361.1; -; Genomic_DNA. DR RefSeq; YP_003625163.1; NC_014145.1. DR ProteinModelPortal; D6CLD3; -. DR EnsemblBacteria; CAZ89361; CAZ89361; THI_2748. DR GeneID; 13880815; -. DR KEGG; thi:THI_2748; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22907 MW; B1773D56737A0151 CRC64; MTDSARRWPL AALRLHLVTD AALCGPRGVE AVVAAAVRGG ATCVQLREKQ LDTRPFVERA RALKALLAPL EVPLIINDRL DVALAAGADG VHVGQSDLPP EDVRRLMPHA LIGLSVENPE QVRAAADMPV DYLGVSPVFS TPSKQDTAPA LGLEGLRAMR AFTDLPLIAI GGIDLNNAAQ VLAAGADGLA VVRALCAAPD PAAAAQALRQ LTDSSTFVHS // ID D6CSL2_THIA3 Unreviewed; 504 AA. AC D6CSL2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE SubName: Full=Putative Phosphomethylpyrimidine kinase ThiD/thiamine-phosphate diphosphorylase fused protein ThiE; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=THI_1602; OS Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Thiomonas. OX NCBI_TaxID=426114; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3As; RA Genoscope - CEA; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22701 / CIP 110005 / 3As; RX PubMed=20195515; DOI=10.1371/journal.pgen.1000859; RA Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M., RA Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V., RA Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J., RA Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., RA Joulian C., Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., RA Ortet P., Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., RA Slyemi D., Talla E., Weiss S., Weissenbach J., Medigue C., RA Bertin P.N.; RT "Structure, function, and evolution of the Thiomonas spp. genome."; RL PLoS Genet. 6:E1000859-E1000859(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP475956; CAZ88281.1; -; Genomic_DNA. DR RefSeq; YP_003624115.1; NC_014145.1. DR ProteinModelPortal; D6CSL2; -. DR EnsemblBacteria; CAZ88281; CAZ88281; THI_1602. DR GeneID; 13881838; -. DR KEGG; thi:THI_1602; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 504 AA; 53470 MW; BFF1C534690D68E4 CRC64; MTTTAYLLTI DAHDPTGGSG QAADLATWAA LGWRGTSITT ALTAQNSYGV QGVQAAEVAL LRNSLRTLLA DGEPAAVKIG MISHAAVAEE VAQFVEARQC PVVWDPQLAS ADGSEPWAQA HGGGLAMRLA QRADLITANR AEASALLDLP AWEMGPPPAA WINAIRSRWL EAGAPHRAVV VKGGNAWGAH STDWYITSST VLPLVSRRLP RSAHGSGSVH ASVCAARLAE GWSVLDAAAE AQLRAHAGID QAIAAGPGRP NTRTDARADS DDLPWLPLPG QSEEAPPDFA RLSGQIGFYP VVPDADWVLR LLEWGVCTIQ LRIKEIEGAE LRMQIREAVQ AAREVPGTQL FINDHWREAI EAGAYGVHLG QDDVHTADLP AIHTAGLRLG LSTHTPAEIA RAHALRPSYI ALGPVFPTTL KAMPYRPLGL ERLTQWRQWL SPRYPVVAIG GISLGQMSAV RATGVSGAAV VSAVTQAVNP RLAVREALHI WPACADEAVA QAMV // ID D6D5K2_9BACE Unreviewed; 202 AA. AC D6D5K2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN ORFNames=BXY_02170; OS Bacteroides xylanisolvens XB1A. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=657309; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XB1A; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Bernalier A.; RT "The genome sequence of Bacteriodes xylanisolvens XB1A."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929033; CBK65500.1; -; Genomic_DNA. DR RefSeq; YP_007791081.1; NC_021017.1. DR ProteinModelPortal; D6D5K2; -. DR EnsemblBacteria; CBK65500; CBK65500; BXY_02170. DR GeneID; 15190739; -. DR KEGG; bxy:BXY_02170; -. DR PATRIC; 42752906; VBIBacXyl109951_2434. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 202 AA; 23627 MW; 6FBE04FC6BF5D5DD CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNRFD ACQDQNYLAV IEHFKKLKKL SD // ID D6D5K6_9BACE Unreviewed; 206 AA. AC D6D5K6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BXY_02220; OS Bacteroides xylanisolvens XB1A. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=657309; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XB1A; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Bernalier A.; RT "The genome sequence of Bacteriodes xylanisolvens XB1A."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929033; CBK65504.1; -; Genomic_DNA. DR RefSeq; YP_007791085.1; NC_021017.1. DR ProteinModelPortal; D6D5K6; -. DR EnsemblBacteria; CBK65504; CBK65504; BXY_02220. DR GeneID; 15190743; -. DR KEGG; bxy:BXY_02220; -. DR PATRIC; 42752916; VBIBacXyl109951_2439. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22641 MW; E1E4F31A05734AB1 CRC64; MISLQFITHQ TEQYSYLESA RMALEGGCKW IQLRMKDAPL EEVEAVALQL KPLCKEHEAI LILDDHVELT KKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYSSILSQ MKEANIEIPV VAIGGITFED IPAILHTGVN GIALSGTILG ADNPVEETRR IIESDL // ID D6DB75_BIFLN Unreviewed; 917 AA. AC D6DB75; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 27. DE SubName: Full=Hydroxymethylpyrimidine synthase; GN ORFNames=BIL_00400; OS Bifidobacterium longum subsp. longum F8. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=722911; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F8; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Bifidobacterium longum longum F8."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929034; CBK69746.1; -; Genomic_DNA. DR RefSeq; YP_007766738.1; NC_021008.1. DR ProteinModelPortal; D6DB75; -. DR EnsemblBacteria; CBK69746; CBK69746; BIL_00400. DR GeneID; 15168730; -. DR KEGG; blg:BIL_00400; -. DR PATRIC; 42765679; VBIBifLon156230_0028. DR KO; K03147; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100355 MW; 00000DA28A98E1F6 CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLADTKA AGWFVVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID D6DFL9_CLOSC Unreviewed; 211 AA. AC D6DFL9; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLS_07240; OS Clostridium cf. saccharolyticum K10. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=717608; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K10; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Clostridium saccharolyticum-like K10."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929037; CBK76493.1; -; Genomic_DNA. DR RefSeq; YP_007848491.1; NC_021047.1. DR ProteinModelPortal; D6DFL9; -. DR EnsemblBacteria; CBK76493; CBK76493; CLS_07240. DR GeneID; 15302769; -. DR KEGG; cso:CLS_07240; -. DR PATRIC; 42835524; VBICloCf158569_2226. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22824 MW; 945D4C78613D6B44 CRC64; MDYSLYLVTD RRFIGKQTLA EAVEQAILGG CTMVQLREKE LSSLDFYWQA IKIKQITDSY HIPLIINDRV DIAMAVQADG VHIGQHDIPA AAVRKMIGKD MLVGVSVSTV EQAIKAQQDG ADYLGVGAMF PTGTKTDADF VSMENLKEIR TAVSLPIVVI GGINKDNAHC FKTIGIDGLA VVSAILAQPN IKVAAEELKA IFSGKESKNG F // ID D6DI52_CLOSC Unreviewed; 219 AA. AC D6DI52; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CLS_18500; OS Clostridium cf. saccharolyticum K10. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=717608; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K10; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Clostridium saccharolyticum-like K10."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929037; CBK77376.1; -; Genomic_DNA. DR RefSeq; YP_007849374.1; NC_021047.1. DR ProteinModelPortal; D6DI52; -. DR EnsemblBacteria; CBK77376; CBK77376; CLS_18500. DR GeneID; 15303652; -. DR KEGG; cso:CLS_18500; -. DR PATRIC; 42837702; VBICloCf158569_3493. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23538 MW; B52B3E0DD3BE931A CRC64; MKFSRDEIRR AMLLYAVTDR SWLREGESLS GVCREVLKGG ATFLQIREKD LDEASFEAEA RDLKELCAEY RVPFVVNDSV EIALKIQADG VHVGQSDIKG RDIRAMIGHD RILGISAGTP EEAAAAEKAG ADYIGVGAVF GTSTKKDARN LSVDALREIR NSVSIPIVAI GGIQPSNLME LAGTGVDGVA VVSAIFAAER PGEAAENLRK LAEEMVRHG // ID D6DNZ9_ENTCL Unreviewed; 213 AA. AC D6DNZ9; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ENC_01300; OS Enterobacter cloacae subsp. cloacae NCTC 9394. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=718254; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 9394; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J.; RT "The genome sequence of Enterobacter cloacae NCTC 9394."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929040; CBK84209.1; -; Genomic_DNA. DR RefSeq; YP_007844296.1; NC_021046.1. DR ProteinModelPortal; D6DNZ9; -. DR EnsemblBacteria; CBK84209; CBK84209; ENC_01300. DR GeneID; 15244386; -. DR KEGG; eclo:ENC_01300; -. DR PATRIC; 42921665; VBIEntClo152217_4129. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23140 MW; 8AD31FC6562FF99A CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIARLLE AGVRTLQLRI KDKRDEEVEA DVIAAIALGR RYHARLFIND YWRLAVKHQA YGVHLGQEDL ETTDLNAIRD AGLRLGVSTH DVMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLTQLA AHVKRLADYP TVAIGGISLE RAPAVLETGV GSIAVVSAIT QAADWQAATA QLLQLAGAGD ERS // ID D6DZM4_9FIRM Unreviewed; 234 AA. AC D6DZM4; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 22-JAN-2014, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN ORFNames=EUR_31270; OS Eubacterium rectale DSM 17629. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=657318; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17629; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Eubacterium rectale A1-86 (DSM 17629)."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929042; CBK92037.1; -; Genomic_DNA. DR RefSeq; YP_007774151.1; NC_021010.1. DR ProteinModelPortal; D6DZM4; -. DR EnsemblBacteria; CBK92037; CBK92037; EUR_31270. DR GeneID; 15176262; -. DR KEGG; ert:EUR_31270; -. DR PATRIC; 42986853; VBIEubRec131464_2940. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 234 AA; 25986 MW; E466DDCC8927087B CRC64; MNKEKLLYEN SKHALQSDNI IAITNRHLCS RPFMEQLERV CKLHPHAIVL REKDMPEAEY LSLARDVIAL CKKYDVQCML HSFINVAMEL EHPYIHLPLP ILEAYVKKIV SGNISTGMSK STDNYQQFFK VIGTSVHSVE DAIKAEQLGA TYMTAGHIFA TDCKKGLPPR GLDFLKNVCD AVEIPVYAIG GINIASNDNS TAYDAMPHIS VPRLADVMEC GATGGCIMSG MMRI // ID D6E157_9FIRM Unreviewed; 216 AA. AC D6E157; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUR_26090; OS Eubacterium rectale DSM 17629. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=657318; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17629; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Eubacterium rectale A1-86 (DSM 17629)."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929042; CBK91578.1; -; Genomic_DNA. DR RefSeq; YP_007773692.1; NC_021010.1. DR ProteinModelPortal; D6E157; -. DR EnsemblBacteria; CBK91578; CBK91578; EUR_26090. DR GeneID; 15175803; -. DR KEGG; ert:EUR_26090; -. DR PATRIC; 42985873; VBIEubRec131464_2454. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23027 MW; 4727BB8E2B33C927 CRC64; MNKTDLKLYA ITDRQWLHGA RLSEHVKLAI EGGATMIQIR DKDILSTDSD AGLKDEYNEA LEIKRICHEH KVPLIINDNV QFAIDIDADG VHLGQDDMNP AEARKLLGTD KIIGVTAKTV EQAKRAEADG ADYLGSGAVF GSTTKLNAKP MTKELLREIT AAVDIPVVAI GGINADNAVT LKGTGIAGIA VVGAIFASAD IKDAAKELAE ICDKIL // ID D6EJ00_STRLI Unreviewed; 223 AA. AC D6EJ00; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSPG_05440; OS Streptomyces lividans TK24. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457428; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TK24; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., RA Walker S., Walsh C.T., Wieland-Brown L.C., Galagan J., Nusbaum C., RA Birren B.; RT "The genome sequence of Streptomyces lividans strain TK24."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657756; EFD69800.2; -; Genomic_DNA. DR ProteinModelPortal; D6EJ00; -. DR EnsemblBacteria; EFD69800; EFD69800; SSPG_05440. DR PATRIC; 25373613; VBIStrLiv48540_3653. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23356 MW; 468C1FD3163723A8 CRC64; MPDTAPTAAR ARLADARLYL CTDARRSQGD LPEFLDAVLA GGVDIVQLRD KGMEAAEELE HLAVFADACA RHGKLLAVND RADVAHAARA DVLHLGQGDL PVPAARAILG DDVLIGRSTH AESEAAAAAA QEGVDYFCTG PCWPTPTKPG RHAPGLDLVR RTAALGTDRP WFAIGGIDLG NLDEVLEAGA RRVVVVRAIT AAEDPGAAAA EFARRLRQAP AHG // ID D6FXN6_9MYCO Unreviewed; 222 AA. AC D6FXN6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TBOG_00843; OS Mycobacterium africanum K85. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=611304; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K85; RG The Broad Institute Genome Sequencing Platform; RA Small P., Gagneaux S., Hopewell P., Young S.K., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain K85."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG663503; EFD42008.2; -; Genomic_DNA. DR ProteinModelPortal; D6FXN6; -. DR SMR; D6FXN6; 1-221. DR EnsemblBacteria; EFD42008; EFD42008; TBOG_00843. DR PATRIC; 30758668; VBIMycTub43399_3219. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID D6GPE6_9ENTR Unreviewed; 211 AA. AC D6GPE6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0485_04984; OS Klebsiella sp. 1_1_55. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=469608; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_55; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., RA Ambrose C., McDonald J., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Klebsiella sp. strain 1_1_55."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG745518; EFD82323.2; -; Genomic_DNA. DR ProteinModelPortal; D6GPE6; -. DR EnsemblBacteria; EFD82323; EFD82323; HMPREF0485_04984. DR PATRIC; 35849051; VBIKleSp73883_5041. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22958 MW; B6B4DFBEFBAA9D3E CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIERLLE AGVRTLQLRI KDQRDSDVEN DVIAAIALGR RYHARLFIND YWQLAIKHQA YGVHLGQEDL ETTDLSAIRK AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLDQLA RHIQRLADYP TVAIGGISLE KAPGVLATGV GSIAVVSAIT QAADWRAATD QLLALAGAGD E // ID D6H1U8_STAAU Unreviewed; 213 AA. AC D6H1U8; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAVG_02242; OS Staphylococcus aureus subsp. aureus M1015. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585156; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M1015; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain M1015."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG749011; EFD96717.2; -; Genomic_DNA. DR ProteinModelPortal; D6H1U8; -. DR EnsemblBacteria; EFD96717; EFD96717; SAVG_02242. DR PATRIC; 35748972; VBIStaAur105385_1639. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D6H9X2_NEIGO Unreviewed; 205 AA. AC D6H9X2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NGMG_00691; OS Neisseria gonorrhoeae DGI2. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=528348; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DGI2; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Yandava C., RA Gujja S., Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Rice P., Seifert H., RA Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Neisseria gonorrhoeae DGI2."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG749050; EFE03770.2; -; Genomic_DNA. DR ProteinModelPortal; D6H9X2; -. DR EnsemblBacteria; EFE03770; EFE03770; NGMG_00691. DR PATRIC; 29980434; VBINeiGon132211_2219. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21779 MW; 1353772F6A7897A9 CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFQ TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID D6HIT0_STAAU Unreviewed; 213 AA. AC D6HIT0; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SCAG_02461; OS Staphylococcus aureus subsp. aureus 58-424. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585144; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=58-424; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain 58-424."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG749070; EFE24985.2; -; Genomic_DNA. DR ProteinModelPortal; D6HIT0; -. DR EnsemblBacteria; EFE24985; EFE24985; SCAG_02461. DR PATRIC; 35791483; VBIStaAur114565_2658. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D6I3N4_ECOLX Unreviewed; 211 AA. AC D6I3N4; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECCG_04546; OS Escherichia coli B088. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=550672; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B088; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli B088."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG749152; EFE60770.2; -; Genomic_DNA. DR ProteinModelPortal; D6I3N4; -. DR EnsemblBacteria; EFE60770; EFE60770; ECCG_04546. DR PATRIC; 35861468; VBIEscCol142334_4069. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22997 MW; 2765939480105927 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDIEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D6IGR2_ECOLX Unreviewed; 211 AA. AC D6IGR2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDG_04651; OS Escherichia coli B185. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=550676; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B185; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli B185."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG749189; EFF03819.2; -; Genomic_DNA. DR ProteinModelPortal; D6IGR2; -. DR SMR; D6IGR2; 10-208. DR EnsemblBacteria; EFF03819; EFF03819; ECDG_04651. DR PATRIC; 35871384; VBIEscCol145366_4251. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D6IX66_ECOLX Unreviewed; 211 AA. AC D6IX66; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECGG_04882; OS Escherichia coli FVEC1412. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656380; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FVEC1412; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli FVEC1412."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG749233; EFE98418.2; -; Genomic_DNA. DR ProteinModelPortal; D6IX66; -. DR EnsemblBacteria; EFE98418; EFE98418; ECGG_04882. DR PATRIC; 35892590; VBIEscCol140962_5128. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 4A5B4907CA38B2E8 CRC64; MYQPDFPPVP FHLGLYPVVD SAQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAITLGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVMATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D6J293_STAAU Unreviewed; 213 AA. AC D6J293; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAZG_02250; OS Staphylococcus aureus subsp. aureus M809. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585157; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M809; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Robinson A., Wong A., Smyth D., Young S.K., Zeng Q., RA Koehrsen M., Godfrey P., Alvarado L., Berlin A., Bochicchio J., RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Wirth D.F., Galagan J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus strain M809."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG749318; EFF08734.2; -; Genomic_DNA. DR ProteinModelPortal; D6J293; -. DR EnsemblBacteria; EFF08734; EFF08734; SAZG_02250. DR PATRIC; 35784045; VBIStaAur4824_1754. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D6JHV0_ECOLX Unreviewed; 211 AA. AC D6JHV0; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECEG_04622; OS Escherichia coli B354. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=550677; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B354; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli B354."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG749343; EFF10523.2; -; Genomic_DNA. DR ProteinModelPortal; D6JHV0; -. DR EnsemblBacteria; EFF10523; EFF10523; ECEG_04622. DR PATRIC; 35882060; VBIEscCol143929_4569. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22997 MW; 58CE6F960030BE0E CRC64; MYQPDFPPVP FHLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEAEA DVVAAITLGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D6JJ44_NEIGO Unreviewed; 205 AA. AC D6JJ44; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NGNG_00958; OS Neisseria gonorrhoeae F62. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=528351; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F62; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., RA Jen D., Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Rice P., Seifert H., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Neisseria gonorrhoeae strain F62."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG749348; EFF40973.2; -; Genomic_DNA. DR ProteinModelPortal; D6JJ44; -. DR EnsemblBacteria; EFF40973; EFF40973; NGNG_00958. DR PATRIC; 36018692; VBINeiGon70821_0294. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21748 MW; 7823772E2E3D96ED CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFP TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID D6JU92_ACIPI Unreviewed; 298 AA. AC D6JU92; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 11-DEC-2013, entry version 21. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=HMPREF0013_01722; OS Acinetobacter sp. SH024. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=575565; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH024; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., Peleg A., Seifert H., Haas B., Henn M.R., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter sp. SH024."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG753601; EFF86391.2; -; Genomic_DNA. DR ProteinModelPortal; D6JU92; -. DR EnsemblBacteria; EFF86391; EFF86391; HMPREF0013_01722. DR PATRIC; 36270798; VBIAciSp53575_1829. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 298 AA; 34132 MW; 13D42C0DD18DCD91 CRC64; MPKPIVDVAI AILIHRGKIL VGWREEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWAWYTRDQL LHLNFPKANK NIIKRLYWPH LIKISNTLST VESNDALLYW RIEEFEPQYI EQLTALDEGQ RSNLIINVDI WRQLSPELQK QIKAVHLKQS QLMNLHKGDL TVGVRYIAAC HDAVSLKQAQ QIGCDAVFIS PVKSTTTHPE AVALGWERFS DLAQNSQIPV FALGGVHPDD LATAQQHGAY GLAGIRNF // ID D6JUU0_ACIPI Unreviewed; 203 AA. AC D6JUU0; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0013_01923; OS Acinetobacter sp. SH024. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=575565; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH024; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., Peleg A., Seifert H., Haas B., Henn M.R., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter sp. SH024."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG753601; EFF86589.2; -; Genomic_DNA. DR ProteinModelPortal; D6JUU0; -. DR EnsemblBacteria; EFF86589; EFF86589; HMPREF0013_01923. DR PATRIC; 36271200; VBIAciSp53575_2025. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21781 MW; 5FE379955B88F8B2 CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKVE KTDQPAEVEQ IKLLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT STKPEAGNVG IEVIKQAAAQ YDVPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID D6KB80_9ACTO Unreviewed; 220 AA. AC D6KB80; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSTG_00869; OS Streptomyces sp. e14. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=645465; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E14; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Streptomyces sp. strain e14."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG753626; EFF90551.2; -; Genomic_DNA. DR ProteinModelPortal; D6KB80; -. DR EnsemblBacteria; EFF90551; EFF90551; SSTG_00869. DR PATRIC; 35769320; VBIStrSp49670_0233. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23220 MW; 9C5C2CCB69B9DA1C CRC64; MSDAAIASAR ERLADARLYL CTDARKDRGD LAEFLDAVLA GGVDIVQLRD KGMEAGEELE HLEVFADACA RHGKLLAVND RADVAHAARA DVLHLGQGDL PVPAARAILG DDVLIGRSTH AEPEADAAAV QDGVDYFCTG PCWPTPTKPG RHAPGLGLVR HTAALGADRP WFAIGGIDLG NLDQVLEAGA RRVVVVRAIT EADDPGAAAA EFAERLREPR // ID D6KL66_9FIRM Unreviewed; 505 AA. AC D6KL66; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE SubName: Full=Hydroxyethylthiazole kinase; GN ORFNames=HMPREF0873_01539; OS Veillonella sp. 3_1_44. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=457416; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_44; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., McDonald J., Ambrose C.E., Strauss J.C., RA Allen-Vercoe E., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Veillonella sp. 3_1_44."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770201; EFG22659.2; -; Genomic_DNA. DR ProteinModelPortal; D6KL66; -. DR EnsemblBacteria; EFG22659; EFG22659; HMPREF0873_01539. DR PATRIC; 36277935; VBIVeiSp18830_1539. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 505 AA; 54126 MW; C0B152F04517FC1B CRC64; MIYNNPNING SNWPELNILE TLRKKNPLVI CITNDVVRTF TANGLLAIGA SPVMSECSED LKDLIVHAAA LLINIGTVTP DKVTYYKEAV KLAKAHEVPI VLDPVGCHAG AYRLSVVLDL IKTGAISLLR GNQSEIKAIY DALNTNHKID SSLSGKGVDG AQVEDSAIIT YRLARQINCP VVATGEEDYV SDGTRVFAVP HGHPIMTAVT GTGCLLGAVL AAFFSSYYPF MHNMSIGEFL AYALAYYGLA GESAVKVSGV KPGSFSVAFM DALYEFDDAM LLSGNRIRPV VVPDQLKVYF ISGTQDVGFN ERHLLDTVEA ACRGGVTCFQ FREKGTGTLE GQQKLELAQQ LKEICAMYNV LYIINDDVDL AVAVNADGVH VGQEDMRLED VRNLVGNKVV GISIHSVEEL HKTDVVYADC VGVGPMYATS SKPDAQEPCG PDRITELRAE GLTLPCVGIG GITLDNATPV LQAGASGVAV ISAIAHADDP YEAAEEFKNL VDNIK // ID D6KLQ4_9FIRM Unreviewed; 172 AA. AC D6KLQ4; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 16-OCT-2013, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF0873_01731; OS Veillonella sp. 3_1_44. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=457416; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_44; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., McDonald J., Ambrose C.E., Strauss J.C., RA Allen-Vercoe E., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Veillonella sp. 3_1_44."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770201; EFG22847.2; -; Genomic_DNA. DR ProteinModelPortal; D6KLQ4; -. DR EnsemblBacteria; EFG22847; EFG22847; HMPREF0873_01731. DR PATRIC; 36278315; VBIVeiSp18830_1722. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 172 AA; 19026 MW; E1C43F952459428A CRC64; MNRKDKLTEV MNACPIYGIT GGTRDVVPLV KDMLSAGIRI IQYREKGKTP ILRYQEAMIL RRLTSNYHAL LIIDDYVDLA LAVHADGVHI GQADLPPNTV RRIVGPNMLI GWSTHSISDL KVANRYTGVI DYIGVGPIFS TQTKPNANPV GISYVYWAKQ FSKFPIVAIG GD // ID D6KQX9_9FIRM Unreviewed; 91 AA. AC D6KQX9; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF0874_01377; OS Veillonella sp. 6_1_27. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=450749; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_27; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., McDonald J., Ambrose C.E., Strauss J.C., RA Allen-Vercoe E., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Veillonella sp. 6_1_27."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770217; EFG24225.2; -; Genomic_DNA. DR EnsemblBacteria; EFG24225; EFG24225; HMPREF0874_01377. DR PATRIC; 36281464; VBIVeiSp6271_1362. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 91 AA; 10044 MW; 549AA06C3491A6C6 CRC64; MDTFTIGNIG VGPIFSTQTK PNANPVGISY IYWAKQFSKA PIVAIGGIKT TNADTVWQVH PDFICAVSEI TESDNIQNTI YELMMGYSRV R // ID D6KR99_9FIRM Unreviewed; 505 AA. AC D6KR99; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE SubName: Full=Hydroxyethylthiazole kinase; GN ORFNames=HMPREF0874_01502; OS Veillonella sp. 6_1_27. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=450749; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_27; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., McDonald J., Ambrose C.E., Strauss J.C., RA Allen-Vercoe E., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Veillonella sp. 6_1_27."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770217; EFG24345.2; -; Genomic_DNA. DR ProteinModelPortal; D6KR99; -. DR EnsemblBacteria; EFG24345; EFG24345; HMPREF0874_01502. DR PATRIC; 36281732; VBIVeiSp6271_1489. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 505 AA; 54152 MW; 466783B0F4FF57A5 CRC64; MIYNNPNING SNWPELNILE TLRKKNPLVI CITNDVVRTF TANGLLAIGA SPVMSECSED LKDLIVHAAA LLINIGTVTP DKVTYYKEAI KLAKAHEVPI VLDPVGCHAG AYRLSVVLDL IKTGAISLLR GNQSEIKAIY DALNTNHKID SSLSGKGVDG AQVEDSAIIT YRLARQINCP VVATGEEDYV SDGTRVFAVP HGHPIMTAVT GTGCLLGAVL AAFFSSYYPF MHNMSIGEFL AYALAYYGLA GESAVKVSGV KPGSFSVAFM DALYEFDDAM LLSGNRIRPV VVPDQLKVYF ISGTQDVGFN ERHLLETVEA ACRGGVTCFQ FREKGTGTLE GQQKLELAQQ LKEICAMYNV LYIINDDVNL AVAVNADGVH VGQEDMRLED VRNLVGNKVV GISIHSVEEL HKTDVVYADC VGVGPMYATS SKPDAQEPCG PDRITELRAE GLTLPCVGIG GITLDNATPV LQAGASGVAV ISAIAHADNP YEAAEEFKNL VDNIK // ID D6L9C9_FUSNV Unreviewed; 206 AA. AC D6L9C9; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 16-APR-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0405_00055; OS Fusobacterium nucleatum subsp. vincentii 3_1_27. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469602; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_27; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 3_1_27."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007064; EFG33793.1; -; Genomic_DNA. DR ProteinModelPortal; D6L9C9; -. DR EnsemblBacteria; EFG33793; EFG33793; HMPREF0405_00055. DR PATRIC; 36478608; VBIFusSp21485_1549. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22625 MW; 8A608BED86F95D99 CRC64; MDLKDCKIYL VTDENSCNGK DFYKCIEEAI KGGVKIVQLR EKTLSTKDFF IKALKVKEIC KSYGVLFIIN DRLDIAQAVE ADGVHLGQSD MPIEKAKEIL KDKFLIGVTA KNIEEAKKAE LLGADYIGSG AIFGTSTKDN AKKLDMKDLK KIVNSIKIPV FAIGGINTNN VCMLKNIGLQ GICSVSGILA EKDCKKAVEN ILKNFN // ID D6L9D5_FUSNV Unreviewed; 206 AA. AC D6L9D5; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 16-APR-2014, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF0405_00061; OS Fusobacterium nucleatum subsp. vincentii 3_1_27. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469602; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_27; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 3_1_27."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007064; EFG33799.1; -; Genomic_DNA. DR ProteinModelPortal; D6L9D5; -. DR EnsemblBacteria; EFG33799; EFG33799; HMPREF0405_00061. DR PATRIC; 36478620; VBIFusSp21485_1555. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 23963 MW; 04B7AF8D603271A8 CRC64; MIENKIKLNI ISNRKLCENE NLEKQIEKIF SAYQRKIILE NFEIVALTLR EKDLYKNEYL KLVEKIYPIC QKYRIDLILH QNYDLVLEDK YNIEGIHLSY NTFKSLNKNI RKELIKKYKK IGVSIHSIDE AKEAENLGAT YIVAGHIFKT DCKKDLEPRG LEFIQELSSA LIIPIFVIGG INQENSHLVI NNGAFGVCMM SSLMKH // ID D6LI37_9FUSO Unreviewed; 190 AA. AC D6LI37; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Regulatory protein TenI; GN ORFNames=HMPREF0400_01401; OS Fusobacterium periodonticum 1_1_41FAA. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469621; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_41FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., Strauss J.C., Ambrose C.E., Allen-Vercoe E., RA Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 1_1_41FAA."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770383; EFG28063.2; -; Genomic_DNA. DR ProteinModelPortal; D6LI37; -. DR EnsemblBacteria; EFG28063; EFG28063; HMPREF0400_01401. DR PATRIC; 36485120; VBIFusSp71368_1935. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 190 AA; 21920 MW; D2B906E73611ACC3 CRC64; MRMKILKSKL KKFFLAYERK IILKNFDIVA LTLREKDLNK NEYLKLIEKV YPICQKYKIN LILHQNYDLN LDEKYKIDGI HLSYNIFKSL NENIKAELIK KYKRIGVSIH SLDEAKEIEN LGASYVVAGH IFETDCKKGL EPRGLKFVED LSSTLTIPIF AIGGIDEKNS LSVIDSGAFS VCMMSSIMKY // ID D6LI43_9FUSO Unreviewed; 206 AA. AC D6LI43; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0400_01407; OS Fusobacterium periodonticum 1_1_41FAA. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469621; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_41FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., Strauss J.C., Ambrose C.E., Allen-Vercoe E., RA Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 1_1_41FAA."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770383; EFG28069.2; -; Genomic_DNA. DR ProteinModelPortal; D6LI43; -. DR EnsemblBacteria; EFG28069; EFG28069; HMPREF0400_01407. DR PATRIC; 36485132; VBIFusSp71368_1941. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22440 MW; 07A90E6AC69A74E6 CRC64; MELKACKIYL VTDEKACLGK DFYVCIEEAI KGGVKIVQLR EKNISTKDFY EKALKVKEIC KNYGALFIIN DRLDIAQAVG ADGVHLGQSD MPIEKAREIL KDKFLIGATA RNVEEAKRAE LLGADYIGSG AIFGTNTKDN AKKLEIGELK KIVASVKIPV FAIGGININN VSSLKNIGLQ GICAVSGILS EKDCKKAVDI MLKNFN // ID D6LK68_9RHIZ Unreviewed; 221 AA. AC D6LK68; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 11-DEC-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAZG_03089; OS Brucella sp. NVSL 07-0026. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520448; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVSL 07-0026; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Tsolis R., Young S., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Walk T., White J., Yandava C., Haas B., Henn M.R., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella sp. NVSL 07-0026."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770507; EFG38598.2; -; Genomic_DNA. DR ProteinModelPortal; D6LK68; -. DR EnsemblBacteria; EFG38598; EFG38598; BAZG_03089. DR PATRIC; 35166789; VBIBruSp103899_0080. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23290 MW; DF832D55309C075C CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQTVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D6LLE5_9RHIZ Unreviewed; 203 AA. AC D6LLE5; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 11-DEC-2013, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAZG_00521; OS Brucella sp. NVSL 07-0026. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520448; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVSL 07-0026; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Tsolis R., Young S., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Walk T., White J., Yandava C., Haas B., Henn M.R., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella sp. NVSL 07-0026."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770510; EFG37199.2; -; Genomic_DNA. DR ProteinModelPortal; D6LLE5; -. DR EnsemblBacteria; EFG37199; EFG37199; BAZG_00521. DR PATRIC; 35168294; VBIBruSp103899_0415. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22288 MW; 4C10F708105D876B CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA SSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D6LZV3_STAAU Unreviewed; 213 AA. AC D6LZV3; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SIAG_02627; OS Staphylococcus aureus subsp. aureus EMRSA16. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=585154; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EMRSA16; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease.; RA Feldgarden M., Robinson D.A., Wong A., Smyth D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Walk T., White J., Yandava C., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Staphylococcus aureus subsp. aureus EMRSA16."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770528; EFG56988.2; -; Genomic_DNA. DR ProteinModelPortal; D6LZV3; -. DR EnsemblBacteria; EFG56988; EFG56988; SIAG_02627. DR PATRIC; 37076919; VBIStaAur50858_2142. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D6M2D0_9ACTO Unreviewed; 235 AA. AC D6M2D0; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSBG_06218; OS Streptomyces sp. SPB74. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=465543; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SPB74; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Streptomyces sp. strain SPB74."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770539; EFG65399.2; -; Genomic_DNA. DR ProteinModelPortal; D6M2D0; -. DR EnsemblBacteria; EFG65399; EFG65399; SSBG_06218. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 235 AA; 24715 MW; B86EC6B3F6544116 CRC64; MPDATPHAAA RTALADARLY LCTDARKRQG DLPAFLDAVL SGGVDIVQLR DKSLEAAEEL ELLQVFADAC RRHGTLLAVN DRADIAHAAR ADVLHLGQGD LPVPAARALT GPDALIGRST HSEAEARAAA TQDGVDYFCT GPCWPTPTKP GRPAPGLPLV RYAAALGTAR PWFAIGGIDA ARLDQVLDAG ARRVVVVRAL TEAADPGDAA RALARRLRAL PLEKPPVHSV DKKSA // ID D6M8F3_9CLOT Unreviewed; 195 AA. AC D6M8F3; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=CLCAR_0687; OS Clostridium carboxidivorans P7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=536227; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P7; RX PubMed=20729368; DOI=10.1128/JB.00877-10; RA Paul D., Austin F.W., Arick T., Bridges S.M., Burgess S.C., RA Dandass Y.S., Lawrence M.L.; RT "Genome sequence of the solvent-producing bacterium Clostridium RT carboxidivorans strain P7T."; RL J. Bacteriol. 192:5554-5555(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770678; EFG89526.1; -; Genomic_DNA. DR ProteinModelPortal; D6M8F3; -. DR EnsemblBacteria; EFG89526; EFG89526; CLCAR_0687. DR PATRIC; 37924178; VBICloCar96475203719_0659. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 195 AA; 21484 MW; 50168B0236B14BAA CRC64; MFNLKEDKKI YVVTNRHLID KSSNLCEVIE KCAFKGADGV ILREKDLENE ALKHLGEKIK IITDKYNIPL IINGNIKVAL DINAYGFHTG FENFKNMKGN ETICEKIAVG VSVHKVEEAV EAEKLGANYL LAGHIFETDC KLGLKGRGMG FLEKICESVT IPVIAIGGIK EDNIKKVLNT KAYGVAIMSS AMKIG // ID D6S6Z7_FINMA Unreviewed; 212 AA. AC D6S6Z7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0391_10219; OS Finegoldia magna ATCC 53516. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Finegoldia. OX NCBI_TaxID=525282; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 53516; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHM02000001; EFH93851.1; -; Genomic_DNA. DR ProteinModelPortal; D6S6Z7; -. DR EnsemblBacteria; EFH93851; EFH93851; HMPREF0391_10219. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23417 MW; 3C8CA3A49BDD4507 CRC64; MNKEFNLGLN LVTNKQTLKG RDLSETIEIA LKNGADSVRL REKNMDTRSI MREAFRIKEI TQSMGKLLIV NDRVDIAKAC DVDGVHLGQK DMPIKYAREI LGDNKIIGIS CHTLEQALEA QEAGADYIGV GAIFPTFTGD DFVRVTIDTL KEIAEKIHIP ITAIGGINKN NIRMIFDCNV DSVSLTSAVF STGDVAASTQ ELKQKFDMIL SR // ID D6S8D4_FINMA Unreviewed; 214 AA. AC D6S8D4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0391_10720; OS Finegoldia magna ATCC 53516. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Finegoldia. OX NCBI_TaxID=525282; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 53516; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHM02000002; EFH93062.1; -; Genomic_DNA. DR ProteinModelPortal; D6S8D4; -. DR EnsemblBacteria; EFH93062; EFH93062; HMPREF0391_10720. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23661 MW; 303AA37F5D65ADDA CRC64; MREKLNLSLY LVTDRTNVVD EEKFLTKIEE ALKGGVTLVQ LREKNISTKE YIDLAKKVKT ICDKFDVPLL IDDRIDVCLA SDCAGVHLGD EDMEIEDARR ILGDNYIIGA TAKSVDRAIQ CEKEGADYLG VGAIYPTKTH VKTKITSVET LIDINNSISI KTVAIGGLNE DNMDVLKSSG ASGIAVVRAL MNDDNPQDKA HRLLEKSKQI LELR // ID D6SEN3_STAAU Unreviewed; 213 AA. AC D6SEN3; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0769_11067; OS Staphylococcus aureus subsp. aureus MN8. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=548470; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MN8; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJA02000002; EFH95684.1; -; Genomic_DNA. DR ProteinModelPortal; D6SEN3; -. DR EnsemblBacteria; EFH95684; EFH95684; HMPREF0769_11067. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D6SNF6_9DELT Unreviewed; 214 AA. AC D6SNF6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Dthio_PD1633; OS Desulfonatronospira thiodismutans ASO3-1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfohalobiaceae; Desulfonatronospira. OX NCBI_TaxID=555779; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ASO3-1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Land M.L., RA Hauser L., Kyrpides N., Mikhailova N., Muyzer G., Woyke T.; RT "The draft genome of Desulfonatronospira thiodismutans ASO3-1."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJN02000002; EFI34282.1; -; Genomic_DNA. DR ProteinModelPortal; D6SNF6; -. DR EnsemblBacteria; EFI34282; EFI34282; Dthio_PD1633. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23133 MW; 763647029C098B84 CRC64; MTKEIDYSLY LVTDNGLCMG RDLTRVVLDA VQGGVSMVQI REKNSTAGEF LNTARALQQR LSDSGVPLII NDRVDVAMAA GAHGVHIGQE DLPYQVVREM LGPDKIIGVS INTYDQLWQA SLTDVDYLSL SPVFPTQTKT DTKEPFGLEG LKKARAMTGK PLITIGGINR DNLADIMATG VDGVALVSAV CSADSPADAA RELVRIIRDN KMRI // ID D6SXK4_GARVA Unreviewed; 876 AA. AC D6SXK4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-MAR-2014, entry version 24. DE SubName: Full=Thiamine biosynthesis protein ThiC; DE EC=2.5.1.3; GN ORFNames=GVAMD_0577; OS Gardnerella vaginalis AMD. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=682147; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AMD; RX PubMed=20540756; DOI=10.1186/1471-2164-11-375; RA Harwich M.D.Jr., Alves J.M., Buck G.A., Strauss J.F.III., RA Patterson J.L., Oki A.T., Girerd P.H., Jefferson K.K.; RT "Drawing the line between commensal and pathogenic Gardnerella RT vaginalis through genome analysis and virulence studies."; RL BMC Genomics 11:375-375(2010). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADAM01000007; EFH27347.1; -; Genomic_DNA. DR EnsemblBacteria; EFH27347; EFH27347; GVAMD_0577. DR PATRIC; 37851626; VBIGarVag146634_0777. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Transferase; Zinc. SQ SEQUENCE 876 AA; 97671 MW; D51A1A46EEF35CD7 CRC64; MRNQFNLSAC FIADPQACNN RPLTDIVDDA LRAGATFIRL HCNNENAKEI TTIARDIAQI IEDNNKCDSV TFVIDERVDV VWQARNQSIK VDGVHLAQSD MEPREARALL GEDAVIGLSV ETESLVKVIN ELPDGCIDYI CVTAMHNPEE GCESTTAAYE LEANHTTLDE AKINTICSAS DFPVLVGGRT ALDDIDTIAH TKAAGWFVSE ALYSSETPES TMREFVEHWK AVRGEEKHGY AKRVIVAENS ESKSSETQEK KPTFINAKEA KDAAKLAKQQ RVDIAARGCT QRDKAHIRKT TPVHFEYEYG SYDLEVPYTE IKLSDTPGVG PNPPFKDYNT EGPKCDPKEG LAPLRLDWIR DRGDVVEYEG RRRNLQDDGK RAIKRGKASK EWRGRTHKPM KGADHPITQM WYARHGITTP EMQYVATREN CDVELVREEI AAGRAVIPCN INHPEAEPMI IGSRFLTKLN ANMGNSAVTS SIDEEVEKLT WATKWGADTV MDLSTGNDIH TTREWILRNS PVPIGTVPMY QALEKVEDDA SKLSWELFRD TVIEQCEQGV DYMTIHAGVL LRYVPLTANR VTGIVSRGGS IMAEWCLQHH QESFLYTHFE ELCEIFAKYD VAFSLGDGLR PGSLADANDA AQLSELMTLG ELTKIAWKHD VQVMIEGPGH VPFDTVRMNI EMEKAICQNA PFYTLGPLTT DTAPGYDHIT SAIGGVEIAR YGTAMLCYVT PKEHLGLPNK DDVKQGVIAY KIACHAADLA KHHPHAMDRD NAISKARFEF RWLDQFNLSY DPDTAIAFHD ETLPAEPAKM AHFCSMCGPK FCSMAISQNI RKRFGGAAQQ EQLVEEARSQ AIADGMKEMS KKFQESGSSL YQSVKA // ID D6SYR6_GARVA Unreviewed; 525 AA. AC D6SYR6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-MAR-2014, entry version 18. DE SubName: Full=Hydroxyethylthiazole kinase, sugar kinase family; DE EC=2.7.1.50; GN ORFNames=GVAMD_0457; OS Gardnerella vaginalis AMD. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=682147; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AMD; RX PubMed=20540756; DOI=10.1186/1471-2164-11-375; RA Harwich M.D.Jr., Alves J.M., Buck G.A., Strauss J.F.III., RA Patterson J.L., Oki A.T., Girerd P.H., Jefferson K.K.; RT "Drawing the line between commensal and pathogenic Gardnerella RT vaginalis through genome analysis and virulence studies."; RL BMC Genomics 11:375-375(2010). CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADAM01000010; EFH26910.1; -; Genomic_DNA. DR EnsemblBacteria; EFH26910; EFH26910; GVAMD_0457. DR PATRIC; 37852441; VBIGarVag146634_1171. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 525 AA; 56208 MW; 940443023BF48464 CRC64; MTTCNTEKTN TCNEANEYCT SSTTQVDTCF SVRARRRMFL NDVRQCIERV RTQQPLTHCI TNVIVQDITA NALLAAGASP IMVTDPEEAH ALAQIATGVL INVGTFHQPE TSEYMRAAVE GCEKADTPWV LDPVGIGVPA LAPRARFVHE IIKHHPTVIR ANASEIMALA GKESNGKGVD SHDNVNDALQ AARELAKKYG SVVAISGEKD AIYAHGCLAR VTGGHKAMTK VVGTGCALGA LVAAYVGANP ERPLAATVAA HVHAAAAGTW AARQTTAPGT FRTLWMDALS TLSVNDMFSL TNIEFTVEPV DWTLYLVTDP RMGNRPEEEV AVESVEGGVT VVQLRDKYSN DAEISAKAKK LRHALIDSGH GDVPVFIDDH VDCAAHLGFN LHVGQKDTPF VEARKAMPAE WMVGLSCARP DLMEKAYREC KENDVPLPDV IGIGAAFETH TKAHDVPPLG VEGVNEVAKV AHSMGVKTLA IGGIHENTVF PIRGLELDGV CTVSALMCAE DAGKVARELK SVITE // ID D6SZL1_GARVA Unreviewed; 876 AA. AC D6SZL1; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-MAR-2014, entry version 23. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN ORFNames=GV51_0781; OS Gardnerella vaginalis 5-1. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=682148; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5-1; RX PubMed=20540756; DOI=10.1186/1471-2164-11-375; RA Harwich M.D.Jr., Alves J.M., Buck G.A., Strauss J.F.III., RA Patterson J.L., Oki A.T., Girerd P.H., Jefferson K.K.; RT "Drawing the line between commensal and pathogenic Gardnerella RT vaginalis through genome analysis and virulence studies."; RL BMC Genomics 11:375-375(2010). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADAN01000003; EFH71954.1; -; Genomic_DNA. DR EnsemblBacteria; EFH71954; EFH71954; GV51_0781. DR PATRIC; 37853105; VBIGarVag144721_0221. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 876 AA; 97690 MW; 309C855394B4D4B5 CRC64; MRNQFNLSAC FIADPQACNN RPLTDIVDDA LRAGATFIRL HCNNENAKEI TTIARDIAQI IEDNNKCDSV TFVIDERVDV VWQARNQSIK VDGVHLAQSD MEPREARALL GEDAVIGLSV ETESLVKVIN ELPDGCIDYI CVTAMRNPEE GCESTTAAYE LEANHTTLDE AKINTICSAS DFPVLVGGRT ALDDIDTIAH TKAAGWFVSE ALYSSETPES TMREFVEHWK AVRGEEKHGY AKRVIVAENS ESKSSETQEK KPTFINAKEA KDAAKLAKQQ RVDIAARGCT QRDKAHIRKT TPIHFEYEYG SYDLEVPYTE IKLSDTPGVG PNPPFKDYNT EGPKCDPKEG LAPLRLDWIR DRGDVVEYEG RRRNLQDDGK RAIKRGKASK EWRGRTHKPM KGADHPITQM WYARHGITTP EMQYVATREN CDVELVREEV AAGRAVIPCN INHPEAEPMI IGSRFLTKLN ANMGNSAVTS SIDEEVEKLT WATKWGADTV MDLSTGNDIH TTREWILRNS PVPIGTVPMY QALEKVEDDA SKLSWELFRD TVIEQCEQGV DYMTIHAGVL LRYVPLTANR VTGIVSRGGS IMAEWCLQHH QESFLYTHFE ELCEIFAKYD VAFSLGDGLR PGSLADANDA AQLSELMTLG ELTKIAWKHD VQVMIEGPGH VPFDTVRMNI EMEKAICQNA PFYTLGPLTT DTAPGYDHIT SAIGGVEIAR YGTAMLCYVT PKEHLGLPNK DDVKQGVIAY KIACHAADLA KHHPHAMDRD NAISKARFEF RWLDQFNLSY DPDTAIAFHD ETLPAEPAKM AHFCSMCGPK FCSMAISQNI RKRFGGAAQQ EQLVEEARSQ AIADGMKEMS KKFQESGSSL YQSVKA // ID D6T067_GARVA Unreviewed; 444 AA. AC D6T067; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-MAR-2014, entry version 17. DE SubName: Full=Hydroxyethylthiazole kinase, sugar kinase family; GN ORFNames=GV51_1318; OS Gardnerella vaginalis 5-1. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=682148; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5-1; RX PubMed=20540756; DOI=10.1186/1471-2164-11-375; RA Harwich M.D.Jr., Alves J.M., Buck G.A., Strauss J.F.III., RA Patterson J.L., Oki A.T., Girerd P.H., Jefferson K.K.; RT "Drawing the line between commensal and pathogenic Gardnerella RT vaginalis through genome analysis and virulence studies."; RL BMC Genomics 11:375-375(2010). CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADAN01000003; EFH72190.1; -; Genomic_DNA. DR EnsemblBacteria; EFH72190; EFH72190; GV51_1318. DR PATRIC; 37853519; VBIGarVag144721_0421. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 444 AA; 47279 MW; 4216D049DE0C1498 CRC64; MVTDPEEAHA LAQIATGVLI NVGTFHQPET SEYMRAAVEG CEKADTPWVL DPVGIGVPAL APRARFIHEI IKHHPTVIRA NASEIMALAG KESNGKGVDS HDNVNDALQA ARELAKKYGS VVAISGEKDA IYAHGCLARV TGGHKTMTKV VGTGCALGAL VAAYVGANPE RPLAATVAAH VHAAAAGTWA ARQTTAPGTF RTLWMDALST LSVNDMFSLT NIEFTVEPVD WTLYLVTDPR MGNRPEEEVA VESVEGGVTV VQLRDKYSDD AEISAKAKKL RHALIDSEHG DVPVFIDDHV DCAAQLGFNL HVGQKDTPFV EARKAMPAEW MVGLSCARPD LMEKAYRECK ENDVPLPDVI GIGAAFETHT KAHDVPPLGV DGVNEVAKVA HSMGVKTLAI GGIHENTVFP IRGLELDGVC TVSALMCAED AGKVARELKS VITE // ID D6T8M2_STAAU Unreviewed; 213 AA. AC D6T8M2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SLAG_02107; OS Staphylococcus aureus A8796. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=553577; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A8796; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Peleg A.Y., Young S., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Neiman D., Park D., Pearson M., RA Richards J., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., RA Stolte C., Sykes S.N., Walk T., White J., Yandava C., Haas B., RA Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus A8796."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADJJ01000011; EFH36275.1; -; Genomic_DNA. DR ProteinModelPortal; D6T8M2; -. DR SMR; D6T8M2; 4-209. DR PRIDE; D6T8M2; -. DR EnsemblBacteria; EFH36275; EFH36275; SLAG_02107. DR PATRIC; 37943886; VBIStaAur75169_2078. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D6UGM3_STAAU Unreviewed; 213 AA. AC D6UGM3; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0782_2664; OS Staphylococcus aureus subsp. aureus ATCC 51811. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=762962; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51811; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVP01000047; EFH24229.1; -; Genomic_DNA. DR ProteinModelPortal; D6UGM3; -. DR EnsemblBacteria; EFH24229; EFH24229; HMPREF0782_2664. DR PATRIC; 38078400; VBIStaAur163139_2417. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23384 MW; 8FEFB3993FF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI ENTVNRFKDF FNN // ID D6V797_9BRAD Unreviewed; 226 AA. AC D6V797; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN ORFNames=AfiDRAFT_2480; OS Afipia sp. 1NLS2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Afipia. OX NCBI_TaxID=666684; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1NLS2; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Prakah O., RA Elkins J.G., Brown S.D., Palumbo A.V., Hemme C., Zhou J., Watson D.B., RA Jardine P.M., Kostka J.E., Green S.J., Woyke T.J.; RT "The draft genome of Afipia sp. 1NLS2."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVZ01000003; EFI51107.1; -; Genomic_DNA. DR ProteinModelPortal; D6V797; -. DR EnsemblBacteria; EFI51107; EFI51107; AfiDRAFT_2480. DR PATRIC; 38096969; VBIAfiSp150213_2490. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 226 AA; 23976 MW; B5F90E4348250368 CRC64; MAPKSSSSAR PAPRLYLATP ALDDTAAFAA SLPPLLAEFD IAALLLRLAD ADERTLTSRI KTLVVPVQKA GTALLVEHHH NLVARAGADG AHVDGLQGME DASSLKPQRI LGVGQLHTRH DAMLAGENGA DYLLFGEPDS HGERPSPDAI FERLQWWAEL FEPPCVGYAA TLEEAALFAG SGADFIMVAD FVWSDARGPK AALAEAQAVI AERFNQAFGA TQASHT // ID D6V8Z3_9BRAD Unreviewed; 202 AA. AC D6V8Z3; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN ORFNames=AfiDRAFT_2939; OS Afipia sp. 1NLS2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Afipia. OX NCBI_TaxID=666684; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1NLS2; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Prakah O., RA Elkins J.G., Brown S.D., Palumbo A.V., Hemme C., Zhou J., Watson D.B., RA Jardine P.M., Kostka J.E., Green S.J., Woyke T.J.; RT "The draft genome of Afipia sp. 1NLS2."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVZ01000004; EFI50631.1; -; Genomic_DNA. DR ProteinModelPortal; D6V8Z3; -. DR EnsemblBacteria; EFI50631; EFI50631; AfiDRAFT_2939. DR PATRIC; 38097884; VBIAfiSp150213_2943. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 202 AA; 21816 MW; 651C403E651F5011 CRC64; MPYPDRFYPV VDTVAWVARL AKLGVGTVQL RAKDLDDIKA NALVRDALAS VRGTATKLVV NDYWRAAIDN GAQHLHLGQE DLVDADLAAI RKAGLTLGVS THDEEELANA LAADPDYVAL GPIFFTTLKS MRFKPQGIER ITRWKQMIGG LQLVAIGGIK LEHAAEIFAA GADSIAVVSD VTQNADPDAR VRAWLDTAME VA // ID D6X8P6_STRPR Unreviewed; 210 AA. AC D6X8P6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSDG_07044; OS Streptomyces pristinaespiralis ATCC 25486. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457429; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25486; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Streptomyces pristinaespiralis strain ATCC RT 25486."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000950; EFH31792.1; -; Genomic_DNA. DR ProteinModelPortal; D6X8P6; -. DR EnsemblBacteria; EFH31792; EFH31792; SSDG_07044. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22070 MW; 6BF5766223BBF7F2 CRC64; MLSDARLYLC TDARKRQGDL PEFLDAVLSS GVDIVQLRDK GMEAGEELEH LQVLADTCRR HGKLLAVNDR ADVAHAIGAD VLHLGQGDLP VPAARAILGD GVLIGRSTHS ESEAAAAAVE PGVDYFCTGP CWPTPTKPGR HAPGLALVRY TAGLAGERPW FAIGGIDAAN LDEVLDAGAR RVVVVRAITE ADDPAAAAAG LAKRVRERTA // ID D6XAA4_9ACTO Unreviewed; 216 AA. AC D6XAA4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSEG_10805; OS Streptomyces sviceus ATCC 29083. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=463191; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29083; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Streptomyces sviceus strain ATCC 29083."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000951; EFH28567.1; -; Genomic_DNA. DR ProteinModelPortal; D6XAA4; -. DR EnsemblBacteria; EFH28567; EFH28567; SSEG_10805. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22835 MW; D38555E11BDC302E CRC64; MPDTARTQLA DARVYLCTDA RGRQGDLAAF LDAVLAGGVD IVQLRDKGME AAEELEHLQV FADACARHGK LLAVNDRADV AHAIGADVLH LGQGDLPVPA ARAILGEDVL IGRSTHAEAE AAAAAVQDGV DYFCTGPCWP TPTKPGRHAP GLDLVRYTAA LRTDRPWFAI GGIDLGNLDE VLEAGARRVV VVRAITEADD PGAAAAEFAK RLRDTR // ID D6XQ89_HELPV Unreviewed; 208 AA. AC D6XQ89; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPV225_0863; OS Helicobacter pylori (strain v225d). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=637913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=v225d; RX PubMed=20400544; DOI=10.1128/JB.00063-10; RA Mane S.P., Dominguez-Bello M.G., Blaser M.J., Sobral B.W., RA Hontecillas R., Skoneczka J., Mohapatra S.K., Crasta O.R., Evans C., RA Modise T., Shallom S., Shukla M., Varon C., Megraud F., RA Maldonado-Contreras A.L., Williams K.P., Bassaganya-Riera J.; RT "Host-interactive genes in Amerindian Helicobacter pylori diverge from RT their Old World homologs and mediate inflammatory responses."; RL J. Bacteriol. 192:3078-3092(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001582; ADI34933.1; -; Genomic_DNA. DR RefSeq; YP_005763782.1; NC_017355.1. DR EnsemblBacteria; ADI34933; ADI34933; HPV225_0863. DR GeneID; 12342455; -. DR KEGG; hpv:HPV225_0863; -. DR PATRIC; 43069338; VBIHelPyl5358_0860. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; HPYL637913:GLEV-858-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22669 MW; D9A3FD0C326B0429 CRC64; MAGSQDFYHI KGGKNDRINA LLDALELALQ SKITAFQFRQ KGDLSLQDPI EIKQLALKCQ KLCQKYGAPF IVNDEVKLAL ELKADGVHVG QEDMAIEEVM TLCKKRLFIG LSVNTLEQAL KARHLDGVAY FGVGPIFPTQ SKKDKQVVGV ELLKKIKDSG VKKPLIAIGG ITTHNASKLR EYGGIAVIST ITQAKDKALA VGKLLKNA // ID D6XYC2_BACIE Unreviewed; 185 AA. AC D6XYC2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bsel_2693; OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=439292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700615 / DSM 15326 / MLS10; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Stolz J.; RT "Complete sequence of Bacillus selenitireducens MLS10."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001791; ADI00191.1; -; Genomic_DNA. DR RefSeq; YP_003700756.1; NC_014219.1. DR ProteinModelPortal; D6XYC2; -. DR EnsemblBacteria; ADI00191; ADI00191; Bsel_2693. DR GeneID; 9265275; -. DR KEGG; bse:Bsel_2693; -. DR PATRIC; 38124808; VBIBacSel78655_2842. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR BioCyc; BSEL439292:GHLG-2765-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 185 AA; 20015 MW; FBB0593AD365C5CD CRC64; MELHTLSTGT LTKASFLQMS ERIAPYADAI HVREPAWMAE DTRRIGNDWT FQASLIINDK TPGARESGGA LHLPEQATAH SRAVGRSVHS LEAALRCEEE GLSYLFAGPV YPPLSKETKA TLGIRQFELI CRSVRTPVIA IGGVEPHRIK ALKEAGASGV AVIGAVFLSE DPARAACELR RELDA // ID D6Y0H0_BACIE Unreviewed; 216 AA. AC D6Y0H0; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Bsel_1042; OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=439292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700615 / DSM 15326 / MLS10; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Stolz J.; RT "Complete sequence of Bacillus selenitireducens MLS10."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001791; ADH98561.1; -; Genomic_DNA. DR RefSeq; YP_003699127.1; NC_014219.1. DR ProteinModelPortal; D6Y0H0; -. DR EnsemblBacteria; ADH98561; ADH98561; Bsel_1042. DR GeneID; 9263594; -. DR KEGG; bse:Bsel_1042; -. DR PATRIC; 38121305; VBIBacSel78655_1117. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; BSEL439292:GHLG-1084-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22736 MW; BE5118E12E906876 CRC64; MKTINDILKV YFIAGTTDAR HMPLPDCLER AIEGGITCFQ YREKGPGALT GDEKTKMGRT LRDICQKRGI PFVVNDDVAL AVALEADGIH VGQEDMNASD VKSRIPDGCF LGVSVHSFKE AEAAKDAGAD YFGIGPVYPT GSKADAKDAI GPAGIRIYRD AGIKMPVVAI GGITPENTPG IMKAGADGVS MISAIAGQED PKAAARAFQH ATTVRT // ID D6Y9E1_THEBD Unreviewed; 221 AA. AC D6Y9E1; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tbis_1343; OS Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / OS JCM 10125 / NBRC 14880 / R51). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Thermobispora. OX NCBI_TaxID=469371; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / NBRC 14880 / RC R51; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Chertkov O., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of Thermobispora bispora DSM 43833."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001874; ADG88061.1; -; Genomic_DNA. DR RefSeq; YP_003651954.1; NC_014165.1. DR ProteinModelPortal; D6Y9E1; -. DR EnsemblBacteria; ADG88061; ADG88061; Tbis_1343. DR GeneID; 9167835; -. DR KEGG; tbi:Tbis_1343; -. DR PATRIC; 38285622; VBITheBis80272_1353. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; TBIS469371:GHSI-1366-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 24070 MW; 41258B3FBEA68EDA CRC64; MIGTDNGTRR ERLARARLYL CTDGRRDRGD LEEFLDAVLA NGVDIVQLRE KGLEAREELE LLEIFRAACD RHGALLAVND RADIAYAARP DILHLGQNDL PVAVAREILG PDILIGRSTH SPEQASAAAA EPGVDYFCCG PIWPTPTKPG RPAAGPELIR YASGLGTQRP WFGIGGIDLN NLDEVIGYGV RRVVVVRAIT EADDPGEAAA RFRDRLRAVP L // ID D6Z474_DESAT Unreviewed; 214 AA. AC D6Z474; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=DaAHT2_1656; OS Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfurivibrio. OX NCBI_TaxID=589865; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19089 / UNIQEM U267 / AHT2; RG US DOE Joint Genome Institute; RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Sorokin D.Y., RA Muyzer G., Woyke T.; RT "Complete sequence of Desulfurivibrio alkaliphilus AHT2."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001940; ADH86349.1; -; Genomic_DNA. DR RefSeq; YP_003690968.1; NC_014216.1. DR ProteinModelPortal; D6Z474; -. DR EnsemblBacteria; ADH86349; ADH86349; DaAHT2_1656. DR GeneID; 9257627; -. DR KEGG; dak:DaAHT2_1656; -. DR PATRIC; 38164496; VBIDesAlk70802_1699. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR BioCyc; DALK589865:GHTX-1695-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23516 MW; 46E8EBA691F1F8BD CRC64; MSTYQQRLQK FIEEATLYPV SCEKLAMGRS DRQWLEAVLA AGVKIVQLRD KEADGRTLLG KARMFRELTR AAGALLIVND RLDVALLSEA DGVHLGNDDL PCEEVRRYAP ELLIGVSCNR EEEAASAEAR GASYYNIGPL FPTGTKEEPR EVLGIDAIAR FSRHSPLPFT VMGGIKKHHL PDLLAAGVKR PAVVTALTQA ADISAEAKEW LSYL // ID D6ZFI0_SEGRD Unreviewed; 219 AA. AC D6ZFI0; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Srot_1234; OS Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / OS DSM 44985 / JCM 13578). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Segniliparaceae; Segniliparus. OX NCBI_TaxID=640132; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578; RX PubMed=21304703; DOI=10.4056/sigs.791633; RA Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T., RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., RA Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K., RA Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Segniliparus rotundus type strain (CDC RT 1076)."; RL Stand. Genomic Sci. 2:203-211(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001958; ADG97704.1; -; Genomic_DNA. DR RefSeq; YP_003658535.1; NC_014168.1. DR ProteinModelPortal; D6ZFI0; -. DR EnsemblBacteria; ADG97704; ADG97704; Srot_1234. DR GeneID; 9179285; -. DR KEGG; srt:Srot_1234; -. DR PATRIC; 38248703; VBISegRot51051_1247. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; SROT640132:GHEU-1260-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23199 MW; 39445DB4E761C7FB CRC64; MDSRDARLER LARARLYVCV DARRGTGDLV EFAEAALSGG LDALQLREKS GHNPLEAQDE LALLAKLQAS TIAHRALLAV NDRADIALAC GADMLHLGQR DLPVAIARQI VGPRVLIGRS THSLPQAQAA IHDPDVDYFC VGPCWSTPTK PGREAVGLEL VAQVAALGAE KPWFAIGGID LERVPQVRSA GASRAVVVRA VTEAEDPRAA AQALRAALA // ID D6ZRJ1_STRP0 Unreviewed; 209 AA. AC D6ZRJ1; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HMPREF0837_11002; OS Streptococcus pneumoniae serotype A19 (strain TCH8431). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=525381; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TCH8431; RX PubMed=20489017; DOI=10.1126/science.1183605; RA Nelson K.E., Weinstock G.M., Highlander S.K., Worley K.C., RA Creasy H.H., Wortman J.R., Rusch D.B., Mitreva M., Sodergren E., RA Chinwalla A.T., Feldgarden M., Gevers D., Haas B.J., Madupu R., RA Ward D.V., Birren B.W., Gibbs R.A., Methe B., Petrosino J.F., RA Strausberg R.L., Sutton G.G., White O.R., Wilson R.K., Durkin S., RA Giglio M.G., Gujja S., Howarth C., Kodira C.D., Kyrpides N., Mehta T., RA Muzny D.M., Pearson M., Pepin K., Pati A., Qin X., Yandava C., RA Zeng Q., Zhang L., Berlin A.M., Chen L., Hepburn T.A., Johnson J., RA McCorrison J., Miller J., Minx P., Nusbaum C., Russ C., Sykes S.M., RA Tomlinson C.M., Young S., Warren W.C., Badger J., Crabtree J., RA Markowitz V.M., Orvis J., Cree A., Ferriera S., Fulton L.L., RA Fulton R.S., Gillis M., Hemphill L.D., Joshi V., Kovar C., RA Torralba M., Wetterstrand K.A., Abouellleil A., Wollam A.M., RA Buhay C.J., Ding Y., Dugan S., FitzGerald M.G., Holder M., RA Hostetler J., Clifton S.W., Allen-Vercoe E., Earl A.M., Farmer C.N., RA Liolios K., Surette M.G., Xu Q., Pohl C., Wilczek-Boney K., Zhu D.; RT "A catalog of reference genomes from the human microbiome."; RL Science 328:994-999(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001993; ADI69230.1; -; Genomic_DNA. DR RefSeq; YP_003724444.1; NC_014251.1. DR ProteinModelPortal; D6ZRJ1; -. DR EnsemblBacteria; ADI69230; ADI69230; HMPREF0837_11002. DR GeneID; 9344258; -. DR KEGG; snc:HMPREF0837_11002; -. DR PATRIC; 38263714; VBIStrPne36006_1000. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE525381:GH2H-1034-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID D6ZRJ8_STRP0 Unreviewed; 210 AA. AC D6ZRJ8; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HMPREF0837_11009; OS Streptococcus pneumoniae serotype A19 (strain TCH8431). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=525381; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TCH8431; RX PubMed=20489017; DOI=10.1126/science.1183605; RA Nelson K.E., Weinstock G.M., Highlander S.K., Worley K.C., RA Creasy H.H., Wortman J.R., Rusch D.B., Mitreva M., Sodergren E., RA Chinwalla A.T., Feldgarden M., Gevers D., Haas B.J., Madupu R., RA Ward D.V., Birren B.W., Gibbs R.A., Methe B., Petrosino J.F., RA Strausberg R.L., Sutton G.G., White O.R., Wilson R.K., Durkin S., RA Giglio M.G., Gujja S., Howarth C., Kodira C.D., Kyrpides N., Mehta T., RA Muzny D.M., Pearson M., Pepin K., Pati A., Qin X., Yandava C., RA Zeng Q., Zhang L., Berlin A.M., Chen L., Hepburn T.A., Johnson J., RA McCorrison J., Miller J., Minx P., Nusbaum C., Russ C., Sykes S.M., RA Tomlinson C.M., Young S., Warren W.C., Badger J., Crabtree J., RA Markowitz V.M., Orvis J., Cree A., Ferriera S., Fulton L.L., RA Fulton R.S., Gillis M., Hemphill L.D., Joshi V., Kovar C., RA Torralba M., Wetterstrand K.A., Abouellleil A., Wollam A.M., RA Buhay C.J., Ding Y., Dugan S., FitzGerald M.G., Holder M., RA Hostetler J., Clifton S.W., Allen-Vercoe E., Earl A.M., Farmer C.N., RA Liolios K., Surette M.G., Xu Q., Pohl C., Wilczek-Boney K., Zhu D.; RT "A catalog of reference genomes from the human microbiome."; RL Science 328:994-999(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001993; ADI69237.1; -; Genomic_DNA. DR RefSeq; YP_003724451.1; NC_014251.1. DR ProteinModelPortal; D6ZRJ8; -. DR EnsemblBacteria; ADI69237; ADI69237; HMPREF0837_11009. DR GeneID; 9344265; -. DR KEGG; snc:HMPREF0837_11009; -. DR PATRIC; 38263728; VBIStrPne36006_1007. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE525381:GH2H-1041-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID D6ZV91_BIFLJ Unreviewed; 917 AA. AC D6ZV91; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN OrderedLocusNames=BLJ_1351; OS Bifidobacterium longum subsp. longum (strain JDM301). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=759350; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JDM301; RX PubMed=20525832; DOI=10.1128/JB.00538-10; RA Wei Y.X., Zhang Z.Y., Liu C., Zhu Y.Z., Zhu Y.Q., Zheng H., Zhao G.P., RA Wang S., Guo X.K.; RT "Complete genome sequence of Bifidobacterium longum JDM301."; RL J. Bacteriol. 192:4076-4077(2010). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002010; ADH00797.1; -; Genomic_DNA. DR RefSeq; YP_003661627.1; NC_014169.1. DR ProteinModelPortal; D6ZV91; -. DR EnsemblBacteria; ADH00797; ADH00797; BLJ_1351. DR GeneID; 9190014; -. DR KEGG; bll:BLJ_1351; -. DR PATRIC; 38140667; VBIBifLon164510_1332. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR OMA; INTICSA; -. DR BioCyc; BLON759350:GHJA-1346-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100207 MW; C63339EA7D0F6AC0 CRC64; MSNEYPYASM RDNFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVQLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICAASEFP VVVGGGVTAA DMAMLAGTKA AGWFAVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVAHTPAADT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LAKAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID D7A4N2_STAND Unreviewed; 201 AA. AC D7A4N2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Snov_2600; OS Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / OS NBRC 12443 / NCIB 9113). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Starkeya. OX NCBI_TaxID=639283; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB RC 9113; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U., RA Woyke T.; RT "Complete sequence of Starkeya novella DSM 506."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002026; ADH89895.1; -; Genomic_DNA. DR RefSeq; YP_003694514.1; NC_014217.1. DR ProteinModelPortal; D7A4N2; -. DR EnsemblBacteria; ADH89895; ADH89895; Snov_2600. DR GeneID; 9333682; -. DR KEGG; sno:Snov_2600; -. DR PATRIC; 38257791; VBIStaNov45716_2605. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; SNOV639283:GCS4-2632-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 177 178 THZ-P binding (By similarity). FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 201 AA; 22365 MW; E27762002EF5EEDC CRC64; MKLDPFYLIV DRASWLPRLL PQGVKLVQLR AKDKEEAELR REIAEARAVC ERYGAQLVVN DHWRLAIEEG CDFVHLGQED LAAADLTAIR SAGLKLGIST HDEAELEVAL LARPDYVALG PVYPTILKKM RWAPQGLERV AKWKKRVGDL PLVGIGGLTI DRAQGVLEAG ADSLAVVTDV LLNDNPERRA REWVLATREM A // ID D7A7B9_STAND Unreviewed; 217 AA. AC D7A7B9; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 16-OCT-2013, entry version 24. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Snov_3075; OS Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / OS NBRC 12443 / NCIB 9113). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Starkeya. OX NCBI_TaxID=639283; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB RC 9113; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U., RA Woyke T.; RT "Complete sequence of Starkeya novella DSM 506."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002026; ADH90350.1; -; Genomic_DNA. DR RefSeq; YP_003694969.1; NC_014217.1. DR ProteinModelPortal; D7A7B9; -. DR EnsemblBacteria; ADH90350; ADH90350; Snov_3075. DR GeneID; 9334159; -. DR KEGG; sno:Snov_3075; -. DR PATRIC; 38258705; VBIStaNov45716_3061. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR BioCyc; SNOV639283:GCS4-3109-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 217 AA; 22047 MW; 8828BCDDD9D8A382 CRC64; MARPTPEPAR PVPRLYVLVP PLEAEGEIAA HAEALRAAGT EADIAAVLVR PGKATEGRAA EALQPLVAAC HAIGAACLVD GNATLATAIG ADGAHLDGVV ALKGAIAVLR PHGIAGAGGL RTKHDAMSAA ETGADYVMFG EPDAAGRRPP FDATLERTEW WAQLFEPPCV AYARTLEEVD ALIEAGADFV AVDGLVLDAP SEGVRALAQR LAAGGAA // ID D7AFR4_GEOSK Unreviewed; 213 AA. AC D7AFR4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=tenI; Synonyms=thiE; OrderedLocusNames=KN400_0565; OS Geobacter sulfurreducens (strain DL-1 / KN400). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=663917; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DL-1 / KN400; RX PubMed=20544019; DOI=10.1371/journal.pone.0010922; RA Nagarajan H., Butler J.E., Klimes A., Qiu Y., Zengler K., Ward J., RA Young N.D., Methe B.A., Palsson B.O., Lovley D.R., Barrett C.L.; RT "De Novo assembly of the complete genome of an enhanced electricity- RT producing variant of Geobacter sulfurreducens using only short RT reads."; RL PLoS ONE 5:E10922-E10922(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002031; ADI83428.1; -; Genomic_DNA. DR RefSeq; YP_006889606.1; NC_017454.1. DR ProteinModelPortal; D7AFR4; -. DR EnsemblBacteria; ADI83428; ADI83428; KN400_0565. DR GeneID; 12438972; -. DR KEGG; gsk:KN400_0565; -. DR PATRIC; 43025146; VBIGeoSul143269_0572. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; GSUL663917:GLDN-565-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22139 MW; 0F2B52608A092621 CRC64; MAKVDFSLYL ITDRHQAGGR DLLAVVEGAL AGGVRCVQLR EKDLPARTLL ELARAMRRLT DRFGARLLIN DRVDIALAAG ADGVHLGEEG MPAAVARELL GSGRLIGVSC HGRGGAAAAV AQGADFITFG PVYPTPSKAA YGEPVGIDQL AATTKEIHIP VFALGGIKEA NIPEALAAGA AGVALISAII ADPDPRERAR ALLALLPPRT RDE // ID D7AFT2_GEOSK Unreviewed; 490 AA. AC D7AFT2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=4-amino-5-hydroxymethyl-2-methylpyrimidine-phosphate kinase and thiamin monophosphate synthase; GN Name=thiD; Synonyms=thiE; OrderedLocusNames=KN400_0583; OS Geobacter sulfurreducens (strain DL-1 / KN400). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=663917; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DL-1 / KN400; RX PubMed=20544019; DOI=10.1371/journal.pone.0010922; RA Nagarajan H., Butler J.E., Klimes A., Qiu Y., Zengler K., Ward J., RA Young N.D., Methe B.A., Palsson B.O., Lovley D.R., Barrett C.L.; RT "De Novo assembly of the complete genome of an enhanced electricity- RT producing variant of Geobacter sulfurreducens using only short RT reads."; RL PLoS ONE 5:E10922-E10922(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002031; ADI83446.1; -; Genomic_DNA. DR RefSeq; YP_006889623.1; NC_017454.1. DR ProteinModelPortal; D7AFT2; -. DR EnsemblBacteria; ADI83446; ADI83446; KN400_0583. DR GeneID; 12438986; -. DR KEGG; gsk:KN400_0583; -. DR PATRIC; 43025182; VBIGeoSul143269_0589. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR BioCyc; GSUL663917:GLDN-583-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 490 AA; 51910 MW; 924B153FCD5E83D4 CRC64; MASNGHTLRL VINRDKHDSV IRGLYLVTDH DDNLIPRVEA AIDGGARVVQ YRNKNQDRES RLALGLELRE LCRRRSIPFI VNDDLEMAVS LKADGLHLGQ GDGDPREARR VLGPGKIIGV STHTLSEALE AQAAGVDYIG LGAMFPSRSK EVEHVAGSEL LAAIRSSISI PIVAIGGITR DNGASVIDAG ADAVAVISAV LSHPDPALAA TEIALLFNRR APFPRGSVLT VAGSDSGGGA GIQADLKTVT LLGSYGSSVL TALTAQNTRG VSGIHGVPPA FVADQLDAVF SDIPVDVVKT GMLFSAETIV AIAAKLTEYR RRMVVVDPVM VAKGGANLID RGAVSVLKER LFPLAYLVTP NIPEAERLTG ANISDEESMR EAARRLHRLG ARNVLLKGGH LLAGDSVDIL FDGAAFHRFV SPRILSKNTH GTGCTFASAI ATYLAQGDPL REAIARAKRY ITAAIRLAQP LGRGHGPVNH ILAAEDVRDR // ID D7ATH4_THEM3 Unreviewed; 211 AA. AC D7ATH4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tmath_0671; OS Thermoanaerobacter mathranii (strain DSM 11426 / CIP 108742 / A3). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=583358; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11426 / CIP 108742 / A3; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Held B., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Zhou J., Hemme C., Woyke T.; RT "Complete sequence of Thermoanaerobacter mathranii subsp. mathranii RT mathranii str. A3."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002032; ADH60421.1; -; Genomic_DNA. DR RefSeq; YP_003676432.1; NC_014209.1. DR ProteinModelPortal; D7ATH4; -. DR EnsemblBacteria; ADH60421; ADH60421; Tmath_0671. DR GeneID; 9242161; -. DR KEGG; tmt:Tmath_0671; -. DR PATRIC; 38279442; VBITheMat18_0694. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; TMAT583358:GHOX-699-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22844 MW; 23C0E04D84E55E00 CRC64; MDLTLYAITD RSYIKDMDIA EAVELAIKGG ATVIQLREKD ISSREFYEIA LKVKEVTKRN RIPLIINDRV DIALAVNADG VHVGQEDLPA DVVRRMIGPH KIVGVSASTV EEALKAQKDG ADYLGVGAVF KTPTKPEAEA IGIEGLKKIK EAVSIPVVAI GGITKDNAYE VMLKSGVDGI SSVSAVFYGD IENNTRKLLE VIAKAINDRR I // ID D7B266_NOCDD Unreviewed; 226 AA. AC D7B266; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ndas_3114; OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / IMRU 509 / OS JCM 7437 / NCTC 10488) (Actinomadura dassonvillei). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptosporangineae; Nocardiopsaceae; Nocardiopsis. OX NCBI_TaxID=446468; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23218 / DSM 43111 / IMRU 509 / JCM 7437 / NCTC 10488; RX PubMed=21304737; RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Djao O.D., Rohde M., Sikorski J., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Nocardiopsis dassonvillei type strain RT (IMRU 509)."; RL Stand. Genomic Sci. 3:325-336(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002040; ADH68523.1; -; Genomic_DNA. DR RefSeq; YP_003681029.1; NC_014210.1. DR ProteinModelPortal; D7B266; -. DR EnsemblBacteria; ADH68523; ADH68523; Ndas_3114. DR GeneID; 9246970; -. DR KEGG; nda:Ndas_3114; -. DR PATRIC; 38216269; VBINocDas52663_3253. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; NDAS446468:GHUM-3144-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23970 MW; 674C55D8D601304F CRC64; MDRVRTSHGT SLRKRLDASL LYLCTDARTG RGDLAEFADA ALAGGVDIIQ LRDKGLEARE EIAALEVMKE ACERYGALLA VNDRADIARA VRADVLHLGQ RDLPVPMARD IIGADPVIGR SNNDVAAAAA SAEEPGSDYF CVGPTWATPT KPGRPAAGLE LVEEAAALGT DRPWFAIGGI DVDNIDRVLD AGARRVVVVR AITEAEDPRA AAAALRQRLA ARAARP // ID D7BI37_MEISD Unreviewed; 208 AA. AC D7BI37; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mesil_0370; OS Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus OS silvanus). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Meiothermus. OX NCBI_TaxID=526227; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700542 / DSM 9946 / VI-R2; RX DOI=10.4056/sigs.1042812; RA Sikorski J., Tindall B., Lowry S., Lucas S., Nolan M., Copeland A., RA Glavina Del Rio T., Tice H., Cheng J., Han C., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Goodwin L., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., RA Rohde M., Goker M., Woyke T., Bristow J., Eisen J., Markowitz V., RA Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.; RT "Complete genome sequence of Meiothermus silvanus type strain (VI- RT R2)."; RL Stand. Genomic Sci. 3:37-46(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002042; ADH62311.1; -; Genomic_DNA. DR RefSeq; YP_003683819.1; NC_014212.1. DR ProteinModelPortal; D7BI37; -. DR EnsemblBacteria; ADH62311; ADH62311; Mesil_0370. DR GeneID; 9249852; -. DR KEGG; msv:Mesil_0370; -. DR PATRIC; 38189430; VBIMeiSil18825_0381. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; MSIL526227:GJ9Q-377-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22808 MW; 35DD67E863FE06DA CRC64; MLGKLYLVAS PRPGQPEAAF LDRLEAALEG GVELLQLRAK GFEAQAILAL GEKLRDLCRR YRVPLVINDR PDLATLLEAD GVHLGQGDLG VAEARRFFTG WIGRSTHEPE QALREQAALE GSGGYLSVGP VWETPTKPGR PATGLEYVRW AAHNLQLPWF AIGGIDEHTL PRVLEAGARR VAVVRAILDA PDPEEAAKRL RRWLDGVD // ID D7BK04_ARCHD Unreviewed; 235 AA. AC D7BK04; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Arch_1279; OS Arcanobacterium haemolyticum (strain ATCC 9345 / DSM 20595 / NBRC OS 15585 / NCTC 8452 / 11018). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Actinomycineae; Actinomycetaceae; Arcanobacterium. OX NCBI_TaxID=644284; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9345 / DSM 20595 / NBRC 15585 / NCTC 8452 / 11018; RX DOI=10.4056/sigs.1123072; RA Yasawong M., Teshima H., Lapidus A., Nolan M., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J., Bruce D., Detter C., Tapia R., RA Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y., Jeffries C., Rohde M., Sikorski J., Pukall R., Goker M., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H.; RT "Complete genome sequence of Arcanobacterium haemolyticum type strain RT (11018)."; RL Stand. Genomic Sci. 3:126-135(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002045; ADH92984.1; -; Genomic_DNA. DR RefSeq; YP_003697603.1; NC_014218.1. DR EnsemblBacteria; ADH92984; ADH92984; Arch_1279. DR GeneID; 9261873; -. DR KEGG; ahe:Arch_1279; -. DR PATRIC; 38111531; VBIArcHae78728_1250. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; AHAE644284:GI54-1322-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 58 62 HMP-PP binding (By similarity). FT REGION 161 163 THZ-P binding (By similarity). FT REGION 211 212 THZ-P binding (By similarity). FT METAL 91 91 Magnesium (By similarity). FT METAL 115 115 Magnesium (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 164 164 HMP-PP (By similarity). FT BINDING 192 192 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 235 AA; 25226 MW; 288971ED3EDC933F CRC64; MKRATPRGGI YLVTDPGLSM ARIGVPYLPD SNDWYQQAIS ETLKTCKAAA DAGVTTIQLR WKNVDARYLY QLAQEVWDIL RNTHVQIVIN DRVDVFLALQ TKGIYVHGVH IGQTDIHPRI VRDLIGERPF IGYSAATPQE LQEANELDVI DWIGLGVVHA TATKTDAPKP LGIDGMIAAA GTARLPVTAI GGIGKRDVAA LAGNVHSAAV VSAIVSATSP YEAAHELVST WNAAA // ID D7CEV6_STRBB Unreviewed; 222 AA. AC D7CEV6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SBI_07858; OS Streptomyces bingchenggensis (strain BCW-1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=749414; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCW-1; RX PubMed=20581206; DOI=10.1128/JB.00596-10; RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L., RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X., RA Xiang W.S.; RT "Genome sequence of the milbemycin-producing bacterium Streptomyces RT bingchenggensis."; RL J. Bacteriol. 192:4526-4527(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002047; ADI10978.1; -; Genomic_DNA. DR RefSeq; YP_004966109.1; NC_016582.1. DR ProteinModelPortal; D7CEV6; -. DR EnsemblBacteria; ADI10978; ADI10978; SBI_07858. DR GeneID; 11615128; -. DR KEGG; sbh:SBI_07858; -. DR PATRIC; 43273864; VBIStrBin158249_8082. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR BioCyc; SBIN749414:GHKA-7936-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23417 MW; 095E3358E7A1EBE2 CRC64; MAAATATATA REQLADARLY LCTGARRRQD DLPEFLDAVL GAGVDIVQLR DKDMEAREEL DHLGVFADAC RRHGKLLAVN DRADVAHAIG SDVLHLGQGD LPVPAARAIL GADVLIGRST HAPAEAEAAA VEPGVDYFCT GPCWPTPTKP GRSAPGLSLV RHTAALKPAR PWFAIGGIDA SNLDEVLEAG ARRIVVVRAI TEAEDPGAAT AELAKRVRAR DL // ID D7CJE1_SYNLT Unreviewed; 497 AA. AC D7CJE1; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 28. DE SubName: Full=Phosphomethylpyrimidine kinase; GN OrderedLocusNames=Slip_0243; OS Syntrophothermus lipocalidus (strain DSM 12680 / TGB-C1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae; OC Syntrophothermus. OX NCBI_TaxID=643648; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12680 / TGB-C1; RX DOI=10.4056/sigs.1233249; RG US DOE Joint Genome Institute (JGI-PGF); RA Djao O., Zhang X., Lucas S., Lapidus A., Glavina Del Rio T., Nolan M., RA Tice H., Cheng J., Han C., Tapia R., Goodwin L., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., RA Pati A., Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y., Jeffries C., Rohde M., Sikorski J., Spring S., Goker M., RA Detter J., Woyke T., Bristow J., Eisen J., Markowitz V., RA Hugenholtz P., Kyrpides N., Klenk H.; RT "Complete genome sequence of Syntrophothermus lipocalidus type strain RT (TGB-C1T)."; RL Stand. Genomic Sci. 3:267-275(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002048; ADI01030.1; -; Genomic_DNA. DR RefSeq; YP_003701595.1; NC_014220.1. DR ProteinModelPortal; D7CJE1; -. DR EnsemblBacteria; ADI01030; ADI01030; Slip_0243. DR GeneID; 9273020; -. DR KEGG; slp:Slip_0243; -. DR PATRIC; 38266852; VBISynLip21176_0257. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR BioCyc; SLIP643648:GHUR-253-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 497 AA; 53071 MW; 7EBCE92189CBB50E CRC64; MTPDEVHKVL TIAGSDSGGG AGIQADLKTF AALGVYGTSV ITAVTAQNTL GVQGVGGIDP ALVEQQMDSV FLDIKVEAAK TGMLYDEGII RAVARKLGEH RVRNVVVDPV MVSTTGHRLL LPEAERAMRE LMMPAADFVT PNPDEASVLW GASIRKEADL HQAARAIRDM GARFVIITGV KRGERCLDLA FDGREFRELE GPYIPTPNTH GTGCTYSAAL ASFLAYGMEP WEAAQAAKDF VTTGLRYSYS PGKGSGPVNH SALYYPGTVA DRAVARLRSL VFANWRKRPE PGREPVLNLI IGSPWCSGQD YAELAEKAIR MGTRVIQLRE KEKDSREMIE VGLRVARSCR EHGAIFIVND RADVAVAVGA DGVHLGQTDI PPEVARAMMG PGKIVGVSVS TVEEARAAIA AGADYLGLGP VFATASKQDA APPCGLETVR QVASFSPVPV IAIGGITPEN AREVLNAGAA GVAVISAVWD SPDPWDQMRR FIEMMRI // ID D7D323_GEOSC Unreviewed; 201 AA. AC D7D323; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=GC56T3_2939; OS Geobacillus sp. (strain C56-T3). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=691437; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C56-T3; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Kourtz L., Brumm P., Mead D., RA Woyke T.; RT "Complete sequence of Geobacillus sp. C56-T3."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002050; ADI27880.1; -; Genomic_DNA. DR RefSeq; YP_003672457.1; NC_014206.1. DR ProteinModelPortal; D7D323; -. DR EnsemblBacteria; ADI27880; ADI27880; GC56T3_2939. DR GeneID; 9238037; -. DR KEGG; gct:GC56T3_2939; -. DR PATRIC; 38173112; VBIGeoSp154431_3191. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR BioCyc; GSP691437:GI2V-3031-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 21113 MW; 9FFC5156A8610405 CRC64; MGVLHFVSTG RQTVDEFAAI CAHTHPYADL IHIREKGKTA REVAAFVAAL LRVGVPLQKI IVNDRVDVAA VYGVKGVQLA YHSLPVRAVR RSFPDLTVGC SVHGSEEAKQ AEQDGAHFCL YGHIFPTDSK PGLPPRGLDS LAEIVAAVSI PVIAIGGIHA GNARRVLEAG AAGVAVLSAV FFAADPVAEA KRLADIVKGR G // ID D7D7K2_GEOSC Unreviewed; 221 AA. AC D7D7K2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GC56T3_2002; OS Geobacillus sp. (strain C56-T3). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=691437; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C56-T3; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Kourtz L., Brumm P., Mead D., RA Woyke T.; RT "Complete sequence of Geobacillus sp. C56-T3."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002050; ADI26987.1; -; Genomic_DNA. DR RefSeq; YP_003671564.1; NC_014206.1. DR ProteinModelPortal; D7D7K2; -. DR EnsemblBacteria; ADI26987; ADI26987; GC56T3_2002. DR GeneID; 9237098; -. DR KEGG; gct:GC56T3_2002; -. DR PATRIC; 38171081; VBIGeoSp154431_2178. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; GSP691437:GI2V-2092-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23055 MW; 40DF21614BB8F035 CRC64; MARIASGEMK ERLAVYFIMG SQNSERPAAD VLKEALDGGV TLFQFREKGP GALKGADKEE LARQLQHLCR AYGVPFIVND DVELALAIDA DGVHVGQDDE DARRVREKIG DKILGVSAHN VEEAMAAVEA GADYLGVGPI YPTSSKEDAK EAQGPDVLRR LREAGITIPI VAIGGITAAN AKTVVEAGAD GVSVISAIAS APSPKAAAAA LAEAVRAART R // ID D7DMW7_METS0 Unreviewed; 330 AA. AC D7DMW7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=M301_0522; OS Methylotenera sp. (strain 301). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylotenera. OX NCBI_TaxID=666681; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N., RA Chistoservova L., Kalyuzhnaya M., Woyke T.; RT "Complete sequence of Methylotenera sp. 301."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002056; ADI28906.1; -; Genomic_DNA. DR RefSeq; YP_003673483.1; NC_014207.1. DR ProteinModelPortal; D7DMW7; -. DR EnsemblBacteria; ADI28906; ADI28906; M301_0522. DR GeneID; 9395774; -. DR KEGG; meh:M301_0522; -. DR PATRIC; 38197357; VBIMetSp140979_0524. DR KO; K03574; -. DR OMA; CGASCHN; -. DR BioCyc; MVER666681:GHRP-542-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 330 AA; 36428 MW; 0FBADB2B7AD50793 CRC64; MNTTKRKITH AAVGVIQRED GWVLLAERPV GKPWAGYWEF PGGKVEEGET PQQALKRELQ EELGIAVASL YPWLTRSFDY EAKYDATGQL DSPAKTVKLH FFIVTKWDGE PRGLENQQLV WQPPENIEVS PMLPANAPIF AALSLPSNYA ITNLSELGED LFFERLKISL DNGLKMLQLR EKQLSNQAFQ TFAERVIQLA KPYKAKVLIN SGNQSASAAL NVAGIHFNST DLMQLQAKPV GMLCGASCHN AEQLAHAAAL GIDYVMLSPV KATRSHPDEE PLGWSQFANL ISDYALPVYA LGGMRPPDLH EAKSHGAHGI AMLRSAWLSE // ID D7DP89_METS0 Unreviewed; 211 AA. AC D7DP89; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=M301_2767; OS Methylotenera sp. (strain 301). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylotenera. OX NCBI_TaxID=666681; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N., RA Chistoservova L., Kalyuzhnaya M., Woyke T.; RT "Complete sequence of Methylotenera sp. 301."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002056; ADI31120.1; -; Genomic_DNA. DR RefSeq; YP_003675697.1; NC_014207.1. DR ProteinModelPortal; D7DP89; -. DR EnsemblBacteria; ADI31120; ADI31120; M301_2767. DR GeneID; 9397231; -. DR KEGG; meh:M301_2767; -. DR PATRIC; 38201965; VBIMetSp140979_2793. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; MVER666681:GHRP-2823-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22220 MW; 651337899874210A CRC64; MISGLYAITP DEADTDLLLA KVEAALQGGI RVLQYRNKQA SYKLQTQQAS AILPLCKQHQ VPFIINDSVE LCLALNADGV HIGADDGNIA EVKARLGANK ILGASCYNRF DLALSAQQAG ATYVAFGACF ASSTKPHAPV ASLDLFKQAN AQLHIPAVAI GGITLENVPS VIQAGANSIA VINAIFNADD VKLAAQQFAR LFKESTLKAT T // ID D7DTM7_METV3 Unreviewed; 206 AA. AC D7DTM7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mvol_0828; OS Methanococcus voltae (strain ATCC BAA-1334 / A3). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=456320; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1334 / A3; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Lowry S., Clum A., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Whitman W.B., Woyke T.; RT "Complete sequence of Methanococcus voltae A3."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002057; ADI36487.1; -; Genomic_DNA. DR RefSeq; YP_003707460.1; NC_014222.1. DR ProteinModelPortal; D7DTM7; -. DR SMR; D7DTM7; 4-206. DR EnsemblBacteria; ADI36487; ADI36487; Mvol_0828. DR GeneID; 9276050; -. DR KEGG; mvo:Mvol_0828; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR BioCyc; MVOL456320:GHV9-841-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22753 MW; BDD66BF23EB61396 CRC64; MRFDKKLKLY VITDSRFGKE VEQVKQALEG GATSIQLRLK DVSTRHFLDT AKDLRKLTRD YDALFFVNDR LDIAMASDAD GIHVGMDDMP VEYVKEMAPE LIIGSSAYNL EEANYGINAG ADYLGVGAVY STNTKLDARY LGVEGLKNIS KSVNIPIVAI GGINHQNCED VLNCDIQGLA VISAILNSNN IVNSSKEMRN IIDKYI // ID D7E2G7_NOSA0 Unreviewed; 347 AA. AC D7E2G7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Aazo_3314; OS Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus. OX NCBI_TaxID=551115; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0708; RX PubMed=20628610; DOI=10.1371/journal.pone.0011486; RA Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K., RA Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.; RT "Genome erosion in a nitrogen-fixing vertically transmitted RT endosymbiotic multicellular cyanobacterium."; RL PLoS ONE 5:E11486-E11486(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002059; ADI64989.1; -; Genomic_DNA. DR RefSeq; YP_003722112.1; NC_014248.1. DR ProteinModelPortal; D7E2G7; -. DR EnsemblBacteria; ADI64989; ADI64989; Aazo_3314. DR GeneID; 9341118; -. DR KEGG; naz:Aazo_3314; -. DR PATRIC; 38230066; VBINosAzo102301_4342. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR BioCyc; TAZO551115:GH0O-3334-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 129 Unknown (By similarity). FT REGION 130 347 Thiamine-phosphate synthase (By FT similarity). FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 347 AA; 38783 MW; 086389DFFB3A7681 CRC64; MVTAHHQGQE TQQVVYRILD ANLDRAREGL RIIEEWCRFG LNDASLAEAC KHLRQELGRW HTAQMRAARD TLGDPGTGLT HPQEEQRADI TSLLQANFCR LQEALRVLEE YGKLYNPNMG SAFKQMRYQV YTLESTLMGY QRHQLLGQSR LYLVTSPVDH FLETVEAALK GGLMLLQFRE KTSDDLTHLE RARKLQQLCH DYGALFIIND RVDLALAVGA DGVHLGQQDM PIAVARQLLG SQRLIGRSTT NPQEMQGAIA EGADYIGVGP VYETPTKVGK AAAGLEYVRY ASKNCPVPWF AIGGIDASNI NDVIDAGGQR VAVVRALMQA EQPTLVTQYF ISQLYRK // ID D7EMM6_MYCTX Unreviewed; 222 AA. AC D7EMM6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TBAG_03564; OS Mycobacterium tuberculosis 94_M4241A. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=515615; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=94_M4241A; RG The Broad Institute Genome Sequencing Platform; RA Small P., Gagneaux S., Hopewell P., Young S.K., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Nusbaum C., Galagan J., Birren B.; RT "Annotation of Mycobacterium tuberculosis strain 94_M4241A."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS985171; EFI28978.1; -; Genomic_DNA. DR ProteinModelPortal; D7EMM6; -. DR SMR; D7EMM6; 1-221. DR EnsemblBacteria; EFI28978; EFI28978; TBAG_03564. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID D7FEK3_HELP3 Unreviewed; 220 AA. AC D7FEK3; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPB8_1053; OS Helicobacter pylori (strain B8). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=693745; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B8; RX PubMed=20507619; DOI=10.1186/1471-2164-11-335; RA Farnbacher M., Jahns T., Willrodt D., Daniel R., Haas R., Goesmann A., RA Kurtz S., Rieder G.; RT "Sequencing, annotation, and comparative genome analysis of the RT gerbil-adapted Helicobacter pylori strain B8."; RL BMC Genomics 11:335-335(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN598874; CBI66610.1; -; Genomic_DNA. DR RefSeq; YP_003729074.1; NC_014256.1. DR EnsemblBacteria; CBI66610; CBI66610; HPB8_1053. DR GeneID; 9348695; -. DR KEGG; hpl:HPB8_1053; -. DR PATRIC; 38176425; VBIHelPyl164240_1019. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; HPYL693745:GJAE-1076-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24183 MW; E608529694625EEE CRC64; MFDANCLKLM FVAGSQDFYH IKGDKNDRIN ALLETLELAL QSQITAFQFR QKGDLALQDP IEIKQLALEC QKLCQKYGVP FIVNDEVQLA LELKADGVHV GQEDMAIEEV ITLCKKRLFI GLSVNTLEQA LKARHLDAVA YFGVGPIFPT PSKKDAKEVV GINLLKKIHD SGVKKPLIAI GGITMHNASK LREYGGIAVI SAITQAKDKA LAIEKLLNNA // ID D7FV85_ECTSI Unreviewed; 276 AA. AC D7FV85; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=Esi_0029_0024; OS Ectocarpus siliculosus (Brown alga). OC Eukaryota; Stramenopiles; PX clade; Phaeophyceae; Ectocarpales; OC Ectocarpaceae; Ectocarpus. OX NCBI_TaxID=2880; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ec32 / CCAP1310/4; RX PubMed=20520714; DOI=10.1038/nature09016; RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G., RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B., RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., RA Brownlee C., Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., RA Collen J., Corre E., Da Silva C., Delage L., Delaroque N., RA Dittami S.M., Doulbeau S., Elias M., Farnham G., Gachon C.M., RA Gschloessl B., Heesch S., Jabbari K., Jubin C., Kawai H., Kimura K., RA Kloareg B., Kupper F.C., Lang D., Le Bail A., Leblanc C., Lerouge P., RA Lohr M., Lopez P.J., Martens C., Maumus F., Michel G., RA Miranda-Saavedra D., Morales J., Moreau H., Motomura T., Nagasato C., RA Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F., Pommier C., RA Potin P., Poulain J., Quesneville H., Read B., Rensing S.A., RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., RA Segurens B., Strittmatter M., Tonon T., Tregear J.W., Valentin K., RA von Dassow P., Yamagishi T., Van de Peer Y., Wincker P.; RT "The Ectocarpus genome and the independent evolution of RT multicellularity in brown algae."; RL Nature 465:617-621(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN648475; CBJ26257.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 276 AA; 28029 MW; B2A6C125E8566514 CRC64; MTGSLYPGGY TTACAAGAAA ASPTRKSGAP LNGLGNEVAH DDAVPLAPPV LELITPDGCA SSSFSETSSL VINIQKAVAG GVSLVQLRDY KSGAKSKADL AVRISTAIEG RALFVVNGEP DAARASGADG VHLPERMMDR LVGLRGQGEW PRIVGCSVHS VAAAVEAARL GADYVQVGTM FATQSHPGKT PEGVGMLNDV RRQLQVEGLD VVLVLGVGGI DASNCGDVVA AGGDGVAAIR CLCSSSDAEG QARRIVQDMW NSAGSRFAGS LGDEIK // ID D7GF47_PROFC Unreviewed; 215 AA. AC D7GF47; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; OrderedLocusNames=PFREUD_16580; OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / OS CIP 103027 / CIRM-BIA1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=754252; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9614 / CIP 103027 / CIRM-BIA1; RX PubMed=20668525; DOI=10.1371/journal.pone.0011748; RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S., RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P., RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., RA Gaillardin C., Lortal S.; RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a RT hardy actinobacterium with food and probiotic applications."; RL PLoS ONE 5:E11748-E11748(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN806773; CBL57158.1; -; Genomic_DNA. DR RefSeq; YP_003688583.1; NC_014215.1. DR ProteinModelPortal; D7GF47; -. DR EnsemblBacteria; CBL57158; CBL57158; PFREUD_16580. DR GeneID; 9283473; -. DR KEGG; pfr:PFREUD_16580; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; PFRE754252:GI1A-1697-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23214 MW; 337C02A614892A07 CRC64; MTSRNRQWRL GRLGRSRLYL CTDSRGSLDD FAAFVEAAYA GGVDIIQLRD KHIDALSELR FLSVLRDAAL RHDALFAVND RADIAAVSDA DIVHVGQDDL PVAETRQVVG REVLIGRSTH SVDQAREARL ADTDYYCIGP VWATPTKQGR PGVGVDAVRA VAQQADDKPW FGIGGVNAQN LAQVTDAGAT RIVVVRALTG ADDPAAAARE LLARL // ID D7GIE6_PROFC Unreviewed; 283 AA. AC D7GIE6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; Synonyms=thiE; OrderedLocusNames=PFREUD_03370; OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / OS CIP 103027 / CIRM-BIA1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=754252; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9614 / CIP 103027 / CIRM-BIA1; RX PubMed=20668525; DOI=10.1371/journal.pone.0011748; RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S., RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P., RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., RA Gaillardin C., Lortal S.; RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a RT hardy actinobacterium with food and probiotic applications."; RL PLoS ONE 5:E11748-E11748(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN806773; CBL55868.1; -; Genomic_DNA. DR RefSeq; YP_003687313.1; NC_014215.1. DR ProteinModelPortal; D7GIE6; -. DR EnsemblBacteria; CBL55868; CBL55868; PFREUD_03370. DR GeneID; 9284329; -. DR KEGG; pfr:PFREUD_03370; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; PFRE754252:GI1A-373-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 171 173 THZ-P binding (By similarity). FT REGION 221 222 THZ-P binding (By similarity). FT METAL 104 104 Magnesium (By similarity). FT METAL 123 123 Magnesium (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 174 174 HMP-PP (By similarity). FT BINDING 201 201 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 283 AA; 29221 MW; 11266D7F85D78659 CRC64; MRPAMLRSED RPMPRSDAQP DAQFDRQPGA GRRRSVDLSV YLVTDTEQCG GVDGVVRTVR EAVPAGVTLV QLRDHHLSDD DFVALGRRLV DVLDGTGVPL LIDDRVHLVG PIGAQGAHVG QDDMPIDRAR AMLGPDAILG LSTQTPGHVA AARAMGEQLV DYLGVGALHS TGTKPEAGDL GMATVASVVE VSPWPVCAIG GVKADDAAPL AAIGCDGMSV VSAICGQPDI AAATRRLVDA WSRATGVPAT HTGHAEGNPV GQASPARQDP SASPNPSPDK AAR // ID D7GVG7_9FIRM Unreviewed; 211 AA. AC D7GVG7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CK3_22240; OS butyrate-producing bacterium SS3/4. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=245014; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS3/4; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Clostridiales sp. SS3/4."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929062; CBL41809.1; -; Genomic_DNA. DR RefSeq; YP_007824286.1; NC_021035.1. DR ProteinModelPortal; D7GVG7; -. DR EnsemblBacteria; CBL41809; CBL41809; CK3_22240. DR GeneID; 15236655; -. DR KEGG; bprs:CK3_22240; -. DR PATRIC; 42791395; VBIButBac106850_0780. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22789 MW; 2DB0EBBFD37ED68A CRC64; MNCRPEDMLL YAVTDRAWLN GETLESQVEK ALKGGATFVQ LREKELDEEK FLEEAKKIKK LCAEYHVPFV INDNVDIALK VDADGVHVGQ SDMEAGKVRE KLGPDKIIGV SCKNVEQALL AKKHGADYLG VGAMYPTGTK KDATAVTPEA LSAVCQAVDI PVVAIGGINK DRLEPLKGTG VDGVAVVSAI FAAEDIEKAT RELKEAVREI L // ID D7H1C3_BRUAO Unreviewed; 203 AA. AC D7H1C3; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 11-DEC-2013, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAYG_00513; OS Brucella abortus bv. 5 str. B3196. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520453; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B3196; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A.M., Perrett L.L., O'Callaghan D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 5 str. B3196."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774511; EFH34116.1; -; Genomic_DNA. DR ProteinModelPortal; D7H1C3; -. DR EnsemblBacteria; EFH34116; EFH34116; BAYG_00513. DR PATRIC; 37826591; VBIBruAbo58081_0230. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID D7H402_BRUAO Unreviewed; 221 AA. AC D7H402; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 11-DEC-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAYG_03019; OS Brucella abortus bv. 5 str. B3196. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520453; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B3196; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A.M., Perrett L.L., O'Callaghan D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 5 str. B3196."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774521; EFH33468.1; -; Genomic_DNA. DR ProteinModelPortal; D7H402; -. DR EnsemblBacteria; EFH33468; EFH33468; BAYG_03019. DR PATRIC; 37829766; VBIBruAbo58081_2110. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID D7HGZ3_VIBCL Unreviewed; 440 AA. AC D7HGZ3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VCRC385_00063; OS Vibrio cholerae RC385. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=345074; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RC385; RG The Broad Institute Genome Sequencing Platform; RA Colwell R., Grim C.J., Young S., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., RA Lewis B., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., Borodovsky M., Heidelberg J., Haas B., RA Nusbaum C., Birren B.; RT "The genome sequence of Vibrio cholerae RC385."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774562; EFH72838.1; -; Genomic_DNA. DR ProteinModelPortal; D7HGZ3; -. DR EnsemblBacteria; EFH72838; EFH72838; VCRC385_00063. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 49029 MW; 7EFBB6C3ACD1D53D CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGFA IQHIRLDVGS EAQFILEKSE ESLRIDSSLC SQEEGFEPCD YYLDYVSENR VLPEAMVCNA RCTVTVGLHD EYGFMLDKWQ YGNAAEQLII YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQC DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQIRYQGQHG IPTVAIGGID CSNIRDVLDC GVTAVAVVRA ITESSDPSLA VQALSSAFAD FVDVEYKLMP ASESCEPLSY LAMEVADAHR // ID D7HSR6_VIBCL Unreviewed; 440 AA. AC D7HSR6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=A53_00068; OS Vibrio cholerae MAK 757. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=412967; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MAK 757; RG The Broad Institute Genome Sequencing Platform; RA Colwell R., Grim C.J., Young S., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., RA Lewis B., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., Borodovsky M., Heidelberg J., Haas B., RA Nusbaum C., Birren B.; RT "The genome sequence of Vibrio cholerae MAK 757."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774585; EFH76256.1; -; Genomic_DNA. DR ProteinModelPortal; D7HSR6; -. DR EnsemblBacteria; EFH76256; EFH76256; A53_00068. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID D7I481_PSESS Unreviewed; 316 AA. AC D7I481; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 22-JAN-2014, entry version 24. DE SubName: Full=7, 8-dihydro-8-oxoguanine-triphosphatase/thiamin-phosphate pyrophosphorylase-like protein; DE EC=2.5.1.3; DE EC=3.-.-.-; GN ORFNames=PSA3335_4021; OS Pseudomonas savastanoi pv. savastanoi NCPPB 3335. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=693985; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCPPB 3335; RX PubMed=20370821; DOI=10.1111/j.1462-2920.2010.02207.x; RA Rodriguez-Palenzuela P., Matas I.M., Murillo J., Lopez-Solanilla E., RA Bardaji L., Perez-Martinez I., Rodriguez-Moskera M.E., Penyalver R., RA Lopez M.M., Quesada J.M., Biehl B.S., Perna N.T., Glasner J.D., RA Cabot E.L., Neeno-Eckwall E., Ramos C.; RT "Annotation and overview of the Pseudomonas savastanoi pv. savastanoi RT NCPPB 3335 draft genome reveals the virulence gene complement of a RT tumour-inducing pathogen of woody hosts."; RL Environ. Microbiol. 12:1604-1620(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCPPB 3335; RA Rodriguez-Palenzuela P.P., Matas I.M., Murillo J., Lopez-Solanilla E., RA Bardaji L., Perez-Martinez I., Rodriguez-Moskera M.E., Penyalver R., RA Lopez M.M., Quesada J.M., Biehl B.S., Perna N.T., Glasner J.D., RA Cabot E.L., Neeno-Eckwall E.C., Ramos C.; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB644159; EFH97977.1; -; Genomic_DNA. DR ProteinModelPortal; D7I481; -. DR EnsemblBacteria; EFH97977; EFH97977; PSA3335_4021. DR PATRIC; 37954567; VBIPseSav158853_4222. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Transferase. SQ SEQUENCE 316 AA; 34062 MW; ABC09200328F7230 CRC64; MKRVHVAAAV IRGADGSVLI ARRADTQHQG GLWEFPGGKV EEGETVQAAL ARELQEELGI QVTAARPLIK VGHDYADKQV LLDVWEVSAF TGEPHGAEGQ PLVWAAPREL PDYDFPAANQ PIVAAARLPG EYLITPDGLD NIELLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPENRWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWQQ AAQLIAGFNK PVFLLGGVGP SERQQAWESG AQGVAGIRAF WPDEIV // ID D7I5I7_PSESS Unreviewed; 205 AA. AC D7I5I7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSA3335_4491; OS Pseudomonas savastanoi pv. savastanoi NCPPB 3335. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=693985; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCPPB 3335; RX PubMed=20370821; DOI=10.1111/j.1462-2920.2010.02207.x; RA Rodriguez-Palenzuela P., Matas I.M., Murillo J., Lopez-Solanilla E., RA Bardaji L., Perez-Martinez I., Rodriguez-Moskera M.E., Penyalver R., RA Lopez M.M., Quesada J.M., Biehl B.S., Perna N.T., Glasner J.D., RA Cabot E.L., Neeno-Eckwall E., Ramos C.; RT "Annotation and overview of the Pseudomonas savastanoi pv. savastanoi RT NCPPB 3335 draft genome reveals the virulence gene complement of a RT tumour-inducing pathogen of woody hosts."; RL Environ. Microbiol. 12:1604-1620(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCPPB 3335; RA Rodriguez-Palenzuela P.P., Matas I.M., Murillo J., Lopez-Solanilla E., RA Bardaji L., Perez-Martinez I., Rodriguez-Moskera M.E., Penyalver R., RA Lopez M.M., Quesada J.M., Biehl B.S., Perna N.T., Glasner J.D., RA Cabot E.L., Neeno-Eckwall E.C., Ramos C.; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB644164; EFH97604.1; -; Genomic_DNA. DR ProteinModelPortal; D7I5I7; -. DR EnsemblBacteria; EFH97604; EFH97604; PSA3335_4491. DR PATRIC; 37955571; VBIPseSav158853_4719. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21968 MW; 8D8113EA1D6B9C94 CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKT SDESRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGSL ELAEQAKADG ATYVAFGRFF NSLTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN AQEVTRRAKA FMALL // ID D7ICS3_9BACE Unreviewed; 202 AA. AC D7ICS3; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Hydroxymethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase; GN ORFNames=HMPREF9007_02086; OS Bacteroides sp. 1_1_14. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469585; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_14; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Strauss J., Daigneault M., RA McDonald J., Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 1_1_14."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774705; EFI04427.1; -; Genomic_DNA. DR ProteinModelPortal; D7ICS3; -. DR EnsemblBacteria; EFI04427; EFI04427; HMPREF9007_02086. DR PATRIC; 37809121; VBIBacSp31_2348. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Kinase; Transferase. SQ SEQUENCE 202 AA; 23421 MW; 5449323C0AB043AC CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHRRIVTH EHFYLKEEFN LMGIHLNARN PSEPHDYAGH VSCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQKA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNKFD ACLDQNYLAV IEHFKKLKKL AD // ID D7ICS8_9BACE Unreviewed; 209 AA. AC D7ICS8; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9007_02091; OS Bacteroides sp. 1_1_14. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469585; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_14; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Strauss J., Daigneault M., RA McDonald J., Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 1_1_14."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774705; EFI04432.1; -; Genomic_DNA. DR ProteinModelPortal; D7ICS8; -. DR EnsemblBacteria; EFI04432; EFI04432; HMPREF9007_02091. DR PATRIC; 37809131; VBIBacSp31_2353. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22914 MW; 3A0A0BC8ACE7CA8E CRC64; MVSLQFITHQ TDRYTYFESA LMALEGGCKW IQLRMKEAPC EEVEAVALQL KPLCKEKEAI LLLDDHVELA KKLEVDGVHL GKKDMPIDQA RQLLGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYAAILSQ MKEANIELPV VAIGGITCED IPAILETGVN GIALSGTILR AEDPAAETRK ILNMKCIIK // ID D7IQW9_9BACE Unreviewed; 242 AA. AC D7IQW9; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0104_01827; OS Bacteroides sp. 3_1_19. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469592; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_19; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Strauss J., Daigneault M., RA McDonald J., Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 3_1_19."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774760; EFI09807.1; -; Genomic_DNA. DR ProteinModelPortal; D7IQW9; -. DR EnsemblBacteria; EFI09807; EFI09807; HMPREF0104_01827. DR PATRIC; 37875953; VBIBacSp40580_1834. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 163 165 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 HMP-PP (By similarity). FT BINDING 199 199 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 242 AA; 26723 MW; 946F179602470887 CRC64; MALNYYFGYD ENGRVGRRTT GLRPPFGGSN RLMFITHRTP KYTECDEVRM AIQGGCSWIQ LRMKDGIYED TVRKCATICA EECERIVDFC VNDDLEAAVT CGATACHLGK NDIPLDIAWE VLKDKLDSNA IFYIGATANT FEDIRLAVER GASYIGLGPY RFTGTKKNLS PILGLEGYRK IIAQCKEAGI DIPIFAIGGI TLEDVGPLME TGITGIAVSG AIINAPDPVE ETRRFIEEIN KY // ID D7IQX0_9BACE Unreviewed; 198 AA. AC D7IQX0; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Hydroxymethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase; GN ORFNames=HMPREF0104_01828; OS Bacteroides sp. 3_1_19. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469592; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_19; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Strauss J., Daigneault M., RA McDonald J., Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 3_1_19."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774760; EFI09808.1; -; Genomic_DNA. DR EnsemblBacteria; EFI09808; EFI09808; HMPREF0104_01828. DR PATRIC; 37875955; VBIBacSp40580_1835. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Kinase; Transferase. SQ SEQUENCE 198 AA; 22176 MW; 38CA86F59D7DE4D9 CRC64; MNKLVVITTP YFFADEASLI ELLFAEGMSR LHLRKPDCKR DELEGLLDNI SPAYYDRIVL HDWFTLAEER ALGGVHLNKR NPEAPPLYKG SISRSCHSLE EIIEYKPVCD YVFLSPIFQS ISKEGYGSGF PLDGLRNAKG IIDDKVIALG GICLQTITKL RDIPFGGVAV LGALWGNDPS LLVADQLIKQ FKRLQVWP // ID D7J277_9BACE Unreviewed; 202 AA. AC D7J277; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Hydroxymethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase; GN ORFNames=HMPREF0106_01530; OS Bacteroides sp. D22. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=585544; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D22; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Strauss J., Sibley C., RA White A., Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain D22."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774801; EFI14231.1; -; Genomic_DNA. DR ProteinModelPortal; D7J277; -. DR EnsemblBacteria; EFI14231; EFI14231; HMPREF0106_01530. DR PATRIC; 37884141; VBIBacSp99518_1533. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Kinase; Transferase. SQ SEQUENCE 202 AA; 23627 MW; 6FBE04FC6BF5D5DD CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNRFD ACQDQNYLAV IEHFKKLKKL SD // ID D7J282_9BACE Unreviewed; 206 AA. AC D7J282; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0106_01535; OS Bacteroides sp. D22. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=585544; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D22; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Strauss J., Sibley C., RA White A., Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain D22."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774801; EFI14236.1; -; Genomic_DNA. DR ProteinModelPortal; D7J282; -. DR EnsemblBacteria; EFI14236; EFI14236; HMPREF0106_01535. DR PATRIC; 37884151; VBIBacSp99518_1538. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22655 MW; C71D2CE7B5A79C06 CRC64; MISLQFITHQ TERYSYLESA RMALEGGCKW IQLRMKDALL EEVEAVALQL KPLCKEHEAI LILDDHVELA KKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYSSILSQ MKEANIEIPV VAIGGITFED IPAILHTGVN GIALSGTILG ADNPVEETRR IIESDL // ID D7JDJ4_9BACT Unreviewed; 225 AA. AC D7JDJ4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0156_00683; OS Bacteroidetes oral taxon 274 str. F0058. OC Bacteria; Bacteroidetes. OX NCBI_TaxID=575590; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0058; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Izard J., Baranova O.V., RA Blanton J.M., Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroidetes oral taxon 274 strain F0058."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774889; EFI17093.1; -; Genomic_DNA. DR ProteinModelPortal; D7JDJ4; -. DR EnsemblBacteria; EFI17093; EFI17093; HMPREF0156_00683. DR PATRIC; 37892734; VBIBacOra127278_0150. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 24374 MW; E647D335B5EEB31F CRC64; MLFLNAKNDY NTYDFDSIRL MYITHPHPTL SICRQVELAC RAGIKLVQLR AKDSGEAELL EYARAAVDIC HRHDALLIVN DSVDVCLQAG ADGVHLGKED EAVDRARQRL GNDKIIGATC NTFADVQHAY RMGADYVGIG PFRHTTTKQR LSPILGIDGL AAIARQMKAH GMYLPTYAIG GITAVDAGSI AECGIHGVAI SSAILCSNDF EGCTKKILNA LSDNQ // ID D7JW98_ECOLX Unreviewed; 211 AA. AC D7JW98; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECFG_05036; OS Escherichia coli FVEC1302. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656379; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FVEC1302; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli FVEC1302."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774919; EFI17758.1; -; Genomic_DNA. DR ProteinModelPortal; D7JW98; -. DR EnsemblBacteria; EFI17758; EFI17758; ECFG_05036. DR PATRIC; 37843283; VBIEscCol146434_5236. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 4A5B4907CA38B2E8 CRC64; MYQPDFPPVP FHLGLYPVVD SAQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAITLGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVMATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D7K183_9BACE Unreviewed; 205 AA. AC D7K183; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9010_01569; OS Bacteroides sp. 3_1_23. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457390; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_23; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Strauss J., Daigneault M., RA McDonald J., Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 3_1_23."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774949; EFI40482.1; -; Genomic_DNA. DR ProteinModelPortal; D7K183; -. DR EnsemblBacteria; EFI40482; EFI40482; HMPREF9010_01569. DR PATRIC; 37818404; VBIBacSp56772_0750. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22561 MW; 5396C877E01764E2 CRC64; MVSLQFITHQ TERYSYLESA RMALEGGCKW IQLRMKEAPL EEVEAVALQL KPLCKEHEAI LVLDDHVELA RKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYSSILSQ MKEANIEIPV VAIGGITYED IPAILHTGVN GIALSGTILG ADNPIEETRR ILNHA // ID D7K188_9BACE Unreviewed; 202 AA. AC D7K188; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Putative hydroxymethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase; GN ORFNames=HMPREF9010_01574; OS Bacteroides sp. 3_1_23. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457390; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_23; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Strauss J., Daigneault M., RA McDonald J., Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 3_1_23."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774949; EFI40487.1; -; Genomic_DNA. DR ProteinModelPortal; D7K188; -. DR SMR; D7K188; 1-202. DR EnsemblBacteria; EFI40487; EFI40487; HMPREF9010_01574. DR PATRIC; 37818414; VBIBacSp56772_0755. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Kinase; Transferase. SQ SEQUENCE 202 AA; 23599 MW; 772F8DFC6BF5D5DD CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNKFD ACQDQNYLAV IEHFKKLKKL SD // ID D7KCC1_ARALL Unreviewed; 923 AA. AC D7KCC1; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 16-APR-2014, entry version 26. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=ARALYDRAFT_470295; OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=81972; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. MN47; RX PubMed=21478890; DOI=10.1038/ng.807; RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M., RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G., RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., RA Schneeberger K., Spannagl M., Wang X., Yang L., Nasrallah M.E., RA Bergelson J., Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., RA Van de Peer Y., Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.; RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome RT size change."; RL Nat. Genet. 43:476-481(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL348713; EFH65699.1; -; Genomic_DNA. DR RefSeq; XP_002889440.1; XM_002889394.1. DR ProteinModelPortal; D7KCC1; -. DR EnsemblPlants; fgenesh2_kg.1__249__AT1G03160.1; fgenesh2_kg.1__249__AT1G03160.1; fgenesh2_kg.1__249__AT1G03160.1. DR GeneID; 9328213; -. DR KEGG; aly:ARALYDRAFT_470295; -. DR GO; GO:0031969; C:chloroplast membrane; IEA:EnsemblPlants/Gramene. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR GO; GO:0010027; P:thylakoid membrane organization; IEA:EnsemblPlants/Gramene. DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants/Gramene. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 923 AA; 101743 MW; 1F1FB046996C14D8 CRC64; MRTLISHRQC VTSPFLISAA SPPFPGRCFQ LSSFTAPRHR RLPSLSIRNV SHESADQTSS SRPRTLYPGG YKRPELAVPG VLLRLDADEV MSGNREETVD LVDRALAKSV QIVVIDGGAT AGKLYEAACL LKSLVKGRAY LLIAERVDIA SAVGASGVAL SDEGLPAIVA RNTLMGSNPD SVVLPLVARI VKDVDSALSA SSSEGADFLI LGSGEDKQVG LLSDSLLKSV KIPIFVTCSS KREELQLLKS GASGFVISLK DLRSSRDVAL RQCLDGAYVV NHETQNKNES ILNDKTLVET SDLPEKNNSA GFIKLEDKQK LIIEMEKSVL GETIEIIQKA APLMEEVSLL IDAVSRIDEP FLMVIVGEFN SGKSTVINAL LGKRYLKEGV VPTTNEITFL CYSDLESEEQ QRCQTHPDGQ YVCYLPAPIL KDINIVDTPG TNVILQRQQR LTEEFVPRAD LLVFVLSADR PLTESEVAFL RYTQQWKKKF VFILNKSDIY RDARELEEAI SFVKENTRKL LNTENVILYP VSARSALEAK LSTASLVGRD DLEVSDPGSN WRVQSFNELE KFLYSFLDSS TATGMERIRL KLETPMAIAE RLLASVESLV RQDCLAARED LASADKIINR TKEYALKMEY ESISWRRQAL SLIDNARLQV VDLIGTTLRL SSLDLAVSYL FKGENSASIA ATSKVQGEIL APALTNAKEL LGKYAEWLQS NTAREGSLSL KSFENKWPTY VNSKTQLGID TYDLLRKTDK FSLKTIQNLS AGTTSKRLEQ DIREVFVVTV GGLGAAGLSA SLLTSVLPTT LEDLLALGLC SAGGYVAIAN FPYRRQAIIG KVNKVADALA QQLEDSMRKD LSDATDNLVN FVNIVAKPYR EEAQLRLDHL LGIQKELSDI RSKLQLLQVD IDNLHVSRDE MRL // ID D7KML2_ARALL Unreviewed; 522 AA. AC D7KML2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 16-APR-2014, entry version 27. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=ARALYDRAFT_472545; OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=81972; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. MN47; RX PubMed=21478890; DOI=10.1038/ng.807; RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M., RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G., RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., RA Schneeberger K., Spannagl M., Wang X., Yang L., Nasrallah M.E., RA Bergelson J., Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., RA Van de Peer Y., Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.; RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome RT size change."; RL Nat. Genet. 43:476-481(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL348713; EFH66805.1; -; Genomic_DNA. DR RefSeq; XP_002890546.1; XM_002890500.1. DR ProteinModelPortal; D7KML2; -. DR EnsemblPlants; fgenesh2_kg.1__2499__AT1G22940.1; fgenesh2_kg.1__2499__AT1G22940.1; fgenesh2_kg.1__2499__AT1G22940.1. DR GeneID; 9326608; -. DR KEGG; aly:ARALYDRAFT_472545; -. DR KO; K14153; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 522 AA; 55886 MW; 76494FDE0A419D01 CRC64; MNSLGGIRSW PANWRSTTAL MTTTENVRKV PQVLTVAGSD SGAGAGIQAD LKVCAARGVY CASVITAVTA QNTRGVQSVH LLPPEFVSEQ LKSVLSDFEF DVVKTGMLPS TEIVEVLLQN LSDFPVRALV VDPVMVSTSG HVLAGSSILS IFRERLLPIA DIITPNVKEA SALLGGFRIE TVADMRSAAK LLHEMGPRFV LVKGGDLPDS SNSVDVYFDG KEFHELRSPR VATRNTHGTG CTLASCIAAE LAKGSSMLSA VKVAKRFVDN ALDYSKDIAI GSGMQGPFDH FFGLKKDPQS SRCSIFNPDD LFLYAVSDSR MNRKWNRSIV DAVKAAIEGG ATIIQLREKE AETREFLEEA KACVDICRSH GVILLINDRI DIALACNADG VHVGQSDLPV DLVRSLLGPD KIIGVSCKTP EQAHQAWKDG ADYIGSGGVF PTNTKANNRT IGLDGLKEVC DASKLPVVAI GGIGISNAES VMQIDAPNLK GVAVVSALFD QDCVLTQAKK LHKTLKESKR EI // ID D7N229_9NEIS Unreviewed; 204 AA. AC D7N229; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9016_02037; OS Neisseria sp. oral taxon 014 str. F0314. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=641149; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0314; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., RA White J., Yandava C., Izard J., Baranova O.V., Blanton J.M., RA Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Neisseria sp. oral taxon 014 strain F0314."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL349412; EFI23641.1; -; Genomic_DNA. DR ProteinModelPortal; D7N229; -. DR EnsemblBacteria; EFI23641; EFI23641; HMPREF9016_02037. DR PATRIC; 37920398; VBINeiSp28275_1459. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21678 MW; AE42177248F6CEF4 CRC64; MRFPPLKSPL KFYAVVPTAE WVERMVRAGA DTVQLRCKTL HGNELKREIE RCVAACRGSR SQLFINDHWR EAVAAGAYGV HLGQEDMDTA DFAAIAAAGL RLGLSTHSLE EMDRALALHP SYVASGAVFP TATKDMPTAP QGLEQLRGQV VRAGGTPVVA IGGITLDNAA DVLATGVASL AVVSAVTKAE NPEAAVKSFQ ALWK // ID D7TGZ0_VITVI Unreviewed; 497 AA. AC D7TGZ0; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 16-APR-2014, entry version 25. DE SubName: Full=Putative uncharacterized protein; GN OrderedLocusNames=VIT_12s0035g00320; OS Vitis vinifera (Grape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; Vitales; Vitaceae; Vitis. OX NCBI_TaxID=29760; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Pinot noir / PN40024; RX PubMed=17721507; DOI=10.1038/nature06148; RG The French-Italian Public Consortium for Grapevine Genome Characterization.; RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., RA Casagrande A., Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., RA Legeai F., Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., RA Poulain J., Bruyere C., Billault A., Segurens B., Gouyvenoux M., RA Ugarte E., Cattonaro F., Anthouard V., Vico V., Del Fabbro C., RA Alaux M., Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., RA Moroldo M., Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., RA Durand E., Pesole G., Laucou V., Chatelet P., Merdinoglu D., RA Delledonne M., Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., RA Pe M.E., Valle G., Morgante M., Caboche M., Adam-Blondon A.-F., RA Weissenbach J., Quetier F., Wincker P.; RT "The grapevine genome sequence suggests ancestral hexaploidization in RT major angiosperm phyla."; RL Nature 449:463-467(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN595990; CBI29762.3; -; Genomic_DNA. DR ProteinModelPortal; D7TGZ0; -. DR EnsemblPlants; VIT_12s0035g00320.t01; VIT_12s0035g00320.t01; VIT_12s0035g00320. DR HOGENOM; HOG000155781; -. DR OMA; PIVWTIA; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 497 AA; 52388 MW; 4F7E1719FBF48CEE CRC64; MKIPHVLTVA GSDSGAGAGI QADLKACAAR GVYCSTVITA VTAQNTVGVQ GVNIVPEDFV AEQLKSVLSD MHVDVVKTGM LPTIGIVKVL HHSLKEFPVQ ALVVDPVMVS TSGDVLAGPS ILAAFREELL PMADIVTPNL KEASALLGGL QLETVSDMCT AAKLIHDMGP RNVLVKGGDL PSSLDAVDIF FDGDDFYELR SSRIKTRNTH GTGCTLASCI AAELAKGSQI LSAVKAAKHY IETALDYSKD IAIGNGFQGP FDHLLKLKSN IRNSFRKQAF NPANLFLYAV TDSGMNKKWG RSITEAVKAA IEGGATIVQL REKDAETRDF LEAAKACVEI CHSHGVPLLI NDRIDVALAC DADGVHVGQS DIPARVVRTL LGPEKIIGVS CKTPEQAEKA WIDGADYIGC GGVYPTNTKA NNITVGLDGL KTVCLASKLP VVAIGGINAS NARTVMEIGV PNLKGVAVVS ALFDRECVLT ETQKLHGDLT QAAAMVK // ID D7TPB4_VITVI Unreviewed; 926 AA. AC D7TPB4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-MAY-2014, entry version 30. DE SubName: Full=Putative uncharacterized protein; GN OrderedLocusNames=VIT_07s0104g00480; OS Vitis vinifera (Grape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; Vitales; Vitaceae; Vitis. OX NCBI_TaxID=29760; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Pinot noir / PN40024; RX PubMed=17721507; DOI=10.1038/nature06148; RG The French-Italian Public Consortium for Grapevine Genome Characterization.; RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., RA Casagrande A., Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., RA Legeai F., Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., RA Poulain J., Bruyere C., Billault A., Segurens B., Gouyvenoux M., RA Ugarte E., Cattonaro F., Anthouard V., Vico V., Del Fabbro C., RA Alaux M., Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., RA Moroldo M., Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., RA Durand E., Pesole G., Laucou V., Chatelet P., Merdinoglu D., RA Delledonne M., Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., RA Pe M.E., Valle G., Morgante M., Caboche M., Adam-Blondon A.-F., RA Weissenbach J., Quetier F., Wincker P.; RT "The grapevine genome sequence suggests ancestral hexaploidization in RT major angiosperm phyla."; RL Nature 449:463-467(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN596005; CBI32337.3; -; Genomic_DNA. DR RefSeq; XP_002275196.1; XM_002275160.2. DR UniGene; Vvi.1661; -. DR PRIDE; D7TPB4; -. DR EnsemblPlants; VIT_07s0104g00480.t01; VIT_07s0104g00480.t01; VIT_07s0104g00480. DR GeneID; 100256371; -. DR KEGG; vvi:100256371; -. DR HOGENOM; HOG000241410; -. DR OMA; YVCYLPA; -. DR GO; GO:0031969; C:chloroplast membrane; IEA:EnsemblPlants/Gramene. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR GO; GO:0010027; P:thylakoid membrane organization; IEA:EnsemblPlants/Gramene. DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants/Gramene. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. PE 4: Predicted; KW Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome. SQ SEQUENCE 926 AA; 103295 MW; 737A08405BEF95A8 CRC64; MVSLLSQPPS IHPLFFIPTH HRYHHHSHRN HTHNHRYPLP LFSRRRSRLS IVSIANNSIP PTSQNKQPRT VYPGGYKRPE IRVPSLVLQL SVDEVLDRAG VLDVVDEAVS KWVGVVVLDG GDGSGGRLYE AACLLKSVVR ERAYLMVAER VDIAAAVNAN GVVLSDKGLP AIVARNTMMD SRSESVILPL VARNVQTANA AFTASNSEGA DFLLYGAVEE KQSEVLATSV FENVKIPIFA VVPSRAKDTS LFEASELLKA GASGLVFSLE DLRLFSDDVL RKLFETVHAM NKRTEDELQN LNKLKSLDVN SGVPGKRRVA GFIKLEDREK EVIETERLVL LEAINIIQKA APLMEEVSLL IDAVSQLDEP FLLAIVGEFN SGKSTVINAL LGRRYLKEGV VPTTNEITFL RYSELDSDGK QRCERHPDGQ YICYLPAPIL KEMNIVDTPG TNVILQRQQR LTEEFVPRAD LLLFVISADR PLTESEVAFL RYTQQWRKKI VFVLNKADLY QNASELEEAV SFIKKNVQKL LNVKHVILYP VSARLALEAK LSASGIGKDY EPSVADSSHW KATSFSEFEN FLYSFLDGST STGMERMRLK LETPIGIAER LFSSCETLVR QDYQYAKQDL ASINEMVSSV KEYAVKMESE NISWRRQTLS LIDTTKARIV KLIDSTLQLS NLDLVGSYVL KGAKSATLPA TSSVQNDIIG PAHADARKLL GEYVTWLQSN NAHEGRLYKE SFERKWPLFV YPHNQVGLET YELLRKGDEL SLKALENFSA GAASRLFDQE IREVFLGVFG GLGAAGFSAS LLTSVLPTTL EDLLALGLCS AGGWLAISNF PARRKGMIEK VTRAADAFAR ELEVAMQKDL LETVENLENF VKLIAKPYQD EAQNRLDKLL EIQDELSNVE KKLQTLQIQI QNLHVS // ID D7UI61_LISMN Unreviewed; 214 AA. AC D7UI61; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMHG_11199; OS Listeria monocytogenes FSL N1-017. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393123; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL N1-017; RG The Broad Institute Genome Sequencing Platform; RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Borowsky M., RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., RA Mauceli E., Brockman W., MacCallum I.A., Rounsley S., Young S., RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., RA White J., Yandava C., Kodira C., Zeng Q., Alvarado L., O'Leary S., RA Wiedmann M., Lauer P.; RT "The Genome Sequence of Listeria monocytogenes FSL N1-017."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AARP04000007; EFK41715.1; -; Genomic_DNA. DR ProteinModelPortal; D7UI61; -. DR EnsemblBacteria; EFK41715; EFK41715; LMHG_11199. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22536 MW; 1648C735A6347B57 CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAA EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILKEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GYPS // ID D7UU76_LISGR Unreviewed; 221 AA. AC D7UU76; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0556_10051; OS Listeria grayi DSM 20601. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=525367; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20601; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCR02000001; EFI85324.1; -; Genomic_DNA. DR ProteinModelPortal; D7UU76; -. DR EnsemblBacteria; EFI85324; EFI85324; HMPREF0556_10051. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23699 MW; 4D14E04F9E69C2FE CRC64; MRVTASDLRL YWIAGTQDLA TGQSLPDMLE EGIRAGITAF QFREKGAGSL ESNEAIIELG KTLREICRLH AIPFIVNDDV DLAIQLEADG IHLGQSDYAV EKALHEHSDR FSIGLSCHSL AEVEKANQLR QLAYLGIGPV FQTISKADAE AELGLNGLQQ LVAASDYPVV AIGGIYPENA RAILAQGVAG LSFISALVRS TDKKQTLHQL AGTTDDSGKI S // ID D7V7S2_LACPN Unreviewed; 217 AA. AC D7V7S2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0531_10199; OS Lactobacillus plantarum subsp. plantarum ATCC 14917. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525338; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14917; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGZ02000005; EFK30494.1; -; Genomic_DNA. DR ProteinModelPortal; D7V7S2; -. DR EnsemblBacteria; EFK30494; EFK30494; HMPREF0531_10199. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22751 MW; 485246DDAE17215A CRC64; MTLKFEPTQL RAYFVCGTQD VPGQDLNVVV QTALDAGITA FQYRDKGNSQ LTTAERFALG QQLRERCAQA HVPFIVDDDV ELALALQADG IHVGQKDDRV TQVIQRVANQ MFVGLSCSTL AEVQIANQLE GIAYLGSGPI FPTTSKADAD PVVGLTGLRQ LVVTATCPVV AIGGITVAQL PAIAATGAAG AAVISMLTRS PDMAATVKAM LTATEGH // ID D7VQB9_9SPHI Unreviewed; 209 AA. AC D7VQB9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0766_13173; OS Sphingobacterium spiritivorum ATCC 33861. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=525373; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33861; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHA02000012; EFK55970.1; -; Genomic_DNA. DR ProteinModelPortal; D7VQB9; -. DR EnsemblBacteria; EFK55970; EFK55970; HMPREF0766_13173. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23494 MW; 61557835DD3693F1 CRC64; MYSRLQYIST GNTVNEQLNN IRKVLENKGD WIQLRWKNAP KTALIDLAFQ VGELKEKFDF TYIINDHVSV AYKVNSDGVH LGLTDLSIQQ ARNFLGAGKI IGGTANTVEH VRQRIAENCD YIGLGPLRFT SSKQNLSPVL GYEGYQNIIQ EIQKEDQHHP PIYAIGGVKQ EDILQLQHIG IYGVAVSSLL TQSVSTQSII QHINHEFYG // ID D7VQC0_9SPHI Unreviewed; 198 AA. AC D7VQC0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0766_13174; OS Sphingobacterium spiritivorum ATCC 33861. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=525373; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33861; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHA02000012; EFK55971.1; -; Genomic_DNA. DR ProteinModelPortal; D7VQC0; -. DR EnsemblBacteria; EFK55971; EFK55971; HMPREF0766_13174. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 198 AA; 22484 MW; 02C5C1BD03612EB0 CRC64; MIIISPDTIT PQHIKLIHAI PWSDALLYHL RLPSAAKDDI TPILEDIDKH LYPFIVLHYH KETALKAGIR RFHLSGDRIK DIEQSQTDLI LSASTHQINE FNSLDTRISY AFISPVYPSI SKVGYQATAD FKSHNIQHRT NFNCRMIALG GITEYNISEL KAMGYDDIAL CGYIWKHPDP LFAADKCLSI SQTTSYVQ // ID D7VQF4_9SPHI Unreviewed; 212 AA. AC D7VQF4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0766_13208; OS Sphingobacterium spiritivorum ATCC 33861. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=525373; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33861; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHA02000012; EFK56005.1; -; Genomic_DNA. DR ProteinModelPortal; D7VQF4; -. DR EnsemblBacteria; EFK56005; EFK56005; HMPREF0766_13208. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). SQ SEQUENCE 212 AA; 23164 MW; BF7BAEAA29097F23 CRC64; MQIHPGFPYP LYLVISEADC QGKDILYVAE QAILGGVDII QLREKHASTS EFIEKALRLK EITEKHQIPL IINDNLKVAI EVNAFGIHVG NSDTPPTVIR DKWPDCSCLG YSIEYLEQLD NPETATADYL GISPVFVTDT KTDTVTEWGL AGIQQIRMHS DKPLIAIGHM NLQNIASVLQ AGADAIAVVS AICAAADPQQ AAYELKNKIL IA // ID D7VX12_9FLAO Unreviewed; 204 AA. AC D7VX12; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0204_11060; OS Chryseobacterium gleum ATCC 35910. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=525257; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35910; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKQ02000003; EFK37214.1; -; Genomic_DNA. DR ProteinModelPortal; D7VX12; -. DR EnsemblBacteria; EFK37214; EFK37214; HMPREF0204_11060. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). SQ SEQUENCE 204 AA; 22838 MW; AFFCDC02560E3CB3 CRC64; MEKLQYISQG NTIQEQELHI RKALDNGIQW VQVRWKNAPE NELINLCEIS KQLCSEYQSV CIINDHVHLA KEIDADGVHV GLNDIAVEEA RLILGENKII GGTANTLSDV IQRINESCNY IGLGPLRFTT TKEKLSPVLG YEGYQKIIDG LREQSIDIPK IFAIGSVAFE DILPLQEIGI YGVAVSDLIT KQPEIINELK KVMI // ID D7VX14_9FLAO Unreviewed; 195 AA. AC D7VX14; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 11-DEC-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0204_11062; OS Chryseobacterium gleum ATCC 35910. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=525257; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35910; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKQ02000003; EFK37216.1; -; Genomic_DNA. DR ProteinModelPortal; D7VX14; -. DR EnsemblBacteria; EFK37216; EFK37216; HMPREF0204_11062. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 195 AA; 22618 MW; 59D1325CF54C1560 CRC64; MILVITPELI VPNETDSINQ MFQEGLNLLH IRKPWISRNE MIEFITKIDD AFHSQLVLHT HYDLGKEYHI SRFHFREIDR EQGKYKPFVP ENIISTSVHH ITTYNTLDKE WEYAFISPFF PSISKKGYGT DSTIKEEIQY RNNPDVKLIA LGGINHDNIH EVFESGADGA ALLGAVWESE EPLKVFKKCR NVLMS // ID D7WFB1_9CORY Unreviewed; 219 AA. AC D7WFB1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0291_12203; OS Corynebacterium genitalium ATCC 33030. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=585529; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33030; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLJ02000003; EFK54545.1; -; Genomic_DNA. DR ProteinModelPortal; D7WFB1; -. DR EnsemblBacteria; EFK54545; EFK54545; HMPREF0291_12203. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). SQ SEQUENCE 219 AA; 22828 MW; EEE535DA1D10C35C CRC64; MTELDLRCYF ITGQGPDIVG TARAAAAGGA GMIQVRSKPI SARSLFELGQ AVAEAVYEVN PATHVLIDDR ADVALALRQA RVPNVAGVHI GQDDLDPRIA RELLGPDAII GLTTGTLELV QDANQYADVI DYIGAGPFRA TPTKDSGREP LGLEGYPPLV AASSLPVVAI GDVTVDDAAD LAAAGVDGVA IVRGIMNAED PQAYVERVIA AFDRGKQSR // ID D7WK65_BACCE Unreviewed; 219 AA. AC D7WK65; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-MAR-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BCSJ1_20293; OS Bacillus cereus SJ1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=699184; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SJ1; RX PubMed=20723231; DOI=10.1186/1471-2180-10-221; RA He M., Li X., Guo L., Miller S.J., Rensing C., Wang G.; RT "Characterization and genomic analysis of chromate resistant and RT reducing Bacillus cereus strain SJ1."; RL BMC Microbiol. 10:221-221(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFM01000080; EFI64343.1; -; Genomic_DNA. DR ProteinModelPortal; D7WK65; -. DR EnsemblBacteria; EFI64343; EFI64343; BCSJ1_20293. DR PATRIC; 40975240; VBIBacCer147688_4148. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23495 MW; 43F68C99705CF0E0 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DLELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GANYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID D7WPQ7_9BACI Unreviewed; 214 AA. AC D7WPQ7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BFZC1_05433; OS Lysinibacillus fusiformis ZC1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=714961; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZC1; RX PubMed=20952126; DOI=10.1016/j.jhazmat.2010.09.072; RA He M., Li X., Liu H., Miller S.J., Wang G., Rensing C.; RT "Characterization and genomic analysis of a highly chromate resistant RT and reducing bacterial strain Lysinibacillus fusiformis ZC1."; RL J. Hazard. Mater. 185:682-688(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADJR01000016; EFI69753.1; -; Genomic_DNA. DR EnsemblBacteria; EFI69753; EFI69753; BFZC1_05433. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23524 MW; 903D038C15E11376 CRC64; MKREDLQLYF IMGTSNVPPQ EQPLYILEKA LQAGITMFQF REKGPHALTG LAYEQFARQC QKLCHQYHVP FIINDDVDLA IRLGADGVHI GQDDLPVGVA RKRVGNMILG VSVHCEEELQ IAINHQADYV GIGPIFPTSS KSDAQPPCGT SFLQEAHSLY PELPIVAIGG INFTNAHSVF QTGVDGVAVI SAICQSKDVD YTVATFRSLT RINK // ID D7X5B8_ECOLX Unreviewed; 211 AA. AC D7X5B8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9552_01807; OS Escherichia coli MS 198-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749549; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 198-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTJ01000199; EFJ74538.1; -; Genomic_DNA. DR ProteinModelPortal; D7X5B8; -. DR EnsemblBacteria; EFJ74538; EFJ74538; HMPREF9552_01807. DR PATRIC; 41745108; VBIEscCol153048_1702. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 4A5B4907CA38B2E8 CRC64; MYQPDFPPVP FHLGLYPVVD SAQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAITLGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVMATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D7XWK2_ECOLX Unreviewed; 211 AA. AC D7XWK2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9536_05479; OS Escherichia coli MS 84-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749533; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 84-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTK01000394; EFJ84252.1; -; Genomic_DNA. DR ProteinModelPortal; D7XWK2; -. DR SMR; D7XWK2; 10-208. DR EnsemblBacteria; EFJ84252; EFJ84252; HMPREF9536_05479. DR PATRIC; 41763376; VBIEscCol149365_5009. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D7Y6A8_ECOLX Unreviewed; 211 AA. AC D7Y6A8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9540_03126; OS Escherichia coli MS 115-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749537; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 115-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTL01000265; EFJ96814.1; -; Genomic_DNA. DR ProteinModelPortal; D7Y6A8; -. DR SMR; D7Y6A8; 20-202. DR EnsemblBacteria; EFJ96814; EFJ96814; HMPREF9540_03126. DR PATRIC; 41770171; VBIEscCol148838_2888. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D7YMU8_ECOLX Unreviewed; 211 AA. AC D7YMU8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9548_03903; OS Escherichia coli MS 182-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749545; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 182-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTM01000326; EFK01363.1; -; Genomic_DNA. DR ProteinModelPortal; D7YMU8; -. DR SMR; D7YMU8; 20-202. DR EnsemblBacteria; EFK01363; EFK01363; HMPREF9548_03903. DR PATRIC; 41781719; VBIEscCol159572_3710. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D7YXF2_ECOLX Unreviewed; 211 AA. AC D7YXF2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9531_01907; OS Escherichia coli MS 45-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749528; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS45-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTO01000129; EFJ92989.1; -; Genomic_DNA. DR ProteinModelPortal; D7YXF2; -. DR SMR; D7YXF2; 9-208. DR EnsemblBacteria; EFJ92989; EFJ92989; HMPREF9531_01907. DR PATRIC; 41798254; VBIEscCol150835_1797. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23030 MW; D9436839F2B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSTIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D7ZA81_ECOLX Unreviewed; 211 AA. AC D7ZA81; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9534_01129; OS Escherichia coli MS 69-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749531; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 69-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTP01000079; EFJ82808.1; -; Genomic_DNA. DR ProteinModelPortal; D7ZA81; -. DR EnsemblBacteria; EFJ82808; EFJ82808; HMPREF9534_01129. DR PATRIC; 41807171; VBIEscCol149851_1076. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22968 MW; FB6435AD7D73F6B8 CRC64; MYQPDFPPVP FHLGLYPVVD SVQWIERLLD AGVLTLQLRI KDRRDEEAEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLP RAPAVMATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D7ZQY3_ECOLX Unreviewed; 211 AA. AC D7ZQY3; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9550_01157; OS Escherichia coli MS 187-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749547; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 187-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTQ01000063; EFK26686.1; -; Genomic_DNA. DR ProteinModelPortal; D7ZQY3; -. DR SMR; D7ZQY3; 20-202. DR EnsemblBacteria; EFK26686; EFK26686; HMPREF9550_01157. DR PATRIC; 41818022; VBIEscCol152054_1118. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D8AAP8_ECOLX Unreviewed; 211 AA. AC D8AAP8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9530_03627; OS Escherichia coli MS 21-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749527; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 21-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTR01000340; EFK19785.1; -; Genomic_DNA. DR ProteinModelPortal; D8AAP8; -. DR EnsemblBacteria; EFK19785; EFK19785; HMPREF9530_03627. DR PATRIC; 41831865; VBIEscCol155740_3437. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23196 MW; 3525E55517F1092E CRC64; MYQPDFPHVP FRLGLYPVVD SVQWIERLLD ADVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLDAIRT AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLVDYP TVAIGGISLP RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGAGD E // ID D8AJR3_ECOLX Unreviewed; 211 AA. AC D8AJR3; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9541_00994; OS Escherichia coli MS 116-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749538; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 116-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTZ01000091; EFK16624.1; -; Genomic_DNA. DR ProteinModelPortal; D8AJR3; -. DR SMR; D8AJR3; 20-202. DR EnsemblBacteria; EFK16624; EFK16624; HMPREF9541_00994. DR PATRIC; 41848065; VBIEscCol149313_0953. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D8AYN4_ECOLX Unreviewed; 211 AA. AC D8AYN4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9547_00698; OS Escherichia coli MS 175-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749544; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 175-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUB01000052; EFJ68059.1; -; Genomic_DNA. DR ProteinModelPortal; D8AYN4; -. DR SMR; D8AYN4; 20-202. DR EnsemblBacteria; EFJ68059; EFJ68059; HMPREF9547_00698. DR PATRIC; 41857716; VBIEscCol149395_0687. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D8BIN5_ECOLX Unreviewed; 211 AA. AC D8BIN5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9553_02864; OS Escherichia coli MS 200-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749550; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 200-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUC01000220; EFJ61060.1; -; Genomic_DNA. DR ProteinModelPortal; D8BIN5; -. DR SMR; D8BIN5; 10-208. DR EnsemblBacteria; EFJ61060; EFJ61060; HMPREF9553_02864. DR PATRIC; 41869052; VBIEscCol157889_2697. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23086 MW; 1A8F52AF19C8B3F0 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ERPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D8BW61_ECOLX Unreviewed; 211 AA. AC D8BW61; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9551_01880; OS Escherichia coli MS 196-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749548; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 196-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUD01000221; EFI89094.1; -; Genomic_DNA. DR ProteinModelPortal; D8BW61; -. DR SMR; D8BW61; 20-202. DR EnsemblBacteria; EFI89094; EFI89094; HMPREF9551_01880. DR PATRIC; 41877773; VBIEscCol147078_1710. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D8CBU4_ECOLX Unreviewed; 211 AA. AC D8CBU4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9549_01778; OS Escherichia coli MS 185-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749546; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 185-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUE01000129; EFJ56777.1; -; Genomic_DNA. DR ProteinModelPortal; D8CBU4; -. DR SMR; D8CBU4; 9-208. DR EnsemblBacteria; EFJ56777; EFJ56777; HMPREF9549_01778. DR PATRIC; 41888690; VBIEscCol149832_1674. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23030 MW; D9436839F2B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSTIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D8D009_COMTE Unreviewed; 313 AA. AC D8D009; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CTS44_00539; OS Comamonas testosteroni S44. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=563045; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S44; RX PubMed=21704702; DOI=10.1016/j.resmic.2011.06.002; RA Xiong J., Li D., Li H., He M., Miller S.J., Yu L., Rensing C., RA Wang G.; RT "Genome analysis and characterization of zinc efflux systems of a RT highly zinc-resistant bacterium, Comamonas testosteroni S44."; RL Res. Microbiol. 162:671-679(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVQ01000006; EFI63744.1; -; Genomic_DNA. DR ProteinModelPortal; D8D009; -. DR EnsemblBacteria; EFI63744; EFI63744; CTS44_00539. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 137 141 HMP-PP binding (By similarity). FT METAL 170 170 Magnesium (By similarity). FT METAL 189 189 Magnesium (By similarity). FT BINDING 169 169 HMP-PP (By similarity). FT BINDING 211 211 HMP-PP (By similarity). FT BINDING 240 240 HMP-PP (By similarity). FT BINDING 269 269 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 313 AA; 33381 MW; 5BC9DE207987C535 CRC64; MDSAEIKALA QAIVHQHCAH FGAQLHHDAN SVELTPQPVP PALRQEPAYL AALEACSELG FIAVDAQTLA QAWQCQSERN NHFDVTHWPD DPRDFGLGKA DPALAFAHCP RELGLYGVLP TAEWVGRMAR AGVPTVQLRF KSGDQAAVAR EVKAAVEAVK GTQARLFIND HWQAALDAGA YGIHVGQEDL DVIGQRDLET ICSSGTRLGV STHGYAEMVR AHAVQPSYIA LGAVFPTTLK KMATAPQGLA RLAAYVRLMQ QYPLVAIGGI SEDLFPAVRA TGVGSVAVVR ALVNAPDPEA AAKHLLARMQ AAA // ID D8DTX2_PREBR Unreviewed; 205 AA. AC D8DTX2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PBR_1558; OS Prevotella bryantii B14. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=752555; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B14; RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8; RG North American Consortium for Rumen Bacteria; RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I., RA Coutinho P.M., Henrissat B., Nelson K.E.; RT "Comparative genome analysis of Prevotella ruminicola and Prevotella RT bryantii: insights into their environmental niche."; RL Microb. Ecol. 60:721-729(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWO01000015; EFI73182.1; -; Genomic_DNA. DR ProteinModelPortal; D8DTX2; -. DR EnsemblBacteria; EFI73182; EFI73182; PBR_1558. DR PATRIC; 41081637; VBIPreBry159466_0412. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 30 34 HMP-PP binding (By similarity). FT REGION 127 129 THZ-P binding (By similarity). FT METAL 63 63 Magnesium (By similarity). FT METAL 82 82 Magnesium (By similarity). FT BINDING 62 62 HMP-PP (By similarity). FT BINDING 101 101 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22490 MW; 10DDCB715DC7CAE4 CRC64; MIQFISHYTE HYSYLDGIRM ALQGGCRWIQ LRMKDATDEE IRPIALQAMQ LCKDAHATFI IDDHVALVKE LGADGVHLGK KDMPIDQARQ ILGPQTIIGG TANTFEDIQA HAASGANYIG CGPFRFTTTK KGLSPILGLE GYRQIVSLMR KAHIDLPIVA IGGITAQDIP DIMQTGVNGI ALSGTVLRAD NPIKEMQRLL QLIKE // ID D8DTX6_PREBR Unreviewed; 197 AA. AC D8DTX6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 16. DE SubName: Full=Putative hydroxymethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase; GN ORFNames=PBR_1562; OS Prevotella bryantii B14. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=752555; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B14; RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8; RG North American Consortium for Rumen Bacteria; RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I., RA Coutinho P.M., Henrissat B., Nelson K.E.; RT "Comparative genome analysis of Prevotella ruminicola and Prevotella RT bryantii: insights into their environmental niche."; RL Microb. Ecol. 60:721-729(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWO01000015; EFI73186.1; -; Genomic_DNA. DR EnsemblBacteria; EFI73186; EFI73186; PBR_1562. DR PATRIC; 41081645; VBIPreBry159466_0416. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Kinase; Transferase. SQ SEQUENCE 197 AA; 22559 MW; B0921938B300E149 CRC64; MFTTVVITMP DKIEREAQRI VELLASAHSA NREGLHVSTT NPKRKYADLI HIRKPNWTFS QIEALIREIP EDYYSRIVLH DHHELAIRYH LYGIHLNRRN PEPIEGWQGS ISKSCHSIEE VITWKKRCNY VSLSPIYNSI SKIGYQAAFT KSQIEQAVKD GIITSKVYAL GGVTYDKLQE LEHTGFGGAL LLGDAWR // ID D8ED79_ECOLX Unreviewed; 211 AA. AC D8ED79; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9346_04494; OS Escherichia coli MS 119-7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=679206; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 119-7; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWU01000045; EFK43944.1; -; Genomic_DNA. DR ProteinModelPortal; D8ED79; -. DR EnsemblBacteria; EFK43944; EFK43944; HMPREF9346_04494. DR PATRIC; 41107801; VBIEscCol144184_4377. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23001 MW; C731953E5F949172 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGVSLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D8EUL0_ECOLX Unreviewed; 211 AA. AC D8EUL0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9345_04903; OS Escherichia coli MS 107-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=679207; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 107-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWV01000039; EFK48688.1; -; Genomic_DNA. DR ProteinModelPortal; D8EUL0; -. DR SMR; D8EUL0; 10-208. DR EnsemblBacteria; EFK48688; EFK48688; HMPREF9345_04903. DR PATRIC; 41119307; VBIEscCol145094_4728. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID D8F275_9DELT Unreviewed; 209 AA. AC D8F275; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NPH_6106; OS delta proteobacterium NaphS2. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=88274; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NaphS2; RX PubMed=21124915; DOI=10.1371/journal.pone.0014072; RA Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., RA Mouser P., Lipton M.S., Deboy R., Methe B.A.; RT "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and RT Analysis of Differential Gene Expression during Anaerobic Growth on RT Naphthalene."; RL PLoS ONE 5:E14072-E14072(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NaphS2; RA DeBoy R., Durkin A.S., Methe B., Young N.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZZ01000236; EFK10141.1; -; Genomic_DNA. DR ProteinModelPortal; D8F275; -. DR EnsemblBacteria; EFK10141; EFK10141; NPH_6106. DR PATRIC; 41129532; VBIDelPro22622_2251. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21999 MW; 4E2EC79DB241BE8C CRC64; MKRIGKLHVL TDTVLQSRFS HTELAKQAIS GGADTIQFRQ KNGSTKELIE IATEIKRICS EMGAAFIVND RIDVAIASEA DGIHLGQEDF PLPLARKLLG KNRIIGGSAG TPEEIEICLR GGVDYIGFGP VYATGSKDDA GPATGIDFLK RIAQTTAVPV IAIGGIDQTN AARVMSAGAH GIAVISCVCC RDNPANAARE LNDIINASS // ID D8G2Y9_9CYAN Unreviewed; 360 AA. AC D8G2Y9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=OSCI_3250006; OS Oscillatoria sp. PCC 6506. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Oscillatoria. OX NCBI_TaxID=272129; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 6506; RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.; RT "The Genome Sequence of the Cyanobacterium Oscillatoria sp. PCC 6506 RT Reveals Several Gene Clusters Responsible for the Biosynthesis of RT Toxins and Secondary Metabolites."; RL J. Bacteriol. 192:5264-5265(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CACA01000290; CBN56979.1; -; Genomic_DNA. DR ProteinModelPortal; D8G2Y9; -. DR EnsemblBacteria; CBN56979; CBN56979; OSCI_3250006. DR PATRIC; 41251869; VBIOscSp14852_3777. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 129 Unknown (By similarity). FT REGION 130 360 Thiamine-phosphate synthase (By FT similarity). FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 360 AA; 40427 MW; AE85575854A02BB0 CRC64; MGDKHSKSIL AQPALCRILD ANLDRSREGL RIIEEWCRFG LNSVELAKEC KQLRQELASW HSVDLRTARD TPGDPGTDLT HPQEEERSSI ESLLQVNFCR VEEALRVVEE YSKIYNPEMG SAFKQMRYRV YTLESSLLAY RRQQQLTRSH FYLVTNPAEH LFAIVEAALQ GGLNIVQYRD KSADDTVRLN KAQKLCELCH RYGALFILND RVDLAIATGA DGVHLGQEDI PISLARQLLG PGRIIGRSTT NKEEMHRAIK DGADYIGVGP VYETPTKPGK SAAGLDYVRY AVEHSTVPWF AIGGIDINNL EEVLKAGADR IAVVRSVMEA EQPTLVTQYF ISQLTRVQTM RSQKNLPGNS // ID D8GCG0_LACCZ Unreviewed; 213 AA. AC D8GCG0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-APR-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LCAZH_0348; OS Lactobacillus casei (strain Zhang). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=498216; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Zhang; RA Meng H.; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Zhang; RX PubMed=20675486; DOI=10.1128/JB.00802-10; RA Zhang W., Yu D., Sun Z., Wu R., Chen X., Chen W., Meng H., Hu S., RA Zhang H.; RT "Complete genome sequence of Lactobacillus casei Zhang, a new RT probiotic strain isolated from traditional homemade koumiss in Inner RT Mongolia, China."; RL J. Bacteriol. 192:5268-5269(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001084; ADK17641.1; -; Genomic_DNA. DR RefSeq; YP_003787491.1; NC_014334.1. DR ProteinModelPortal; D8GCG0; -. DR EnsemblBacteria; ADK17641; ADK17641; LCAZH_0348. DR GeneID; 9458268; -. DR KEGG; lcz:LCAZH_0348; -. DR PATRIC; 42376624; VBILacCas45142_0334. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; LCAS498216:GH2S-348-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22607 MW; 1C71894D5791C1D5 CRC64; MNATDLKLYL VTHRYDDNEA TFLAKIAAAC ENGVTMVQLR EKMLSTRAYF ELAQRVKLIT DRYQIPLIID DRVDICLAVD AAGVHIGDDE LPVAMTRQLI GPDKVLGVST KTVETAVAAV AAGADYLGVG AIFPTQTKAN AAVTPIATLK AITAQVAVPV VAIGGVKEAN LATFKDTGIA GVAIVSEIMQ APDIAHKVQA LRTKLKAVLP NDR // ID D8GRI4_CLOLD Unreviewed; 203 AA. AC D8GRI4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; OrderedLocusNames=CLJU_c33060; OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=748727; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55383 / DSM 13528 / PETC; RX PubMed=20616070; DOI=10.1073/pnas.1004716107; RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A., RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.; RT "Clostridium ljungdahlii represents a microbial production platform RT based on syngas."; RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001666; ADK16352.1; -; Genomic_DNA. DR RefSeq; YP_003781454.1; NC_014328.1. DR ProteinModelPortal; D8GRI4; -. DR EnsemblBacteria; ADK16352; ADK16352; CLJU_c33060. DR GeneID; 9446922; -. DR KEGG; clj:CLJU_c33060; -. DR PATRIC; 42487983; VBICloLju82977_3349. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR BioCyc; CLJU748727:GHMO-3305-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21928 MW; 15E4D0B59E3DDC09 CRC64; MEVDYSLYLV TDRSFLKDKS LQQAVEESIL GGVTLVQLRE KDASTREFYE IAKEVKKVTD HYKVPFLIND RLDIAQAVDA DGVHLGQSDM PINTARKILG KDKIIGISAG NVDEALEAEK NGADYIGIGT IFFTGTKKDI DTPIGIEGLR KIYSSINIPA VAIGGVNETN FKEVFSTGVD GISVISAILG KSDITAASKA LCK // ID D8GS59_CLOLD Unreviewed; 200 AA. AC D8GS59; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; Synonyms=thiE; OrderedLocusNames=CLJU_c13440; OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=748727; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55383 / DSM 13528 / PETC; RX PubMed=20616070; DOI=10.1073/pnas.1004716107; RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A., RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.; RT "Clostridium ljungdahlii represents a microbial production platform RT based on syngas."; RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001666; ADK14412.1; -; Genomic_DNA. DR RefSeq; YP_003779514.1; NC_014328.1. DR EnsemblBacteria; ADK14412; ADK14412; CLJU_c13440. DR GeneID; 9444961; -. DR KEGG; clj:CLJU_c13440; -. DR PATRIC; 42483884; VBICloLju82977_1313. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEEAVIA; -. DR BioCyc; CLJU748727:GHMO-1344-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 102 102 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 158 158 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 200 AA; 22196 MW; 4888AEE25DA57C7D CRC64; MNKKLYIVTN RRLVKNKNMI DILKASILGG ADAIILREKD LTYRQLVPIA EEIKKITDSS NIPLIINNSI ETALKVNAKG FHTSYQNYMN SNLKLKCTVG VSVHNTLEAI NAQKKGADYL LTGHIFETDC KKGLKGRGIS FLKEVLSNIS IPVIAIGGIT ETNIDTVLET KVRGAAVMSL VMTSDDPFTT TYNLKKHFKR // ID D8GZQ5_BACAI Unreviewed; 219 AA. AC D8GZQ5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; Synonyms=thiE; OrderedLocusNames=BACI_c04280; OS Bacillus cereus var. anthracis (strain CI). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=637380; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CI; RX PubMed=20634886; DOI=10.1371/journal.pone.0010986; RA Klee S.R., Brzuszkiewicz E.B., Nattermann H., Bruggemann H., Dupke S., RA Wollherr A., Franz T., Pauli G., Appel B., Liebl W., Couacy-Hymann E., RA Boesch C., Meyer F.D., Leendertz F.H., Ellerbrok H., Gottschalk G., RA Grunow R., Liesegang H.; RT "The genome of a Bacillus isolate causing anthrax in chimpanzees RT combines chromosomal properties of B. cereus with B. anthracis RT virulence plasmids."; RL PLoS ONE 5:E10986-E10986(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001746; ADK03164.1; -; Genomic_DNA. DR RefSeq; YP_003790302.1; NC_014335.1. DR ProteinModelPortal; D8GZQ5; -. DR EnsemblBacteria; ADK03164; ADK03164; BACI_c04280. DR GeneID; 9452946; -. DR KEGG; bal:BACI_c04280; -. DR PATRIC; 42175397; VBIBacCer111781_0693. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; BCER637380:GHO7-414-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23482 MW; D33A0EEF285CFD9C CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID D8H1Z9_BACAI Unreviewed; 208 AA. AC D8H1Z9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 20. DE SubName: Full=Transcriptional regulator TenI; DE EC=2.5.1.3; GN Name=thiE2; OrderedLocusNames=BACI_c07600; OS Bacillus cereus var. anthracis (strain CI). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=637380; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CI; RX PubMed=20634886; DOI=10.1371/journal.pone.0010986; RA Klee S.R., Brzuszkiewicz E.B., Nattermann H., Bruggemann H., Dupke S., RA Wollherr A., Franz T., Pauli G., Appel B., Liebl W., Couacy-Hymann E., RA Boesch C., Meyer F.D., Leendertz F.H., Ellerbrok H., Gottschalk G., RA Grunow R., Liesegang H.; RT "The genome of a Bacillus isolate causing anthrax in chimpanzees RT combines chromosomal properties of B. cereus with B. anthracis RT virulence plasmids."; RL PLoS ONE 5:E10986-E10986(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001746; ADK03447.1; -; Genomic_DNA. DR RefSeq; YP_003790585.1; NC_014335.1. DR EnsemblBacteria; ADK03447; ADK03447; BACI_c07600. DR GeneID; 9453272; -. DR KEGG; bal:BACI_c07600; -. DR PATRIC; 42176078; VBIBacCer111781_0996. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR BioCyc; BCER637380:GHO7-740-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 208 AA; 23239 MW; B4C18C25B68527A0 CRC64; MNMKNELHVI SNGYMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLKKGFPA SKLVINDRID IAILLNIPRV QLGYRSTDVR SVKEKFSYLH VGYSVHSLEE AIEAFKNGAD SLVYGHVFPI ECKKGVPARG LEEISDIARS LSIPIIAIGG ITPENTKDIL ASEVSGIAVM SGIVSSSNPY SKAKSYKESI RKWVEKHV // ID D8HD65_STAAF Unreviewed; 213 AA. AC D8HD65; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SAOV_2132c; OS Staphylococcus aureus subsp. aureus (strain ED133). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=685039; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ED133; RX PubMed=20624747; RA Guinane C.M., Ben Zakour N.L., Tormo-Mas M.A., Weinert L.A., RA Lowder B.V., Cartwright R.A., Smyth D.S., Smyth C.J., Lindsay J.A., RA Gould K.A., Witney A., Hinds J., Bollback J.P., Rambaut A., RA Penades J.R., Fitzgerald J.R.; RT "Evolutionary genomics of Staphylococcus aureus reveals insights into RT the origin and molecular basis of ruminant host adaptation."; RL Genome Biol. Evol. 2:454-466(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001996; ADI98587.1; -; Genomic_DNA. DR RefSeq; YP_005737569.1; NC_017337.1. DR ProteinModelPortal; D8HD65; -. DR EnsemblBacteria; ADI98587; ADI98587; SAOV_2132c. DR GeneID; 12324184; -. DR KEGG; sue:SAOV_2132c; -. DR PATRIC; 43200014; VBIStaAur142340_2183. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SAUR685039:GLKK-2128-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23301 MW; A8845F534C160E89 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLGEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D8HJJ7_AMYMU Unreviewed; 219 AA. AC D8HJJ7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AMED_8579; OS Amycolatopsis mediterranei (strain U-32). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Amycolatopsis. OX NCBI_TaxID=749927; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=U-32; RX PubMed=20567260; DOI=10.1038/cr.2010.87; RA Zhao W., Zhong Y., Yuan H., Wang J., Zheng H., Wang Y., Cen X., Xu F., RA Bai J., Han X., Lu G., Zhu Y., Shao Z., Yan H., Li C., Peng N., RA Zhang Z., Zhang Y., Lin W., Fan Y., Qin Z., Hu Y., Zhu B., Wang S., RA Ding X., Zhao G.P.; RT "Complete genome sequence of the rifamycin SV-producing Amycolatopsis RT mediterranei U32 revealed its genetic characteristics in phylogeny and RT metabolism."; RL Cell Res. 20:1096-1108(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002000; ADJ50274.1; -; Genomic_DNA. DR RefSeq; YP_003770676.1; NC_014318.1. DR ProteinModelPortal; D8HJJ7; -. DR EnsemblBacteria; ADJ50274; ADJ50274; AMED_8579. DR GeneID; 9442714; -. DR KEGG; amd:AMED_8579; -. DR PATRIC; 42164769; VBIAmyMed151214_8907. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; AMED749927:GCZN-8505-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22846 MW; 82C1A8E84F9D5BC3 CRC64; MPALSGDKIR ARLDSARLYL CTDARTNRGD LAAFADAALA GGVDIVQLRD KTGALEAAGE IAALEVLAEA CARHGALLSV NDRADVALAV GADVLHLGQD DIPVPLARRI LGDEVVIGRS THSLDQALAA AAEPGVDYFC TGPCWPTPTK PGRPAPGLDL VRATAAWTPD RPWFAIGGID GPRLPEVLDA GASRIVVVRA ITEAEDPEAA ARELRARLP // ID D8IBR7_BRAP9 Unreviewed; 229 AA. AC D8IBR7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-APR-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BP951000_0589; OS Brachyspira pilosicoli (strain ATCC BAA-1826 / 95/1000). OC Bacteria; Spirochaetes; Spirochaetales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=759914; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1826 / 95/1000; RX PubMed=20625514; DOI=10.1371/journal.pone.0011455; RA Wanchanthuek P., Bellgard M.I., La T., Ryan K., Moolhuijzen P., RA Chapman B., Black M., Schibeci D., Hunter A., Barrero R., RA Phillips N.D., Hampson D.J.; RT "The complete genome sequence of the pathogenic intestinal spirochete RT Brachyspira pilosicoli and comparison with other Brachyspira RT genomes."; RL PLoS ONE 5:E11455-E11455(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002025; ADK30590.1; -; Genomic_DNA. DR RefSeq; YP_003785091.1; NC_014330.1. DR EnsemblBacteria; ADK30590; ADK30590; BP951000_0589. DR GeneID; 9450708; -. DR KEGG; bpo:BP951000_0589; -. DR PATRIC; 42195617; VBIBraPil164347_0580. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; BPIL759914:GHZ5-588-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 56 60 HMP-PP binding (By similarity). FT REGION 156 158 THZ-P binding (By similarity). FT REGION 207 208 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 159 159 HMP-PP (By similarity). FT BINDING 187 187 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 25988 MW; 2AD7A24A594724DB CRC64; MNNFKNLKNK KDKRDYLKEN YFNKSIYCVT AEDFSKGRNN IEVVGSMLEA GIKIIQYREK ENPKKYMREK YEECVKIREM TRKSNALFIV DDYADLALAV EADGVHIGQN DMPIEVVRKI VGDDMIIGLS TKNIDEANEA FNSSADYIGV GPIFDTNTKI DANSAVGVEY LDYIAKNIDM PFVCIGGIKL NNMDLLIEHN AKCLCMLTEI VASDDIKNKC ETLIKKMHS // ID D8IX80_HERSS Unreviewed; 210 AA. AC D8IX80; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Hsero_0430; OS Herbaspirillum seropedicae (strain SmR1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Herbaspirillum. OX NCBI_TaxID=757424; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SmR1; RA Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., RA Colauto N.B., Fernandez M.A., Fungaro M.H.P., Grisard E.C., RA Hungria M., Madeira H.M.F., Nodari R.O., Osaku C.A., Petzl-Erler M.L., RA Terenzi H., Vieira L.G.E., Almeida M.I.M., Alves L.R., Arantes O.M.N., RA Balsanelli E., Barcellos F.G., Baura V.A., Binde D.R., Campo R.J., RA Chubatsu L.S., Chueire L.M.O., Ciferri R.R., Correa L.C., RA da Conceicao Silva J.L., Dabul A.N.G., Dambros B.P., Faoro H., RA Favetti A., Friedermann G., Furlaneto M.C., Gasques L.S., RA Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P., RA Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M., RA Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C., RA Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P., RA Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., RA Prioli S.M.A.P., Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., RA Rigo L.U., Rocha C.L.M.S.C., Rocha S.N., Santos K., Satori D., RA Silva A.G., Simao R.C.G., Soares M.A.M., Souza E.M., Steffens M.B.R., RA Steindel M., Tadra-Sfeir M.Z., Takahashi E.K., Torres R.A., RA Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E., Weiss V.A., RA Yates M.A., Souza E.M.; RT "The genome of Herbaspirillum seropedicae SmR1, an endophytic, RT nitrogen-fixing, plant-growth promoting beta-Proteobacteria."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002039; ADJ61955.1; -; Genomic_DNA. DR RefSeq; YP_003773863.1; NC_014323.1. DR ProteinModelPortal; D8IX80; -. DR EnsemblBacteria; ADJ61955; ADJ61955; Hsero_0430. DR GeneID; 9401031; -. DR KEGG; hse:Hsero_0430; -. DR PATRIC; 42359533; VBIHerSer153339_0440. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; HSER757424:GCTT-430-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22941 MW; DDD6FBB377EFC14A CRC64; MKPEYAKHLR GLYIVTPDWD DTAQLLAATE LALQQGAALV QYRHKTADAQ QRQAQASALL ALCRQYQVPL IINDHVDLCL DIDADGIHVG GTDASIAEVR KAVGPDRIVG ASCYGTLELA HAAYRDGASY VAFGGFYPSR VKKYDFRTAP EIIAHSKREI PLPVVVIGGI TLENAPPLVE QGADMVAVIS SVYLVPVEER KTRELADLYR // ID D8JEZ5_ACISD Unreviewed; 203 AA. AC D8JEZ5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AOLE_04820; OS Acinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=436717; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 1667 / KCTC 23045 / DR1; RX PubMed=20639327; DOI=10.1128/JB.00722-10; RA Jung J., Baek J.H., Park W.; RT "Complete genome sequence of the diesel-degrading Acinetobacter sp. RT strain DR1."; RL J. Bacteriol. 192:4794-4795(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002080; ADI89861.1; -; Genomic_DNA. DR RefSeq; YP_003731234.1; NC_014259.1. DR ProteinModelPortal; D8JEZ5; -. DR EnsemblBacteria; ADI89861; ADI89861; AOLE_04820. DR GeneID; 9381385; -. DR KEGG; acd:AOLE_04820; -. DR PATRIC; 42140967; VBIAciSp20010_0964. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; AOLE436717:GHCD-998-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21832 MW; 01884E48FC3D562B CRC64; MRGLYLITND DPIQLLLEKL DAALATHQVA ILQYRRKKVE KADQPAEVEQ IKLLCEKYQV PFVINDDLKL AVQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YIAFGAVYAT STKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILDRSTAE IPARVQAWAQ LFS // ID D8JFT6_ACISD Unreviewed; 300 AA. AC D8JFT6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 11-DEC-2013, entry version 22. DE SubName: Full=Putative bifunctional protein; GN OrderedLocusNames=AOLE_05600; OS Acinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=436717; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 1667 / KCTC 23045 / DR1; RX PubMed=20639327; DOI=10.1128/JB.00722-10; RA Jung J., Baek J.H., Park W.; RT "Complete genome sequence of the diesel-degrading Acinetobacter sp. RT strain DR1."; RL J. Bacteriol. 192:4794-4795(2010). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002080; ADI90017.1; -; Genomic_DNA. DR RefSeq; YP_003731390.1; NC_014259.1. DR ProteinModelPortal; D8JFT6; -. DR EnsemblBacteria; ADI90017; ADI90017; AOLE_05600. DR GeneID; 9381546; -. DR KEGG; acd:AOLE_05600; -. DR PATRIC; 42141282; VBIAciSp20010_1117. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR BioCyc; AOLE436717:GHCD-1159-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 300 AA; 34408 MW; E69437D99F1F4951 CRC64; MPKPIVDVAI AILIHRGKIL VGWREEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWAWYTREQL LHLNFPKANK DIIKRLYWPH FIKISPTLTP VENDDTLVYW RSEKDSFDQA DLEKLALLDT DQLSKLIVNI DVWHKLKPEL KTHIKTVHLK QSQLMSLHKG DLEVGVRFIA ACHDAVSLQH AQQIGCDAVF ISPVKVTETH PDASALGWDR LNDLIEKCQI PVFALGGMSP DDLVTAQQHG AYGLAGIRNF // ID D8JSF2_HYPDA Unreviewed; 214 AA. AC D8JSF2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN OrderedLocusNames=Hden_2449; OS Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIB OS 11706 / TK 0415). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Hyphomicrobium. OX NCBI_TaxID=582899; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002083; ADJ24246.1; -; Genomic_DNA. DR RefSeq; YP_003756567.1; NC_014313.1. DR ProteinModelPortal; D8JSF2; -. DR EnsemblBacteria; ADJ24246; ADJ24246; Hden_2449. DR GeneID; 9388356; -. DR KEGG; hdn:Hden_2449; -. DR PATRIC; 42373627; VBIHypDen91677_2535. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVSAHED; -. DR BioCyc; HDEN582899:GIWL-2483-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 214 AA; 22442 MW; 011D2D3F69E597C7 CRC64; MSSGSKLYLD YVITGPSAQS RPVLSAVLEA SPVASLLIRP GPGAAYDAQV VRELTALAQK QGVAVLVNDV RIASDVGADG VHVAWSADVV ERYRSVRQAA GRDLIVGADA GRTRDDAMQI GEADADYVAF GIPPHVDDRS RAAERQLDLV TWWSEVFEIP CVALDVANAE HARALSAAGA DFVGITIAAD QSASEAAARV RAYSEAVSAH EDAT // ID D8JTE0_HYPDA Unreviewed; 204 AA. AC D8JTE0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Hden_2662; OS Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIB OS 11706 / TK 0415). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Hyphomicrobium. OX NCBI_TaxID=582899; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002083; ADJ24458.1; -; Genomic_DNA. DR RefSeq; YP_003756779.1; NC_014313.1. DR ProteinModelPortal; D8JTE0; -. DR EnsemblBacteria; ADJ24458; ADJ24458; Hden_2662. DR GeneID; 9388571; -. DR KEGG; hdn:Hden_2662; -. DR PATRIC; 42374095; VBIHypDen91677_2767. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; HDEN582899:GIWL-2698-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 30 34 HMP-PP binding (By similarity). FT REGION 179 180 THZ-P binding (By similarity). FT METAL 63 63 Magnesium (By similarity). FT METAL 82 82 Magnesium (By similarity). FT BINDING 62 62 HMP-PP (By similarity). FT BINDING 101 101 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 159 159 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22121 MW; A2E6BAE7747B658B CRC64; MPVKLAPFYP IVPDIGWLER IVPLGVKLVQ LRIKDAARDD VIDQTRRALA VTRAHGCQLV VNDYWDVAIE AGADFIHLGQ DDLETADLAA LRQAGVRFGV STHDEAELAK ALSVNPDYVA LGPIYPTKLK VMPWAPQGLE RIKLWRSKIG ALPLVAIGGL TPDRADGAVD AGANSLAVIT DFVTAEDANA RVKEWLAWAA GRQN // ID D8K0E3_DEHLB Unreviewed; 291 AA. AC D8K0E3; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Dehly_0766; OS Dehalogenimonas lykanthroporepellens (strain ATCC BAA-1523 / JCM 15061 OS / BL-DC-9). OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalogenimonas. OX NCBI_TaxID=552811; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1523 / JCM 15061 / BL-DC-9; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Daligault H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ovchinnikova G., Rainey F.A., Yan J., RA da Costa M.S., Moe W.M., Woyke T.; RT "Complete sequence of Dehalogenimonas lykanthroporepellens BL-DC-9."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002084; ADJ26071.1; -; Genomic_DNA. DR RefSeq; YP_003758392.1; NC_014314.1. DR EnsemblBacteria; ADJ26071; ADJ26071; Dehly_0766. DR GeneID; 9390466; -. DR KEGG; dly:Dehly_0766; -. DR PATRIC; 42249881; VBIDehLyk78720_0803. DR KO; K00788; -. DR OMA; NCARVEE; -. DR BioCyc; DLYK552811:GH8P-793-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 291 AA; 31239 MW; F5CBFF58DA4C1FAE CRC64; MPNGNNLTQL HSQTLRAIDA NLDRATEGLR VLEDIARFCL NSSGYSLALK SLRHDLTESI HYSSIQLLSA RDATADVGRR ADNDKTVFKN LTETVSANAR RVEQSLRVLE ELARLPETGL AAGFIEQARY RVYEMEKSLA GALTRQERLS RLGNSYLVTG SPEKAATALT RQDTSVQLND AGNRGELWRQ VLAFSRSRSG DSGLLIIGEY ADIAVAVSAD GVAIDGGSLP PDAVRNLLSI DQLIGYAATD VAEAESAVSA GADYLICAAG LKTSLAGRVE IPVVLPLEEL P // ID D8K3Q6_DEHLB Unreviewed; 213 AA. AC D8K3Q6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dehly_0248; OS Dehalogenimonas lykanthroporepellens (strain ATCC BAA-1523 / JCM 15061 OS / BL-DC-9). OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalogenimonas. OX NCBI_TaxID=552811; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1523 / JCM 15061 / BL-DC-9; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Daligault H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ovchinnikova G., Rainey F.A., Yan J., RA da Costa M.S., Moe W.M., Woyke T.; RT "Complete sequence of Dehalogenimonas lykanthroporepellens BL-DC-9."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002084; ADJ25575.1; -; Genomic_DNA. DR RefSeq; YP_003757896.1; NC_014314.1. DR ProteinModelPortal; D8K3Q6; -. DR EnsemblBacteria; ADJ25575; ADJ25575; Dehly_0248. DR GeneID; 9389928; -. DR KEGG; dly:Dehly_0248; -. DR PATRIC; 42248765; VBIDehLyk78720_0263. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTLLQYR; -. DR BioCyc; DLYK552811:GH8P-254-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22675 MW; C30F2292079892B8 CRC64; MRLPVTDLYA VLSSAHSAGR GNVRTAELLL QAGVRIIQYR EKEFPFDRQL AECAEIARLS GLHNACFIVN DSLELALAAG AGGLHLGQSD LPPAVARVRL GRDKIIGYSV TCPAEVDRAL AMSDIDYLGV GPVYATATKR DATRPGGLEL IDYALRLSPV PVVAIGGIGR HNAAELARRG VPTLAMVTEL VGAPDIAERV RELRAVMWGD SPA // ID D8K9T0_NITWC Unreviewed; 217 AA. AC D8K9T0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Nwat_2491; OS Nitrosococcus watsoni (strain C-113). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=105559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C-113; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Malfatti S.A., Chain P.S.G., Land M., Hauser L., RA Kyrpides N., Ivanova N., Cambell M.A., Heidelberg J.F., Klotz M.G., RA Woyke T.; RT "Complete sequence of chromosome of Nitrosococcus watsoni C-113."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002086; ADJ29288.1; -; Genomic_DNA. DR RefSeq; YP_003761609.1; NC_014315.1. DR ProteinModelPortal; D8K9T0; -. DR EnsemblBacteria; ADJ29288; ADJ29288; Nwat_2491. DR GeneID; 9393986; -. DR KEGG; nwa:Nwat_2491; -. DR PATRIC; 42237647; VBINitWat28885_2678. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; NWAT105559:GHXU-2538-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23300 MW; A4FAEA5D221B1EBC CRC64; MSSSIRGLYA IADTHLLPRQ DLGNAVALAL QGGASLIQYR DKSQEVARRY EEAESLHQIC RQYQAPLIIN DDALLAAEIG AEGVHLGRDD SSIRSARKIL GAKAIIGISC YNELARAIAA EQASADYVAF GRVFPSITKP EPVWASLALL REARKSLNLP IVAIGGITPE NAPQVIEAGA SAVAVIGGLF RSQDIRATAA AYQQLFPSWR LPKPRLS // ID D8KA54_NITWC Unreviewed; 317 AA. AC D8KA54; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-OCT-2013, entry version 23. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=Nwat_0402; OS Nitrosococcus watsoni (strain C-113). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=105559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C-113; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Malfatti S.A., Chain P.S.G., Land M., Hauser L., RA Kyrpides N., Ivanova N., Cambell M.A., Heidelberg J.F., Klotz M.G., RA Woyke T.; RT "Complete sequence of chromosome of Nitrosococcus watsoni C-113."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002086; ADJ27369.1; -; Genomic_DNA. DR RefSeq; YP_003759690.1; NC_014315.1. DR ProteinModelPortal; D8KA54; -. DR EnsemblBacteria; ADJ27369; ADJ27369; Nwat_0402. DR GeneID; 9391855; -. DR KEGG; nwa:Nwat_0402; -. DR PATRIC; 42233099; VBINitWat28885_0441. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; NWAT105559:GHXU-408-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 317 AA; 35062 MW; 101162AE4273C8DC CRC64; MVLQVAAGAI FNREGQVLLS KRPPHVHQGN LWEFPGGKLQ PGEEIRQALS RELWEELGIQ VLQARPLLQV RHDYPDRSVL LHVWRVERFS GMPKGQEGQP VVWVQPENLS AYPLPAANSP IVTAVCLPPT YLITKEPAGN QIVFLSSLRR SLQAGVRLVQ LRAKKLSSEH YQDLTWKVQR LCFEYKAILL VNTVPAQAAE WGADGVHLTG NHLMHLSQRP LPADKWVAAS CHNAEQLAHA ASIGVDFAVL GPVCHTSTHP QALPLGWERF QTLIAQIPFP VYALGGLGPE HVKEAWSRGA QGIAAIRGLW GDRGSRD // ID D8KIG7_LACLN Unreviewed; 218 AA. AC D8KIG7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LLNZ_06275; OS Lactococcus lactis subsp. cremoris (strain NZ9000). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=746361; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NZ9000; RX PubMed=20639323; DOI=10.1128/JB.00533-10; RA Linares D.M., Kok J., Poolman B.; RT "Genome sequences of Lactococcus lactis MG1363 (revised) and NZ9000 RT and comparative physiological studies."; RL J. Bacteriol. 192:5806-5812(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002094; ADJ60213.1; -; Genomic_DNA. DR RefSeq; YP_006356635.1; NC_017949.1. DR ProteinModelPortal; D8KIG7; -. DR EnsemblBacteria; ADJ60213; ADJ60213; LLNZ_06275. DR GeneID; 13019860; -. DR KEGG; lln:LLNZ_06275; -. DR PATRIC; 43095965; VBILacLac151604_1261. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; LLAC746361:GLFF-1235-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23698 MW; F5BA2C42AECE10EB CRC64; MTKKTLDLSV YFIAGSQNFS ECSLDEATQK IALIIKSGVT VYQFRDKGTI YKEQKQRLSI AQKLQKVSEE AGVSFIVNDD VELARELNAD GIHIGQTDES VSKVREKVGQ EMWLGLSVTN ADELKTAQSS GADYLGIGPI YPTNSKNDAA KPIGIKDLRL MLLENQLPIV GIGGITQDSL TELSAIGLDG LAVISLLTEA ENPKKVAQMI RQKITKNG // ID D8LP23_ECTSI Unreviewed; 575 AA. AC D8LP23; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-APR-2014, entry version 16. DE SubName: Full=Thiamine monophosphate synthase; GN Name=Th1; ORFNames=Esi_0052_0039; OS Ectocarpus siliculosus (Brown alga). OC Eukaryota; Stramenopiles; PX clade; Phaeophyceae; Ectocarpales; OC Ectocarpaceae; Ectocarpus. OX NCBI_TaxID=2880; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ec32 / CCAP1310/4; RX PubMed=20520714; DOI=10.1038/nature09016; RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G., RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B., RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., RA Brownlee C., Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., RA Collen J., Corre E., Da Silva C., Delage L., Delaroque N., RA Dittami S.M., Doulbeau S., Elias M., Farnham G., Gachon C.M., RA Gschloessl B., Heesch S., Jabbari K., Jubin C., Kawai H., Kimura K., RA Kloareg B., Kupper F.C., Lang D., Le Bail A., Leblanc C., Lerouge P., RA Lohr M., Lopez P.J., Martens C., Maumus F., Michel G., RA Miranda-Saavedra D., Morales J., Moreau H., Motomura T., Nagasato C., RA Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F., Pommier C., RA Potin P., Poulain J., Quesneville H., Read B., Rensing S.A., RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., RA Segurens B., Strittmatter M., Tonon T., Tregear J.W., Valentin K., RA von Dassow P., Yamagishi T., Van de Peer Y., Wincker P.; RT "The Ectocarpus genome and the independent evolution of RT multicellularity in brown algae."; RL Nature 465:617-621(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN648730; CBN80294.1; -; Genomic_DNA. DR ProteinModelPortal; D8LP23; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 575 AA; 59794 MW; CC03C9C02125CE89 CRC64; MFPSWRGVLL SSLCVRKLSA FAAAPLLPRR GRFGGTRSQS TSRAAMSSGE GCPKPIVWTI AGSDSGGGAG IQADLHAMHS LGVHGCSVIT AMTAQNSHAV THVEYASVEM IQATIDALQS DLPPAAVKLG MMGTDAVVSV VGAFLEGYKG NVVCDPVMVS TSGSRLLPEG AEALMKERVF PRATMITPNL IEAEVLLGRS LRTPADVEAG AASLLASSAA GGVLIKGGHS EDEREPGGAD RPSARQRYSQ DYWTDGTPGG SFWLTTPRVD SDDTHGTGCT LSSAAAACLA KGLDPADSVV LAKAYVTQGI RVARRFGKGP GPVAHTGWPS RADCFPWVTA TAEGGAGGRP EAFPKCHDDW GLYPVVETAE WVEKLLSLGV RDIQLRVKGA SPEALDAEVA RAAQACRDSA AGAGGGGGRL WVNDFWRAAV RHGAYGVHLG QEDLEAGGGE ALSAISKAGL RLGLSTHSYL ELARATAVRP SYISLGPVFE TTSKKVAFSP RGAVLVGAWR ALVDVPLIAI GGISLERAPE VLEAGADSIA VISAITKADD VEEAVRQWDT AFEARRRPLS PSPSS // ID D8M3M2_BLAHO Unreviewed; 443 AA. AC D8M3M2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 16. DE SubName: Full=Singapore isolate B (sub-type 7) whole genome shotgun sequence assembly, scaffold_2; GN ORFNames=GSBLH_T00002614001; OS Blastocystis hominis. OC Eukaryota; Stramenopiles; Blastocystis. OX NCBI_TaxID=12968; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Singapore isolate B / Subtype 7; RX PubMed=21439036; DOI=10.1186/gb-2011-12-3-r29; RA Denoeud F., Roussel M., Noel B., Wawrzyniak I., Da Silva C., RA Diogon M., Viscogliosi E., Brochier-Armanet C., Couloux A., RA Poulain J., Segurans B., Anthouard V., Texier C., Blot N., Poirier P., RA Choo N.G., Tan K.S., Artiguenave F., Jaillon O., Aury J.M., Delbac F., RA Wincker P., Vivares C.P., El Alaoui H.; RT "Genome sequence of the stramenopile Blastocystis, a human anaerobic RT parasite."; RL Genome Biol. 12:R29.1-R29.16(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN668650; CBK22495.2; -; Genomic_DNA. DR ProteinModelPortal; D8M3M2; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 443 AA; 46771 MW; F6D78B4C63AF1FD2 CRC64; MVSEALRPAG VSPEHVVTSR LVYGADGTAG GALDPLCGGC LAKRERLREI LRGETPGRNA REEDIIAYED RGNVETGETG EGKSVKPAQS IDQSAAHQSA STQSADQTNA QSNDQTNDQT NDQTNVQSSW YASALSLLSL SSPVFSVGIG DGLGDLAMLL STDLPIVLSP GSSFRRVCAR FGLALRPLLL LDCPPSPRTL YVADDWAQIL AVLCFAHIDA ALQPLPAEPR RRCTPAECRL MALTSDALNA EGGEAMERAI LESVEGGATM IQIRDKTEDF DRMISHANQL KEMLRRRNVP LIINDRVDVA ILSDADGVHI GQSDMDAALC RRLLGPSKIL GVSAQTPSQA VKAQRDGADY LGCGAVFPTQ SKDDADAVGL EGLRRVCEAV SIPVVSIGGV TAGNAGATMK EGAVGVAVIS AIFGRSDVKE AAKELRDAVE KAL // ID D8MH76_LEUGT Unreviewed; 211 AA. AC D8MH76; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LEGAS_1546; OS Leuconostoc gasicomitatum (strain DSM 15947 / CECT 5767 / JCM 12535 / OS LMG 18811 / TB1-10). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=762550; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15947 / CECT 5767 / JCM 12535 / LMG 18811 / TB1-10; RA Johansson P., Paulin L., Vihavainen E.J., Salovuori N., Alatalo E.R., RA Bjoerkroth J.K., Auvinen P.; RT "Genome sequence and comparative genomics of a food spoilage lactic RT acid bacterium Leuconostoc gasicomitatum 18811T."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN822744; CBL92194.1; -; Genomic_DNA. DR RefSeq; YP_003773013.1; NC_014319.1. DR EnsemblBacteria; CBL92194; CBL92194; LEGAS_1546. DR GeneID; 9398793; -. DR KEGG; lgs:LEGAS_1546; -. DR PATRIC; 42384789; VBILeuGas160647_1562. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MLARYFI; -. DR BioCyc; LGAS762550:GHH1-1901-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22983 MW; 02420FBE6581E59F CRC64; MIFNRAMLAR YFILGTQNVT DERMFYKVLE EALSNGITLF QYREKGFGSL VGANKLRVAQ RVRELTSAYH VPFVIDDDIV LAHIVHADGV HFGQGDGNIA ANIVASHGMF VGVSVSTQAE YERISLLSGI DNIGIGPVFE TKSKADAKPA IGLIALERLV EQSRWPTVAI GGISQDNLAT VLATDVDGAA VISMISDSSN IENVLKYWQQ L // ID D8MKZ1_ERWBE Unreviewed; 215 AA. AC D8MKZ1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EbC_02660; OS Erwinia billingiae (strain Eb661). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=634500; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Eb661; RX PubMed=20565991; DOI=10.1186/1471-2164-11-393; RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H., RA Knaust F., Geider K., Reinhardt R.; RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E. RT tasmaniensis with the pear pathogen E. pyrifoliae."; RL BMC Genomics 11:393-393(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP236843; CAX57797.1; -; Genomic_DNA. DR RefSeq; YP_003739657.1; NC_014306.1. DR ProteinModelPortal; D8MKZ1; -. DR EnsemblBacteria; CAX57797; CAX57797; EbC_02660. DR GeneID; 9428970; -. DR KEGG; ebi:EbC_02660; -. DR PATRIC; 42303338; VBIErwBil95213_0535. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; EBIL634500:GHYX-290-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23176 MW; DAC5711733382DCE CRC64; MSRSAFPPTS AQLGLYPVVE TVAWIARLLE AGVRTIQLRI KDLPEAAVEN DIAAAIELGK RYQARLFIND YWQLAIKYQA YGVHLGQEDL DVADLDAIHR AGLRLGLSTH DDAELDRALA EKPSYIALGH VFPTQTKNMP SSPQGLQELQ RHISRLKGIS TVAIGGISLE RAPQVLATGV GSIAVVSAIT LAPDWQAATA QLLDLAGNGD EAHVQ // ID D8N110_RALSL Unreviewed; 198 AA. AC D8N110; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 11-DEC-2013, entry version 20. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase (ThiE); DE EC=2.5.1.3; GN ORFNames=RPSI07_mp0975; OS Ralstonia solanacearum (Pseudomonas solanacearum). OG Plasmid megaplasmid mpPSI07. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=305; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PSI07; RA Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E., RA Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G., RA Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.; RT "Genomes of three tomato pathogens within the Ralstonia solanacearum RT species complex reveal significant evolutionary divergence."; RL BMC Genomics 11:379-379(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP885891; CBJ35313.1; -; Genomic_DNA. DR RefSeq; YP_003749938.1; NC_014310.1. DR EnsemblBacteria; CBJ35313; CBJ35313; RPSI07_mp0975. DR GeneID; 9411473; -. DR KEGG; rsl:RPSI07_mp0975; -. DR PATRIC; 42534643; VBIRalSol167236_0946. DR HOGENOM; HOG000155781; -. DR BioCyc; RSOL859657:GJJ9-4373-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Transferase. SQ SEQUENCE 198 AA; 21695 MW; DB21452C89A9C686 CRC64; MRRVSLPDFY QITPEPVGSP YFEKFFAELT DTLRSGIRLL QLRAKQLEPR EHLDVARRTR DLCRQFGAIL MLNGPIDMAR EVGCDGVHLS SDALMSLRSR PAPDTVLISA ACHSVAQLEQ AARVEVDFVT LSPVLRTRTH PDADPLGWES FSELVQCSRV PVFALGGMSP ETLDQAKSAG AWGVAAISAT WCQQSAGA // ID D8NA79_RALSL Unreviewed; 384 AA. AC D8NA79; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 22-JAN-2014, entry version 17. DE SubName: Full=THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; DE EC=2.5.1.3; GN Name=thiE; ORFNames=CMR15_30801; OS Ralstonia solanacearum CMR15. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=859655; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CMR15; RA Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E., RA Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G., RA Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.; RT "Genomes of three tomato pathogens within the Ralstonia solanacearum RT species complex reveal significant evolutionary divergence."; RL BMC Genomics 11:379-379(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP885895; CBJ39548.1; -; Genomic_DNA. DR RefSeq; YP_005998300.1; NC_017559.1. DR ProteinModelPortal; D8NA79; -. DR GeneID; 16107084; -. DR KEGG; rsm:CMR15_30801; -. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 384 AA; 40193 MW; 6BD536AB2B843EBA CRC64; MSASALRFAA AWPDAAALAD RLIDRHADAF GRAPHAWSVI DRADDAATAA AVLLTTDAAQ AEHARAAGAA VVLSEARNGE RLDTVHDRLG TYRFAAPATG AVFDERFVAM FGAALALAFE PRDALCVARA WVAEAPADAL AWPACFDALP RVLEPALPCA ASPDLAFAPC PAQLGVYAVV PDAEWVERLV ALEVPTVQLR IKSDDAGAIA EQARRAAAAA RGSRTRLFLN DHWRVALDLH AQRPDSGLYG IHLGQEDIDD ADLAAIRASG LRLGISTHGY AEMLRVAALN PSYLALGAVF ATPTKTMPTV PQGLGRLFAH AAAMRSRVLA PPLVAIGGID LAAMPRVLES GIGSVAVVRA ITQAEDVPAA VQALQATFAA HVRA // ID D8NDK9_RALSL Unreviewed; 204 AA. AC D8NDK9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 22-JAN-2014, entry version 18. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase (ThiE); DE EC=2.5.1.3; GN ORFNames=CMR15_mp20067; OS Ralstonia solanacearum CMR15. OG Plasmid CMR15_mp. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=859655; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CMR15; PLASMID=CMR15_mp; RA Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E., RA Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G., RA Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.; RT "Genomes of three tomato pathogens within the Ralstonia solanacearum RT species complex reveal significant evolutionary divergence."; RL BMC Genomics 11:379-379(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CMR15; PLASMID=CMR15_mp; RA Genoscope - CEA; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP885896; CBJ40643.1; -; Genomic_DNA. DR RefSeq; YP_006060895.1; NC_017589.1. DR ProteinModelPortal; D8NDK9; -. DR GeneID; 13915960; -. DR KEGG; rsm:CMR15_mp20067; -. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Transferase. SQ SEQUENCE 204 AA; 22144 MW; 16965ED82AA39251 CRC64; MGHGHSMRSV SLPDFYQVTP EPAGSPDFEP FFAELTDTLR SGVRLLQLRA KRLDAREHLA VAQRTRDLCR QFGTILILNG PIDMAREAGC DGVHLSSDAL MSLRSRPVPE TVLVSAACHS AEQLEHAARM AVDFVTLSPV LPTRTHPEAE PLGWERFAAL VQGARIPVFA LGGMRPEMLD QAKQAGAWGI AAISATWRRP SAGG // ID D8NRH2_RALSL Unreviewed; 391 AA. AC D8NRH2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 22-JAN-2014, entry version 19. DE SubName: Full=THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; DE EC=2.5.1.3; GN Name=thiE; ORFNames=RCFBP_21343; OS Ralstonia solanacearum CFBP2957. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=859656; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFBP2957; RA Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E., RA Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G., RA Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.; RT "Genomes of three tomato pathogens within the Ralstonia solanacearum RT species complex reveal significant evolutionary divergence."; RL BMC Genomics 11:379-379(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP885897; CBJ44517.1; -; Genomic_DNA. DR RefSeq; YP_003747098.1; NC_014307.1. DR EnsemblBacteria; CBJ44517; CBJ44517; RCFBP_21343. DR GeneID; 9417683; -. DR KEGG; rsc:RCFBP_21343; -. DR PATRIC; 42549275; VBIRalSol166517_3139. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 391 AA; 40943 MW; 5CA99660503DF285 CRC64; MSVNVLYVST AWPGAVALAA QIVDRHAEAF GRAPHAWHVT DRADEATTAA TVLLTADAAQ ADRARAAGAA VVLTETRDGE RIDTVHDRLG TYRFAGAATG EALGERFVAM FGAALVLAFE PRDALCVARA WIAEAPADAL AWPARFEALP RVLEPALPCA ASPELTFAPC PTRLGIYAVV PDADWVERLV ALGVPTVQLR VKSDKSDDAQ AVAGQVRRAA AAARGSTTRL FINDHWRVAL DVHAARPDGA PDSGLYGIHL GQEDIDDADL PAIRASGLRL GISTHGYAEM LRVAPLNPSY LALGAVFATP TKTMPTVPQG LGRLFAHAAA MRTRVPAPPL VAIGGIDLAA MPRVLQSGVG CVAVVRALTQ AEDVPAAVQA LQATFAAHVR A // ID D8P0P6_RALSL Unreviewed; 384 AA. AC D8P0P6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 13-NOV-2013, entry version 20. DE SubName: Full=THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; DE EC=2.5.1.3; GN Name=thiE; ORFNames=RPSI07_3274; OS Ralstonia solanacearum (Pseudomonas solanacearum). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=305; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PSI07; RA Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E., RA Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G., RA Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.; RT "Genomes of three tomato pathogens within the Ralstonia solanacearum RT species complex reveal significant evolutionary divergence."; RL BMC Genomics 11:379-379(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP885906; CBJ52624.1; -; Genomic_DNA. DR EnsemblBacteria; CBJ52624; CBJ52624; RPSI07_3274. DR PATRIC; 42542666; VBIRalSol167236_4901. DR HOGENOM; HOG000155781; -. DR BioCyc; RSOL859657:GJJ9-3312-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 384 AA; 40290 MW; 61C301EC3D8FBAA6 CRC64; MSASALRFAA AWPDAAALAG RIIDRHADAF GRAPHAWSVT DHADEATTAT TVLLTADRAQ AERARAAGAG VVLTETRNGE RIDTVHDRLG TYRFASTATG EALGERFVAM FGAALALAFE PRDALCVARA WIAEAPADAL AWPARFDTLP RVLEPALPCA ASPDLAFAPC PTQLGVYAVV PDAAWVERLV AFKVPTVQLR VKSDNAQAVA EQVRRAAAAA HGSQTRLFIN DHWRVALDVH AQTPDSGLYG IHLGQEDIDD ADLAAIRAAG LRLGISTHGY AEMLRVAPLN PSYLALGAVF ATPTKTMPTV PQGLGRLFAY AAAMRTRVPA PPLVAIGGID LAAMPRVLES GVGCVAVVRA ITQAGDVPAA VQALQATFAA HVRA // ID D8P6H9_RALSL Unreviewed; 195 AA. AC D8P6H9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 13-NOV-2013, entry version 20. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase (ThiE); DE EC=2.5.1.3; GN ORFNames=RCFBP_mp30432; OS Ralstonia solanacearum CFBP2957. OG Plasmid RCFBPv3_mp. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=859656; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CFBP2957; PLASMID=RCFBPv3_mp; RA Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E., RA Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G., RA Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.; RT "Genomes of three tomato pathogens within the Ralstonia solanacearum RT species complex reveal significant evolutionary divergence."; RL BMC Genomics 11:379-379(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CFBP2957; PLASMID=RCFBPv3_mp; RA Genoscope - CEA; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP885907; CBJ54515.1; -; Genomic_DNA. DR RefSeq; YP_003748883.1; NC_014309.1. DR ProteinModelPortal; D8P6H9; -. DR GeneID; 9413888; -. DR PATRIC; 42552705; VBIRalSol166517_4857. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Plasmid; Transferase. SQ SEQUENCE 195 AA; 21265 MW; 280EABB7FAD1E79A CRC64; MSLPDFYQIT PEPVGSPHFE TFFAELTDTL GSGIRLLQLR AKQLGPREHL DVARRTRDLC RQSGAILMLN GPIDMAREVG CDGVHLGSDA LMSLRSRPVP DTVLLSAACH SAEQLEQAAR MAVDFVTLSP VLRTRTHPDA DPLGWERFTE LAQRARVPVF ALGGMHPDML DQAKRAGAWG VAAISATWCH RSAGA // ID D8PFZ3_9BACT Unreviewed; 204 AA. AC D8PFZ3; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NIDE2470; OS Candidatus Nitrospira defluvii. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira. OX NCBI_TaxID=330214; RN [1] RP NUCLEOTIDE SEQUENCE. RX DOI=10.1073/pnas.1003860107 ; RA Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B., RA Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.; RT "A Nitrospira metagenome illuminates the physiology and evolution of RT globally important nitrite-oxidizing bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RA Genoscope - CEA; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929003; CBK42180.1; -; Genomic_DNA. DR RefSeq; YP_003798105.1; NC_014355.1. DR ProteinModelPortal; D8PFZ3; -. DR EnsemblBacteria; CBK42180; CBK42180; NIDE2470. DR GeneID; 9485734; -. DR KEGG; nde:NIDE2470; -. DR PATRIC; 42243921; VBICanNit28252_2343. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; NDEF330214:GI4U-2426-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 125 127 THZ-P binding (By similarity). FT REGION 176 177 THZ-P binding (By similarity). FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 156 156 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21498 MW; 55328297AEE86D3A CRC64; MLDPTVRPDR PLPDLLREAA AHGVRLFQYR DKQATMREAY AKALALRQAA SDAGALLIVN DRCDLAMAVN ADGVHLGQDD LPIVYARQLL GPEKIIGLST HNATQVREAV TAQPDYVGFG PIFSTSTKAD HDPVVGLEGL RAARALTSLP MFAIGGITAE SLGEIMAAGA DGVAVISAIL KAPDLGAAIR AFQQHVPTPD SQAL // ID D8PHL8_9BACT Unreviewed; 208 AA. AC D8PHL8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; ORFNames=NIDE3059; OS Candidatus Nitrospira defluvii. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira. OX NCBI_TaxID=330214; RN [1] RP NUCLEOTIDE SEQUENCE. RX DOI=10.1073/pnas.1003860107 ; RA Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B., RA Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.; RT "A Nitrospira metagenome illuminates the physiology and evolution of RT globally important nitrite-oxidizing bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RA Genoscope - CEA; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929003; CBK42755.1; -; Genomic_DNA. DR RefSeq; YP_003798680.1; NC_014355.1. DR ProteinModelPortal; D8PHL8; -. DR EnsemblBacteria; CBK42755; CBK42755; NIDE3059. DR GeneID; 9486384; -. DR KEGG; nde:NIDE3059; -. DR PATRIC; 42245061; VBICanNit28252_2911. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; NDEF330214:GI4U-3003-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22428 MW; 7DBCD85E90F320E4 CRC64; MPSVDFRLYL VTDRHQTAGR PLVSVVGRAV NAGVRAVQLR ERDLPIRALL SLSLDLQREL PDMQLFINDR VDLAVGLGCR GVHLRESSLP APVVRTLLRP SQLLGLSVHS IQGAVAAERH GADFVVLGPI YDTPSKREYG APLGLQVLEQ AARAVTIPIF AIGGMTTSRT REMLQAGAFG VAVLSSILSA SNVEAETEKF LAAIERES // ID D8Q9F4_SCHCM Unreviewed; 530 AA. AC D8Q9F4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-APR-2014, entry version 20. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=SCHCODRAFT_68987; OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Agaricomycetidae; Agaricales; Schizophyllaceae; OC Schizophyllum. OX NCBI_TaxID=578458; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H4-8 / FGSC 9210; RX PubMed=20622885; DOI=10.1038/nbt.1643; RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., RA Stajich J.E., de Vries R.P., Record E., Levasseur A., Baker S.E., RA Bartholomew K.A., Coutinho P.M., Erdmann S., Fowler T.J., RA Gathman A.C., Lombard V., Henrissat B., Knabe N., Kuees U., RA Lilly W.W., Lindquist E., Lucas S., Magnuson J.K., Piumi F., RA Raudaskoski M., Salamov A., Schmutz J., Schwarze F.W.M.R., RA vanKuyk P.A., Horton J.S., Grigoriev I.V., Woesten H.A.B.; RT "Genome sequence of the model mushroom Schizophyllum commune."; RL Nat. Biotechnol. 28:957-963(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL377308; EFI95224.1; -; Genomic_DNA. DR RefSeq; XP_003030127.1; XM_003030081.1. DR ProteinModelPortal; D8Q9F4; -. DR GeneID; 9588325; -. DR KEGG; scm:SCHCODRAFT_68987; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 530 AA; 54065 MW; F20CF99519F35CF5 CRC64; MPIDYALYLV TGRDLLPPGQ PFAATLAAAL EHGVTLVQLR EKTADTGEFL AVARETKAIC DAHNVPLLIN DRADIALAVG AAGVHVGQDD MNARDVRKLL PAGAIVGVSC NSADDVRRAI ADGADYIGIG AVYGTATKNV KNPLLGPRAV GPLLALLDGT DVRAVAIGGI NAGNLARTLQ GSVSDSGHAL DGVAVVSDIM ASRDPAAASA KLAGIVKAFK EGRAASAPSA ALKVEDLLDG VVRVMKVVKE INPLVHQITN TVVTTQSANI TLAAGGSPIM ATAPEEMDDL AKVAGAVLIN IGTLREDVVR AMRVVGPAAN LSRTPLVFDP VGVGATDFRK RTVKELLDAF QISVLKGNAG ELAAVAGSNE VRAKGVDSAG PGFADPAWFV RGLARKEKTT TLLTGPVDYL SDGVRAVKIA NGHEILGRVT GSGCMLGSLV ATYCAAAAHV ADVDAGFDGE TSRAGSAADT VRGDMLVGAL AGVLVLSIAA EKAVARGDVY GPGTFLPALM DEVAGLTPGE VRARARVEVV // ID D8RPD6_SELML Unreviewed; 904 AA. AC D8RPD6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-APR-2014, entry version 17. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=SELMODRAFT_413416; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiophyta; Isoetopsida; Selaginellales; Selaginellaceae; OC Selaginella. OX NCBI_TaxID=88036; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551031; DOI=10.1126/science.1203810; RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., RA Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., RA Bonawitz N.D., Chapple C., Cheng C., Correa L.G., Dacre M., RA DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L., RA Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L., RA Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y., RA Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U., RA Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E., RA Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S., RA Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M., RA Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., RA Shinohara N., Shippen D.E., Sorensen I., Sotooka R., Sugimoto N., RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., RA Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., RA Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R., RA Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S., RA Rokhsar D., Grigoriev I.V.; RT "The Selaginella genome identifies genetic changes associated with the RT evolution of vascular plants."; RL Science 332:960-963(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL377585; EFJ26018.1; -; Genomic_DNA. DR RefSeq; XP_002972797.1; XM_002972751.1. DR EnsemblPlants; EFJ26018; EFJ26018; SELMODRAFT_413416. DR GeneID; 9637468; -. DR KEGG; smo:SELMODRAFT_413416; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 904 AA; 98044 MW; 7BB3734892B16B06 CRC64; MIRNSSAAHA VARIHAAPST SSQQICQIPL PSTAPLQIPA LLRNLSFSHS RSHKRAPGSC VLATNAAAAS AGVFPGGTRR ASVRLPGLGL RLKAEDILED GEEKKAVLDS AVAAGLNLVI LEDGKEDSLR FYDAARIVMS IVRGRADVLI VERVDIAAAA GSNGVVLSDQ GLPSVVARRM MQNAMPEAVV LPLVARRVTS YQSAEIATIT EGADFLLLQC EQASSASAKA LVEGICKRVK IPVFLEWARQ EEDAVKLLKV GAGGIILDSL PAAAEVSSFV TDLASKVASS VYTKSGKGLS LNGEGAKSSS TAAAAVLSSI EQQAKLLIEE ERPILTSAVE IIKEASPQME EVGLLVDAVK QLEELFLLVV VGEFNSGKSS VINALLGDRF LKQGVLPTTN EITLLKYSDE SYEERPARHP DGHLMRYLSA GLLKQMNLVD TPGTNVILQR QQRLTEEFVP RADLVLFVIG AERPLTESEA SSHTSFCISR FDVIRLLSGF FFTVEEVRRF VADNVRQLLN IEAAMIFPIS ARKALHAKVK AKQLESKNLE RDPLWTASGF DKLEQYVLDF LGGSSDAGAE RIRLKLETPI GIAAALLSAA RKQVEADAAN NEVDQKVLDE MEDQFTSYKQ LLGTNVDLQV QLVITAVAEA TARALKFVDK RLQVTSVDTA SKYLLPRNET SSAGAATFER EIIGTALSDV KNAIEDHKLW VTLNTQRQLE KYVEIGKSRW PDTEVVTDSW SENVSFSGRS LTALDEFDVK AANLLLEQEL REAVFSTFES LGIAGASASL LTSVLPTTLE DLIALGLCSA GGLVSIFKLS SLREEIKRKV EQVAQSLSLK LEEEMKAELQ ESIQSIESSV LQFTAPYRSL VEKESTRIAA VQEKLVVIDK ELQMLRKNIQ NLGS // ID D8SM44_SELML Unreviewed; 905 AA. AC D8SM44; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-APR-2014, entry version 16. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=SELMODRAFT_445893; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiophyta; Isoetopsida; Selaginellales; Selaginellaceae; OC Selaginella. OX NCBI_TaxID=88036; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551031; DOI=10.1126/science.1203810; RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., RA Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., RA Bonawitz N.D., Chapple C., Cheng C., Correa L.G., Dacre M., RA DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L., RA Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L., RA Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y., RA Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U., RA Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E., RA Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S., RA Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M., RA Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., RA Shinohara N., Shippen D.E., Sorensen I., Sotooka R., Sugimoto N., RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., RA Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., RA Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R., RA Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S., RA Rokhsar D., Grigoriev I.V.; RT "The Selaginella genome identifies genetic changes associated with the RT evolution of vascular plants."; RL Science 332:960-963(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL377627; EFJ14423.1; -; Genomic_DNA. DR RefSeq; XP_002984373.1; XM_002984327.1. DR UniGene; Smo.12207; -. DR EnsemblPlants; EFJ14423; EFJ14423; SELMODRAFT_445893. DR GeneID; 9644412; -. DR KEGG; smo:SELMODRAFT_445893; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 905 AA; 98168 MW; DDE2B2D690B0C868 CRC64; MIRDSSAAHA VARIHAAPST SSQQICQIPL PSTAPLQIPA LLRNLSFSHS RSHKRAPGSC VLATNAAAAS AGVFPGGTRR ASVRLPGLGL RLKAEDILED GEEKKAVLDS AVAAGLNLVI LEDGKEDSLR FYDAARIVMS IVRGRADVLI VERVDIAAAA GSNGVVLSDQ GLPSVVARRM MQNAMPEAVV LPLVARRVTS YQSAEIATIT EGADFLLLQC EQASSASAKA LVEGICKRVK IPVFLEWARQ EEDAVKLLKV GAGGIILDSL PAAAEVSSFV TDLASKVASS VYTKSGKGLS LNGEGAKSSS TAAAAVLSSI EQQAKLLIEE ERPILTSAVE IIKEASPQME EVGLLVDAVK QLEELFLLVV VGEFNSGKSS VINALLGDRF LKQGVLPTTN EITLLKYSDE SYEERPARHP DGHLMRYLSA GLLKQMNLVD TPGTNVILQR QQRLTEEFVP RADLVLFVIG AERPLTESEA SSHTSFPPIS RFDVIRLLSG FFSTVEEVRR FVADNVRQLL NIEAAMIFPI SARKALHAKV KAKQLESKNL ERDPLWTASG FDKLEQYVLD FLGGSSDAGA ERIRLKLETP IGIAAALLSA ARKQVEADAE NNEVDRKVLD EMEDQFTSYK QLLGTNVDLQ VQRVITAVAE ATARALKFVD KRLQVTSVDT ASKYLLPRNE TSSAGAATFE REIIGTALSD VKNAIEDHKL WVTLNTQRQL EKYVEIGKSR WPDTEVVTDS WSENVSFSGR SLTALDEFDV KAADLLLEQE LREAVFSTFG SLGIAGASAS FLTSVLPTTL EDLIALGLCS AGGLVSIFKL SSLREEIKRK VEQVAQSLSL KLEEEMKAEL QESIQSIESS VLQFTAPYRS LVEKESTRIA AVQEKLVVID KELQMLRKNI QNLGS // ID D8T631_SELML Unreviewed; 527 AA. AC D8T631; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-APR-2014, entry version 24. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=SELMODRAFT_132867; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiophyta; Isoetopsida; Selaginellales; Selaginellaceae; OC Selaginella. OX NCBI_TaxID=88036; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551031; DOI=10.1126/science.1203810; RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., RA Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., RA Bonawitz N.D., Chapple C., Cheng C., Correa L.G., Dacre M., RA DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L., RA Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L., RA Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y., RA Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U., RA Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E., RA Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S., RA Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M., RA Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., RA Shinohara N., Shippen D.E., Sorensen I., Sotooka R., Sugimoto N., RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., RA Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., RA Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R., RA Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S., RA Rokhsar D., Grigoriev I.V.; RT "The Selaginella genome identifies genetic changes associated with the RT evolution of vascular plants."; RL Science 332:960-963(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL377679; EFJ07905.1; -; Genomic_DNA. DR RefSeq; XP_002991097.1; XM_002991051.1. DR ProteinModelPortal; D8T631; -. DR EnsemblPlants; EFJ07905; EFJ07905; SELMODRAFT_132867. DR GeneID; 9634430; -. DR KEGG; smo:SELMODRAFT_132867; -. DR KO; K14153; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 527 AA; 55568 MW; FD207310880E956F CRC64; MLNLACSFRF KSVTAAAAFS TDSPVHVPCV LTIAGSDSGA GAGIQADIKA CAARGVYCCS AITSVTAQNT IGVQGISTLP AAFVEQQINS VLDDIHVDVV KTGMLASPEI IQSVCSRIKQ YSIGSLVVDP VMVSTSGHEL SGPSILDRLR KALLPLATIV TPNMLEASVL ADGKPVNTVL DMREVAAEIH RMGPRYVLVK GGHLKNSHDL VDVLYDGSEW HELRGSRIKT RSTHGTGCTL AASIAAELAK GLDVLPAVMA AKEYVAKALE HSSSIKIGGG AQGPMNHFFQ LADWGKLSSR QCRFDPRKLF LYAVTDSGMN KRWDRSTPAA VEQAIQGGAT IIQIREKEAE TLEFIKIAEA SLAIGRKYGV PVLINDRVDV AVACNADGVH LGQTDMPVRL ARSILGPGKI IGTSCKTVEQ AVKAYEDGAD YIGCGGVYPT TTKKKNKTIG LDGLRLLCEA SPLPVVAIGG ISAANVEEVM NSRPAMLHGV AVVSTLFDQS DVGQATRDLR ASMTAALSES TAGKVFS // ID D8T7X1_SELML Unreviewed; 527 AA. AC D8T7X1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-APR-2014, entry version 22. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=SELMODRAFT_133962; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiophyta; Isoetopsida; Selaginellales; Selaginellaceae; OC Selaginella. OX NCBI_TaxID=88036; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551031; DOI=10.1126/science.1203810; RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., RA Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., RA Bonawitz N.D., Chapple C., Cheng C., Correa L.G., Dacre M., RA DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L., RA Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L., RA Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y., RA Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U., RA Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E., RA Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S., RA Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M., RA Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., RA Shinohara N., Shippen D.E., Sorensen I., Sotooka R., Sugimoto N., RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., RA Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., RA Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R., RA Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S., RA Rokhsar D., Grigoriev I.V.; RT "The Selaginella genome identifies genetic changes associated with the RT evolution of vascular plants."; RL Science 332:960-963(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL377687; EFJ07229.1; -; Genomic_DNA. DR RefSeq; XP_002991658.1; XM_002991612.1. DR ProteinModelPortal; D8T7X1; -. DR EnsemblPlants; EFJ07229; EFJ07229; SELMODRAFT_133962. DR GeneID; 9632922; -. DR KEGG; smo:SELMODRAFT_133962; -. DR KO; K14153; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 527 AA; 55482 MW; FE5CAC1A067FF541 CRC64; MLNLACSFRF KSVTATAAFS TDSPAHVPCV LTIAGSDSGA GAGIQADIKA CAARGVYCCS AITSVTAQNT IGVQGISTLP AAFVEQQINS VLDDIHVDVV KTGMLASPEI IQSVCSRIKH YSIGSLVVDP VMVSTSGHEL SGPSILDRLR KALLPLATIV TPNMSEASVL ADGKPVNTVL DMREVAAEIH RMGPRYVLVK GGHLKNSHDL VDVLYDGSGW HELRGSRIKT RSTHGTGCTL AASIAAELAK GLDVLPAVMA AKEYVAKALE HSSSIKIGGG AQGPMNHFFQ LADWGKLSSR QCRFDPRKLF LYAVTDSGMN KRWDRSTPAA VEQAIQGGAT IIQIREKEAE TLEFIEIAEA SLAIGRKYGV PVLINDRVDV AVACNADGVH LGQTDMPVRL ARSILGPGKI IGTSCKTVEQ AVKAYEDGAD YIGCGGVYPT TTKKKNKTIG LDGLRLLCEA SPLPVVAIGG ISAANVEEVM NSRPAMLHGV AVVSTLFDQS DVGQATRDLR ASMTAALSES TAGKVFS // ID D8TH71_VOLCA Unreviewed; 963 AA. AC D8TH71; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-APR-2014, entry version 16. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=VOLCADRAFT_120148; OS Volvox carteri (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; OC Chlamydomonadales; Volvocaceae; Volvox. OX NCBI_TaxID=3067; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=f. Nagariensis / Eve; RX PubMed=20616280; DOI=10.1126/science.1188800; RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., RA Nishii I., Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., RA Hellsten U., Chapman J., Simakov O., Rensing S.A., Terry A., RA Pangilinan J., Kapitonov V., Jurka J., Salamov A., Shapiro H., RA Schmutz J., Grimwood J., Lindquist E., Lucas S., Grigoriev I.V., RA Schmitt R., Kirk D., Rokhsar D.S.; RT "Genomic analysis of organismal complexity in the multicellular green RT alga Volvox carteri."; RL Science 329:223-226(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL378323; EFJ53019.1; -; Genomic_DNA. DR RefSeq; XP_002946024.1; XM_002945978.1. DR UniGene; Vca.11954; -. DR ProteinModelPortal; D8TH71; -. DR GeneID; 9625542; -. DR KEGG; vcn:VOLCADRAFT_120148; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 963 AA; 100578 MW; BD9B071D0171D529 CRC64; MQQARVQLPA VALQVEASKV LSDAALPDAM SQALQGGCNM IVLWDSNANA ASMYDAALRI QDLLRGRAAL LLVDRTDIAL AVGAQGVLLT NQALVGRVVS DEGAAITAAA DGANLVLVTV GSNVHGPGGG APPSAAVLEA SKSGQRSGNA IPLLMSVRAT GAGSGVEEAL EADIDGVAVS PEALPEVARC CFDLPETSSI IDYTTAILTR LNVKAATAGT AKRPKQQKQQ QQAEDQAAAA EPATAQSRQA HASTAAAAAA APAVVAPPPR QPVPAISPAA PSAPRSPSSP APLSSRPLRR LLDPERETLL LDEKATLAEA LSFLEETLPG VSELSLLRDA LKALDEPFLV AVVGEFNSGK SSVINALLGR RYLAEGILPT TNEISILKYS ATAGATAATA QLEQQADGLY VRYLPAKLLQ DLSIVDTPGT NVILERQQRL TEEYVPRADL VLFVMSADRP FSESEVRFLE YIRQWQKKVV FVVNKADILD SVDEVEAVKE FVARNAQRIL RLDRPTVIAV SSRAALRAKL AAAGLSFTSS LDADGPFSSA AGEAASLEAE SLDAALPSSP DWRSSNFAEL ERQVSNFLVG RGAGGGEGVR LKLQTPLFVA DALLGAAGRQ LAVDLAAARA ELEGLQLVSK QLTKFRSEME KDATAQRAAL QQVLSGVLSR AERFVDQTVQ LSNAPLLVSI AAGNKEYPFR AAFEKEVIGN GFDSLRAAVS EHSSWLRANC DAQREYYASF AAARGEAAGV VTIAPSAASS NGTAAAAAAG VAADRTHSNA EASTFTSTPL AVSATAITAA SSGPSASSPA LLAVSEFNVR AISTLLDTEL QQAMATTVGT AAGAPLFGLF AMQLIPNTLE DILLAGLSGA VSYVSLLNLP LRRADLKGKI SRVASNFVSD VQSKMEVEVA DEVAGVMRAV AKLMEPLEQA YGTEVARLEA RQADLARLAD GLKDLQRRVA NLE // ID D8TQN2_VOLCA Unreviewed; 1251 AA. AC D8TQN2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-APR-2014, entry version 21. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=VOLCADRAFT_89047; OS Volvox carteri (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; OC Chlamydomonadales; Volvocaceae; Volvox. OX NCBI_TaxID=3067; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=f. Nagariensis / Eve; RX PubMed=20616280; DOI=10.1126/science.1188800; RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., RA Nishii I., Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., RA Hellsten U., Chapman J., Simakov O., Rensing S.A., Terry A., RA Pangilinan J., Kapitonov V., Jurka J., Salamov A., Shapiro H., RA Schmutz J., Grimwood J., Lindquist E., Lucas S., Grigoriev I.V., RA Schmitt R., Kirk D., Rokhsar D.S.; RT "Genomic analysis of organismal complexity in the multicellular green RT alga Volvox carteri."; RL Science 329:223-226(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL378332; EFJ50063.1; -; Genomic_DNA. DR RefSeq; XP_002948683.1; XM_002948637.1. DR ProteinModelPortal; D8TQN2; -. DR GeneID; 9623508; -. DR KEGG; vcn:VOLCADRAFT_89047; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.910.10; -; 2. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF03070; TENA_THI-4; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; SSF48613; 2. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 1251 AA; 128131 MW; 881674BC1B992BBD CRC64; MPSGLPATNG LSMELWQSVQ KEVYMSLHDP FVQGLAQGTL DRRAFQHYIA QDAYFLKYFA RAYGIALSKA LALDDDTFAV LGRLLRGVHE ELQLHGVYAA RWGVHLPHHT HTHTHEHTKT RTEVQVPGAP SPETSFPAYE CIGNGGGGCD GGDGGEGVVV FDGPSAATKA YTDFLMEVAE DGGQDGGVVE ILAAMLPCSR LYGFLGCALK AAHAGAGGGG GGGAGGGGGG GAPSQGEYWE WVRTYSSPEY LAIPALKEAV FDRLAVHADR AKLLSLYRRA MQLEAEFFAA QPFSPPRRRI AALVIDFDET CTAKDTVGGL MRLAEAAAAQ GRPTPGDTSW ARTTLGDLAA NYLARQGELL REILPEEHPD AESYDAEGLS SFLERLSDFD ERMNLVVEES GILKGSTEAE VAAAGTTVVL RPECRETLRA ALDRGIPVEV VSVNWSDVFV GTALGAPLAP TACRTEEVAN AQEGAQHQHQ QQAAAALRDT APPGRSPSSA SASAASGVRL RCNSLQIGPD GFTSGALVKR VQTARDKRRE LRAVMKERAK RSGTAAAGPP PAAAAAVAGG AADNSGSAGG GHSDGGDGDG GGDGLIVYVG DSTSDLGAML EADVGVVVGA NRLLRRVAAR FGVRLRPLAA VPLAARGGSY CGSSGGGGGG VLYEAAGWEE IRAFLFGVES EAAAEGARGG ASVGPSEGQV VAEEEGKKET AAAAAAVIKG SSTEAPAAAA ATQSLPRVLS IAGSDSGGGA GIQADVKAML ARGVFAMTAL TALTAQNTHG VSAVHAVPPE FLRQQIDAVL SGNMRMGADL GADAIKTGML PNAEAVHVVA ERLPLVVDPV LVSTSGHSLA EGGVAAALLR DLLPLATLAT PNIPEAEALL GAGSIQTVDD MRRAARELQL RTGCSAVLVK GGHLKPVCGA AAEAPAEVVD VLYDGEQIHE LRAAWVRTEN THGTGCTLAS AIAAELAKGL PLLAAVTAAR TALHEALRAS AALSLGGGVQ RPFHHLHLMT PGPLTVPAAS AASVSSSLRR VDLTTLRRQL RLYGVTDPYC NKKCNRTLLE AVTLAVRGGA TIIQLREKDT DGGDFAREAA AALKVCRQYG VPLIINDRVD VALAVGADGV HVGQSDLPTA VVRALIGPSR ILGVSVKTPQ QARDAAAAGA DYLGAGAVLP TGTKDTDVIG LEGLGAVCAA AAPLPVVSIG GVSAGNAADT IRVGCAGIAV VSAIFGAEDA EGAARALLKV VDDALVTRDA D // ID D8USC1_9MICC Unreviewed; 219 AA. AC D8USC1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0734_01529; OS Rothia dentocariosa M567. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Rothia. OX NCBI_TaxID=563032; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M567; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., RA White J., Yandava C., Sibley C.D., Field T.R., Grinwis M., RA Eshaghurshan C.S., Surette M.G., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Rothia dentocariosa strain M567."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL379575; EFJ76649.1; -; Genomic_DNA. DR ProteinModelPortal; D8USC1; -. DR EnsemblBacteria; EFJ76649; EFJ76649; HMPREF0734_01529. DR PATRIC; 40965442; VBIRotDen115472_1571. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 157 159 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 110 110 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 160 160 HMP-PP (By similarity). SQ SEQUENCE 219 AA; 23542 MW; D8C41C8CDDACC92E CRC64; MSTQETLLSQ SNRGPMTTSN TAGTATPLDL SLYLVTGENP VETVRRARHA TCIQVRSKPI SARNLYALAE EIARIALPHQ KILIDDRVDV ALALRARGVR IDGVHIGQDD LPVADARRLL GEHAIIGLTT GTRELVERAN AVAHLIDYIG AGPFRPSPTK ASNRPPLGIE GLRELAELSE VPVVAIGDIW PQDCPSIRET GVAGVAMARA FVENPELQA // ID D9N9B8_STREE Unreviewed; 210 AA. AC D9N9B8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpBS458_01489; OS Streptococcus pneumoniae BS458. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=512769; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BS458; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWA01000027; EFL71602.1; -; Genomic_DNA. DR ProteinModelPortal; D9N9B8; -. DR EnsemblBacteria; EFL71602; EFL71602; CGSSpBS458_01489. DR PATRIC; 40904802; VBIStrPne101635_1466. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID D9N9C5_STREE Unreviewed; 209 AA. AC D9N9C5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpBS458_01524; OS Streptococcus pneumoniae BS458. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=512769; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BS458; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWA01000027; EFL71609.1; -; Genomic_DNA. DR EnsemblBacteria; EFL71609; EFL71609; CGSSpBS458_01524. DR PATRIC; 40904816; VBIStrPne101635_1473. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23362 MW; A51A41EFBB2CC783 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID D9NFZ4_STREE Unreviewed; 209 AA. AC D9NFZ4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpBS457_10814; OS Streptococcus pneumoniae BS457. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=512768; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BS457; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWB01000025; EFL73790.1; -; Genomic_DNA. DR EnsemblBacteria; EFL73790; EFL73790; CGSSpBS457_10814. DR PATRIC; 40909669; VBIStrPne54866_1535. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23362 MW; A51A41EFBB2CC783 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID D9NG01_STREE Unreviewed; 210 AA. AC D9NG01; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpBS457_10849; OS Streptococcus pneumoniae BS457. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=512768; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BS457; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWB01000025; EFL73797.1; -; Genomic_DNA. DR ProteinModelPortal; D9NG01; -. DR EnsemblBacteria; EFL73797; EFL73797; CGSSpBS457_10849. DR PATRIC; 40909683; VBIStrPne54866_1542. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID D9NKP0_STREE Unreviewed; 209 AA. AC D9NKP0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpBS397_05602; OS Streptococcus pneumoniae BS397. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=512767; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BS397; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWC01000003; EFL76684.1; -; Genomic_DNA. DR EnsemblBacteria; EFL76684; EFL76684; CGSSpBS397_05602. DR PATRIC; 40913132; VBIStrPne5623_0940. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23362 MW; A51A41EFBB2CC783 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID D9NKP7_STREE Unreviewed; 210 AA. AC D9NKP7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpBS397_05637; OS Streptococcus pneumoniae BS397. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=512767; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BS397; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWC01000003; EFL76691.1; -; Genomic_DNA. DR ProteinModelPortal; D9NKP7; -. DR EnsemblBacteria; EFL76691; EFL76691; CGSSpBS397_05637. DR PATRIC; 40913146; VBIStrPne5623_0947. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID D9NRF7_STREE Unreviewed; 209 AA. AC D9NRF7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp14BS292_08625; OS Streptococcus pneumoniae SP14-BS292. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=497962; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP14-BS292; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWQ01000002; EFL68007.1; -; Genomic_DNA. DR EnsemblBacteria; EFL68007; EFL68007; CGSSp14BS292_08625. DR PATRIC; 40917175; VBIStrPne94055_0590. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23362 MW; A51A41EFBB2CC783 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID D9NRG4_STREE Unreviewed; 210 AA. AC D9NRG4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp14BS292_08660; OS Streptococcus pneumoniae SP14-BS292. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=497962; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP14-BS292; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWQ01000002; EFL68014.1; -; Genomic_DNA. DR ProteinModelPortal; D9NRG4; -. DR EnsemblBacteria; EFL68014; EFL68014; CGSSp14BS292_08660. DR PATRIC; 40917189; VBIStrPne94055_0597. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID D9P086_STREE Unreviewed; 209 AA. AC D9P086; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpBS293_04253; OS Streptococcus pneumoniae SP-BS293. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=497963; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP-BS293; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWU01000007; EFL69360.1; -; Genomic_DNA. DR EnsemblBacteria; EFL69360; EFL69360; CGSSpBS293_04253. DR PATRIC; 40923872; VBIStrPne26129_1502. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23362 MW; A51A41EFBB2CC783 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID D9P093_STREE Unreviewed; 210 AA. AC D9P093; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpBS293_04288; OS Streptococcus pneumoniae SP-BS293. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=497963; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP-BS293; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWU01000007; EFL69367.1; -; Genomic_DNA. DR ProteinModelPortal; D9P093; -. DR EnsemblBacteria; EFL69367; EFL69367; CGSSpBS293_04288. DR PATRIC; 40923886; VBIStrPne26129_1509. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID D9P3Z2_ACTPL Unreviewed; 164 AA. AC D9P3Z2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=APP2_1146; OS Actinobacillus pleuropneumoniae serovar 2 str. 4226. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754254; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4226; RX PubMed=20802047; DOI=10.1128/JB.00867-10; RA Zhan B., Angen O., Hedegaard J., Bendixen C., Panitz F.; RT "Draft genome sequences of Actinobacillus pleuropneumoniae serotypes 2 RT and 6."; RL J. Bacteriol. 192:5846-5847(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXN01000004; EFL79143.1; -; Genomic_DNA. DR EnsemblBacteria; EFL79143; EFL79143; APP2_1146. DR PATRIC; 41121132; VBIActPle155200_0508. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 164 AA; 18587 MW; B5C3AB1868D18CA2 CRC64; MYDIRQMLQL YFIAGTQDCP NPTEDRSQNL LLILEQALQA GITCFQFRDK SKNSLEDQPN AQKALAIQCR DLCRLYNVPF IVDDNVALAI EIDADGVHVG QKDMSPIMIR QMTDKLLIIG LSNNTLEDLW RSEQMIEVDY CGLGPVFPTN SKEKHNPPIG LDFV // ID D9PEI1_ACTPL Unreviewed; 133 AA. AC D9PEI1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=APP6_0790; OS Actinobacillus pleuropneumoniae serovar 6 str. Femo. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754256; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Femo; RX PubMed=20802047; DOI=10.1128/JB.00867-10; RA Zhan B., Angen O., Hedegaard J., Bendixen C., Panitz F.; RT "Draft genome sequences of Actinobacillus pleuropneumoniae serotypes 2 RT and 6."; RL J. Bacteriol. 192:5846-5847(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXO01000035; EFL79767.1; -; Genomic_DNA. DR EnsemblBacteria; EFL79767; EFL79767; APP6_0790. DR PATRIC; 40901619; VBIActPle158270_2167. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 133 AA; 14314 MW; 04C6D7250D7B4710 CRC64; MALAIEIDAD GVHVGQKDMS PIMIRQMTDK PLIIGLSNNT LEDLWRSEQM IEVDYCGLGP VFPTNSKEKH NPPIGLDFVK KAREAGIRKP IVSIGGVKAE HVATLKQNGA DGVAVITAIS LASDVSQAVK RLL // ID D9PHJ2_9ZZZZ Unreviewed; 192 AA. AC D9PHJ2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Protein containing Thiamine monophosphate synthase domain; DE EC=2.5.1.3; GN ORFNames=LDC_0992; OS sediment metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=749907; RN [1] RP NUCLEOTIDE SEQUENCE. RG CONSOLIDER consortium CSD2007-00005; RA Guazzaroni M.-E., Richter M., Garcia-Salamanca A., Yarza P., RA Ferrer M.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RX PubMed=21735153; DOI=10.1007/s00248-011-9903-y; RA Ferrer M., Guazzaroni M.E., Richter M., Garcia-Salamanca A., Yarza P., RA Suarez-Suarez A., Solano J., Alcaide M., van Dillewijn P., RA Molina-Henares M.A., Lopez-Cortes N., Al-Ramahi Y., Guerrero C., RA Acosta A., de Eugenio L.I., Martinez V., Marques S., Rojo F., RA Santero E., Genilloud O., Perez-Perez J., Rossello-Mora R., RA Ramos J.L.; RT "Taxonomic and Functional Metagenomic Profiling of the Microbial RT Community in the Anoxic Sediment of a Sub-saline Shallow Lake (Laguna RT de Carrizo, Central Spain)."; RL Microb. Ecol. 0:0-0(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZX01000372; EFK96992.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 192 AA; 21431 MW; 350BD6B279840576 CRC64; MKSYAISDKT NLDFNNLEAS IKRIASKASM ILYRDKNNPN YEENSKLFLQ TAKKYPFEKI LLHSDYDLAL KLKADGIHLT STQIDDIPLA KEKGLFVIVS THTLNEASKA QKLGADMITL SPIYDSPNKG KPIGLDTLKD ITSTLNIPVI ALGGILTGEQ IQECKNAGAN WFASIRYFYK KIFFCFLGIC SI // ID D9PQ77_FINMA Unreviewed; 212 AA. AC D9PQ77; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9261_1779; OS Finegoldia magna ACS-171-V-Col3. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Finegoldia. OX NCBI_TaxID=768713; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-171-V-Col3; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Nelson K.E.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECM01000010; EFK94284.1; -; Genomic_DNA. DR ProteinModelPortal; D9PQ77; -. DR EnsemblBacteria; EFK94284; EFK94284; HMPREF9261_1779. DR PATRIC; 41152644; VBIFinMag162455_0544. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23461 MW; 67152E1CA9AE7BC1 CRC64; MNKQFNLGLN LVTNKQTLKG RDLTETIEIA LKNGADSVRL REKNMDTRSI MQEAFKIKEI TQRMGKLLIV NDRVDIAKAC DVDGVHLGQK DMPIKYAREM LGDDKIIGIS CHTLEQALEA QEAGADYIGV GAIFPTFTGD DFVRVTIDTL KEISEKIHVP ITAIGGINKN NIRMIFDSNV DSVSLTSAVF STGDVAASTQ ELKQKFDMIL KK // ID D9PTG8_FINMA Unreviewed; 214 AA. AC D9PTG8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9261_0210; OS Finegoldia magna ACS-171-V-Col3. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Finegoldia. OX NCBI_TaxID=768713; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-171-V-Col3; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Nelson K.E.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECM01000030; EFK93133.1; -; Genomic_DNA. DR ProteinModelPortal; D9PTG8; -. DR EnsemblBacteria; EFK93133; EFK93133; HMPREF9261_0210. DR PATRIC; 41155021; VBIFinMag162455_1691. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23786 MW; 8D168C04091C419D CRC64; MRKKLNLSLY LVTDRTNVAC EEEFLTKIEE SLKGGVTLVQ LREKNISTRE YIDLAKKVKI ICDKFEVPLL IDDRIDVCLA SNCAGVHLGD EDMEIKDARR ILGDNYIIGA TAKSVERAVQ CEKEGADYLG VGAIYPTKTH VKTKITSVDT LRDINNSINI KTVAIGGLNE DNMDVLKNSG ASGIAVVRAL MNDDNPQEKA HRLLEKSKQI LELR // ID D9QGC6_BRESC Unreviewed; 212 AA. AC D9QGC6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Bresu_1430; OS Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 OS / NBRC 16000 / CB 81) (Caulobacter subvibrioides). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=633149; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002102; ADL00742.1; -; Genomic_DNA. DR RefSeq; YP_003818365.1; NC_014375.1. DR ProteinModelPortal; D9QGC6; -. DR EnsemblBacteria; ADL00742; ADL00742; Bresu_1430. DR GeneID; 9503287; -. DR KEGG; bsb:Bresu_1430; -. DR PATRIC; 42202021; VBIBreSub37974_1441. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR BioCyc; BSUB633149:GHJJ-1444-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22220 MW; CE64210B09E68FB6 CRC64; MIPPRCQLYL ITPPVIDDLD VFAGRLERAL DAGPVAALQI RLKPADEATI TAAVQRLAPL AQRRDVAVIL NDRPDLAAAL GCDGVHVGQS DASVASARRI MGKSAMIGAT CHDSRHLAME AAEAGADYVA FGAFFPTTTK TTEHRPDPEI LTIWQEVMEI PSVAIGGITV ENAATLVTAG ADFLAVSAGV WGYAEGEAAA VRRFAAIMAT GD // ID D9QJU2_BRESC Unreviewed; 216 AA. AC D9QJU2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bresu_0379; OS Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 OS / NBRC 16000 / CB 81) (Caulobacter subvibrioides). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=633149; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002102; ADK99693.1; -; Genomic_DNA. DR RefSeq; YP_003817317.1; NC_014375.1. DR ProteinModelPortal; D9QJU2; -. DR EnsemblBacteria; ADK99693; ADK99693; Bresu_0379. DR GeneID; 9502224; -. DR KEGG; bsb:Bresu_0379; -. DR PATRIC; 42199884; VBIBreSub37974_0383. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ACHSERA; -. DR BioCyc; BSUB633149:GHJJ-381-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 216 AA; 21847 MW; EA9A5CAAEF627067 CRC64; MSEPVMMGEA AARLWANAQA LARAAAAVRG GAPSRVPPLL FFTDPVRTPR PWETAARMPQ GSGIVYRAFG AADARDTADR LRAITAARGI SLLIGMDGAL AEAVGADGLH LPERALSAAY ALSGRRPDWI LTGAVHSVEA ARTARDLDAV VLSPIYPAGG ASSARAALGL EALSQAARVR TVIALGGVTA GNVAELLDTG AAGVAAVSGI ADAFAD // ID D9QRD8_ACEAZ Unreviewed; 211 AA. AC D9QRD8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Acear_1573; OS Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halobacteroidaceae; OC Acetohalobium. OX NCBI_TaxID=574087; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49924 / DSM 5501 / Z-7288; RX DOI=10.4056/sigs.1062906; RA Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A., RA Glavina Del Rio T., Nolan M., Tice H., Cheng J., Han C., Brambilla E., RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., RA Pati A., Bruce D., Detter C., Tapia R., Goodwin L., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Rohde M., RA Goker M., Spring S., Woyke T., Bristow J., Eisen J., Markowitz V., RA Hugenholtz P., Kyrpides N., Klenk H.; RT "Complete genome sequence of Acetohalobium arabaticum type strain (Z- RT 7288)."; RL Stand. Genomic Sci. 3:57-65(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002105; ADL13079.1; -; Genomic_DNA. DR RefSeq; YP_003828144.1; NC_014378.1. DR ProteinModelPortal; D9QRD8; -. DR EnsemblBacteria; ADL13079; ADL13079; Acear_1573. DR GeneID; 9513630; -. DR KEGG; aar:Acear_1573; -. DR PATRIC; 42137397; VBIAceAra30843_1609. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; AARA574087:GHPK-1655-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23751 MW; 2DA59994A15D0DF7 CRC64; MVKNVLDTDL YCLTAEEYSL GRSNIEVVDK MLRADIEIIQ YRAKKKKMLY KYKECLKLRK MTKQAGVKFI INDDVDLALA VDADGIHIGQ EDLPIEEVRN LVGQDKIIGL STHSPQQARE AQNRGADYIG VGPIFKTNTK EDVCNPVGLE YLDYVVENID LPFVAIGGIK EHNMDIVKAR GAKCISMVTE IVGAENIINK IKNIREKINQ K // ID D9QT37_ACEAZ Unreviewed; 213 AA. AC D9QT37; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Acear_2047; OS Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halobacteroidaceae; OC Acetohalobium. OX NCBI_TaxID=574087; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49924 / DSM 5501 / Z-7288; RX DOI=10.4056/sigs.1062906; RA Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A., RA Glavina Del Rio T., Nolan M., Tice H., Cheng J., Han C., Brambilla E., RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., RA Pati A., Bruce D., Detter C., Tapia R., Goodwin L., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Rohde M., RA Goker M., Spring S., Woyke T., Bristow J., Eisen J., Markowitz V., RA Hugenholtz P., Kyrpides N., Klenk H.; RT "Complete genome sequence of Acetohalobium arabaticum type strain (Z- RT 7288)."; RL Stand. Genomic Sci. 3:57-65(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002105; ADL13537.1; -; Genomic_DNA. DR RefSeq; YP_003828602.1; NC_014378.1. DR ProteinModelPortal; D9QT37; -. DR EnsemblBacteria; ADL13537; ADL13537; Acear_2047. DR GeneID; 9514106; -. DR KEGG; aar:Acear_2047; -. DR PATRIC; 42138349; VBIAceAra30843_2085. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; AARA574087:GHPK-2131-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22766 MW; 72B0176544A7BED4 CRC64; MEDWDLYLVT EEELSSGRCT LEVVKAAING GVDLIQLRDK GKDLAYRYEL GLKIRELTAE AGVDLIINNR VDLALALEAD GVHLGQDDLP LKAAQKLLPE DKIIGISAST VEEALQAEAG GADYLGVGSI FATDSKDLKN DRSAVGLNRL AEIKSKVDIP VAAIGGLNQD NISEVIAAGA DVISVISAVT QAEDIEWKTE ELKGIIKEAK KGR // ID D9RAV6_CLOSW Unreviewed; 213 AA. AC D9RAV6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Closa_3630; OS Clostridium saccharolyticum (strain ATCC 35040 / DSM 2544 / NRCC 2533 OS / WM1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=610130; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35040 / DSM 2544 / NRCC 2533 / WM1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., Mouttaki H., Lin L., Zhou J., Hemme C.L., Woyke T.; RT "Complete sequence of Clostridium saccharolyticum WM1."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002109; ADL06153.1; -; Genomic_DNA. DR RefSeq; YP_003823776.1; NC_014376.1. DR ProteinModelPortal; D9RAV6; -. DR EnsemblBacteria; ADL06153; ADL06153; Closa_3630. DR GeneID; 9508948; -. DR KEGG; csh:Closa_3630; -. DR PATRIC; 42269123; VBICloSac91065_3918. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; CSAC610130:GHTP-3710-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22789 MW; 6099BF8C1DE44AEF CRC64; MKFHKDMLLL YAVTDQAYTG EKTLAAQIEE ALSAGVTLLQ LREKHMDKNA FLEEALMVRQ ITRRYGIPLI INDDVETALK CDADGVHVGQ DDLPPAEVRR LIGPDRILGV TAKNIDQAKK AWSDGADYIG AGAIFPSSTK KEAIPLSLEQ LSGICRSVPI PVTAIGGITA ENVSILKGTG AAGAAVVSGI FGQKNITEAV HCLKEQLLKV VSL // ID D9RBQ2_STAAJ Unreviewed; 213 AA. AC D9RBQ2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SAA6159_02005; OS Staphylococcus aureus (strain JKD6159). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=869816; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JKD6159; RX PubMed=20729356; DOI=10.1128/JB.00878-10; RA Chua K., Seemann T., Harrison P.F., Davies J.K., Coutts S.J., Chen H., RA Haring V., Moore R., Howden B.P., Stinear T.P.; RT "Complete genome sequence of Staphylococcus aureus strain JKD6159, a RT unique Australian clone of ST93-IV community methicillin-resistant RT Staphylococcus aureus."; RL J. Bacteriol. 192:5556-5557(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002114; ADL23930.1; -; Genomic_DNA. DR RefSeq; YP_005740140.1; NC_017338.1. DR ProteinModelPortal; D9RBQ2; -. DR EnsemblBacteria; ADL23930; ADL23930; SAA6159_02005. DR GeneID; 12326745; -. DR KEGG; suj:SAA6159_02005; -. DR PATRIC; 43205634; VBIStaAur164993_2101. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SAUR869816:GLKN-2049-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23372 MW; 11B047A587F3FC42 CRC64; MFNQSYLNVY FICGISDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D9RNY2_STAAK Unreviewed; 213 AA. AC D9RNY2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SAA6008_02129; OS Staphylococcus aureus (strain JKD6008). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=546342; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JKD6008; RX PubMed=20802046; DOI=10.1128/JB.00951-10; RA Howden B.P., Seemann T., Harrison P.F., McEvoy C.R., Stanton J.A., RA Rand C.J., Mason C.W., Jensen S.O., Firth N., Davies J.K., RA Johnson P.D., Stinear T.P.; RT "Complete genome sequence of Staphylococcus aureus strain JKD6008, an RT ST239 clone of methicillin-resistant Staphylococcus aureus with RT intermediate-level vancomycin resistance."; RL J. Bacteriol. 192:5848-5849(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002120; ADL66149.1; -; Genomic_DNA. DR RefSeq; YP_005745463.1; NC_017341.1. DR ProteinModelPortal; D9RNY2; -. DR SMR; D9RNY2; 4-209. DR PRIDE; D9RNY2; -. DR EnsemblBacteria; ADL66149; ADL66149; SAA6008_02129. DR GeneID; 12331457; -. DR KEGG; suk:SAA6008_02129; -. DR PATRIC; 43211555; VBIStaAur110820_2238. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SAUR546342:GLKM-2171-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID D9RRX5_PREMB Unreviewed; 211 AA. AC D9RRX5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HMPREF0659_A5798; OS Prevotella melaninogenica (strain ATCC 25845 / DSM 7089 / JCM 6325 / OS VPI 2381 / B282) (Bacteroides melaninogenicus). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=553174; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25845 / DSM 7089 / JCM 6325 / VPI 2381 / B282; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RT "Genome sequence of Prevotella melaninogenica strain ATCC 25845."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002122; ADK96036.1; -; Genomic_DNA. DR RefSeq; YP_003813877.1; NC_014370.1. DR ProteinModelPortal; D9RRX5; -. DR EnsemblBacteria; ADK96036; ADK96036; HMPREF0659_A5798. DR GeneID; 9496645; -. DR KEGG; pmz:HMPREF0659_A5798; -. DR PATRIC; 42431347; VBIPreMel47739_0781. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMEL553174:GH7V-793-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 30 34 HMP-PP binding (By similarity). FT REGION 127 129 THZ-P binding (By similarity). FT METAL 63 63 Magnesium (By similarity). FT METAL 82 82 Magnesium (By similarity). FT BINDING 62 62 HMP-PP (By similarity). FT BINDING 101 101 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23387 MW; FD6A284A292EEA23 CRC64; MIQFITHTNE RYDYIDGVRM ALEGGCRWIQ LRMKDASEEE VLKTAKSTRK LCRQYDAVLI LDDYVELVER TGADGVHLGK NDMPIDKARR LIGKDKIIGG TANTFEDIKR IYSAGADYIG CGPFRFTTTK KKLSPILGLD GYSRIIEQMT AYGINIPVIA IGGILLQDVS DIMQTGVSGV AVSGAILNAN NGYDPVTTMK RFINELKSNN K // ID D9RRX8_PREMB Unreviewed; 195 AA. AC D9RRX8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 13-NOV-2013, entry version 21. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN OrderedLocusNames=HMPREF0659_A5801; OS Prevotella melaninogenica (strain ATCC 25845 / DSM 7089 / JCM 6325 / OS VPI 2381 / B282) (Bacteroides melaninogenicus). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=553174; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25845 / DSM 7089 / JCM 6325 / VPI 2381 / B282; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RT "Genome sequence of Prevotella melaninogenica strain ATCC 25845."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002122; ADK96376.1; -; Genomic_DNA. DR RefSeq; YP_003813880.1; NC_014370.1. DR ProteinModelPortal; D9RRX8; -. DR EnsemblBacteria; ADK96376; ADK96376; HMPREF0659_A5801. DR GeneID; 9496264; -. DR KEGG; pmz:HMPREF0659_A5801; -. DR PATRIC; 42431353; VBIPreMel47739_0784. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR OrthoDB; EOG679THR; -. DR BioCyc; PMEL553174:GH7V-796-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 195 AA; 22171 MW; CE449C6A842BC1BA CRC64; MKWIIITSPE FLSGEATFIS KLFSQGLDLL HLRKPEASLE AYKQLLLQIP EQWHSRIVLH EHFELAEEYK LHGIHLNRLC SVAPKAYHGS ISCSCHTIEE VITQKDSKDY VFLSPIFDSI SKVGYHAAFS PTSLKQAAME NIIDEKVIAL GGITANNIFL VKEWHFGGVA LLGDIWKRMS DPQVDEYLNH IRTLL // ID D9RYY9_THEOJ Unreviewed; 212 AA. AC D9RYY9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Toce_0020; OS Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 / OS JW/IW-1228P). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Thermosediminibacter. OX NCBI_TaxID=555079; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P; RX PubMed=21304740; RA Pitluck S., Yasawong M., Munk C., Nolan M., Lapidus A., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., RA Tapia R., Han C., Goodwin L., Liolios K., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Thermosediminibacter oceani type strain RT (JW/IW-1228P)."; RL Stand. Genomic Sci. 3:108-116(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002131; ADL06817.1; -; Genomic_DNA. DR RefSeq; YP_003824440.1; NC_014377.1. DR ProteinModelPortal; D9RYY9; -. DR EnsemblBacteria; ADL06817; ADL06817; Toce_0020. DR GeneID; 9509647; -. DR KEGG; toc:Toce_0020; -. DR PATRIC; 42455003; VBITheOce34679_0021. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; TOCE555079:GHIS-20-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22795 MW; 1E6F04A3FC065C28 CRC64; MKPDFTLYAV TERSYLHGRD LVEAVEEAIR AGITVLQLRE KDAPGREFYE LALRLRELTR VYGIPFIIND RVDIALAVDA DGVHVGQEDI PADVARKIIG PGKILGVSAK TVEEAIRAEK DGADYLGVGA IFPSPTKPSS EAIGLEGLIK IKNAVKIPVV AIGGITVQNA NEVMATGVDG ICCISAVFCG DITENVRALR RAISQSFFIG DF // ID D9SIE0_GALCS Unreviewed; 210 AA. AC D9SIE0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Galf_0152; OS Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea OS capsiferriformans (strain ES-2)). OC Bacteria; Proteobacteria; Betaproteobacteria; Gallionellales; OC Gallionellaceae; Gallionella. OX NCBI_TaxID=395494; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ES-2; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C., RA Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., RA Ivanova N., Mikhailova N., Shelobolina E.S., Picardal F., Roden E., RA Emerson D., Woyke T.; RT "Complete sequence of Gallionella capsiferriformans ES-2."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002159; ADL54197.1; -; Genomic_DNA. DR RefSeq; YP_003845961.1; NC_014394.1. DR ProteinModelPortal; D9SIE0; -. DR EnsemblBacteria; ADL54197; ADL54197; Galf_0152. DR GeneID; 9611462; -. DR KEGG; gca:Galf_0152; -. DR PATRIC; 42336853; VBIGalCap53152_0158. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; GCAP395494:GHXI-152-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 21875 MW; 891148205E513314 CRC64; MKAKISGLYA ITPEEPDTVQ LLDKVRCALQ GGVNLLQYRN KLSVPAVRGE QASALRQLTR EFGVPLIIND DAVLAQQVDA DGVHLGGEDG SIAAARQVLG FDKIIGVSCY NRLSLAQQAE DLGADYVAFG AFFASSVKPD ASVAELSLLQ KARGVIALPV VAIGGITLEN GASVLEAGAD ALAVISALFS APDITLAARQ FANLNTQLSV // ID D9SJ57_GALCS Unreviewed; 314 AA. AC D9SJ57; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=Galf_0288; OS Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea OS capsiferriformans (strain ES-2)). OC Bacteria; Proteobacteria; Betaproteobacteria; Gallionellales; OC Gallionellaceae; Gallionella. OX NCBI_TaxID=395494; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ES-2; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C., RA Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., RA Ivanova N., Mikhailova N., Shelobolina E.S., Picardal F., Roden E., RA Emerson D., Woyke T.; RT "Complete sequence of Gallionella capsiferriformans ES-2."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002159; ADL54333.1; -; Genomic_DNA. DR RefSeq; YP_003846097.1; NC_014394.1. DR ProteinModelPortal; D9SJ57; -. DR EnsemblBacteria; ADL54333; ADL54333; Galf_0288. DR GeneID; 9611609; -. DR KEGG; gca:Galf_0288; -. DR PATRIC; 42337159; VBIGalCap53152_0300. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR BioCyc; GCAP395494:GHXI-299-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 34412 MW; 793AF1B4960E92C0 CRC64; MSALLQKVVE VAAAVLQRPD GTFLLAQRPA DKIWAGYWEF PGGKVEAGET AHDALVRELH EELGIEVLTA YPWLTRVFTY PHATVRLSFF RVTEWRGELY PHEGQQFSWQ QAQDVRVSPV LPANAPILRA LELPALYAIS NVAELGVESF LIKLQAQLDA GLQLIQLREK NLTPERLREL AVRTVAMAHA AGAKVLINGD LALAREVGAD GVHLTSLQLA ELTERPSVAW CAASCHTDEE LQRAQRLGCD FAMLSPVLPT QSHPGAAHLG WERFSALAAG SSIPVYALGG LTRAEMSIAW QRGAHGIALL RQAW // ID D9SRT6_CLOC7 Unreviewed; 217 AA. AC D9SRT6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Clocel_0682; OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / OS 743B). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=573061; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., Hemme C.L., Woyke T.; RT "Complete sequence of Clostridium cellulovorans 743B."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002160; ADL50453.1; -; Genomic_DNA. DR RefSeq; YP_003842217.1; NC_014393.1. DR ProteinModelPortal; D9SRT6; -. DR EnsemblBacteria; ADL50453; ADL50453; Clocel_0682. DR GeneID; 9607527; -. DR KEGG; ccb:Clocel_0682; -. DR PATRIC; 41735599; VBICloCel81632203721_1605. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; CCEL573061:GIXD-719-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 49 53 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23834 MW; 62348941CF50C836 CRC64; MASRESYERG IYNLREGGIY CITDEDSSRG RSNIEVVEEM LASGIRIIQY RAKDKTAREK YSQCLAIRNL TKAADCTFIV DDDVEIAMMV EADGIHVGQT DLPVDDVRRY VGADMILGLS THEPSQALDA IAVGADYIGV GPIFPTKTKK NVCDPVGLTY LDYVVKNIDL PFVAIGGIKA HNLTSVIEHG AKTISLVTEI TAAEDIPLTI KNLYKMF // ID D9TF17_MICAI Unreviewed; 267 AA. AC D9TF17; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Micau_5484; OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / JCM 10878 / OS NBRC 16125 / INA 9442). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Micromonospora. OX NCBI_TaxID=644283; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Ovchinnikova G., Hirsch A.M., Woyke T.; RT "Complete sequence of Micromonospora aurantiaca ATCC 27029."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002162; ADL48990.1; -; Genomic_DNA. DR RefSeq; YP_003838566.1; NC_014391.1. DR ProteinModelPortal; D9TF17; -. DR EnsemblBacteria; ADL48990; ADL48990; Micau_5484. DR GeneID; 9603587; -. DR KEGG; mau:Micau_5484; -. DR PATRIC; 42396777; VBIMicAur74833_5528. DR HOGENOM; HOG000155781; -. DR OMA; VMRAEDP; -. DR BioCyc; MAUR644283:GHOD-5532-MONOMER; -. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 267 AA; 27610 MW; AAB6162C36FAC982 CRC64; MEGRPRTKIY TGPTGVVLLT DRRVAKRALV DVVAGAVGGG VRWVVLREKD LPRAERLALA VELRAILAEA GGTLVVAGPD PLDGDAVHLP AAGPYPPPAV GLVGRSCHDT AELARLTTEH YATLSPVYET RTKPGYGPPL QPDGLRELIA VTKVPVLALG GIETAAQVSA CVEAGATGVA VLGTIMRADD PTETATTLGR AFQEAATRVA RTHPARSDHG PHATGLRPTV PTEGSSLTAR SGHGRPQPRP QPLSAAAVTA TTGEENQ // ID D9TF21_MICAI Unreviewed; 208 AA. AC D9TF21; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Micau_5488; OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / JCM 10878 / OS NBRC 16125 / INA 9442). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Micromonospora. OX NCBI_TaxID=644283; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Ovchinnikova G., Hirsch A.M., Woyke T.; RT "Complete sequence of Micromonospora aurantiaca ATCC 27029."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002162; ADL48994.1; -; Genomic_DNA. DR RefSeq; YP_003838570.1; NC_014391.1. DR ProteinModelPortal; D9TF21; -. DR EnsemblBacteria; ADL48994; ADL48994; Micau_5488. DR GeneID; 9603591; -. DR KEGG; mau:Micau_5488; -. DR PATRIC; 42396785; VBIMicAur74833_5532. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; MAUR644283:GHOD-5536-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 20840 MW; CAC9D648DFCC8C04 CRC64; MLSLGRLHLI TDTRPGRDPL AVLRAALPVA GADLVVQVRV EDDATDREAY ELACRVTEAC RPYGAQCLVN DRLHVALAVD AAGGHVGADD LPVAAARRVL GPDAVLGATA REPVGARTAV DAGASYLGVG PCHVTTTKSG LPDPIGPEGI RAVAEAVSVP VIAIGGVTAA SVPALRAAGA YGVAVVGALS LAADPAHATA ELLRALTC // ID D9TI46_CALOO Unreviewed; 219 AA. AC D9TI46; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=COB47_0339; OS Caldicellulosiruptor obsidiansis (strain ATCC BAA-2073 / strain OB47). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=608506; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-2073 / strain OB47; RX PubMed=20851897; DOI=10.1128/JB.00950-10; RA Elkins J.G., Lochner A., Hamilton-Brehm S.D., Davenport K.W., RA Podar M., Brown S.D., Land M.L., Hauser L.J., Klingeman D.M., RA Raman B., Goodwin L.A., Tapia R., Meincke L.J., Detter J.C., RA Bruce D.C., Han C.S., Palumbo A.V., Cottingham R.W., Keller M., RA Graham D.E.; RT "Complete genome sequence of the cellulolytic thermophile RT Caldicellulosiruptor obsidiansis OB47T."; RL J. Bacteriol. 192:6099-6100(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002164; ADL41678.1; -; Genomic_DNA. DR RefSeq; YP_003839664.1; NC_014392.1. DR ProteinModelPortal; D9TI46; -. DR EnsemblBacteria; ADL41678; ADL41678; COB47_0339. DR GeneID; 9604757; -. DR KEGG; cob:COB47_0339; -. DR PATRIC; 42227806; VBICalObs143161_0383. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; COBS608506:GH1S-340-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24504 MW; 92D10E3D0EDA2F85 CRC64; MTKEEKLELF SIYTIYGMTA EKFSNGRSNI EVVKAMLDSG IKIIQYREKY KSLKEKYKEC LEIRKLTEDY GALLIVNDHV DLCQMVGADG VHLGQEDLPA DEVRKLLGDK FIIGVTTHTK DQVLKAKEDG ADYVGLGPIF ASFTKDNPHP PIGLEMVRWA AENSPLPFVA IGGIKEHNLK DVLANGARCI CAVTEIVGAD DIRKKIESLF KILRSFERS // ID D9TSC2_THETC Unreviewed; 209 AA. AC D9TSC2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tthe_1873; OS Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM OS 571 / NCIB 9385 / NCA 3814) (Clostridium thermosaccharolyticum). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Thermoanaerobacterium. OX NCBI_TaxID=580327; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., Hemme C.L., Woyke T.; RT "Complete sequence of Thermoanaerobacterium thermosaccharolyticum DSM RT 571."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002171; ADL69362.1; -; Genomic_DNA. DR RefSeq; YP_003852446.1; NC_014410.1. DR ProteinModelPortal; D9TSC2; -. DR EnsemblBacteria; ADL69362; ADL69362; Tthe_1873. DR GeneID; 9707435; -. DR KEGG; ttm:Tthe_1873; -. DR PATRIC; 42453114; VBITheThe89703_1898. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; TTHE580327:GHGH-1922-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22606 MW; 8809AE203709BBD5 CRC64; MKDFDVSIYL VTDRNLLKAG IDFYDAVEEA LKNGVTMLQL REKDISSKEF YEIAVRLKDI AAKYSIPFII NDRIDIALSV DADGVHLGQE DLPCSIARKI MGDKKIIGIS AGSVDEAVKA ERDGADYIGA GAVFYTGTKK DIGEAIGLLN LEKIKKAVNI PVVAIGGIKY SNAQDVMKTG VDGISVVSEI MASDDIGFAT RRLKDAISK // ID D9UHN4_9ACTO Unreviewed; 236 AA. AC D9UHN4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSLG_01319; OS Streptomyces sp. SPB78. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=591157; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SPB78; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Streptomyces sp. strain SPB78."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657742; EFK99260.1; -; Genomic_DNA. DR ProteinModelPortal; D9UHN4; -. DR EnsemblBacteria; EFK99260; EFK99260; SSLG_01319. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 236 AA; 24896 MW; F04907446FA6C758 CRC64; MPDRTPHAAA RTVLADARLY LCTDARKHRN DLPAFLDAVL SGGVDIVQLR DKSLEAAEEL ELLQVFADAC RRHGKLLAVN DRADVAHAAR ADVLHLGQGD LPVPAARALI GPDALIGRST HSEAEAAAAA VQDGVDYFCT GPCWPTPTKP GRPAPGLPLV RYAAALGTTR PWFAIGGIDA ARLDEVLDAG ARRVVVVRAL TEAVLPGACG PRARFFVLRA LPLGTPSVQS VDKKSA // ID D9V3D6_9ACTO Unreviewed; 221 AA. AC D9V3D6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSMG_07010; OS Streptomyces sp. AA4. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=591158; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AA4; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Streptomyces sp. strain AA4."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657746; EFL11339.1; -; Genomic_DNA. DR ProteinModelPortal; D9V3D6; -. DR EnsemblBacteria; EFL11339; EFL11339; SSMG_07010. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23118 MW; C13F40F8B6E2EBDE CRC64; MPALTGDQIR TRLADARLYL CTDARTSRGD LAEFADAALA GGVDIVQLRD KTGGAPLEAK QEIAALEVLA EACARHGALL SVNDRADVAL AVGADVLHLG QDDIPVSLAR RVLGDDVVIG RSTHSEQQAT AAATETGVNY FCTGPCWPTP TKPGRYAPGL DLVRATAASG TDRPWFAIGG IDETRLPEVL AAGATRIVVV RAITEAEDPK AAAQTLKAQL R // ID D9VS36_9ACTO Unreviewed; 212 AA. AC D9VS36; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSNG_01937; OS Streptomyces sp. C. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=253839; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Streptomyces sp. strain C."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657750; EFL14685.1; -; Genomic_DNA. DR ProteinModelPortal; D9VS36; -. DR EnsemblBacteria; EFL14685; EFL14685; SSNG_01937. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22386 MW; B5A93E44C2CB3686 CRC64; MQQLSDARLY LCTDARKRQG DLPEFLDAVL AGGVDIVQLR DKGMEAGEEL DHLRVFAEAA RRHGKLLAVN DRADVAHAIG SDVLHLGQGD IPVPAARAIL GDGVLIGRSC HAESEVDAAV AEPGVDYFCT GPCWPTPTKP GRHAPGLDLV RYTASLAQDR PWFAIGGIDG GNLDEVLDAG ATRVVVVRAI TEATDPGAAA AELAKRVRAR LG // ID D9W958_9ACTO Unreviewed; 228 AA. AC D9W958; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSOG_06554; OS Streptomyces himastatinicus ATCC 53653. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457427; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 53653; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Streptomyces hygroscopicus strain ATCC 53653."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657754; EFL26840.1; -; Genomic_DNA. DR ProteinModelPortal; D9W958; -. DR EnsemblBacteria; EFL26840; EFL26840; SSOG_06554. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT METAL 87 87 Magnesium (By similarity). FT METAL 106 106 Magnesium (By similarity). FT BINDING 86 86 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 183 183 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 24185 MW; 215DAC98BF602563 CRC64; MPVRRTTRGE THPMTAREQL ADARLYLCTD ARKRQGDLPE FLDAVLAAGV DVVQLREKGM EAAEELDHLA VFADACRRHG KLLAVNDRAD VAHAAGAGVL HLGQGDLPVP AARAILGDGP LIGRSTHAEA EVDAALAEPG VDYFCTGPCW PTPTKPGRHA PGLSLVRHAA ARRPARPWFA IGGIDASNLD EVLEAGARRI VVVRAITEAE DPAAATESLA KRVRAADV // ID D9X287_STRVR Unreviewed; 78 AA. AC D9X287; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 11-DEC-2013, entry version 16. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=SSQG_02047; OS Streptomyces viridochromogenes DSM 40736. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=591159; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 40736; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Streptomyces viridochromogenes strain DSM 40736."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657757; EFL31529.1; -; Genomic_DNA. DR ProteinModelPortal; D9X287; -. DR EnsemblBacteria; EFL31529; EFL31529; SSQG_02047. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 78 AA; 8396 MW; 8F32DC0D64C46992 CRC64; MLAHPHQARP HAPGLDLVRY TAALGTDRPW FAIGGIDLAN LDQVLEAGAR RVVVVRAITE ADDPGAAAAE FAKRLREQ // ID D9XNZ7_9ACTO Unreviewed; 225 AA. AC D9XNZ7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSRG_04618; OS Streptomyces griseoflavus Tu4000. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=467200; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tu4000; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Streptomyces griseoflavus strain Tu4000."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657758; EFL41814.1; -; Genomic_DNA. DR ProteinModelPortal; D9XNZ7; -. DR EnsemblBacteria; EFL41814; EFL41814; SSRG_04618. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 23519 MW; A8FECFF12B5E7077 CRC64; MPDTTAADTA RARLADARVY LCTDARRRQG DLAEFLDAVL AGGVDIVQLR DKGMEAGEEL EHLAVLADAC ARHGRLLAVN DRADVAHAAG ADVLHLGQGD LPVPAARALL GDGVLIGRST HAESEAAAAA VQPGVDYFCT GPCWPTPTKP GRHAPGLDLV RYTAALAPER PWFAIGGIDL GNLDEVLDAG ARRVVVVRAL TEADDPGAAA AEFAKRLRQA EPARA // ID D9Y5W6_9BURK Unreviewed; 215 AA. AC D9Y5W6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0189_00408; OS Burkholderiales bacterium 1_1_47. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales. OX NCBI_TaxID=469610; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_47; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Strauss J., Daigneault M., RA McDonald J., Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Burkholderiales bacterium strain 1_1_47."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL383995; EFL83331.1; -; Genomic_DNA. DR ProteinModelPortal; D9Y5W6; -. DR EnsemblBacteria; EFL83331; EFL83331; HMPREF0189_00408. DR PATRIC; 40951956; VBIBurBac67366_1275. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22413 MW; CA6F08C8ED4039B8 CRC64; MKSGKKLDLS LYLVLDANLC KTPEGMAETA RKAVEGGCTV VQLRAPEWKK KKQLRAAFLL KELLKDTDVL FIVDDHIDIA LLSGADGVHV GQEDIDPKYV RQLLGPDAVI GLSVGSIKEL NTIGPDVDYI GIGPVFSTKT KVDAGAAVGL GLLEYISKEA GLPNVAIGGI NQSNAADCIR HGADGIAVVS AICGAEDPKA AAAAIKKAVN DALSI // ID D9YBK2_9DELT Unreviewed; 215 AA. AC D9YBK2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0326_01011; OS Desulfovibrio sp. 3_1_syn3. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=457398; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_syn3; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Strauss J., Daigneault M., RA McDonald J., Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., RA Birren B.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_syn3; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Daigneault M., RA McDonald J., Ambrose C.E., Allen-Vercoe E., Walker B., Young S., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Desulfovibrio sp. 3_1_syn3."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADDR02000001; EFL87236.1; -; Genomic_DNA. DR ProteinModelPortal; D9YBK2; -. DR EnsemblBacteria; EFL87236; EFL87236; HMPREF0326_01011. DR PATRIC; 40957688; VBIDesSp67086_1001. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23162 MW; 16B99FD2BBAA41BB CRC64; MPAILPGRTD LYALTDSRLS LGRPLAVVAG ALLESGVRIL QYREKKLKAG KMLEECRLLR RLTERAGACF IVNDHIDIAM LVGADGVHIG QEDLPVPEVR RLVGPDMLIG LSTHTPEQAV AAVNAGADYI GVGPIFATQT KEDVVDPVGF EYLEWVARNT ELPFVAIGGI KEHNIADVAR HGARCCALVS ELVGAQDIHA KVEAVRRAMR EGLGV // ID E0DCL0_9CORY Unreviewed; 730 AA. AC E0DCL0; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.7.4.7; GN Name=thiD; ORFNames=HMPREF0299_6060; OS Corynebacterium matruchotii ATCC 14266. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=553207; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14266; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACSH02000002; EFM50028.1; -; Genomic_DNA. DR ProteinModelPortal; E0DCL0; -. DR EnsemblBacteria; EFM50028; EFM50028; HMPREF0299_6060. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.910.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF03070; TENA_THI-4; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; SSF48613; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Transferase. SQ SEQUENCE 730 AA; 77718 MW; 9423AA3F80F99F00 CRC64; MREPIWDLYL VTDPGSDPDA VPAIVTQAIT GGVTVVQLRD KHATKPQIRQ RAQALKDAIQ AVTAVSNADP STIPLFINDH VDIAAELGLH AHIGQGDLSY VAARRQLPAE LMLGLSIETA DQLEHVVETC RASGVRLPDV VGIGPVRATE TKPDHATPLG VAGVQRIARM AAAHGMKSVA IGGVDKHIAA ELQQVDGVCV VSAIMSSPDP AAAAGELRAA FAMRRPSVPR VLSIAGTDPT GGAGAQADLK SIAAAGGYGM NAITALVAQN THGVRSIHTP PLSFLREQLD AVVSDVTIDA VKIGMLGSAD IVACVRQWLA EHPMPLVVLD PVMVATSGDR LLDPDAEQAV IEFAHHVDIV TPNVPELAVL LSAPEPARTF EEALSQAAEF AQKSNTIVIA KGGHLDGKLA NNAVVYPDGR ITTITTPRID TTNTHGTGCS LSSALATRLA AGDTITEAIE WVSYWLADSI RAGAALEVGT PGGHGPIDHF HQVRRQAACA STKPWKFTGE VRYRPTIPAA GPYTQSLWDS MGEVWSQIMG LPFIMGLRDG SLSKREFDFY LNQDAHYLAN YSRALAVLAA KAGEPQYQVE WAESARDCLV VEAQLHHEWL GGISGDTSPV TLGYTNFLTA TAYGDDYVVG AAAVLPCYWI YAEVGACLAA SNHPDHPYHE WLKTYGDQSF VTTTEAALRR VEHALVQATG VQRAAATAAF QVACAYEREF FDQASRSEIR // ID E0DM93_9RHIZ Unreviewed; 203 AA. AC E0DM93; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BIBO1_1149; OS Brucella inopinata BO1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=470735; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BO1; RA Setubal J.C., Boyle S., Crasta O.R., Kenyon R.W., Mane S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Frace M.A., Sammons S.A., Hoffmaster A.R., Tiller R.V., RA Olsen-Rasmussen M., De B.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADEZ01000012; EFM57038.1; -; Genomic_DNA. DR EnsemblBacteria; EFM57038; EFM57038; BIBO1_1149. DR PATRIC; 41366309; VBIBruSp109945_1223. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Glycosyltransferase; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22357 MW; 151BC189B0113135 CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RIKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALEE GCNFIHLGQE DLDGADLDAI RTGGLKLGVS SHDEAELDRA LSVKPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS IERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID E0DMW2_9RHIZ Unreviewed; 221 AA. AC E0DMW2; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.4.1.1; GN ORFNames=BIBO1_1378; OS Brucella inopinata BO1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=470735; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BO1; RA Setubal J.C., Boyle S., Crasta O.R., Kenyon R.W., Mane S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Frace M.A., Sammons S.A., Hoffmaster A.R., Tiller R.V., RA Olsen-Rasmussen M., De B.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADEZ01000017; EFM56641.1; -; Genomic_DNA. DR EnsemblBacteria; EFM56641; EFM56641; BIBO1_1378. DR PATRIC; 41366809; VBIBruSp109945_1462. DR GO; GO:0004645; F:phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Glycosyltransferase; Transferase. SQ SEQUENCE 221 AA; 23363 MW; D51AFB0A0AF9FEF3 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDMGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRIGADG IHIEGKPADL VEAIEKHTPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID E0DUA1_9RHIZ Unreviewed; 221 AA. AC E0DUA1; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.4.1.1; GN ORFNames=BROD_0637; OS Brucella sp. NF 2653. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=693748; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NF 2653; RA Setubal J.C., Boyle S., Crasta O.R., Kenyon R.W., Mane S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Frace M.A., Sammons S.A., Hoffmaster A.R., Tiller R.V., RA Olsen-Rasmussen M., De B.K.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFB01000029; EFM63287.1; -; Genomic_DNA. DR ProteinModelPortal; E0DUA1; -. DR EnsemblBacteria; EFM63287; EFM63287; BROD_0637. DR PATRIC; 41379181; VBIBruSp153798_0651. DR GO; GO:0004645; F:phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Glycosyltransferase; Transferase. SQ SEQUENCE 221 AA; 23290 MW; 7E9D87E9975AD09D CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHTPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID E0DX37_9RHIZ Unreviewed; 203 AA. AC E0DX37; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BROD_1682; OS Brucella sp. NF 2653. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=693748; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NF 2653; RA Setubal J.C., Boyle S., Crasta O.R., Kenyon R.W., Mane S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Frace M.A., Sammons S.A., Hoffmaster A.R., Tiller R.V., RA Olsen-Rasmussen M., De B.K.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFB01000061; EFM62296.1; -; Genomic_DNA. DR ProteinModelPortal; E0DX37; -. DR EnsemblBacteria; EFM62296; EFM62296; BROD_1682. DR PATRIC; 41381535; VBIBruSp153798_1782. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Glycosyltransferase; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22285 MW; 22A37428236D936D CRC64; MTALDPFYPI FDSADWLERM VPLGIKLVQL RIKDKADAQL RAEIRAARDN CAAHDCQLIV NDYWKLALEE GCNFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVKPDYIAL GPIYPTILKK MKWHQQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID E0E1D8_9FIRM Unreviewed; 484 AA. AC E0E1D8; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF0634_0307; OS Peptostreptococcus stomatis DSM 17678. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptostreptococcus. OX NCBI_TaxID=596315; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17678; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGQ01000010; EFM65293.1; -; Genomic_DNA. DR EnsemblBacteria; EFM65293; EFM65293; HMPREF0634_0307. DR PATRIC; 41389573; VBIPepSto8168_0228. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 484 AA; 52558 MW; 0664D7EA09F059A9 CRC64; MNKERLIEDL CEAIVNLRDK KPLIEQVTNY VTINDCANVT LAIGASPVMG DGFEEVDQMT MISDALVINY GVINGASLKT MIKAGKTANK HNIGIVLDPV GVGATQFRNE AIVDLLTQVH PTIIKGNASE IMSLSGMNTK SKGVDSSADS LEAIDAALKV ARDHRCVCAV TGRIDIITDG RYIVKIYNES DLLSYITGTG CMITSLAASF LGGGASPLVS AVGGILAMSI AGEEAAIREN EENNGIASYR EDVMNNIYKF NQYSIRDLAN IEVEKVEYKY PLYLVTDEKA CKGKDFYESV EASIRGGAKI VQLREKNMDT RDFFKRALKL KEICHKHGVD FVINDRLDIA MAVDADGVHL GQSDMPIEKA KEILGHKKII GISAKNMEEA LEAQKYGADY IGVGAIFATD TKKDSGLIDL ETLKDMTNQI NIPVLAIGGI GLGKLGYLKD TGIDGICVIS DILGSDDPEK RTRELLEEYR SIDV // ID E0E1P2_9FIRM Unreviewed; 391 AA. AC E0E1P2; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-APR-2014, entry version 17. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF0634_0179; OS Peptostreptococcus stomatis DSM 17678. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptostreptococcus. OX NCBI_TaxID=596315; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17678; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGQ01000019; EFM65156.1; -; Genomic_DNA. DR ProteinModelPortal; E0E1P2; -. DR EnsemblBacteria; EFM65156; EFM65156; HMPREF0634_0179. DR PATRIC; 41389850; VBIPepSto8168_0347. DR OrthoDB; EOG64FKGZ; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00972; tRNA_aden_deaminase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn-bd. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR028883; tRNA_aden_deaminase. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES; 1. PE 3: Inferred from homology; SQ SEQUENCE 391 AA; 44167 MW; C802AA4E9C7CFF62 CRC64; MEKRGERNKK KLMVVTNRKI CQEGLLKRLE EVFVAYRQGI YLEDFLIEGL VLREKDLDQE VYLKLLGDVQ ELCQAYEIDI YAHKYWKSAI ELGIKNIHMP LYDLLDLARD GEKYQSFIDH FDRIGVSTHS LDEASQAQRL GASHIFAGHI FPTDCKKGLD PRGLDFLDKM CKTSKLPVYA IGGIGPDRVD QVLERGAQGV AVMSGLMRDG KFGHKACGPA RSMDKSDQGS LGSGQIGASD KAYFMSEALK EARKAYAMKE TPIGAVVVYD GQIVGRGFNQ VELTGDPTQH AEMVAIQEAA KALGRWRLYD CQMYVTMEPC LMCAGAIENS RIKSLYIGAS HKKNHLVGKH NDFKLEVYKD RKIDYEFGIL EKEASKILTD FFKERREEKS K // ID E0E736_ACTPL Unreviewed; 213 AA. AC E0E736; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 18. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=appser1_6000; OS Actinobacillus pleuropneumoniae serovar 1 str. 4074. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=228399; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4074; RX PubMed=20802045; DOI=10.1128/JB.00535-10; RA Xu Z., Chen X., Li L., Li T., Wang S., Chen H., Zhou R.; RT "Comparative genomic characterization of Actinobacillus RT pleuropneumoniae."; RL J. Bacteriol. 192:5625-5636(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADOD01000012; EFM85953.1; -; Genomic_DNA. DR EnsemblBacteria; EFM85953; EFM85953; appser1_6000. DR PATRIC; 41508787; VBIActPle54414203709_0601. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 213 AA; 23601 MW; 24123DFCD4BF1FE2 CRC64; MGRQTIGRIR NCQNKEMIMY DIRQMLQLYF IAGTQDCPNP TEDRSQNLLL ILEQALQAGI TCFQFRDKSK NSLEDQPNAQ KALAIEIDAD GVHVGQKDMS PIMIRQMTDK PLIIGLSNNT LEDLWRSEQM IEVDYCGLGP VFPTNSKEKH NPPIGLDFVK KAREAGIRKP IVSIGGVKAE HVATLKQNGA DGIAVITAIS LASDVSQAVK RLL // ID E0ED07_ACTPL Unreviewed; 164 AA. AC E0ED07; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=appser2_5050; OS Actinobacillus pleuropneumoniae serovar 2 str. S1536. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=871925; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S1536; RX PubMed=20802045; DOI=10.1128/JB.00535-10; RA Xu Z., Chen X., Li L., Li T., Wang S., Chen H., Zhou R.; RT "Comparative genomic characterization of Actinobacillus RT pleuropneumoniae."; RL J. Bacteriol. 192:5625-5636(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADOE01000010; EFM88170.1; -; Genomic_DNA. DR EnsemblBacteria; EFM88170; EFM88170; appser2_5050. DR PATRIC; 41513105; VBIActPle169096_0506. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 164 AA; 18587 MW; B5C3AB1868D18CA2 CRC64; MYDIRQMLQL YFIAGTQDCP NPTEDRSQNL LLILEQALQA GITCFQFRDK SKNSLEDQPN AQKALAIQCR DLCRLYNVPF IVDDNVALAI EIDADGVHVG QKDMSPIMIR QMTDKLLIIG LSNNTLEDLW RSEQMIEVDY CGLGPVFPTN SKEKHNPPIG LDFV // ID E0EJ73_ACTPL Unreviewed; 137 AA. AC E0EJ73; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=appser4_5440; OS Actinobacillus pleuropneumoniae serovar 4 str. M62. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754255; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M62; RX PubMed=20802045; DOI=10.1128/JB.00535-10; RA Xu Z., Chen X., Li L., Li T., Wang S., Chen H., Zhou R.; RT "Comparative genomic characterization of Actinobacillus RT pleuropneumoniae."; RL J. Bacteriol. 192:5625-5636(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADOF01000019; EFM90326.1; -; Genomic_DNA. DR EnsemblBacteria; EFM90326; EFM90326; appser4_5440. DR PATRIC; 41517611; VBIActPle152992_0543. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 137 AA; 14773 MW; F4559C416708A1E3 CRC64; MDDNVALAIE IDADGVHVGQ KDMSPIMIRQ MTDKLLIIGL SNNTLEDLWR SEQMIEVDYC GLGPVFPTNS KEKHNPPIGL DFVKKAREAG IRKPIVSIGG VKAEHVATLK QNGADGVAVI TAISLASDVS QAVKRLL // ID E0EQQ0_ACTPL Unreviewed; 137 AA. AC E0EQQ0; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=appser6_6160; OS Actinobacillus pleuropneumoniae serovar 6 str. Femo. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754256; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Femo; RX PubMed=20802045; DOI=10.1128/JB.00535-10; RA Xu Z., Chen X., Li L., Li T., Wang S., Chen H., Zhou R.; RT "Comparative genomic characterization of Actinobacillus RT pleuropneumoniae."; RL J. Bacteriol. 192:5625-5636(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADOG01000009; EFM92412.1; -; Genomic_DNA. DR EnsemblBacteria; EFM92412; EFM92412; appser6_6160. DR PATRIC; 41522357; VBIActPle158270203710_0619. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 137 AA; 14757 MW; 828EF1F7A6A4B0B7 CRC64; MDDNVALAIE IDADGVHVGQ KDMSPIMIRQ MTDKPLIIGL SNNTLEDLWR SEQMIEVDYC GLGPVFPTNS KEKHNPPIGL DFVKKAREAG IRKPIVSIGG VKAEHVATLK QNGADGVAVI TAISLASDVS QAVKRLL // ID E0EWZ1_ACTPL Unreviewed; 195 AA. AC E0EWZ1; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 18. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=appser9_5980; OS Actinobacillus pleuropneumoniae serovar 9 str. CVJ13261. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754258; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CVJ13261; RX PubMed=20802045; DOI=10.1128/JB.00535-10; RA Xu Z., Chen X., Li L., Li T., Wang S., Chen H., Zhou R.; RT "Comparative genomic characterization of Actinobacillus RT pleuropneumoniae."; RL J. Bacteriol. 192:5625-5636(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADOI01000017; EFM94605.1; -; Genomic_DNA. DR EnsemblBacteria; EFM94605; EFM94605; appser9_5980. DR PATRIC; 41526911; VBIActPle147488_0597. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 195 AA; 21471 MW; 5DCB1312D9F2DA7A CRC64; MYDIRQMLQL YFIAGTQDCP NPTEDRSQNL LLILEQALQA GITCFQFRDK SKNSLEDQPN AQKALAIEID ADGVHVGQKD MSPIMIRQMT DKPLIIGLSN NTLEDLWRSE QMIEVDYCGL GPVFPTNSKE KHNPPIGLDF VKKAREAGIR KPIVSIGGVK AEHVATLKQN GADGIAVITA ISLASDVSQA VKRLL // ID E0F341_ACTPL Unreviewed; 137 AA. AC E0F341; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=appser10_5620; OS Actinobacillus pleuropneumoniae serovar 10 str. D13039. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754259; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D13039; RX PubMed=20802045; DOI=10.1128/JB.00535-10; RA Xu Z., Chen X., Li L., Li T., Wang S., Chen H., Zhou R.; RT "Comparative genomic characterization of Actinobacillus RT pleuropneumoniae."; RL J. Bacteriol. 192:5625-5636(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADOJ01000008; EFM96869.1; -; Genomic_DNA. DR EnsemblBacteria; EFM96869; EFM96869; appser10_5620. DR PATRIC; 41531404; VBIActPle151137_0566. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 137 AA; 14704 MW; C39EE0F6B6A5B0AB CRC64; MDDNVALAIE IDADGVHVGQ KDMSPIMIRQ MTDKPLIIGL SNNTLEDLWC SEQMIEVDYC GLGPVFPTNS KEKHNPPIGL DFVKKAREAG IRKPIVSIGG VKAEHVATLK QNGADGVAVI TAISLASDVS QAVKRLL // ID E0F9E3_ACTPL Unreviewed; 195 AA. AC E0F9E3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 18. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=appser11_6060; OS Actinobacillus pleuropneumoniae serovar 11 str. 56153. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754260; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=56153; RX PubMed=20802045; DOI=10.1128/JB.00535-10; RA Xu Z., Chen X., Li L., Li T., Wang S., Chen H., Zhou R.; RT "Comparative genomic characterization of Actinobacillus RT pleuropneumoniae."; RL J. Bacteriol. 192:5625-5636(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADOK01000012; EFM99015.1; -; Genomic_DNA. DR EnsemblBacteria; EFM99015; EFM99015; appser11_6060. DR PATRIC; 41536003; VBIActPle158651_0606. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 195 AA; 21471 MW; 5DCB1312D9F2DA7A CRC64; MYDIRQMLQL YFIAGTQDCP NPTEDRSQNL LLILEQALQA GITCFQFRDK SKNSLEDQPN AQKALAIEID ADGVHVGQKD MSPIMIRQMT DKPLIIGLSN NTLEDLWRSE QMIEVDYCGL GPVFPTNSKE KHNPPIGLDF VKKAREAGIR KPIVSIGGVK AEHVATLKQN GADGIAVITA ISLASDVSQA VKRLL // ID E0FFH2_ACTPL Unreviewed; 92 AA. AC E0FFH2; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=appser12_5540; OS Actinobacillus pleuropneumoniae serovar 12 str. 1096. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754261; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1096; RX PubMed=20802045; DOI=10.1128/JB.00535-10; RA Xu Z., Chen X., Li L., Li T., Wang S., Chen H., Zhou R.; RT "Comparative genomic characterization of Actinobacillus RT pleuropneumoniae."; RL J. Bacteriol. 192:5625-5636(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADOL01000014; EFN01084.1; -; Genomic_DNA. DR EnsemblBacteria; EFN01084; EFN01084; appser12_5540. DR PATRIC; 41540446; VBIActPle154243_0558. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 92 AA; 10093 MW; 59BA70C5BE922B8A CRC64; MDDNVALAIE IDADGVHVGQ KDMSPIMIRQ MTDKPLIIGL SNNTLEDLWC SEQMIEVDYC GLGPVFPTNS KEKHNPPIGL ASDVSQAVKR LL // ID E0FLK9_ACTPL Unreviewed; 218 AA. AC E0FLK9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=appser13_5940; OS Actinobacillus pleuropneumoniae serovar 13 str. N273. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754262; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=N273; RX PubMed=20802045; DOI=10.1128/JB.00535-10; RA Xu Z., Chen X., Li L., Li T., Wang S., Chen H., Zhou R.; RT "Comparative genomic characterization of Actinobacillus RT pleuropneumoniae."; RL J. Bacteriol. 192:5625-5636(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADOM01000011; EFN03257.1; -; Genomic_DNA. DR ProteinModelPortal; E0FLK9; -. DR EnsemblBacteria; EFN03257; EFN03257; appser13_5940. DR PATRIC; 41544885; VBIActPle159548_0597. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 24090 MW; 491DAAE0E7ED3954 CRC64; MYDIRQMLQL YFIAGTQDCP NPTEDRSQNL LLILEQALQA GITCFQFRDK SKNSLEDQPN AQKALAIQCR DLCRLYNVPF IVDDNVALAI EIDADGVHVG QKDMSPIMIR QMTDKPLIIG LSNNTLEDLW RSEQMIEVDY CGLGPVFPTN SKEKHNPPIG LDFVKKAREA GIRKPIVSIG GVKAEHVATL KQNGADGVAV ITAISLASDV SQAVKRLL // ID E0G2Z8_ENTFL Unreviewed; 211 AA. AC E0G2Z8; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9498_01326; OS Enterococcus faecalis TX4248. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749495; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX4248; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBR01000038; EFM83047.1; -; Genomic_DNA. DR EnsemblBacteria; EFM83047; EFM83047; HMPREF9498_01326. DR PATRIC; 43417987; VBIEntFae153771_1244. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22878 MW; A6E656410B430126 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGGDEI PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTRVAGV SLVSEIMLAE QIAEKVQGLM RVTERMLEAR K // ID E0GAA0_ENTFL Unreviewed; 211 AA. AC E0GAA0; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9514_00577; OS Enterococcus faecalis TX0855. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749511; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0855; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBV01000009; EFM80703.1; -; Genomic_DNA. DR ProteinModelPortal; E0GAA0; -. DR EnsemblBacteria; EFM80703; EFM80703; HMPREF9514_00577. DR PATRIC; 43422913; VBIEntFae156740_0542. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22866 MW; A6E43F880C487223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E0GPM4_ENTFL Unreviewed; 211 AA. AC E0GPM4; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9521_02622; OS Enterococcus faecalis TX2134. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749518; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX2134; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBW01000077; EFM75468.1; -; Genomic_DNA. DR ProteinModelPortal; E0GPM4; -. DR EnsemblBacteria; EFM75468; EFM75468; HMPREF9521_02622. DR PATRIC; 43432744; VBIEntFae149765_2452. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID E0GUC6_ENTFL Unreviewed; 211 AA. AC E0GUC6; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9515_01027; OS Enterococcus faecalis TX0860. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749512; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0860; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBX01000019; EFM73847.1; -; Genomic_DNA. DR ProteinModelPortal; E0GUC6; -. DR EnsemblBacteria; EFM73847; EFM73847; HMPREF9515_01027. DR PATRIC; 41556462; VBIEntFae147180_0965. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22866 MW; 98C1A43B92687A05 CRC64; MREQLKVYLV TGRYDFSDTK FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E0H5X2_ENTFL Unreviewed; 211 AA. AC E0H5X2; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9505_01985; OS Enterococcus faecalis TX0109. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749502; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0109; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBY01000063; EFM69775.1; -; Genomic_DNA. DR EnsemblBacteria; EFM69775; EFM69775; HMPREF9505_01985. DR PATRIC; 41564337; VBIEntFae157598_1842. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22861 MW; E4C2537D7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM HVTERMLEAR K // ID E0HAC2_ENTFL Unreviewed; 211 AA. AC E0HAC2; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9509_00525; OS Enterococcus faecalis TX0411. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749506; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0411; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECA01000026; EFM68143.1; -; Genomic_DNA. DR ProteinModelPortal; E0HAC2; -. DR EnsemblBacteria; EFM68143; EFM68143; HMPREF9509_00525. DR PATRIC; 41567378; VBIEntFae154435_0482. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID E0I3N0_9BACL Unreviewed; 233 AA. AC E0I3N0; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PaecuDRAFT_0405; OS Paenibacillus curdlanolyticus YK9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=717606; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YK9; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., RA Anderson I.J., Johnson E., Loganathan U., Mulhopadhyay B., RA Kyrpides N., Woyke T.J.; RT "The draft genome of Paenibacillus curdlanolyticus YK9."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDD01000001; EFM12894.1; -; Genomic_DNA. DR ProteinModelPortal; E0I3N0; -. DR EnsemblBacteria; EFM12894; EFM12894; PaecuDRAFT_0405. DR PATRIC; 41184967; VBIPaeCur159330_0403. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 25112 MW; 2BA0CAC9519D9878 CRC64; MSASQWQQEE QLRRLLSVYL IMGSNNCLKD PMVVLEEAIQ GGITMFQYRE KGSGALAGDE RFSLASRLRG KCREHHIPFI VNDDVDLALA LDADGVHVGQ EDENASAVRR RIGADRILGV SAYDLPEAEA AIRMGADYLG VGPLYRTQTK EDAKAASGLD VIASMRMQHI RIPIVGIGGI RPDNAEQVIG AGADGVSVIT AITHAGDERS ATKALSDAVE RGLHNRAKGG YFL // ID E0I6A1_9BACL Unreviewed; 298 AA. AC E0I6A1; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PaecuDRAFT_1173; OS Paenibacillus curdlanolyticus YK9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=717606; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YK9; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., RA Anderson I.J., Johnson E., Loganathan U., Mulhopadhyay B., RA Kyrpides N., Woyke T.J.; RT "The draft genome of Paenibacillus curdlanolyticus YK9."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDD01000003; EFM11567.1; -; Genomic_DNA. DR ProteinModelPortal; E0I6A1; -. DR EnsemblBacteria; EFM11567; EFM11567; PaecuDRAFT_1173. DR PATRIC; 41186507; VBIPaeCur159330_1174. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b. DR InterPro; IPR010035; Thi_S. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003749; ThiS/MoaD. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02597; ThiS; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF54285; SSF54285; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR01683; thiS; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 298 AA; 31715 MW; 1904400DEDED7B8E CRC64; MMTERQSRFH EGIRLYVITG ANYHPGRTLA DVMEQTLIGG ADIIQLRDKT ASQRELLEQA RVLRELTKRY GVPLIINDYI DIALEVGADG VHLGQDDRSL AEARERLGQD AIIGISTHQL LHALTAQAGG ADYIGVGPVY PTGTKPGKAA VTTNYVTEAA ASVKIPFVAI GGITLDNVDT VLAAGATRVC AVSAVVGAPD PAAVCRSFKE WIAAADTARI AGRAFFAAEG SVIVSVNVNG KATRTAARSV LELVREHGLE NRRMVVELDG EIVERAAWER TPIRDGAAVE LVHFVGGG // ID E0J6X5_ECOLW Unreviewed; 211 AA. AC E0J6X5; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 30. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECW_m4351, WFL_21180; GN ORFNames=EschWDRAFT_4333; OS Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / NCIMB 8666 OS / NRRL B-766 / W). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=566546; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=W; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., RA Tremaine M., Landick R., Keating D., Woyke T.J.; RT "The draft genome of Escherichia coli W."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / NCIMB 8666 / NRRL B-766 / W, RC and W; RX PubMed=21208457; DOI=10.1186/1471-2164-12-9; RA Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y., RA Nielsen L.K.; RT "The genome sequence of E. coli W (ATCC 9637): comparative genome RT analysis and an improved genome-scale reconstruction of E. coli."; RL BMC Genomics 12:9-9(2011). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / NCIMB 8666 / NRRL B-766 / W, RC and W; RX PubMed=22075923; DOI=10.1007/s10295-011-1052-2; RA Turner P.C., Yomano L.P., Jarboe L.R., York S.W., Baggett C.L., RA Moritz B.E., Zentz E.B., Shanmugam K.T., Ingram L.O.; RT "Optical mapping and sequencing of the Escherichia coli KO11 genome RT reveal extensive chromosomal rearrangements, and multiple tandem RT copies of the Zymomonas mobilis pdc and adhB genes."; RL J. Ind. Microbiol. Biotechnol. 39:629-639(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002185; ADT77645.1; -; Genomic_DNA. DR EMBL; CP002967; AFH13877.1; -; Genomic_DNA. DR EMBL; AEDF01000040; EFN36072.1; -; Genomic_DNA. DR RefSeq; YP_006126887.1; NC_017635.1. DR RefSeq; YP_006175663.1; NC_017664.1. DR SMR; E0J6X5; 10-208. DR EnsemblBacteria; ADT77645; ADT77645; ECW_m4351. DR EnsemblBacteria; AFH13877; AFH13877; WFL_21180. DR EnsemblBacteria; EFN36072; EFN36072; EschWDRAFT_4333. DR GeneID; 12698101; -. DR GeneID; 12752729; -. DR KEGG; ell:WFL_21180; -. DR KEGG; elw:ECW_m4351; -. DR PATRIC; 41598137; VBIEscCol201000_4748. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E0M4W5_9ENTR Unreviewed; 208 AA. AC E0M4W5; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PanABDRAFT_4434; OS Pantoea sp. aB. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=517433; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Adams A., RA Adams S., Raffa K., Currie C., Woyke T.J.; RT "The draft genome of Pantoea sp. aB."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDL01000020; EFM17545.1; -; Genomic_DNA. DR EnsemblBacteria; EFM17545; EFM17545; PanABDRAFT_4434. DR PATRIC; 41211745; VBIPanSp97966_4529. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22651 MW; CBEAAAA046DA39B6 CRC64; MPAFPATAPR LGLYPVVDSP EWIERLLEMG VSTLQLRIKD QPDAIAEPAI AHAIALGKRY DARLFINDYW QLAIKHQAYG IHLGQEDMDV ADLARIHQAG LRLGLSTHDD AELDRALAIQ PSYIALGHIF PTQTKEMPSA PQGIEQLKRH LARLTHIPTV AIGGISIARA PEVLATGVGS IAVVSAITQA DDWREATRTL MALAEPGH // ID E0MPM9_9RHOB Unreviewed; 215 AA. AC E0MPM9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_2; Synonyms=thiE; ORFNames=R2A130_1476; OS Ahrensia sp. R2A130. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ahrensia. OX NCBI_TaxID=744979; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R2A130; RA Suzuki M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEB01000017; EFL88989.1; -; Genomic_DNA. DR EnsemblBacteria; EFL88989; EFL88989; R2A130_1476. DR PATRIC; 41236779; VBIAhrSp149844_2384. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22901 MW; B3B7E24238DB43E7 CRC64; MTALDISLYG ILDPARSNGR PLPELAAAAA RGGATLLQYR DKTSDTRTMV ETAHDILEAL EDFDIPLLIN DRVDVALAVG AHGVHLGQTD METQDARDLL GDDAIIGLTI KNRSHATNAP VDLLDYVCIG GVFQTLSKDN PVAIGLDGWS SVAGHFRQID HRLPVGAIAG IDETNCADVM SNGADGVAII SAMFMADDVE AVTKNLVKII KESRR // ID E0MQH7_9RHOB Unreviewed; 224 AA. AC E0MQH7; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_1; ORFNames=R2A130_1127; OS Ahrensia sp. R2A130. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ahrensia. OX NCBI_TaxID=744979; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R2A130; RA Suzuki M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEB01000017; EFL88644.1; -; Genomic_DNA. DR EnsemblBacteria; EFL88644; EFL88644; R2A130_1127. DR PATRIC; 41236087; VBIAhrSp149844_2040. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 224 AA; 23176 MW; 2EB578D89D928315 CRC64; MLVRHGDALA RLTADDLAKA LSCGDVASLI LSPVSADGIM DETAFQTIVE PLVPVAQAAG IAVIIEHHSR VAGRLGADGL QLGQDPADLA DAVSRLTPAM MVGAANVKTR HNALVLGEIQ PDYIMFGKTG SDIRDEANPK NVALGDWWSK LVELPCIVLG GASADSVLDV AKAGVEFVAL DAALDGVPSD DATIAPQPSA MGDAIARANQ LLDEHAPRFD AENS // ID E0MXN1_9CORY Unreviewed; 224 AA. AC E0MXN1; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0277_1265; OS Corynebacterium accolens ATCC 49726. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=862512; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49726; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEED01000101; EFM43680.1; -; Genomic_DNA. DR EnsemblBacteria; EFM43680; EFM43680; HMPREF0277_1265. DR PATRIC; 43436410; VBICorAcc166488_1694. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). SQ SEQUENCE 224 AA; 23141 MW; A5015057F7DA9506 CRC64; MRAKQLDLRC YHVTGVPQEK VVQVAAAAAA GGAGVIQVRS KPISVRDLTA LAIDVAAAVE EANPATRVLI DDRVDVAAAL MGNHNIHGVH IGQDDLDPRL ARRILREDAI IGLTTGTLEL VQGANEYADV IDYIGAGPFR PTPTKSSGRA PLGLEGYPPL VAASAVPVVA IGDVQAADAE ALAETGVAGV AIVRAFMDFD DPAALATTVI RDFDRANAAT GSHA // ID E0MXT3_9CORY Unreviewed; 94 AA. AC E0MXT3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine-phosphate diphosphorylase domain protein; DE EC=2.5.1.3; DE Flags: Fragment; GN Name=thiE2; ORFNames=HMPREF0277_1317; OS Corynebacterium accolens ATCC 49726. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=862512; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49726; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEED01000102; EFM43672.1; -; Genomic_DNA. DR EnsemblBacteria; EFM43672; EFM43672; HMPREF0277_1317. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. FT NON_TER 1 1 SQ SEQUENCE 94 AA; 9450 MW; FD8489CBFB952A83 CRC64; IDPQQAPDVI GIGPVYSTAT KKNAPAGIGP DAAGRLATAA RERGIESVAI GGIKAHNAHE LSGSDFAGIC VVSDIMTADD PAAAAHNLKE AYRG // ID E0MXT4_9CORY Unreviewed; 69 AA. AC E0MXT4; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; DE Flags: Fragment; GN Name=thiE3; ORFNames=HMPREF0277_1318; OS Corynebacterium accolens ATCC 49726. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=862512; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49726; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEED01000103; EFM43609.1; -; Genomic_DNA. DR EnsemblBacteria; EFM43609; EFM43609; HMPREF0277_1318. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. FT NON_TER 69 69 SQ SEQUENCE 69 AA; 7618 MW; A4F5BF47C6D7B6DF CRC64; MNIDWTLYLI TDPELTGGRD QVVPIVQEAV RGGATVVQLR DKDANDEEIE ATARELLEVL GDVPLLIND // ID E0NBW1_NEIME Unreviewed; 205 AA. AC E0NBW1; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0602_1993; OS Neisseria meningitidis ATCC 13091. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=862513; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 13091; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEF01000103; EFM03537.1; -; Genomic_DNA. DR EnsemblBacteria; EFM03537; EFM03537; HMPREF0602_1993. DR PATRIC; 41900053; VBINeiMen168195_0220. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21612 MW; 0A11E353CF7D41AD CRC64; MTFLPLKSPL KFYAVVPTAD WVGRMVKAGV DTVQLRCKTL HGDELKREIA RCAAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID E0NDU2_PEDAC Unreviewed; 118 AA. AC E0NDU2; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF0623_0464; OS Pediococcus acidilactici DSM 20284. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=862514; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20284; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEG01000002; EFL96413.1; -; Genomic_DNA. DR EnsemblBacteria; EFL96413; EFL96413; HMPREF0623_0464. DR PATRIC; 41902086; VBIPedAci166297_0450. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 118 AA; 12419 MW; C9D933ED5199CB13 CRC64; MAVARRILGP NKIIGATTKT VAQARRAVEE GANYLGVGAI FPTTTHVKTV HTSVATLKRI KQEAKITVFA IGGLNAENLS VLRNTNVDGV AAVSAIMKAT QPQQVAQQLK STVIDVLS // ID E0NDU3_PEDAC Unreviewed; 65 AA. AC E0NDU3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF0623_0465; OS Pediococcus acidilactici DSM 20284. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=862514; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20284; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEG01000002; EFL96414.1; -; Genomic_DNA. DR EnsemblBacteria; EFL96414; EFL96414; HMPREF0623_0465. DR PATRIC; 41902088; VBIPedAci166297_0451. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 65 AA; 7459 MW; 4B0D461F80EF0546 CRC64; MLEKPLLYLD TGRLGLNQQQ FLERIKLACQ GGVDLLQLRE KEISSAEYYK LAGHVKRLPT VTKSR // ID E0NHQ1_PEDAC Unreviewed; 226 AA. AC E0NHQ1; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0623_1574; OS Pediococcus acidilactici DSM 20284. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=862514; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20284; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEG01000008; EFL95068.1; -; Genomic_DNA. DR EnsemblBacteria; EFL95068; EFL95068; HMPREF0623_1574. DR PATRIC; 41904367; VBIPedAci166297_1561. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23946 MW; BFC031C65098FA3F CRC64; MKFNPTMLQA YFIAGTQDVA SKTDFLPTVE RIVQAGATAF QFRNKGAVKT ASRDEVVELA RACHQITQKY QIPLFIDDDV DLALAVGAEG IHVGQKDERI TSVLERVGDR MIVGLSCNTA AQITAANQLN GVDYLGTGTV YETNSKADAG NALGVDKLRE LVQMSKFPVV AIGGITLKRV AETVATGAAG IAAISMFIQM TDPAQQIAEI KATIAQVGGV ACSPKK // ID E0NN28_9FIRM Unreviewed; 211 AA. AC E0NN28; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9225_1567; OS Peptoniphilus duerdenii ATCC BAA-1640. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Peptoniphilus. OX NCBI_TaxID=862517; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1640; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEH01000048; EFM24701.1; -; Genomic_DNA. DR EnsemblBacteria; EFM24701; EFM24701; HMPREF9225_1567. DR PATRIC; 41908037; VBIPepDue168552_1346. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23157 MW; A3E9318BEF35C705 CRC64; MRKFKDALYL VTDSTNLDEE EYLNRVYKAC KSGVDIVQIR EKDKTAREIM RLGEAVKEIT DKFNIPLIID DRVDIAYALG VGVHLGSSDI PVTIARKILG KDAIIGSSAK SVEVAKECEK DGANYLGVGA IRPTKTKVIT KLTSVDTLDD ISKNVDIDVF AIGGLNKDNI EILNGLDISG VCVVRAIMQR SDADIAVQEL KQKIKCIRSQ C // ID E0NPU9_9BACT Unreviewed; 202 AA. AC E0NPU9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 13-NOV-2013, entry version 15. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF0658_0200; OS Prevotella marshii DSM 16973. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=862515; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16973; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEI01000008; EFM02825.1; -; Genomic_DNA. DR EnsemblBacteria; EFM02825; EFM02825; HMPREF0658_0200. DR PATRIC; 41239588; VBIPreMar165560_0192. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23269 MW; 7F2FE19929479334 CRC64; MKLVIMTSPT FFVEEDKILT ALFDEGLDNL HIYKPGTAPT YAERLLSLLP EDYYRKITVH DHYYLKKEYG LAGIHLDRLD EMPPQGYKGH ITRSCDDLSL LKETRKKSDY VFLHNIFDSL HDKNIKSSFS AEELVNAAHK GIIDKKVYAL GGMTIDCIKQ MKDLGFGGIV VCGDLWNRFD IHNELNYKEV IRHFDKLRKA VG // ID E0P2T8_9FIRM Unreviewed; 219 AA. AC E0P2T8; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9166_2405; OS Selenomonas sp. oral taxon 149 str. 67H29BP. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=864563; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=67H29BP; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEJ01000056; EFM22049.1; -; Genomic_DNA. DR EnsemblBacteria; EFM22049; EFM22049; HMPREF9166_2405. DR PATRIC; 41913693; VBISelSp164981_2199. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23657 MW; 4A47065A41FDAF7B CRC64; MNEMLVRKED LLLYAVTDRR WLHGGRLYDA AERALQGGAT FLQLREKSAG TMPRASLLEE ARALRLLCRR YRVPFVIDDD VELAMAIGVD GVHVGQSDME AGAARQRIGK DKILGVSVQT VKEARIAAEC GADYLGVGAV FPTNSKEDAE AVHYETLKEI CSATAVPVVA IGGINDENVM QLAGSGIAGV AVISAIFAKE DIRLAAQRLL HKVKEAKGR // ID E0P3M2_STAAU Unreviewed; 213 AA. AC E0P3M2; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0783_0301; OS Staphylococcus aureus subsp. aureus ATCC BAA-39. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=862516; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-39; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEK01000027; EFM08031.1; -; Genomic_DNA. DR ProteinModelPortal; E0P3M2; -. DR SMR; E0P3M2; 4-209. DR PRIDE; E0P3M2; -. DR EnsemblBacteria; EFM08031; EFM08031; HMPREF0783_0301. DR PATRIC; 41914303; VBIStaAur165978_0086. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID E0PDX0_STREI Unreviewed; 210 AA. AC E0PDX0; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9319_1043; OS Streptococcus equinus ATCC 700338. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=864569; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700338; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEL01000014; EFM27480.1; -; Genomic_DNA. DR EnsemblBacteria; EFM27480; EFM27480; HMPREF9319_1043. DR PATRIC; 43440747; VBIStrBov165195_0579. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22609 MW; D0ED6845742031E0 CRC64; MDKEILQVYF ICGTANCPEG KFLEILEAAF KSGVTCFQFR EKGANALKGD EKVVLARKVK ELCRKYQIPL IINDDVDLAL ELDADGIHLG QDDLPITKAR QLFPNKIIGL SVGSTIEYQQ SAVGLVDYIG VGPIFPTSSK NDAGEVIGLK GLNDVRDYDK EIPIVAIGGI TFGDVAAIKQ SGADGVAVIS AIAQSKQVEV DTQRLSSCFD // ID E0PK95_STRGY Unreviewed; 210 AA. AC E0PK95; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9352_1181; OS Streptococcus gallolyticus subsp. gallolyticus TX20005. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=545774; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX20005; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEM01000015; EFM29358.1; -; Genomic_DNA. DR ProteinModelPortal; E0PK95; -. DR EnsemblBacteria; EFM29358; EFM29358; HMPREF9352_1181. DR PATRIC; 43445181; VBIStrGal111396_0737. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22695 MW; B32CAC167AC003AB CRC64; MDKEILQVYF ICGTANCPEG KFLEILEAAF KSGVTCFQFR EKGANALKGG EKVVLARKVK ELCRKYQIPL IINDDVDLAL ELDADGIHLG QDDLPITKAR QLFPNKIIGL SVGSTIEYQR SAVELVDYIG VGPIFPTSSK NDAGEVIGLK GLNDVRDYDK EIPIVAIGGI TFGDVAAIKQ SGADGVAVIS AIAQSKQVEV DTQRLSSFFD // ID E0PQ88_STRMT Unreviewed; 210 AA. AC E0PQ88; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF8571_0705; OS Streptococcus mitis ATCC 6249. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=864567; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 6249; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEN01000012; EFM31335.1; -; Genomic_DNA. DR EnsemblBacteria; EFM31335; EFM31335; HMPREF8571_0705. DR PATRIC; 43448677; VBIStrMit169061_0855. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22669 MW; B273AB85D99A592E CRC64; MNREALRLYL VTNRYQDSLG SFLEKVETAC RSGVTIVQLR EKNLTTNQYY HLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVNRALEAE TSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKAHA FLTKLDDMIS // ID E0Q255_9STRE Unreviewed; 210 AA. AC E0Q255; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9189_1193; OS Streptococcus sp. oral taxon 071 str. 73H25AP. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=864570; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=73H25AP; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEP01000011; EFM34969.1; -; Genomic_DNA. DR EnsemblBacteria; EFM34969; EFM34969; HMPREF9189_1193. DR PATRIC; 43457336; VBIStrSp169195_1574. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22790 MW; E009CFDDE30350CD CRC64; MNREVLKLYL VTNRYQDSLE NFLEKVETAC RSGVTIIQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDICLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE TSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDDIVS // ID E0Q5A3_9BIFI Unreviewed; 855 AA. AC E0Q5A3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE SubName: Full=Thiamine biosynthesis protein ThiC; DE EC=2.5.1.3; GN Name=thiC; ORFNames=HMPREF0168_0310; OS Bifidobacterium dentium ATCC 27679. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=871562; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27679; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEQ01000006; EFM42278.1; -; Genomic_DNA. DR EnsemblBacteria; EFM42278; EFM42278; HMPREF0168_0310. DR PATRIC; 43459471; VBIBifDen165269_1172. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Transferase; Zinc. SQ SEQUENCE 855 AA; 94665 MW; F2A5F5841F8F6093 CRC64; MNDYPYASMR DCFDMSAYFV VGPQDCKGRP ITDVVDDALR GGATFIQLRA KNTDAKDLTL MAQDIAQIIE DNDKSDAVAF VIDDRVDVVW QARNKGIKVD GVHIGQTDME PREARALLGE EAIVGLSAET ESLVRLINEL PNGCIDYIGA GPLHVSTTKP EASVGGNDGS GNTLDEDQIN TICTASDFPV VVGGGVTAND MEMLARSKAA GWFVVSAIAG ADDPEAATRE MVTRWKAVRG ETKHGFAPRV QSADTATTTD TQMTESNNGK FTNAKEAKAS SKLAKQQRVD IAARGSKQRD KAHVRKTTPV HFENRFGSYD LEVPYTEIKL SDTPGVGPNA PFKDYNTEGP KCDPKEGLAP LRLDWIRDRG DVEEYEGRRR NLEDDGKRAI KRGKASKEWR GRQHKPLKAK DHPITQMWYA RHDIITPEMR YVAEREHCDV ELVRSELAAG RAVMPCNINH PEAEPMIIGS RFLTKLNANM GNSAVTSSID EEVEKLTWAT KWGADTVMDL STGNDIHTTR EWILRNSPVP IGTVPMYQAL EKVEDDASKL SWELFRDTVI EQCEQGVDYM TIHAGVLLRF VPLTANRMTG IVSRGGSIMA EWCLQHHQES FLYTHFDELC EIFAKYDVAF SLGDGLRPGS LADANDAAQF AELMTLGELT QRAWEHDVQV MIEGPGHIPF DTVRMNIEME KAICKDAPFY TLGPLTTDTA PGYDHITSAI GGVEIARYGT AMLCYVTPKE HLGLPNKDDV KQGVIAYKIA CHAADIAKHH PHAIDRDNAM SKARFEFRWL DQFNLSYDPD TAIAFHDDTL PAEPAKMAHF CSMCGPKFCS MAISQNIRRK FGNAEAQEKL VADAQ // ID E0QCG8_CAMCO Unreviewed; 210 AA. AC E0QCG8; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9399_0410; OS Campylobacter coli JV20. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=864566; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JV20; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEER01000018; EFM37615.1; -; Genomic_DNA. DR EnsemblBacteria; EFM37615; EFM37615; HMPREF9399_0410. DR PATRIC; 43464211; VBICamCol168266_0255. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23316 MW; B6320E033DA3A612 CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESF VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID E0QCL9_CAMCO Unreviewed; 201 AA. AC E0QCL9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN Name=thiE2; ORFNames=HMPREF9399_0461; OS Campylobacter coli JV20. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=864566; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JV20; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEER01000018; EFM37666.1; -; Genomic_DNA. DR EnsemblBacteria; EFM37666; EFM37666; HMPREF9399_0461. DR PATRIC; 43464315; VBICamCol168266_0306. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID E0QI34_9FIRM Unreviewed; 444 AA. AC E0QI34; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0379_0682; OS Eubacterium yurii subsp. margaretiae ATCC 43715. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=864565; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43715; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEES01000026; EFM39525.1; -; Genomic_DNA. DR ProteinModelPortal; E0QI34; -. DR EnsemblBacteria; EFM39525; EFM39525; HMPREF0379_0682. DR PATRIC; 43468464; VBIEubYur165861_0529. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF13419; HAD_2; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 444 AA; 50609 MW; 2F7646C9888557BD CRC64; MIFILVLKKA VKMKNLSCYD YSIYYVTDEE LLHPSYDLYK SVEDAIIGGA IMIQLREKNT TTRDFIEKAL KIKDICAKYE VPLIINDRVD VALAIGADGV HLGQDDMDLK SARKIFGQDK IIGISASNLQ EAKLAEQGGA TYIGVGAMYS TNTKTDADLT TMEELKKIRQ EVKIPIVVIG GINQKTIPNF KDTDIDGLAI VSAIATSDNQ IESTKMLKNQ FYRNNEVKAV ILDIDLTMLE TEELWDRVLD KIMGKYGFNC NETDKKFIWD NSFEVVAKYL SEKFKLKITE DDLLKLIHDF SIEEYANSEI KLKKGLEKFL TLMNEKNIRL AVCTSLSKKQ YETVLKNTGL IDKFELILSA TETGLDKSDK KIYETVSSKL GIHPRNILAF DDELRAIRAA KRAGMRTALM KNTKNNTEDR YTLSMIDYPV YDFDEFMKID IRWD // ID E0QU33_ECOLX Unreviewed; 211 AA. AC E0QU33; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECNC101_00090; OS Escherichia coli NC101. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=753642; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NC101; RA Suzuki H., Richards V., Lefebure T., Pavinski Bitar P., Lang P., RA Stanhope M.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEFA01000001; EFM55049.1; -; Genomic_DNA. DR EnsemblBacteria; EFM55049; EFM55049; ECNC101_00090. DR PATRIC; 41686439; VBIEscCol150923_0019. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22995 MW; 11322A867C948B07 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIHA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E0RA44_PAEP6 Unreviewed; 237 AA. AC E0RA44; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PPE_03735; OS Paenibacillus polymyxa (strain E681). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=349520; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E681; RX PubMed=20851896; DOI=10.1128/JB.00983-10; RA Kim J.F., Jeong H., Park S.Y., Kim S.B., Park Y.K., Choi S.K., RA Ryu C.M., Hur C.G., Ghim S.Y., Oh T.K., Kim J.J., Park C.S., RA Park S.H.; RT "Genome sequence of the polymyxin-producing plant-probiotic RT rhizobacterium Paenibacillus polymyxa E681."; RL J. Bacteriol. 192:6103-6104(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000154; ADM71535.1; -; Genomic_DNA. DR RefSeq; YP_003872073.1; NC_014483.1. DR EnsemblBacteria; ADM71535; ADM71535; PPE_03735. DR GeneID; 9776477; -. DR KEGG; ppy:PPE_03735; -. DR PATRIC; 42413228; VBIPaePol94484_3733. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MLARYFI; -. DR BioCyc; PPOL349520:GH6J-3718-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 237 AA; 25577 MW; EB9625FDF8C08B49 CRC64; MSSRILPQMM RQHLQMYLVL GSVNCLAEPG WVVQEALAGG ATMVQFREKG LGALTGVPMF ELARQLQDLC RHAGVPFIIN DDVELALELD ADGVHIGQDD ESADSVRERI GNRVLGVSAH TIEEARRAIL QGADYLGVGP IYPTISKDDA HAVQGPAILY EMRKAGIDVP IVGIGGITVD RVEEVARAGA DGVAVISAVT QSEQVRGAVK ELNKNMVSFL KDPIYMFDND STDHPAF // ID E0RAR3_PAEP6 Unreviewed; 197 AA. AC E0RAR3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 21. DE SubName: Full=Regulatory protein tenI; GN OrderedLocusNames=PPE_02543; OS Paenibacillus polymyxa (strain E681). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=349520; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E681; RX PubMed=20851896; DOI=10.1128/JB.00983-10; RA Kim J.F., Jeong H., Park S.Y., Kim S.B., Park Y.K., Choi S.K., RA Ryu C.M., Hur C.G., Ghim S.Y., Oh T.K., Kim J.J., Park C.S., RA Park S.H.; RT "Genome sequence of the polymyxin-producing plant-probiotic RT rhizobacterium Paenibacillus polymyxa E681."; RL J. Bacteriol. 192:6103-6104(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000154; ADM70372.1; -; Genomic_DNA. DR RefSeq; YP_003870910.1; NC_014483.1. DR EnsemblBacteria; ADM70372; ADM70372; PPE_02543. DR GeneID; 9775295; -. DR KEGG; ppy:PPE_02543; -. DR PATRIC; 42410840; VBIPaePol94484_2555. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR BioCyc; PPOL349520:GH6J-2536-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 197 AA; 21075 MW; DE70EAFD255696F6 CRC64; MEKGTFAQAA QVAAVICPYV HYVHARLKQN GASALLSLTR SMVEQGVPLQ QIVVNDRVDV ALLTLVGAVQ LPANGLPVAD VKSLLPKGTR FGVSVHSLEE AQTAERAGAD YVLYGHVYET HCKPGIVPRG LAQLEPICRL SNIPVIALGG IQPHHIPELY RAGVSGIAVM SGIWETESPV AAAMEYRRMA DLVVHSL // ID E0RNC0_SPITD Unreviewed; 383 AA. AC E0RNC0; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=STHERM_c01440; OS Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta. OX NCBI_TaxID=665571; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 6192; RA Angelov A., Mientus M., Wittenberg S., Lehmann R., Liesegang H., RA Daniel R., Liebl W.; RT "The genome sequence of Spirochaeta thermophila DSM6192."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1; RX PubMed=20935097; DOI=10.1128/JB.01023-10; RA Angelov A., Liebl S., Ballschmiter M., Bomeke M., Lehmann R., RA Liesegang H., Daniel R., Liebl W.; RT "Genome sequence of the polysaccharide-degrading, thermophilic RT anaerobe Spirochaeta thermophila DSM 6192."; RL J. Bacteriol. 192:6492-6493(2010). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001698; ADN01120.1; -; Genomic_DNA. DR RefSeq; YP_003873393.1; NC_014484.1. DR EnsemblBacteria; ADN01120; ADN01120; STHERM_c01440. DR GeneID; 9755398; -. DR KEGG; sta:STHERM_c01440; -. DR PATRIC; 42519485; VBISpiThe146732_0146. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; NCARVEE; -. DR BioCyc; STHE665571:GI3Y-144-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 383 AA; 42784 MW; 039FA39D5CFA94A8 CRC64; MRGLYRMLDA NWNRAAEGLR VLEDVARFVW NDGPLAERLK GMRHRVRGVL REREGLMAGA RDVEGDVGKG MGVRGDGREG LEGLVRGNCA RVEEALRSME EALRSMGLER EAGVCEEVRY GMYEVEGRLA GWLRRVRVAR AFDGGVYAIT AEEYSRGRGN LRVMREALEG GARIVQYREK EKSYRAMYEE ARALRELCRE YGALFVVNDH VELALMVEAD GVHVGQDDWP VEEVRRVVGP GMVVGLSTHG PAQAQAAVER GVVDYIGVGP VFPTSTKKDV CAPVGLEYVA YASREVRIPW VAIGGIKEHN LDAVCELGAR CVAMVTEIVG AEDVRGKVRR VRERVEGWRG RAPAPRWVRE WEAVLARQEA PTDQRRPTGE EEL // ID E0S1U5_BUTPB Unreviewed; 210 AA. AC E0S1U5; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-APR-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=bpr_I1028; OS Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316) OS (Clostridium proteoclasticum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=515622; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51982 / DSM 14932 / B316; RX PubMed=20689770; DOI=10.1371/journal.pone.0011942; RA Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., RA Kong Z., Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., RA Attwood G.T.; RT "The Glycobiome of the Rumen Bacterium Butyrivibrio proteoclasticus RT B316 Highlights Adaptation to a Polysaccharide-Rich Environment."; RL PLoS ONE 5:E11942-E11942(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001810; ADL33770.1; -; Genomic_DNA. DR RefSeq; YP_003830352.1; NC_014387.1. DR EnsemblBacteria; ADL33770; ADL33770; bpr_I1028. DR GeneID; 9574683; -. DR KEGG; bpb:bpr_I1028; -. DR PATRIC; 42221331; VBIButPro41874_1038. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR BioCyc; BPRO515622:GHKV-1053-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22740 MW; 0AAE67B476FE0DEC CRC64; MNTQLYLVTD STGLSEDEFL KKVENAILGG VTILQLREKD KTTREYIDLG RKVHEITAKY DIPLIIDDRI DVAMAIDAEG VHLGQSDMPV DIARKILGKN KIIGATTKTV EQALEAYRNG ADYLGVGAIY PTTTKVKTVL TSVDTLRDIC KAVPIPANAI GGLNKDNIQV LKGVPIAGIC VVTAIMKAPD SRTAASELKR AYEELNMAGK // ID E0SGG8_DICD3 Unreviewed; 211 AA. AC E0SGG8; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dda3937_00234; OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Dickeya. OX NCBI_TaxID=198628; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3937; RX PubMed=21217001; DOI=10.1128/JB.01513-10; RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N., RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., RA Expert D., Plunkett G.III., San Francisco M.J., Charkowski A.O., RA Py B., Bell K., Rauscher L., Rodriguez-Palenzuela P., Toussaint A., RA Holeva M.C., He S.Y., Douet V., Boccara M., Blanco C., Toth I., RA Anderson B.D., Biehl B.S., Mau B., Flynn S.M., Barras F., RA Lindeberg M., Birch P.R., Tsuyumu S., Shi X., Hibbing M., Yap M.N., RA Carpentier M., Dassa E., Umehara M., Kim J.F., Rusch M., Soni P., RA Mayhew G.F., Fouts D.E., Gill S.R., Blattner F.R., Keen N.T., RA Perna N.T.; RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii RT 3937."; RL J. Bacteriol. 193:2076-2077(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002038; ADM96454.1; -; Genomic_DNA. DR RefSeq; YP_003881011.1; NC_014500.1. DR EnsemblBacteria; ADM96454; ADM96454; Dda3937_00234. DR GeneID; 9731631; -. DR KEGG; ddd:Dda3937_00234; -. DR PATRIC; 42312799; VBIDicDad25310_0246. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; DDAD198628:GHFQ-245-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22729 MW; 714693AF4A0032A3 CRC64; MNGAFPATDA RLGLYPVVDS VEWIERLLGA GVHTIQLRIK DQPADQAEPD IIRSIALGRR YQARLFINDY WQLAVKHQAY GVHLGQEDLD TADLDAIRAA GLRLGVSTHD DAELARAVAI KPSYIALGHI FPTQTKAMPS APQGLVELAR HIRALDGRFP TVAIGGISID RVPAVLETGV GSIAVVSAIT QAADWRAATA TLLRLTEGRE A // ID E0SXH5_STRZA Unreviewed; 209 AA. AC E0SXH5; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; Synonyms=thiE; OrderedLocusNames=SPAP_0694; OS Streptococcus pneumoniae (strain AP200). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=574093; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AP200; RA Camilli R., Bonnal R.J.P., Iacono M., Corti G., Rizzi E., RA Del Grosso M., Mulas L., Marchetti M., Iannelli F., Superti F., RA De Bellis G., Oggioni M.R., Pantosti A.; RT "Complete genome sequence of Streptococcus pneumoniae strain AP200."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002121; ADM84287.1; -; Genomic_DNA. DR RefSeq; YP_003876289.1; NC_014494.1. DR ProteinModelPortal; E0SXH5; -. DR EnsemblBacteria; ADM84287; ADM84287; SPAP_0694. DR GeneID; 9726710; -. DR KEGG; snp:SPAP_0694; -. DR PATRIC; 42436129; VBIStrPne98725_0742. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SPNE574093:GHDB-693-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID E0SXI2_STRZA Unreviewed; 210 AA. AC E0SXI2; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; OrderedLocusNames=SPAP_0701; OS Streptococcus pneumoniae (strain AP200). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=574093; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AP200; RA Camilli R., Bonnal R.J.P., Iacono M., Corti G., Rizzi E., RA Del Grosso M., Mulas L., Marchetti M., Iannelli F., Superti F., RA De Bellis G., Oggioni M.R., Pantosti A.; RT "Complete genome sequence of Streptococcus pneumoniae strain AP200."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002121; ADM84294.1; -; Genomic_DNA. DR RefSeq; YP_003876296.1; NC_014494.1. DR ProteinModelPortal; E0SXI2; -. DR EnsemblBacteria; ADM84294; ADM84294; SPAP_0701. DR GeneID; 9726717; -. DR KEGG; snp:SPAP_0701; -. DR PATRIC; 42436143; VBIStrPne98725_0749. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SPNE574093:GHDB-700-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; AEAC90751A95738D CRC64; MNREALRLYL VTNRYQDSVE SFLAKIETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID E0T5S9_EDWTF Unreviewed; 214 AA. AC E0T5S9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ETAF_0150; OS Edwardsiella tarda (strain FL6-60). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Edwardsiella. OX NCBI_TaxID=718251; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FL6-60; RA van Soest J.J., Henkel C.V., Jansen H.J., van den Hondel C.A.M.J.J., RA Bloemberg G.V., Meijer A.H., Spaink H.P.; RT "Genome comparisons of Edwardsiella bacteria analysed using deep RT sequencing technology."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002154; ADM40273.1; -; Genomic_DNA. DR RefSeq; YP_005697765.1; NC_017309.1. DR ProteinModelPortal; E0T5S9; -. DR EnsemblBacteria; ADM40273; ADM40273; ETAF_0150. DR GeneID; 12858015; -. DR KEGG; etd:ETAF_0150; -. DR PATRIC; 42914730; VBIEdwTar147555_0151. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; ETAR718251:GLCN-162-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23306 MW; BA231F8E66A67581 CRC64; MRQPLFAPVP TRLGLYPVVD SVEWIERLLR AGVRTLQLRI KDCREDQIGD ELAQAIALGH HYQARLFIND YWRQAIRLGA YGVHLGQEDL DRADLAAIRR AGLRLGLSTH DDAEMDRALA AGPSYVALGH VFPTDSKQMA TAPQGLSDLR RQVARLGTYP SVAIGGISIA RVPDVLACGV GSIALVSAIT RAPDWLAATD TLLQLIEGRH ANDA // ID E0TCN2_PARBH Unreviewed; 213 AA. AC E0TCN2; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PB2503_02722; OS Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC OS 12087). OC Bacteria; Proteobacteria; Alphaproteobacteria; Parvularculales; OC Parvularculaceae; Parvularcula. OX NCBI_TaxID=314260; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087; RA Kang D.-M., Oh H.-M., Cho J.-C.; RT "Genome sequence of Parvularcula bermudensis HTCC2503."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002156; ADM08621.1; -; Genomic_DNA. DR RefSeq; YP_003853762.1; NC_014414.1. DR ProteinModelPortal; E0TCN2; -. DR EnsemblBacteria; ADM08621; ADM08621; PB2503_02722. DR GeneID; 9708786; -. DR KEGG; pbr:PB2503_02722; -. DR PATRIC; 42425021; VBIParBer119301_0454. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IGRTCHG; -. DR BioCyc; PBER314260:GI0G-452-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22264 MW; 2BAE3D0574171ED7 CRC64; MADRALYLIT PNFSDSAAFC SELDAALRAA AKDDIPVACV QLRLKEKSDE VILAAATAVR EVTAAHGVAF LVNDRADLAA RLSADGVHLG QQDGDIGEAR RLLGEEADIG VTCHASRHLA MIAAEEGADY VAFGAFYPSE TKDSQYRAEL SLVEDWTLMT TMPCVAIGGL TAENSAPVLA AGADYLAVCG AVFAHPEGAA AGIRKFAPLF GHA // ID E0TFA3_PARBH Unreviewed; 219 AA. AC E0TFA3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=PB2503_04732; OS Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC OS 12087). OC Bacteria; Proteobacteria; Alphaproteobacteria; Parvularculales; OC Parvularculaceae; Parvularcula. OX NCBI_TaxID=314260; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087; RA Kang D.-M., Oh H.-M., Cho J.-C.; RT "Genome sequence of Parvularcula bermudensis HTCC2503."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002156; ADM09021.1; -; Genomic_DNA. DR RefSeq; YP_003854163.1; NC_014414.1. DR ProteinModelPortal; E0TFA3; -. DR EnsemblBacteria; ADM09021; ADM09021; PB2503_04732. DR GeneID; 9709187; -. DR KEGG; pbr:PB2503_04732; -. DR PATRIC; 42425835; VBIParBer119301_0861. DR KO; K00788; -. DR BioCyc; PBER314260:GI0G-856-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 219 AA; 24056 MW; 68DFAC9BA71B18D5 CRC64; MADIAHNVRH LSQLAWRLRN AAPPRRGALP PFALALFTDD RRQGDLCQVM SRLPSARALK GPVAVIFRHY GLDDPTRRGL FCRLIPILES RGHLLFCAGR GGPPWPNRHA THGRHRTSWP VHDLRQGHQG RLAYSDLGYV SPIFPTASHP DRAPLGPLRG ARIAAALPYP CFALGGIDLE TGRRLVGLPF WGIGVIGALT APRRDRSSEP DSAFEQKGG // ID E0TLY6_STRZ6 Unreviewed; 209 AA. AC E0TLY6; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; Synonyms=thiE; OrderedLocusNames=SP670_0767; OS Streptococcus pneumoniae (strain 670-6B). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=189423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=670-6B; RA Neuendorf B., Radune D., Fedorova N.B., Khouri H.M., Dodson R.J., RA Daugherty S.C., Hollingshead S., Tettelin H.; RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae RT and closely related species."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002176; ADM90835.1; -; Genomic_DNA. DR RefSeq; YP_003878935.1; NC_014498.1. DR ProteinModelPortal; E0TLY6; -. DR EnsemblBacteria; ADM90835; ADM90835; SP670_0767. DR GeneID; 9729489; -. DR KEGG; snb:SP670_0767; -. DR PATRIC; 42515642; VBIStrPne54539_0817. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SPNE189423:GHX7-765-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID E0TLZ3_STRZ6 Unreviewed; 210 AA. AC E0TLZ3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; OrderedLocusNames=SP670_0774; OS Streptococcus pneumoniae (strain 670-6B). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=189423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=670-6B; RA Neuendorf B., Radune D., Fedorova N.B., Khouri H.M., Dodson R.J., RA Daugherty S.C., Hollingshead S., Tettelin H.; RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae RT and closely related species."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002176; ADM90842.1; -; Genomic_DNA. DR RefSeq; YP_003878942.1; NC_014498.1. DR ProteinModelPortal; E0TLZ3; -. DR EnsemblBacteria; ADM90842; ADM90842; SP670_0774. DR GeneID; 9729496; -. DR KEGG; snb:SP670_0774; -. DR PATRIC; 42515656; VBIStrPne54539_0824. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; SPNE189423:GHX7-772-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID E0TW79_BACPZ Unreviewed; 220 AA. AC E0TW79; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BSUW23_18935; OS Bacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472 OS / W23). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=655816; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23059 / NRRL B-14472 / W23; RA Zeigler D.R.; RT "Complete genome sequence of Bacillus subtilis subsp. spizizenii str. RT W23."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=W23; RA Zeigler D.R.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002183; ADM39821.1; -; Genomic_DNA. DR RefSeq; YP_003868130.1; NC_014479.1. DR ProteinModelPortal; E0TW79; -. DR EnsemblBacteria; ADM39821; ADM39821; BSUW23_18935. DR GeneID; 9724794; -. DR KEGG; bss:BSUW23_18935; -. DR PATRIC; 42193828; VBIBacSub57968_3862. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; BSUB655816:GCOR-3864-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23652 MW; 31370F7877001EA7 CRC64; MTRISREMMK ELLSVYFIMG SNNTKADPVT VVQKALKGGA TLYQFREKGG DALTGEARIE FAKKVQEACR EAGIPFIVND DVELALKLKA DGIHIGQEDA NAKEVRDAIG DMILGVSTHT MSEVKQAEED GADYVGLGPI YPTETKKDTR AVQGVSLIEA VRRQGIDIPI VGIGGITIEN AAPVIQAGAD GVSMISAISQ AEDPEGAARK FHEEVQTPRR // ID E0TZK7_BACPZ Unreviewed; 205 AA. AC E0TZK7; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Inhibitor of thiaminase TenA; GN Name=tenI; OrderedLocusNames=BSUW23_05895; OS Bacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472 OS / W23). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=655816; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23059 / NRRL B-14472 / W23; RA Zeigler D.R.; RT "Complete genome sequence of Bacillus subtilis subsp. spizizenii str. RT W23."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=W23; RA Zeigler D.R.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002183; ADM37232.1; -; Genomic_DNA. DR RefSeq; YP_003865541.1; NC_014479.1. DR EnsemblBacteria; ADM37232; ADM37232; BSUW23_05895. DR GeneID; 9722170; -. DR KEGG; bss:BSUW23_05895; -. DR PATRIC; 42188459; VBIBacSub57968_1204. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR BioCyc; BSUB655816:GCOR-1240-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 22812 MW; BEC01EECADB3107E CRC64; MELHAITDDC KPVEELARAI IAIRNEVDFI HIRERSKSAA DILKLLGLIS EGGVDKRKLI MNGRVDIALF STIHRVQLPS SSFSPKQVRA RFPHLHIGRS VHSLEEAVQA EKEDADYVLF GHVFETDCKK GLEGRGVSLL SDIKQRISVP VIAIGGMTPD RLRDVKRAGA EGIAVMSGIF SSADPLEAAR RYSRKLKEMR YEKAL // ID E0UJG1_CYAP2 Unreviewed; 368 AA. AC E0UJG1; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cyan7822_5094; OS Cyanothece sp. (strain PCC 7822). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=497965; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7822; RX PubMed=21972240; DOI=10.1128/mBio.00214-11; RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., RA Min H., Sherman L.A., Pakrasi H.B.; RT "Novel metabolic attributes of the genus Cyanothece, comprising a RT group of unicellular nitrogen-fixing Cyanobacteria."; RL MBio 2:E214-E214(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002198; ADN16979.1; -; Genomic_DNA. DR RefSeq; YP_003890254.1; NC_014501.1. DR ProteinModelPortal; E0UJG1; -. DR EnsemblBacteria; ADN16979; ADN16979; Cyan7822_5094. DR GeneID; 9741599; -. DR KEGG; cyj:Cyan7822_5094; -. DR PATRIC; 42291183; VBICyaSp18455_5322. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR BioCyc; CSP497965:GJAC-5146-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 129 Unknown (By similarity). FT REGION 130 368 Thiamine-phosphate synthase (By FT similarity). FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 368 AA; 41442 MW; 413268FF28FCDDD8 CRC64; MEEQYSQIRG QQSAIQRILD ANLDRAREGL RIIEEWCRFG LNHSQLAEQC KEMRQELARW HSTELRMARD TPGDPGTALT HPQEETRSSI EHLLQANLCR IEEALRVLEE YGKLYNPEMG IVFKQMRYRA YTLESHLLVY RRHQKLRESL LYLVTCPHEN IFAVVEAALS AGLTLVQYRD KETEDLSRLS IAYKLSQLCY DYGALFIVND RVDLALAVNA DGVHLGQQDM PIALAREILG SQKIIGRSTT NPQEMQQAIA EGADYIGVGP VYETPTKAGK AAAGLEYVRY AAKNSSLPWF AIGGIDTANI KDVLTAGAQR VSVVRAIMQA EQPALITGQL LSLLTRKRTF PQLQPKTNVL TINESTEK // ID E0USD8_SULAO Unreviewed; 187 AA. AC E0USD8; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Saut_1052; OS Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 OS / OK10). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Sulfurimonas. OX NCBI_TaxID=563040; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10; RX DOI=10.4056/sigs.1173118; RA Sikorski J., Munk C., Lapidus A., Djao O., Lucas S., RA Glavina Del Rio T., Nolan M., Tice H., Han C., Cheng J., Tapia R., RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Sims D., Meincke L., Brettin T., Detter J., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., RA Rohde M., Lang E., Spring S., Goker M., Woyke T., Bristow J., RA Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H.; RT "Complete genome sequence of Sulfurimonas autotrophica type strain RT (OK10T)."; RL Stand. Genomic Sci. 3:194-202(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002205; ADN09101.1; -; Genomic_DNA. DR RefSeq; YP_003892113.1; NC_014506.1. DR EnsemblBacteria; ADN09101; ADN09101; Saut_1052. DR GeneID; 9758594; -. DR KEGG; sua:Saut_1052; -. DR PATRIC; 42441712; VBISulAut92361_1061. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NADIAFI; -. DR BioCyc; SAUT563040:GH0V-1085-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 187 AA; 21013 MW; A7FA59D69A64D095 CRC64; MRLYALCDQD MLNEKGISLE TFLDIAKSHN AEVIQYRNKN ADIAFIKEQL IKIRQQYDGF LIVNDAYELV EFCDGVHVGQ EDLKKIDEDV LKAVKILRSV IKEDKILGIS THNEQEVLKA NTMDLNYIGL GAYRNTSTKK DIINVLGESL DTIAAKSKHH VAAIGGVKLH DKFEHAVYNV IGSGLLK // ID E0UTV0_SULAO Unreviewed; 171 AA. AC E0UTV0; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Saut_1347; OS Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 OS / OK10). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Sulfurimonas. OX NCBI_TaxID=563040; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10; RX DOI=10.4056/sigs.1173118; RA Sikorski J., Munk C., Lapidus A., Djao O., Lucas S., RA Glavina Del Rio T., Nolan M., Tice H., Han C., Cheng J., Tapia R., RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Sims D., Meincke L., Brettin T., Detter J., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., RA Rohde M., Lang E., Spring S., Goker M., Woyke T., Bristow J., RA Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H.; RT "Complete genome sequence of Sulfurimonas autotrophica type strain RT (OK10T)."; RL Stand. Genomic Sci. 3:194-202(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002205; ADN09394.1; -; Genomic_DNA. DR RefSeq; YP_003892406.1; NC_014506.1. DR EnsemblBacteria; ADN09394; ADN09394; Saut_1347. DR GeneID; 9758891; -. DR KEGG; sua:Saut_1347; -. DR PATRIC; 42442302; VBISulAut92361_1354. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGYSAH; -. DR BioCyc; SAUT563040:GH0V-1382-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 171 AA; 19242 MW; 0D5241359D6A4033 CRC64; MKKYLITANP SYFQLRKYMP DFALYRDKEN KNYADEAQNF VQMCKPLKIL KVFLHQDYEL AAKLGAHGVH LTSKQFDEIP KAKELGLEVI ISTHTHDEVH VAEAMGADYV TYSPVFASPD KGEPKGVEDL QSIVSMTDVK IFALGGIISQ KEVDAVANTD AYGFASIRYF L // ID E0WV56_9ENTR Unreviewed; 232 AA. AC E0WV56; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=REG_1971; OS Candidatus Regiella insecticola LSR1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; aphid secondary symbionts; Candidatus Regiella. OX NCBI_TaxID=663321; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LSR1; RX PubMed=19840097; RA Degnan P.H., Leonardo T.E., Cass B.N., Hurwitz B., Stern D., RA Gibbs R.A., Richards S., Moran N.A.; RT "Dynamics of genome evolution in facultative symbionts of aphids."; RL Environ. Microbiol. 0:0-0(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL379746; EFL91106.1; -; Genomic_DNA. DR EnsemblBacteria; EFL91106; EFL91106; REG_1971. DR PATRIC; 40950468; VBICanReg142427_2465. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT REGION 204 205 THZ-P binding (By similarity). FT METAL 88 88 Magnesium (By similarity). FT METAL 107 107 Magnesium (By similarity). FT BINDING 87 87 HMP-PP (By similarity). FT BINDING 126 126 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 184 184 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 232 AA; 25226 MW; 66C40ABBD52CD301 CRC64; MNCIRQQSIY RQGQPMNLPD APFANTSCRL GLYPVVDSLT WINRMLDSGV TSLQLRIKHL AAIQLEKTIV SAISLSQQYP DAKLFINDYW QLAIKHQAYG VHLGQEDLST ADLSAMQAAG LRLGISTHDE QELAQARQIR PSYIALGHIF PTQTKQMPSS PQGLAALKRQ VKNTPDYPTV AIGGISIERV LPVLACGVGG VAVVSAITKA ADWRQATAAL LRLIENQGIA DG // ID E0XQV4_9GAMM Unreviewed; 208 AA. AC E0XQV4; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase; OS uncultured gamma proteobacterium HF0010_11K06. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=710980; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=20695878; DOI=10.1111/j.1462-2920.2010.02314.x; RA Rich V.I., Pham V.D., Eppley J., Shi Y., DeLong E.F.; RT "Time-series analyses of Monterey Bay coastal microbial picoplankton RT using a 'genome proxy' microarray."; RL Environ. Microbiol. 13:116-134(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GU474847; ADI16795.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 208 AA; 23678 MW; C19424CE8D89F069 CRC64; MIQGLYAITP SGLEENDLLT KTEVLLKEGI KLIQYRDKIL DKKTLQEKAH ALLKLTKKYG AKLLINDHVE ICLEISADGF HLGLEDYLYE GNIELLKKNK EFISKKLICG LSCKWNKELV VNPPENEIKW TYLAVGSFYP SNTKSTIPET NENVKRKFLS YTDKPLVAIG GINKKNIGEV RSLGYSCFAL SEALFINPKH VLNEYKRL // ID E0XRR9_9GAMM Unreviewed; 70 AA. AC E0XRR9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 06-MAR-2013, entry version 8. DE SubName: Full=Putative uncharacterized protein; OS uncultured gamma proteobacterium HF0070_03O15. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=710982; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=20695878; DOI=10.1111/j.1462-2920.2010.02314.x; RA Rich V.I., Pham V.D., Eppley J., Shi Y., DeLong E.F.; RT "Time-series analyses of Monterey Bay coastal microbial picoplankton RT using a 'genome proxy' microarray."; RL Environ. Microbiol. 13:116-134(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GU474854; ADI17110.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. PE 4: Predicted; SQ SEQUENCE 70 AA; 8052 MW; 987340C9B0A969C1 CRC64; MLAKELGCDY VFLSPIIKKY DSEPIGWDNF FEIKNIFSEI KVIPLGGISE KNSMQDSFAG ISHWWDLQNP // ID E0XVV6_9GAMM Unreviewed; 311 AA. AC E0XVV6; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; OS uncultured gamma proteobacterium HF4000_23L14. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=710988; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=20695878; DOI=10.1111/j.1462-2920.2010.02314.x; RA Rich V.I., Pham V.D., Eppley J., Shi Y., DeLong E.F.; RT "Time-series analyses of Monterey Bay coastal microbial picoplankton RT using a 'genome proxy' microarray."; RL Environ. Microbiol. 13:116-134(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GU474893; ADI18547.1; -; Genomic_DNA. DR ProteinModelPortal; E0XVV6; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 311 AA; 34925 MW; AFA8E264ACD1F272 CRC64; MSSNKKIIVE EVVVGILLNK NGQILVAKRR NNQFMPSYWE LPGGKIKAGE NKKDSLKREL SEELGVTVNK SSLKHTMFHQ YPNKVVKLWI YNVDKYSGEP SGQEGQDTSW CSLDQLNNYK LLPTMRVIVH KISLPEHYWI TPDDHHSESV IEKCREHLIA GTMIVQLRSK VSLDHTYIDK VYKLCQDYQA SLILNTPNKT YQELCDGWHL TSNELLSLKE RPCDNNKLLG VSTHNALEAE YAENISADYI SLSPVNSTPS HPDIPPLGWQ VASDIISKSN LPVYLLGGMS KEVLDKALSI GAQGVAGISQ I // ID E1CYI1_VIBPH Unreviewed; 444 AA. AC E1CYI1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=VIPARP466_2979; OS Vibrio parahaemolyticus Peru-466. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=563771; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Peru-466; RA Gill A., Ramamurthy T., Nair G.B., Stine O.C., Durkin A.S., RA Fouts D.E.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Peru-466; RX PubMed=21645368; DOI=10.1186/1471-2164-12-294; RA Chen Y., Stine O.C., Badger J.H., Gil A.I., Nair G.B., Nishibuchi M., RA Fouts D.E.; RT "Comparative genomic analysis of Vibrio parahaemolyticus: serotype RT conversion and virulence."; RL BMC Genomics 12:294-294(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFM01000080; EFO38643.1; -; Genomic_DNA. DR ProteinModelPortal; E1CYI1; -. DR EnsemblBacteria; EFO38643; EFO38643; VIPARP466_2979. DR PATRIC; 28374609; VBIVibPar126771_2795. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 444 AA; 49173 MW; BFD241E09C3971C7 CRC64; MAKILIPSSL IPLTGAVLQC LLLAKEQGFS IDEIELGVSP TQFIQLVLGQ NTFRVGTDLI DVCEEAETAD FVLYYQSGLS VSECRQQPSS AIFIGIQDVE SKLDDSVKTT SADVLDIWRH PVNDEIRALS VASTSRTTTL QTDQHLAWTV TLLALDFPIE DALTLARPMT NVSRETLING ETMVKQEWAS QFADFPTPVL EDCRLGIKVG WSSHGQSVNF PHLSKQSLGL YPVVDDVSWI ERLLPLGINT IQLRIKDPYQ PDLEQQIARA IELGRQYDAQ VFINDYWQLA IKHGAFGVHL GQEDIEDSNL SQLSTAGICL GLSTHGYYEL LRIVQINPSY IALGHIFSTT TKQMPSKPQG LVRLALYQKL NDSIPYGESV GYPTVAIGGI DQSNAEQVWQ CGVSSLAVVR AITLSESPKQ VIEFFDQLMN TTSTSLVMED YRAY // ID E1D233_VIBPH Unreviewed; 204 AA. AC E1D233; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VIPARP466_A0115; OS Vibrio parahaemolyticus Peru-466. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=563771; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Peru-466; RA Gill A., Ramamurthy T., Nair G.B., Stine O.C., Durkin A.S., RA Fouts D.E.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Peru-466; RX PubMed=21645368; DOI=10.1186/1471-2164-12-294; RA Chen Y., Stine O.C., Badger J.H., Gil A.I., Nair G.B., Nishibuchi M., RA Fouts D.E.; RT "Comparative genomic analysis of Vibrio parahaemolyticus: serotype RT conversion and virulence."; RL BMC Genomics 12:294-294(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFM01000139; EFO34639.1; -; Genomic_DNA. DR ProteinModelPortal; E1D233; -. DR EnsemblBacteria; EFO34639; EFO34639; VIPARP466_A0115. DR PATRIC; 28377225; VBIVibPar126771_4040. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21796 MW; 30ED16DCD5F62066 CRC64; MNAYRLYLVT DDQQDLPTLK HVVRKAVEGG VTMVQVREKH GDVREFIERA QAVKTILEGT GVPLIINDRV DVALAVDADG VHLGQSDMPA EIARQLIGPN KILGLSIETE DQLAEADSLP IDYIGLSAIF ATPTKTNTKK HWGIGGLKMA LNTTSLPIVA IGGINETNIP ALSATGVHGL ALVSAICHAE NPTKAAEYLL SLMD // ID E1DA66_VIBPH Unreviewed; 444 AA. AC E1DA66; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=VIPARAQ4037_0967; OS Vibrio parahaemolyticus AQ4037. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=563772; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AQ4037; RA Ramamurthy T., Nair G.B., Stine O.C., Durkin A.S., Fouts D.E.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AQ4037; RX PubMed=21645368; DOI=10.1186/1471-2164-12-294; RA Chen Y., Stine O.C., Badger J.H., Gil A.I., Nair G.B., Nishibuchi M., RA Fouts D.E.; RT "Comparative genomic analysis of Vibrio parahaemolyticus: serotype RT conversion and virulence."; RL BMC Genomics 12:294-294(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFN01000075; EFO44706.1; -; Genomic_DNA. DR ProteinModelPortal; E1DA66; -. DR EnsemblBacteria; EFO44706; EFO44706; VIPARAQ4037_0967. DR PATRIC; 28354552; VBIVibPar20386_2264. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 444 AA; 49239 MW; 4A6F227B445DFBFF CRC64; MAKILIPSSL IPLTGAVLQC LLLAKEQGFS IDEIELGVSP TQFIQLVLGQ NTFRVGTDLI DVCEEAETAD FVLYYQSGLS VSECRQQPSS AIFIGIEDVE SKHDNSVETT SADVLDIWRH PINDEIRALS VASTSRTTTL QTDQHLAWMV TLLALDFPIE DALTLARPMT NVSRETLING ETMVKQEWAS QFADFPTPVL EDCRLGIKVG WSSYGQSVNF PHLSKQSLGL YPVVDDVSWI ERLLPLGINT IQLRIKDPYQ SDLEQQIARA IELGRQYDAQ VFINDYWQLA IKHGAFGVHL GQEDIEDSNL SQLSTAGICL GLSTHGYYEL LRIVQINPSY IALGHIFPTT TKQMPSKPQG LVRLALYQKL IDSIPYGESV GYPTVAIGGI DQSNAEQVWQ CGVSSLAVVR AITLSKSPKQ VIEFFDQLMS TTSTSLVMED YRAY // ID E1DCU4_VIBPH Unreviewed; 204 AA. AC E1DCU4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VIPARAQ4037_A0091; OS Vibrio parahaemolyticus AQ4037. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=563772; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AQ4037; RA Ramamurthy T., Nair G.B., Stine O.C., Durkin A.S., Fouts D.E.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AQ4037; RX PubMed=21645368; DOI=10.1186/1471-2164-12-294; RA Chen Y., Stine O.C., Badger J.H., Gil A.I., Nair G.B., Nishibuchi M., RA Fouts D.E.; RT "Comparative genomic analysis of Vibrio parahaemolyticus: serotype RT conversion and virulence."; RL BMC Genomics 12:294-294(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFN01000103; EFO48089.1; -; Genomic_DNA. DR ProteinModelPortal; E1DCU4; -. DR EnsemblBacteria; EFO48089; EFO48089; VIPARAQ4037_A0091. DR PATRIC; 28356467; VBIVibPar20386_3189. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21906 MW; 26884BC204704564 CRC64; MNAYRLYLVT DDQQDLPTLK HVVRKAVEGG VTMVQVREKH GDVREFIERA QAVKTILEGT GVPLIINDRV DVALAVDADG VHLGQSDMPA EIARQLIGPN KILGLSIETE DQLAEVDSLP IDYIGLSAIF ATPTKTNTKK HWGIEGLKMA LNTTPLPIVA IGGINETNIP ALSATGVHGL ALVSAICHAE NPTKAAEYLL SLMD // ID E1DJF7_VIBPH Unreviewed; 444 AA. AC E1DJF7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=VIPARAN5034_2168; OS Vibrio parahaemolyticus AN-5034. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=563773; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AN-5034; RA Gill A., Ramamurthy T., Nair G.B., Stine O.C., Durkin A.S., RA Fouts D.E.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AN-5034; RX PubMed=21645368; DOI=10.1186/1471-2164-12-294; RA Chen Y., Stine O.C., Badger J.H., Gil A.I., Nair G.B., Nishibuchi M., RA Fouts D.E.; RT "Comparative genomic analysis of Vibrio parahaemolyticus: serotype RT conversion and virulence."; RL BMC Genomics 12:294-294(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFO01000010; EFO43840.1; -; Genomic_DNA. DR ProteinModelPortal; E1DJF7; -. DR EnsemblBacteria; EFO43840; EFO43840; VIPARAN5034_2168. DR PATRIC; 28342150; VBIVibPar136058_1016. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 444 AA; 49173 MW; BFD241E09C3971C7 CRC64; MAKILIPSSL IPLTGAVLQC LLLAKEQGFS IDEIELGVSP TQFIQLVLGQ NTFRVGTDLI DVCEEAETAD FVLYYQSGLS VSECRQQPSS AIFIGIQDVE SKLDDSVKTT SADVLDIWRH PVNDEIRALS VASTSRTTTL QTDQHLAWTV TLLALDFPIE DALTLARPMT NVSRETLING ETMVKQEWAS QFADFPTPVL EDCRLGIKVG WSSHGQSVNF PHLSKQSLGL YPVVDDVSWI ERLLPLGINT IQLRIKDPYQ PDLEQQIARA IELGRQYDAQ VFINDYWQLA IKHGAFGVHL GQEDIEDSNL SQLSTAGICL GLSTHGYYEL LRIVQINPSY IALGHIFSTT TKQMPSKPQG LVRLALYQKL NDSIPYGESV GYPTVAIGGI DQSNAEQVWQ CGVSSLAVVR AITLSESPKQ VIEFFDQLMN TTSTSLVMED YRAY // ID E1DUT1_VIBPH Unreviewed; 204 AA. AC E1DUT1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VIPARAN5034_A1408; OS Vibrio parahaemolyticus AN-5034. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=563773; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AN-5034; RA Gill A., Ramamurthy T., Nair G.B., Stine O.C., Durkin A.S., RA Fouts D.E.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AN-5034; RX PubMed=21645368; DOI=10.1186/1471-2164-12-294; RA Chen Y., Stine O.C., Badger J.H., Gil A.I., Nair G.B., Nishibuchi M., RA Fouts D.E.; RT "Comparative genomic analysis of Vibrio parahaemolyticus: serotype RT conversion and virulence."; RL BMC Genomics 12:294-294(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFO01000050; EFO42162.1; -; Genomic_DNA. DR ProteinModelPortal; E1DUT1; -. DR EnsemblBacteria; EFO42162; EFO42162; VIPARAN5034_A1408. DR PATRIC; 28349164; VBIVibPar136058_4403. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21796 MW; 30ED16DCD5F62066 CRC64; MNAYRLYLVT DDQQDLPTLK HVVRKAVEGG VTMVQVREKH GDVREFIERA QAVKTILEGT GVPLIINDRV DVALAVDADG VHLGQSDMPA EIARQLIGPN KILGLSIETE DQLAEADSLP IDYIGLSAIF ATPTKTNTKK HWGIGGLKMA LNTTSLPIVA IGGINETNIP ALSATGVHGL ALVSAICHAE NPTKAAEYLL SLMD // ID E1E201_STAAU Unreviewed; 213 AA. AC E1E201; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0773_10113; OS Staphylococcus aureus subsp. aureus TCH70. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=548475; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TCH70; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHH02000002; EFK83485.1; -; Genomic_DNA. DR ProteinModelPortal; E1E201; -. DR EnsemblBacteria; EFK83485; EFK83485; HMPREF0773_10113. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23384 MW; 8FEFB3993FF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI ENTVNRFKDF FNN // ID E1EEH8_VIBPH Unreviewed; 204 AA. AC E1EEH8; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VIPARK5030_A1748; OS Vibrio parahaemolyticus K5030. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=627611; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K5030; RA Ramamurthy T., Nair G.B., Stine O.C., Durkin A.S., Fouts D.E.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K5030; RX PubMed=21645368; DOI=10.1186/1471-2164-12-294; RA Chen Y., Stine O.C., Badger J.H., Gil A.I., Nair G.B., Nishibuchi M., RA Fouts D.E.; RT "Comparative genomic analysis of Vibrio parahaemolyticus: serotype RT conversion and virulence."; RL BMC Genomics 12:294-294(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKB01000054; EFO49599.1; -; Genomic_DNA. DR ProteinModelPortal; E1EEH8; -. DR EnsemblBacteria; EFO49599; EFO49599; VIPARK5030_A1748. DR PATRIC; 28362951; VBIVibPar56209_1783. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21796 MW; 30ED16DCD5F62066 CRC64; MNAYRLYLVT DDQQDLPTLK HVVRKAVEGG VTMVQVREKH GDVREFIERA QAVKTILEGT GVPLIINDRV DVALAVDADG VHLGQSDMPA EIARQLIGPN KILGLSIETE DQLAEADSLP IDYIGLSAIF ATPTKTNTKK HWGIGGLKMA LNTTSLPIVA IGGINETNIP ALSATGVHGL ALVSAICHAE NPTKAAEYLL SLMD // ID E1EHT6_VIBPH Unreviewed; 444 AA. AC E1EHT6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=VIPARK5030_2971; OS Vibrio parahaemolyticus K5030. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=627611; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K5030; RA Ramamurthy T., Nair G.B., Stine O.C., Durkin A.S., Fouts D.E.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K5030; RX PubMed=21645368; DOI=10.1186/1471-2164-12-294; RA Chen Y., Stine O.C., Badger J.H., Gil A.I., Nair G.B., Nishibuchi M., RA Fouts D.E.; RT "Comparative genomic analysis of Vibrio parahaemolyticus: serotype RT conversion and virulence."; RL BMC Genomics 12:294-294(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKB01000119; EFO51260.1; -; Genomic_DNA. DR ProteinModelPortal; E1EHT6; -. DR EnsemblBacteria; EFO51260; EFO51260; VIPARK5030_2971. DR PATRIC; 28365290; VBIVibPar56209_2889. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 444 AA; 49173 MW; BFD241E09C3971C7 CRC64; MAKILIPSSL IPLTGAVLQC LLLAKEQGFS IDEIELGVSP TQFIQLVLGQ NTFRVGTDLI DVCEEAETAD FVLYYQSGLS VSECRQQPSS AIFIGIQDVE SKLDDSVKTT SADVLDIWRH PVNDEIRALS VASTSRTTTL QTDQHLAWTV TLLALDFPIE DALTLARPMT NVSRETLING ETMVKQEWAS QFADFPTPVL EDCRLGIKVG WSSHGQSVNF PHLSKQSLGL YPVVDDVSWI ERLLPLGINT IQLRIKDPYQ PDLEQQIARA IELGRQYDAQ VFINDYWQLA IKHGAFGVHL GQEDIEDSNL SQLSTAGICL GLSTHGYYEL LRIVQINPSY IALGHIFSTT TKQMPSKPQG LVRLALYQKL NDSIPYGESV GYPTVAIGGI DQSNAEQVWQ CGVSSLAVVR AITLSESPKQ VIEFFDQLMN TTSTSLVMED YRAY // ID E1EQF4_ENTFL Unreviewed; 211 AA. AC E1EQF4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0347_6426; OS Enterococcus faecalis TUSoD Ef11. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=553209; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TUSoD Ef11; RA Shrivastava S., Sebastian Y., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TUSoD Ef11; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACOX02000002; EFK77105.1; -; Genomic_DNA. DR ProteinModelPortal; E1EQF4; -. DR EnsemblBacteria; EFK77105; EFK77105; HMPREF0347_6426. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID E1FGF3_9THEO Unreviewed; 211 AA. AC E1FGF3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Teth561_PD2431; OS Thermoanaerobacter sp. X561. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=588857; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=X561; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Saunders E., Detter C., Han C., Tapia R., Land M.L., RA Hauser L., Kyrpides N., Ovchinnikova G., Zhou J., Phelps T.J., RA Hemme C., Woyke T.; RT "The draft genome of Thermoanaerobacter sp. X561."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACXP02000007; EFK83563.1; -; Genomic_DNA. DR ProteinModelPortal; E1FGF3; -. DR EnsemblBacteria; EFK83563; EFK83563; Teth561_PD2431. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23018 MW; 437BD72098B68280 CRC64; MDLTLYAITD RSYIKNMDIA EAVELAIKGG ATVIQLREKD ISSREFYEIA LKVKEVTKRN RIPLIINDRV DIALAVDADG VHVGQEDLPA DIVRKIIGRD KIVGVSARTV EEALKAQRDG ADYLGVGAVF KTPTKPEAEA IGIEGLKKIK EAVTIPVVAI GGITKDNAYE VMLKSGVDGI SSVSAVFYGD IENNTRKLLE VIKKAINDRR I // ID E1H4C8_STREE Unreviewed; 210 AA. AC E1H4C8; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpBS455_10214; OS Streptococcus pneumoniae BS455. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=595501; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BS455; RA Ehrlich G.D.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHN01000092; EFL64347.1; -; Genomic_DNA. DR ProteinModelPortal; E1H4C8; -. DR EnsemblBacteria; EFL64347; EFL64347; CGSSpBS455_10214. DR PATRIC; 41061041; VBIStrPne159703_2101. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID E1H4D5_STREE Unreviewed; 209 AA. AC E1H4D5; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpBS455_10249; OS Streptococcus pneumoniae BS455. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=595501; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BS455; RA Ehrlich G.D.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHN01000092; EFL64354.1; -; Genomic_DNA. DR EnsemblBacteria; EFL64354; EFL64354; CGSSpBS455_10249. DR PATRIC; 41061055; VBIStrPne159703_2108. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23362 MW; A51A41EFBB2CC783 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID E1H5X9_MYCTX Unreviewed; 222 AA. AC E1H5X9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TMAG_01673; OS Mycobacterium tuberculosis SUMu001. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=675512; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SUMu001; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Galagan J., Pepperell C., Hoeppner V., Gagneux S., Small P., RA Schoolnik G., Feldman M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain SUMu001."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHQ01000012; EFO76258.1; -; Genomic_DNA. DR ProteinModelPortal; E1H5X9; -. DR SMR; E1H5X9; 1-221. DR EnsemblBacteria; EFO76258; EFO76258; TMAG_01673. DR PATRIC; 41393659; VBIMycTub143957_0363. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID E1HMQ9_ECOLX Unreviewed; 211 AA. AC E1HMQ9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9543_02359; OS Escherichia coli MS 146-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749540; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 146-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTN01000143; EFK90806.1; -; Genomic_DNA. DR ProteinModelPortal; E1HMQ9; -. DR SMR; E1HMQ9; 20-202. DR EnsemblBacteria; EFK90806; EFK90806; HMPREF9543_02359. DR PATRIC; 41789284; VBIEscCol151630_2259. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E1HXE5_ECOLX Unreviewed; 211 AA. AC E1HXE5; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9535_00752; OS Escherichia coli MS 78-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749532; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 78-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTY01000058; EFK75250.1; -; Genomic_DNA. DR ProteinModelPortal; E1HXE5; -. DR SMR; E1HXE5; 20-202. DR EnsemblBacteria; EFK75250; EFK75250; HMPREF9535_00752. DR PATRIC; 41837663; VBIEscCol151935_0712. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E1IXI3_ECOLX Unreviewed; 211 AA. AC E1IXI3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9348_04940; OS Escherichia coli MS 145-7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=679204; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 145-7; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWS01000043; EFO55971.1; -; Genomic_DNA. DR ProteinModelPortal; E1IXI3; -. DR SMR; E1IXI3; 10-208. DR EnsemblBacteria; EFO55971; EFO55971; HMPREF9348_04940. DR PATRIC; 42101842; VBIEscCol143813_4754. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E1J1M0_ECOLX Unreviewed; 211 AA. AC E1J1M0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9347_00768; OS Escherichia coli MS 124-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=679205; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 124-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWT01000004; EFK70117.1; -; Genomic_DNA. DR ProteinModelPortal; E1J1M0; -. DR SMR; E1J1M0; 10-208. DR EnsemblBacteria; EFK70117; EFK70117; HMPREF9347_00768. DR PATRIC; 41088364; VBIEscCol139996_0724. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E1K1U9_DESFR Unreviewed; 214 AA. AC E1K1U9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DesfrDRAFT_3849; OS Desulfovibrio fructosivorans JJ. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=596151; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JJ; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Wall J.D., RA Stahl D.A., Arkin A.P., Dehal P., Stolyar S.M., Hazen T.C., RA Woyke T.J.; RT "The draft genome of Desulfovibrio fructosovorans JJ."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECZ01000045; EFL49405.1; -; Genomic_DNA. DR EnsemblBacteria; EFL49405; EFL49405; DesfrDRAFT_3849. DR PATRIC; 41172496; VBIDesFru57976_3957. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 21940 MW; 0851EA9270435941 CRC64; MSRPAFDLGV YLVTDRPALL GRELLDVVGL AVAGGATMVQ LREKTAATRE FVELARAVLG VTRPRGVPLL INDRVDVALA AGADGVHVGQ DDMHPADVRA LLGAKAIIGL SVTGEDEARA ARGMPVDYLG AGPVFATATK KDAGAPQGLP GLAAMLALSE VPVVAIGAIK EGNAREVMET GVAGVAVVSA ICSATDPREA AVQLRHIVEA GRKR // ID E1KQ50_9BACT Unreviewed; 204 AA. AC E1KQ50; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9296_0914; OS Prevotella disiens FB035-09AN. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=866771; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FB035-09AN; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDO01000027; EFL46406.1; -; Genomic_DNA. DR EnsemblBacteria; EFL46406; EFL46406; HMPREF9296_0914. DR PATRIC; 41213979; VBIPreDis168850_1018. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22373 MW; 90407D48D5DCA797 CRC64; MTNIQFITHE NERFGYIEGT ELALRGGCKW VQLRMKNATD EQFLSVGRQV AALCRNYHAT FLLDDRVHLV HELGADGVHL GKNDMPVDEA RPLLGHEKII GGTANTFADI QRLATQGANY IGCGPFRYTT TKQNLAPVLG LKGYETLLNQ MKEAQIQIPL IAIGGILHDD IPDLLGIGVS GIAISGAVLN AENPKEEMEK LIKI // ID E1KQ53_9BACT Unreviewed; 198 AA. AC E1KQ53; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF9296_0917; OS Prevotella disiens FB035-09AN. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=866771; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FB035-09AN; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDO01000027; EFL46380.1; -; Genomic_DNA. DR EnsemblBacteria; EFL46380; EFL46380; HMPREF9296_0917. DR PATRIC; 41213985; VBIPreDis168850_1021. DR OrthoDB; EOG679THR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 198 AA; 22082 MW; C361A6A113CE6305 CRC64; MRFIVITEPT FIPNEATIIA KLLRLGVDLV HIRKLEATAE AVENLIKAIP VEYHTRLVLH DNFELSARFL LYGLHLNRRN SVLPKGFKGS VSRSCHTFEE VKTYKSLCDY VFLSPIFDSI SKQGYASSFT PQTLLTAQKQ GIIDEKVVAL GGITAENIVP IQRYGFGGVA LLGDVWNRIN DANFDDYIKK IATAAAKP // ID E1KS71_9BACT Unreviewed; 204 AA. AC E1KS71; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF9296_1532; OS Prevotella disiens FB035-09AN. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=866771; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FB035-09AN; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDO01000046; EFL45569.1; -; Genomic_DNA. DR EnsemblBacteria; EFL45569; EFL45569; HMPREF9296_1532. DR PATRIC; 41215559; VBIPreDis168850_1783. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 204 AA; 23333 MW; 70BC4D02C7FABAAF CRC64; MGMKLVVMTK STYFVEEDKI LTLLFEAGLE HLHISKTDES SLYLERLLML IPTKYHKYIT VYQHFDMAKK LSLAGIHLDN LEVEPPIGYK GQIGRTCKNS MLLKEMRKNS DYVILKNVYE DSSDATKTPV LSSMELTELK KQGRLGKHVY AMGGVTLECI PELKNYGFGG VVVGNDFWNK IDLRADTDFK GILNYFHQLR QATE // ID E1KZD8_FINMA Unreviewed; 212 AA. AC E1KZD8; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9289_0031; OS Finegoldia magna BVS033A4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Finegoldia. OX NCBI_TaxID=866773; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BVS033A4; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDP01000044; EFL53575.1; -; Genomic_DNA. DR ProteinModelPortal; E1KZD8; -. DR EnsemblBacteria; EFL53575; EFL53575; HMPREF9289_0031. DR PATRIC; 41220872; VBIFinMag167610_1576. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23461 MW; 67152E1CA9AE7BC1 CRC64; MNKQFNLGLN LVTNKQTLKG RDLTETIEIA LKNGADSVRL REKNMDTRSI MQEAFKIKEI TQRMGKLLIV NDRVDIAKAC DVDGVHLGQK DMPIKYAREM LGDDKIIGIS CHTLEQALEA QEAGADYIGV GAIFPTFTGD DFVRVTIDTL KEISEKIHVP ITAIGGINKN NIRMIFDSNV DSVSLTSAVF STGDVAASTQ ELKQKFDMIL KK // ID E1KZV4_FINMA Unreviewed; 214 AA. AC E1KZV4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9289_0940; OS Finegoldia magna BVS033A4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Finegoldia. OX NCBI_TaxID=866773; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BVS033A4; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDP01000049; EFL53435.1; -; Genomic_DNA. DR EnsemblBacteria; EFL53435; EFL53435; HMPREF9289_0940. DR PATRIC; 41221211; VBIFinMag167610_1741. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23786 MW; 4795352F9B7CB158 CRC64; MRKKLNLSLY LVTDRTNVAC EEEFLTKIEE SLKGGVTLVQ LREKNISTRE YIDLAKKVKI ICDKFDVPLL IDDRIDVCLA SNCAGVHLGD EDMEIKDARR ILGDNYIIGA TAKSVERAIQ CEKEGADYLG VGAIYPTKTH VKTKITSVDT LRDINNSINI KTVAIGGLNE DNMDVLKNSG ASGIAVVRAL MNDDNPQEKA HRLLEKSKQI LELR // ID E1L3V6_9FIRM Unreviewed; 505 AA. AC E1L3V6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 16. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF9321_0257; OS Veillonella atypica ACS-049-V-Sch6. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=866776; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-049-V-Sch6; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDR01000005; EFL56937.1; -; Genomic_DNA. DR EnsemblBacteria; EFL56937; EFL56937; HMPREF9321_0257. DR PATRIC; 41224284; VBIVeiAty166341_0031. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 505 AA; 54295 MW; 89CD424CC452B2C4 CRC64; MNHENPYMKG CTWPELNILE TLRHQNPLVI CITNDVVRTF TANGLLTIGA SPIMSECSED LKDLIVHASA LLINIGTLTP DKASYYKEAI QLAKVREVPV VLDPVGCHAG AYRLSVVLDL IETGNISLLR GNQSEIKAVY DALSHDDTAN NSTAGKGVDG AQVEDSAVIA YRLARLINCP VVATGAEDYV SDGTRVFAVP HGHSLMTAVT GTGCLLGAVL AAFLGIYHPF KDSLSIGEFL AYALAYYGLA GENAVKTSGI KPGSFSVAFM DALYTLDDTV LMSENRIRPI VLPDQLQVYF VCGTQDTELN KKRLLEIVEE ACRGGVTCFQ FREKGDGTLE GQQKLELAQR LQQICAKYNV LFIINDDVEL AVAVNADGVH VGQGDMRLED VRHLVGHKVV GISIHSVEEL RKTDVVYADC VGVGPMYATS SKPDAQEPCG PERISKLKAE GLTLPCVGIG GITLDNAREV LYAGACGVAV ISAIAHAEKP YEAALRFKQL ASNSQ // ID E1L9U5_9FIRM Unreviewed; 501 AA. AC E1L9U5; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 16. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF9684_0843; OS Veillonella atypica ACS-134-V-Col7a. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=866778; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-134-V-Col7a; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDS01000011; EFL58644.1; -; Genomic_DNA. DR EnsemblBacteria; EFL58644; EFL58644; HMPREF9684_0843. DR PATRIC; 41228617; VBIVeiAty168093_0295. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 501 AA; 53911 MW; 854296591E4E2248 CRC64; MNPYIHNQIR PEFNILYTLR KKNPLVICIT NDVVRTFTAN GLLAIGASPI MSECSEDLKD LIVYASALLI NIGTLTPEKV GYYKEAIKLA KEYDVPIILD PVGCHAGAYR LSVVLDLIKT GSISLLRGNQ SEVKAVYDAL SSDNKDEISP LGKGVDGAQV ADSAIIAYRL ARLINCPVVA TGEEDYVSDG TRVFAVPHGH SIMTAVTGTG CLLGAVLAAF FGIYDLFKDS LSTGEFLAYA LAYYGLAGES AVKVSGIKPG SFSVAFMDAL YTLDDEVLVS ENRVRPVVVP DQLQVYFVCG TQDTELNKKR LLEIVEDACR GGITCFQFRE KGDGTLEGQQ KLELAQQLQH ICAKYHVLYI INDDVELAVA VNADGIHVGQ DDMCLEDVRN IVGHKVVGIS IHSIEELHKT DVLYADCVGV GPMYTTSSKP DAQEPCGPER TAELQAEGLT LPCVGIGGIT LDNTMAVLHA GACGVAVISA IAHAEKPHEA VRQFKELASS L // ID E1LF53_STRMT Unreviewed; 210 AA. AC E1LF53; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SMSK321_0236; OS Streptococcus mitis SK321. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=585202; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK321; RA Daugherty S.C., Tallon L.J., Jones K.M., Liu X., Kilian M., RA Tettelin H.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDT01000008; EFN97478.1; -; Genomic_DNA. DR EnsemblBacteria; EFN97478; EFN97478; SMSK321_0236. DR PATRIC; 41667069; VBIStrMit102292_0250. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22910 MW; 0D50CEB946A8DD47 CRC64; MNREALRLYL VTNRYQDSLE SFLEKIETAC RSGVTIVQLR EKNLTTNQYY QLAKEVKEIT DAYQVPLIID DRLDVCLAVN AAGLHIGEDE LPVSVARQVL GPDKILGVTA KTVKRALEAE ESGADYLGTG AIFPTTTKEN ATITLISTLK TICQRVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDDIIF // ID E1LJU3_STRMT Unreviewed; 209 AA. AC E1LJU3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SMSK564_0118; OS Streptococcus mitis SK564. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=585203; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK564; RA Daugherty S.C., Tallon L.J., Jones K.M., Liu X., Kilian M., RA Tettelin H.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDU01000006; EFN99325.1; -; Genomic_DNA. DR EnsemblBacteria; EFN99325; EFN99325; SMSK564_0118. DR PATRIC; 41670680; VBIStrMit11393_0129. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23351 MW; 70B2027B16106CB7 CRC64; MFHKELLKLY FICGTTTCQG KDLYRVVEEA LKGGITLFQF REKGEGSLEG KEKVELAIKL QNLCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDLGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID E1LJV0_STRMT Unreviewed; 210 AA. AC E1LJV0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SMSK564_0125; OS Streptococcus mitis SK564. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=585203; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK564; RA Daugherty S.C., Tallon L.J., Jones K.M., Liu X., Kilian M., RA Tettelin H.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDU01000006; EFN99332.1; -; Genomic_DNA. DR EnsemblBacteria; EFN99332; EFN99332; SMSK564_0125. DR PATRIC; 41670694; VBIStrMit11393_0136. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22925 MW; 5CFD91D3282A7761 CRC64; MNREALRLYL VTNRYQDSLE SFLEKIERAC RSGVTIVQLR EKNLTTNQYY QLAKEVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQRVAIPV VAIGGLTSEN IDQLAATGIA GVAVVRDLMQ AEDIETKTQA FLTKLHDIIS // ID E1M3Y0_STRMT Unreviewed; 209 AA. AC E1M3Y0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SM12261_1252; OS Streptococcus mitis NCTC 12261. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=246201; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 12261; RA Daugherty S.C., Kilian M., Tettelin H.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDX01000020; EFN94758.1; -; Genomic_DNA. DR EnsemblBacteria; EFN94758; EFN94758; SM12261_1252. DR PATRIC; 41685536; VBIStrMit12054_1368. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23171 MW; BEA79535F452F405 CRC64; MFHKELLKLY FICGTTTCQG KDLYTVVEEA LKGGITLFQF REKGEGALKG IEKVELAIKL QALCKKYNVP FIVNDDIDLA LEIDADGVHV GQDDLGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLKLMRKLL PQMPLVAIGG IQTQHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEK // ID E1M3Y7_STRMT Unreviewed; 210 AA. AC E1M3Y7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SM12261_1259; OS Streptococcus mitis NCTC 12261. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=246201; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 12261; RA Daugherty S.C., Kilian M., Tettelin H.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDX01000020; EFN94765.1; -; Genomic_DNA. DR EnsemblBacteria; EFN94765; EFN94765; SM12261_1259. DR PATRIC; 41685550; VBIStrMit12054_1375. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22905 MW; FAFB999CCC7FE799 CRC64; MNREALRLYL VTNRYQDSLQ SFLEKIETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE EGGADYLGTG AIFPTTTKEN APITLISTLK TICQRVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIETKTQA FLTKLDDIIF // ID E1NBJ7_9BIFI Unreviewed; 855 AA. AC E1NBJ7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 19. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; ORFNames=HMPREF9003_0588; OS Bifidobacterium dentium JCVIHMP022. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=553191; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JCVIHMP022; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEHJ01000027; EFO77548.1; -; Genomic_DNA. DR EnsemblBacteria; EFO77548; EFO77548; HMPREF9003_0588. DR PATRIC; 42111154; VBIBifDen39005_1384. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 855 AA; 94665 MW; F2A5F5841F8F6093 CRC64; MNDYPYASMR DCFDMSAYFV VGPQDCKGRP ITDVVDDALR GGATFIQLRA KNTDAKDLTL MAQDIAQIIE DNDKSDAVAF VIDDRVDVVW QARNKGIKVD GVHIGQTDME PREARALLGE EAIVGLSAET ESLVRLINEL PNGCIDYIGA GPLHVSTTKP EASVGGNDGS GNTLDEDQIN TICTASDFPV VVGGGVTAND MEMLARSKAA GWFVVSAIAG ADDPEAATRE MVTRWKAVRG ETKHGFAPRV QSADTATTTD TQMTESNNGK FTNAKEAKAS SKLAKQQRVD IAARGSKQRD KAHVRKTTPV HFENRFGSYD LEVPYTEIKL SDTPGVGPNA PFKDYNTEGP KCDPKEGLAP LRLDWIRDRG DVEEYEGRRR NLEDDGKRAI KRGKASKEWR GRQHKPLKAK DHPITQMWYA RHDIITPEMR YVAEREHCDV ELVRSELAAG RAVMPCNINH PEAEPMIIGS RFLTKLNANM GNSAVTSSID EEVEKLTWAT KWGADTVMDL STGNDIHTTR EWILRNSPVP IGTVPMYQAL EKVEDDASKL SWELFRDTVI EQCEQGVDYM TIHAGVLLRF VPLTANRMTG IVSRGGSIMA EWCLQHHQES FLYTHFDELC EIFAKYDVAF SLGDGLRPGS LADANDAAQF AELMTLGELT QRAWEHDVQV MIEGPGHIPF DTVRMNIEME KAICKDAPFY TLGPLTTDTA PGYDHITSAI GGVEIARYGT AMLCYVTPKE HLGLPNKDDV KQGVIAYKIA CHAADIAKHH PHAIDRDNAM SKARFEFRWL DQFNLSYDPD TAIAFHDDTL PAEPAKMAHF CSMCGPKFCS MAISQNIRRK FGNAEAQEKL VADAQ // ID E1P1N1_NEILA Unreviewed; 205 AA. AC E1P1N1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NLY_01640; OS Neisseria lactamica Y92-1009. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=869214; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y92-1009; RA Vaughan T.E., Desmond L., Budd E., Hayes K., Dewar J., Loveridge C., RA Young G., Vincent G.A., Stubbington M., Elmore M.J., Hudson M.J., RA Gorringe A.R., Vipond R.; RT "Genome sequence of Neisseria lactamica Y92-1009."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y92-1009; RA Vaughan T.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CACL01000007; CBX22066.1; -; Genomic_DNA. DR EnsemblBacteria; CBX22066; CBX22066; NLY_01640. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21765 MW; 91F4B181D7486E15 CRC64; MTFPPLKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKTL HGDELKREIA RCAAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSAA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQARGTPVVA IGGIDLNNAQ AVLATGVSSL AAVRAVTEAE NPEAAVKAFQ ALWNG // ID E1PBJ4_ECOAB Unreviewed; 211 AA. AC E1PBJ4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 28. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECABU_c45090; OS Escherichia coli OR:K5:H- (strain ABU 83972). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=655817; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABU 83972; RX PubMed=20865122; DOI=10.1371/journal.ppat.1001078; RA Zdziarski J., Brzuszkiewicz E., Wullt B., Liesegang H., Biran D., RA Voigt B., Gronberg-Hernandez J., Ragnarsdottir B., Hecker M., RA Ron E.Z., Daniel R., Gottschalk G., Hacker J., Svanborg C., RA Dobrindt U.; RT "Host imprints on bacterial genomes--rapid, divergent evolution in RT individual patients."; RL PLoS Pathog. 6:e1001078-e1001078(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001671; ADN48911.1; -; Genomic_DNA. DR RefSeq; YP_006108442.1; NC_017631.1. DR ProteinModelPortal; E1PBJ4; -. DR SMR; E1PBJ4; 9-208. DR EnsemblBacteria; ADN48911; ADN48911; ECABU_c45090. DR GeneID; 12729789; -. DR KEGG; eab:ECABU_c45090; -. DR PATRIC; 42954039; VBIEscCol35126_4699. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; ECOL655817:GI9N-4390-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23030 MW; D9436839F2B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSTIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E1PPL3_CAMJM Unreviewed; 201 AA. AC E1PPL3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-APR-2014, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=CJM1_1018; OS Campylobacter jejuni subsp. jejuni serotype HS21 (strain M1 / 99/308). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=645464; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M1 / 99/308; RX PubMed=20865039; DOI=10.1371/journal.pone.0012253; RA Friis C., Wassenaar T.M., Javed M.A., Snipen L., Lagesen K., RA Hallin P.F., Newell D.G., Toszeghy M., Ridley A., Manning G., RA Ussery D.W.; RT "Genomic characterization of Campylobacter jejuni strain M1."; RL PLoS ONE 5:e12253-e12253(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001900; ADN91213.1; -; Genomic_DNA. DR RefSeq; YP_005657963.1; NC_017280.1. DR ProteinModelPortal; E1PPL3; -. DR EnsemblBacteria; ADN91213; ADN91213; CJM1_1018. DR GeneID; 12247804; -. DR KEGG; cjm:CJM1_1018; -. DR PATRIC; 42814447; VBICamJej14675_1007. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR BioCyc; CJEJ645464:GLA6-1014-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 23486 MW; 61622900362A43FB CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICVKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG IDFLKSLLEF SQIPLYAIGG INTQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID E1PPV7_CAMJM Unreviewed; 210 AA. AC E1PPV7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CJM1_1058; OS Campylobacter jejuni subsp. jejuni serotype HS21 (strain M1 / 99/308). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=645464; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M1 / 99/308; RX PubMed=20865039; DOI=10.1371/journal.pone.0012253; RA Friis C., Wassenaar T.M., Javed M.A., Snipen L., Lagesen K., RA Hallin P.F., Newell D.G., Toszeghy M., Ridley A., Manning G., RA Ussery D.W.; RT "Genomic characterization of Campylobacter jejuni strain M1."; RL PLoS ONE 5:e12253-e12253(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001900; ADN91253.1; -; Genomic_DNA. DR RefSeq; YP_005658003.1; NC_017280.1. DR EnsemblBacteria; ADN91253; ADN91253; CJM1_1058. DR GeneID; 12247844; -. DR KEGG; cjm:CJM1_1058; -. DR PATRIC; 42814530; VBICamJej14675_1048. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; CJEJ645464:GLA6-1054-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22955 MW; 3DA973D7D1B83EBA CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKVTPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKAVLD ELKGINLSGV AVVRAIMDAK DAFLAAKELK CKIYENLPLK // ID E1PV83_HELPT Unreviewed; 219 AA. AC E1PV83; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPSAT_02505; OS Helicobacter pylori (strain Sat464). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=794851; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sat464; RA Kersulyte D., Jahuira Arias H., Gilman R.H., Berg D.E.; RT "Complete genome sequence of Helicobacter pylori strain Sat464."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002071; ADO05248.1; -; Genomic_DNA. DR RefSeq; YP_005768156.1; NC_017359.1. DR EnsemblBacteria; ADO05248; ADO05248; HPSAT_02505. DR GeneID; 12347547; -. DR KEGG; hpt:HPSAT_02505; -. DR PATRIC; 43065395; VBIHelPyl163788_0504. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; HPYL794851:GLEN-503-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23904 MW; CEF078C619A51068 CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLSLQDP IEIKQLALEC QKLCQKYGAP FIVNDEVQLA LELKADGVHV GQEDMAIEEV MALCKKRLFI GLSVNTLEQA LKVRHLDGVA YFGVGPIFPT QSKKDKQVVG VELLKKIKDS GIKKPLIAIG GITAHNASKL REYGGIAVIS AITQAKDKAL AVGKLLKNA // ID E1PZV6_HELPM Unreviewed; 219 AA. AC E1PZV6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPSJM_04290; OS Helicobacter pylori (strain SJM180). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=765962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SJM180; RA Kersulyte D., Velapatino B., Gilman R.H., Berg D.E.; RT "Complete genome sequence of Helicobacter pylori strain SJM180."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002073; ADO02447.1; -; Genomic_DNA. DR RefSeq; YP_003928764.1; NC_014560.1. DR EnsemblBacteria; ADO02447; ADO02447; HPSJM_04290. DR GeneID; 9787582; -. DR KEGG; hpm:HPSJM_04290; -. DR PATRIC; 42495182; VBIHelPyl169273_0854. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; HPYL765962:GH29-849-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23909 MW; 93269467038A2A3E CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLETLELAL QSKITAFQFR QKGDLALQDP IEIKQLALKC QKLCQKYGTP FIVNDEAKLA LELKADGVHV GQEDMAIEEV MTLCKKRSFI GLSVNTLEQA LKARHLDGVA YFGVGPIFPT QSKKDKQVVG VELLKKIKDS GIKKPLIAIG GITTHNASKL REYGGIAVIS AIAQAKDKAL AVGKLLKNA // ID E1Q2I2_HELPP Unreviewed; 220 AA. AC E1Q2I2; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPPC_04270; OS Helicobacter pylori (strain PeCan4). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=765963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PeCan4; RA Kersulyte D., Vasquez J., Gilman R.H., Berg D.E.; RT "Complete genome sequence of Helicobacter pylori strain PeCan4."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002074; ADO07080.1; -; Genomic_DNA. DR RefSeq; YP_003927130.1; NC_014555.1. DR EnsemblBacteria; ADO07080; ADO07080; HPPC_04270. DR GeneID; 9785909; -. DR KEGG; hpc:HPPC_04270; -. DR PATRIC; 42491809; VBIHelPyl173672_0863. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; HPYL765963:GH9T-829-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24206 MW; AD00DB2E39637EB1 CRC64; MFDANCLKLM FVAGSQDFYH IKGDRTNALL ETLELALESK ITAFQFRQKG DLALQDPIEI KQLALECQKL CKKYGVPFII NDEVRLALEL KADGVHVGQE DMAIEEVVTL CQKRLFIGLS VNTLEQALKA HHLDAVAYLG VGPIFPTLSK KDAKEVVGVN LLKKIRDSGV KKPLIAIGGI TMHNAPKLHE YGGIAVISAI TQAKDKALAI ETLLKIREGF // ID E1Q751_HELPC Unreviewed; 219 AA. AC E1Q751; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPCU_04500; OS Helicobacter pylori (strain Cuz20). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=765964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Cuz20; RA Kersulyte D., Herrera P., Gilman R.H., Berg D.E.; RT "Complete genome sequence of Helicobacter pylori strain Cuz20."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002076; ADO04060.1; -; Genomic_DNA. DR RefSeq; YP_005766968.1; NC_017358.1. DR EnsemblBacteria; ADO04060; ADO04060; HPCU_04500. DR GeneID; 12346412; -. DR KEGG; hpu:HPCU_04500; -. DR PATRIC; 43062826; VBIHelPyl160354_0910. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; HPYL765964:GLEA-881-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23938 MW; C3116E96EAAB8926 CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLSLQDP IEIKQLALKC QKLCQKYGAP FIVNDEVQLA LELKADGVHV GQEDMAIEEV MTLCKKCLFI GLSVNTLEQA LKARHLDGVA YFGVGPIFPT QSKKDKQVVG VELLKKIKDR GIKKPLIAIG GITTHNASKL REYGGIAVIS AITQAKDKAL AVGKLLNDA // ID E1QKY1_DESB2 Unreviewed; 218 AA. AC E1QKY1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Deba_2987; OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / VKM B-1802 / OS 2st14). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfarculales; OC Desulfarculaceae; Desulfarculus. OX NCBI_TaxID=644282; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14; RX DOI=10.4056/sigs.1243258; RA Sun H., Spring S., Lapidus A., Davenport K., Glavina Del Rio T., RA Tice H., Nolan M., Copeland A., Cheng J., Lucas S., Tapia R., RA Goodwin L., Pitluck S., Ivanova N., Pagani I., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Hauser L., RA Chang Y., Jeffries C., Detter J., Han C., Rohde M., Brambilla E., RA Goker M., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H., Land M.; RT "Complete genome sequence of Desulfarculus baarsii type strain RT (2st14)."; RL Stand. Genomic Sci. 3:276-284(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002085; ADK86340.1; -; Genomic_DNA. DR RefSeq; YP_003808934.1; NC_014365.1. DR EnsemblBacteria; ADK86340; ADK86340; Deba_2987. DR GeneID; 9495473; -. DR KEGG; dbr:Deba_2987; -. DR PATRIC; 42301565; VBIDesBaa100999_3060. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; DBAA644282:GH2J-3039-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 22072 MW; 6D2FC276F59925F8 CRC64; MNDVGRLHVL TDTVLQTRFS AVELARLAIR GGADVIQLRQ KDGATNQMID TARQLKAVCA GAGVDLIIND RLDVAMAVDA DGVHLGQDDF PINKARRMLG PGKVIGGSAD SLEEALQCQA DGADYVGFGP VFPTTSKDDA GPVAGLEALA RVAAGLRIPV VAIGGVNAGN AAQIMAAGAH GLAVISAVCC QLDPEAATTA LLRAMGLAAA PAAAARKG // ID E1QR94_VULDI Unreviewed; 205 AA. AC E1QR94; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Vdis_1205; OS Vulcanisaeta distributa (strain DSM 14429 / JCM 11212 / NBRC 100878 / OS IC-017). OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Vulcanisaeta. OX NCBI_TaxID=572478; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017; RX DOI=10.4056/sigs.1113067; RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., RA Lucas S., Nolan M., Glavina Del Rio T., Cheng J., Bruce D., RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y., RA Jeffries C., Rohde M., Spring S., Goker M., Wirth R., Woyke T., RA Bristow J., Eisen J., Markowitz V., Hugenholtz P., Klenk H., RA Kyrpides N.; RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC- RT 017T)."; RL Stand. Genomic Sci. 3:117-125(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002100; ADN50591.1; -; Genomic_DNA. DR RefSeq; YP_003901642.1; NC_014537.1. DR EnsemblBacteria; ADN50591; ADN50591; Vdis_1205. DR GeneID; 9752137; -. DR KEGG; vdi:Vdis_1205; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; VDIS572478:GHT7-1225-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21970 MW; 8F8A4E5900548C2B CRC64; MKLPKGIYGI TDTSYTIKNH VEAARAFLEG GVRIVQYRRK EGSIRVMLEE ARAIRRLCNE YGAVFIVDDR VDIAILSDAD GVHVGLDDAP VDEIRRRFGG LIIGASASTV DEALQGERAG ANYIGAGSVF PSPTRPDYRI TGLDGLRSIV RSVNIPVYAI GGITLESIPA IKATGAWGAA VISGILAAKD PVKMARAFVE AWENA // ID E1RC14_SPISS Unreviewed; 217 AA. AC E1RC14; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Spirs_0759; OS Spirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta. OX NCBI_TaxID=573413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11293 / JCM 15392 / SEBR 4228; RX DOI=10.4056/sigs.1143106; RA Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., RA Nolan M., Glavina Del Rio T., Tice H., Cheng J., Pitluck S., RA Liolios K., Ivanova N., Tapia R., Han C., Bruce D., Goodwin L., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y., RA Jeffries C., Detter J., Rohde M., Brambilla E., Spring S., Goker M., RA Sikorski J., Woyke T., Bristow J., Eisen J., Markowitz V., RA Hugenholtz P., Klenk H., Kyrpides N.; RT "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR RT 4228)."; RL Stand. Genomic Sci. 3:136-144(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002116; ADK79894.1; -; Genomic_DNA. DR RefSeq; YP_003802488.1; NC_014364.1. DR EnsemblBacteria; ADK79894; ADK79894; Spirs_0759. DR GeneID; 9488839; -. DR KEGG; ssm:Spirs_0759; -. DR PATRIC; 42525398; VBISpiSma89994_0776. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; SSMA573413:GI0C-767-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23413 MW; B92FE18B596FEC75 CRC64; MYKSINAAMS LCLVTDAGFR PADEFLSTVE TALKNGATMV QYREKSGRYC DKEIYDRGIE LVTLCHRFGV PLVVDDRLDI AMAIGADGLH IGQNDLPLPV AKQIWPEGGI FGVSVADLRE MRLAQEQGAD YLGVGAFPTT TKKDYSNVEA KLLSSMVKES SLPMMAIGGI QAENASIPIG WGCVGVAVIS AIWKAPDPAV ATRHILETVR KAKGDRV // ID E1RFA2_METP4 Unreviewed; 213 AA. AC E1RFA2; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mpet_0273; OS Methanoplanus petrolearius (strain DSM 11571 / OCM 486 / SEBR 4847). OC Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales; OC Methanomicrobiaceae; Methanoplanus. OX NCBI_TaxID=679926; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11571 / OCM 486 / SEBR 4847; RX PubMed=21304750; RA Brambilla E., Djao O.D., Daligault H., Lapidus A., Lucas S., RA Hammon N., Nolan M., Tice H., Cheng J.F., Han C., Tapia R., RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Methanoplanus petrolearius type strain RT (SEBR 4847)."; RL Stand. Genomic Sci. 3:203-211(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002117; ADN35050.1; -; Genomic_DNA. DR RefSeq; YP_003893488.1; NC_014507.1. DR ProteinModelPortal; E1RFA2; -. DR EnsemblBacteria; ADN35050; ADN35050; Mpet_0273. DR GeneID; 9742716; -. DR KEGG; mpi:Mpet_0273; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; MPET679926:GHOF-278-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22291 MW; 9BCF2DCA262162CD CRC64; MPYDLYVVTD REIGRGRTHQ EIALEAAAGG ADVIQFRDKT LLIREFIETA KEIRDITSAS GAMFIVNDRI DAALAVGADG VHLGQNDMTA DWARRISPPG FIIGISVGNV AEAIEAESAG ADYVALSPVF STVSKDDAGP GHGLEMLSRI RSNVDIPVIG IGGIGLHNVK DVLSAGADGI AVISAVAGAD DIRSAAEEMK KIIAVEKRKN GLG // ID E1RL05_XYLFG Unreviewed; 204 AA. AC E1RL05; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=XFLM_02725; OS Xylella fastidiosa (strain GB514). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=788929; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB514; RA Dowd S.E., Morano L., Bextine B., Lara A., Koirala M., Schreiber H.L., RA Ojeda M.; RT "Unraveling the first Xylella fastidiosa subsp. fastidiosa genome from RT Texas."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002165; ADN62544.1; -; Genomic_DNA. DR RefSeq; YP_005999910.1; NC_017562.1. DR ProteinModelPortal; E1RL05; -. DR EnsemblBacteria; ADN62544; ADN62544; XFLM_02725. DR GeneID; 12588383; -. DR KEGG; xff:XFLM_02725; -. DR PATRIC; 43284393; VBIXylFas171671_0668. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR BioCyc; XFAS788929:GLMT-522-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21869 MW; 1DE42CE42C6D56EA CRC64; MPQPRGIYLI TPDETDTARL IAHTAPLLNG IVWLQYRNKL ANTALRTEQA QALLALCRPT GIPLLINDDL ELAQTIGADG VHLGMHDSNA SIARAQLGPH AIIGVSCYNQ IERAKQAIKA GASYVGFGAF YPSHTKTTPY RATPELLRQT THLGVPRVAI GGLTPKNIAP IIEAGAELLA VISGIYSAKN PITALKAYQS QFNI // ID E1RQK4_XYLFG Unreviewed; 320 AA. AC E1RQK4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=XFLM_07450; OS Xylella fastidiosa (strain GB514). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=788929; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB514; RA Dowd S.E., Morano L., Bextine B., Lara A., Koirala M., Schreiber H.L., RA Ojeda M.; RT "Unraveling the first Xylella fastidiosa subsp. fastidiosa genome from RT Texas."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002165; ADN63404.1; -; Genomic_DNA. DR RefSeq; YP_006000770.1; NC_017562.1. DR ProteinModelPortal; E1RQK4; -. DR EnsemblBacteria; ADN63404; ADN63404; XFLM_07450. DR GeneID; 12589279; -. DR KEGG; xff:XFLM_07450; -. DR PATRIC; 43286812; VBIXylFas171671_1822. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; XFAS788929:GLMT-1418-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 320 AA; 35468 MW; E7754B57E973CFA1 CRC64; MTDSLRSIHV VAAVIADVRG RLLLSRRTEN SDMPGLWEFP GGKRESGETS EQALARELYE ELGISADVGE WLMEVPQLYP GKRLRLEVRR VRAWKGGLRG REGQALTWVE PDKLLRYSMP PADQPVVGML RQPDRYLVTP EPGEQDAEWL DAVEHAYRLG IERIQLRMRQ HDPVRWSGLV RQAVQRRGRA HVEVLLNRDI ALAEALGIGV HLGAEQLAVL DARPLPVGLP VGASCHCLAD LCHAQRIGCD FAVLGPVLPT ESHPGAVTLG WERFEQLREQ VALPIYAIGG MCADQVKEAR RHGAQGIAAM RGLWPGGAKQ // ID E1S4A2_ECOUM Unreviewed; 211 AA. AC E1S4A2; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=UM146_16700; OS Escherichia coli (strain UM146). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=869729; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UM146; RX PubMed=21075930; DOI=10.1128/JB.01290-10; RA Krause D.O., Little A.C., Dowd S.E., Bernstein C.N.; RT "Complete genome sequence of adherent invasive Escherichia coli UM146 RT isolated from ileal Crohn's disease biopsy tissue."; RL J. Bacteriol. 193:583-583(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UM146; RA Krause D.O., Little A.C., Dowd S.E., Bernstein C.N.; RT "Complete genome sequence of adherent invasive Escherichia coli UM146 RT isolated from ileal Crohn's disease biopsy tissue."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002167; ADN72694.1; -; Genomic_DNA. DR RefSeq; YP_006112206.1; NC_017632.1. DR ProteinModelPortal; E1S4A2; -. DR SMR; E1S4A2; 9-208. DR EnsemblBacteria; ADN72694; ADN72694; UM146_16700. DR GeneID; 12701849; -. DR KEGG; elu:UM146_16700; -. DR PATRIC; 42973528; VBIEscCol167775_3570. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; ECOL869729:GI9Z-3338-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E1S904_HELP9 Unreviewed; 217 AA. AC E1S904; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=hp908_0858; OS Helicobacter pylori (strain 908). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=869727; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=908; RX PubMed=20952566; DOI=10.1128/JB.01110-10; RA Devi S.H., Taylor T.D., Avasthi T.S., Kondo S., Suzuki Y., Megraud F., RA Ahmed N.; RT "Genome of Helicobacter pylori strain 908."; RL J. Bacteriol. 192:6488-6489(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002184; ADN79984.1; -; Genomic_DNA. DR RefSeq; YP_005765358.1; NC_017357.1. DR EnsemblBacteria; ADN79984; ADN79984; hp908_0858. DR GeneID; 12343698; -. DR KEGG; hpi:hp908_0858; -. DR PATRIC; 43059382; VBIHelPyl166603_0867. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; HPYL869727:GLE7-872-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23884 MW; 4447CB36BDB0720C CRC64; MFDADCLKLM FVAGSQDFYH IKGDRTNALL DTLELALQSK ITAFQFRQKG DLVLQDPVEI KRLALECQKL CKKYGAPFII NDEVRLALEL KADGVHVGQE DMAIEEVVTL CQKRLFIGLS VNTLEQALKA RHLDHVSYLG VGPIFPTPSK KDAKEVVGVN LLKKIHDSGV EKPLIAIGGI TTDNASKLWE YGGIAVISAI TQAKDKALAV ERLLKNA // ID E1SAT1_PANVC Unreviewed; 208 AA. AC E1SAT1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Pvag_3472; OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=712898; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C9-1; RX PubMed=20952567; DOI=10.1128/JB.01122-10; RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A., RA Stockwell V.O., Frey J.E., Duffy B.; RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9- RT 1."; RL J. Bacteriol. 192:6486-6487(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002206; ADO11595.1; -; Genomic_DNA. DR RefSeq; YP_003933044.1; NC_014562.1. DR EnsemblBacteria; ADO11595; ADO11595; Pvag_3472. DR GeneID; 9791984; -. DR KEGG; pva:Pvag_3472; -. DR PATRIC; 42423125; VBIPanVag152020_3620. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; PVAG712898:GHQ2-3464-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22549 MW; 1A6F37E6526A2632 CRC64; MPAFPATAPR LGLYPVVDSP EWLERLLEMG VRTLQLRIKD QPDEAAEPAI AQAIALGKRY DARLFINDYW QLAIKHHAYG VHLGQEDLDV ADLARIHQAG LRLGLSTHDD AELDRALAIQ PSYIALGHIF PTQTKEMPSA PQGIAQLNQH LTRLSHIPTV AIGGISIARA PEVLATGVGS IAVVSAITQA DDWRAATRTL LALARPGD // ID E1SUA3_FERBD Unreviewed; 528 AA. AC E1SUA3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 27. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN OrderedLocusNames=Fbal_2033; OS Ferrimonas balearica (strain DSM 9799 / CCM 4581 / PAT). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Ferrimonadaceae; Ferrimonas. OX NCBI_TaxID=550540; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9799 / CCM 4581 / PAT; RX DOI=10.4056/sigs.1161239; RA Nolan M., Sikorski J., Davenport K., Lucas S., Glavina Del Rio T., RA Tice H., Cheng J., Goodwin L., Pitluck S., Liolios K., Ivanova N., RA Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y., Jeffries C., Tapia R., Brettin T., RA Detter J., Han C., Yasawong M., Rohde M., Tindall B., Goker M., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H., Lapidus A.; RT "Complete genome sequence of Ferrimonas balearica type strain (PAT)."; RL Stand. Genomic Sci. 3:174-182(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002209; ADN76236.1; -; Genomic_DNA. DR RefSeq; YP_003913310.1; NC_014541.1. DR ProteinModelPortal; E1SUA3; -. DR EnsemblBacteria; ADN76236; ADN76236; Fbal_2033. DR GeneID; 9770814; -. DR KEGG; fbl:Fbal_2033; -. DR PATRIC; 42325733; VBIFerBal3052_2055. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR BioCyc; FBAL550540:GHY2-2099-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 528 AA; 55283 MW; 6D4F4B618B23A641 CRC64; MTQSDGAAVS PQTLGKPPIV WTIAGSDSGG GAGIQADLLT MRDLGGHGCS VITCITAQSS VAVDHVEAVS VKGMLAQLDT LWADLPPQAI KIGLLPGPAH IEALADWFAA HQAGLPPVIL DPVLVASSGG MLNVCEASDQ FDALLPYVEV ITPNGDELAA LTGMVIDSPA AVVAACQQLH QRGARAVLAK GGHFDHLHPG RCVDYFSSAA LTTLFDGPRI ATQHTHGSGC TLASALATVL AQGYVMEDAL AVVRAYLHNG LMGAVALGAG PGPLARTGWP QRLDSFPTVP LPGSELARAY GLEASVQLPQ QPFARCDVSA LGIYPVVDSV EWVERLLALG VKTLQLRIKD KSPEAVSADI QRAIVLGHQH QARLFINDYW QLAIEHGAYG VHLGQEDMET ADLAAIERAG LRLGLSTHGY YEILRAHALK PSYIALGHIF PTPTKEMPSA PQGLARLGRY VALVQPHCPA VAIGGIDVSR AYQVAQSGVG SIAVVRAVTQ ADDVAVALAQ LQQAFESAPT LESVDAER // ID E1SYF2_THESX Unreviewed; 211 AA. AC E1SYF2; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Thet_0623; OS Thermoanaerobacter sp. (strain X513). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=573062; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X513; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., Hemme C.L., Woyke T.; RT "Complete sequence of Thermoanaerobacter sp. X513."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002210; ADN54266.1; -; Genomic_DNA. DR RefSeq; YP_003903557.1; NC_014538.1. DR ProteinModelPortal; E1SYF2; -. DR EnsemblBacteria; ADN54266; ADN54266; Thet_0623. DR GeneID; 9760381; -. DR KEGG; thx:Thet_0623; -. DR PATRIC; 42445322; VBITheSp37765_0642. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; TSP573062:GHR1-650-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23018 MW; 437BD72098B68280 CRC64; MDLTLYAITD RSYIKNMDIA EAVELAIKGG ATVIQLREKD ISSREFYEIA LKVKEVTKRN RIPLIINDRV DIALAVDADG VHVGQEDLPA DIVRKIIGRD KIVGVSARTV EEALKAQRDG ADYLGVGAVF KTPTKPEAEA IGIEGLKKIK EAVTIPVVAI GGITKDNAYE VMLKSGVDGI SSVSAVFYGD IENNTRKLLE VIKKAINDRR I // ID E1TAU0_BURSG Unreviewed; 370 AA. AC E1TAU0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BC1003_3172; OS Burkholderia sp. (strain CCGE1003). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=640512; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCGE1003; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., RA Ovchinnikova G., Martinez-Romero E., Rogel M.A., Auchtung J., RA Tiedje J.M., Woyke T.; RT "Complete sequence of chromosome 1 of Burkholderia sp. CCGE1003."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002217; ADN59119.1; -; Genomic_DNA. DR RefSeq; YP_003908410.1; NC_014539.1. DR ProteinModelPortal; E1TAU0; -. DR EnsemblBacteria; ADN59119; ADN59119; BC1003_3172. DR GeneID; 9768091; -. DR KEGG; bgf:BC1003_3172; -. DR PATRIC; 42212899; VBIBurSp98639_3420. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR BioCyc; BSP640512:GBXV-3231-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 370 AA; 39813 MW; 3D238BEF618BBFDE CRC64; MTQTLTLKDR DLFWPPADEL TEAAERIRAR LGDWPPTHAP WRICLTAPDE PNGGDLIVVA DAARHGEQMA RWLVQGAAVV EAAEHKATLH LGGEKYRLEG HLAEDWIAAL AAFLDCGFDP HDALVLALAW RDGDETRTHA GGDAFPCNLA TFPRLAGLPQ APAEAFARCP ERLGLYPVLP NAQWVERVLG FGVKTVQLRR KSAHPADELQ REIARCVAAG RRHDAQVFIN DHWQAALEAG AYGVHLGQED VHTADLAALA AAGIRLGLST HGFYEILKAL HFRPSYIALG AVFPTTTKVM PTAPQGLKRL ARYVRLLDGV VPLVAIGGID LQVLPAVLET GVGCAAVVRA VTEAADPAAA VAALQQAFTQ // ID E1TQS3_LACPS Unreviewed; 217 AA. AC E1TQS3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LPST_C0094; OS Lactobacillus plantarum (strain ST-III). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=889932; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST-III; RA Wang Y., Chen C., Ai L., Zhou F., Zhou Z., Wang L., Zhang H., Guo B., RA Chen W.; RT "Complete genome sequence of probiotic Lactobacillus plantarum ST- RT III."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002222; ADN97318.1; -; Genomic_DNA. DR RefSeq; YP_003923412.1; NC_014554.1. DR EnsemblBacteria; ADN97318; ADN97318; LPST_C0094. DR GeneID; 9782035; -. DR KEGG; lps:LPST_C0094; -. DR PATRIC; 42497030; VBILacPla173910_0096. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; LPLA889932:GHWQ-97-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22779 MW; 657D94227E141259 CRC64; MTLKFEPTQL RAYFVCGTQD VPGQDLNVVV QTALDAGITA FQYRDKGNSQ LTTAERFALG QQLRERCAQA HVPFIVDDDV ELALALQADG IHVGQKDDRV TQVIQRVANQ MFVGLSCSTL AEVRIANQLE GIAYLGSGPI FPTTSKADAD PVVGLTGLRQ LVVTATCPVV AIGGITVAQL PAIAATGAAG AAVISMLTRS PDMAATVKAM LTATEGH // ID E1UD38_LISML Unreviewed; 214 AA. AC E1UD38; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=lmo4a_0338; OS Listeria monocytogenes serotype 4a (strain L99). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=563174; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L99; RX PubMed=22530965; DOI=10.1186/1471-2164-13-144; RA Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B., RA Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., RA Goesmann A., Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., RA Garrido P., Rusniok C., Buchrieser C., Goebel W., Chakraborty T.; RT "Comparative genomics and transcriptomics of lineages I, II, and III RT strains of Listeria monocytogenes."; RL BMC Genomics 13:144-144(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM211688; CAR83040.1; -; Genomic_DNA. DR RefSeq; YP_005925329.1; NC_017529.1. DR ProteinModelPortal; E1UD38; -. DR EnsemblBacteria; CAR83040; CAR83040; lmo4a_0338. DR GeneID; 12515591; -. DR KEGG; lml:lmo4a_0338; -. DR PATRIC; 43106631; VBILisMon174077_0352. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; LMON563174:GLFX-353-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22444 MW; 1CA16767F5492E91 CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGVGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEGIRQVI ASCAGKMKIG LSVHSVSEAA EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GIKLPIVGIG GINEKNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GSPS // ID E1URJ2_BACAS Unreviewed; 230 AA. AC E1URJ2; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Inhibitor of thiaminase TenA; GN Name=tenI; OrderedLocusNames=BAMF_1240; OS Bacillus amyloliquefaciens (strain ATCC 23350 / DSM 7 / BCRC 11601 / OS NBRC 15535 / NRRL B-14393). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=692420; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM7; RX DOI=10.1099/ijs.0.023267-0 ; RA Borriss R., Chen X., Rueckert C., Blom J., Becker A., Baumgarth B., RA Fan B., Pukall R., Schumann P., Sproer C., Junge H., Vater J., RA Puhler A., Klenk H.P.; RT "Relationship of Bacillus amyloliquefaciens clades associated with RT strains DSM7T and FZB42: a proposal for Bacillus amyloliquefaciens RT subsp. amyloliquefaciens subsp. nov. and Bacillus amyloliquefaciens RT subsp. plantarum subsp. nov. based on their discriminating complete RT genome sequences."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23350 / DSM 7 / BCRC 11601 / NBRC 15535 / NRRL B-14393; RX PubMed=21262282; DOI=10.1016/j.jbiotec.2011.01.006; RA Ruckert C., Blom J., Chen X., Reva O., Borriss R.; RT "Genome sequence of B. amyloliquefaciens type strain DSM7(T) reveals RT differences to plant-associated B. amyloliquefaciens FZB42."; RL J. Biotechnol. 155:78-85(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN597644; CBI42366.1; -; Genomic_DNA. DR RefSeq; YP_003919836.1; NC_014551.1. DR ProteinModelPortal; E1URJ2; -. DR EnsemblBacteria; CBI42366; CBI42366; BAMF_1240. DR GeneID; 9780271; -. DR KEGG; bao:BAMF_1240; -. DR PATRIC; 42471508; VBIBacAmy172706_1332. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR BioCyc; BAMY692420:GHU2-1327-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 230 AA; 25578 MW; 0431F61070EB11A9 CRC64; MNINFGEWLI KKKAGPERAE KRWSPLELHA VTDNRKPVAE LAEDILSIQH EVSFIHIRER DKTAGEIMQL LALLKKGGAD KDKLVINDRA DVALFANIHR VQLPARSFSV KQVRNRFPHL HIGRSVHSLK EAVQAEKEDA DYVVFGHVFE TECKQGLEAR GISLLSDIKS TLSIPVIAIG GVTLQTIGKA KQAKPDGIAV MSGIFSAENP EEAAKRYARA IREADYEEAL // ID E1UTH5_BACAS Unreviewed; 222 AA. AC E1UTH5; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BAMF_3666; OS Bacillus amyloliquefaciens (strain ATCC 23350 / DSM 7 / BCRC 11601 / OS NBRC 15535 / NRRL B-14393). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=692420; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM7; RX DOI=10.1099/ijs.0.023267-0 ; RA Borriss R., Chen X., Rueckert C., Blom J., Becker A., Baumgarth B., RA Fan B., Pukall R., Schumann P., Sproer C., Junge H., Vater J., RA Puhler A., Klenk H.P.; RT "Relationship of Bacillus amyloliquefaciens clades associated with RT strains DSM7T and FZB42: a proposal for Bacillus amyloliquefaciens RT subsp. amyloliquefaciens subsp. nov. and Bacillus amyloliquefaciens RT subsp. plantarum subsp. nov. based on their discriminating complete RT genome sequences."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23350 / DSM 7 / BCRC 11601 / NBRC 15535 / NRRL B-14393; RX PubMed=21262282; DOI=10.1016/j.jbiotec.2011.01.006; RA Ruckert C., Blom J., Chen X., Reva O., Borriss R.; RT "Genome sequence of B. amyloliquefaciens type strain DSM7(T) reveals RT differences to plant-associated B. amyloliquefaciens FZB42."; RL J. Biotechnol. 155:78-85(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN597644; CBI44792.1; -; Genomic_DNA. DR RefSeq; YP_003922262.1; NC_014551.1. DR EnsemblBacteria; CBI44792; CBI44792; BAMF_3666. DR GeneID; 9778726; -. DR KEGG; bao:BAMF_3666; -. DR PATRIC; 42476785; VBIBacAmy172706_3940. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; BAMY692420:GHU2-3786-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23553 MW; 3A14191D1C159089 CRC64; MTRISREMMK DILSVYFIMG SNNTSADPVS VVKKAIEGGA TLFQFREKGS GSLTGEDLVL FAKQVQDVCR RAGIPFIIND DVELALRLEA DGVHIGQDDA DAEETRAAIG DMILGVSAHN VSEVKLAEAA GADYVGMGPV YPTETKKDAE AVQGVTLIEE VRRQGITIPI VGIGGITADN AAPVIEAGAD GVSMISAISQ AEDPKAAARR FFEEVRRSKA KS // ID E1V9M3_HALED Unreviewed; 315 AA. AC E1V9M3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 13-NOV-2013, entry version 23. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=HELO_1973; OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB OS 2198 / 1H9). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=768066; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9; RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x; RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G., RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., RA Oesterhelt D., Kunte H.J.; RT "A blueprint of ectoine metabolism from the genome of the industrial RT producer Halomonas elongata DSM 2581(T)."; RL Environ. Microbiol. 13:1973-1994(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN869568; CBV41857.1; -; Genomic_DNA. DR RefSeq; YP_003897042.1; NC_014532.1. DR ProteinModelPortal; E1V9M3; -. DR EnsemblBacteria; CBV41857; CBV41857; HELO_1973. DR GeneID; 9747300; -. DR KEGG; hel:HELO_1973; -. DR PATRIC; 42353181; VBIHalElo161731_1035. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; HELO768066:GJEE-1009-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 35581 MW; 70898CBF2009C532 CRC64; MVKRRVHVAA AAIISADSRE VLLARRPSNV DQGGLWEFPG GKLAPYETGL EALKRELHEE LGVEIRRAQP LIRIHHEYAD KHVLLDVWQV HDFAGEPFGR EGQAVRWVPM EELHSYPFPA ANLPILRAVM LPTEYLISAE EDDEDVFLER LERAMREDGV RLVQLRAKTL DEDAYVARAE KALAMCRRFG ARLMLNGEPS LLERVEADGI HLTSERLMSL ERRPISEEKW LAASTHDQAQ LTQAHRIGCD FVTLSPLRTT PSHPEVAPIG WHDFQQLVEH AGMPVFALGG MTRHDANHAR AVGAQGIASI RDFWK // ID E1VBN0_HALED Unreviewed; 209 AA. AC E1VBN0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HELO_4303; OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB OS 2198 / 1H9). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=768066; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9; RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x; RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G., RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., RA Oesterhelt D., Kunte H.J.; RT "A blueprint of ectoine metabolism from the genome of the industrial RT producer Halomonas elongata DSM 2581(T)."; RL Environ. Microbiol. 13:1973-1994(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN869568; CBV44187.1; -; Genomic_DNA. DR RefSeq; YP_003899372.1; NC_014532.1. DR EnsemblBacteria; CBV44187; CBV44187; HELO_4303. DR GeneID; 9748599; -. DR KEGG; hel:HELO_4303; -. DR PATRIC; 42358284; VBIHalElo161731_3542. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; HELO768066:GJEE-3385-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21556 MW; 2F665353FDF94863 CRC64; MRVDLSLYLV TDPELCAERG LEETVVAAVR GGVTLVQLRD KHASDAELVP VARRLKTALA GSSVPLLIND RLEVALASGA DGLHIGQDDG EVDDARAALG ADAILGLSVQ TPEQLARINA AKLDYLGLGP VFATPSKRDH AQPLGFDGLA ELAGASPLPT VAIGGLKAEH VEAVRRAGAD GLAVISAICG TPDPEAAARS FHQGVAPRR // ID E1VGF0_9GAMM Unreviewed; 208 AA. AC E1VGF0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HDN1F_03090; OS gamma proteobacterium HdN1. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=83406; RN [1] RP NUCLEOTIDE SEQUENCE. RA Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., RA Ehrenreich P., Behrends A., Wilkes H., Kube M., Reinhardt R., RA Zedelius J.; RT "Alkane degradation by a new type of denitrifying bacterium with RT possible involvement of the electron acceptor in substrate RT activation."; RL Environ. Microbiol. 0:0-0(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929140; CBL43892.1; -; Genomic_DNA. DR RefSeq; YP_003809558.1; NC_014366.1. DR EnsemblBacteria; CBL43892; CBL43892; HDN1F_03090. DR GeneID; 9700062; -. DR KEGG; gpb:HDN1F_03090; -. DR PATRIC; 42343309; VBIGamPro61291_0337. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; GPRO83406:GIWA-314-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22095 MW; 5F527F63B1837BDA CRC64; MRGLYVITDP ILTPPDLLEK KVRAALLGGA AIVQYRNKDA GAKARRLQEA QSLRALTDEY GALLIINDDT ELALACNADG VHVGLEDTPI ALARAQLGLQ RIVGATCHGD TQLALRAIEE GADYVAFGRF FGSNTKPDAP PAALDAIRPA LSRLTRPAVA IGGIRLENAQ PLVNAGFAML AVVGDVFSHD SAEITLHCAA YARLFQNK // ID E1VHH2_9GAMM Unreviewed; 326 AA. AC E1VHH2; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 22-JAN-2014, entry version 21. DE SubName: Full=Mutator MutT; GN Name=mutT; ORFNames=HDN1F_06810; OS gamma proteobacterium HdN1. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=83406; RN [1] RP NUCLEOTIDE SEQUENCE. RA Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., RA Ehrenreich P., Behrends A., Wilkes H., Kube M., Reinhardt R., RA Zedelius J.; RT "Alkane degradation by a new type of denitrifying bacterium with RT possible involvement of the electron acceptor in substrate RT activation."; RL Environ. Microbiol. 0:0-0(2010). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929140; CBL44264.1; -; Genomic_DNA. DR RefSeq; YP_003809925.1; NC_014366.1. DR ProteinModelPortal; E1VHH2; -. DR EnsemblBacteria; CBL44264; CBL44264; HDN1F_06810. DR GeneID; 9702490; -. DR KEGG; gpb:HDN1F_06810; -. DR PATRIC; 42344131; VBIGamPro61291_0737. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR BioCyc; GPRO83406:GIWA-697-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 326 AA; 35428 MW; 2E4AABD21DA26952 CRC64; MTTPVHVVAA VIRGRDGRIL LAQRPAHLHQ GGKWEFPGGK VEAGEGAEQA LARELREELG ITPVVTRPLI QVQHRYPQEG AHPEKTVFLD VWEVVAFSGQ PSGRERQRVE WVAQDALEDY EFPPANQPIV VAAQLPSTIL ITPEPAEFPA ESFYSHLDAS LEAGVGWVIL RSNKLSAQDF TELAAGVAEL CAEFEVPLSL NPPPEVLKQM LKKGDAGLPE GVGLHLSEAA LREYQDEYDG CVSASCHSPE ALRLAEERNV TFALLSPIQA TASHPDVEPL GWVRASEWIK PSKVPIYALG SLGNADVIVA RKNGAQGVAG IRAFWK // ID E1VRP7_ARTAR Unreviewed; 213 AA. AC E1VRP7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 27. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AARI_00580; OS Arthrobacter arilaitensis (strain DSM 16368 / CIP 108037 / JCM 13566 / OS Re117). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=861360; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16368 / CIP 108037 / JCM 13566 / Re117; RX PubMed=21124797; DOI=10.1371/journal.pone.0015489; RA Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B., RA Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., RA Irlinger F., Vallaeys T.; RT "The Arthrobacter arilaitensis Re117 genome sequence reveals its RT genetic adaptation to the surface of cheese."; RL PLoS ONE 5:E15489-E15489(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16368 / CIP 108037 / JCM 13566 / Re117; RA Genoscope.; RT "Complete genome sequence of Arthrobacter arilaitensis (strain DSM RT 16368 / CIP 108037 / JCM 13566 / Re117)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ311875; CBT74300.1; -; Genomic_DNA. DR RefSeq; YP_003915271.1; NC_014550.1. DR EnsemblBacteria; CBT74300; CBT74300; AARI_00580. DR GeneID; 9794440; -. DR KEGG; aai:AARI_00580; -. DR PATRIC; 42166623; VBIArtAri166201_0101. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; AARI861360:GI6T-62-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 21779 MW; 64EE9ED443585972 CRC64; MHNYGAYLVA NTASCTPRST LEVIEGAVAG GIGWIQLRAK DESAREFFEL ACAAAKLTEG KAQLLINDRI DVYLAARAAG AAVNGIHIGQ KDVPVQLARQ IIGEGIIGLS ASSDEQLAQA NKVASVIDYL GVGAIRATPT KKDHPAPLGL DGFARAAALA KLPCVAIGAI TQDDAAAIRA GGGAGLAVVR AICNAEDPQL ASAQLVAAWE ASK // ID E1W4F6_HAEP3 Unreviewed; 225 AA. AC E1W4F6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PARA_11420; OS Haemophilus parainfluenzae (strain T3T1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=862965; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T3T1; RA Crook D., Hood D., Moxon R., Parkhill J., Aslett M., Bentley S.D.; RT "The genome sequence of Haemophilus parainfluenzae T3T1."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ312002; CBW15248.1; -; Genomic_DNA. DR RefSeq; YP_004822837.1; NC_015964.1. DR EnsemblBacteria; CBW15248; CBW15248; PARA_11420. DR GeneID; 11117005; -. DR KEGG; hpr:PARA_11420; -. DR PATRIC; 43051434; VBIHaePar168133_1143. DR KO; K00788; -. DR BioCyc; HPAR862965:GH07-1174-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 24759 MW; BB473039CA1F46A8 CRC64; MKNIQEILPL YFVAGTQDCR HLGDNLADNL LSVLRQALEG GITCFQFRDK GKFSLENSPT EQRALAIKCR DLCRQYNVPF IVDDNVDLAL EIEADGIHVG QSDTPVKTIR ARTHKPFIIG WSINRLDEAK IGEELSEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRKA GITKPLVAIG GVKLEHVKTL RKYGADGIAV ITAISQAKDI KASTKALKEA SGCNH // ID E1WEK7_SALTS Unreviewed; 211 AA. AC E1WEK7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SL1344_4102; OS Salmonella typhimurium (strain SL1344). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=216597; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SL1344; RA Dougan G., Barrow P., Achtman M., Parkhill J., Thomson N.R.; RT "The genome sequence of Salmonella enterica subsp. enterica serovar RT Typhimurium SL1344."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SL1344; RX PubMed=22538806; DOI=10.1073/pnas.1201061109; RA Kroger C., Dillon S.C., Cameron A.D., Papenfort K., Sivasankaran S.K., RA Hokamp K., Chao Y., Sittka A., Hebrard M., Handler K., Colgan A., RA Leekitcharoenphon P., Langridge G.C., Lohan A.J., Loftus B., RA Lucchini S., Ussery D.W., Dorman C.J., Thomson N.R., Vogel J., RA Hinton J.C.; RT "The transcriptional landscape and small RNAs of Salmonella enterica RT serovar Typhimurium."; RL Proc. Natl. Acad. Sci. U.S.A. 109:E1277-E1286(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ312003; CBW20190.1; -; Genomic_DNA. DR RefSeq; YP_005183968.1; NC_016810.1. DR ProteinModelPortal; E1WEK7; -. DR EnsemblBacteria; CBW20190; CBW20190; SL1344_4102. DR PATRIC; 43194559; VBISalEnt88447_4565. DR OMA; AVRPSYI; -. DR BioCyc; SENT216597:GJB7-4184-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22983 MW; 803CF861FC550D88 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE SGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID E1WP98_BACF6 Unreviewed; 204 AA. AC E1WP98; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BF638R_2547; OS Bacteroides fragilis (strain 638R). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=862962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=638R; RA Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., RA Bertalan M., Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., RA Bignell A., Barron A., Clark L., Bentley S.D., Parkhill J.; RT "Twenty-eight divergent polysaccharide loci specifying within- and RT amongst-strain capsule diversity in three strains of Bacteroides RT fragilis."; RL Microbiology 156:3255-3269(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ312004; CBW23053.1; -; Genomic_DNA. DR RefSeq; YP_005111593.1; NC_016776.1. DR EnsemblBacteria; CBW23053; CBW23053; BF638R_2547. DR GeneID; 11702993; -. DR KEGG; bfg:BF638R_2547; -. DR PATRIC; 42748121; VBIBacFra167533_2614. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; BFRA862962:GHND-2473-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22029 MW; 4F3DFB89174A051A CRC64; MLSLQFITHQ TENYSYLESA RMALEGGCKW IQLRMKEASP EEVEAVALQL KPLCKAKEAI LILDDHVELA KKLEVDGVHL GKKDMPIGEA RQILGEAFII GGTANTFEDV KLHHAAGADY LGIGPFRFTT TKKNLSPVLG LEGYTSILAQ MNEAGIRIPV VAIGGIVAED IPAIMETGVN GIALSGAILQ APDPVEETKR ILNI // ID E1WPA4_BACF6 Unreviewed; 202 AA. AC E1WPA4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase; GN OrderedLocusNames=BF638R_2553; OS Bacteroides fragilis (strain 638R). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=862962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=638R; RA Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., RA Bertalan M., Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., RA Bignell A., Barron A., Clark L., Bentley S.D., Parkhill J.; RT "Twenty-eight divergent polysaccharide loci specifying within- and RT amongst-strain capsule diversity in three strains of Bacteroides RT fragilis."; RL Microbiology 156:3255-3269(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ312004; CBW23059.1; -; Genomic_DNA. DR RefSeq; YP_005111599.1; NC_016776.1. DR ProteinModelPortal; E1WPA4; -. DR SMR; E1WPA4; 1-202. DR EnsemblBacteria; CBW23059; CBW23059; BF638R_2553. DR GeneID; 11702999; -. DR KEGG; bfg:BF638R_2553; -. DR PATRIC; 42748133; VBIBacFra167533_2620. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR BioCyc; BFRA862962:GHND-2479-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 23245 MW; A6533F52928C16DB CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHKRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYSGH ISCSCHSVEE VKNKKHFYDY VFMSPVYDSI SKEGYNSPYT AEELRLAAKD KIIDNKVMAL GGITPDNILE VKDFGFGGAV VLGDLWGKFD ACSDQDYLAV IEHFKKLKRM AD // ID E1XA52_HAEI1 Unreviewed; 226 AA. AC E1XA52; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HIB_05280; OS Haemophilus influenzae (strain 10810). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=862964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=10810; RA Crook D., Hood D., Moxon R., Bentley S.D., Aslett M., Parkhill J.; RT "The genome sequence of Haemophilus influenzae 10810."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ312006; CBW28716.1; -; Genomic_DNA. DR RefSeq; YP_005178558.1; NC_016809.1. DR EnsemblBacteria; CBW28716; CBW28716; HIB_05280. DR GeneID; 11768901; -. DR KEGG; hiu:HIB_05280; -. DR PATRIC; 43038361; VBIHaeInf165663_0545. DR KO; K00788; -. DR BioCyc; HINF862964:GHI0-554-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24759 MW; 34F34A2DC6C39046 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMSVQEIR AKTDKPLIIG WSVNRLDEAK MGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QTATKALREA SDEYAK // ID E1XFJ0_STRZO Unreviewed; 209 AA. AC E1XFJ0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPNOXC06500; OS Streptococcus pneumoniae serotype 3 (strain OXC141). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=869215; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OXC141; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ312027; CBW32307.1; -; Genomic_DNA. DR RefSeq; YP_006064131.1; NC_017592.1. DR ProteinModelPortal; E1XFJ0; -. DR EnsemblBacteria; CBW32307; CBW32307; SPNOXC06500. DR GeneID; 12891029; -. DR KEGG; snx:SPNOXC_06500; -. DR PATRIC; 43230520; VBIStrPne166247_0749. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SPNE869215:GLLA-652-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID E1XFJ7_STRZO Unreviewed; 210 AA. AC E1XFJ7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPNOXC06570; OS Streptococcus pneumoniae serotype 3 (strain OXC141). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=869215; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OXC141; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ312027; CBW32314.1; -; Genomic_DNA. DR RefSeq; YP_006064138.1; NC_017592.1. DR ProteinModelPortal; E1XFJ7; -. DR EnsemblBacteria; CBW32314; CBW32314; SPNOXC06570. DR GeneID; 12891036; -. DR KEGG; snx:SPNOXC_06570; -. DR PATRIC; 43230534; VBIStrPne166247_0756. DR KO; K00788; -. DR OMA; MEASHIS; -. DR BioCyc; SPNE869215:GLLA-659-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID E1XIW0_STRZN Unreviewed; 209 AA. AC E1XIW0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPNINV200_06330; OS Streptococcus pneumoniae serotype 14 (strain INV200). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=869216; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=INV200; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ312029; CBW34266.1; -; Genomic_DNA. DR RefSeq; YP_006065959.1; NC_017593.1. DR EnsemblBacteria; CBW34266; CBW34266; SPNINV200_06330. DR GeneID; 12893405; -. DR KEGG; snv:SPNINV200_06330; -. DR PATRIC; 43225704; VBIStrPne166962_0723. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SPNE869216:GLL9-638-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23362 MW; A51A41EFBB2CC783 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID E1XIW7_STRZN Unreviewed; 210 AA. AC E1XIW7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPNINV200_06400; OS Streptococcus pneumoniae serotype 14 (strain INV200). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=869216; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=INV200; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ312029; CBW34273.1; -; Genomic_DNA. DR RefSeq; YP_006065966.1; NC_017593.1. DR EnsemblBacteria; CBW34273; CBW34273; SPNINV200_06400. DR GeneID; 12893412; -. DR KEGG; snv:SPNINV200_06400; -. DR PATRIC; 43225718; VBIStrPne166962_0730. DR KO; K00788; -. DR OMA; MEASHIS; -. DR BioCyc; SPNE869216:GLL9-645-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22772 MW; FD46268D3AB58688 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIIQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID E1XQB8_STRZI Unreviewed; 209 AA. AC E1XQB8; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=INV104_05970; OS Streptococcus pneumoniae serotype 1 (strain INV104). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=869269; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=INV104; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ312030; CBW36280.1; -; Genomic_DNA. DR RefSeq; YP_006062275.1; NC_017591.1. DR ProteinModelPortal; E1XQB8; -. DR EnsemblBacteria; CBW36280; CBW36280; INV104_05970. DR GeneID; 12888871; -. DR KEGG; sni:INV104_05970; -. DR PATRIC; 43220827; VBIStrPne166045_0775. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SPNE869269:GLL8-602-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID E1XQC5_STRZI Unreviewed; 210 AA. AC E1XQC5; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=INV104_06040; OS Streptococcus pneumoniae serotype 1 (strain INV104). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=869269; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=INV104; RX PubMed=17675389; DOI=10.1128/JB.00690-07; RA Hiller N.L., Janto B., Hogg J.S., Boissy R., Yu S., Powell E., RA Keefe R., Ehrlich N.E., Shen K., Hayes J., Barbadora K., Klimke W., RA Dernovoy D., Tatusova T., Parkhill J., Bentley S.D., Post J.C., RA Ehrlich G.D., Hu F.Z.; RT "Comparative genomic analyses of seventeen Streptococcus pneumoniae RT strains: insights into the pneumococcal supragenome."; RL J. Bacteriol. 189:8186-8195(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ312030; CBW36287.1; -; Genomic_DNA. DR RefSeq; YP_006062282.1; NC_017591.1. DR ProteinModelPortal; E1XQC5; -. DR EnsemblBacteria; CBW36287; CBW36287; INV104_06040. DR GeneID; 12888878; -. DR KEGG; sni:INV104_06040; -. DR PATRIC; 43220841; VBIStrPne166045_0782. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; SPNE869269:GLL8-609-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22744 MW; A3239DF7871A7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID E1YBB4_9DELT Unreviewed; 535 AA. AC E1YBB4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=N47_C18490; OS uncultured Desulfobacterium sp. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfobacterium; environmental samples. OX NCBI_TaxID=201089; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=21176053; DOI=10.1111/j.1462-2920.2010.02391.x; RA Bergmann F., Selesi D., Weinmaier T., Tischler P., Rattei T., RA Meckenstock R.U.; RT "Genomic insights into the metabolic potential of the polycyclic RT aromatic hydrocarbon degrading sulfate-reducing Deltaproteobacterium RT N47."; RL Environ. Microbiol. 13:1125-1137(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR695867; CBX27791.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009030; F:thiamine-phosphate kinase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR000728; AIR_synth_N_dom. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016188; PurM_N-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR006283; ThiL. DR InterPro; IPR003733; TMP_synthase. DR PANTHER; PTHR30270; PTHR30270; 1. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55326; SSF55326; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR01379; thiL; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 535 AA; 57227 MW; D392093AAC969AE1 CRC64; MFGKNLKKAL RFYFITDDSA PVLTPSEQAK IAIRAGAGAI QYRNKSFTSM YYDEASEIRD LCRCNGVLFI VNDNILLAKL LKADGVHLGQ YDESSAAARK ILGPDAIVGI SVSTPEELYK SNISNCDYIG TGPVFFTGTK KDAKKVIGLF GLKSVAEKSC LPVVAIGGID ASSAPSCFAG GAAGVAVISA ISRAPDPLNS ALKLGEACFC SSRSYIESPW SHDAGPGEFG LIEKLIKNIP AHPEAIVSPG DDACLLSAIS NPVITSDTQR EGVHFLLNRQ TPEEIGIKAV EITLSDLAAC YARPVALFIN LCLPSYVSGN TVEEIYKGVL NALNKHECAL AGGNISSGSE LALDLFAIGE ARKDLFPKRL NAKPGYGLYC TGPLGLARAG LELLNNNDTD FPDLVLKFKF PKARFDAAHI LANAGIDCVM DISDGLYGDA GHIAKASQVT IELDLNSCPF DPSLLLFCQK YGRKTEEIIV EGGEDYELLF ACHPDTYKTI ADKLKTSFQA GRCLAFNGKH IISPFGTGSF RHGKK // ID E1YVC9_9PORP Unreviewed; 198 AA. AC E1YVC9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 13-NOV-2013, entry version 15. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF9008_00607; OS Parabacteroides sp. 20_3. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=469591; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=20_3; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Strauss J., Sibley C., RA White A., Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 20_3."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774987; EFK62462.1; -; Genomic_DNA. DR EnsemblBacteria; EFK62462; EFK62462; HMPREF9008_00607. DR PATRIC; 40936525; VBIBacSp9858_2694. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 198 AA; 22132 MW; 15CA86F587B0CB11 CRC64; MNKLVVITTP YFFADEASLI ELLFAEGMSR LHLRKPDCKR DELEGLLDNI SPAYYDRIVL HDWFTLAEER ALGGVHLNKR NPEAPPLYKG SISRSCHSLE EIIEYKPVCD YVFLSPIFQS ISKEGYGSGF PLDGLRNAKG IIDDKVIALG GICPQTITKL KDIPFGGVAV LGALWGNDPS LLVADQLIKQ FKRLQVWP // ID E1YVD0_9PORP Unreviewed; 242 AA. AC E1YVD0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9008_00608; OS Parabacteroides sp. 20_3. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=469591; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=20_3; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Strauss J., Sibley C., RA White A., Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 20_3."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774987; EFK62463.1; -; Genomic_DNA. DR EnsemblBacteria; EFK62463; EFK62463; HMPREF9008_00608. DR PATRIC; 40936527; VBIBacSp9858_2695. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 163 165 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 HMP-PP (By similarity). FT BINDING 199 199 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 242 AA; 26741 MW; F1CF1868910CC287 CRC64; MALNYYFGYD ENGRVGRRTT GLRPPFGGNN RLMFITHRTP KYTECDEVRM AIQGGCSWIQ LRMKDGIYED TVRTCATICA EECERIVDFC VNDDLEAAVT CGATACHLGK NDMPLDIAWE VLKDKLDSNA IFYIGATANT FEDIRLAVER GASYIGLGPY RFTGTKKNLS PILGLEGYRK IIAQCKEAGI DIPIFAIGGI TLEDVGPLME TGITGIAVSG AIINAPDPVE ETRRFIEEIN KY // ID E1Z522_CHLVA Unreviewed; 202 AA. AC E1Z522; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-APR-2014, entry version 10. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=CHLNCDRAFT_138010; OS Chlorella variabilis (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; Chlorellales; OC Chlorellaceae; Chlorella. OX NCBI_TaxID=554065; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NC64A; RX PubMed=20852019; DOI=10.1105/tpc.110.076406; RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A., RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A., RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., RA Van Etten J.L.; RT "The Chlorella variabilis NC64A genome reveals adaptation to RT photosymbiosis, coevolution with viruses, and cryptic sex."; RL Plant Cell 22:2943-2955(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL433836; EFN59447.1; -; Genomic_DNA. DR RefSeq; XP_005851549.1; XM_005851487.1. DR GeneID; 17358603; -. DR KEGG; cvr:CHLNCDRAFT_138010; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 21437 MW; 19F125D6B6BCFC20 CRC64; MAFRLVLITP PEAATPRELE LATSLFKRGL CTLHLRKPSC DREQVAQYLA ALPPDARRRT VLHQHHDLAK QSSIGGIHYR EAERPPGVIK APPGLSVSTS FHTLPDLGVC RGEVDYCFLS PIYASISKPG YGEAAFPDPG ELAGGLAGSR YPVLALGGVT RDKFGELAEL GFAGAALLGA VWAAEDPLAA WEAAVAEAAR LG // ID E1ZK33_CHLVA Unreviewed; 671 AA. AC E1ZK33; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-APR-2014, entry version 21. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=CHLNCDRAFT_58425; OS Chlorella variabilis (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; Chlorellales; OC Chlorellaceae; Chlorella. OX NCBI_TaxID=554065; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NC64A; RX PubMed=20852019; DOI=10.1105/tpc.110.076406; RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A., RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A., RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., RA Van Etten J.L.; RT "The Chlorella variabilis NC64A genome reveals adaptation to RT photosymbiosis, coevolution with viruses, and cryptic sex."; RL Plant Cell 22:2943-2955(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL433850; EFN53733.1; -; Genomic_DNA. DR RefSeq; XP_005845835.1; XM_005845773.1. DR ProteinModelPortal; E1ZK33; -. DR GeneID; 17353267; -. DR KEGG; cvr:CHLNCDRAFT_58425; -. DR KO; K14153; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.910.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF03070; TENA_THI-4; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; SSF48613; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 671 AA; 69532 MW; C9C9BF9DB4CB2E28 CRC64; MPAPRDAGTA AEGYSAAMQR CPPNQAHLVG ALGELLQGVQ EELKLHDRVC CGEAWVEWGV DLSRHQQPNP ATRAYVDFLH KVAADPRQGV AAILAAMVPC LRLYAYLACQ LSRAFPFADH EYTEWNTRGV AAVHVAPVEF IRAQMAAVLG DIGADVVKTG MLPTPEVVEA VAQELQAQGL VKLVVDPVLV STSGDALATA GVVEAIRAHL FPLATIVTPN VPEASKLLDG RSIADLDGMK AAAEELHRYG PQWVLIKGGH LISEAGQGGL PELDAWPEGL APQRTVTDVL FDGKNMIELS EPYISTGNTH GTGCSLASAI AAELAKGADV ATAVRLAKKY VWRMLERSRD LPLGQGSQKP MNHGWAIADW STDLAAAGAA AAEQSAADQL PSCSHTAEAA REQVLAAAAR GTRIPNTCDL RVYAVTDPAC NAQHGRTNAG EWQAGRGRRS EAVQLALDGG ATVVQLREKD AEGGAFLEQV NACNGAGCPA SSPCCSSQAE GTLSSQAAAV LEVCRSRGVP LLINDRVDVA LAVGADGVHV GQGDLPAAAV RRMIGPDRIL GVSGKTPEEA VRAEVEGADY LGAGAVFPTG TKDSEVIGVQ RLAEVCRAVS IPVVSIGGIK ASNAAETIAA GCAGAAVVSG IFGADSPADA SRELLAAVDA ALAQRAAQLE P // ID E1ZLW1_CHLVA Unreviewed; 997 AA. AC E1ZLW1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-APR-2014, entry version 13. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=CHLNCDRAFT_137054; OS Chlorella variabilis (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; Chlorellales; OC Chlorellaceae; Chlorella. OX NCBI_TaxID=554065; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NC64A; RX PubMed=20852019; DOI=10.1105/tpc.110.076406; RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A., RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A., RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., RA Van Etten J.L.; RT "The Chlorella variabilis NC64A genome reveals adaptation to RT photosymbiosis, coevolution with viruses, and cryptic sex."; RL Plant Cell 22:2943-2955(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL433852; EFN53205.1; -; Genomic_DNA. DR RefSeq; XP_005845307.1; XM_005845245.1. DR GeneID; 17352612; -. DR KEGG; cvr:CHLNCDRAFT_137054; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 997 AA; 103650 MW; DB18D69BBB6DF83D CRC64; MQQRLHAAAQ ARLLPGLHRL GCGACPAPIL AFRVGAQRVD SSSPRLARRG TALVTTARQS SQEAGSGASG GVGLFPAGKR QARVQLPALM LAVTAADVLD PAQAGGALEA LSAAVAGGAT AVVLAQGADG GGSGGAELYE AAVRLKELLR GRAVLLIADR TDIVDAAGAD GALLTGAGLP TMVAKRMLQD GLALVGRVVS SAEAAAEAAA DGANFVILEP SGPGLAAPNS AEAVASQQQQ RSSASIPVVA AVSGEAGRDQ LAQLLAAGVD GLVVQLGDLQ PVAAALARRQ PAGAGEAAAA VMQQLAGGVA PPAASLPADA AAAAAGPPQA VQQAVQLSQL LSTSREELVD AERQLFTEAS PAAAVLAFLE RWCPQMGEAQ LLRDAVKQLD ELFLLVVLGE FNSGKSAVVN ALLGQRYLAE GILPTTNEIN VLKHADPEHV QTAAQDGDGV FTRYLPAELL REVNVVDTPG TNVILGRQQR LTEEYVPRAD LVLFVLSADR PLTESEVRFL QYVRQWGKKV VFVVNKTDIL SSAAEVAEVV SFVRSNAARV LGVDEPQVLA VSARAAMQAK LEVLGDGSNG NGKLSGEQAA ALAAHPAWQR SGFEPLERFI FEFLTGGNPA AAAAATAGSN GTARGGGEGR QAGAESVRLK LESPLFVADA LLGAAAQQLE QELAVAQQDA ASVSIVRSQL AAFRREMEKE GQLQRDEVQR QVAGTAKKAA AIVDSMLQAR CHAVLCHDLS NMEVITSYLF GRADDKRALP VAAKFDEEMA AEATAGLTGL VKEHSAWLAS NCQRQLANYR HAPTPCAVLD VPPISRLALA RRVHLTFAEQ RAAALDETLD GLLSTELEGL DSDAGARRRW REMRQLTTEA EVAAADGGPP PDAEAALVML EEEVREAVIS TAGTAAGAAG FGVLLTAILP TTVEDLLALC LAAMVGYVSI LNLPMRRAEA KRKLEHTTTA FAQLTAAEVR RVEQAEAARG QLVDTLDRLK QRVANVE // ID E2CBZ6_9RHOB Unreviewed; 202 AA. AC E2CBZ6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=TRICHSKD4_0531; OS Roseibium sp. TrichSKD4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseibium. OX NCBI_TaxID=744980; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TrichSKD4; RA Mann E., Barbeau K., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL476302; EFO34044.1; -; Genomic_DNA. DR EnsemblBacteria; EFO34044; EFO34044; TRICHSKD4_0531. DR PATRIC; 41697762; VBIRosSp158592_0510. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 22334 MW; EF730DF8B740720F CRC64; MKLDPFYLIV DRASWIERLG PLGLKLVQLR VKDLEDDDLR AEIRSAKSIC DRLGVTLVIN DFWQMAIEEK CNWIHLGQED LTDVDLDAIR AAGLKFGLSS HDDAELDTAI AAKPDYIALG PVFPTILKKM KWAPQGLEKL RIWKERIGDI PLVAIGGLTP ERASAALDHG ADIASVVTDI TLNDNPEARA KEWIAATAKA RG // ID E2CJC4_9RHOB Unreviewed; 213 AA. AC E2CJC4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TRICHSKD4_3184; OS Roseibium sp. TrichSKD4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseibium. OX NCBI_TaxID=744980; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TrichSKD4; RA Mann E., Barbeau K., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL476315; EFO31491.1; -; Genomic_DNA. DR EnsemblBacteria; EFO31491; EFO31491; TRICHSKD4_3184. DR PATRIC; 41702910; VBIRosSp158592_3037. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 213 AA; 22615 MW; ABD0BE570AD0D1DE CRC64; MNRPRLFLIT PPSFETAEMA TKLSEALAGG DVACVLIYMP EASSRDVQAA AELLVPIAQE AGAAALIYGD TQAAGRTGAD GVHVDKSLDD IKMAVESFQP AKIVGAGGTK LKHEDMETAE TGIDYLFFGK LDLEEQDEAH SKTLSKADWW AELFETPCVA LGGKTLHSVE AAAATGADFV ALKDAVWTHT DGPVAAVKAA NEILEKHPFE EDD // ID E2JWT3_ECO57 Unreviewed; 211 AA. AC E2JWT3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECH7EC4206_A3678; OS Escherichia coli O157:H7 str. EC4206. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=444447; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4206; RA Rosovitz M.J., Ravel J.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4206; RA Rasko D., Rosovitz M., Myers G., Seshadri R., Cer R., Jiang L., RA Ravel J., Fricke W.F., Sebastian Y.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHK02000001; EDZ77586.1; -; Genomic_DNA. DR ProteinModelPortal; E2JWT3; -. DR SMR; E2JWT3; 10-209. DR EnsemblBacteria; EDZ77586; EDZ77586; ECH7EC4206_A3678. DR PATRIC; 26622452; VBIEscCol88510_2401. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E2KA35_ECO57 Unreviewed; 211 AA. AC E2KA35; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECH7EC4045_A0750; OS Escherichia coli O157:H7 str. EC4045. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=444448; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4045; RA Rosovitz M.J., Ravel J.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4045; RA Eppinger M., Sebastian Y., Ravel J.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHL02000001; EDZ83310.1; -; Genomic_DNA. DR ProteinModelPortal; E2KA35; -. DR SMR; E2KA35; 10-209. DR EnsemblBacteria; EDZ83310; EDZ83310; ECH7EC4045_A0750. DR PATRIC; 26574383; VBIEscCol57045_2235. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E2KQF1_ECO57 Unreviewed; 211 AA. AC E2KQF1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECH74042_A1306; OS Escherichia coli O157:H7 str. EC4042. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=444449; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4042; RA Rosovitz M.J., Ravel J.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4042; RA Eppinger M., Sebastian Y., Ravel J.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHM02000001; EDZ87251.1; -; Genomic_DNA. DR ProteinModelPortal; E2KQF1; -. DR SMR; E2KQF1; 10-209. DR EnsemblBacteria; EDZ87251; EDZ87251; ECH74042_A1306. DR PATRIC; 26565227; VBIEscCol358_3479. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E2LT12_MONPE Unreviewed; 129 AA. AC E2LT12; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 22-JAN-2014, entry version 12. DE SubName: Full=Uncharacterized protein; DE Flags: Fragment; GN ORFNames=MPER_10198; OS Moniliophthora perniciosa (strain FA553 / isolate CP02) OS (Witches'-broom disease fungus) (Marasmius perniciosus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Agaricomycetidae; Agaricales; Marasmiaceae; OC mitosporic Marasmiaceae; Moniliophthora. OX NCBI_TaxID=554373; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FA553 / isolate CP02; RX PubMed=19019209; DOI=10.1186/1471-2164-9-548; RA Mondego J.M.C., Carazzolle M.F., Costa G.G.L., Formighieri E.F., RA Parizzi L.P., Rincones J., Cotomacci C., Carraro D.M., Cunha A.F., RA Carrer H., Vidal R.O., Estrela R.C., Garcia O., Thomazella D.P.T., RA de Oliveira B.V., Pires A.B.L., Rio M.C.S., Araujo M.R.R., RA de Moraes M.H., Castro L.A.B., Gramacho K.P., Goncalves M.S., RA Moura Neto J.P., Goes Neto A., Barbosa L.V., Guiltinan M.J., RA Bailey B.A., Meinhardt L.W., Cascardo J.C.M., Pereira G.A.G.; RT "A genome survey of Moniliophthora perniciosa gives new insights into RT Witches' broom disease of cacao."; RL BMC Genomics 9:548-548(2008). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABRE01015295; EEB91438.1; -; Genomic_DNA. DR RefSeq; XP_002390508.1; XM_002390467.1. DR GeneID; 7932113; -. DR KEGG; mpr:MPER_10198; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. FT NON_TER 1 1 SQ SEQUENCE 129 AA; 13605 MW; 049E3EED4CB1085B CRC64; MIDYSIYLVT GRDLLPAGKD FFETLEQVML FASLQGGVTV VQIREKKADT AEKSANGVDI ALAINASGVH VGQSDMPIAI ARKLLPKGAI IGASCNNLEE VKKALTDGAD YIGIGAVWAT TTKALDKPV // ID E2M708_PSEUB Unreviewed; 316 AA. AC E2M708; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 19. DE SubName: Full=MutT/nudix family protein; GN ORFNames=PSPTOT1_0314; OS Pseudomonas syringae pv. tomato T1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=546231; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T1; RX PubMed=19061402; DOI=10.1094/MPMI-22-1-0052; RA Almeida N.F., Yan S., Lindeberg M., Studholme D.J., Schneider D.J., RA Condon B., Liu H., Viana C.J., Warren A., Evans C., Kemen E., RA Maclean D., Angot A., Martin G.B., Jones J.D., Collmer A., RA Setubal J.C., Vinatzer B.A.; RT "A draft genome sequence of Pseudomonas syringae pv. tomato T1 reveals RT a type III effector repertoire significantly divergent from that of RT Pseudomonas syringae pv. tomato DC3000."; RL Mol. Plant Microbe Interact. 22:52-62(2009). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABSM01000001; EEB61950.1; -; Genomic_DNA. DR ProteinModelPortal; E2M708; -. DR EnsemblBacteria; EEB61950; EEB61950; PSPTOT1_0314. DR PATRIC; 25620402; VBIPseSyr88081_0011. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34190 MW; CB509F95F7ED2E29 CRC64; MKRVHVAAAV IRGTDGRVLI ARRAESQHQG GLWEFPGGKV EAGETVEIAL ARELQEELGI VVTATRPLIK VCHDYPDKQV LLDVWEVSAF TGEPHGAEGQ PLVWASPREL ANYDFPAANQ PIVAAARLPG EYLITPEGLD NIELLRGLQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAQ QLRKYASNGR PFPENRWLAA SCHSAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWEQ ATRLIAGFNK PVFLLGGVGP AQRQQAWESG AQGVAGIRAF WPDEII // ID E2M7T3_PSEUB Unreviewed; 205 AA. AC E2M7T3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-MAR-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSPTOT1_0589; OS Pseudomonas syringae pv. tomato T1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=546231; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T1; RX PubMed=19061402; DOI=10.1094/MPMI-22-1-0052; RA Almeida N.F., Yan S., Lindeberg M., Studholme D.J., Schneider D.J., RA Condon B., Liu H., Viana C.J., Warren A., Evans C., Kemen E., RA Maclean D., Angot A., Martin G.B., Jones J.D., Collmer A., RA Setubal J.C., Vinatzer B.A.; RT "A draft genome sequence of Pseudomonas syringae pv. tomato T1 reveals RT a type III effector repertoire significantly divergent from that of RT Pseudomonas syringae pv. tomato DC3000."; RL Mol. Plant Microbe Interact. 22:52-62(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABSM01000001; EEB62225.1; -; Genomic_DNA. DR ProteinModelPortal; E2M7T3; -. DR EnsemblBacteria; EEB62225; EEB62225; PSPTOT1_0589. DR PATRIC; 25620954; VBIPseSyr88081_0285. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22007 MW; A70BC30808744997 CRC64; MKLRGLYAIT DSQLLTGKFL SYVEAALDGG VTLLQYRDKT GDDSRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGQL ELAEQAKADG ATYVAFGRFF NSQTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAET PQEVTRRAKA FMALL // ID E2MYE6_CORAY Unreviewed; 260 AA. AC E2MYE6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CORAM0001_1434; OS Corynebacterium amycolatum SK46. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=553204; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK46; RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABZU01000016; EEB62529.1; -; Genomic_DNA. DR ProteinModelPortal; E2MYE6; -. DR EnsemblBacteria; EEB62529; EEB62529; CORAM0001_1434. DR PATRIC; 29090746; VBICorAmy112151_1848. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 2. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 208 208 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 260 AA; 27710 MW; AFF9C999E2CCEE6B CRC64; MNASSAATRT TRRALLADAR LYLCTDSRAS RGDLREFLHA CYEGGTDIIQ LRDKRVDTRD EIAAVETLAE VAAEHGKLFA VNDRADIAAL TGADILHVGQ EDLTTEQARQ IVGPEVLIGR SNRNLDMFAA SLADDGIDYA VIGPVYATPT KPDRQPVGVD MVREAAALVR RVRAQGSAES HQDSVADIVR PHDRSASDPV KPWWAIGGIN AETAGEVIGA GAERIVVVRA LTEAANPEEA ARALRAAVTG VDGIDSHGDK // ID E2NA09_9BACE Unreviewed; 205 AA. AC E2NA09; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BACCELL_01107; OS Bacteroides cellulosilyticus DSM 14838. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=537012; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14838; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14838; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides cellulosilyticus (DSM 14838)."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCH01000105; EEF91231.1; -; Genomic_DNA. DR ProteinModelPortal; E2NA09; -. DR EnsemblBacteria; EEF91231; EEF91231; BACCELL_01107. DR PATRIC; 26970708; VBIBacCel136693_0927. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 205 AA; 23055 MW; 824EC89828C000A3 CRC64; MKDRKMKLII ITSPDFIPDE ARIVTELFKA GLDLLHVRKP DADVHAVENL LQGIAPEYRT RIVIHDFFSL KDKYLLGGIH LNSRHPEAPA NYEGILSRAC HSLEEVETTV SLFNYVLMSP VYDSISKQGY RSGYSKDELK QAQESGVIHE KVVALGGISE VNLAEIKSLG FGGAALLGDI WNRYHTWKDA EELLAHFRRL KKIAG // ID E2NA12_9BACE Unreviewed; 206 AA. AC E2NA12; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACCELL_01110; OS Bacteroides cellulosilyticus DSM 14838. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=537012; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14838; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14838; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides cellulosilyticus (DSM 14838)."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCH01000105; EEF91234.1; -; Genomic_DNA. DR ProteinModelPortal; E2NA12; -. DR EnsemblBacteria; EEF91234; EEF91234; BACCELL_01110. DR PATRIC; 26970714; VBIBacCel136693_0930. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22536 MW; 7671C8C0AC47C241 CRC64; MFDVQFITHF TASISYSDSA RIALEGGCRW VQLRMKDASS EELKATAVQV QELCRQYGAT FIIDDHVELV KQIGADGVHL GKLDMPIKEA RERLGKDFII GGTANTFEDI RQHAADGADY IGCGPFRFTT TKQKLSPILG LDGYHSILTQ MREEGITIPV VAIGGITRED IPSLKASGLN GIALSGGILK AENPVREMET IIRLTQ // ID E2NJH3_9BACE Unreviewed; 202 AA. AC E2NJH3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BACCELL_04459; OS Bacteroides cellulosilyticus DSM 14838. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=537012; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14838; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14838; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides cellulosilyticus (DSM 14838)."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCH01000345; EEF87940.1; -; Genomic_DNA. DR ProteinModelPortal; E2NJH3; -. DR EnsemblBacteria; EEF87940; EEF87940; BACCELL_04459. DR PATRIC; 26976707; VBIBacCel136693_3964. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23366 MW; 5FD518103F8AEBBD CRC64; MKLIVVTAPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHRRIVTH EHFYLKEEFD LMGIHLNTRN PHEPHDYSGH VSYTCHSVEE VKSKKHFYDY VFMSPVYDCI SKEGILSGYT PEELRAAGKE RIIDTKVMAL GGITPDNILE IKDFGFGGAV VLGDLWNKFN VCTDRDYLGV IRHFKKLKEM AD // ID E2NVI2_9FIRM Unreviewed; 472 AA. AC E2NVI2; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.7.4.7; GN Name=thiD; ORFNames=CATMIT_02622; OS Catenibacterium mitsuokai DSM 15897. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Catenibacterium. OX NCBI_TaxID=451640; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15897; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCK01000430; EEF92773.1; -; Genomic_DNA. DR ProteinModelPortal; E2NVI2; -. DR EnsemblBacteria; EEF92773; EEF92773; CATMIT_02622. DR PATRIC; 30396728; VBICatMit90418_1921. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 472 AA; 51371 MW; 6ADF5342A00E6D30 CRC64; MKFNNDMLRL YAVTDRHWTG EQTLYEQVRD VLMGGATCLQ LREKDLDEAS FYEEAKNIKE LCRLFDVPFI INDNVMLAKE IDADGVHVGQ DDMACAKARE ILGPDKIIGV SAHTIEEARI AKEQGADYLG VGAIFPTSSK DDAEVLGIKR LKEMTETVDL PMVAIGGISY DNCLLLKDTG IDGIAVISAL FGQKHIKQAT IDLKKRVDAL YETMHTCLTI AGSDSSGGAG IQADLKTMLA NKVFGMSAIT ALTAQNTTGV TDIMDVTPEF LESQIRAVFD DIYPEAVKIG MVSSKALIHT IVEMLKHYDA KHIVVDPVMV ATSGAKLISD EAISTLKEEL LPIAEVITPN IPETEVLTDM EVKTVEDMEI AAKKIYDTYH CAVLVKGGHQ LNDANDYLYN GEKGTWFKGH RIDNSNTHGT GCTLSSAIAS NLAKGYTLEE SVRHAKTYLS GAIGAMLDLG QGSGPMDHGY NI // ID E2P1R1_PASHA Unreviewed; 509 AA. AC E2P1R1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=COI_1790; OS Mannheimia haemolytica serotype A2 str. OVINE. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Mannheimia. OX NCBI_TaxID=669261; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OVINE; RX PubMed=19966002; DOI=10.1128/JB.01527-09; RA Lawrence P.K., Kittichotirat W., Bumgarner R.E., McDermott J.E., RA Herndon D.R., Knowles D.P., Srikumaran S.; RT "Genome sequences of Mannheimia haemolytica serotype A2: ovine and RT bovine isolates."; RL J. Bacteriol. 192:1167-1168(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZX01000091; EEY09590.1; -; Genomic_DNA. DR ProteinModelPortal; E2P1R1; -. DR EnsemblBacteria; EEY09590; EEY09590; COI_1790. DR PATRIC; 36004874; VBIManHae140233_1709. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 509 AA; 55290 MW; F174A5A559E3DBD4 CRC64; MSNYSNSPYQ PNVIWTVAGS DSCAGAGLQT DLHTFHDFNL VGCSVVTSVT AQHPHGVLCV TPVDDHTFRQ QFEALLVQGY PNAIKIGLLC SQAQVEILCE YIQKIRAESS HYCYVVYDPV AVASSGQALS DSILLPIVQQ KLYPLVDLIT PNGTELALLS DTEIQTFGDV KTASHKLFAQ GIKAVLAKGG HFEWLGETVR DYLLTANEIY AFSHARQQSV NTHGTGCTYA SAVGAMLATG FDLADAVTVA TAYLQKGLSE KQGRGQTALS SLCHTGYPDD IAFFPQTELI SAPLKLPKEP FAPTEYQLGL YPVVDSVKWL ERLILVGVKT LQIRIKNRPL AEIEQEIAHS VALAKQHNVR LFVNDYWQLA MKYQAYGVHL GQEDLATADL NAIQQSGLRL GVSTHCYFEI MRALAVKPSY IAFGHVFPTQ TKVMPSQPQG LTNLAKYVAL VAPLNIPTVA IGGINEQSIE NVMHTGVGSA AVVSAVTQAK DWQQAVKNLA KFANGGRNE // ID E2PBF3_PASHA Unreviewed; 509 AA. AC E2PBF3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=COK_2510; OS Mannheimia haemolytica serotype A2 str. BOVINE. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Mannheimia. OX NCBI_TaxID=669262; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BOVINE; RX PubMed=19966002; DOI=10.1128/JB.01527-09; RA Lawrence P.K., Kittichotirat W., Bumgarner R.E., McDermott J.E., RA Herndon D.R., Knowles D.P., Srikumaran S.; RT "Genome sequences of Mannheimia haemolytica serotype A2: ovine and RT bovine isolates."; RL J. Bacteriol. 192:1167-1168(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZY01000083; EEY11478.1; -; Genomic_DNA. DR ProteinModelPortal; E2PBF3; -. DR EnsemblBacteria; EEY11478; EEY11478; COK_2510. DR PATRIC; 36011755; VBIManHae138272_2400. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 509 AA; 55290 MW; F174A5A559E3DBD4 CRC64; MSNYSNSPYQ PNVIWTVAGS DSCAGAGLQT DLHTFHDFNL VGCSVVTSVT AQHPHGVLCV TPVDDHTFRQ QFEALLVQGY PNAIKIGLLC SQAQVEILCE YIQKIRAESS HYCYVVYDPV AVASSGQALS DSILLPIVQQ KLYPLVDLIT PNGTELALLS DTEIQTFGDV KTASHKLFAQ GIKAVLAKGG HFEWLGETVR DYLLTANEIY AFSHARQQSV NTHGTGCTYA SAVGAMLATG FDLADAVTVA TAYLQKGLSE KQGRGQTALS SLCHTGYPDD IAFFPQTELI SAPLKLPKEP FAPTEYQLGL YPVVDSVKWL ERLILVGVKT LQIRIKNRPL AEIEQEIAHS VALAKQHNVR LFVNDYWQLA MKYQAYGVHL GQEDLATADL NAIQQSGLRL GVSTHCYFEI MRALAVKPSY IAFGHVFPTQ TKVMPSQPQG LTNLAKYVAL VAPLNIPTVA IGGINEQSIE NVMHTGVGSA AVVSAVTQAK DWQQAVKNLA KFANGGRNE // ID E2PC83_NEIPO Unreviewed; 205 AA. AC E2PC83; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NEIPOLOT_00199; OS Neisseria polysaccharea ATCC 43768. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=546267; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43768; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADBE01000012; EFH23996.1; -; Genomic_DNA. DR ProteinModelPortal; E2PC83; -. DR EnsemblBacteria; EFH23996; EFH23996; NEIPOLOT_00199. DR PATRIC; 37855767; VBINeiPol102132_0162. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21895 MW; F0620FA7FF88E15F CRC64; MTFPPVKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKTL HGDELKREIA RCVAACRGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAE EVLATGVSSL AVVRAVTEAT NPEAVVKAFQ ALWNE // ID E2PMB4_9RHIZ Unreviewed; 221 AA. AC E2PMB4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.4.1.1; GN ORFNames=BIBO2_1211; OS Brucella sp. BO2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=693750; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BO2; RA Setubal J.C., Boyle S., Crasta O.R., Kenyon R.W., Mane S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Frace M.A., Sammons S.A., Hoffmaster A.R., Tiller R.V., RA Olsen-Rasmussen M., De B.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFA01000075; EFM59884.1; -; Genomic_DNA. DR ProteinModelPortal; E2PMB4; -. DR EnsemblBacteria; EFM59884; EFM59884; BIBO2_1211. DR PATRIC; 41373609; VBIBruSp146994_1332. DR GO; GO:0004645; F:phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Glycosyltransferase; Transferase. SQ SEQUENCE 221 AA; 23290 MW; 7E9D87E9975AD09D CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHTPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID E2PQ28_9RHIZ Unreviewed; 203 AA. AC E2PQ28; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-OCT-2013, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BIBO2_2285; OS Brucella sp. BO2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=693750; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BO2; RA Setubal J.C., Boyle S., Crasta O.R., Kenyon R.W., Mane S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Frace M.A., Sammons S.A., Hoffmaster A.R., Tiller R.V., RA Olsen-Rasmussen M., De B.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFA01000126; EFM58843.1; -; Genomic_DNA. DR EnsemblBacteria; EFM58843; EFM58843; BIBO2_2285. DR PATRIC; 41375975; VBIBruSp146994_2470. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Glycosyltransferase; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22328 MW; 46AEFC75EFC2939B CRC64; MTALDPFYPI FDSADWLERM VPLGIKLVQL RVKDKADVQL RAEIRAARDI CAAHDCQLIV NDYWKLALEE GCNFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGD IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID E2PZT9_STRC2 Unreviewed; 222 AA. AC E2PZT9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SCLAV_1319; OS Streptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 / OS NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=443255; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / RC NRRL 3585 / VKM Ac-602; RX PubMed=20624727; RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U., RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., RA Bovenberg R.A.L., Breitling R., Takano E.; RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich RT evolutionary reservoir of secondary metabolic pathways."; RL Genome Biol. Evol. 2:212-224(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000913; EFG06398.1; -; Genomic_DNA. DR ProteinModelPortal; E2PZT9; -. DR EnsemblBacteria; EFG06398; EFG06398; SCLAV_1319. DR PATRIC; 36461691; VBIStrCla15562203751_4723. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23219 MW; ED01DBF76DD546E0 CRC64; MSTARAALLD ARLYLCTDAR RQQGDLPEFL DAVLGAGVDV VQLRDKGLEA AEELEHLRVF ADACRRHGTL LSVNDRADIA HAIGADVLHL GQGDLPVPAA RAVIGEAPLI GRSTHSTAEA AAAAVQPGVD YFCTGPCWPT PTKPGRHAPG LELVRATAAL GTDRPWFAIG GIDHQNLDEV LDAGARRIVV VRAITEADDP AAATAELAAR IRALPLPDGS AA // ID E2QJ19_ECOLX Unreviewed; 211 AA. AC E2QJ19; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LF82_2248; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LF82 / AIEC; RA Peyretaillade E., Claret L., Bonnet R., Dossat C., Barbe V., RA Vacherie B., Segurens B., Peyret P., Darfeuille-Michaud A.; RT "Complete genome sequence of adherent invasive Escherichia coli strain RT LF82 isolated from a patient with Crohn's disease."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU651637; CAP78449.1; -; Genomic_DNA. DR RefSeq; YP_002558838.1; NC_011993.1. DR ProteinModelPortal; E2QJ19; -. DR SMR; E2QJ19; 9-208. DR EnsemblBacteria; CAP78449; CAP78449; LF82_2248. DR GeneID; 7395015; -. DR KEGG; elf:LF82_2248; -. DR PATRIC; 48658201; VBIEscCol74806_4079. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E2S0X6_9CORY Unreviewed; 209 AA. AC E2S0X6; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0305_10178; OS Corynebacterium pseudogenitalium ATCC 33035. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=525264; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33035; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYQ02000003; EFQ81292.1; -; Genomic_DNA. DR ProteinModelPortal; E2S0X6; -. DR EnsemblBacteria; EFQ81292; EFQ81292; HMPREF0305_10178. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR000652; Triosephosphate_isomerase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS51440; TIM_2; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21681 MW; CF94B3F3BEC71AC5 CRC64; MAIDWTLYLV TDPDLAGGRD NVVSIVQEAV RGGVTVVQLR DKEASDEQIE RTARELLGVL GDVPLFINDR VEVAAKLGCH LHIGQDDMAF REAREKLGEG QLIGLSIGSS DELAAIADDA RPDVIGIGPV HSTGTKKNAP AGMGPAAAAA LAHAARERGI ESVAIGGIKT HNAHELAGSE FAGICVVSDI MAAEDPAAAA AHLKEAFHG // ID E2SWU9_9RALS Unreviewed; 384 AA. AC E2SWU9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF1004_01650; OS Ralstonia sp. 5_7_47FAA. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=658664; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_7_47FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Jen D., Larson L., Mehta T., RA Neiman D., Park D., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Allen-Vercoe E., Strauss J., Daigneault M., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Ralstonia sp. strain 5_7_47FAA."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACUF01000027; EFP66647.1; -; Genomic_DNA. DR EnsemblBacteria; EFP66647; EFP66647; HMPREF1004_01650. DR PATRIC; 42059408; VBIRalSp146006_1896. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 384 AA; 40180 MW; FC0D653E7A9DBA82 CRC64; MSLSALRFSA AWPEAAALAA QIVDRHAEAF GRASHAWSVT DRADEATSAA TVLLTTDAGQ AERARSAGAA VVLTAVEGDL LIDTVHDRLG TYRFTSAAQG DAFDARFVAV FGAALALAFE PRDALCVARA WIAEANADAL AWPTQFDALP RVLEPALPCP TAADLAFALG PTQLGVYAVV PDADWVARLV ALKVPTVQLR FKSDDAQAVV DQVRRAEAAA RGSATRLFIN DHWQVALDVY TQAPNSGIYG IHLGQEDIDE ADLVAIRSAG LRLGISTHGF AEMLRVAPLN PSYLALGAVF ATPTKTMPTV PQGLGRLFAY AAAMRTREPA PALVAIGGID LAAMPRVLES GVGSVAVVRA ITQAADVPAA VDALQATFAA HVRA // ID E2T8C1_MYCTX Unreviewed; 222 AA. AC E2T8C1; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TMBG_03646; OS Mycobacterium tuberculosis SUMu002. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=675513; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SUMu002; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Galagan J., Pepperell C., Hoeppner V., Gagneux S., Small P., RA Schoolnik G., Feldman M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain SUMu002."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHR01000033; EFP16554.1; -; Genomic_DNA. DR ProteinModelPortal; E2T8C1; -. DR SMR; E2T8C1; 1-221. DR EnsemblBacteria; EFP16554; EFP16554; TMBG_03646. DR PATRIC; 41404510; VBIMycTub139685_0958. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID E2TI63_MYCTX Unreviewed; 222 AA. AC E2TI63; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TMCG_03234; OS Mycobacterium tuberculosis SUMu003. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=675514; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SUMu003; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Galagan J., Pepperell C., Hoeppner V., Gagneux S., Small P., RA Schoolnik G., Feldman M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain SUMu003."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHS01000017; EFP20916.1; -; Genomic_DNA. DR ProteinModelPortal; E2TI63; -. DR SMR; E2TI63; 1-221. DR EnsemblBacteria; EFP20916; EFP20916; TMCG_03234. DR PATRIC; 41413122; VBIMycTub145585_0475. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID E2TUT1_MYCTX Unreviewed; 222 AA. AC E2TUT1; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TMDG_02889; OS Mycobacterium tuberculosis SUMu004. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=675515; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SUMu004; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Galagan J., Pepperell C., Hoeppner V., Gagneux S., Small P., RA Schoolnik G., Feldman M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain SUMu004."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHT01000025; EFP24731.1; -; Genomic_DNA. DR ProteinModelPortal; E2TUT1; -. DR SMR; E2TUT1; 1-221. DR EnsemblBacteria; EFP24731; EFP24731; TMDG_02889. DR PATRIC; 41422862; VBIMycTub141803_0632. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID E2U6Q9_MYCTX Unreviewed; 222 AA. AC E2U6Q9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TMEG_02990; OS Mycobacterium tuberculosis SUMu005. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=675516; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SUMu005; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Galagan J., Pepperell C., Hoeppner V., Gagneux S., Small P., RA Schoolnik G., Feldman M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain SUMu005."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHU01000029; EFP28308.1; -; Genomic_DNA. DR ProteinModelPortal; E2U6Q9; -. DR SMR; E2U6Q9; 1-221. DR EnsemblBacteria; EFP28308; EFP28308; TMEG_02990. DR PATRIC; 41432934; VBIMycTub145504_0953. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID E2UHR5_MYCTX Unreviewed; 222 AA. AC E2UHR5; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TMFG_01707; OS Mycobacterium tuberculosis SUMu006. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=675517; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SUMu006; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Galagan J., Pepperell C., Hoeppner V., Gagneux S., Small P., RA Schoolnik G., Feldman M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain SUMu006."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHV01000023; EFP32173.1; -; Genomic_DNA. DR ProteinModelPortal; E2UHR5; -. DR SMR; E2UHR5; 1-221. DR EnsemblBacteria; EFP32173; EFP32173; TMFG_01707. DR PATRIC; 41442338; VBIMycTub141178_0928. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID E2V534_MYCTX Unreviewed; 222 AA. AC E2V534; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TMHG_03427; OS Mycobacterium tuberculosis SUMu008. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=675519; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SUMu008; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Galagan J., Pepperell C., Hoeppner V., Gagneux S., Small P., RA Schoolnik G., Feldman M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain SUMu008."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHX01000035; EFP40013.1; -; Genomic_DNA. DR ProteinModelPortal; E2V534; -. DR SMR; E2V534; 1-221. DR EnsemblBacteria; EFP40013; EFP40013; TMHG_03427. DR PATRIC; 41461400; VBIMycTub142773_0953. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID E2VEE5_MYCTX Unreviewed; 222 AA. AC E2VEE5; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TMIG_01305; OS Mycobacterium tuberculosis SUMu009. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=675520; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SUMu009; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Galagan J., Pepperell C., Hoeppner V., Gagneux S., Small P., RA Schoolnik G., Feldman M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain SUMu009."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHY01000010; EFP44666.1; -; Genomic_DNA. DR ProteinModelPortal; E2VEE5; -. DR SMR; E2VEE5; 1-221. DR EnsemblBacteria; EFP44666; EFP44666; TMIG_01305. DR PATRIC; 41469235; VBIMycTub139772_0159. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID E2VQT5_MYCTX Unreviewed; 222 AA. AC E2VQT5; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TMJG_02150; OS Mycobacterium tuberculosis SUMu010. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=675521; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SUMu010; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Galagan J., Pepperell C., Hoeppner V., Gagneux S., Small P., RA Schoolnik G., Feldman M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain SUMu010."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHZ01000009; EFP48587.1; -; Genomic_DNA. DR ProteinModelPortal; E2VQT5; -. DR SMR; E2VQT5; 1-221. DR EnsemblBacteria; EFP48587; EFP48587; TMJG_02150. DR PATRIC; 41478636; VBIMycTub141587_0151. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID E2W1Z8_MYCTX Unreviewed; 222 AA. AC E2W1Z8; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TMKG_02742; OS Mycobacterium tuberculosis SUMu011. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=675522; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SUMu011; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Galagan J., Pepperell C., Hoeppner V., Gagneux S., Small P., RA Schoolnik G., Feldman M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain SUMu011."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADIA01000010; EFP52528.1; -; Genomic_DNA. DR ProteinModelPortal; E2W1Z8; -. DR SMR; E2W1Z8; 1-221. DR EnsemblBacteria; EFP52528; EFP52528; TMKG_02742. DR PATRIC; 41488229; VBIMycTub145761_0160. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID E2WDX1_MYCTX Unreviewed; 222 AA. AC E2WDX1; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TMLG_01838; OS Mycobacterium tuberculosis SUMu012. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=675523; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SUMu012; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Galagan J., Pepperell C., Hoeppner V., Gagneux S., Small P., RA Schoolnik G., Feldman M., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain SUMu012."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADIB01000027; EFP56180.1; -; Genomic_DNA. DR ProteinModelPortal; E2WDX1; -. DR SMR; E2WDX1; 1-221. DR EnsemblBacteria; EFP56180; EFP56180; TMLG_01838. DR PATRIC; 41498621; VBIMycTub142090_0466. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID E2X2C9_ECOLX Unreviewed; 211 AA. AC E2X2C9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EC182770_4802; OS Escherichia coli 1827-70. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670888; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1827-70; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUK01000028; EFP98653.1; -; Genomic_DNA. DR ProteinModelPortal; E2X2C9; -. DR SMR; E2X2C9; 20-202. DR EnsemblBacteria; EFP98653; EFP98653; EC182770_4802. DR PATRIC; 44761155; VBIEscCol139245_4761. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E2X3I5_SHIDY Unreviewed; 164 AA. AC E2X3I5; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SD1617_0404; OS Shigella dysenteriae 1617. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=754093; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1617; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUT01000007; EFP73782.1; -; Genomic_DNA. DR EnsemblBacteria; EFP73782; EFP73782; SD1617_0404. DR PATRIC; 42072374; VBIShiDys151583_0433. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 164 AA; 17436 MW; BCC724EAEFB9F4FE CRC64; MEADVVAAIA LGRRYNARLF INDYWRLAIK HQAYGVHLGQ EDLQATDLSA IRAAGLRLGV STHDDMEIDV ALAARPSYIA LGHVFPTQTK QMPSAAQGLE QLARHVERLA DYPTVAIGGI SLPRAPAVIA TGVGSIAVVS AITQAADWRL ATAQLLEIAG VGDE // ID E2XXC8_PSEFL Unreviewed; 317 AA. AC E2XXC8; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 22-JAN-2014, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=mutT; ORFNames=PFWH6_4697; OS Pseudomonas fluorescens WH6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=746360; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH6; RX PubMed=20920191; DOI=10.1186/1471-2164-11-522; RA Kimbrel J.A., Givan S.A., Halgren A.B., Creason A.L., Mills D.I., RA Banowetz G.M., Armstrong D.J., Chang J.H.; RT "An improved, high-quality draft genome sequence of the Germination- RT Arrest Factor-producing Pseudomonas fluorescens WH6."; RL BMC Genomics 11:522-522(2010). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAZ01000036; EFQ61585.1; -; Genomic_DNA. DR EnsemblBacteria; EFQ61585; EFQ61585; PFWH6_4697. DR PATRIC; 44839941; VBIPseFlu158595_5232. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Transferase. SQ SEQUENCE 317 AA; 34363 MW; 6A06384815B28419 CRC64; MSAVKRVHVA AAVIRGVDGR ILLARRADTQ HQGGLWEFPG GKVEADESVA VALSRELQEE LGIQVTTARP LIKVHHDYPD KQVLLDVWEV SAFTGEPHGA EGQPLEWVAP RDLINFAFPA ANAPIVAAAR LPAEYLITPG ELETPTLLRG IQKAIAGGIK LVQLRAPNGY DPKYRDLAVD AVGLCAGKAQ LMLKGPFEWL GDFPAAGWHM TSAQLRKYAS KGRPLPKDRW LAASCHNAEE LALAQLMDVD FVTLSPVQPT RTHPDAQPLG WEQAAQLIRG FSRPVFLLGG VGPGEREQAW EAGAQGVAGI RAFWPQV // ID E2XYL4_PSEFL Unreviewed; 209 AA. AC E2XYL4; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PFWH6_5136; OS Pseudomonas fluorescens WH6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=746360; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH6; RX PubMed=20920191; DOI=10.1186/1471-2164-11-522; RA Kimbrel J.A., Givan S.A., Halgren A.B., Creason A.L., Mills D.I., RA Banowetz G.M., Armstrong D.J., Chang J.H.; RT "An improved, high-quality draft genome sequence of the Germination- RT Arrest Factor-producing Pseudomonas fluorescens WH6."; RL BMC Genomics 11:522-522(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAZ01000040; EFQ61078.1; -; Genomic_DNA. DR EnsemblBacteria; EFQ61078; EFQ61078; PFWH6_5136. DR PATRIC; 44840827; VBIPseFlu158595_5662. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22460 MW; A6CB91243B65C386 CRC64; MKLRGLYAIT DSQLLAGKFL AYVEAALDGG VTLLQYRDKS SDEARRLREA EKLRELCSRY KTRLIINDDA ELAARLGVGV HLGQTDGPLT PARALLGSKA IIGATCHSQI ELAEQAAKEG ASYVAFGRFF NSTTKPGAPA ATVDMLAQAR QRLHLPICVI GGVTLENAEP LVAHGADLLA VVHGLFGADS TQEVTRRARA FNDLLKYSV // ID E2Y3U5_ENTFL Unreviewed; 211 AA. AC E2Y3U5; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9504_01056; OS Enterococcus faecalis TX0102. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749501; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0102; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBD01000023; EFQ13421.1; -; Genomic_DNA. DR ProteinModelPortal; E2Y3U5; -. DR EnsemblBacteria; EFQ13421; EFQ13421; HMPREF9504_01056. DR PATRIC; 44850746; VBIEntFae147483_1019. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22866 MW; A6E43F880C487223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E2YF88_ENTFL Unreviewed; 211 AA. AC E2YF88; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9493_02239; OS Enterococcus faecalis DAPTO 516. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749490; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DAPTO 516; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBS01000039; EFQ67102.1; -; Genomic_DNA. DR ProteinModelPortal; E2YF88; -. DR EnsemblBacteria; EFQ67102; EFQ67102; HMPREF9493_02239. DR PATRIC; 44864893; VBIEntFae153879_2141. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22881 MW; E4C24F8F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E2YPX3_ENTFL Unreviewed; 211 AA. AC E2YPX3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9492_02537; OS Enterococcus faecalis DAPTO 512. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749489; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DAPTO512; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBT01000056; EFQ09086.1; -; Genomic_DNA. DR ProteinModelPortal; E2YPX3; -. DR EnsemblBacteria; EFQ09086; EFQ09086; HMPREF9492_02537. DR PATRIC; 44871661; VBIEntFae151659_2412. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22881 MW; E4C24F8F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E2YSR0_ENTFL Unreviewed; 211 AA. AC E2YSR0; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9512_00376, UMA_02549; OS Enterococcus faecalis EnGen0311. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749509; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0635; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH245; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., RA McCowan C., Murphy C., Neiman D., Pearson M., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Enterococcus faecalis WH245."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBZ01000004; EFQ17551.1; -; Genomic_DNA. DR EMBL; AJEF01000017; EOI90961.1; -; Genomic_DNA. DR EnsemblBacteria; EFQ17551; EFQ17551; HMPREF9512_00376. DR EnsemblBacteria; EOI90961; EOI90961; UMA_02549. DR PATRIC; 44879200; VBIEntFae151097_0363. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID E2Z3M2_ENTFL Unreviewed; 211 AA. AC E2Z3M2; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9510_00941; OS Enterococcus faecalis TX0470. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749507; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0470; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECC01000023; EFQ71326.1; -; Genomic_DNA. DR ProteinModelPortal; E2Z3M2; -. DR EnsemblBacteria; EFQ71326; EFQ71326; HMPREF9510_00941. DR PATRIC; 44886720; VBIEntFae155759_0886. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22936 MW; A6E424940A930223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTRVAGV SLVSEIMLAE QIAEKVQGLM RVTERMLEAR K // ID E2ZBG7_9FIRM Unreviewed; 196 AA. AC E2ZBG7; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF9429_00794; OS Megasphaera micronuciformis F0359. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=706434; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0359; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECS01000036; EFQ04195.1; -; Genomic_DNA. DR EnsemblBacteria; EFQ04195; EFQ04195; HMPREF9429_00794. DR PATRIC; 44911087; VBIMegMic155926_0703. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 21628 MW; ED5EF7ED800252FD CRC64; MRKVIAITNR HLVHRDYWDQ LEQIVASPVE SLVLREKDLS EDEYIDYAKK ALSLCNIHGK QCILHNFGRV AVRLHIPRFQ CSLDYLKTHT SISYYMSTLG VSVHTAEEAH EAEKLGATYV IAGHVFRTPS KEAYSPIGVS TVKDICNAVS VPVYALGGVN PTTVGELKAT PVKGIALMSG LMESNDIPSY VASLQV // ID E2ZC73_9FIRM Unreviewed; 213 AA. AC E2ZC73; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9429_01244; OS Megasphaera micronuciformis F0359. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=706434; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0359; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECS01000037; EFQ04060.1; -; Genomic_DNA. DR EnsemblBacteria; EFQ04060; EFQ04060; HMPREF9429_01244. DR PATRIC; 44911962; VBIMegMic155926_1132. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23297 MW; 0FA199D4ABFE0650 CRC64; MTKEEHIQRL KDDPIYVVMG EALSLGRKNT EVAKTLLDVG VRIIQYREKH KTWREKYAEA AEIAVMCKKY GATFIMNDSV DLAVACGADG IHVGQDDAPV QIVKKIAGQN VFVGVSTNTT KELQGALADG ADYVGFGPMF PTSSKSDADE VVTEETIRSA LEFPLPVVTI GGIGLENIRT LYDRGFRSFA MISAVVSQKD IKKAVDDLRQ ALK // ID E2ZJK4_9FIRM Unreviewed; 211 AA. AC E2ZJK4; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9436_01853; OS Faecalibacterium cf. prausnitzii KLE1255. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=748224; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KLE1255; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECU01000156; EFQ06645.1; -; Genomic_DNA. DR ProteinModelPortal; E2ZJK4; -. DR EnsemblBacteria; EFQ06645; EFQ06645; HMPREF9436_01853. DR PATRIC; 44920339; VBIFaeCf154181_1524. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22633 MW; 04BDD81B5BF4B3AA CRC64; MKCDKQNMLL YAVTDHAWVG KQTLYEQVES ALKGGVTCVQ LREKELDDEA FLKEAVEIHA LCQRYGVPFF VNDNVDIAIR CHAEGVHVGQ EDMAAAQVRA RVGEGMMIGV SVHSVEEALE AVKHGADCLG VGAAFATHTK TDVDVLPHET LKAICDAVDI PVVAIGGIHK ENILQLKGTG VDGVALVSAI FAADDIETEC KGLKALSEQI I // ID E2ZSU9_PSEAI Unreviewed; 315 AA. AC E2ZSU9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-MAR-2014, entry version 20. DE SubName: Full=Putative pyrophosphohydrolase; GN ORFNames=PA39016_000840031; OS Pseudomonas aeruginosa 39016. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=798130; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=39016; RA Stewart R.M.K., Wiehlmann L., Ashelford K.E., Preston S.J., RA Campbell B.J., Neal T.J., Hall N., Tuft S., Kaye S.B., Winstanley C.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=39016; RX PubMed=21227987; DOI=10.1128/JCM.02036-10; RA Stewart R.M., Wiehlmann L., Ashelford K.E., Preston S.J., RA Frimmersdorf E., Campbell B.J., Neal T.J., Hall N., Tuft S., RA Kaye S.B., Winstanley C.; RT "Genetic characterization indicates that a specific subpopulation of RT Pseudomonas aeruginosa is associated with keratitis infections."; RL J. Clin. Microbiol. 49:993-1003(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEX01000069; EFQ38228.1; -; Genomic_DNA. DR ProteinModelPortal; E2ZSU9; -. DR EnsemblBacteria; EFQ38228; EFQ38228; PA39016_000840031. DR PATRIC; 44932891; VBIPseAer163554_3117. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34041 MW; FBCE869C3EE6B47B CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EDGEPVRAAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEAHGAEGQ PLAWVEPREL ADYEFPAANA PIVQAARLPA HYLITPDGLE PGELISGVRK AVEAGIRLIQ LRAPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDADELAL AASMGVEFVT LSPVQPTESH PGEPALGWDK AAELIAGFNQ PVYLLGGLGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID E2ZZ93_PSEAI Unreviewed; 209 AA. AC E2ZZ93; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-MAR-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PA39016_001790016; OS Pseudomonas aeruginosa 39016. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=798130; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=39016; RA Stewart R.M.K., Wiehlmann L., Ashelford K.E., Preston S.J., RA Campbell B.J., Neal T.J., Hall N., Tuft S., Kaye S.B., Winstanley C.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=39016; RX PubMed=21227987; DOI=10.1128/JCM.02036-10; RA Stewart R.M., Wiehlmann L., Ashelford K.E., Preston S.J., RA Frimmersdorf E., Campbell B.J., Neal T.J., Hall N., Tuft S., RA Kaye S.B., Winstanley C.; RT "Genetic characterization indicates that a specific subpopulation of RT Pseudomonas aeruginosa is associated with keratitis infections."; RL J. Clin. Microbiol. 49:993-1003(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEX01000163; EFQ40472.1; -; Genomic_DNA. DR ProteinModelPortal; E2ZZ93; -. DR SMR; E2ZZ93; 24-200. DR EnsemblBacteria; EFQ40472; EFQ40472; PA39016_001790016. DR PATRIC; 44932050; VBIPseAer163554_2646. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22146 MW; 898DA261D0AFA265 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER HGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAQ LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID E3B9P1_9MICO Unreviewed; 231 AA. AC E3B9P1; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0321_1077; OS Dermacoccus sp. Ellin185. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Dermacoccaceae; Dermacoccus. OX NCBI_TaxID=188626; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ellin185; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEIQ01000064; EFP58268.1; -; Genomic_DNA. DR EnsemblBacteria; EFP58268; EFP58268; HMPREF0321_1077. DR PATRIC; 42130715; VBIDerSp75128_1314. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 145 147 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 231 AA; 23472 MW; 34ACFD3975B86E5A CRC64; MSDGRGVELY LVTDTALCGG PDGVVETAEA AARGGVDMIQ IRDHDASTRE LCSLTTRVID AVATARRVRV VVDDRLDVAL AVGADGVHLG QSDLDPVVAR RLADRVVGEG FHLGWSVSNL EQVAAATRLP RGTVDLLGIG PFRATPTKPD AAQPLGLDGV GAITDAARAG GFANVVIGGV KLPDLRALVA AGAQGVAVVS AICGQPDPLA ATQALRRELD AAGGSSTGSL R // ID E3BIB3_9VIBR Unreviewed; 436 AA. AC E3BIB3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VIBC2010_03085; OS Vibrio caribbenthicus ATCC BAA-2122. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=796620; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-2122; RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0; RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., RA Naum M., McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.; RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge RT Scleritoderma cyanea."; RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEIU01000061; EFP97241.1; -; Genomic_DNA. DR EnsemblBacteria; EFP97241; EFP97241; VIBC2010_03085. DR PATRIC; 44964457; VBIVibCar171609_1441. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 436 AA; 49374 MW; 5B02435763C67242 CRC64; MIVISLPQTA MSLKPQIMSC LECAFSYGLQ SDNIHIEVNR SEWITIKTLE REIKIVSDLF TSIQSNTKCD FKLNYHNDSN GPEEISHINI YIGVKSSSPE GIHYQDVWCQ SMDDGGEGVT YSYMPINDKA NQQHCAWFIS LISLGFCFKD SLVVTRAALC DVSRETLAHE KNNMPDWPTN YLDFPKLIGN RRRLSEDSFE QYNHHCFPQI PKTSFSLYPV VDDILWIRKL LPLGIKIIQL RIKDGNKRDL EQQIIEAIEL GREYNAMVFI NDHWQLAIEH GAFGVHLGQE DIEQVDLDRL IASGIHLGIS SHGYYEVLRA QSYQPSYVAL GHIFATTTKE MPSQPQGLSK LKLYQNLIDS MELASTHEMS IPTVAIGGID LGNVSDVMKC GVTCVAVVRA LTLSESLEDD LEKFQSFSPI ERQEQSSKIG DYDVIR // ID E3C6I3_9LACO Unreviewed; 217 AA. AC E3C6I3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9265_1794; OS Lactobacillus oris PB013-T2-3. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=908339; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PB013-T2-3; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEKL01000025; EFQ53665.1; -; Genomic_DNA. DR EnsemblBacteria; EFQ53665; EFQ53665; HMPREF9265_1794. DR PATRIC; 44992937; VBILacOri169381_0506. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23332 MW; 421F7945500D57B9 CRC64; MKFEPTMLRA YLVGGSQDTH HAPAELLTKT EEALQAGITA FQYREKGSSN LSADQRLKLA QQLRELTRHY RVPFFIDDDE ELALAVGADG VHVGQKDQRI EQVIQRAQGK LMIGYSCNRP AQIEKANQLA AVDYIGSGPV FPTQSKADAD PALGLSRLAL LNRLSEQPVV AIGGITADNI AATLATGVAG AAVISMVFQS DDISQTVHQM LTASSQS // ID E3CXM3_9BACT Unreviewed; 210 AA. AC E3CXM3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Apau_2056; OS Aminomonas paucivorans DSM 12260. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Aminomonas. OX NCBI_TaxID=584708; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 12260; RX PubMed=21304733; RA Pitluck S., Yasawong M., Held B., Lapidus A., Nolan M., Copeland A., RA Lucas S., Del Rio T.G., Tice H., Cheng J.F., Chertkov O., Goodwin L., RA Tapia R., Han C., Liolios K., Ivanova N., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Pukall R., Spring S., Rohde M., RA Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Non-contiguous finished genome sequence of Aminomonas paucivorans RT type strain (GLU-3)."; RL Stand. Genomic Sci. 3:285-293(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001022; EFQ24467.1; -; Genomic_DNA. DR EnsemblBacteria; EFQ24467; EFQ24467; Apau_2056. DR PATRIC; 44974302; VBIAmiPau86579_2108. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 21529 MW; 9A46FFE926DFE41E CRC64; MTGDLRSHLK LYVIPDLRAG APRSLMEQAR AALAGGAGTV QLRHKTASGR ELCRLGEALA ALCDDAGALF FVNDRLDVAL ACGASGVHLG LEDLPVAVAR RLAPPDFLVG ATARTPEQAL RAWKDGADYL GVGAVAPTPT KEDTTVIGPE GFAAVAASVP LPCVAVGGIT AAAVPDLRRR GAAGVVVVRE AVGAPDPAEA CRRLRELLDA // ID E3D3Y0_NEIM7 Unreviewed; 205 AA. AC E3D3Y0; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NMBB_2378; OS Neisseria meningitidis serogroup B (strain alpha710). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=630588; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=alpha710; RX PubMed=20709895; DOI=10.1128/JB.00883-10; RA Joseph B., Schneiker-Bekel S., Schramm-Gluck A., Blom J., Claus H., RA Linke B., Schwarz R.F., Becker A., Goesmann A., Frosch M., Schoen C.; RT "Comparative genome biology of a serogroup B carriage and disease RT strain supports a polygenic nature of meningococcal virulence."; RL J. Bacteriol. 192:5363-5377(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001561; ADO32489.1; -; Genomic_DNA. DR RefSeq; YP_005883621.1; NC_017505.1. DR EnsemblBacteria; ADO32489; ADO32489; NMBB_2378. DR GeneID; 12400003; -. DR KEGG; nmp:NMBB_2378; -. DR PATRIC; 43138248; VBINeiMen23504_2772. DR KO; K00788; -. DR BioCyc; NMEN630588:GLHP-2055-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21866 MW; 27098830E9788923 CRC64; MTFPPLKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKTL HGDELKREIA CCVAACQGSR TQLFINDHWR VAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQARGTPVVA IGGIDLNNAQ AVLATGVSSL AVVRAVTEAE NPEAVVKAFQ ALWNE // ID E3D857_GARV3 Unreviewed; 491 AA. AC E3D857; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=HMPREF0421_20208; OS Gardnerella vaginalis (strain ATCC 14019 / 317). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=525284; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14019 / 317; RX PubMed=20865041; DOI=10.1371/journal.pone.0012411; RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., RA Sutton G., Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., RA Gibbs R.A., Leigh S.R., Stumpf R., White B.A., Highlander S.K., RA Nelson K.E., Wilson B.A.; RT "Comparative genomics of Gardnerella vaginalis strains reveals RT substantial differences in metabolic and virulence potential."; RL PLoS ONE 5:E12411-E12411(2010). CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002104; ADP38292.1; -; Genomic_DNA. DR RefSeq; YP_003985315.1; NC_014644.1. DR EnsemblBacteria; ADP38292; ADP38292; HMPREF0421_20208. DR GeneID; 9903750; -. DR KEGG; gvg:HMPREF0421_20208; -. DR PATRIC; 42627257; VBIGarVag39333_0202. DR HOGENOM; HOG000106869; -. DR OrthoDB; EOG628F8M; -. DR BioCyc; GVAG525284:GI3V-217-MONOMER; -. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Thiamine biosynthesis; Transferase. SQ SEQUENCE 491 AA; 51935 MW; E5EE3F7CDD1AC8C8 CRC64; MLVASNSFKM YVNASKLCAQ KNPLTHCVTN NVVQEITANV LLAAGASPAM VVDAEEAEVF AQIASGVLVN IGTYRPVDKE SMDAAIRGAV KAHTPWVLDP VAVGGLAPRT QYAREIVKSH PAVIRANASE ILGLAGEESG GKGVDAGDSV DSAVAAAKKL VKRYGSVVAI SGEKDAIYGH GCSARVSGGH EIMTKVVGTG CSLGALVAAY VGANRNRPFA ATVAAHVHAA AAGTWAAQRS TLPGSFRKLW MDALMDLSAD EMLKLANIEF ELDPVDWSLY FITDPKMSDR AEEDIAVDCV KGGASVVQLR DKYANSETFN NKAQSLRDKM LANGCGDVPI FVDDRIDCAK SLGFNLHVGQ TDTPYIEARK SIPAEWMVGL SIEKLEQLDY VYNECAKENV ALPDVIGIGP IWPTATKPDA APALGVEGVE KIAKRAKELG ISTLGIGGVN ENTVFPIKST SIDGLCVVSA LMLAQNPCEE AHKLRDAITK E // ID E3D992_GARV3 Unreviewed; 513 AA. AC E3D992; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=HMPREF0421_20554; OS Gardnerella vaginalis (strain ATCC 14019 / 317). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=525284; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14019 / 317; RX PubMed=20865041; DOI=10.1371/journal.pone.0012411; RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., RA Sutton G., Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., RA Gibbs R.A., Leigh S.R., Stumpf R., White B.A., Highlander S.K., RA Nelson K.E., Wilson B.A.; RT "Comparative genomics of Gardnerella vaginalis strains reveals RT substantial differences in metabolic and virulence potential."; RL PLoS ONE 5:E12411-E12411(2010). CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002104; ADP38636.1; -; Genomic_DNA. DR RefSeq; YP_003985659.1; NC_014644.1. DR ProteinModelPortal; E3D992; -. DR EnsemblBacteria; ADP38636; ADP38636; HMPREF0421_20554. DR GeneID; 9904109; -. DR KEGG; gvg:HMPREF0421_20554; -. DR PATRIC; 42627981; VBIGarVag39333_0552. DR HOGENOM; HOG000106869; -. DR KO; K00878; -. DR OrthoDB; EOG628F8M; -. DR BioCyc; GVAG525284:GI3V-576-MONOMER; -. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Thiamine biosynthesis; Transferase. SQ SEQUENCE 513 AA; 55083 MW; 37F674D62C230DD4 CRC64; MEELNESNAN IDTNIDTSFS VRARRRMFLN DVRSCIERVR AKKPLTHCIT NNIVQEITAN VLLSAGATPI MVCDPDEAAG IAKIASGVLV NVGTFEEIKG KAIRKAIETC EETQTPWVLD PVGVGVDELT TRTKFVREIV KRNPTVIRAN ASEILALVGQ NSQMKGVDAQ DPVNSALEAA KKLAKEYGSV ISISGEKDAV YGHGCLVRIT GGHKAMTKVV GTGCALGSLV AAYVGANPER PVAATVAAHV HAAAAGTFAA RQTTAPGTFK TLWIDALQTL SVNNMFELTN IEFSIEPTDW TLYLVTDPRM GNRSEEQVAV ESIDGGVTVV QLRDKYSNDT EISEKAIKLR KTLIKAKHGD IPIFIDDHVD TAAKLGFNLH IGQKDTPFVT ARKSMPAEWM IGLSCARVDL MEKAYKECKE NDTPLPDVIG IGAAFATNTK AHDVPPLGVE GVNEVAKVAH SMGVKTLAIG GIHENTVFPI KDLSIDGVCT VSALMCAEDP KKVASDLKSV ITR // ID E3D9G5_GARV3 Unreviewed; 881 AA. AC E3D9G5; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 25. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; OrderedLocusNames=HMPREF0421_20627; OS Gardnerella vaginalis (strain ATCC 14019 / 317). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=525284; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14019 / 317; RX PubMed=20865041; DOI=10.1371/journal.pone.0012411; RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., RA Sutton G., Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., RA Gibbs R.A., Leigh S.R., Stumpf R., White B.A., Highlander S.K., RA Nelson K.E., Wilson B.A.; RT "Comparative genomics of Gardnerella vaginalis strains reveals RT substantial differences in metabolic and virulence potential."; RL PLoS ONE 5:E12411-E12411(2010). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002104; ADP38709.1; -; Genomic_DNA. DR RefSeq; YP_003985732.1; NC_014644.1. DR EnsemblBacteria; ADP38709; ADP38709; HMPREF0421_20627. DR GeneID; 9904186; -. DR KEGG; gvg:HMPREF0421_20627; -. DR PATRIC; 42628130; VBIGarVag39333_0624. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR OrthoDB; EOG6NWBM5; -. DR BioCyc; GVAG525284:GI3V-653-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 881 AA; 98129 MW; 07C954C93BE3FFB2 CRC64; MTSNYPYASM RDQFNLNTCF IANPKLCKSR ALTDIVDDSL RAGSTFIRLN CADESAKEIT SIARDIAQII EDNDKCDSVT FVIDGRVDVV WQARNQGIKV DGVHLAQSDM EPKEARALLG EDAIIGLSVE TESLVKVINE LPDGCIDYIC VTAMRNPEDG CENITPTYEL EPNHTILDVA KINTICSASD FPVLVGGRTS LEDVDMIARS KAAGLFVSEA LYASETPEST MSEFVERFTH IRGNQKHGYA KRVIVQEKAD EKANNTPKFI NAKEAKDAAK LAKQQRVDIA SRGCTQRDKA HIRKTTPVHF EYEYGSYDLE VPYTEIKLSD TPGVGPNPPF KDYNTEGPKC DPKEGLAPLR LDWIRDRGDV VEYEGRSRNL QDDGKRAIKR GKASKEWRGR THKPMKAADH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSEVASGRA VIPCNINHPE AEPMIIGSRF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMAEW CLQHHQESFL YTHFEELCEI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTKI AWQHDVQVMI EGPGHVPFDT VRMNIEMEKA ICQNAPFYTL GPLTTDTAPG YDHITSAIGG VEIARYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADLAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDETLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKRFG GADQQEQLVE EARSQAIAEG MKEMSKKFQE AGSTLYQSAK A // ID E3DCI1_ERWSE Unreviewed; 214 AA. AC E3DCI1; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 16-APR-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EJP617_13550; OS Erwinia sp. (strain Ejp617). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=215689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ejp617; RX PubMed=21075933; DOI=10.1128/JB.01246-10; RA Park D.H., Thapa S.P., Choi B.S., Kim W.S., Hur J.H., Cho J.M., RA Lim J.S., Choi I.Y., Lim C.K.; RT "Complete Genome Sequence of Japanese Erwinia Strain Ejp617, a RT Bacterial Shoot Blight Pathogen of Pear."; RL J. Bacteriol. 193:586-587(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002124; ADP11036.1; -; Genomic_DNA. DR RefSeq; YP_005817923.1; NC_017445.1. DR EnsemblBacteria; ADP11036; ADP11036; EJP617_13550. DR GeneID; 12429341; -. DR KEGG; erj:EJP617_13550; -. DR PATRIC; 42939514; VBIErwSp41759_1458. DR KO; K00788; -. DR BioCyc; ESP215689:GLCY-1384-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23249 MW; C298D41EC9C54BF7 CRC64; MSRGAFPTTA ARLGLYPVVD NVQWIARLLD TGVRTLQLRI KDRAEQQVEQ QVAEAIALGK RYQARLFIND YWRLAVKHQA YGVHLGQQDL DIADLDSIHA AGLRLGLSTH DDAELDRALV ERPSYIALGH VFPTQTKDMP SEPQGLAALT RYVKRLSGIP TVAIGGISLV RAPAVLATGV GSIAVVSAIT QASDWQAATR QLLALAEAQR PARV // ID E3DNX0_HALPG Unreviewed; 219 AA. AC E3DNX0; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Hprae_0440; OS Halanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae; OC Halanaerobium. OX NCBI_TaxID=572479; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33744 / DSM 2228 / GSL; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Chertkov O., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Halanaerobium praevalens DSM 2228."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002175; ADO76594.1; -; Genomic_DNA. DR RefSeq; YP_005835754.1; NC_017455.1. DR ProteinModelPortal; E3DNX0; -. DR EnsemblBacteria; ADO76594; ADO76594; Hprae_0440. DR GeneID; 12442379; -. DR KEGG; hpk:Hprae_0440; -. DR PATRIC; 43054113; VBIHalPra106773_0446. DR KO; K00788; -. DR BioCyc; HPRA572479:GLDS-449-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23640 MW; 1CA25DD772219287 CRC64; MKIKAWDLYL ITEQSLSAGR KSLEIVKEAA AAGVDVIQLR DKNLSLRAKF KLGQKIKEIC LKQKIKFIVN DRVDLALALD ADGVHLGQSD LPLKAARKVL GKDKIIGISA WKPAEIKEAE AGGADYLGVG AVFSTKSKKL NSAKNGIGLA KINEIRKTTK LPLVAIGGLN KENAAEVIKS GADCISVISA LTKAKKVKAE TKEFKNIIQT AKKRLREGI // ID E3DVL0_BACA1 Unreviewed; 205 AA. AC E3DVL0; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Transcriptional regulator TenI; GN OrderedLocusNames=BATR1942_03475; OS Bacillus atrophaeus (strain 1942). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=720555; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1942; RA Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., RA Bruce D., Karavis M., McGregor P., Hong C., Park K.H., Akmal A., RA Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P., RA Lindquist J., Liem A., Fochler E., Tapia R., Bishop-Lilly K., RA Detter C., Han C., Sozhamannan S., Rosenzweig C.N., Skowronski E.; RT "Genomic signatures of strain selection and enhancement in Bacillus RT atrophaeus subsp. Globigii, a historical biowarfare simulant."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002207; ADP31649.1; -; Genomic_DNA. DR RefSeq; YP_003972580.1; NC_014639.1. DR EnsemblBacteria; ADP31649; ADP31649; BATR1942_03475. DR GeneID; 9890683; -. DR KEGG; bae:BATR1942_03475; -. DR PATRIC; 42568198; VBIBacAtr152324_0713. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR BioCyc; BATR720555:GHTA-715-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 22949 MW; CEB624F8A90A12E5 CRC64; MELHAITDNC QRVEHLAASI IAVKDEVDFI HIRERSKSAD DILKLLELIY QGGVEKQKLI VNDRVDIALF ANIHRVQLPD HSFSAKRVRA RFPHLHIGRS VHSLEEAVQA EREDADYVLF GHVFETECKQ GLEGRGVQLL TEIKQTLAIP VIALGGITPS RIPEVRQADP AGIAVMSGIF SAPDPLEASR SYSRKLKENK YEKAL // ID E3DZJ9_BACA1 Unreviewed; 222 AA. AC E3DZJ9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BATR1942_17065; OS Bacillus atrophaeus (strain 1942). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=720555; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1942; RA Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., RA Bruce D., Karavis M., McGregor P., Hong C., Park K.H., Akmal A., RA Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P., RA Lindquist J., Liem A., Fochler E., Tapia R., Bishop-Lilly K., RA Detter C., Han C., Sozhamannan S., Rosenzweig C.N., Skowronski E.; RT "Genomic signatures of strain selection and enhancement in Bacillus RT atrophaeus subsp. Globigii, a historical biowarfare simulant."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002207; ADP34332.1; -; Genomic_DNA. DR RefSeq; YP_003975263.1; NC_014639.1. DR EnsemblBacteria; ADP34332; ADP34332; BATR1942_17065. DR GeneID; 9893398; -. DR KEGG; bae:BATR1942_17065; -. DR PATRIC; 42573766; VBIBacAtr152324_3474. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; BATR720555:GHTA-3430-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23611 MW; 2F9B04B324FE0FDB CRC64; MTRISREMMK DLLSVYFIMG SNNTEAEPLS VVQKALKGGV TLFQFREKGS NALIGADQLA FAEKMQSACR KAGVPFIVND DVELAVKLKA DGVHIGQDDA DAKEVRAAIG DMILGVSAHT MSEVKQAEAD GADYVGMGPI YPTETKKDTK AVQGVSLIEA VRRQGISIPI VGIGGITLEN AAPVIEAGAD GVSMISAISM AQDPEESAQH FYQVIQKQKP TS // ID E3E5U5_PAEPS Unreviewed; 229 AA. AC E3E5U5; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PPSC2_c4214; OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=886882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC2; RX PubMed=21037012; DOI=10.1128/JB.01234-10; RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F., RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., RA Du B.; RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of RT plant growth-promoting Rhizobacterium with broad-spectrum RT antimicrobial activity."; RL J. Bacteriol. 193:311-312(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002213; ADO58164.1; -; Genomic_DNA. DR RefSeq; YP_003948405.1; NC_014622.1. DR ProteinModelPortal; E3E5U5; -. DR EnsemblBacteria; ADO58164; ADO58164; PPSC2_c4214. DR GeneID; 9852503; -. DR KEGG; ppm:PPSC2_c4214; -. DR PATRIC; 42511534; VBIPaePol172748_4026. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MLARYFI; -. DR BioCyc; PPOL886882:GBY1-4326-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 24464 MW; E115A209C789250B CRC64; MSGRILPEIM RRHLQMYLVV GSVNCLAEPS RVVQEALAGG TTMIQFREKG RSALTGVPML ELARQLQDLC HHAGIPFIVN DDVELALELN ADGVHIGQDD ESADSVRARI GNRILGVSAH TIEEARRAIL QGADYLGVGP IYPTISKDDA HAVQGPAILY EMRKAGIDLP IVGIGGITID RVKEVVSAGA DGVAVISAVT QAEQIRVAAE GLKKKVVLSI KHPGMSQKL // ID E3E7Q9_PAEPS Unreviewed; 191 AA. AC E3E7Q9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=PPSC2_c2899; OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=886882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC2; RX PubMed=21037012; DOI=10.1128/JB.01234-10; RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F., RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., RA Du B.; RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of RT plant growth-promoting Rhizobacterium with broad-spectrum RT antimicrobial activity."; RL J. Bacteriol. 193:311-312(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002213; ADO56864.1; -; Genomic_DNA. DR RefSeq; YP_003947105.1; NC_014622.1. DR EnsemblBacteria; ADO56864; ADO56864; PPSC2_c2899. DR GeneID; 9851203; -. DR KEGG; ppm:PPSC2_c2899; -. DR PATRIC; 42508990; VBIPaePol172748_2771. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR BioCyc; PPOL886882:GBY1-2992-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 191 AA; 20434 MW; 562B58E58BCB6245 CRC64; MNVPQVAAAI CPYIHYVHAR SKQKGASALL SLTRSMIKQE VPLRQIVVND RVDVALLTSA GAVQLPANGL SVVDAKSLLS EGTRCGVSVH SLEEVQTAEQ AGADYVLFGH VYETHCKAGL VPRGIAQLER ICRLSDIPVI ALGGIQPHHV PELYHAGASG IAVMSGIWEA KSPVAAAMEY RRMVDLVVHD L // ID E3EM14_BIFBS Unreviewed; 918 AA. AC E3EM14; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=Thiamine biosynthesis protein thiC; GN Name=thiE; OrderedLocusNames=BBIF_0505; OS Bifidobacterium bifidum (strain S17). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=883062; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S17; RX PubMed=21037011; DOI=10.1128/JB.01180-10; RA Zhurina D., Zomer A., Gleinser M., Brancaccio V.F., Auchter M., RA Waidmann M.S., Westermann C., van Sinderen D., Riedel C.U.; RT "Complete genome sequence of Bifidobacterium bifidum S17."; RL J. Bacteriol. 193:301-302(2011). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002220; ADO52710.1; -; Genomic_DNA. DR RefSeq; YP_003938284.1; NC_014616.1. DR EnsemblBacteria; ADO52710; ADO52710; BBIF_0505. DR GeneID; 9846713; -. DR KEGG; bbi:BBIF_0505; -. DR PATRIC; 42478429; VBIBifBif172477_0517. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR OMA; INTICSA; -. DR BioCyc; BBIF883062:GH1R-524-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 918 AA; 100244 MW; 8DBA526721194E6B CRC64; MSNEYPFASM RDSFDLSAYF VVGPQDCKDR PLTEVIDQAL HGGATFIQLR AKGADASELT EMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQSDM EPREARAMLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSSTK PEASVGGNDG SGKTLDAAQI NTICSASEFP VVVGGGVTAA DMAMLAGTKA AGWFAVSAIA GAEDPEAATR EMVSGWKAVR ADERHGYAPR IVTHTPATDT QAAQEGSAAA GAEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF SYEYGSYDLE VPYTEIKLSD TPGVGPNAPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL QDDGKRAIKR GRATKEWRGR THQPMRAKDH PVTQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHGAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVA DAVTGKIPEG VETPANPVTD DTVVSANVLS PEEILAGMDA MGEKYRAQGG KLYSKASE // ID E3F4A2_KETVY Unreviewed; 212 AA. AC E3F4A2; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=EIO_1699; OS Ketogulonicigenium vulgare (strain Y25). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ketogulonicigenium. OX NCBI_TaxID=880591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y25; RX PubMed=21037005; DOI=10.1128/JB.01189-10; RA Xiong X.H., Han S., Wang J.H., Jiang Z.H., Chen W., Jia N., Wei H.L., RA Cheng H., Yang Y.X., Zhu B., You S., He J.Y., Hou W., Chen M.X., RA Yu C.J., Jiao Y.H., Zhang W.C.; RT "Complete genome sequence of the bacterium Ketogulonicigenium vulgare RT Y25."; RL J. Bacteriol. 193:315-316(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002224; ADO42821.1; -; Genomic_DNA. DR RefSeq; YP_003964121.1; NC_014625.1. DR EnsemblBacteria; ADO42821; ADO42821; EIO_1699. DR GeneID; 9872322; -. DR KEGG; kvu:EIO_1699; -. DR PATRIC; 43495705; VBIKetVul170732_1938. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR BioCyc; KVUL880591:GHQW-1699-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 212 AA; 23295 MW; 8732AD9CD1801335 CRC64; MTDTTTAADD LPQIYLISPP TFDLDVFPDL MARCLDAVET SCVRLSLATR DEDVIQRAAD SLRQITHDRD IALVIENHAL LVERLGLDGV HLTDGSRSVH KMRRDLGEDA IVGTYCGTSR HDGMTAGDMG ADYVSFGPVG QSLLGTGERA TLDLFQWWSE MIEVPAVTEG GLDEELIRQL APYSDFFGFG EEIWATEDPV ATYQRLVAAT RG // ID E3G350_ENTLS Unreviewed; 211 AA. AC E3G350; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Entcl_4166; OS Enterobacter lignolyticus (strain SCF1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=701347; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCF1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., RA Woo H., Hazen T.C., Woyke T.; RT "Complete sequence of Enterobacter cloacae SCF1."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002272; ADO50399.1; -; Genomic_DNA. DR RefSeq; YP_003943683.1; NC_014618.1. DR EnsemblBacteria; ADO50399; ADO50399; Entcl_4166. DR GeneID; 9909255; -. DR KEGG; esc:Entcl_4166; -. DR PATRIC; 42602606; VBIEntClo171306_4244. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; ECLO701347:GH9V-4251-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22968 MW; 826F08DA9B88188F CRC64; MYQPDFPPVP FRLGLYPVVD SVEWIARLLD AGVRTLQLRI KDKRDDEVEA DVVAAIALGR RYNARLFIND YWRLAISHQA YGVHLGQEDL QTTDLAAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTRTKQMP SAPQGLEQLT RHITRLANYP TVAIGGISLE RTPSVLATGV GSVAVVSAIT QAADWQLATA QLLDMAGAGN E // ID E3GFH9_EUBLK Unreviewed; 217 AA. AC E3GFH9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ELI_3352; OS Eubacterium limosum (strain KIST612). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=903814; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIST612; RA Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., RA Chang I.S., Choi I.-G.; RT "The genome sequence of Eubacterium limosum (strain KIST612)."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KIST612; RA Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., RA Chang I.S., Choi I.-G.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002273; ADO38313.1; -; Genomic_DNA. DR RefSeq; YP_003961276.1; NC_014624.2. DR EnsemblBacteria; ADO38313; ADO38313; ELI_3352. DR GeneID; 9885248; -. DR KEGG; elm:ELI_3352; -. DR PATRIC; 42609513; VBIEubLim172772_3097. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR BioCyc; ELIM903814:GH0C-3417-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23203 MW; F029CB4F9B86815F CRC64; MKNNVKKEDM LLYIVTDRSW LGESTLEEEV CAAIDGGATF LQIREKDMAH QDFLHEARNL KELARAAGIP YVINDEVEIA LEVDADGVHI GQSDGAVAET RKKIGPNKIL GVSAQTLEQA LAAEKEGADY LGVGAVFSTS TKTDAKAVSF ETLKSICSSV KIPVVAIGGI SEENLLELSG SKVDGVAVIS AVFAQPDTRA AAQKIRKLSE KMVKSND // ID E3GKC1_EUBLK Unreviewed; 201 AA. AC E3GKC1; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=ELI_0854; OS Eubacterium limosum (strain KIST612). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=903814; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIST612; RA Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., RA Chang I.S., Choi I.-G.; RT "The genome sequence of Eubacterium limosum (strain KIST612)."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KIST612; RA Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., RA Chang I.S., Choi I.-G.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002273; ADO35868.1; -; Genomic_DNA. DR RefSeq; YP_003958831.1; NC_014624.2. DR EnsemblBacteria; ADO35868; ADO35868; ELI_0854. DR GeneID; 9882754; -. DR KEGG; elm:ELI_0854; -. DR PATRIC; 42604843; VBIEubLim172772_0804. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ASHIFAT; -. DR BioCyc; ELIM903814:GH0C-853-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 21576 MW; E34A94D072054E52 CRC64; MFEIIAVTSR GCCPASREFA AQAARIAASG VSKVILREKD LPPADYKVLS RDFLRECGDA GAELLLHCFA AVAKELNHPK IHLPLPVLEA QPGLRRDFKT IGVSVHSLEQ ARSALRLGAD YLSAGHVFAT DCKKGRTPRG LGFLSEICGE MPIPVYAIGG ISAENIRSVQ EAGAAGACVM SSIMRSEAPE EYVKTLIQKI K // ID E3GRT8_HAEI2 Unreviewed; 226 AA. AC E3GRT8; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=R2846_0161; OS Haemophilus influenzae (strain R2846 / 12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=262727; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R2846 / 12; RA VanWagoner T.M., Erwin A.L., Kaul R., Mahaffey M., Zhou Y., RA Aggarwal G., Chang J., Deng H., Gillett W., Haugen E., Kibukawa M., RA Phelps K., Saenphimma C., Sivam D., Worthy E.A., Olson M.V., RA Stull T.L., Smith A.L.; RT "Genome sequence of the middle ear isolate Haemophilus influenzae RT R2846."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002276; ADO95625.1; -; Genomic_DNA. DR RefSeq; YP_005828680.1; NC_017452.1. DR ProteinModelPortal; E3GRT8; -. DR EnsemblBacteria; ADO95625; ADO95625; R2846_0161. DR GeneID; 12596839; -. DR KEGG; hie:R2846_0161; -. DR PATRIC; 43041685; VBIHaeInf30952_0165. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; HINF262727:GLDQ-161-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24721 MW; 5E34364400694040 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID E3H564_ROTDC Unreviewed; 204 AA. AC E3H564; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HMPREF0733_11310; OS Rothia dentocariosa (strain ATCC 17931 / CDC X599 / XDIA). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Rothia. OX NCBI_TaxID=762948; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17931 / CDC X599 / XDIA; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RT "The complete genome of Rothia dentocariosa ATCC 17931."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002280; ADP40767.1; -; Genomic_DNA. DR RefSeq; YP_003984201.1; NC_014643.1. DR ProteinModelPortal; E3H564; -. DR EnsemblBacteria; ADP40767; ADP40767; HMPREF0733_11310. DR GeneID; 9902593; -. DR KEGG; rdn:HMPREF0733_11310; -. DR PATRIC; 42677484; VBIRotDen160907_1277. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; RDEN762948:GHPW-1344-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). SQ SEQUENCE 204 AA; 21950 MW; 7DC9F4BCE96E1B13 CRC64; MTTNSAAETA TPLDLSLYLV TGENPVETVR RARHATCIQV RSKPISAHDL YALAEEIARI ALPHQKILID DRVDVALALR ARGVRIDGVH IGQDDLPVAD ARRLLGEHAI IGLTTGTREL VERANTVAHL IDYIGAGPFR PSPTKASNRP PLGVEGLREL AELSKVPVVA IGDIWPQDCP SIRETGVAGV AMARAFVENP ELQA // ID E3H8I5_ILYPC Unreviewed; 211 AA. AC E3H8I5; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ilyop_1186; OS Ilyobacter polytropus (strain DSM 2926 / CuHBu1). OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Ilyobacter. OX NCBI_TaxID=572544; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2926 / CuHBu1; RX PubMed=21304735; RA Sikorski J., Chertkov O., Lapidus A., Nolan M., Lucas S., RA Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Brambilla E., Yasawong M., Rohde M., Pukall R., RA Spring S., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Ilyobacter polytropus type strain RT (CuHbu1)."; RL Stand. Genomic Sci. 3:304-314(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002281; ADO82967.1; -; Genomic_DNA. DR RefSeq; YP_003967315.1; NC_014632.1. DR EnsemblBacteria; ADO82967; ADO82967; Ilyop_1186. DR GeneID; 9868694; -. DR KEGG; ipo:Ilyop_1186; -. DR PATRIC; 42646087; VBIIlyPol34265_1224. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; IPOL572544:GJ9I-1212-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23540 MW; 30188655D482D946 CRC64; MRSRITIPTG LYGITGEAFS NGKSNLQCVE SMIKAGIKII QYREKDKPLR DKINDIKKIR ELCRENEVLF IINDHVDMAI LVDADGVHVG QEDMHPSDVR QLIGPDKIIG LSTHSQEEGL ACLEEDIDYI GVGPVFPTTT KDRKAVGLEY LDFAVKNLDI PFVAIGGIKE HNIETILEAG AKRICLVSEI IGAKDITKKI QKLNQIIEKK Y // ID E3HWL8_ACHXA Unreviewed; 320 AA. AC E3HWL8; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 11-DEC-2013, entry version 21. DE SubName: Full=NUDIX domain protein 2; DE EC=3.6.1.-; GN OrderedLocusNames=AXYL_00569; OS Achromobacter xylosoxidans (strain A8). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=762376; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A8; RX PubMed=21097610; DOI=10.1128/JB.01299-10; RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.; RT "Complete genome sequence of the haloaromatic acids-degrading RT bacterium Achromobacter xylosoxidans A8."; RL J. Bacteriol. 193:791-792(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002287; ADP13927.1; -; Genomic_DNA. DR RefSeq; YP_003976642.1; NC_014640.1. DR EnsemblBacteria; ADP13927; ADP13927; AXYL_00569. DR GeneID; 9894901; -. DR KEGG; axy:AXYL_00569; -. DR PATRIC; 42554122; VBIAchXyl160325_0573. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; AXYL762376:GJUB-569-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 320 AA; 34113 MW; 30F630CF17E75B03 CRC64; MSEKIVDVAA GLILRPDGML LLGQRPEGKP WAGWWELPGG KLEPGETVLQ ALARELQEEI GIRVTQSRPW VTYVHAYPHT TVRLAFCHVT GWEGEPRSLE NQRLEWVAPA QAASVGDLLP ATLPPLRWLQ LPTSYGISSV GSRAGVAAFL GRLEAALARG VKLVQLREPQ WPDGVASPSL HEVLQQVQKR CRAAGARVLV NSVHPAAWWR EADGVHLRAA DAAKLTARPE LPAGALVGAS AHDNAQVVHA RELGADFAVL GPVLDTPSHP GAATLGWEGF VEGNRDAGIP VFALGGQSTQ TVSQALRHGA HGIAGIRGLI // ID E3HWQ0_ACHXA Unreviewed; 221 AA. AC E3HWQ0; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AXYL_00601; OS Achromobacter xylosoxidans (strain A8). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=762376; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A8; RX PubMed=21097610; DOI=10.1128/JB.01299-10; RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.; RT "Complete genome sequence of the haloaromatic acids-degrading RT bacterium Achromobacter xylosoxidans A8."; RL J. Bacteriol. 193:791-792(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002287; ADP13959.1; -; Genomic_DNA. DR RefSeq; YP_003976674.1; NC_014640.1. DR EnsemblBacteria; ADP13959; ADP13959; AXYL_00601. DR GeneID; 9894933; -. DR KEGG; axy:AXYL_00601; -. DR PATRIC; 42554186; VBIAchXyl160325_0605. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; AXYL762376:GJUB-601-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23256 MW; 7474E57405C77208 CRC64; MKALRFPTGL YGVTPEWDDT DRLLLAVRQA ADGGMRSLQL RRKNVPDAVR AAQARALAPL CRELGVLFLI NDDWRLALEV GADGAHVGRE DESLARIRAE AGPDLILGGS SYDDLGRAQE LLAAGADYIA FGAMYASSVK PDTVRAPLSV LTEARRLTDN CDAPRPAVVA IGGITPDNAP LVAQAGADAI AVITALFEAP SIRAAAAACS APYSVNPNRK P // ID E3HZF3_RHOVT Unreviewed; 192 AA. AC E3HZF3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Rvan_0621; OS Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / OS LMG 4299). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Rhodomicrobium. OX NCBI_TaxID=648757; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002292; ADP69899.1; -; Genomic_DNA. DR RefSeq; YP_004010998.1; NC_014664.1. DR EnsemblBacteria; ADP69899; ADP69899; Rvan_0621. DR GeneID; 9931391; -. DR KEGG; rva:Rvan_0621; -. DR PATRIC; 42668290; VBIRhoVan113057_0646. DR KO; K00788; -. DR BioCyc; RVAN648757:GHZT-627-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 192 AA; 19942 MW; B87988111ACC3463 CRC64; MNEKPCGLIV AIPPALETEW AARLSELVAS FRPAGLIVRP SRENAALVKA AAPLELAVLV AGEIREAARA GATGVWFPSS EDADFAGARK ALGADAILGT ACGVSRHAAM EAAEAGVDFL AFDAAADLDA AVDASAWWDE VAEVPVALIV GATKPERDRV LDARPDFLLV EESVTAGESL IFATEFGLQS QT // ID E3I1R9_RHOVT Unreviewed; 199 AA. AC E3I1R9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 16-OCT-2013, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Rvan_0862; OS Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / OS LMG 4299). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Rhodomicrobium. OX NCBI_TaxID=648757; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002292; ADP70138.1; -; Genomic_DNA. DR RefSeq; YP_004011237.1; NC_014664.1. DR ProteinModelPortal; E3I1R9; -. DR EnsemblBacteria; ADP70138; ADP70138; Rvan_0862. DR GeneID; 9931636; -. DR KEGG; rva:Rvan_0862; -. DR PATRIC; 42668824; VBIRhoVan113057_0909. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; RVAN648757:GHZT-872-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 199 AA; 21453 MW; C903D3F45FFE3800 CRC64; MTTALPRFYP VVPDVTFVER LARVGIKLIQ LRMKDAASTE IAPAITQALE TCRVHGAALV VNDHWREAID CGAPWVHLGQ GDLDTADVAA IRRAGLKLGL STHSHEELDR ALTFDPDYIA LGPVYQTTLK VMPWAPQGLA RVGEWKALAK RPLVAIGGIT LERAPDVYAA GADSIAVVSD VVFAPDPEAR AQDWLALSA // ID E3IB78_GEOS0 Unreviewed; 219 AA. AC E3IB78; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GY4MC1_1607; OS Geobacillus sp. (strain Y4.1MC1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=581103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y4.1MC1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., RA Ovchinnikova G., Brumm P., Mead D., Woyke T.; RT "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002293; ADP74384.1; -; Genomic_DNA. DR RefSeq; YP_003988995.1; NC_014650.1. DR EnsemblBacteria; ADP74384; ADP74384; GY4MC1_1607. DR GeneID; 9928484; -. DR KEGG; gmc:GY4MC1_1607; -. DR PATRIC; 42633231; VBIGeoSp111282_1737. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; GSP581103:GHT2-1678-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23147 MW; 70A04CC1DE3FE91B CRC64; MARIAREEMK QRLKVYFIMG SVNCKKSPFE VLTEAIDGGI TLFQFREKGS GALVGEQKYE FAKQLQAICQ KRGIPFIVND DVELALAIDA DGVHIGQDDE DARIVREKIG DKILGVSAHN LAEAQAAAAA GADYIGVGPI YPTKSKADAK QAQGPGMIRL LRDNGIDIPI VGIGGITAEN ASEVMNAGAD GVSVISAIAS APSPLLATKQ LAQTVLNNE // ID E3IDW7_GEOS0 Unreviewed; 202 AA. AC E3IDW7; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 16-OCT-2013, entry version 22. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=GY4MC1_3187; OS Geobacillus sp. (strain Y4.1MC1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=581103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y4.1MC1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., RA Ovchinnikova G., Brumm P., Mead D., Woyke T.; RT "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002293; ADP75864.1; -; Genomic_DNA. DR RefSeq; YP_003990475.1; NC_014650.1. DR ProteinModelPortal; E3IDW7; -. DR EnsemblBacteria; ADP75864; ADP75864; GY4MC1_3187. DR GeneID; 9930067; -. DR KEGG; gmc:GY4MC1_3187; -. DR PATRIC; 42636790; VBIGeoSp111282_3517. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR BioCyc; GSP581103:GHT2-3262-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 202 AA; 22008 MW; D836052E014B8613 CRC64; MERQLHIIST GKQPLEQFVA ICARVHPYVD AIHVREKRKT AREISEFLTE LIGRGIPPKK IIVNDRIDVA VVFGVKGVQL AHHSLSVHQT KRHFPSLSVG CSVHSLEEAM EAEKSGADYC IYGHIFPTAS KLGAPPRGIE SLRNIVHHVN IPVIAIGGIH SDNAEQVLQA GAHGIAVMSA VFCAKDPVSE AKKLAKIVKK MA // ID E3IK37_DESVR Unreviewed; 219 AA. AC E3IK37; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Deval_2187; OS Desulfovibrio vulgaris (strain RCH1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=573059; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCH1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Chakraborty R., RA Arkin A.P., Dehal P., Wall J.D., Deutschbauer A.M., Hazen T.C., RA Woyke T.; RT "Complete sequence of chromosome of Desulfovibrio vulgaris RCH1."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002297; ADP87331.1; -; Genomic_DNA. DR RefSeq; YP_005702969.1; NC_017310.1. DR ProteinModelPortal; E3IK37; -. DR EnsemblBacteria; ADP87331; ADP87331; Deval_2187. DR GeneID; 12866784; -. DR KEGG; dvg:Deval_2187; -. DR PATRIC; 42912033; VBIDesVul75230_2302. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; DVUL573059:GLCM-2238-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22455 MW; 1B76358C9963C708 CRC64; MTRVRKAAVD YGLYLVTDAG LTDARLHEVV TAAISGGVGI VQLREKATPT RAFVDRARAL VALLRPRGIP LLINDRVDVA LAAGADGVHV GQSDMHVGDV RALMGPDAIV GLSVETPAQA KAAEHAPVDY LGVSPVFATA TKPDAAPPWG VAGLCGLRRM TRHVLVGIGG IGPVNAAEVL HAGAEGIAVV SAICGAADPL AATRALRAVV DEVRVPVRI // ID E3ISH7_DESVR Unreviewed; 226 AA. AC E3ISH7; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Deval_1943; OS Desulfovibrio vulgaris (strain RCH1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=573059; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCH1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Chakraborty R., RA Arkin A.P., Dehal P., Wall J.D., Deutschbauer A.M., Hazen T.C., RA Woyke T.; RT "Complete sequence of chromosome of Desulfovibrio vulgaris RCH1."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002297; ADP87091.1; -; Genomic_DNA. DR RefSeq; YP_005702729.1; NC_017310.1. DR ProteinModelPortal; E3ISH7; -. DR EnsemblBacteria; ADP87091; ADP87091; Deval_1943. DR GeneID; 12866534; -. DR KEGG; dvg:Deval_1943; -. DR PATRIC; 42911505; VBIDesVul75230_2044. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; DVUL573059:GLCM-1988-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23899 MW; 56DCC90A1670FDA7 CRC64; MPVILPGTTP DADIYCLTDS GLCLGRPTVD VVDAMLQAGA RIIQYREKEK KAGEMLRECL ELRRMTREAG ACFIVNDHVD IAILCDADGV HIGQDDLPVG EVRRLIGPDR AIGLSTHSPE QAMAAVAAGV DYIGVGPIFA TKTKKDVCDP VGYAYLDWVV THLDIPFVAI GGIKLHNIGE VAAHGARCCA LVSEIVGAVD IVAQVQTVRR AMRGVAAAGT DSPQAG // ID E3JCP6_FRASU Unreviewed; 274 AA. AC E3JCP6; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=FraEuI1c_1830; OS Frankia sp. (strain EuI1c). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=298654; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EuI1c; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.; RT "Complete sequence of Frankia sp. EuI1c."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002299; ADP79886.1; -; Genomic_DNA. DR RefSeq; YP_004015756.1; NC_014666.1. DR EnsemblBacteria; ADP79886; ADP79886; FraEuI1c_1830. DR GeneID; 9972260; -. DR KEGG; fri:FraEuI1c_1830; -. DR PATRIC; 42615668; VBIFraSp2231_1879. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CVGPVHA; -. DR BioCyc; FSP298654:GHN6-1854-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 96 100 HMP-PP binding (By similarity). FT REGION 194 196 THZ-P binding (By similarity). FT METAL 129 129 Magnesium (By similarity). FT METAL 148 148 Magnesium (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 167 167 HMP-PP (By similarity). FT BINDING 197 197 HMP-PP (By similarity). FT BINDING 230 230 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 274 AA; 27892 MW; F0D7A67F69C8540D CRC64; MADDLTDLTG LAGDAELDEP AARQTGPSAL DVIAEQAIVD LALAEAPDGA PLARAERLAR LADARLYLCT PRQPAFDAFL DGVLAPAGGP GVDLIQLREK GLEWRAEAAA LGRMVAAGRR HGALVSGNDR ADLASVAGVD ILHVGQDDIP PATARRLLGP DVIIGLSTHD EDQLAAAIED PDVDYFCVGP VWPTPTKEGR PGVGLGLVAT AVAAAPPFAP GAKPWFAIGG IDAERLDEVL ATGARRAVVV RAITGAADPA AAAAALAGRL RAAG // ID E3KEB3_PUCGT Unreviewed; 568 AA. AC E3KEB3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 2. DT 16-APR-2014, entry version 22. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=PGTG_08842; OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL) OS (Black stem rust fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia. OX NCBI_TaxID=418459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CRL 75-36-700-3; RG The Broad Institute Genome Sequencing Platform; RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., RA Brockman W., Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., RA Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., RA Larson L., White J., Zeng Q., Kodira C., Yandava C., Alvarado L., RA O'Leary S., Szabo L., Dean R., Schein J.; RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL RT 75-36-700-3."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CRL 75-36-700-3 / race SCCL; RX PubMed=21536894; DOI=10.1073/pnas.1019315108; RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E., RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., RA Cantarel B.L., Chiu R., Coutinho P.M., Feau N., Field M., Frey P., RA Gelhaye E., Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., RA Kuees U., Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., RA Murat C., Pangilinan J.L., Park R., Pearson M., Quesneville H., RA Rouhier N., Sakthikumar S., Salamov A.A., Schmutz J., Selles B., RA Shapiro H., Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., RA Rouze P., Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C., RA Grigoriev I.V., Szabo L.J., Martin F.; RT "Obligate biotrophy features unraveled by the genomic analysis of rust RT fungi."; RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS178283; EFP82646.2; -; Genomic_DNA. DR RefSeq; XP_003327065.2; XM_003327017.2. DR EnsemblFungi; EFP82646; EFP82646; PGTG_08842. DR GeneID; 10530029; -. DR KEGG; pgr:PGTG_08842; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 568 AA; 61678 MW; A52767B15574AB2E CRC64; MIDYSLYLVT SSEDLPAGAT VESTVREAVR AGVKIVQLRE KNLSTKLFLE RAKALREICQ PPVKLIINDR IDIAHASNAD GVHLGQDDMP LLDAQNIFRV QEIIGISVNT VEEAVAAVRT GASYLGVGTC WPTGTKSIPE HKIIGPRGIK TIRDELDRLG LSVPLVAIGG INATNLIRTL YGCTSNHLYT DRYAESPIGV AVVSAIMKSP DPYQSTQTLK NMIQEFKGWL RAPAEPFSNP QVKIQLKLAV AMMKFHSKTS TPLIHHITNT VVQNDCANLT LAYGCSPIMS SNLNEMEDLV NLTTGSLVLN LGTFDDNQVR AMKLAGRQAN LTGKPVIFDP VGVGASRERK KKANEILNAV QMSVIKGNQA EIASLARFNS NGVSSCGVDS SGEVEEPALL VKHLARQELC VVVMTGKTDW VSDGTHVFRL NNGVSELSGI TGSGCMTGTS IGCFASLAQQ EVVKDTHSGL LLNLKNIHHD FGETLLASIL GISTINVVAE MVHQVEHEKL EHGPMNLKIK IMDRISLSRQ IEPFWQAIHA DIKLSSDFFH DDVAHHDEAS SNGATRTE // ID E3PBW2_ECOH1 Unreviewed; 211 AA. AC E3PBW2; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ETEC_4253; OS Escherichia coli O78:H11 (strain H10407 / ETEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=316401; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H10407 / ETEC; RX PubMed=20802035; DOI=10.1128/JB.00710-10; RA Crossman L.C., Chaudhuri R.R., Beatson S.A., Wells T.J., Desvaux M., RA Cunningham A.F., Petty N.K., Mahon V., Brinkley C., Hobman J.L., RA Savarino S.J., Turner S.M., Pallen M.J., Penn C.W., Parkhill J., RA Turner A.K., Johnson T.J., Thomson N.R., Smith S.G., Henderson I.R.; RT "A commensal gone bad: complete genome sequence of the prototypical RT enterotoxigenic Escherichia coli strain H10407."; RL J. Bacteriol. 192:5822-5831(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN649414; CBJ03758.1; -; Genomic_DNA. DR RefSeq; YP_006117789.1; NC_017633.1. DR EnsemblBacteria; CBJ03758; CBJ03758; ETEC_4253. DR GeneID; 12882256; -. DR KEGG; elh:ETEC_4253; -. DR PATRIC; 42965024; VBIEscCol136115_4828. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; ECOL316401:GLD0-4344-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23019 MW; F6C95CC3824F07F3 CRC64; MYQPDFPPVP FRSGLYSVVD SLQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E3PTC4_CLOSD Unreviewed; 217 AA. AC E3PTC4; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CLOST_2008; OS Clostridium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / NCIB OS 10654). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=499177; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / NCIB 10654; RX PubMed=20937090; DOI=10.1186/1471-2164-11-555; RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R., RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M., RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.; RT "Clostridium sticklandii, a specialist in amino acid RT degradation:revisiting its metabolism through its genome sequence."; RL BMC Genomics 11:555-555(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP565809; CBH22128.1; -; Genomic_DNA. DR RefSeq; YP_003937033.1; NC_014614.1. DR EnsemblBacteria; CBH22128; CBH22128; CLOST_2008. DR GeneID; 9856472; -. DR KEGG; cst:CLOST_2008; -. DR PATRIC; 42274648; VBICloSti32817_1996. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; CSTI499177:GJE9-2071-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23541 MW; F687F9EA1495C646 CRC64; MKKSELRKKT DYSLYLVTDR LCLSGKDLFH SVEDAIKGGV TVVQLREKTA SCREFYQIGL KLKEITRRHN IPLIINDRVD IALALDAEGV HVGQEDLDAL LVRKLLGQDK ILGVSAKTLS QATKAIESDA DYIGVGAIFP TLTKADASEL SLLDISDICS KINIPVLGIG GINQENISKL NNLGLDGVCV VSAILGQADC LNATKNLRQS VDNLLKI // ID E3QCM7_COLGM Unreviewed; 533 AA. AC E3QCM7; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE SubName: Full=Hydroxyethylthiazole kinase; GN ORFNames=GLRG_03759; OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize OS anthracnose fungus) (Glomerella graminicola). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae; OC mitosporic Glomerellaceae; Colletotrichum. OX NCBI_TaxID=645133; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M1.001 / M2 / FGSC 10212; RX PubMed=22885923; DOI=10.1038/ng.2372; RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J., RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., RA Altmueller J., Alvarado-Balderrama L., Bauser C.A., Becker C., RA Birren B.W., Chen Z., Choi J., Crouch J.A., Duvick J.P., Farman M.A., RA Gan P., Heiman D., Henrissat B., Howard R.J., Kabbage M., Koch C., RA Kracher B., Kubo Y., Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., RA Moore N., Neumann U., Nordstroem K., Panaccione D.G., Panstruga R., RA Place M., Proctor R.H., Prusky D., Rech G., Reinhardt R., RA Rollins J.A., Rounsley S., Schardl C.L., Schwartz D.C., Shenoy N., RA Shirasu K., Sikhakolli U.R., Stueber K., Sukno S.A., Sweigard J.A., RA Takano Y., Takahara H., Trail F., van der Does H.C., Voll L.M., RA Will I., Young S., Zeng Q., Zhang J., Zhou S., Dickman M.B., RA Schulze-Lefert P., Ver Loren van Themaat E., Ma L.-J., RA Vaillancourt L.J.; RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi RT deciphered by genome and transcriptome analyses."; RL Nat. Genet. 44:1060-1065(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG697341; EFQ28615.1; -; Genomic_DNA. DR EnsemblFungi; EFQ28615; EFQ28615; GLRG_03759. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 533 AA; 55050 MW; 1B7675DE392D148F CRC64; MPQPTVDYSL YLVTDSTPAI LGDRDLASVV AAAVRGGVTV VQYRDKTSDT GALVANARRL HAVTRAAGVP LLINDRVDVA LAVGCEGVHI GQDDMELATA RKILGPDAII GVTASTVEEA LKACEDGADY LGIGTVFATS TKENTKHIIG TAGLRRILAE LASAGHIPRV KTVCIGGLKP SNIQRVLYQS APSPPSGPSL DGVALVSAIV AATDPESESR RLLELVRTSS SYRQIVSSSS GGGPSADVGS LLDRVPDVIS AVASASPLSH NMTNLVVQNF AANVALAVGA SPIMANYGEE AADLARLGGS LVVNMGTVTP EGIANYLQAL SAYNAAGRPV VFDPVGAGAT SVRRAAVQTI LAGGYLDLIK GNEGEVATVH GQAAAPEQQQ KGVDSSSTLS HAQKARIVRD LARRERNVVL MTGATDYVSD GGRTFAVENG HELLGQITGT GCVLGTTVSA ALAAWEDDRL LAVLAGLLHF EIAAERAAVR GDVQGPGTFV PAFIDELARI RRQTVDGDLA WLSGAKVKAV HVE // ID E3S6Y3_PYRTT Unreviewed; 560 AA. AC E3S6Y3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 16-APR-2014, entry version 16. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=PTT_18545; OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus) OS (Drechslera teres f. teres). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae; OC Pleosporaceae; Pyrenophora. OX NCBI_TaxID=861557; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0-1; RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109; RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., RA Moffat C.S., Oliver R.P., Friesen T.L.; RT "A first genome assembly of the barley fungal pathogen Pyrenophora RT teres f. teres."; RL Genome Biol. 11:R109.1-R109.14(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL537489; EFQ86284.1; -; Genomic_DNA. DR RefSeq; XP_003305638.1; XM_003305590.1. DR EnsemblFungi; EFQ86284; EFQ86284; PTT_18545. DR GeneID; 10514407; -. DR KEGG; pte:PTT_18545; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 560 AA; 58999 MW; C7AED5B55FD268D2 CRC64; MEKQKVDYSL YLVTDSTEAI LGSRDLADVV EQALSGGVTI VQYRDKTSDT GLLISTAKKL HEKCKAHGIP LVINDRVDVA LAVGCEGVHL GQDDMSVVEA RRILGDSNII GATVSSIEEA RIAVERGADY LGIGTLYATN TKKNTKDIIG ITGIRKILRY LDNGTEAEKK IKTVCIGGVN ASNVQRITHQ LLAPTPLNRT PKTIDGIAVV SAIVGSSNPK SASQHLSQLL HSPPPFTLHS TAPHFWHQNP SDELSSILHK ALQCTKAVKT KTPLSHNMTN LVVQNFAANV ALAIGASPIM ANYGLEAPDL ARLKGGLVVN MGTVTPDGLL NYAQAIAAYN AAGGPIVLDP VGAGATSIRR EAVKTLMSAG YFDLIKGNER EILTVAKTSG LEICLPSSTS EGHNQQRGVD SGTALLNLTQ RASLVAHLAA RERNIVLMTG ATDLISDGTR TYAISNGHEY LGLITGSGCT LGTTLSAYMA ANPADKLIAA VAGLLQFEIA AERAAGRETV KGPGTFVPVF LDELWGFGEG VVKGTEEGLG DVARVECMKD LGGDGLVKEV // ID E3XJK4_ECOLX Unreviewed; 211 AA. AC E3XJK4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EC236275_1144; OS Escherichia coli 2362-75. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670897; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2362-75; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUL01000050; EFR17915.1; -; Genomic_DNA. DR EnsemblBacteria; EFR17915; EFR17915; EC236275_1144. DR PATRIC; 44763499; VBIEscCol143135_1064. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23000 MW; CC43679342B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E3Y423_SHIFL Unreviewed; 211 AA. AC E3Y423; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SF2457T_2782; OS Shigella flexneri 2a str. 2457T. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=198215; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2457T; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUV01000046; EFS13083.1; -; Genomic_DNA. DR RefSeq; NP_838896.1; NC_004741.1. DR ProteinModelPortal; E3Y423; -. DR SMR; E3Y423; 10-208. DR EnsemblBacteria; EFS13083; EFS13083; SF2457T_2782. DR GeneID; 1079890; -. DR KEGG; sfx:S3670; -. DR PATRIC; 18709162; VBIShiFle31049_4015. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E3YCJ6_LISMN Unreviewed; 53 AA. AC E3YCJ6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 22-JAN-2014, entry version 10. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN ORFNames=NT04LM_0648; OS Listeria monocytogenes FSL F2-208. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=702458; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL F2-208; RX PubMed=21126366; DOI=10.1186/1471-2164-11-688; RA den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H., RA Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.; RT "Comparative genomics of the bacterial genus Listeria: Genome RT evolution is characterized by limited gene acquisition and limited RT gene loss."; RL BMC Genomics 11:688-688(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXE01000466; EFR85895.1; -; Genomic_DNA. DR EnsemblBacteria; EFR85895; EFR85895; NT04LM_0648. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. FT NON_TER 53 53 SQ SEQUENCE 53 AA; 5746 MW; 610E2D6FB9D04B13 CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERK // ID E3YLW8_9LIST Unreviewed; 214 AA. AC E3YLW8; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NT05LM_0482; OS Listeria marthii FSL S4-120. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=702457; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL S4-120; RX PubMed=21126366; DOI=10.1186/1471-2164-11-688; RA den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H., RA Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.; RT "Comparative genomics of the bacterial genus Listeria: Genome RT evolution is characterized by limited gene acquisition and limited RT gene loss."; RL BMC Genomics 11:688-688(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXF01000277; EFR88904.1; -; Genomic_DNA. DR EnsemblBacteria; EFR88904; EFR88904; NT05LM_0482. DR PATRIC; 44802332; VBILisMar157200_0591. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22330 MW; CD1E326C00C299B4 CRC64; MRAELAAYFI AGTQDVVRGT LPSVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ KLCAKYQVPF IINDDVALAL EIGADGIHVG QTDEAIRQVI ASCAGKMKIG LSVHSVSEAA EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GITIPIVGIG GINETNSTEV LAAGADGVSV ISAITRSEDC KSVIKQLKNP GSPS // ID E3YVI0_LISIO Unreviewed; 208 AA. AC E3YVI0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN ORFNames=NT07LI_0671; OS Listeria innocua FSL S4-378. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=702456; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL S4-378; RX PubMed=21126366; DOI=10.1186/1471-2164-11-688; RA den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H., RA Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.; RT "Comparative genomics of the bacterial genus Listeria: Genome RT evolution is characterized by limited gene acquisition and limited RT gene loss."; RL BMC Genomics 11:688-688(2010). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXG01000469; EFR92017.1; -; Genomic_DNA. DR EnsemblBacteria; EFR92017; EFR92017; NT07LI_0671. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT NON_TER 208 208 SQ SEQUENCE 208 AA; 21982 MW; D4573F2210469F38 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK AGITCFQYRE KVAGSLQTAS ERKEMALECQ QLCAKFQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAA EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSEDC QIIINKLK // ID E3Z4A5_LISIO Unreviewed; 214 AA. AC E3Z4A5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NT06LI_0431; OS Listeria innocua FSL J1-023. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=702455; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL J1-023; RX PubMed=21126366; DOI=10.1186/1471-2164-11-688; RA den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H., RA Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.; RT "Comparative genomics of the bacterial genus Listeria: Genome RT evolution is characterized by limited gene acquisition and limited RT gene loss."; RL BMC Genomics 11:688-688(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXH01000236; EFR95073.1; -; Genomic_DNA. DR EnsemblBacteria; EFR95073; EFR95073; NT06LI_0431. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22605 MW; 5F71D9A6723A84A0 CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVRLAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVNEAA EAERLGAMDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GSPS // ID E3ZCR6_LISIV Unreviewed; 214 AA. AC E3ZCR6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NT05LI_0395; OS Listeria ivanovii FSL F6-596. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=702454; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL F6-596; RX PubMed=21126366; DOI=10.1186/1471-2164-11-688; RA den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H., RA Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.; RT "Comparative genomics of the bacterial genus Listeria: Genome RT evolution is characterized by limited gene acquisition and limited RT gene loss."; RL BMC Genomics 11:688-688(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXI01000236; EFR98245.1; -; Genomic_DNA. DR EnsemblBacteria; EFR98245; EFR98245; NT05LI_0395. DR PATRIC; 44807614; VBILisIva154985_1168. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22861 MW; 3F4D9EB2065A964D CRC64; MRGALAVYFI AGTQDIVRGN LPWVLEQALI AGITCFQYRE KGARSLQSKD ERKEMALTCQ QLCQEYQVPF IVNDDVTLAL EIGADGIHVG QDDEEILEVI RRVAGKMKIG LSVHSVSEAE EAVRLGAIDY IGVGPIFPTI SKDDAEPVSG AGILEEIRRA GIAIPIVGIG GINEANCAEV LVAGADGVSV ISAITRSDNC QATIQNLKNL RSAN // ID E3ZLZ6_LISSE Unreviewed; 214 AA. AC E3ZLZ6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NT03LS_0440; OS Listeria seeligeri FSL N1-067. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=702453; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL N1-067; RX PubMed=21126366; DOI=10.1186/1471-2164-11-688; RA den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H., RA Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.; RT "Comparative genomics of the bacterial genus Listeria: Genome RT evolution is characterized by limited gene acquisition and limited RT gene loss."; RL BMC Genomics 11:688-688(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXJ01000180; EFS01357.1; -; Genomic_DNA. DR EnsemblBacteria; EFS01357; EFS01357; NT03LS_0440. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22887 MW; 3F5BF262065A964D CRC64; MRGALAVYFI AGTQDIVRGN LPWVLEQALI AGITCFQYRE KGARSLQSKD ERKEMALTCQ QLCQEYQVPF IVNDDVTLAL EIGADGIHVG QDDEEILEVI RRVAGKMKIG LSVHSVSEAE EAVRLGAIDY IGVGPIFPTI SKDDAEPVSG AGILEEIRRA GIAIPIVGIG GINEANCAEV LVAGADGVSV ISAITRLDNC QATIQNLKNL RSAN // ID E3ZVU5_LISSE Unreviewed; 214 AA. AC E3ZVU5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NT04LS_0388; OS Listeria seeligeri FSL S4-171. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=702452; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL S4-171; RX PubMed=21126366; DOI=10.1186/1471-2164-11-688; RA den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H., RA Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.; RT "Comparative genomics of the bacterial genus Listeria: Genome RT evolution is characterized by limited gene acquisition and limited RT gene loss."; RL BMC Genomics 11:688-688(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXK01000221; EFS04432.1; -; Genomic_DNA. DR EnsemblBacteria; EFS04432; EFS04432; NT04LS_0388. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22959 MW; D2ED290C3EB83665 CRC64; MRGALAVYFI AGTQDIVRGN LPWVLEQALI AGITCFQYRE KGARSLQSKD ERKEMALTCQ QLCQEYQVPF IVNDDVTLAL EIGADGIHVG QDDEEILEVI RRVAEKMKIG LSVHSVSEAE EAVRLGAIDY IGVGPIFPTI SKDDAEPVSG AGILEEIRRA GIAIPIVGIG GINEANCAEV LVAGADGVSV ISAITRLDNC QATIQNLKNL RSAN // ID E4A583_PROAA Unreviewed; 217 AA. AC E4A583; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9573_00535; OS Propionibacterium acnes HL072PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765075; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL072PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXR01000011; EFT24225.1; -; Genomic_DNA. DR ProteinModelPortal; E4A583; -. DR EnsemblBacteria; EFT24225; EFT24225; HMPREF9573_00535. DR PATRIC; 51982608; VBIProAcn160582_0499. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4AA26_PROAA Unreviewed; 216 AA. AC E4AA26; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9573_02377; OS Propionibacterium acnes HL072PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765075; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL072PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXR01000071; EFT22453.1; -; Genomic_DNA. DR ProteinModelPortal; E4AA26; -. DR EnsemblBacteria; EFT22453; EFT22453; HMPREF9573_02377. DR PATRIC; 51986202; VBIProAcn160582_2207. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4ADV2_PROAA Unreviewed; 226 AA. AC E4ADV2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9622_01068; OS Propionibacterium acnes HL037PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765124; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL037PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXV01000025; EFT15819.1; -; Genomic_DNA. DR EnsemblBacteria; EFT15819; EFT15819; HMPREF9622_01068. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 151 153 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23534 MW; D9305CDB7DA17FDE CRC64; MKSARGEGFA MSRPEFDLSV YLVTDTAQCG GPDGVVETVR RAIVGGVTLV QFRDHDLSDD EFVTLGRRVR DACISGGVPL IIDDRVHLVA EIGADGAHVG QSDMPVDQAR AVLGDDLLIG LSAQAPVHVK AALSHGRDVI DYLGVGALHG TGTKPEAEEL GLAGICDVVN ASPWPVCVIG GVSASDAPYV SRMGCDGLSV VSAICGSTDP ESSARELAEA WRRAKE // ID E4AIW1_PROAA Unreviewed; 214 AA. AC E4AIW1; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9622_02855; OS Propionibacterium acnes HL037PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765124; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL037PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXV01000069; EFT14088.1; -; Genomic_DNA. DR EnsemblBacteria; EFT14088; EFT14088; HMPREF9622_02855. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 214 AA; 22005 MW; B66EC551F31299E4 CRC64; MTLDLRCYLV TSGTDHRTVE TAASAAAAGA GMVQVRAKDV STRDSLGLVL QVGEAVRRAN SATRVVVDDR ADVAWAAMRA HGNVHGVHVG SADLPVRDAR AILGPDAIVG YTTGTLDLVR SVEPFADALD YVGAGPFRPT PTKDSGRVPL GVQGYPELVA ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVIQA FDRV // ID E4AKF3_PROAA Unreviewed; 217 AA. AC E4AKF3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9613_00503; OS Propionibacterium acnes HL002PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765115; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL002PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXW01000010; EFT03383.1; -; Genomic_DNA. DR ProteinModelPortal; E4AKF3; -. DR EnsemblBacteria; EFT03383; EFT03383; HMPREF9613_00503. DR PATRIC; 52002840; VBIProAcn162097_0474. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4AN37_PROAA Unreviewed; 216 AA. AC E4AN37; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9613_01452; OS Propionibacterium acnes HL002PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765115; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL002PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXW01000027; EFT02396.1; -; Genomic_DNA. DR ProteinModelPortal; E4AN37; -. DR EnsemblBacteria; EFT02396; EFT02396; HMPREF9613_01452. DR PATRIC; 52004717; VBIProAcn162097_1375. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4AU51_PROAA Unreviewed; 216 AA. AC E4AU51; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9609_01069; OS Propionibacterium acnes HL027PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765111; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL027PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXX01000066; EFT00210.1; -; Genomic_DNA. DR ProteinModelPortal; E4AU51; -. DR EnsemblBacteria; EFT00210; EFT00210; HMPREF9609_01069. DR PATRIC; 52008972; VBIProAcn162038_0966. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4AW32_PROAA Unreviewed; 201 AA. AC E4AW32; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; DE Flags: Fragment; GN Name=thiE; ORFNames=HMPREF9609_01760; OS Propionibacterium acnes HL027PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765111; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL027PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXX01000080; EFS99488.1; -; Genomic_DNA. DR EnsemblBacteria; EFS99488; EFS99488; HMPREF9609_01760. DR PATRIC; 52010284; VBIProAcn162038_1598. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Transferase. FT NON_TER 1 1 SQ SEQUENCE 201 AA; 20576 MW; 0E8B20690F5631D7 CRC64; HTIETAAAAA GAGAGMVQVR AKELSTRDLL SLVLQVGEAV RRANPATRVV VDDRADVAWA AIRARGNVHG VHVGLTDLPV RDARAMLGPD AIVGYTTGTL DLVRSAEPFA DALDYVGAGP FRPTPTKESG RSPLGVQGYP ALVGASSLPV VAIGDVQVAD VPVLAAPGVA GVAMVRAIMA SDDPAAVVRQ VVQSFDEVRV S // ID E4B0M1_PROAA Unreviewed; 217 AA. AC E4B0M1; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9606_00709; OS Propionibacterium acnes HL036PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765108; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL036PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXY01000015; EFS90281.1; -; Genomic_DNA. DR ProteinModelPortal; E4B0M1; -. DR EnsemblBacteria; EFS90281; EFS90281; HMPREF9606_00709. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4B3M1_PROAA Unreviewed; 216 AA. AC E4B3M1; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9606_01766; OS Propionibacterium acnes HL036PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765108; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL036PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXY01000050; EFS89233.1; -; Genomic_DNA. DR ProteinModelPortal; E4B3M1; -. DR EnsemblBacteria; EFS89233; EFS89233; HMPREF9606_01766. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4B780_PROAA Unreviewed; 217 AA. AC E4B780; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9577_00483; OS Propionibacterium acnes HL110PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765079; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL110PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYG01000028; EFT26769.1; -; Genomic_DNA. DR ProteinModelPortal; E4B780; -. DR EnsemblBacteria; EFT26769; EFT26769; HMPREF9577_00483. DR PATRIC; 52043724; VBIProAcn164130_0424. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22508 MW; 6BD5C5023BD76D6C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRFPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRTIMASDDP AAVVRQVVQS FDEVRVS // ID E4BC80_PROAA Unreviewed; 216 AA. AC E4BC80; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9577_02224; OS Propionibacterium acnes HL110PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765079; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL110PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYG01000074; EFT25356.1; -; Genomic_DNA. DR ProteinModelPortal; E4BC80; -. DR EnsemblBacteria; EFT25356; EFT25356; HMPREF9577_02224. DR PATRIC; 52047063; VBIProAcn164130_2013. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22548 MW; D68AAF1B366F1623 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAGMRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4BFJ7_PROAA Unreviewed; 226 AA. AC E4BFJ7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9621_00683; OS Propionibacterium acnes HL037PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765123; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL037PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYH01000020; EFS75051.1; -; Genomic_DNA. DR EnsemblBacteria; EFS75051; EFS75051; HMPREF9621_00683. DR PATRIC; 52049260; VBIProAcn164498_0630. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 151 153 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23534 MW; D9305CDB7DA17FDE CRC64; MKSARGEGFA MSRPEFDLSV YLVTDTAQCG GPDGVVETVR RAIVGGVTLV QFRDHDLSDD EFVTLGRRVR DACISGGVPL IIDDRVHLVA EIGADGAHVG QSDMPVDQAR AVLGDDLLIG LSAQAPVHVK AALSHGRDVI DYLGVGALHG TGTKPEAEEL GLAGICDVVN ASPWPVCVIG GVSASDAPYV SRMGCDGLSV VSAICGSTDP ESSARELAEA WRRAKE // ID E4BKX3_PROAA Unreviewed; 214 AA. AC E4BKX3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9621_02662; OS Propionibacterium acnes HL037PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765123; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL037PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYH01000049; EFS73053.1; -; Genomic_DNA. DR EnsemblBacteria; EFS73053; EFS73053; HMPREF9621_02662. DR PATRIC; 52053130; VBIProAcn164498_2461. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 214 AA; 22005 MW; B66EC551F31299E4 CRC64; MTLDLRCYLV TSGTDHRTVE TAASAAAAGA GMVQVRAKDV STRDSLGLVL QVGEAVRRAN SATRVVVDDR ADVAWAAMRA HGNVHGVHVG SADLPVRDAR AILGPDAIVG YTTGTLDLVR SVEPFADALD YVGAGPFRPT PTKDSGRVPL GVQGYPELVA ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVIQA FDRV // ID E4BPR6_PROAA Unreviewed; 216 AA. AC E4BPR6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9617_01118; OS Propionibacterium acnes HL056PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765119; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL056PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYI01000015; EFS71718.1; -; Genomic_DNA. DR EnsemblBacteria; EFS71718; EFS71718; HMPREF9617_01118. DR PATRIC; 52055791; VBIProAcn160441_1046. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22628 MW; CC3F100B367E1034 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALYG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4BT28_PROAA Unreviewed; 217 AA. AC E4BT28; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9617_02306; OS Propionibacterium acnes HL056PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765119; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL056PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYI01000041; EFS70600.1; -; Genomic_DNA. DR ProteinModelPortal; E4BT28; -. DR EnsemblBacteria; EFS70600; EFS70600; HMPREF9617_02306. DR PATRIC; 52058112; VBIProAcn160441_2154. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4BUP4_PROAA Unreviewed; 217 AA. AC E4BUP4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9616_00301; OS Propionibacterium acnes HL007PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765118; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL007PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYJ01000005; EFS69793.1; -; Genomic_DNA. DR ProteinModelPortal; E4BUP4; -. DR EnsemblBacteria; EFS69793; EFS69793; HMPREF9616_00301. DR PATRIC; 52059205; VBIProAcn164462_0270. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4BZ50_PROAA Unreviewed; 216 AA. AC E4BZ50; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9616_01893; OS Propionibacterium acnes HL007PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765118; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL007PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYJ01000025; EFS68499.1; -; Genomic_DNA. DR EnsemblBacteria; EFS68499; EFS68499; HMPREF9616_01893. DR PATRIC; 52062264; VBIProAcn164462_1730. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22628 MW; CC3F100B367E1034 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALYG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4C2S3_PROAA Unreviewed; 217 AA. AC E4C2S3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9611_00614; OS Propionibacterium acnes HL063PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765113; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL063PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYK01000007; EFS64030.1; -; Genomic_DNA. DR ProteinModelPortal; E4C2S3; -. DR EnsemblBacteria; EFS64030; EFS64030; HMPREF9611_00614. DR PATRIC; 52065030; VBIProAcn161660_0578. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4C733_PROAA Unreviewed; 216 AA. AC E4C733; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9611_01784; OS Propionibacterium acnes HL063PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765113; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL063PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYK01000018; EFS62768.1; -; Genomic_DNA. DR ProteinModelPortal; E4C733; -. DR EnsemblBacteria; EFS62768; EFS62768; HMPREF9611_01784. DR PATRIC; 52067362; VBIProAcn161660_1696. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4CAH0_PROAA Unreviewed; 217 AA. AC E4CAH0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9604_00731; OS Propionibacterium acnes HL036PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765106; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL036PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYL01000003; EFS59122.1; -; Genomic_DNA. DR ProteinModelPortal; E4CAH0; -. DR EnsemblBacteria; EFS59122; EFS59122; HMPREF9604_00731. DR PATRIC; 52070258; VBIProAcn162879_0682. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4CEV1_PROAA Unreviewed; 216 AA. AC E4CEV1; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9604_01792; OS Propionibacterium acnes HL036PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765106; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL036PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYL01000016; EFS57888.1; -; Genomic_DNA. DR ProteinModelPortal; E4CEV1; -. DR EnsemblBacteria; EFS57888; EFS57888; HMPREF9604_01792. DR PATRIC; 52072308; VBIProAcn162879_1667. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4CI46_PROAA Unreviewed; 217 AA. AC E4CI46; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9591_00886; OS Propionibacterium acnes HL086PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765093; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL086PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYP01000007; EFS77460.1; -; Genomic_DNA. DR ProteinModelPortal; E4CI46; -. DR EnsemblBacteria; EFS77460; EFS77460; HMPREF9591_00886. DR PATRIC; 52090832; VBIProAcn163957_0837. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4CK29_PROAA Unreviewed; 216 AA. AC E4CK29; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9591_01683; OS Propionibacterium acnes HL086PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765093; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL086PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYP01000020; EFS76296.1; -; Genomic_DNA. DR EnsemblBacteria; EFS76296; EFS76296; HMPREF9591_01683. DR PATRIC; 52092430; VBIProAcn163957_1605. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22636 MW; 0B272CF11EC99A01 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG FSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4CPH4_PROAA Unreviewed; 217 AA. AC E4CPH4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9587_00489; OS Propionibacterium acnes HL025PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765089; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL025PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYQ01000004; EFS51814.1; -; Genomic_DNA. DR EnsemblBacteria; EFS51814; EFS51814; HMPREF9587_00489. DR PATRIC; 52095227; VBIProAcn164189_0466. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22390 MW; E5AE81023BCB1FFC CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4CSL5_PROAA Unreviewed; 216 AA. AC E4CSL5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9587_01904; OS Propionibacterium acnes HL025PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765089; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL025PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYQ01000017; EFS50804.1; -; Genomic_DNA. DR ProteinModelPortal; E4CSL5; -. DR EnsemblBacteria; EFS50804; EFS50804; HMPREF9587_01904. DR PATRIC; 52098030; VBIProAcn164189_1817. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4CXS2_PROAA Unreviewed; 217 AA. AC E4CXS2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9612_00931; OS Propionibacterium acnes HL063PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765114; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL063PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYS01000020; EFS66595.1; -; Genomic_DNA. DR ProteinModelPortal; E4CXS2; -. DR EnsemblBacteria; EFS66595; EFS66595; HMPREF9612_00931. DR PATRIC; 52106184; VBIProAcn160968_0849. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4D0Y5_PROAA Unreviewed; 216 AA. AC E4D0Y5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9612_02059; OS Propionibacterium acnes HL063PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765114; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL063PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYS01000037; EFS65665.1; -; Genomic_DNA. DR EnsemblBacteria; EFS65665; EFS65665; HMPREF9612_02059. DR PATRIC; 52108357; VBIProAcn160968_1892. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22572 MW; 68DE5AAB2FB1D32B CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVVTVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4D381_PROAA Unreviewed; 217 AA. AC E4D381; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9605_00217; OS Propionibacterium acnes HL036PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765107; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL036PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYU01000001; EFS62361.1; -; Genomic_DNA. DR ProteinModelPortal; E4D381; -. DR EnsemblBacteria; EFS62361; EFS62361; HMPREF9605_00217. DR PATRIC; 52114921; VBIProAcn161340_0200. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4D8K0_PROAA Unreviewed; 216 AA. AC E4D8K0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9605_02128; OS Propionibacterium acnes HL036PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765107; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL036PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYU01000021; EFS60732.1; -; Genomic_DNA. DR ProteinModelPortal; E4D8K0; -. DR EnsemblBacteria; EFS60732; EFS60732; HMPREF9605_02128. DR PATRIC; 52118644; VBIProAcn161340_1982. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4DCU0_PROAA Unreviewed; 216 AA. AC E4DCU0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9593_01090; OS Propionibacterium acnes HL046PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765095; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL046PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYV01000051; EFS56126.1; -; Genomic_DNA. DR ProteinModelPortal; E4DCU0; -. DR EnsemblBacteria; EFS56126; EFS56126; HMPREF9593_01090. DR PATRIC; 52121629; VBIProAcn160200_0996. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4DFS6_PROAA Unreviewed; 217 AA. AC E4DFS6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9593_02140; OS Propionibacterium acnes HL046PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765095; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL046PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYV01000072; EFS55479.1; -; Genomic_DNA. DR ProteinModelPortal; E4DFS6; -. DR EnsemblBacteria; EFS55479; EFS55479; HMPREF9593_02140. DR PATRIC; 52123685; VBIProAcn160200_1983. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4DK13_PROAA Unreviewed; 216 AA. AC E4DK13; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9589_01301; OS Propionibacterium acnes HL059PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765091; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL059PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYW01000018; EFS53860.1; -; Genomic_DNA. DR ProteinModelPortal; E4DK13; -. DR EnsemblBacteria; EFS53860; EFS53860; HMPREF9589_01301. DR PATRIC; 52127205; VBIProAcn162008_1221. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4DLX2_PROAA Unreviewed; 217 AA. AC E4DLX2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9589_01684; OS Propionibacterium acnes HL059PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765091; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL059PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYW01000023; EFS53255.1; -; Genomic_DNA. DR EnsemblBacteria; EFS53255; EFS53255; HMPREF9589_01684. DR PATRIC; 52127963; VBIProAcn162008_1586. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22404 MW; 9A94D047D4950F06 CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGDAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4DTL5_PROAA Unreviewed; 216 AA. AC E4DTL5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9580_01186; OS Propionibacterium acnes HL087PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765082; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL087PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYX01000016; EFS45851.1; -; Genomic_DNA. DR ProteinModelPortal; E4DTL5; -. DR EnsemblBacteria; EFS45851; EFS45851; HMPREF9580_01186. DR PATRIC; 52132001; VBIProAcn162489_1120. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4DUY5_PROAA Unreviewed; 217 AA. AC E4DUY5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9580_01994; OS Propionibacterium acnes HL087PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765082; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL087PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYX01000020; EFS45480.1; -; Genomic_DNA. DR ProteinModelPortal; E4DUY5; -. DR EnsemblBacteria; EFS45480; EFS45480; HMPREF9580_01994. DR PATRIC; 52133564; VBIProAcn162489_1876. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4DWV3_PROAA Unreviewed; 217 AA. AC E4DWV3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9576_00107; OS Propionibacterium acnes HL110PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765078; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL110PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYY01000001; EFS44628.1; -; Genomic_DNA. DR EnsemblBacteria; EFS44628; EFS44628; HMPREF9576_00107. DR PATRIC; 52134874; VBIProAcn161395_0098. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22395 MW; B564C189E7C2A32B CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVN // ID E4E0V9_PROAA Unreviewed; 216 AA. AC E4E0V9; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9576_01542; OS Propionibacterium acnes HL110PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765078; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL110PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYY01000016; EFS42986.1; -; Genomic_DNA. DR ProteinModelPortal; E4E0V9; -. DR EnsemblBacteria; EFS42986; EFS42986; HMPREF9576_01542. DR PATRIC; 52137686; VBIProAcn161395_1446. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4E7I1_PROAA Unreviewed; 216 AA. AC E4E7I1; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9574_01298; OS Propionibacterium acnes HL074PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765076; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL074PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYZ01000049; EFS38318.1; -; Genomic_DNA. DR EnsemblBacteria; EFS38318; EFS38318; HMPREF9574_01298. DR PATRIC; 52142308; VBIProAcn163939_1182. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22628 MW; CC3F100B367E1034 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALYG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4EAR7_PROAA Unreviewed; 217 AA. AC E4EAR7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9574_02456; OS Propionibacterium acnes HL074PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765076; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL074PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYZ01000082; EFS37183.1; -; Genomic_DNA. DR ProteinModelPortal; E4EAR7; -. DR EnsemblBacteria; EFS37183; EFS37183; HMPREF9574_02456. DR PATRIC; 52144561; VBIProAcn163939_2260. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4ECR6_PROAA Unreviewed; 217 AA. AC E4ECR6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9566_00571; OS Propionibacterium acnes HL045PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765068; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL045PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZA01000003; EFT21829.1; -; Genomic_DNA. DR ProteinModelPortal; E4ECR6; -. DR EnsemblBacteria; EFT21829; EFT21829; HMPREF9566_00571. DR PATRIC; 52146066; VBIProAcn163430_0533. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4EGT0_PROAA Unreviewed; 216 AA. AC E4EGT0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9566_01903; OS Propionibacterium acnes HL045PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765068; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL045PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZA01000025; EFT19978.1; -; Genomic_DNA. DR EnsemblBacteria; EFT19978; EFT19978; HMPREF9566_01903. DR PATRIC; 52148612; VBIProAcn163430_1745. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22628 MW; CC3F100B367E1034 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALYG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4EJZ4_PROAA Unreviewed; 217 AA. AC E4EJZ4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9585_00379; OS Propionibacterium acnes HL083PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765087; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL083PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZC01000006; EFS49605.1; -; Genomic_DNA. DR ProteinModelPortal; E4EJZ4; -. DR EnsemblBacteria; EFS49605; EFS49605; HMPREF9585_00379. DR PATRIC; 52155991; VBIProAcn162598_0344. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4EPK9_PROAA Unreviewed; 216 AA. AC E4EPK9; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9585_02023; OS Propionibacterium acnes HL083PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765087; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL083PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZC01000028; EFS47594.1; -; Genomic_DNA. DR ProteinModelPortal; E4EPK9; -. DR EnsemblBacteria; EFS47594; EFS47594; HMPREF9585_02023. DR PATRIC; 52159248; VBIProAcn162598_1905. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4ERX7_PROAA Unreviewed; 217 AA. AC E4ERX7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9564_00281; OS Propionibacterium acnes HL053PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765066; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL053PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZD01000001; EFT19415.1; -; Genomic_DNA. DR ProteinModelPortal; E4ERX7; -. DR EnsemblBacteria; EFT19415; EFT19415; HMPREF9564_00281. DR PATRIC; 52160876; VBIProAcn162000_0268. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4EWH5_PROAA Unreviewed; 216 AA. AC E4EWH5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9564_01915; OS Propionibacterium acnes HL053PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765066; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL053PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZD01000027; EFT17307.1; -; Genomic_DNA. DR EnsemblBacteria; EFT17307; EFT17307; HMPREF9564_01915. DR PATRIC; 52164082; VBIProAcn162000_1799. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22628 MW; CC3F100B367E1034 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALYG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4F2I6_PROAA Unreviewed; 217 AA. AC E4F2I6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9575_01443; OS Propionibacterium acnes HL110PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765077; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL110PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZE01000022; EFS40864.1; -; Genomic_DNA. DR EnsemblBacteria; EFS40864; EFS40864; HMPREF9575_01443. DR PATRIC; 52168301; VBIProAcn163277_1334. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22394 MW; 79C3DA9FEA713D0E CRC64; MTLDLRCYLV TSGTGRHTVK TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVN // ID E4F4Q3_PROAA Unreviewed; 216 AA. AC E4F4Q3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9575_02290; OS Propionibacterium acnes HL110PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765077; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL110PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZE01000028; EFS40400.1; -; Genomic_DNA. DR ProteinModelPortal; E4F4Q3; -. DR EnsemblBacteria; EFS40400; EFS40400; HMPREF9575_02290. DR PATRIC; 52169903; VBIProAcn163277_2111. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4F7F2_PROAA Unreviewed; 217 AA. AC E4F7F2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9567_00535; OS Propionibacterium acnes HL013PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765069; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL013PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZH01000005; EFS36261.1; -; Genomic_DNA. DR ProteinModelPortal; E4F7F2; -. DR EnsemblBacteria; EFS36261; EFS36261; HMPREF9567_00535. DR PATRIC; 52182109; VBIProAcn160133_0486. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4F8I8_PROAA Unreviewed; 216 AA. AC E4F8I8; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9567_01460; OS Propionibacterium acnes HL013PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765069; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL013PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZH01000006; EFS35973.1; -; Genomic_DNA. DR ProteinModelPortal; E4F8I8; -. DR EnsemblBacteria; EFS35973; EFS35973; HMPREF9567_01460. DR PATRIC; 52183880; VBIProAcn160133_1343. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4FFC2_PROAA Unreviewed; 217 AA. AC E4FFC2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9620_00746; OS Propionibacterium acnes HL037PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765122; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL037PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZI01000009; EFT13364.1; -; Genomic_DNA. DR EnsemblBacteria; EFT13364; EFT13364; HMPREF9620_00746. DR PATRIC; 52187545; VBIProAcn162021_0684. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22405 MW; 88007D603CB803B1 CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGGGA GMVEVRAQEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4FIW8_PROAA Unreviewed; 216 AA. AC E4FIW8; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9620_02010; OS Propionibacterium acnes HL037PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765122; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL037PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZI01000029; EFT12067.1; -; Genomic_DNA. DR ProteinModelPortal; E4FIW8; -. DR EnsemblBacteria; EFT12067; EFT12067; HMPREF9620_02010. DR PATRIC; 52189978; VBIProAcn162021_1852. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4FMJ9_PROAA Unreviewed; 217 AA. AC E4FMJ9; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9618_00713; OS Propionibacterium acnes HL082PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765120; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL082PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZJ01000009; EFT08256.1; -; Genomic_DNA. DR EnsemblBacteria; EFT08256; EFT08256; HMPREF9618_00713. DR PATRIC; 52192499; VBIProAcn161122_0660. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22353 MW; BEC5CA235C63A33A CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMGQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVN // ID E4FQZ3_PROAA Unreviewed; 216 AA. AC E4FQZ3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9618_02289; OS Propionibacterium acnes HL082PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765120; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL082PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZJ01000025; EFT07058.1; -; Genomic_DNA. DR ProteinModelPortal; E4FQZ3; -. DR EnsemblBacteria; EFT07058; EFT07058; HMPREF9618_02289. DR PATRIC; 52195542; VBIProAcn161122_2116. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4FTM0_PROAA Unreviewed; 217 AA. AC E4FTM0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9600_00225; OS Propionibacterium acnes HL050PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765102; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL050PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZK01000002; EFS85771.1; -; Genomic_DNA. DR ProteinModelPortal; E4FTM0; -. DR EnsemblBacteria; EFS85771; EFS85771; HMPREF9600_00225. DR PATRIC; 52196671; VBIProAcn163404_0211. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4FYA7_PROAA Unreviewed; 216 AA. AC E4FYA7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9600_01758; OS Propionibacterium acnes HL050PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765102; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL050PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZK01000021; EFS83761.1; -; Genomic_DNA. DR ProteinModelPortal; E4FYA7; -. DR EnsemblBacteria; EFS83761; EFS83761; HMPREF9600_01758. DR PATRIC; 52199633; VBIProAcn163404_1625. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4G358_PROAA Unreviewed; 216 AA. AC E4G358; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9598_01082; OS Propionibacterium acnes HL050PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765100; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL050PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZL01000023; EFS82272.1; -; Genomic_DNA. DR ProteinModelPortal; E4G358; -. DR EnsemblBacteria; EFS82272; EFS82272; HMPREF9598_01082. DR PATRIC; 52203318; VBIProAcn163241_0993. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4G659_PROAA Unreviewed; 217 AA. AC E4G659; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9598_02147; OS Propionibacterium acnes HL050PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765100; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL050PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZL01000034; EFS81167.1; -; Genomic_DNA. DR ProteinModelPortal; E4G659; -. DR EnsemblBacteria; EFS81167; EFS81167; HMPREF9598_02147. DR PATRIC; 52205347; VBIProAcn163241_1973. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4G8T3_PROAA Unreviewed; 217 AA. AC E4G8T3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9596_00478; OS Propionibacterium acnes HL005PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765098; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL005PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZM01000005; EFT34611.1; -; Genomic_DNA. DR EnsemblBacteria; EFT34611; EFT34611; HMPREF9596_00478. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22350 MW; 81AFC189E7C2BDC9 CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQP FDEVRVS // ID E4GBS0_PROAA Unreviewed; 216 AA. AC E4GBS0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9596_01353; OS Propionibacterium acnes HL005PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765098; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL005PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZM01000008; EFT34173.1; -; Genomic_DNA. DR ProteinModelPortal; E4GBS0; -. DR EnsemblBacteria; EFT34173; EFT34173; HMPREF9596_01353. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4GHB7_PROAA Unreviewed; 216 AA. AC E4GHB7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9595_00753; OS Propionibacterium acnes HL005PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765097; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL005PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZN01000009; EFT31689.1; -; Genomic_DNA. DR ProteinModelPortal; E4GHB7; -. DR EnsemblBacteria; EFT31689; EFT31689; HMPREF9595_00753. DR PATRIC; 52207730; VBIProAcn164441_0697. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4GIS0_PROAA Unreviewed; 217 AA. AC E4GIS0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9595_01434; OS Propionibacterium acnes HL005PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765097; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL005PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZN01000016; EFT31078.1; -; Genomic_DNA. DR EnsemblBacteria; EFT31078; EFT31078; HMPREF9595_01434. DR PATRIC; 52209019; VBIProAcn164441_1318. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22350 MW; 81AFC189E7C2BDC9 CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQP FDEVRVS // ID E4GNY5_PROAA Unreviewed; 217 AA. AC E4GNY5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9594_00651; OS Propionibacterium acnes HL005PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765096; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL005PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZP01000015; EFT29383.1; -; Genomic_DNA. DR ProteinModelPortal; E4GNY5; -. DR EnsemblBacteria; EFT29383; EFT29383; HMPREF9594_00651. DR PATRIC; 52212561; VBIProAcn162628_0586. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4GTM8_PROAA Unreviewed; 216 AA. AC E4GTM8; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9594_02326; OS Propionibacterium acnes HL005PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765096; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL005PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZP01000076; EFT27673.1; -; Genomic_DNA. DR EnsemblBacteria; EFT27673; EFT27673; HMPREF9594_02326. DR PATRIC; 52215834; VBIProAcn162628_2135. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22628 MW; CC3F100B367E1034 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALYG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4GWD5_PROAA Unreviewed; 216 AA. AC E4GWD5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9619_00880; OS Propionibacterium acnes HL082PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765121; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL082PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZR01000020; EFT11019.1; -; Genomic_DNA. DR ProteinModelPortal; E4GWD5; -. DR EnsemblBacteria; EFT11019; EFT11019; HMPREF9619_00880. DR PATRIC; 52223274; VBIProAcn162481_0809. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22548 MW; D68AAF1B366F1623 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAGMRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4GZT5_PROAA Unreviewed; 217 AA. AC E4GZT5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9619_01842; OS Propionibacterium acnes HL082PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765121; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL082PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZR01000039; EFT09618.1; -; Genomic_DNA. DR ProteinModelPortal; E4GZT5; -. DR EnsemblBacteria; EFT09618; EFT09618; HMPREF9619_01842. DR PATRIC; 52225181; VBIProAcn162481_1716. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4H412_PROAA Unreviewed; 217 AA. AC E4H412; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9614_00764; OS Propionibacterium acnes HL002PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765116; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL002PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZS01000012; EFT05554.1; -; Genomic_DNA. DR ProteinModelPortal; E4H412; -. DR EnsemblBacteria; EFT05554; EFT05554; HMPREF9614_00764. DR PATRIC; 52228121; VBIProAcn163701_0696. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4H813_PROAA Unreviewed; 216 AA. AC E4H813; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9614_02235; OS Propionibacterium acnes HL002PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765116; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL002PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZS01000030; EFT04254.1; -; Genomic_DNA. DR ProteinModelPortal; E4H813; -. DR EnsemblBacteria; EFT04254; EFT04254; HMPREF9614_02235. DR PATRIC; 52230993; VBIProAcn163701_2074. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4HAP2_PROAA Unreviewed; 216 AA. AC E4HAP2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9608_00619; OS Propionibacterium acnes HL067PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765110; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL067PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZT01000012; EFS95775.1; -; Genomic_DNA. DR ProteinModelPortal; E4HAP2; -. DR EnsemblBacteria; EFS95775; EFS95775; HMPREF9608_00619. DR PATRIC; 52232909; VBIProAcn160320_0589. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4HDX4_PROAA Unreviewed; 217 AA. AC E4HDX4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9608_01702; OS Propionibacterium acnes HL067PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765110; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL067PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZT01000030; EFS94626.1; -; Genomic_DNA. DR ProteinModelPortal; E4HDX4; -. DR EnsemblBacteria; EFS94626; EFS94626; HMPREF9608_01702. DR PATRIC; 52235022; VBIProAcn160320_1593. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4HLE6_PROAA Unreviewed; 214 AA. AC E4HLE6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9607_01751; OS Propionibacterium acnes HL044PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765109; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL044PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZU01000028; EFS92122.1; -; Genomic_DNA. DR EnsemblBacteria; EFS92122; EFS92122; HMPREF9607_01751. DR PATRIC; 52240323; VBIProAcn160378_1645. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 214 AA; 22005 MW; B66EC551F31299E4 CRC64; MTLDLRCYLV TSGTDHRTVE TAASAAAAGA GMVQVRAKDV STRDSLGLVL QVGEAVRRAN SATRVVVDDR ADVAWAAMRA HGNVHGVHVG SADLPVRDAR AILGPDAIVG YTTGTLDLVR SVEPFADALD YVGAGPFRPT PTKDSGRVPL GVQGYPELVA ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVIQA FDRV // ID E4HM37_PROAA Unreviewed; 226 AA. AC E4HM37; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9607_01981; OS Propionibacterium acnes HL044PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765109; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL044PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZU01000033; EFS91820.1; -; Genomic_DNA. DR EnsemblBacteria; EFS91820; EFS91820; HMPREF9607_01981. DR PATRIC; 52240776; VBIProAcn160378_1860. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 151 153 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23534 MW; D9305CDB7DA17FDE CRC64; MKSARGEGFA MSRPEFDLSV YLVTDTAQCG GPDGVVETVR RAIVGGVTLV QFRDHDLSDD EFVTLGRRVR DACISGGVPL IIDDRVHLVA EIGADGAHVG QSDMPVDQAR AVLGDDLLIG LSAQAPVHVK AALSHGRDVI DYLGVGALHG TGTKPEAEEL GLAGICDVVN ASPWPVCVIG GVSASDAPYV SRMGCDGLSV VSAICGSTDP ESSARELAEA WRRAKE // ID E4HTR6_PROAA Unreviewed; 216 AA. AC E4HTR6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9603_01450; OS Propionibacterium acnes HL001PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765105; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL001PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZV01000033; EFS86982.1; -; Genomic_DNA. DR ProteinModelPortal; E4HTR6; -. DR EnsemblBacteria; EFS86982; EFS86982; HMPREF9603_01450. DR PATRIC; 52245435; VBIProAcn164464_1326. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22548 MW; D68AAF1B366F1623 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAGMRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4HVB6_PROAA Unreviewed; 217 AA. AC E4HVB6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9603_02004; OS Propionibacterium acnes HL001PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765105; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL001PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZV01000042; EFS86449.1; -; Genomic_DNA. DR EnsemblBacteria; EFS86449; EFS86449; HMPREF9603_02004. DR PATRIC; 52246532; VBIProAcn164464_1855. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22444 MW; 9A9A24188BCB0106 CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVYVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4HY98_PROAA Unreviewed; 217 AA. AC E4HY98; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9597_00640; OS Propionibacterium acnes HL005PA4. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765099; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL005PA4; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZW01000007; EFS80170.1; -; Genomic_DNA. DR ProteinModelPortal; E4HY98; -. DR EnsemblBacteria; EFS80170; EFS80170; HMPREF9597_00640. DR PATRIC; 52248951; VBIProAcn163821_0580. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E4I0V0_PROAA Unreviewed; 216 AA. AC E4I0V0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9597_01589; OS Propionibacterium acnes HL005PA4. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765099; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL005PA4; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZW01000015; EFS79434.1; -; Genomic_DNA. DR ProteinModelPortal; E4I0V0; -. DR EnsemblBacteria; EFS79434; EFS79434; HMPREF9597_01589. DR PATRIC; 52250772; VBIProAcn163821_1456. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E4KND2_9LACT Unreviewed; 211 AA. AC E4KND2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9257_0480; OS Eremococcus coleocola ACS-139-V-Col8. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Eremococcus. OX NCBI_TaxID=908337; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-139-V-Col8; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENN01000010; EFR31554.1; -; Genomic_DNA. DR EnsemblBacteria; EFR31554; EFR31554; HMPREF9257_0480. DR PATRIC; 45018524; VBIEreCol171777_0598. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22087 MW; 707334B94A8B419F CRC64; MKQISNPYRL YLVTDPTGLS ADGFLQVIDQ ACQAGVSLVQ LREKTATSRD LFQKAQAVKA ITDRYQIPLI IDDRLDICQA VGAAGLHVGD EDLPVEVARK ILGPDAIIGV SSKSLDAAQA AVAGGASYLG VGAIFPTKTK VKTQATSIET LKKITRTVPV PVVAIGGIKS HNLDQLTASG VAGVAMVSEI MQAPDVAGKV AELNQLLTQV L // ID E4KW99_9PORP Unreviewed; 673 AA. AC E4KW99; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF9294_1629; OS Porphyromonas asaccharolytica PR426713P-I. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=910312; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PR426713P-I; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENO01000057; EFR33873.1; -; Genomic_DNA. DR EnsemblBacteria; EFR33873; EFR33873; HMPREF9294_1629. DR PATRIC; 45024259; VBIPorAsa169717_1644. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 673 AA; 74564 MW; 3082E3E0D9360A45 CRC64; MIVITPPERQ YIEGLASDII DVASNCICKV HLRIPGASET DFRKVLDSLE PAYHQHIVLC DHYALLAEYD VAGVYLPYRR VAEWRDIPLA PHQTIAVGAH SLQELQELPF TPHYALLSPL FDSISKEGYQ GNPALLSCRE ELLKLPYPVY ALGGITPERQ ETVAKAGYAG VAVLGDIWSQ PQERRQERLD QYQTPAILSV AGHDPTSGAG IGVDTRIAND LSVQCYSVIS TLTAQSLHRF VSATATPSDQ LQTSLTTLLT DHPVTVAKLG MVPDLQQAVQ IVALMKALGV KRIIWDPILQ PTAAEETQTH LWTEEQDKLA TLLHEVSLVT PNKPEAQALF GTDDPAELQR IAQEHGVAIL LKGGHDTTSP HLVVNQLITR DGIYPFYTHR YDKSIHGTGC MLSAAIASYW AMEYSLVNSV QRACHYLATI FAEQPNRPGR QLLCSKIFRE DRKKQHLYAH FALQYVTNES DPDRLYNKVS QYLEAGGRWV QLRLKEATTE ERIEMGLRLR TLTDRYHACL LIDDDIIATI AVDADGVHLG KRDCPPQEAR RTLGDEYIIG YTVNSRDDLP RALAADIDYI GVGPYRDTQT KALLAPILGL EGISQIAQQV QETDRCYTTP QIVAIGGIQP EDAETLLSNE DIDGIAVSGA IEHATDMART ISQLQCGTSN YPR // ID E4KZ74_9FIRM Unreviewed; 462 AA. AC E4KZ74; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Putative hydroxyethylthiazole kinase; GN ORFNames=HMPREF9286_1279; OS Peptoniphilus harei ACS-146-V-Sch2b. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Peptoniphilus. OX NCBI_TaxID=908338; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-146-V-Sch2b; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENP01000020; EFR32841.1; -; Genomic_DNA. DR EnsemblBacteria; EFR32841; EFR32841; HMPREF9286_1279. DR PATRIC; 45026366; VBIPepHar169446_1016. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 462 AA; 50431 MW; FAC87B8B437DA485 CRC64; MKIKCDLKKL RDKAPLVHVI SNGVTRGRVA DFALSIGASP MMAEYSKEVS EIAKKASALV LNMGMLNEDK IEAIKIAAKT AKENNIPLIL DPVGVGSSKI RRDLAKYLLD NFKFNVIRGN FNEINYLAGG KASAGIDSRD KNLSEEDFIE LAIKVNEKTG ATLVISGKYE VIANSHMLIS IPGGHDSLRK ISGLGDMESA MIGSLLAAPM SNLKACAISA IFFRQLAREV IVDGSINAQD IISKIQRLDE ISGDIEILSP SYKFARPSLY GISDGNDLLK IKNAIRAGMK IYQLRDKASD EALLGEKILK LKKEIEETCL FILNDNLKLA KEYATSLHLG QDDEEISLAR KILGRDPIIG ATAKTSELAI EAENMGASYI GSGAFFETET KKDASTINLE RYKEIRDSVL IPAFPIGGIN KENLDLFKGE DIPGLCMSSG IFSLDENEVE KNVREIISKL NS // ID E4L7J9_9FIRM Unreviewed; 212 AA. AC E4L7J9; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9220_1232; OS Dialister microaerophilus UPII 345-E. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Dialister. OX NCBI_TaxID=910314; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UPII 345-E; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENT01000004; EFR43255.1; -; Genomic_DNA. DR EnsemblBacteria; EFR43255; EFR43255; HMPREF9220_1232. DR PATRIC; 45032471; VBIDiaMic169777_0188. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23577 MW; 6C6142A40F58F1FB CRC64; MKNNIDYTLY LVTDNHVSDF EKFCYKIEKA ICNGVTTVQL REKNLETNLF YKKALKVKEL TDKYNVPLII NDRIDIMLAI DAAGVHLGQF DMPADIARKI IGQNKILGIS ASNLTEAKKA YEDGADYLGV GAMFATQTKP DADVTSMKEL KKIRENVDIP IVVIGGINCK TIPLFSKIKV DGFAVVSAIM SEKDSGKASK DLIKEIQKVK IR // ID E4LE57_9FIRM Unreviewed; 505 AA. AC E4LE57; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF9199_0163; OS Veillonella sp. oral taxon 158 str. F0412. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=879309; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0412; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENU01000018; EFR60026.1; -; Genomic_DNA. DR EnsemblBacteria; EFR60026; EFR60026; HMPREF9199_0163. DR PATRIC; 45037371; VBIVeiSp174732_1171. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 505 AA; 54035 MW; 6C3DD8473A3454A5 CRC64; MTYENPYMNG QIWPELNILE ILRQRNPLVI CITNDVVRTF TANGLLAIGA SPVMSECSED LKDLIVHASA LLINIGTLTP DKVSYYKDAI ALAKKHEVPI VIDPVGCHAG AYRLSVVLDL IKTGEISLVR GNQSEIKAIY DALSPNNQAD TSTTGKGVDG GQIEDSAVIA YRLARLINCP VVATGEEDYV SDGTRVFAVP HGHPIMTAVT GTGCLLGAVL AAFFSAYYPC KNRLSIGEFL GYALAYYGLA GESAVQVSGV QPGSFSVAFM DSLYTLDDAV LMSENRIRPV VAPDQLQVYF IGGTQDVGLN ENRLLSVVED ACRGGVTCFQ FREKGAGTLV GKQKLELAQQ LKQICAKYNV LYVINDDVDL AMAVNADGVH VGQEDMRLEE VRNLVGHKVV GISIHSVEEL HKTDVIYADC VGVGPMYATS SKPDAQEPCG PNRITELQAE GLTLPCVGIG GITLDNAKPV LQAGACGVAV ISAIAHADSP YEAAQQFKHL FDGIK // ID E4LKQ6_9FIRM Unreviewed; 233 AA. AC E4LKQ6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9162_1925; OS Selenomonas sp. oral taxon 137 str. F0430. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=879310; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0430; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENV01000009; EFR40431.1; -; Genomic_DNA. DR EnsemblBacteria; EFR40431; EFR40431; HMPREF9162_1925. DR PATRIC; 45042288; VBISelSp169704_1571. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 208 209 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 24629 MW; 36329B751E9AA240 CRC64; MSMRKKFDLS AYLVIGPENT NGCPVARVIA EAVRADFTFV QIRSKTAEAR ELIDLTRAAA EIIAAQEKSE RVALVVNDRL DVALAARDAG IKVDGVHVGQ SDIPPEICRK YLGEDAVVGL SARTSALIDY VRACDTSCID YFGAGPLHPT ATKPDAGRDA AGHIVTRSLT ELSELHRVSP LPVVVGGGVK AGDLPALRAA GVEGFFVVSA VASVAHPFAA ADELVRTWRA ARS // ID E4LZ39_9CLOT Unreviewed; 209 AA. AC E4LZ39; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9406_3177; OS Clostridium sp. HGF2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=908340; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGF2; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENW01000056; EFR35964.1; -; Genomic_DNA. DR EnsemblBacteria; EFR35964; EFR35964; HMPREF9406_3177. DR PATRIC; 45051696; VBICloSp171430_3739. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22607 MW; 18EAD73688CED112 CRC64; MRFDLTLYLV SDSTGLSEDE FLRRLEQALR GGVTLLQLRE KNRTTLEYYE LARKVKKLTD AYGVPLMIDD RVDIALAVDA AGVHVGAEDM PVREARRLMG PDKIVGATAK RVDTAMQAEA DGADYLGVGA IYPTTTKVKT VLTSVETLQD ICAHVSILVG AIGGLNAENC EILKGTGIKG ICVVSAIMKQ ENSYDAAKAL KAKIMTICK // ID E4N9T7_KITSK Unreviewed; 215 AA. AC E4N9T7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=KSE_21450; OS Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC OS A-0304 / NBRC 14216 / KM-6054) (Streptomyces setae). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Kitasatospora. OX NCBI_TaxID=452652; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 / RC KM-6054; RX PubMed=21059706; DOI=10.1093/dnares/dsq026; RA Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y., RA Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S., RA Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T., RA Horinouchi S., Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A., RA Nomoto F., Miura H., Takahashi Y., Fujita N.; RT "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary RT snapshot of the family Streptomycetaceae."; RL DNA Res. 17:393-406(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010968; BAJ27968.1; -; Genomic_DNA. DR RefSeq; YP_004903924.1; NC_016109.1. DR ProteinModelPortal; E4N9T7; -. DR EnsemblBacteria; BAJ27968; BAJ27968; KSE_21450. DR GeneID; 11347110; -. DR KEGG; ksk:KSE_21450; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; KSET452652:GJFD-2132-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23125 MW; 09AD84069F2D3749 CRC64; MTAAPTARQR LADARLYLCT DARREQGDLP EFLDAVLGAG VDVVQLRDKG LEARQELEHL EVFADAARRH GKLLAVNDRA DVAYGARPDV LHLGQDDLPV AVARRILGDD VLIGRSCHAE SEVDTALTEP GVDYFCTGPV WPTPTKPGRP APGLDLVRYA AARRPERPWF AIGGIDQDNL QQVLDAGATR IVVVRALTAA EDPAAAAAAL AARLR // ID E4NUZ4_HALBP Unreviewed; 214 AA. AC E4NUZ4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Hbor_34620; ORFNames=C499_06640; OS Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM OS 10706 / PR3). OG Plasmid pHBOR02. OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halogeometricum. OX NCBI_TaxID=469382; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / PR3; RX PubMed=21304651; DOI=10.4056/sigs.23264; RA Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A., RA Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., RA Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., RA Anderson I., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., D'haeseleer P., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.; RT "Complete genome sequence of Halogeometricum borinquense type strain RT (PR3)."; RL Stand. Genomic Sci. 1:150-159(2009). RN [2] RP NUCLEOTIDE SEQUENCE. RC PLASMID=pHBOR02; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Mikhailova N., Anderson I., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindal B., Klenk H.-P., Eisen J.A.; RT "The complete plasmid2 of Halogeometricum borinquense DSM 11551."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 11551; RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., RA Darling A., Eisen J.A., Facciotti M.T.; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001692; ADQ68983.1; -; Genomic_DNA. DR EMBL; AOHT01000019; ELY29194.1; -; Genomic_DNA. DR RefSeq; YP_004038119.1; NC_014731.1. DR EnsemblBacteria; ADQ68983; ADQ68983; Hbor_34620. DR EnsemblBacteria; ELY29194; ELY29194; C499_06640. DR GeneID; 9988775; -. DR KEGG; hbo:Hbor_34620; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; HBOR469382:GCNS-3461-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Plasmid; KW Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22320 MW; 76A18B72C1E47B7F CRC64; MNIPMRTYLV TQGDRSRGRG TGSIVRAAIE GGVDIVQMRE KHTSARERYE LGKELRALTR EADIPFVVND RVDIAAAVDA DGVHLGDDDL PVSVARDHLG EEAIIGRSVS TPEAASEAER AGADYLGVGA VFATDTKDVN EGEAEIGTET IAEIAETVDI PIVGIGGINA DNATEVVNAG AAGVAVVTTI TDADDPAAAT QQLRQAVENG RTTV // ID E4P093_BIFBP Unreviewed; 918 AA. AC E4P093; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=ThiE/ThiC Thiamine biosynthesis protein; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=BBPR_0480; OS Bifidobacterium bifidum (strain PRL2010). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=702459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRL2010; RX PubMed=20974960; DOI=10.1073/pnas.1011100107; RA Turroni F., Bottacini F., Foroni E., Mulder I., Kim J.H., Zomer A., RA Sanchez B., Bidossi A., Ferrarini A., Giubellini V., Delledonne M., RA Henrissat B., Coutinho P., Oggioni M., Fitzgerald G.F., Mills D., RA Margolles A., Kelly D., van Sinderen D., Ventura M.; RT "Genome analysis of Bifidobacterium bifidum PRL2010 reveals metabolic RT pathways for host-derived glycan foraging."; RL Proc. Natl. Acad. Sci. U.S.A. 107:19514-19519(2010). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001840; ADP35587.1; -; Genomic_DNA. DR RefSeq; YP_003970624.1; NC_014638.1. DR EnsemblBacteria; ADP35587; ADP35587; BBPR_0480. DR GeneID; 9888641; -. DR KEGG; bbp:BBPR_0480; -. DR PATRIC; 42576588; VBIBifBif153886_0498. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR BioCyc; BBIF702459:GHBC-465-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Transferase; Zinc. SQ SEQUENCE 918 AA; 100181 MW; 5C46E21EA98CEAB2 CRC64; MSNEYPFASM RDSFDLSAYF VVGPQDCKDR PLTEVIDQAL HGGATFIQLR AKGADASELT EMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQSDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSSTK PEASVGGNDG SGKTLDAAQI NTICSASEFP VVVGGGVTAA DMAMLAGTKA AGWFAVSAIA GAEDPEAATR EMVSGWKAVR GDKRHGYAPR IVTHTPATDA QAAQEGSAAA GAEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF SYEYGSYDLE VPYTEIKLSD TPGVGPNAPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL QDDGKRAIKR GRATKEWRGR THQPMRAKDH PVTQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHGAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVA DAVTGKIPEG VETPANPVTD DTVVSANVLS PEEILAGMDA MGEKYRAQGG KLYSKASE // ID E4P5L8_ECO8N Unreviewed; 211 AA. AC E4P5L8; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NRG857_19925; OS Escherichia coli O83:H1 (strain NRG 857C / AIEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=685038; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRG 857C / AIEC; RX PubMed=21108814; DOI=10.1186/1471-2164-11-667; RA Nash J.H., Villegas A., Kropinski A.M., Aguilar-Valenzuela R., RA Konczy P., Mascarenhas M., Ziebell K., Torres A.G., Karmali M.A., RA Coombes B.K.; RT "Genome sequence of adherent-invasive Escherichia coli and comparative RT genomic analysis with other E. coli pathotypes."; RL BMC Genomics 11:667-667(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001855; ADR29394.1; -; Genomic_DNA. DR RefSeq; YP_006122328.1; NC_017634.1. DR ProteinModelPortal; E4P5L8; -. DR SMR; E4P5L8; 9-208. DR EnsemblBacteria; ADR29394; ADR29394; NRG857_19925. DR GeneID; 12876341; -. DR KEGG; eln:NRG857_19925; -. DR PATRIC; 45451917; VBIEscCol181005_4066. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E4PLV6_MARAH Unreviewed; 219 AA. AC E4PLV6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HP15_348; OS Marinobacter adhaerens (strain HP15). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=225937; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HP15; RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., RA Yarza P., Gloeckner F.O., Ullrich M.S.; RT "Complete genome sequence of Marinobacter adhaerens type strain RT (HP15)."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001978; ADP96112.1; -; Genomic_DNA. DR RefSeq; YP_005884040.1; NC_017506.1. DR EnsemblBacteria; ADP96112; ADP96112; HP15_348. DR GeneID; 12403827; -. DR KEGG; mad:HP15_348; -. DR PATRIC; 43112794; VBIMarBac104501_0342. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; MADH225937:GLG5-350-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22672 MW; 1D95E3F835EBA139 CRC64; MSKGLRPGLY AITDSVLTPP ETLIESVEAA LRGGAVMVQY REKSVPMAER ISQAVSLQAL CRNAGVPLLI NDDPDLAKRV GAAGVHMGQT DGSVAAARRL LGDEAIIGIT CHADLALAQA ALGAGADYLA FGRFYTSSTK PGAPAAPPGV LTDAKRFGLP ITAIGGVTTD NGEPLIRAGA DMLAVVGGLF GGDTHDIEMR AKAFERLFAS HHPLFSLPE // ID E4PP29_MARAH Unreviewed; 323 AA. AC E4PP29; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 13-NOV-2013, entry version 21. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=HP15_577; OS Marinobacter adhaerens (strain HP15). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=225937; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HP15; RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., RA Yarza P., Gloeckner F.O., Ullrich M.S.; RT "Complete genome sequence of Marinobacter adhaerens type strain RT (HP15)."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001978; ADP96341.1; -; Genomic_DNA. DR RefSeq; YP_005884269.1; NC_017506.1. DR ProteinModelPortal; E4PP29; -. DR EnsemblBacteria; ADP96341; ADP96341; HP15_577. DR GeneID; 12400592; -. DR KEGG; mad:HP15_577; -. DR PATRIC; 43113299; VBIMarBac104501_0583. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; MADH225937:GLG5-594-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 323 AA; 34643 MW; 137F68CE3B3B0167 CRC64; MSARETPVKE VHVAVAVIVR DGRVLIARRP DHVHQGGLLE FPGGKVEPGE TVQAALVREI AEETGLHVPA GSLEPVIGIR HDYGDKRVFL DVWETSAAEG EARGCEGQPV EWLTPEQLRD EDFPAANRPI IRALRLPRQL AITGSENGLE PALAHLQEGL SAARPPLVLL RAPALSPLAY RELAANALPV CEKTGATLIV HGGPEVFRAI PGAHGLHLPW REAAKLSARP VPEDVWLGVS CHDRQEIDHA TAIGADYVTL GPVQPTESHP GAPTLGWSVF ADLVSEAVLP VFALGGLSPG DLREARQRGG QGIAGIRFWW PQS // ID E4Q309_CALOW Unreviewed; 221 AA. AC E4Q309; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Calow_0242; OS Caldicellulosiruptor owensensis (strain ATCC 700167 / DSM 13100 / OL). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=632518; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OL; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.; RT "Complete sequence of Caldicellulosiruptor owensensis OL."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700167 / DSM 13100 / OL; RX PubMed=21216991; DOI=10.1128/JB.01515-10; RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A., RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., RA Woyke T., Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., RA Detter J.C., Walston-Davenport K., Han S., Adams M.W., Kelly R.M.; RT "Complete genome sequences for the anaerobic, extremely thermophilic RT plant biomass-degrading bacteria Caldicellulosiruptor hydrothermalis, RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor RT kronotskyensis, Caldicellulosiruptor owensensis, and RT Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002216; ADQ03845.1; -; Genomic_DNA. DR RefSeq; YP_004001645.1; NC_014657.1. DR EnsemblBacteria; ADQ03845; ADQ03845; Calow_0242. DR GeneID; 9959621; -. DR KEGG; cow:Calow_0242; -. DR PATRIC; 42589556; VBICalOwe108203_0265. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; COWE632518:GHVV-243-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 24542 MW; BFDD595B25F38215 CRC64; MSLTKEEKLK LFSTYTIYGM TAEKFSKGRS NIEVVKAMLG SGIKLIQYRE KYKSLKEKYK ECLEIRKLTE DYGALLIVND NADLCQIVGA DGVHLGQEDL PADEVRKILG DEYIIGVTTH KKEQVLKAKE DGADYVGLGP IFASFTKDNP HPPIGLEMVK WAAENSPLPF VAIGGIKEHN LKDVLANGAR CICAVTEVVG ADDIQKKIKS FFEILKEFGR S // ID E4Q8D3_CALH1 Unreviewed; 221 AA. AC E4Q8D3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Calhy_2276; OS Caldicellulosiruptor hydrothermalis (strain DSM 18901 / VKM B-2411 / OS 108). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=632292; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=108; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.; RT "Complete sequence of Caldicellulosiruptor hydrothermalis 108."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18901 / VKM B-2411 / 108; RX PubMed=21216991; DOI=10.1128/JB.01515-10; RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A., RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., RA Woyke T., Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., RA Detter J.C., Walston-Davenport K., Han S., Adams M.W., Kelly R.M.; RT "Complete genome sequences for the anaerobic, extremely thermophilic RT plant biomass-degrading bacteria Caldicellulosiruptor hydrothermalis, RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor RT kronotskyensis, Caldicellulosiruptor owensensis, and RT Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002219; ADQ07980.1; -; Genomic_DNA. DR RefSeq; YP_003993349.1; NC_014652.1. DR EnsemblBacteria; ADQ07980; ADQ07980; Calhy_2276. DR GeneID; 9936845; -. DR KEGG; chd:Calhy_2276; -. DR PATRIC; 42588269; VBICalHyd101559_2384. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; CHYD632292:GHA8-2338-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 25025 MW; 032D0B0E22FAE86A CRC64; MSLNKEEKLQ LFKNYNIYGL TAEKFSNGRS NIEVVKAMLD GGIRIIQYRE KYKSLNEKYE ECLQIRKLTK QYSALLIVND HVDLCQMVGA DGVHLGQEDY PVKEVRKILG EDFIIGVTTH TKEQVEKAVE DGADYIGLGP VFQSFTKDKP HPPIGLEMVS WAATYCKIPF VVIGGIKEHN LKDVLEAGAK CVSLVTEIVG SDDISQKIKR LWDIIKEFER S // ID E4QIX3_METS6 Unreviewed; 316 AA. AC E4QIX3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE SubName: Full=Mutator MutT protein; GN Name=thiE; OrderedLocusNames=MPQ_0527; OS Methylovorus sp. (strain MP688). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylovorus. OX NCBI_TaxID=887061; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MP688; RA Xiong X., Wang J., Zhang W., Yang L., Zhi J., Wang X., Cui Y., RA Dong F., Li M., Yang Y., Du B.; RT "Complete genome sequence of the PQQ high-production bacteria RT Methylovorus sp. MP688."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP688; RX PubMed=21148725; DOI=10.1128/JB.01431-10; RA Xiong X.H., Zhi J.J., Yang L., Wang J.H., Zhao Y., Wang X., Cui Y.J., RA Dong F., Li M.X., Yang Y.X., Wei N., An J.J., Du B.H., Liang L., RA Zhang J.S., Zhou W., Cheng S.F., He T., Wang L., Chen H.P., Liu D.S., RA Zhang W.C.; RT "Complete genome sequence of the bacterium Methylovorus sp. strain RT MP688, a high-level producer of pyrroloquinolone quinone."; RL J. Bacteriol. 193:1012-1013(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002252; ADQ83709.1; -; Genomic_DNA. DR RefSeq; YP_004038945.1; NC_014733.1. DR ProteinModelPortal; E4QIX3; -. DR EnsemblBacteria; ADQ83709; ADQ83709; MPQ_0527. DR GeneID; 9995365; -. DR KEGG; mep:MPQ_0527; -. DR PATRIC; 45263316; VBIMetSp170262_0508. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR BioCyc; MSP887061:GHJT-527-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 316 AA; 34778 MW; 978E1E7885210BC4 CRC64; MTDKPVVHAA VAVLVREDGK VLLAQRPEGK PWAGWWEFPG GKIEQGESVL QALKREIEEE LGTAIVEAYP WITRRFAYPE RTVQLHFYQV RRWAGEPHGR EGQALSWQWP SAVDVGPLLP ANEPLLRMLS LPSIYAITQL EALGEPVFLA RLERALQGGL KLIQVREKHL SEEALLAFAT KVLALARPYG ARVLLNASPE LASRVHADGV HLSSQALMAL EQKPEGLVVG ASCHDAHELA RAAELELDFV VFSPVLRTLS HPDAKPLGWH GFAEGIAGYA LPVYALGGLQ ASHLQEAWRH GAHGIAMLRG CWNENS // ID E4QQ13_METS6 Unreviewed; 208 AA. AC E4QQ13; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MPQ_2744; OS Methylovorus sp. (strain MP688). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylovorus. OX NCBI_TaxID=887061; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MP688; RA Xiong X., Wang J., Zhang W., Yang L., Zhi J., Wang X., Cui Y., RA Dong F., Li M., Yang Y., Du B.; RT "Complete genome sequence of the PQQ high-production bacteria RT Methylovorus sp. MP688."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP688; RX PubMed=21148725; DOI=10.1128/JB.01431-10; RA Xiong X.H., Zhi J.J., Yang L., Wang J.H., Zhao Y., Wang X., Cui Y.J., RA Dong F., Li M.X., Yang Y.X., Wei N., An J.J., Du B.H., Liang L., RA Zhang J.S., Zhou W., Cheng S.F., He T., Wang L., Chen H.P., Liu D.S., RA Zhang W.C.; RT "Complete genome sequence of the bacterium Methylovorus sp. strain RT MP688, a high-level producer of pyrroloquinolone quinone."; RL J. Bacteriol. 193:1012-1013(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002252; ADQ85883.1; -; Genomic_DNA. DR RefSeq; YP_004041119.1; NC_014733.1. DR EnsemblBacteria; ADQ85883; ADQ85883; MPQ_2744. DR GeneID; 9997583; -. DR KEGG; mep:MPQ_2744; -. DR PATRIC; 45267709; VBIMetSp170262_2655. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FQFRVKG; -. DR BioCyc; MSP887061:GHJT-2744-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21794 MW; 6E09A0A53ED67564 CRC64; MTPIKGLYAV TPDLDDTERL CEIVIEAILG GATLVQYRNK EAGHVLRIAQ AQALLAICRQ HGVPLIINDH VKLCLALDAD GVHIGGTDGD IAATRQRIGN KLLGASCYNR IDLALQAQAA GADYVAFGAC FSSQTKPQAP EAALSLFNMN PALTVPKVAI GGITLDNAPQ AVAAGADMLA VIGSLWGSSD IRRTAQQFSR LYNGPSSS // ID E4QVS2_HAEI6 Unreviewed; 226 AA. AC E4QVS2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=R2866_0156; OS Haemophilus influenzae (strain R2866). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=262728; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R2866; RA VanWagoner T.M., Erwin A.L., Kaul R., Mahaffey M., Zhou Y., RA Aggarwal G., Chang J., Deng H., Gillett W., Haugen E., Kibukawa M., RA Phelps K., Saenphimmachak C., Sivam D., Worthey E.A., Olson M.V., RA Stull T.L., Smith A.L.; RT "Genome sequence of the invasive non-typeable isolate Haemophilus RT influenzae R2866."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002277; ADO80149.1; -; Genomic_DNA. DR RefSeq; YP_005826880.1; NC_017451.1. DR ProteinModelPortal; E4QVS2; -. DR EnsemblBacteria; ADO80149; ADO80149; R2866_0156. DR GeneID; 12594941; -. DR KEGG; hiz:R2866_0156; -. DR PATRIC; 43045399; VBIHaeInf103652_0164. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; HINF262728:GLDR-156-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24758 MW; D2FC00C9C781EEE7 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAINCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNV GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID E4R1J7_BIFLM Unreviewed; 917 AA. AC E4R1J7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE SubName: Full=ThiE; GN Name=thiE; OrderedLocusNames=BBMN68_161; OS Bifidobacterium longum subsp. longum (strain BBMN68). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=890402; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BBMN68; RX PubMed=21097614; DOI=10.1128/JB.01213-10; RA Hao Y., Huang D., Guo H., Xiao M., An H., Zhao L., Zuo F., Zhang B., RA Hu S., Song S., Chen S., Ren F.; RT "Complete genome sequence of Bifidobacterium longum subsp. longum RT BBMN68, a new strain from a healthy chinese centenarian."; RL J. Bacteriol. 193:787-788(2011). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002286; ADQ02496.1; -; Genomic_DNA. DR RefSeq; YP_003999775.1; NC_014656.1. DR EnsemblBacteria; ADQ02496; ADQ02496; BBMN68_161. DR GeneID; 9958182; -. DR KEGG; blb:BBMN68_161; -. DR PATRIC; 42579833; VBIBifLon171405_0169. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR BioCyc; BLON890402:GJ8K-162-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100385 MW; 055148B3837F7F86 CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLADTKA AGWFVVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVTFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID E4R6X1_PSEPB Unreviewed; 207 AA. AC E4R6X1; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PPUBIRD1_4566; OS Pseudomonas putida (strain BIRD-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=931281; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BIRD-1; RA Matilla M.A., Pizarro P., Roca A., Fernandez M., Duque E., Molina L., RA van der Lelie D., Gomez M.J., Ramos J.-L.; RT "Complete genome of the plant-growth promoting rhizobacteria RT Pseudomonas putida BIRD-1."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BIRD-1; RX PubMed=21183676; DOI=10.1128/JB.01281-10; RA Matilla M.A., Pizarro-Tobias P., Roca A., Fernandez M., Duque E., RA Molina L., Wu X., van der Lelie D., Gomez M.J., Segura A., Ramos J.L.; RT "Complete genome of the plant growth-promoting rhizobacterium RT Pseudomonas putida BIRD-1."; RL J. Bacteriol. 193:1290-1290(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002290; ADR62129.1; -; Genomic_DNA. DR RefSeq; YP_005932334.1; NC_017530.1. DR EnsemblBacteria; ADR62129; ADR62129; PPUBIRD1_4566. DR GeneID; 12522742; -. DR KEGG; ppb:PPUBIRD1_4566; -. DR PATRIC; 45411244; VBIPsePut176522_4607. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; PPUT931281:GLIU-4502-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21718 MW; 39525BABD271BEA0 CRC64; MKLRGLYAIT DSQLLAGRFL SHVEAALEGG VCLLQYRDKS DDAARRLREA EGLMKLCERY GTQLLINDDA ELAARLGVGV HLGQTDGPLT PARALLGRQA IIGSTCHASL ELATQAASEG ASYVAFGRFF NSVTKPGAPA ANVGLLEQAR AQVKLPIAVI GGITLDNAAP LVAHGADLLA VIHGLFGADS AQEVTRRARA FNALFAS // ID E4RIB0_PSEPB Unreviewed; 314 AA. AC E4RIB0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 13-NOV-2013, entry version 20. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=PPUBIRD1_4214; OS Pseudomonas putida (strain BIRD-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=931281; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BIRD-1; RA Matilla M.A., Pizarro P., Roca A., Fernandez M., Duque E., Molina L., RA van der Lelie D., Gomez M.J., Ramos J.-L.; RT "Complete genome of the plant-growth promoting rhizobacteria RT Pseudomonas putida BIRD-1."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BIRD-1; RX PubMed=21183676; DOI=10.1128/JB.01281-10; RA Matilla M.A., Pizarro-Tobias P., Roca A., Fernandez M., Duque E., RA Molina L., Wu X., van der Lelie D., Gomez M.J., Segura A., Ramos J.L.; RT "Complete genome of the plant growth-promoting rhizobacterium RT Pseudomonas putida BIRD-1."; RL J. Bacteriol. 193:1290-1290(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002290; ADR61792.1; -; Genomic_DNA. DR RefSeq; YP_005931997.1; NC_017530.1. DR ProteinModelPortal; E4RIB0; -. DR EnsemblBacteria; ADR61792; ADR61792; PPUBIRD1_4214. DR GeneID; 12522391; -. DR KEGG; ppb:PPUBIRD1_4214; -. DR PATRIC; 45410510; VBIPsePut176522_4249. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; PPUT931281:GLIU-4158-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 34398 MW; 41C9A0C7B7DD2355 CRC64; MKRIHVVAAV IRGADGRILI ARRADTQHQG GLWEFPGGKV EEGESVEVAL ARELREELGI EVSHSRALIK VSHDYSDKQV LLDVREVEAF TGEPHGAEGQ PLEWVAPRDL PQYEFPEANK PIVAAARLPD QYLITPDGLE VPQMLKGIQK AVANGIRLIQ LRAPDMYDPK YRDVAVDAVG LCAGKAQLML KGPLEWLGDF PAAGWHLTAA QLRKYAARGR PFPKERWLAA SCHSAEELAL AEQMGVDFVT LSPVQATQTH PEAVPLGWDE AQRLIAGFNK PVYLLGGVGP GEREHAWEAG AQGVAGIRAF WPEV // ID E4RMU9_HALHG Unreviewed; 217 AA. AC E4RMU9; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Halsa_0715; OS Halanaerobium hydrogeniformans (Halanaerobium sp. (strain OS sapolanicus)). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae; OC Halanaerobium. OX NCBI_TaxID=656519; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=sapolanicus; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Begemann M.B., Mormile M.R., Wall J.D., Elias D.A., Woyke T.; RT "Complete sequence of Halanaerobium sp. sapolanicus."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002304; ADQ14166.1; -; Genomic_DNA. DR RefSeq; YP_003994520.1; NC_014654.1. DR ProteinModelPortal; E4RMU9; -. DR EnsemblBacteria; ADQ14166; ADQ14166; Halsa_0715. DR GeneID; 9968305; -. DR KEGG; has:Halsa_0715; -. DR PATRIC; 42640004; VBIHalSp157090_0751. DR KO; K00788; -. DR BioCyc; HHYD656519:GHYV-719-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23195 MW; 71E9252EDA7371BB CRC64; MKDTNWSLYL ITEENLSQGR TSLEVVKKAV AGGVDAVQLR DKSLSVRERY SLGLKLKEFT ASRGVKLIIN DRVDLAQALD ADGVHLGQDD LPLKEARAIL GPDKIIGITA TELKAAQKAE KEGADYLGVG SVFKSNSKKV AAFKAGIGTA GINKLRKELS LPITAIGGIQ TANAAEVIKA GADNIAVISA LSQAEDIQKS AQEFRKIIVK AKKEREV // ID E4RW17_LEAB4 Unreviewed; 201 AA. AC E4RW17; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Lbys_0382; OS Leadbetterella byssophila (strain DSM 17132 / KACC 11308 / 4M15). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Leadbetterella. OX NCBI_TaxID=649349; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17132; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Teshima H., Brettin T., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of Leadbetterella byssophila DSM 17132."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17132 / KACC 11308 / 4M15; RX PubMed=21475582; DOI=10.4056/sigs.1413518; RA Abt B., Teshima H., Lucas S., Lapidus A., Del Rio T.G., Nolan M., RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., RA Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Rohde M., Goker M., Tindall B.J., Detter J.C., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Leadbetterella byssophila type strain RT (4M15)."; RL Stand. Genomic Sci. 4:2-12(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002305; ADQ16160.1; -; Genomic_DNA. DR RefSeq; YP_003996513.1; NC_014655.1. DR ProteinModelPortal; E4RW17; -. DR EnsemblBacteria; ADQ16160; ADQ16160; Lbys_0382. DR GeneID; 9954222; -. DR KEGG; lby:Lbys_0382; -. DR PATRIC; 42650649; VBILeaBys116579_0392. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; LBYS649349:GHFA-389-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 128 130 THZ-P binding (By similarity). FT REGION 179 180 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 102 102 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 159 159 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 201 AA; 22108 MW; E42397AA8302270F CRC64; MQLYLVISQD ACGSRDFLEV AKEAILGGVD IIQLREKKLQ EEEFLYRAQA LHKITQLHKI PLVINDNLNV ALEVGAEGVH VGLNDMPPVQ VRKKWKGMMG WSIEYLDQLT SPEIHAVDYI AASPVFSTPT KEDTVTEWGI EGIKKIKSLS KLPLVAIGGV NIKNARKILE AGADSLAVVS AICQAKDPKG AAYQLKSFFN P // ID E4S837_CALKI Unreviewed; 219 AA. AC E4S837; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-APR-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Calkr_0325; OS Caldicellulosiruptor kristjanssonii (strain ATCC 700853 / DSM 12137 / OS I77R1B). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=632335; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=177R1B; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Blumer-Schuette S.E., Kelly R.M., Woyke T.; RT "Complete sequence of chromosome of Caldicellulosiruptor RT kristjanssonii 177R1B."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700853 / DSM 12137 / I77R1B; RX PubMed=21216991; DOI=10.1128/JB.01515-10; RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A., RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., RA Woyke T., Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., RA Detter J.C., Walston-Davenport K., Han S., Adams M.W., Kelly R.M.; RT "Complete genome sequences for the anaerobic, extremely thermophilic RT plant biomass-degrading bacteria Caldicellulosiruptor hydrothermalis, RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor RT kronotskyensis, Caldicellulosiruptor owensensis, and RT Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002326; ADQ39885.1; -; Genomic_DNA. DR RefSeq; YP_004025498.1; NC_014721.1. DR EnsemblBacteria; ADQ39885; ADQ39885; Calkr_0325. DR GeneID; 9982961; -. DR KEGG; cki:Calkr_0325; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; CKRI632335:GI3P-330-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24303 MW; 1108A41720BC2815 CRC64; MTKEEKLKLF STYTIYGMTA EKFSNGRSNI EVVKAMLDGG IKIIQYREKY KSLKEKYKEC LEIRKLTEDY GALLIVNDHA DLCQMVGADG VHLGQSDLPA VEVRKLLGDK FIIGVTTHTK EQVLKAKEDG ADYVGLGPIY ASFTKDNPHP PIGLEMVRWA AENSPLPFVA IGGIKDHNLK EVLANGARCI CAVTEIVGAD NIQLKIEGLF KILKSFERS // ID E4SH64_CALK2 Unreviewed; 219 AA. AC E4SH64; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-APR-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Calkro_2256; OS Caldicellulosiruptor kronotskyensis (strain DSM 18902 / VKM B-2412 / OS 2002). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=632348; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2002; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Blumer-Schuette S.E., Kelly R.M., Woyke T.; RT "Complete sequence of Caldicellulosiruptor kronotskyensis 2002."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18902 / VKM B-2412 / 2002; RX PubMed=21216991; DOI=10.1128/JB.01515-10; RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A., RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., RA Woyke T., Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., RA Detter J.C., Walston-Davenport K., Han S., Adams M.W., Kelly R.M.; RT "Complete genome sequences for the anaerobic, extremely thermophilic RT plant biomass-degrading bacteria Caldicellulosiruptor hydrothermalis, RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor RT kronotskyensis, Caldicellulosiruptor owensensis, and RT Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002330; ADQ47089.1; -; Genomic_DNA. DR RefSeq; YP_004024908.1; NC_014720.1. DR EnsemblBacteria; ADQ47089; ADQ47089; Calkro_2256. DR GeneID; 9982241; -. DR KEGG; ckn:Calkro_2256; -. DR PATRIC; 42811597; VBICalKro6863_2374. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; CKRO632348:GI5C-2314-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24506 MW; 3FA6DF119AC0081F CRC64; MTKEEKLRLF STYTIYGMTA EKFSNGRSNI EIVKAMLDSG IKIIQYREKY KSLKEKYKEC LEIRKLTEDY EALLIVNDHA DLCQMVGADG VHLGQEDLPA DEVRKLLGDK FIIGVTTHTE DQVLKAKEDG ADYVGLGPVF TSFTKDNPHP PIGLEMVKWA AENSPLPFVA IGGIKEHNLK EVLASGARCI CAVTEIVGAD DIHQKIESLF KILKSFERS // ID E4T9H3_RIEAD Unreviewed; 207 AA. AC E4T9H3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-APR-2014, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Riean_0486; ORFNames=RA0C_0710; OS Riemerella anatipestifer (strain ATCC 11845 / DSM 15868 / JCM 9532 / OS NCTC 11014). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Riemerella. OX NCBI_TaxID=693978; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11845 / DSM 15868 / JCM 9532 / NCTC 11014, and DSM 15868; RX PubMed=21677851; DOI=10.4056/sigs.1553862; RA Mavromatis K., Lu M., Misra M., Lapidus A., Nolan M., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., RA Detter J.C., Brambilla E.M., Rohde M., Goker M., Gronow S., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., RA Kyrpides N.C.; RT "Complete genome sequence of Riemerella anatipestifer type strain RT (ATCC 11845)."; RL Stand. Genomic Sci. 4:144-153(2011). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11845; RX PubMed=22628503; DOI=10.1128/JB.00366-12; RA Wang X., Zhu D., Wang M., Cheng A., Jia R., Zhou Y., Chen Z., Luo Q., RA Liu F., Wang Y., Chen X.Y.; RT "Complete Genome Sequence of Riemerella anatipestifer Reference RT Strain."; RL J. Bacteriol. 194:3270-3271(2012). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11845; RA Cheng A.-C., Wang M.-S., Zhu D.-K., Wang X.-J.; RT "Riemerella anatipestifer ATCC 11845 Complete Genome."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002346; ADQ81654.1; -; Genomic_DNA. DR EMBL; CP003388; AFD55668.1; -; Genomic_DNA. DR RefSeq; YP_004045160.1; NC_014738.1. DR RefSeq; YP_005394211.1; NC_017045.1. DR EnsemblBacteria; ADQ81654; ADQ81654; Riean_0486. DR EnsemblBacteria; AFD55668; AFD55668; RA0C_0710. DR GeneID; 10001223; -. DR GeneID; 11997132; -. DR KEGG; rai:RA0C_0710; -. DR KEGG; ran:Riean_0486; -. DR PATRIC; 45351629; VBIRieAna155424_0489. DR HOGENOM; HOG000166809; -. DR KO; K00788; -. DR BioCyc; RANA693978:GHF6-493-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 207 AA; 23726 MW; BAAF6760ABA260BC CRC64; MEIKNGIYLI VNPSMHRDTL LIKLEKIISE GIVAVQIWDN FNDNDNILDI INRIIEICHK ENIPVLINNR WELLREVNID GVHFDVQPND IEAIRRELGR KVIMGITCNN DLEHVQWANK QKMDYISFCS IFPSSTANSC EFVRFDTVRE AQKITQIPIF LAGGITPENV GELTYLNCSG IAVVSGIMDS EQPIQEIKKY KLKLKKT // ID E4TGI6_CALNY Unreviewed; 212 AA. AC E4TGI6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Calni_0756; OS Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / OS Yu37-1). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae. OX NCBI_TaxID=768670; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19672; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A., RA Brettin T., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Calditerrivibrio nitroreducens RT DSM 19672."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19672 / NBRC 101217 / Yu37-1; RX PubMed=21475587; DOI=10.4056/sigs.1523807; RA Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A., RA Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., RA Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Land M.; RT "Complete genome sequence of Calditerrivibrio nitroreducens type RT strain (Yu37-1)."; RL Stand. Genomic Sci. 4:54-62(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002347; ADR18667.1; -; Genomic_DNA. DR RefSeq; YP_004050830.1; NC_014758.1. DR EnsemblBacteria; ADR18667; ADR18667; Calni_0756. DR GeneID; 10008767; -. DR KEGG; cni:Calni_0756; -. DR PATRIC; 45189231; VBICalNit163602_0830. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; CNIT768670:GHD1-769-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23759 MW; F3219A791DFA6178 CRC64; MCSKYRQKIS HYLKLYLILE TDMLKIPLEE FIPQVVSGGV TAIQLRDKKL TAKQRYENGL KIKEFIKDKD IMITVNDRLD LALALEIDAI HVGVKDIPPY VIKELYPDIL VGYSCNNFED LEVAEKSKVS YIGVGPAFLT STKDDLRPLI GPDGIKEIIS KTDIPSVAIG GINLQNCHQL VDTGVKGVAV SSEICRSPNP YETAKKFREF FP // ID E4TGQ7_CALNY Unreviewed; 185 AA. AC E4TGQ7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Calni_1866; OS Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / OS Yu37-1). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae. OX NCBI_TaxID=768670; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19672; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A., RA Brettin T., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Calditerrivibrio nitroreducens RT DSM 19672."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19672 / NBRC 101217 / Yu37-1; RX PubMed=21475587; DOI=10.4056/sigs.1523807; RA Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A., RA Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., RA Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Land M.; RT "Complete genome sequence of Calditerrivibrio nitroreducens type RT strain (Yu37-1)."; RL Stand. Genomic Sci. 4:54-62(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002347; ADR19770.1; -; Genomic_DNA. DR RefSeq; YP_004051933.1; NC_014758.1. DR EnsemblBacteria; ADR19770; ADR19770; Calni_1866. DR GeneID; 10009906; -. DR KEGG; cni:Calni_1866; -. DR PATRIC; 45191545; VBICalNit163602_1958. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; YTLSPIF; -. DR BioCyc; CNIT768670:GHD1-1908-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 185 AA; 20956 MW; A48243D53F9FCE32 CRC64; MKILFILDYT TYRENIFDVA KVASIYADAI WFRIKNIDAV DILYLSKRLR NELPSSHLIL SERPDIAQIA SFNGVQIGSK SIPTYAVKKA FPDLELGYSA HSINEIEEVE ADYYTLSPIF YTKKDYDVYP LGPVDVSLVG KRIFALGGIN INNVAKLLNQ GYYGIAGISF FNDLQELSRK LKNSR // ID E4TLK4_MARTH Unreviewed; 208 AA. AC E4TLK4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Ftrac_2330; OS Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB OS 1408 / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter OS tractuosus). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae; OC Marivirga. OX NCBI_TaxID=643867; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 / RC H-43; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Spring S., Schroeder M., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Marivirga tractuosa DSM 4126."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002349; ADR22308.1; -; Genomic_DNA. DR RefSeq; YP_004054416.1; NC_014759.1. DR EnsemblBacteria; ADR22308; ADR22308; Ftrac_2330. DR GeneID; 10012479; -. DR KEGG; mtt:Ftrac_2330; -. DR PATRIC; 45218037; VBIMarTra126157_2416. DR HOGENOM; HOG000166809; -. DR KO; K00788; -. DR BioCyc; MTRA643867:GI2X-2364-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 208 AA; 23368 MW; 3BFF82E0499ED275 CRC64; MKKLAGLYLV IDPSQEHDSL LNKLHTALKG GIDIVQIWDH WPKAQDKETQ LEFIKRAKKL TKDFQVPLLM NQDWELAVET GLDGVHFDRL PADFPSIQPQ LKGQYIGLTV TNNLEEVQMA EQNSLSYISF CSVFPSPSVD SCDIVQPESI KKAKEISNMP IFLSGGINQE NFEQLKALPF NGIAVISGIL NEEDPEAAAK KYKEKLQD // ID E4TWH5_SULKY Unreviewed; 185 AA. AC E4TWH5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN OrderedLocusNames=Sulku_1130; OS Sulfuricurvum kujiense (strain ATCC BAA-921 / DSM 16994 / JCM 11577 / OS YK-1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Sulfuricurvum. OX NCBI_TaxID=709032; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1; RX PubMed=22675602; DOI=10.4056/sigs.2456004; RA Han C., Kotsyurbenko O., Chertkov O., Held B., Lapidus A., Nolan M., RA Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Brambilla E.M., Rohde M., Spring S., RA Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of the sulfur compounds oxidizing RT chemolithoautotroph Sulfuricurvum kujiense type strain (YK-1(T))."; RL Stand. Genomic Sci. 6:94-103(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002355; ADR33793.1; -; Genomic_DNA. DR RefSeq; YP_004059993.1; NC_014762.1. DR EnsemblBacteria; ADR33793; ADR33793; Sulku_1130. DR GeneID; 10018293; -. DR KEGG; sku:Sulku_1130; -. DR PATRIC; 45371065; VBISulKuj150841_1392. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SKUJ709032:GHTQ-1156-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 185 AA; 20345 MW; B887AF5C1B60DB8D CRC64; MQLYALCDTQ TLHQKGVDTL SFAKRAKSLG ASVLQYRNKH SDIATIKTEL IALRQVWEGF LIINDHYELA PFCDGVHIGQ EDLYTIDPDP ARAIKILKMA IGEDKIIGLS THNVEEIEIA NRLDLNYVGL GAYRATSTKS DAKVLGDRLD AIAAHSKHPV AAIGGVKLDD RFQHVAYHVI GSGLL // ID E4U1W9_SULKY Unreviewed; 183 AA. AC E4U1W9; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Sulku_0821; OS Sulfuricurvum kujiense (strain ATCC BAA-921 / DSM 16994 / JCM 11577 / OS YK-1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Sulfuricurvum. OX NCBI_TaxID=709032; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1; RX PubMed=22675602; DOI=10.4056/sigs.2456004; RA Han C., Kotsyurbenko O., Chertkov O., Held B., Lapidus A., Nolan M., RA Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Brambilla E.M., Rohde M., Spring S., RA Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of the sulfur compounds oxidizing RT chemolithoautotroph Sulfuricurvum kujiense type strain (YK-1(T))."; RL Stand. Genomic Sci. 6:94-103(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002355; ADR33487.1; -; Genomic_DNA. DR RefSeq; YP_004059687.1; NC_014762.1. DR EnsemblBacteria; ADR33487; ADR33487; Sulku_0821. DR GeneID; 10017984; -. DR KEGG; sku:Sulku_0821; -. DR PATRIC; 45370444; VBISulKuj150841_1083. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SKUJ709032:GHTQ-847-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 183 AA; 19843 MW; 0A0FEBEF3EA2DB38 CRC64; MKSYLITDPS LYGTTPDSIE SALPAVFSQN LPDFALFRDK QSSDYAELAS VFIRICRNHT VSKVLLHGDY ALASVLGADG VHLTSTQSEE IAEAKALGLY VVISTHTHEE AIKAQKLGAD AITYSPIFFS PNKGEPKGLE DLKEIVAKIE IPIFALGGIT AQEQINAVEK CGAYGFASIR YFI // ID E4UQA6_ARTGP Unreviewed; 520 AA. AC E4UQA6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE SubName: Full=Hydroxyethylthiazole kinase; GN ORFNames=MGYG_02201; OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum OS gypseum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Arthroderma. OX NCBI_TaxID=535722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4604 / CBS 118893; RX PubMed=22951933; DOI=10.1128/mBio.00259-12; RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W., RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E., RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I., RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., RA Summerbell R.C., Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., RA White T.C.; RT "Comparative genome analysis of Trichophyton rubrum and related RT dermatophytes reveals candidate genes involved in infection."; RL MBio 3:E259-E259(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS989823; EFQ99187.1; -; Genomic_DNA. DR RefSeq; XP_003174670.1; XM_003174622.1. DR GeneID; 10029970; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 520 AA; 54889 MW; 8C02B2EF4DEF3244 CRC64; MPVNLSLYLV TDSTPKILGE RDLCSVVEQA VQGGVTIVQY RDKHSDTKDL IEAATKLHAI TLNHGIPLII NDRVDVALAV GAEGVHLGQD DMDIALARKI LPKGTIIGVT VSSVEEAQAA VEGGADYLGI GTVYATPTKT NTKSIIGTAG VKRILSCVAS LNPKVGTVAI GGINLSNVQR VIYQSQDTKK GLEGVAIVSA IMAAENPRAA AAQFLKKVSQ NPAFATFPVP PRENEEHLLL DRVDGLVRKV ATVHPLCHNM INYVVANFAA NVALAIGASP IMSGYGLEAP DLAKNKGSLL INMGTLNSES LDNYLQGIRA YNEAGNPVVL DPVGAAATQL RRQSVKTLMQ GGYFDLIKGN ESEIGHIYGH TGNQVGVDSG PSTLDIKEKA MLVRDLALRE RCIVLLTGPT DYLSDGARTL AIHNGHPLLG QVTGTGCAIG TVTSAFLAVE KQDKLLAVLS ALLMFEIAAE RAVSNGVKGP GSFVPALLDE LYSLRTQATE SKAASLDVLK KAAKVNFIHF // ID E4V8A5_BIFBI Unreviewed; 918 AA. AC E4V8A5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; ORFNames=BBNG_00394; OS Bifidobacterium bifidum NCIMB 41171. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=398513; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCIMB 41171; RG The Broad Institute Genome Sequencing Platform; RA Goulas T., Tzortzis G., Gibson G.R., Ward D., Mehta T., Young S., RA Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., RA Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., RA Galagan J., Nusbaum C., Birren B.; RT "Annotation of Bifidobacterium bifidum strain NCIMB 41171."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990229; EFR49847.1; -; Genomic_DNA. DR ProteinModelPortal; E4V8A5; -. DR EnsemblBacteria; EFR49847; EFR49847; BBNG_00394. DR PATRIC; 27197913; VBIBifBif36250_1141. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 918 AA; 100226 MW; A7B2F8DF7E6FBAB7 CRC64; MSNEYPFASM RDSFDLSAYF VVGPQDCKDR PLTEVIDQAL HGGATFIQLR AKGADASELT EMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQSDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSSTK PEASVGGNDG SGKTLDAAQI NTICSASEFP VVVGGGVTAA DMAMLAGTKA AGWFAVSAIA GAEDPEAATR EMVSGWKAVR ADERHGYAPR IVTHTPATDT QAAQEGSAAA GAEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF SYEYGSYDLE VPYTEIKLSD TPGVGPNAPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL QDDGKRAIKR GRATKEWRGR THQPMRAKDH PVTQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHGAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVA DAVTGKIPEG VETPANPVTD DTVVSANVLS PEEILAGMDA MGEKYRAQGG KLYSKASE // ID E4VDX7_9HELI Unreviewed; 213 AA. AC E4VDX7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HCMG_00279; OS Helicobacter canadensis MIT 98-5491. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=537970; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MIT 98-5491; RG The Broad Institute Genome Sequencing Platform; RA Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T., RA Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., RA Shea T., Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., RA Galagan J., Nusbaum C., Birren B.; RT "Annotation of Helicobacter canadensis strain MIT 98-5491."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990368; EFR48106.1; -; Genomic_DNA. DR EnsemblBacteria; EFR48106; EFR48106; HCMG_00279. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 213 AA; 24240 MW; 622F16B44986A917 CRC64; MSNIWRFVML QGIYAISDEI LTPYQEIFAM LQKAIEGGIS IFQFRDKSHQ DNQIESLVAE LMDYCEQEQI LFVLNDRIEL AMKLQTKGLH IGKKQEVHPY SLEELYMIRK SYGGILGISC YGDLQLAQNA KEIGADYIAF GSCFASPTKT QAKVISLDLF QKIQGIKKCA IGGINQQNIH QLQNVDMVAC ISSIWKGDII KNIDNLKRNW KNL // ID E4VK02_9HELI Unreviewed; 231 AA. AC E4VK02; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HCCG_01378; OS Helicobacter cinaedi CCUG 18818. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=537971; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 18818; RG The Broad Institute Genome Sequencing Platform; RA Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T., RA Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., RA Shea T., Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., RA Galagan J., Nusbaum C., Birren B.; RT "Annotation of Helicobacter cinaedi strain CCUG 18818."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990392; EFR46831.1; -; Genomic_DNA. DR ProteinModelPortal; E4VK02; -. DR EnsemblBacteria; EFR46831; EFR46831; HCCG_01378. DR PATRIC; 26844328; VBIHelCin131914_1229. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 231 AA; 25504 MW; A287B3A6F54D6416 CRC64; MSVNTRLQGI YAISDEILTP YEILSQCVES ALKAGVRIFQ LRDKSHSDEW LCPIAKELLK LCERYNALFV LNDRLDLALR LNAPALHIGR DDGEFSRVRE RFSGILGASS YGDLQRAKVL ESLGADYVAF GAFFPSPTKP NAAAAPLELL IQAKQTLKIP ICAIGGISTQ NIHLLKNADM NAVISSLWAN NSQDSSTLES TRTNSTYTES TLQNRLDSIT HNAKALQQYC K // ID E4VMG2_9HELI Unreviewed; 186 AA. AC E4VMG2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HCCG_01693; OS Helicobacter cinaedi CCUG 18818. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=537971; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 18818; RG The Broad Institute Genome Sequencing Platform; RA Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T., RA Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., RA Shea T., Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., RA Galagan J., Nusbaum C., Birren B.; RT "Annotation of Helicobacter cinaedi strain CCUG 18818."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990393; EFR47145.1; -; Genomic_DNA. DR ProteinModelPortal; E4VMG2; -. DR EnsemblBacteria; EFR47145; EFR47145; HCCG_01693. DR PATRIC; 26844987; VBIHelCin131914_1759. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 186 AA; 20821 MW; B9819AF9D29A2CA7 CRC64; MKTTNFTPIL ITPCIDRAYL QKLPLYAKSA SWLMYRHKDD EFVDDFLSLT RPLSHKTLLL NLSFTNPIEA VKLSTRFDGL HLKSHFLDFI APLKSHFADK KIIGYSAHSI EEVKSALALG ATYCTLSPIY PSQNKGKPLG IESLRNLPKS LRSHIVALGG INKSHIQTLK NLGLFGFAGI SYFLES // ID E4VRJ7_BACFG Unreviewed; 204 AA. AC E4VRJ7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BFAG_02076; OS Bacteroides fragilis 3_1_12. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457424; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_12; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RT "Annotation of Bacteroides fragilis strain 3_1_12."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973213; EFR53381.1; -; Genomic_DNA. DR ProteinModelPortal; E4VRJ7; -. DR EnsemblBacteria; EFR53381; EFR53381; BFAG_02076. DR PATRIC; 27022452; VBIBacFra64498_1494. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22157 MW; 1FCC473E79BFF820 CRC64; MLSLQFITHQ TGKYSYFESA CMALEGGCKW IQLRMKEASP EEVETVARQL KPLCKTHGAI LILDDHVELA QKLEVDGVHL GKKDMPVSEA RKILGEAFII GGTANTFEDV KMHFSAGADY LGIGPFRFTT TKKNLSPVLG LEGYTSILSQ MDECGIRIPV VAIGGIVTED IPAIMKTGVN GIALSGAILQ APNPVEETRR ILNI // ID E4VRT3_BACFG Unreviewed; 202 AA. AC E4VRT3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=BFAG_02082; OS Bacteroides fragilis 3_1_12. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457424; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_12; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RT "Annotation of Bacteroides fragilis strain 3_1_12."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973213; EFR53387.1; -; Genomic_DNA. DR ProteinModelPortal; E4VRT3; -. DR EnsemblBacteria; EFR53387; EFR53387; BFAG_02082. DR PATRIC; 27022464; VBIBacFra64498_1500. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23217 MW; 3660752F1134E000 CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHKRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYSGH ISCSCHSVEE VKNKKHFYDY VFMSPIYDSI SKEGYNSPYT AEELRQAGKD KIIDGKVMAL GGITPENILE VKDFGFGGAV VLGDLWGKFD ACSDRDYLAV IEHFKKLKKM AD // ID E4W8W6_RHOE1 Unreviewed; 230 AA. AC E4W8W6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=REQ_39060; OS Rhodococcus equi (strain 103S) (Corynebacterium equi). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=685727; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=103S; RX PubMed=20941392; DOI=10.1371/journal.pgen.1001145; RA Letek M., Gonzalez P., Macarthur I., Rodriguez H., Freeman T.C., RA Valero-Rello A., Blanco M., Buckley T., Cherevach I., Fahey R., RA Hapeshi A., Holdstock J., Leadon D., Navas J., Ocampo A., Quail M.A., RA Sanders M., Scortti M.M., Prescott J.F., Fogarty U., Meijer W.G., RA Parkhill J., Bentley S.D., Vazquez-Boland J.A.; RT "The genome of a pathogenic rhodococcus: cooptive virulence RT underpinned by key gene acquisitions."; RL PLoS Genet. 6:E1001145-E1001145(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN563149; CBH49891.1; -; Genomic_DNA. DR RefSeq; YP_004008570.1; NC_014659.1. DR ProteinModelPortal; E4W8W6; -. DR EnsemblBacteria; CBH49891; CBH49891; REQ_39060. DR GeneID; 9966143; -. DR KEGG; req:REQ_39060; -. DR PATRIC; 42665307; VBIRhoEqu141084_3913. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; REQU685727:GHKP-3786-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 157 159 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 160 160 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 24305 MW; 71FC2F09591C7920 CRC64; MHASQSVKHL TPRERLADAR LYLCTDARRD KGDLAQFVDA ALAGGVDIVQ LRDKGSAGER EFGPMEVKEE LAALAVIGAA ARRHGALLAV NDRADVALAA GADVLHLGQN DLPVHYARQI VGPDVVIGRS TNNRAQASLA AIEEDVDYFC TGPVWATPTK PGRAASGIEL VRSTAEAQPS RPWFAIGGVD HERLPEILEA GATRIVVVRA ITAADDPKAA ARALSDALRG // ID E4ZAW5_NEIL0 Unreviewed; 205 AA. AC E4ZAW5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NLA_2510; OS Neisseria lactamica (strain 020-06). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=489653; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=020-06; RA Bennett J.S., Bentley S.D., Vernikos G.S., Quail M.A., Cherevach I., RA White B., Parkhill J., Maiden M.C.; RT "Independent evolution of the core and accessory gene sets in the RT genus Neisseria: insights gained from the genome of Neisseria RT lactamica isolate 020-06."; RL BMC Genomics 11:652-652(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN995097; CBN86492.1; -; Genomic_DNA. DR RefSeq; YP_004047882.1; NC_014752.1. DR EnsemblBacteria; CBN86492; CBN86492; NLA_2510. DR GeneID; 10007278; -. DR KEGG; nla:NLA_2510; -. DR PATRIC; 45298398; VBINeiLac170077_0290. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; NLAC489653:GJ91-263-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21794 MW; 277B2A40B4ECD66E CRC64; MTFPPLKSPL KFYAVVPTAD WVERMVEAGA DTVQLRCKTL HGDELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSAA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQARGTPVVA IGGIDLNNAQ AVLATGVSSL AAVRAVTEAE NPEAAVKAFQ ALWNG // ID E5A1E5_LEPMJ Unreviewed; 633 AA. AC E5A1E5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-APR-2014, entry version 17. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=LEMA_P105400.1; OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race OS Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae; OC Leptosphaeriaceae; Leptosphaeria; Leptosphaeria maculans complex. OX NCBI_TaxID=985895; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8; RX PubMed=21326234; DOI=10.1038/ncomms1189; RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P., RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S., RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L., RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J., RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J., RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G., RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H., RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.; RT "Effector diversification within compartments of the Leptosphaeria RT maculans genome affected by Repeat-Induced Point mutations."; RL Nat. Commun. 2:202-202(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929131; CBX97409.1; -; Genomic_DNA. DR RefSeq; XP_003840888.1; XM_003840840.1. DR EnsemblFungi; CBX97409; CBX97409; LEMA_P105400.1. DR GeneID; 13283813; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 633 AA; 67277 MW; 9588BCC3DA558251 CRC64; MTSQTSELHC NTFNSSHVQF SPDSDCATHF GYAKIGSLRS ERHPCAPQST LHEPLQHDSA TRYPPTRASG PVAMMKDKAD YSLYLVTDST KPILGDRDLV HVVEQALLGG VTLVQYRDKT SDTGALISTA RAIHEKCKAH NIPLLVNDRV DVALAVGCEG VHIGQDDMSV SSARQLLGPD KIIGATVSSV EEARIAVEQG ADYLGIGTLY ATQTKKNTKD IIGINGIRGI LRYLDTADEA SKKIKTVCIG GVNATNIPLI IHQLFAPTPS NRSPKTIDGV AVVSAIIASP DPKSSSQTLL NLVHSPPPPF KSPSALPTFW LENDTEEITH VLRTALAATK AVKSKTPLTH NMTNLVVQNF AANIALALGA SPIMANYGPE ATDLANLPGT AAALVINMGS VNPDGLANYT QAIRAYNAAG RPIIFDPVGA AATHVRRTAV SHLLAAGYFD LIKGNEREIL QVARATGFAV TDADETSRVQ RGVDSGAPLF SLREKAHVVS MLARRERNVV LMTGAVDVIS DGDRTYSISN GHAYLGLVTG SGCTLGTTLS AYLAAYPKDK LLAGVAGLLH FEVAAQRAAA REDVRGPGSF VPAFIDEVFR IGEEVGEGKM DWEGVARVEC VKGVEEGAVL RLE // ID E5AH66_CHLP1 Unreviewed; 212 AA. AC E5AH66; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cpsi_2161; OS Chlamydophila psittaci (strain RD1) (Chlamydia psittaci). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=929557; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RD1; RX PubMed=21183672; DOI=10.1128/JB.01435-10; RA Seth-Smith H.M., Harris S.R., Rance R., West A.P., Severin J.A., RA Ossewaarde J.M., Cutcliffe L.T., Skilton R.J., Marsh P., Parkhill J., RA Clarke I.N., Thomson N.R.; RT "Genome sequence of the zoonotic pathogen Chlamydophila psittaci."; RL J. Bacteriol. 193:1282-1283(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ482149; CBY16742.1; -; Genomic_DNA. DR RefSeq; YP_004064187.1; NC_014796.1. DR EnsemblBacteria; CBY16742; CBY16742; Cpsi_2161. DR GeneID; 13101173; -. DR KEGG; chr:Cpsi_2161; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22829 MW; 3D460DE4B76332CC CRC64; MEENFFKLIL ITNKQNISVE EYLDFVCACV HSGVTSVQLR EKELSYRELL GFGEALKSML DPLEIPLIVS DSVSVCLDLD ATGVHLGQTD GDVIEARELL GSDKIIGWNV NTLDQLLNAN TLPIDYLGLS AMFATQNKPD ATNLWGFSGL EQAVSLCEHP IVAIGGIDES NAAEVIEAGA AGIAAIGVFH SAQNPGLVTK TLREIVDRGL RC // ID E5APT6_BURRH Unreviewed; 374 AA. AC E5APT6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 11-DEC-2013, entry version 18. DE SubName: Full=Thiamin-phosphate pyrophosphorylase (EC 2.5.1.3); DE EC=2.5.1.3; GN OrderedLocusNames=RBRH_02305; OS Burkholderia rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=882378; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19002 / CIP 109453 / HKI 454; RX PubMed=21131495; DOI=10.1128/JB.01318-10; RA Lackner G., Moebius N., Partida-Martinez L., Hertweck C.; RT "Complete genome sequence of Burkholderia rhizoxinica, an endosymbiont RT of Rhizopus microsporus."; RL J. Bacteriol. 193:783-784(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR687359; CBW74618.1; -; Genomic_DNA. DR RefSeq; YP_004028762.1; NC_014722.1. DR EnsemblBacteria; CBW74618; CBW74618; RBRH_02305. DR GeneID; 9986755; -. DR KEGG; brh:RBRH_02305; -. DR PATRIC; 45183962; VBIBurRhi170666_1786. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; BRHI882378:GJIB-1124-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 374 AA; 40198 MW; 938D9A74666162B5 CRC64; MSGAFLRERE VFYPPADELL EAAERIRARL GDWPRASQPV RICLAPPPQP GPGDVIVVTD VQPHAADTAR WVAAGATVLD ASARAMRLHQ GDAVRTLEAA PCDDWIAAFA AFLDCGCAPH DALCLALAWR QGDEYAQDPW PCDVSRFPRV LGLPDAPVQP FAACPAALGL YPVVPTADWI ERLLALGVRT VQLRRKVDGA GDAADPRALA VLRADVRRAV AAGRRYDDAR VFINDHWQLA LDEGAYGVHL GQEDLSRADI GALAHAGLRL GLSSHGYYEI LVALHFKPSY IALGAVFPTT TKAMPSVPQG LARLARYVRL LDGVVPCVAI GGIDLQTLDD VLATGVRGAA LVRAVTQAHD VEKAIFALQR GFIR // ID E5AS94_BURRH Unreviewed; 190 AA. AC E5AS94; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 11-DEC-2013, entry version 18. DE SubName: Full=Thiamin-phosphate pyrophosphorylase (EC 2.5.1.3); DE EC=2.5.1.3; GN OrderedLocusNames=RBRH_03843; OS Burkholderia rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=882378; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19002 / CIP 109453 / HKI 454; RX PubMed=21131495; DOI=10.1128/JB.01318-10; RA Lackner G., Moebius N., Partida-Martinez L., Hertweck C.; RT "Complete genome sequence of Burkholderia rhizoxinica, an endosymbiont RT of Rhizopus microsporus."; RL J. Bacteriol. 193:783-784(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR687359; CBW75476.1; -; Genomic_DNA. DR RefSeq; YP_004029620.1; NC_014722.1. DR EnsemblBacteria; CBW75476; CBW75476; RBRH_03843. DR GeneID; 9987847; -. DR KEGG; brh:RBRH_03843; -. DR PATRIC; 45185634; VBIBurRhi170666_2592. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; BRHI882378:GJIB-2004-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 190 AA; 20825 MW; CEDE7F47CD60376B CRC64; MRLPKRYLIT PDPSDADPPA LFLEQLKRTL DSGIELVQLR SKKLNAIHYM RLAEKAMDLC QQHHALLLLN AHAPRSARHN VDGLHLDSQS LMACDERPLP TTKLVAASCH TMAELEKAQS IGADFVTLSP VLRTASHPDV EPLGWDGFLA LASRATLPVY ALGGLPADAL PHAERHGAYG IAGIRCFWKS // ID E5B0R6_ERWAM Unreviewed; 214 AA. AC E5B0R6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EAIL5_0247; OS Erwinia amylovora ATCC BAA-2158. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=889211; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-2158; RA Powney R., Smits T.H., Sawbridge T., Frey B., Blom J., Frey J.E., RA Plummer K.M., Beer S.V., Luck J., Duffy B., Rodoni B.; RT "Genome Sequence of an Erwinia amylovora Strain with Pathogenicity RT Restricted to Rubus Plants."; RL J. Bacteriol. 193:785-786(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR719184; CBX79067.1; -; Genomic_DNA. DR ProteinModelPortal; E5B0R6; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23235 MW; 599283DC58CED601 CRC64; MSRGAFPATA ARLGLYPVVD NVQWIARLLE AGVRTIQLRI KDRTEQEVET QVAGAIALGK RYQARLFIND YWRLAVKHQA YGVHLGQEDL NIADLDSIYA AGLRLGLSTH DDDELDRALA EKPSYIALGH VFPTRTKDMP SAPQGLEALS RYIKRLPGIS TVAIGGISLE RAPAVLATGV GSIAVVSAIT QASDWQAATR QLLALAETQR PPRA // ID E5BGJ1_9FUSO Unreviewed; 212 AA. AC E5BGJ1; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FSBG_01111; OS Fusobacterium gonidiaformans 3-1-5R. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469605; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_5R; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 3_1_5R."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657972; EFS21614.1; -; Genomic_DNA. DR ProteinModelPortal; E5BGJ1; -. DR EnsemblBacteria; EFS21614; EFS21614; FSBG_01111. DR PATRIC; 30293703; VBIFusSp3217_1035. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23835 MW; 50606E2C49B49334 CRC64; MRKRIEIPKG IYGITGDNFS NGKSNLDCVK EMIEGGIRIL QYRDKTKSML EKYQEAKEIA KLCKEKGVIF IINDHVDLAL LVNADGVHIG QDDYPVEEVR ALLGNDKIIG LSTHSPEQGF KAFQNENVDY IGVGPIFPTT TKDTKAVGLE YLDFAIQNLH LPLVAIGGIH EDNLEKILAR KVEHFCMVSG IVGAKNIRET VQNLWKQWEE NQ // ID E5BJA5_9FUSO Unreviewed; 212 AA. AC E5BJA5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FSEG_00185; OS Fusobacterium necrophorum D12. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=556263; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D12; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. D12."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDG02000011; EFS22578.1; -; Genomic_DNA. DR ProteinModelPortal; E5BJA5; -. DR EnsemblBacteria; EFS22578; EFS22578; FSEG_00185. DR PATRIC; 28737489; VBIFusSp43879_0137. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23831 MW; 1361BA57B2490DF2 CRC64; MRKRIEIPKG IYGITGDNFS HGKSNLECVK AMIEGGIRII QYRDKIKSMR EKYQEAKEIA KLCKENKVLF IVNDHVDLAL LVDADGVHIG QDDYPVEEVR SLLGPDKIIG LSTHSPKQGL EAFQNENVDY IGVGPIFPTT TKDTKAVGLE YLDFAIKNLS LPFVAIGGIH EHNLQEILTR NVSRFCMVSG IVGAENIMKT VKKLYKQWEE TQ // ID E5CFN8_9BACE Unreviewed; 202 AA. AC E5CFN8; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 13-NOV-2013, entry version 16. DE SubName: Full=Uncharacterized protein; GN ORFNames=BSGG_4261; OS Bacteroides sp. D2. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=556259; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., RA Strauss J., Sibley C., White A., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. D2."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGA02000014; EFS33561.1; -; Genomic_DNA. DR ProteinModelPortal; E5CFN8; -. DR SMR; E5CFN8; 1-202. DR EnsemblBacteria; EFS33561; EFS33561; BSGG_4261. DR PATRIC; 30562665; VBIBacSp21829_4473. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23599 MW; 772F8DFC6BF5D5DD CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNKFD ACQDQNYLAV IEHFKKLKKL SD // ID E5CFP3_9BACE Unreviewed; 205 AA. AC E5CFP3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSGG_4266; OS Bacteroides sp. D2. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=556259; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., RA Strauss J., Sibley C., White A., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroides sp. D2."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGA02000014; EFS33566.1; -; Genomic_DNA. DR ProteinModelPortal; E5CFP3; -. DR EnsemblBacteria; EFS33566; EFS33566; BSGG_4266. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22561 MW; 5396C877E01764E2 CRC64; MVSLQFITHQ TERYSYLESA RMALEGGCKW IQLRMKEAPL EEVEAVALQL KPLCKEHEAI LVLDDHVELA RKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYSSILSQ MKEANIEIPV VAIGGITYED IPAILHTGVN GIALSGTILG ADNPIEETRR ILNHA // ID E5CJJ2_STAHO Unreviewed; 197 AA. AC E5CJJ2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF0798_01273; OS Staphylococcus hominis subsp. hominis C80. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=435837; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C80; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Sibley C.D., Field T.R., Grinwis M., RA Eshaghurshan C.S., Surette M.G., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus hominis subsp. hominis C80."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL545255; EFS19909.1; -; Genomic_DNA. DR EnsemblBacteria; EFS19909; EFS19909; HMPREF0798_01273. DR PATRIC; 44621217; VBIStaHom42890_0490. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 197 AA; 22551 MW; 6799758F6042DF6C CRC64; MMFIFIAITK YKDLTNDDVQ HFLDISDGID GLLFRTPMSS SDLSSFLTSL IEKGFPKSKI IIHSDVHLLE QLHLSHIHFR EMDEDAFSYK STHPEIEVSM STHSIESVKA AYEHDLDYVF FGHIFKTPSK PNQLPRSKAE IQRVLEIPIP IYAIGGITEK TILQLPHGFK GICAISFFMN ASLQQIELLR KEWLKDA // ID E5CKJ5_STAHO Unreviewed; 212 AA. AC E5CKJ5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0798_02030; OS Staphylococcus hominis subsp. hominis C80. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=435837; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C80; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Sibley C.D., Field T.R., Grinwis M., RA Eshaghurshan C.S., Surette M.G., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus hominis subsp. hominis C80."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL545257; EFS19707.1; -; Genomic_DNA. DR ProteinModelPortal; E5CKJ5; -. DR EnsemblBacteria; EFS19707; EFS19707; HMPREF0798_02030. DR PATRIC; 44621961; VBIStaHom42890_0845. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23190 MW; 7FB8A445669AF2A9 CRC64; MFDSKSLQVY FICGTQDIIG DQNIKDVLKA ALESGITLFQ FREKGPNALV GDEKEALAKE LKTLCHEYKV PFLINDDVDL AEKIDADGIH VGQDDEIIAS FANRFKNKII GLSVGNVKEY QQSDLEHVDY IGVGPMYETS SKSDASAPVG PEMIATLKNI NPSLPMVAIG GITEDNCELI AKEGADGVSV ISVITHSQNI DKTVNKLKHY FK // ID E5CTJ1_9STAP Unreviewed; 212 AA. AC E5CTJ1; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0786_02307; OS Staphylococcus caprae C87. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=435838; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C87; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Sibley C.D., Field T.R., Grinwis M., RA Eshaghurshan C.S., Surette M.G., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus caprae C87."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL545276; EFS16827.1; -; Genomic_DNA. DR EnsemblBacteria; EFS16827; EFS16827; HMPREF0786_02307. DR PATRIC; 44618207; VBIStaCap114454_1469. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23722 MW; 6035111EA14F68B9 CRC64; MFSSEQLQVY FICGTQDIPE NRTIEQVLDE ALKAGITMYQ FREKGPSSLI GEEKKQLAIN LKRKCERYHV PFIVNDDIEL AKYIDADGVH VGQDDKEVKD FAMQFRNKII GLSVGNLDEY QQSDLSQVDY IGVGPMYTTT SKDDANAPVG PHMITKLRDY VGELPIVAIG GINETNIEPI AEAGADGVSV ISAITRSKNI DKTVKHFRKY FN // ID E5CTZ5_9STAP Unreviewed; 196 AA. AC E5CTZ5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF0786_01249; OS Staphylococcus caprae C87. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=435838; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C87; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Sibley C.D., Field T.R., Grinwis M., RA Eshaghurshan C.S., Surette M.G., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus caprae C87."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL545278; EFS16237.1; -; Genomic_DNA. DR EnsemblBacteria; EFS16237; EFS16237; HMPREF0786_01249. DR PATRIC; 44619012; VBIStaCap114454_2040. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 22438 MW; 4CE650823F982D13 CRC64; MHIFIAITYD KTLTTQDLEH FLNIEEGIDA LLIRTSMPKN ELKKILIQLI NQGFPKDKMI IHSDTALLEE LNLSRIHFKE NVKTAFAYKK SHPEIQVGMS THSIDTIYTC IDEGIDYVFY GHIFPTPSHP HDAPRSHDEI VEALTLPIPI YAIGGISEQT ISKLEYGFDG ICAISFFMNA SLKEIKELRR KWLQHA // ID E5QR75_STAAH Unreviewed; 213 AA. AC E5QR75; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HMPREF0772_11100; OS Staphylococcus aureus (strain TCH60). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=548473; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TCH60; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RT "Complete genome sequence of Staphylococcus aureus strain TCH60."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TCH60; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002110; ADQ76562.1; -; Genomic_DNA. DR RefSeq; YP_005747182.1; NC_017342.1. DR ProteinModelPortal; E5QR75; -. DR EnsemblBacteria; ADQ76562; ADQ76562; HMPREF0772_11100. DR GeneID; 12332770; -. DR KEGG; suq:HMPREF0772_11100; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SAUR548473:GLKT-1133-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID E5R9A0_STAAG Unreviewed; 213 AA. AC E5R9A0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECTR2_1947; OS Staphylococcus aureus (strain ECT-R 2). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=889933; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ECT-R 2; RA Lindqvist M., Isaksson B., Grub C., Jonassen T.O., Hallgren A.; RT "Detection and characterisation of SCCmec remnants in MR-MSSA causing RT a clonal outbreak in a Swedish county."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR714927; CBX35285.1; -; Genomic_DNA. DR RefSeq; YP_005750635.1; NC_017343.1. DR ProteinModelPortal; E5R9A0; -. DR SMR; E5R9A0; 4-209. DR PRIDE; E5R9A0; -. DR EnsemblBacteria; CBX35285; CBX35285; ECTR2_1947. DR GeneID; 12336528; -. DR KEGG; suc:ECTR2_1947; -. DR KO; K00788; -. DR BioCyc; SAUR889933:GLKJ-1947-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID E5TGX6_STAAU Unreviewed; 213 AA. AC E5TGX6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSa00_02051; OS Staphylococcus aureus subsp. aureus CGS00. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=543538; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGS00; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWS01000010; EFU23651.1; -; Genomic_DNA. DR ProteinModelPortal; E5TGX6; -. DR EnsemblBacteria; EFU23651; EFU23651; CGSSa00_02051. DR PATRIC; 51826066; VBIStaAur135964_2361. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID E5TN37_STAAU Unreviewed; 213 AA. AC E5TN37; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSa01_03466; OS Staphylococcus aureus subsp. aureus CGS01. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=543539; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGS01; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWT01000015; EFU27317.1; -; Genomic_DNA. DR ProteinModelPortal; E5TN37; -. DR SMR; E5TN37; 4-209. DR PRIDE; E5TN37; -. DR EnsemblBacteria; EFU27317; EFU27317; CGSSa01_03466. DR PATRIC; 51830138; VBIStaAur89039_1705. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID E5TY87_STAAU Unreviewed; 213 AA. AC E5TY87; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSa03_07571; OS Staphylococcus aureus subsp. aureus CGS03. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=543540; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGS03; RA Ehrlich G.D.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWY01000017; EFT84762.1; -; Genomic_DNA. DR ProteinModelPortal; E5TY87; -. DR SMR; E5TY87; 4-209. DR PRIDE; E5TY87; -. DR EnsemblBacteria; EFT84762; EFT84762; CGSSa03_07571. DR PATRIC; 51836792; VBIStaAur24630_2196. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID E5UCX0_ALCXX Unreviewed; 190 AA. AC E5UCX0; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN ORFNames=HMPREF0005_02195; OS Achromobacter xylosoxidans C54. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=562971; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C54; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R., RA Grinwis M., Eshaghurshan C.S., Surette M., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Achromobacter xylosoxidans strain C54."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACRC01000630; EFV83218.1; -; Genomic_DNA. DR EnsemblBacteria; EFV83218; EFV83218; HMPREF0005_02195. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT NON_TER 1 1 SQ SEQUENCE 190 AA; 19950 MW; 0A05F84330827C54 CRC64; EGGMRALQLR RKDVPDRVRA EQARALAPLC RELGVVFLIN DDWRLALEVG ADGAHVGRDD DSLARIRAEA GPDLILGGSS YDDLARAREL LDAGADYIAF GAMFASRVKP DTVRAPLSVL TEARALVEER DAPRPAVVAI GGITPENAAQ VAAAGADSIA VITGLFEAPA IRAAAAACAA PYSINRNLKP // ID E5UKV8_NEIMU Unreviewed; 205 AA. AC E5UKV8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0604_01354; OS Neisseria mucosa C102. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=435832; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C102; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R., RA Grinwis M., Eshaghurshan C.S., Surette M., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Neisseria mucosa strain C102."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACRG01000009; EFV80539.1; -; Genomic_DNA. DR EnsemblBacteria; EFV80539; EFV80539; HMPREF0604_01354. DR PATRIC; 44613600; VBINeiMuc94085_1447. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006162; PPantetheine_attach_site. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22123 MW; 7D17DDC17070ADBD CRC64; MNFPPLKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKTL HGDELKREIE RCVAACQNSA TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIEAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV RQARGTPVVA IGGIDLNNAE DVLATGVSSL AVVRAVTEAE NPEAVVKAFQ ALWDQ // ID E5US20_9BACE Unreviewed; 208 AA. AC E5US20; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9011_01489; OS Bacteroides sp. 3_1_40A. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469593; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_40A; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 3_1_40A."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACRT01000035; EFV68043.1; -; Genomic_DNA. DR ProteinModelPortal; E5US20; -. DR EnsemblBacteria; EFV68043; EFV68043; HMPREF9011_01489. DR PATRIC; 44628149; VBIBacSp86371_1297. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 23078 MW; C08790A5F80A9015 CRC64; MEDKTVELQF ITHFTDTYSY YDSARMALEG GCRWIQLRMK DTPVDEVERE AIRLQGLCKD YGATFIIDDH VELVKKIHAD GVHLGKKDMP VAEARGILGK EFIIGGTANT FDDVKMHYKA GADYIGCGPF RFTTTKKDLS PVLGLEGYRS IILQMKEANI HLPIVAIGGI TLEDIPSIME TGITGIALSG TILRAKDPVA ETKRIMNL // ID E5US29_9BACE Unreviewed; 202 AA. AC E5US29; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=HMPREF9011_01498; OS Bacteroides sp. 3_1_40A. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469593; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_40A; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 3_1_40A."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACRT01000035; EFV68052.1; -; Genomic_DNA. DR ProteinModelPortal; E5US29; -. DR SMR; E5US29; 1-202. DR EnsemblBacteria; EFV68052; EFV68052; HMPREF9011_01498. DR PATRIC; 44628167; VBIBacSp86371_1306. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 22933 MW; 0AE478B2289391FD CRC64; MKLILITPPT YFVEEDKIIT ALFEEGLDTL HLRKPGTAPM FAERLLTLIP EQYHKRIVVH GHFYLKEEYK LKGIHLNGRN PNLPEGYKGH VSCSCHSLDE VKERKSSCDY VFLSPVFNSI SKLNYNSAYT AEELRTAAKA GIIDKKVIAL GGIDEENLLE VKDFGFGGAA ILGALWNKFD ACTDRDYRCV IEHFRKLRDL AD // ID E5V2P5_9BACL Unreviewed; 215 AA. AC E5V2P5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0432_00651; OS Gemella morbillorum M424. OC Bacteria; Firmicutes; Bacilli; Bacillales; OC Bacillales Family XI. Incertae Sedis; Gemella. OX NCBI_TaxID=562982; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M424; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Sibley C., Field T.R., Grinwis M., RA Eshaghurshan C., Surette M., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Gemella moribillum strain M424."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACRX01000009; EFV35618.1; -; Genomic_DNA. DR EnsemblBacteria; EFV35618; EFV35618; HMPREF0432_00651. DR PATRIC; 44636489; VBIGemMor7618_0658. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23565 MW; 2E1897023DF0EC4E CRC64; MFNKELLKLY FICGTTTCLG KDLYTVVEDA LKGGITLFQF REKGKGALEG KEKVELAVKI QDLCKKYNVP FIVNDDIELA LEIDADGVHV GQGDGNVEKI RKLLPDKIIG LSVGNEEELR ESKIEFVDYI GVGPVHSTIS KNDAGGAIGY KGLKKMRKLA PEIPIVAIGG IKKEDIKNIA AIGVEGVSII SAISYSESIK QTVEQMINEY KNYVE // ID E5V8T3_9BACE Unreviewed; 202 AA. AC E5V8T3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=HMPREF1007_01166; OS Bacteroides sp. 4_1_36. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457393; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_1_36; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Sibley C., Strauss J., RA Daigneault M., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 4_1_36."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTC01000048; EFV26742.1; -; Genomic_DNA. DR ProteinModelPortal; E5V8T3; -. DR EnsemblBacteria; EFV26742; EFV26742; HMPREF1007_01166. DR PATRIC; 44641054; VBIBacSp136900_1421. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23273 MW; 7B69F50F0095840E CRC64; MKLIVVTAPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHKRIITH EHFYLQEEFS LMGIHLNTRN PKEPHDYSGH ISCTCHSLDE VQNKKHFYDY LFLSPIYNCI TKSGVTSGFT AEELRQAGKS KVIDSRVMAL GGITPDNILE IKDYGFGGAV VMGDLWNKFN ACTDRDYLEV IRHFKKLKKM AD // ID E5VCA7_9BACE Unreviewed; 240 AA. AC E5VCA7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1007_02391; OS Bacteroides sp. 4_1_36. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457393; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_1_36; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Sibley C., Strauss J., RA Daigneault M., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 4_1_36."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTC01000086; EFV25555.1; -; Genomic_DNA. DR EnsemblBacteria; EFV25555; EFV25555; HMPREF1007_02391. DR PATRIC; 44643693; VBIBacSp136900_2505. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 63 67 HMP-PP binding (By similarity). FT REGION 160 162 THZ-P binding (By similarity). FT METAL 96 96 Magnesium (By similarity). FT METAL 115 115 Magnesium (By similarity). FT BINDING 95 95 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 HMP-PP (By similarity). FT BINDING 196 196 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 240 AA; 26791 MW; CA80784A3008985C CRC64; MDKMHPEGIH AHHHYQSSLR RVRKMKDERL KNGGMQFITH YTERYSYLDA ARMALEGGCR WVQLRMKDTP VETIEPVALE VQALCRQYGA TFIIDDHVEL AKKLHADGVH LGKKDMPIAD ARRILGAEYI IGGTANTFED VLQHYKAGAD YIGCGPFRYT TTKKNLSPIL GLEGYTAIIH RMQEKDIHLP IVAIGGITIA DIPAVMQTGV SGIALSGTVL HADSPADEMK RIISLMENEK // ID E5VCB2_9BACE Unreviewed; 197 AA. AC E5VCB2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF1007_02396; OS Bacteroides sp. 4_1_36. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457393; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_1_36; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Sibley C., Strauss J., RA Daigneault M., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. strain 4_1_36."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTC01000086; EFV25560.1; -; Genomic_DNA. DR EnsemblBacteria; EFV25560; EFV25560; HMPREF1007_02396. DR PATRIC; 44643703; VBIBacSp136900_2510. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 197 AA; 21853 MW; 46353D30CE5416CF CRC64; MKLIVITTPQ FFEGEAAAVT SLFQNGLEIL HLRKPGASAE EMEYFLRQLP MEYMPRIVTH EQFQLASVFG LKGIHLNGRN PQIPFGYKGH ISCSCHSLEE VLKHKSDCSY VFLSPIYDSI SKEGYSSAYS CDTLKKAQQA GIIDSNVMAL GGISLEHLPE IAVLGFGGAV LLGDIWQQAK EDFIPHFLHL KQLSSPL // ID E5VG87_9FIRM Unreviewed; 213 AA. AC E5VG87; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0996_00056; OS Lachnospiraceae bacterium 5_1_63FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658089; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_63FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Ambrose C., Strauss J., RA Daigneault M., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium strain 5_1_63FAA."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTS01000004; EFV17911.1; -; Genomic_DNA. DR EnsemblBacteria; EFV17911; EFV17911; HMPREF0996_00056. DR PATRIC; 44646657; VBILacBac124763_0055. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23400 MW; D6E38888A0345A26 CRC64; MRVNADAMTL YAVTDRTWVE DTTLMDQVKE ALEGGITFLQ LREKHLSKEE FIKEAREMKE LSKEYKVPFV INDNIEVALA VDADGVHIGQ DDMSVEEARK LLGEDKIIGV SAHNVEEAIK AQKGGADYLG VGAVCATSTK KDANVVSKEE IKKICHTVEI PVVAIGGIKK ENIKTLEGTD VDGVAVVSAI FAAKDIKKDT KQLRSLVEEM KQK // ID E5VIL1_9FIRM Unreviewed; 185 AA. AC E5VIL1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0996_00872; OS Lachnospiraceae bacterium 5_1_63FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658089; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_63FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Ambrose C., Strauss J., RA Daigneault M., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium strain 5_1_63FAA."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTS01000016; EFV17296.1; -; Genomic_DNA. DR EnsemblBacteria; EFV17296; EFV17296; HMPREF0996_00872. DR PATRIC; 44648384; VBILacBac124763_0903. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 185 AA; 20617 MW; 1D5C7623A2CD670D CRC64; MNKPCFIAVT NRNLCKRPFF DVIEDLSKKD VKTIVLREKD LSEEEYYEIA EKCKEICDRN GASLTIHNFI DVARRLGIKK IHLPYPVFLK EAGNLSDFES VSTSIHKPEE AIKAQKLGVD FVFAGHVFVT DCKKGLPPRG LEFLTDVVNA VKIPVYGIGG INEENIAKIM ECGAAGGCMM SGFMK // ID E5VQ05_9FIRM Unreviewed; 192 AA. AC E5VQ05; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF1011_00077; OS Anaerostipes sp. 3_2_56FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Anaerostipes. OX NCBI_TaxID=665937; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_2_56FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Ambrose C., Strauss J., RA Daigneault M., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Anaerostipes sp. strain 3_2_56FAA."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWB01000006; EFV24066.1; -; Genomic_DNA. DR ProteinModelPortal; E5VQ05; -. DR EnsemblBacteria; EFV24066; EFV24066; HMPREF1011_00077. DR PATRIC; 44653190; VBIAnaSp142028_0742. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 192 AA; 20971 MW; D50C446C5CA6D8F4 CRC64; MNQEWIAVTD RKQCGGEFLK TVQTLAGQGL KTIILREKDL SEEEYGELAA RCMEICRKTG ASLTLHKYFH AARGLGADRI HLPYPVFREN AGKIDQHIHV STSIHAPGEA VEAERMGAEF VIAGHIFQTD CKKGVPPRGL EFLRETVQSV SIPVYAIGGI TPYNIGDVLD TGAAGGCMMS GFMKSPKIID KP // ID E5VSN7_9FIRM Unreviewed; 216 AA. AC E5VSN7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1011_01010; OS Anaerostipes sp. 3_2_56FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Anaerostipes. OX NCBI_TaxID=665937; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_2_56FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Ambrose C., Strauss J., RA Daigneault M., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Anaerostipes sp. strain 3_2_56FAA."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWB01000036; EFV23174.1; -; Genomic_DNA. DR ProteinModelPortal; E5VSN7; -. DR EnsemblBacteria; EFV23174; EFV23174; HMPREF1011_01010. DR PATRIC; 44655213; VBIAnaSp142028_1681. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23648 MW; 8170BE8B714F2173 CRC64; MQRLRVESEA MTLYAVTDSA WTGGQTLMEQ VKDALDGGIT FLQLREKDLE YDAFLQEAIE MAKLSRKYGV PFVINDEVEI ALKCGADGVH VGQEDMACRN ARDILGPDKI IGVSVHNVKE ALKAQADGAD YLGLGAVKAT PTKTDARVVE FEEIKKVCDA VNIPVVAIGG IKKDNMMELK GSHVDGIAVV SAIFGAENIR KETEELRKKA EELRIR // ID E5W4S8_9BACI Unreviewed; 203 AA. AC E5W4S8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=TenI protein; GN ORFNames=HMPREF1012_01800; OS Bacillus sp. BT1B_CT2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=665958; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BT1B_CT2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA McDonald J., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacillus sp. strain BT1B_CT2."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWC01000005; EFV71920.1; -; Genomic_DNA. DR ProteinModelPortal; E5W4S8; -. DR SMR; E5W4S8; 1-191. DR EnsemblBacteria; EFV71920; EFV71920; HMPREF1012_01800. DR PATRIC; 44664318; VBIBacSp145545_1960. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 203 AA; 22376 MW; 3BE3AB481BF14203 CRC64; MHLHAITDDK HSVEELSAKI ISIHDAVDFI HIRERSKKVS EISSLIDRLA EEGVDKRKLI INDRVDIALF HHIHRVQLPS HGFSVKSVRS RFPHLKIGKS VHSPEEAVQA ETEGADYVLF GHIFETDCKK GRKGRGALSL AEVKAAVRIP VIAIGGITEQ RLAEVKMADG IAVMSGIFSH DRPNEAAARL ASLAKGDSYE KAL // ID E5W9A6_9BACI Unreviewed; 224 AA. AC E5W9A6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1012_03465; OS Bacillus sp. BT1B_CT2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=665958; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BT1B_CT2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA McDonald J., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacillus sp. strain BT1B_CT2."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWC01000017; EFV70654.1; -; Genomic_DNA. DR EnsemblBacteria; EFV70654; EFV70654; HMPREF1012_03465. DR PATRIC; 44668118; VBIBacSp145545_3844. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23620 MW; 38CCB4D4F480DA91 CRC64; MTRVSEEAMK DLLSVYFIMG SNNTAGDPLT VIEKALKGGA TLFQFREKGE GALKAGDQTA FARQVQALCK QFNVPFIIND DVELALELDA DGVHIGQDDD KAADVRARIG DKILGVSAHT LEEVLKAEKD GADYIGAGPV YPTETKRDTK AVQGVSLIQE IRRQGIGIPV VGIGGITVEN CVPVIEAGAD GISVISAISK AADPKQAAEA FSEKVQAAKQ SAHS // ID E5WMJ0_9BACI Unreviewed; 222 AA. AC E5WMJ0; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1013_03675; OS Bacillus sp. 2_A_57_CT2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=665959; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_A_57_CT2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWD01000055; EFV76037.1; -; Genomic_DNA. DR ProteinModelPortal; E5WMJ0; -. DR EnsemblBacteria; EFV76037; EFV76037; HMPREF1013_03675. DR PATRIC; 44678604; VBIBacSp146025_4333. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23545 MW; C213BE7053ACB50B CRC64; MAVNPQAMRS LLKVYFIMGS TNCCQNPEDV LQAAIKGGIT LFQFREKGAG CLHGKEKESL AKKLQAICKQ SNIPFIVNDD IELAVKINAD GVHIGQDDEA ADVVRRKIGS KILGVSVHSM QEAETAIRQG ADYIGIGPIY PTSTKADAKA VQGLTFLTEL RSADIQIPVV GIGGITSENA SPLIEAGADG VSVISAISQA DSPEKAAAKL YDAVNRIMRN AH // ID E5WQ22_9BACI Unreviewed; 203 AA. AC E5WQ22; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1013_04664; OS Bacillus sp. 2_A_57_CT2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=665959; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_A_57_CT2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWD01000066; EFV75231.1; -; Genomic_DNA. DR ProteinModelPortal; E5WQ22; -. DR EnsemblBacteria; EFV75231; EFV75231; HMPREF1013_04664. DR PATRIC; 44680880; VBIBacSp146025_5142. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT REGION 127 129 THZ-P binding (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 101 101 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 157 157 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 22179 MW; 8367376A4C279B91 CRC64; MRKQLHVISD GKLSLEAFAE IAGEVEPFAD RFHLREKHRT SRELYEGVKL LCNEGIPIHK IVINDRVDVA WACKTGVHLA FHSLPVRVVK THFLDMPIGC SVHSPEEAEE AAKQGADYIL FGHIFETDSK KGIPPRGTGS LEALKKAVEI PVMAIGGIKP EKVPEVLEAG ADGIAVMSGI LQAKDPAEAA KLFSKKLNEE GEK // ID E5X2Z8_9BACE Unreviewed; 212 AA. AC E5X2Z8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1016_03305; OS Bacteroides eggerthii 1_2_48FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=665953; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_2_48FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Ambrose C., Strauss J., RA Daigneault M., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides eggerthii strain 1_2_48FAA."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWG01000040; EFV28584.1; -; Genomic_DNA. DR EnsemblBacteria; EFV28584; EFV28584; HMPREF1016_03305. DR PATRIC; 44690721; VBIBacEgg142087_3509. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23641 MW; 2AB26F6A3411AF07 CRC64; MKTVQFITHY TEKYSYLDSA RMALKGGCRW IQLRMKDAGK EEIVSVAMEL RNLCNDCGAI FIIDDHVELV REIGADGVHL GKNDMSVAEA RRILGDEYII GGTANTYEDV KKHWLNGVNY IGCGPFRYTT TKQKLSPILG LEGYKEIIRK MQEEKICHLP VVAIGGITFA DIPAIMQTGV TGIALSGTVL RADNPVEEMR KILAVINQTD NY // ID E5X303_9BACE Unreviewed; 197 AA. AC E5X303; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF1016_03310; OS Bacteroides eggerthii 1_2_48FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=665953; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_2_48FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Ambrose C., Strauss J., RA Daigneault M., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides eggerthii strain 1_2_48FAA."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWG01000040; EFV28589.1; -; Genomic_DNA. DR EnsemblBacteria; EFV28589; EFV28589; HMPREF1016_03310. DR PATRIC; 44690731; VBIBacEgg142087_3514. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 197 AA; 21752 MW; B47E9FBC9DB09568 CRC64; MKLIVITQPE FFEDEAAAIT SLFDAGLEIL HLRKPGASYE DMDKLLRRLP AEYMERIVTH DHFGLASERN LKGVHLNRRN PAAPAGFTGH VSRSCHSLEE VAEYKAACNY VFLSPIYNSI SKEGYAAAYA FDDLQKAHRA GIIDSGVMAL GGVTAEHLPE INSLGFGGVG LLGDIWQRTG TDFINHFREL LRSASVF // ID E5XAC2_9ACTN Unreviewed; 216 AA. AC E5XAC2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1023_02013; OS Eggerthella sp. 1_3_56FAA. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Eggerthella. OX NCBI_TaxID=665943; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_3_56FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Ambrose C., Strauss J., RA Daigneault M., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Eggerthella sp. strain 1_3_56FAA."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWN01000100; EFV32677.1; -; Genomic_DNA. DR ProteinModelPortal; E5XAC2; -. DR EnsemblBacteria; EFV32677; EFV32677; HMPREF1023_02013. DR PATRIC; 44696309; VBIEggSp144542_2088. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22147 MW; 474E0E7B75D894D0 CRC64; MYPRENLRRA MALYAVTDRA WLGERTLSAC VEEALAGGAT FVQLREKDAP QAEVVLRARA LAPLCREAGV PFVVDDDVEA ARIAGVDGVH VGQDDAACVE AREKLGPDAI VGVSVQTVEQ ALVAQADGAD YLGVGAVFGT PTKPDAADVG TDGLAAICAA VDIPVVAIGG LNERTIPELA GTGADGAAVV SAIFAAEDIE EETRRLRAAV QAALGA // ID E5XCM2_9ACTN Unreviewed; 196 AA. AC E5XCM2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF1023_02813; OS Eggerthella sp. 1_3_56FAA. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Eggerthella. OX NCBI_TaxID=665943; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_3_56FAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Ambrose C., Strauss J., RA Daigneault M., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Eggerthella sp. strain 1_3_56FAA."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWN01000127; EFV31906.1; -; Genomic_DNA. DR EnsemblBacteria; EFV31906; EFV31906; HMPREF1023_02813. DR PATRIC; 44698036; VBIEggSp144542_2794. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 20856 MW; 2BAA1DE751947097 CRC64; MFVTDRLRCA LPLPQQTAFL AESGAIDAVI LREKDLDDAA YELLAAEMAA VCARCGIAFV AHAHVEAARR LGCAAVHLPL PLLRAQGRPD GFAWVGTNVH EADEVAEAEV LGADVLVASP VFAPSCKPAS TARGLPFLRA VLDRAHAPVF ALGGITDENE RLIREAGAAG ACRMADYARR RGVRQAAPCK YERSRG // ID E5XN52_9ACTO Unreviewed; 219 AA. AC E5XN52; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9336_00922; OS Segniliparus rugosus ATCC BAA-974. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Segniliparaceae; Segniliparus. OX NCBI_TaxID=679197; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-974; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C., RA Wortman J., Nusbaum C., Birren B.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-974; RX PubMed=22675588; RA Earl A.M., Desjardins C.A., Fitzgerald M.G., Arachchi H.M., Zeng Q., RA Mehta T., Griggs A., Birren B.W., Toney N.C., Carr J., Posey J., RA Butler W.R.; RT "High quality draft genome sequence of Segniliparus rugosus CDC RT 945(T)= (ATCC BAA-974(T))."; RL Stand. Genomic Sci. 5:389-397(2011). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-974; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Walker B., RA Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Segniliparus rugosus CDC 945."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZI02000003; EFV14229.1; -; Genomic_DNA. DR ProteinModelPortal; E5XN52; -. DR EnsemblBacteria; EFV14229; EFV14229; HMPREF9336_00922. DR PATRIC; 44705913; VBISegRug139851_1049. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23217 MW; 913489598A693E34 CRC64; MDTREARLAR LAQARLYVCV DARRDRGDLV AFAEAALSGG VDLLQLRDKS KQDPLEAGDE LALLARLKQS TSAHGALLAV NDRADVALAS GADVLHLGQR DLPVGIARRI LGPDVLIGRS THSPEQARAA IEDPDVDYFC VGPCWTTPTK PGRAAVGLEL VAQVAALAPA KPWFAIGGVD LDRLPQVRDA GARRVVVVRA VTEAKDPKAS AQALRAELA // ID E5XVL7_9BIFI Unreviewed; 917 AA. AC E5XVL7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE SubName: Full=ThiC family protein; GN ORFNames=HMPREF0177_00019; OS Bifidobacterium sp. 12_1_47BFAA. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=469594; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=12_1_47BFAA; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Ambrose C., Strauss J., RA McDonald J., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Bifidobacterium sp. strain 12_1_47BFAA."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADCN01000001; EFV38337.1; -; Genomic_DNA. DR EnsemblBacteria; EFV38337; EFV38337; HMPREF0177_00019. DR PATRIC; 44711260; VBIBifSp48270_0019. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100278 MW; 76CDE11FBEB252F8 CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLAGTKA AGWFVVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRHRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID E5YBC8_BILWA Unreviewed; 214 AA. AC E5YBC8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0179_03501; OS Bilophila wadsworthia 3_1_6. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Bilophila. OX NCBI_TaxID=563192; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_6; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Sibley C., Ambrose C.E., RA Strauss J., Daigneault M., Haas B., Nusbaum C., Birren B.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_6; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C., Strauss J., RA Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bilophila wadsworthia 3_1_6."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADCP02000001; EFV42690.1; -; Genomic_DNA. DR ProteinModelPortal; E5YBC8; -. DR EnsemblBacteria; EFV42690; EFV42690; HMPREF0179_03501. DR PATRIC; 44723594; VBIBilWad76794_3928. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23050 MW; 5E68ADBB83BB8F51 CRC64; MPRLLPGTSP ETDLYALTDD ELSLGRPAVE VAKALLDSGI KILQYREKEK KAGQMLKECL ELRRLTREAG ACFIVNDHVD IAVLCEADGV HVGQEDLPVE AVRRLVGPDM IIGLSTHTPD QARAAVASGA DYIGVGPIYP TQTKKDVCAP VTLDYLDWVV ANITLPFVAI GGIKRHNIAD VIAHGARCCA IVSEFVSAPD IPARVAEVRS AMKK // ID E5YSS7_9BACL Unreviewed; 211 AA. AC E5YSS7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PVOR_07740; OS Paenibacillus vortex V453. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=715225; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=V453; RX PubMed=21167037; DOI=10.1186/1471-2164-11-710; RA Sirota-Madi A., Olender T., Helman Y., Ingham C., Brainis I., Roth D., RA Hagi E., Brodsky L., Leshkowitz D., Galatenko V., Nikolaev V., RA Mugasimangalam R.C., Bransburg-Zabary S., Gutnick D.L., Lancet D., RA Ben-Jacob E.; RT "Genome sequence of the pattern forming Paenibacillus vortex bacterium RT reveals potential for thriving in complex environments."; RL BMC Genomics 11:710-710(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHJ01000014; EFU42168.1; -; Genomic_DNA. DR EnsemblBacteria; EFU42168; EFU42168; PVOR_07740. DR PATRIC; 44736078; VBIPaeVor147550_1536. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22162 MW; A7F4C50813EF5355 CRC64; MMRQHLRMYL VLGSVNCIAE PEWVVQEAIV GGATMVQFRE KGRAALTGEP RIQLARRIRN LCRQAGVPFI VNDDVGLALK LNADGVHIGQ DDESAASVRE RIGKRILGVS AHTIEEARRA ILHGADYIGV GPIYPTVSKE DAKPVQGPGL LRAMRAAGID MPIVGIGGIT AEKAEEVVGA GADGVAVISA VTAAGSVRDA AASIRAKADV I // ID E5YTC7_9BACL Unreviewed; 206 AA. AC E5YTC7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PVOR_08830; OS Paenibacillus vortex V453. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=715225; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=V453; RX PubMed=21167037; DOI=10.1186/1471-2164-11-710; RA Sirota-Madi A., Olender T., Helman Y., Ingham C., Brainis I., Roth D., RA Hagi E., Brodsky L., Leshkowitz D., Galatenko V., Nikolaev V., RA Mugasimangalam R.C., Bransburg-Zabary S., Gutnick D.L., Lancet D., RA Ben-Jacob E.; RT "Genome sequence of the pattern forming Paenibacillus vortex bacterium RT reveals potential for thriving in complex environments."; RL BMC Genomics 11:710-710(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHJ01000014; EFU42368.1; -; Genomic_DNA. DR EnsemblBacteria; EFU42368; EFU42368; PVOR_08830. DR PATRIC; 44736517; VBIPaeVor147550_1752. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22279 MW; 244B2987D7B5078D CRC64; MKDFRLYAIT GEQFHPGRDM LDVMEQAILG GVDIIQLRDK KSPKAEVLAK AKALRKLTSR YDVTFIVNDY VDIALEADAD GIHLGQGDMP LTEARRLVGS KIIGISTHAI EEALLAESQG ADYIGVGPVY RTATKEDVVD PVTEAYVREV AHAIQIPFVA IGGIKLHNVD QVLMAGATRI CAVSEIVGSS NVKGTCEAFI SKLEAK // ID E5Z6G3_CAMJU Unreviewed; 210 AA. AC E5Z6G3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CSQ_0527; OS Campylobacter jejuni subsp. jejuni DFVF1099. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=691336; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFVF1099; RA Takamiya Wik M., Ozen A.I., Rasmussen M., Gilbert T., Ussery D.W., RA Knoechel S.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFVF1099; RX PubMed=21914871; DOI=10.1128/JB.05753-11; RA Takamiya M., Ozen A., Rasmussen M., Alter T., Gilbert T., Ussery D.W., RA Knochel S.; RT "Genome Sequences of Two Stress-Tolerant Campylobacter jejuni Poultry RT Strains, 305 and DFVF1099."; RL J. Bacteriol. 193:5546-5547(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHK01000009; EFV07338.1; -; Genomic_DNA. DR EnsemblBacteria; EFV07338; EFV07338; CSQ_0527. DR PATRIC; 51866437; VBICamJej151155_0449. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22998 MW; C812FDED06C6616C CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID E5Z6M2_CAMJU Unreviewed; 73 AA. AC E5Z6M2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-MAR-2014, entry version 19. DE SubName: Full=Uncharacterized protein; GN ORFNames=CSQ_0034; OS Campylobacter jejuni subsp. jejuni DFVF1099. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=691336; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFVF1099; RA Takamiya Wik M., Ozen A.I., Rasmussen M., Gilbert T., Ussery D.W., RA Knoechel S.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFVF1099; RX PubMed=21914871; DOI=10.1128/JB.05753-11; RA Takamiya M., Ozen A., Rasmussen M., Alter T., Gilbert T., Ussery D.W., RA Knochel S.; RT "Genome Sequences of Two Stress-Tolerant Campylobacter jejuni Poultry RT Strains, 305 and DFVF1099."; RL J. Bacteriol. 193:5546-5547(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHK01000011; EFV07272.1; -; Genomic_DNA. DR EnsemblBacteria; EFV07272; EFV07272; CSQ_0034. DR PATRIC; 51866565; VBICamJej151155_0509. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 73 AA; 8479 MW; AEF09DD3E3B02DB8 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFLI GSV // ID E5Z6M3_CAMJU Unreviewed; 126 AA. AC E5Z6M3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine monophosphate synthase/TENI family protein; DE EC=2.5.1.3; GN ORFNames=CSQ_0035; OS Campylobacter jejuni subsp. jejuni DFVF1099. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=691336; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFVF1099; RA Takamiya Wik M., Ozen A.I., Rasmussen M., Gilbert T., Ussery D.W., RA Knoechel S.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFVF1099; RX PubMed=21914871; DOI=10.1128/JB.05753-11; RA Takamiya M., Ozen A., Rasmussen M., Alter T., Gilbert T., Ussery D.W., RA Knochel S.; RT "Genome Sequences of Two Stress-Tolerant Campylobacter jejuni Poultry RT Strains, 305 and DFVF1099."; RL J. Bacteriol. 193:5546-5547(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHK01000011; EFV07273.1; -; Genomic_DNA. DR EnsemblBacteria; EFV07273; EFV07273; CSQ_0035. DR PATRIC; 51866567; VBICamJej151155_0510. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 126 AA; 14596 MW; CA4DC659B44633F5 CRC64; MGHRYFHAPL SLLRKEPKLT KYFHILGTSV HSKEELLEAM SYKVNYAFVG HIFESSCKMG LEPKGIDFLK SLLEFSQIPL YAIGGINAQN IENFKDINVV GVCMREILMK EKDLKKYLLE CRQNLR // ID E5ZB71_CAMJU Unreviewed; 210 AA. AC E5ZB71; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CSS_0272; OS Campylobacter jejuni subsp. jejuni 305. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=691337; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=305; RA Takamiya Wik M., Ozen A.I., Rasmussen M., Gilbert T., Alter T., RA Ussery D.W., Knoechel S.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=305; RX PubMed=21914871; DOI=10.1128/JB.05753-11; RA Takamiya M., Ozen A., Rasmussen M., Alter T., Gilbert T., Ussery D.W., RA Knochel S.; RT "Genome Sequences of Two Stress-Tolerant Campylobacter jejuni Poultry RT Strains, 305 and DFVF1099."; RL J. Bacteriol. 193:5546-5547(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHL01000043; EFV09693.1; -; Genomic_DNA. DR ProteinModelPortal; E5ZB71; -. DR EnsemblBacteria; EFV09693; EFV09693; CSS_0272. DR PATRIC; 51870167; VBICamJej148309_0204. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23001 MW; 753C83D43B0EB44A CRC64; MKNKLDLSLY LVATKGSKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID E5ZBI6_CAMJU Unreviewed; 201 AA. AC E5ZBI6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine monophosphate synthase/TENI family protein; DE EC=2.5.1.3; GN ORFNames=CSS_0380; OS Campylobacter jejuni subsp. jejuni 305. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=691337; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=305; RA Takamiya Wik M., Ozen A.I., Rasmussen M., Gilbert T., Alter T., RA Ussery D.W., Knoechel S.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=305; RX PubMed=21914871; DOI=10.1128/JB.05753-11; RA Takamiya M., Ozen A., Rasmussen M., Alter T., Gilbert T., Ussery D.W., RA Knochel S.; RT "Genome Sequences of Two Stress-Tolerant Campylobacter jejuni Poultry RT Strains, 305 and DFVF1099."; RL J. Bacteriol. 193:5546-5547(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHL01000065; EFV09583.1; -; Genomic_DNA. DR EnsemblBacteria; EFV09583; EFV09583; CSS_0380. DR PATRIC; 51870393; VBICamJej148309_0303. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23404 MW; FCB55F8B19041BEC CRC64; MWGKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID E5ZHI1_CAMJU Unreviewed; 201 AA. AC E5ZHI1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Thiamine monophosphate synthase/TENI family protein; DE EC=2.5.1.3; GN ORFNames=CSU_0320; OS Campylobacter jejuni subsp. jejuni 327. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=691338; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=327; RA Takamiya Wik M., Ozen A.I., Rasmussen M., Gilbert T., Alter T., RA Knoechel S.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=327; RX PubMed=21677848; RA Takamiya M., Ozen A., Rasmussen M., Alter T., Gilbert T., Ussery D.W., RA Knochel S.; RT "Genome Sequence of Campylobacter jejuni strain 327, a strain isolated RT from a turkey slaughterhouse."; RL Stand. Genomic Sci. 4:113-122(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHM01000015; EFV11117.1; -; Genomic_DNA. DR ProteinModelPortal; E5ZHI1; -. DR EnsemblBacteria; EFV11117; EFV11117; CSU_0320. DR PATRIC; 51874914; VBICamJej152004_0293. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23486 MW; 61622900362A43FB CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICVKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG IDFLKSLLEF SQIPLYAIGG INTQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID E5ZHM4_CAMJU Unreviewed; 210 AA. AC E5ZHM4; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CSU_0365; OS Campylobacter jejuni subsp. jejuni 327. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=691338; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=327; RA Takamiya Wik M., Ozen A.I., Rasmussen M., Gilbert T., Alter T., RA Knoechel S.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=327; RX PubMed=21677848; RA Takamiya M., Ozen A., Rasmussen M., Alter T., Gilbert T., Ussery D.W., RA Knochel S.; RT "Genome Sequence of Campylobacter jejuni strain 327, a strain isolated RT from a turkey slaughterhouse."; RL Stand. Genomic Sci. 4:113-122(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHM01000015; EFV11160.1; -; Genomic_DNA. DR EnsemblBacteria; EFV11160; EFV11160; CSU_0365. DR PATRIC; 51875007; VBICamJej152004_0338. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23096 MW; 3DBC66D294B76B0A CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKVTPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKEVLD ELKGINLSGV AVVRAIMDTK DAFLAAKELK RKIYENLPLK // ID E5ZRB4_ECOLX Unreviewed; 211 AA. AC E5ZRB4; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9539_01704; OS Escherichia coli MS 110-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749536; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 110-3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTW01000115; EFU47737.1; -; Genomic_DNA. DR ProteinModelPortal; E5ZRB4; -. DR SMR; E5ZRB4; 9-208. DR EnsemblBacteria; EFU47737; EFU47737; HMPREF9539_01704. DR PATRIC; 47823652; VBIEscCol159911_1532. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E6A5C2_ECOLX Unreviewed; 211 AA. AC E6A5C2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9544_01196; OS Escherichia coli MS 153-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749541; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 153-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTX01000108; EFU53701.1; -; Genomic_DNA. DR ProteinModelPortal; E6A5C2; -. DR SMR; E6A5C2; 9-208. DR EnsemblBacteria; EFU53701; EFU53701; HMPREF9544_01196. DR PATRIC; 48581530; VBIEscCol155243_1030. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23030 MW; D9436839F2B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSTIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E6AI07_ECOLX Unreviewed; 211 AA. AC E6AI07; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9545_00191; OS Escherichia coli MS 16-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749542; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 16-3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUA01000027; EFU59961.1; -; Genomic_DNA. DR EnsemblBacteria; EFU59961; EFU59961; HMPREF9545_00191. DR PATRIC; 47831290; VBIEscCol151359_0161. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23000 MW; CC43679342B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E6B3N9_ECOLX Unreviewed; 211 AA. AC E6B3N9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EC3431_2175; OS Escherichia coli 3431. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670892; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3431; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUM01000089; EFU97963.1; -; Genomic_DNA. DR EnsemblBacteria; EFU97963; EFU97963; EC3431_2175. DR PATRIC; 47867006; VBIEscCol139805_2261. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22957 MW; F900772C696C311C CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA GVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E6BRU3_ECOLX Unreviewed; 211 AA. AC E6BRU3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9350_05150; OS Escherichia coli MS 85-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=679202; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 85-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWQ01000045; EFU33034.1; -; Genomic_DNA. DR ProteinModelPortal; E6BRU3; -. DR SMR; E6BRU3; 10-208. DR EnsemblBacteria; EFU33034; EFU33034; HMPREF9350_05150. DR PATRIC; 47940162; VBIEscCol146587_4705. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E6BWV8_PROAA Unreviewed; 217 AA. AC E6BWV8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9590_02320; OS Propionibacterium acnes HL059PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765092; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL059PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXS01000008; EFT71622.1; -; Genomic_DNA. DR ProteinModelPortal; E6BWV8; -. DR EnsemblBacteria; EFT71622; EFT71622; HMPREF9590_02320. DR PATRIC; 51988359; VBIProAcn164385_0767. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E6C050_PROAA Unreviewed; 216 AA. AC E6C050; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9590_00597; OS Propionibacterium acnes HL059PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765092; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL059PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXS01000014; EFT70360.1; -; Genomic_DNA. DR ProteinModelPortal; E6C050; -. DR EnsemblBacteria; EFT70360; EFT70360; HMPREF9590_00597. DR PATRIC; 51989947; VBIProAcn164385_1537. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E6C3H6_PROAA Unreviewed; 217 AA. AC E6C3H6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9602_01127; OS Propionibacterium acnes HL030PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765104; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL030PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXZ01000012; EFT81982.1; -; Genomic_DNA. DR ProteinModelPortal; E6C3H6; -. DR EnsemblBacteria; EFT81982; EFT81982; HMPREF9602_01127. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E6C831_PROAA Unreviewed; 216 AA. AC E6C831; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9602_02085; OS Propionibacterium acnes HL030PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765104; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL030PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXZ01000057; EFT80461.1; -; Genomic_DNA. DR EnsemblBacteria; EFT80461; EFT80461; HMPREF9602_02085. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22572 MW; 68DE5AAB2FB1D32B CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVVTVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E6CAB2_PROAA Unreviewed; 217 AA. AC E6CAB2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9601_00184; OS Propionibacterium acnes HL030PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765103; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL030PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYB01000013; EFT79575.1; -; Genomic_DNA. DR ProteinModelPortal; E6CAB2; -. DR EnsemblBacteria; EFT79575; EFT79575; HMPREF9601_00184. DR PATRIC; 52018037; VBIProAcn164108_0402. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E6CGF8_PROAA Unreviewed; 216 AA. AC E6CGF8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9601_02001; OS Propionibacterium acnes HL030PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765103; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL030PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYB01000065; EFT77514.1; -; Genomic_DNA. DR EnsemblBacteria; EFT77514; EFT77514; HMPREF9601_02001. DR PATRIC; 52022268; VBIProAcn164108_2443. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22504 MW; D68C19AB366F1623 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAGMRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTAP KSSARELAEA WRTAKE // ID E6CHF6_PROAA Unreviewed; 217 AA. AC E6CHF6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9599_01692; OS Propionibacterium acnes HL050PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765101; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL050PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYC01000006; EFT76966.1; -; Genomic_DNA. DR ProteinModelPortal; E6CHF6; -. DR EnsemblBacteria; EFT76966; EFT76966; HMPREF9599_01692. DR PATRIC; 52022967; VBIProAcn160350_0300. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E6CMK5_PROAA Unreviewed; 216 AA. AC E6CMK5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9599_01158; OS Propionibacterium acnes HL050PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765101; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL050PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYC01000052; EFT75309.1; -; Genomic_DNA. DR ProteinModelPortal; E6CMK5; -. DR EnsemblBacteria; EFT75309; EFT75309; HMPREF9599_01158. DR PATRIC; 52026526; VBIProAcn160350_1989. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22548 MW; D68AAF1B366F1623 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAGMRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E6CQT7_PROAA Unreviewed; 217 AA. AC E6CQT7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9583_00732; OS Propionibacterium acnes HL038PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765085; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL038PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYD01000021; EFT69016.1; -; Genomic_DNA. DR ProteinModelPortal; E6CQT7; -. DR EnsemblBacteria; EFT69016; EFT69016; HMPREF9583_00732. DR PATRIC; 52028794; VBIProAcn164540_0680. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E6CTC6_PROAA Unreviewed; 216 AA. AC E6CTC6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9583_01707; OS Propionibacterium acnes HL038PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765085; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL038PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYD01000044; EFT68096.1; -; Genomic_DNA. DR EnsemblBacteria; EFT68096; EFT68096; HMPREF9583_01707. DR PATRIC; 52030571; VBIProAcn164540_1532. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22628 MW; CC3F100B367E1034 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALYG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E6CYJ5_PROAA Unreviewed; 217 AA. AC E6CYJ5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9582_00540; OS Propionibacterium acnes HL060PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765084; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL060PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYE01000017; EFT66546.1; -; Genomic_DNA. DR ProteinModelPortal; E6CYJ5; -. DR EnsemblBacteria; EFT66546; EFT66546; HMPREF9582_00540. DR PATRIC; 52034177; VBIProAcn161541_0744. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E6D1Y1_PROAA Unreviewed; 216 AA. AC E6D1Y1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9582_00975; OS Propionibacterium acnes HL060PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765084; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL060PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYE01000044; EFT65138.1; -; Genomic_DNA. DR ProteinModelPortal; E6D1Y1; -. DR EnsemblBacteria; EFT65138; EFT65138; HMPREF9582_00975. DR PATRIC; 52036505; VBIProAcn161541_1854. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22548 MW; D68AAF1B366F1623 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAGMRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E6D5Z1_PROAA Unreviewed; 216 AA. AC E6D5Z1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9578_00443; OS Propionibacterium acnes HL110PA4. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765080; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL110PA4; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYF01000036; EFT63807.1; -; Genomic_DNA. DR ProteinModelPortal; E6D5Z1; -. DR EnsemblBacteria; EFT63807; EFT63807; HMPREF9578_00443. DR PATRIC; 52039439; VBIProAcn161024_0843. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22548 MW; D68AAF1B366F1623 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAGMRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E6D7L6_PROAA Unreviewed; 217 AA. AC E6D7L6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9578_00972; OS Propionibacterium acnes HL110PA4. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765080; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL110PA4; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYF01000059; EFT63313.1; -; Genomic_DNA. DR ProteinModelPortal; E6D7L6; -. DR EnsemblBacteria; EFT63313; EFT63313; HMPREF9578_00972. DR PATRIC; 52040343; VBIProAcn161024_1266. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22508 MW; 6BD5C5023BD76D6C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRFPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRTIMASDDP AAVVRQVVQS FDEVRVS // ID E6DDI2_PROAA Unreviewed; 217 AA. AC E6DDI2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9615_01035; OS Propionibacterium acnes HL002PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765117; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL002PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYR01000013; EFT58710.1; -; Genomic_DNA. DR EnsemblBacteria; EFT58710; EFT58710; HMPREF9615_01035. DR PATRIC; 52101424; VBIProAcn162882_0977. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22223 MW; 31519439183CF6DA CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GVGQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQGVQS FDEVRVS // ID E6DGS9_PROAA Unreviewed; 216 AA. AC E6DGS9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9615_02103; OS Propionibacterium acnes HL002PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765117; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL002PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYR01000020; EFT57784.1; -; Genomic_DNA. DR ProteinModelPortal; E6DGS9; -. DR EnsemblBacteria; EFT57784; EFT57784; HMPREF9615_02103. DR PATRIC; 52103496; VBIProAcn162882_1976. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E6DJS1_PROAA Unreviewed; 216 AA. AC E6DJS1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9610_00750; OS Propionibacterium acnes HL027PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765112; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL027PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYT01000011; EFT56444.1; -; Genomic_DNA. DR ProteinModelPortal; E6DJS1; -. DR EnsemblBacteria; EFT56444; EFT56444; HMPREF9610_00750. DR PATRIC; 52110939; VBIProAcn162506_0688. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E6DP09_PROAA Unreviewed; 217 AA. AC E6DP09; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9610_02118; OS Propionibacterium acnes HL027PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765112; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL027PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYT01000037; EFT54875.1; -; Genomic_DNA. DR EnsemblBacteria; EFT54875; EFT54875; HMPREF9610_02118. DR PATRIC; 52113575; VBIProAcn162506_1952. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22308 MW; 2FEAC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVPS FDEVRVS // ID E6DSW4_PROAA Unreviewed; 217 AA. AC E6DSW4; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9565_00880; OS Propionibacterium acnes HL053PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765067; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL053PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZB01000020; EFT50958.1; -; Genomic_DNA. DR EnsemblBacteria; EFT50958; EFT50958; HMPREF9565_00880. DR PATRIC; 52151847; VBIProAcn161742_0802. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22395 MW; B564C189E7C2A32B CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVN // ID E6DW80_PROAA Unreviewed; 216 AA. AC E6DW80; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9565_02070; OS Propionibacterium acnes HL053PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765067; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL053PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZB01000032; EFT49657.1; -; Genomic_DNA. DR ProteinModelPortal; E6DW80; -. DR EnsemblBacteria; EFT49657; EFT49657; HMPREF9565_02070. DR PATRIC; 52154150; VBIProAcn161742_1907. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E6E1Q8_PROAA Unreviewed; 216 AA. AC E6E1Q8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9572_01001; OS Propionibacterium acnes HL072PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765074; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL072PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZF01000025; EFT60751.1; -; Genomic_DNA. DR ProteinModelPortal; E6E1Q8; -. DR EnsemblBacteria; EFT60751; EFT60751; HMPREF9572_01001. DR PATRIC; 52173261; VBIProAcn164220_1270. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E6E3N1_PROAA Unreviewed; 217 AA. AC E6E3N1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9572_01798; OS Propionibacterium acnes HL072PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765074; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL072PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZF01000030; EFT60114.1; -; Genomic_DNA. DR ProteinModelPortal; E6E3N1; -. DR EnsemblBacteria; EFT60114; EFT60114; HMPREF9572_01798. DR PATRIC; 52174818; VBIProAcn164220_2024. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E6E796_PROAA Unreviewed; 217 AA. AC E6E796; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9569_00779; OS Propionibacterium acnes HL078PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765071; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL078PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZG01000023; EFT53676.1; -; Genomic_DNA. DR ProteinModelPortal; E6E796; -. DR EnsemblBacteria; EFT53676; EFT53676; HMPREF9569_00779. DR PATRIC; 52177256; VBIProAcn161088_0717. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E6EAX6_PROAA Unreviewed; 216 AA. AC E6EAX6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9569_02088; OS Propionibacterium acnes HL078PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765071; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL078PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZG01000053; EFT52775.1; -; Genomic_DNA. DR EnsemblBacteria; EFT52775; EFT52775; HMPREF9569_02088. DR PATRIC; 52179825; VBIProAcn161088_1936. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22530 MW; 21184C5A811E64C2 CRC64; MSRPGFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E6EEL5_PROAA Unreviewed; 217 AA. AC E6EEL5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9592_01160; OS Propionibacterium acnes HL046PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765094; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL046PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZQ01000015; EFT74099.1; -; Genomic_DNA. DR ProteinModelPortal; E6EEL5; -. DR EnsemblBacteria; EFT74099; EFT74099; HMPREF9592_01160. DR PATRIC; 52217850; VBIProAcn163534_0631. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID E6EHP4_PROAA Unreviewed; 216 AA. AC E6EHP4; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9592_02411; OS Propionibacterium acnes HL046PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765094; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL046PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZQ01000023; EFT73236.1; -; Genomic_DNA. DR ProteinModelPortal; E6EHP4; -. DR EnsemblBacteria; EFT73236; EFT73236; HMPREF9592_02411. DR PATRIC; 52219929; VBIProAcn163534_1633. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID E6ELL6_ENTFT Unreviewed; 211 AA. AC E6ELL6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9496_00561; OS Enterococcus faecalis (strain TX4000 / JH2-2). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749493; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX4000; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBB01000020; EFT42337.1; -; Genomic_DNA. DR ProteinModelPortal; E6ELL6; -. DR EnsemblBacteria; EFT42337; EFT42337; HMPREF9496_00561. DR PATRIC; 52262438; VBIEntFae150385_0526. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 44C250957E384C82 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVAFVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQELM RVTERMLEVR K // ID E6ETS7_ENTFL Unreviewed; 211 AA. AC E6ETS7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9511_00068; OS Enterococcus faecalis TX0630. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749508; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0630; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBE01000006; EFU91783.1; -; Genomic_DNA. DR ProteinModelPortal; E6ETS7; -. DR EnsemblBacteria; EFU91783; EFU91783; HMPREF9511_00068. DR PATRIC; 52267225; VBIEntFae158812_0065. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID E6F3N3_ENTFL Unreviewed; 211 AA. AC E6F3N3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9502_00247; OS Enterococcus faecalis TX0031. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749499; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0031; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBF01000005; EFT98278.1; -; Genomic_DNA. DR EnsemblBacteria; EFT98278; EFT98278; HMPREF9502_00247. DR PATRIC; 52274341; VBIEntFae154338_0233. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22808 MW; A6E43D580D987123 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGGDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E6FCG4_ENTFL Unreviewed; 211 AA. AC E6FCG4; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9497_00569; OS Enterococcus faecalis TX4244. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749494; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX4244; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBH01000008; EFT92752.1; -; Genomic_DNA. DR EnsemblBacteria; EFT92752; EFT92752; HMPREF9497_00569. DR PATRIC; 52280521; VBIEntFae157284_0551. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22880 MW; E4C84F2F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITKKVQGLM RVTERMLEAR K // ID E6FNC8_ENTFL Unreviewed; 211 AA. AC E6FNC8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9519_01508; OS Enterococcus faecalis TX1346. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749516; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX1346; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBI01000037; EFU17532.1; -; Genomic_DNA. DR EnsemblBacteria; EFU17532; EFU17532; HMPREF9519_01508. DR PATRIC; 52288138; VBIEntFae148577_1432. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22899 MW; A6E42A9C5D187223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGMAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E6FWY7_ENTFL Unreviewed; 211 AA. AC E6FWY7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9518_01710; OS Enterococcus faecalis TX1342. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749515; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX1342; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBJ01000035; EFU14445.1; -; Genomic_DNA. DR ProteinModelPortal; E6FWY7; -. DR EnsemblBacteria; EFU14445; EFU14445; HMPREF9518_01710. DR PATRIC; 52294160; VBIEntFae158213_1592. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID E6G364_ENTFL Unreviewed; 211 AA. AC E6G364; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9516_01080; OS Enterococcus faecalis TX1302. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749513; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX1302; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBK01000025; EFU09359.1; -; Genomic_DNA. DR EnsemblBacteria; EFU09359; EFU09359; HMPREF9516_01080. DR PATRIC; 52298523; VBIEntFae154271_1009. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22861 MW; E4C2537D7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM HVTERMLEAR K // ID E6GDE2_ENTFL Unreviewed; 211 AA. AC E6GDE2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9503_02136; OS Enterococcus faecalis TX0043. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749500; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0043; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBL01000034; EFT99651.1; -; Genomic_DNA. DR ProteinModelPortal; E6GDE2; -. DR EnsemblBacteria; EFT99651; EFT99651; HMPREF9503_02136. DR PATRIC; 52306299; VBIEntFae157737_2039. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID E6GMK8_ENTFL Unreviewed; 211 AA. AC E6GMK8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9501_02174; OS Enterococcus faecalis TX0027. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749498; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0027; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBM01000059; EFT47078.1; -; Genomic_DNA. DR ProteinModelPortal; E6GMK8; -. DR EnsemblBacteria; EFT47078; EFT47078; HMPREF9501_02174. DR PATRIC; 52312015; VBIEntFae154977_2066. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID E6GY80_ENTFL Unreviewed; 211 AA. AC E6GY80; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9506_02800; OS Enterococcus faecalis TX0309A. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749503; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0309A; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBN01000086; EFU92516.1; -; Genomic_DNA. DR ProteinModelPortal; E6GY80; -. DR EnsemblBacteria; EFU92516; EFU92516; HMPREF9506_02800. DR PATRIC; 52319412; VBIEntFae155518_2615. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; FA22A90EE15C1754 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKVVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E6H722_ENTFL Unreviewed; 211 AA. AC E6H722; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9507_02683; OS Enterococcus faecalis TX0309B. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749504; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0309B; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBO01000063; EFU85942.1; -; Genomic_DNA. DR ProteinModelPortal; E6H722; -. DR EnsemblBacteria; EFU85942; EFU85942; HMPREF9507_02683. DR PATRIC; 52325516; VBIEntFae155297_2508. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; FA22A90EE15C1754 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKVVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E6HD45_ENTFL Unreviewed; 211 AA. AC E6HD45; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9500_01568; OS Enterococcus faecalis TX0017. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749497; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0017; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBP01000036; EFT44557.1; -; Genomic_DNA. DR ProteinModelPortal; E6HD45; -. DR EnsemblBacteria; EFT44557; EFT44557; HMPREF9500_01568. DR PATRIC; 52329690; VBIEntFae149717_1479. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22866 MW; A6E43F880C487223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E6HQ17_ENTFL Unreviewed; 211 AA. AC E6HQ17; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9494_02662; OS Enterococcus faecalis TX2137. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749491; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX2137; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEBQ01000131; EFT37391.1; -; Genomic_DNA. DR ProteinModelPortal; E6HQ17; -. DR EnsemblBacteria; EFT37391; EFT37391; HMPREF9494_02662. DR PATRIC; 52337855; VBIEntFae149436_2421. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22881 MW; E4C24F8F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E6HSS7_ENTFL Unreviewed; 211 AA. AC E6HSS7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9508_00621; OS Enterococcus faecalis TX0312. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749505; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0312; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECB01000015; EFU03663.1; -; Genomic_DNA. DR ProteinModelPortal; E6HSS7; -. DR EnsemblBacteria; EFU03663; EFU03663; HMPREF9508_00621. DR PATRIC; 52339859; VBIEntFae148422_0580. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22866 MW; A6E43F880C487223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E6I4F0_ENTFL Unreviewed; 211 AA. AC E6I4F0; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9499_01935; OS Enterococcus faecalis TX0012. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749496; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0012; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECD01000040; EFT93936.1; -; Genomic_DNA. DR ProteinModelPortal; E6I4F0; -. DR EnsemblBacteria; EFT93936; EFT93936; HMPREF9499_01935. DR PATRIC; 52348029; VBIEntFae151224_1832. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID E6IAP8_ENTFL Unreviewed; 211 AA. AC E6IAP8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9513_01362; OS Enterococcus faecalis TX0645. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749510; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX0645; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECE01000050; EFU06078.1; -; Genomic_DNA. DR ProteinModelPortal; E6IAP8; -. DR EnsemblBacteria; EFU06078; EFU06078; HMPREF9513_01362. DR PATRIC; 52352379; VBIEntFae148101_1274. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; E4C2509F7E3D7054 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID E6IHZ1_ENTFL Unreviewed; 211 AA. AC E6IHZ1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9517_00696; OS Enterococcus faecalis TX1341. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749514; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX1341; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECF01000012; EFU12773.1; -; Genomic_DNA. DR ProteinModelPortal; E6IHZ1; -. DR EnsemblBacteria; EFU12773; EFU12773; HMPREF9517_00696. DR PATRIC; 52357657; VBIEntFae149520_0652. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22895 MW; A6E420980C487223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEVR K // ID E6IWF9_ENTFL Unreviewed; 211 AA. AC E6IWF9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9495_02307; OS Enterococcus faecalis TX2141. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749492; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX2141; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECG01000080; EFT87848.1; -; Genomic_DNA. DR EnsemblBacteria; EFT87848; EFT87848; HMPREF9495_02307. DR PATRIC; 52366884; VBIEntFae160038_2200. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22925 MW; 85C4D9F9747C283C CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGVDYLGVGA IFPTMTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID E6J486_9ACTO Unreviewed; 258 AA. AC E6J486; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ES5_00065; OS Dietzia cinnamea P4. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Dietziaceae; Dietzia. OX NCBI_TaxID=910954; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P4; RX PubMed=21901521; DOI=10.1007/s10482-011-9633-7; RA Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., RA Sorensen S.J., Cardoso J.S., Padula M., Leitao A.C., Seldin L., RA van Elsas J.D.; RT "Insight from the draft genome of Dietzia cinnamea P4 reveals RT mechanisms of survival in complex tropical soil habitats and RT biotechnology potential."; RL Antonie Van Leeuwenhoek 101:289-302(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEKG01000003; EFV93598.1; -; Genomic_DNA. DR EnsemblBacteria; EFV93598; EFV93598; ES5_00065. DR PATRIC; 46570951; VBIDieCin172986_0011. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 56 60 HMP-PP binding (By similarity). FT REGION 161 163 THZ-P binding (By similarity). FT REGION 225 226 THZ-P binding (By similarity). FT METAL 95 95 Magnesium (By similarity). FT METAL 113 113 Magnesium (By similarity). FT BINDING 94 94 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 164 164 HMP-PP (By similarity). FT BINDING 205 205 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 258 AA; 26250 MW; CB7D35052148A27E CRC64; MSDARPDRDV GEARLDRGAG VDWRLYLVTD PHLGGGRDAV PGIAYEAVLG GVGVVQVRDK EGDDDEFATH AVAVAEAVAR ACTETGRVVP VFVNDRADVA RELGLHLHVG QRDIPFARAR AAMPDHLMVG LSIESDSQLA AALAGPGPVP DVIGVSPVWA TATKTDTAAA LGPEGADRLA RAAHAHRSGG GVRGAAGVRA VGIGGVTPAT VAQLAATELD GICVVSAIMA APDPRAAAAE LLARWEAGKS LPPEGEPA // ID E6J5X1_9ACTO Unreviewed; 179 AA. AC E6J5X1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE Flags: Fragment; GN Name=thiE; ORFNames=ES5_03046; OS Dietzia cinnamea P4. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Dietziaceae; Dietzia. OX NCBI_TaxID=910954; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P4; RX PubMed=21901521; DOI=10.1007/s10482-011-9633-7; RA Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., RA Sorensen S.J., Cardoso J.S., Padula M., Leitao A.C., Seldin L., RA van Elsas J.D.; RT "Insight from the draft genome of Dietzia cinnamea P4 reveals RT mechanisms of survival in complex tropical soil habitats and RT biotechnology potential."; RL Antonie Van Leeuwenhoek 101:289-302(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEKG01000078; EFV92994.1; -; Genomic_DNA. DR EnsemblBacteria; EFV92994; EFV92994; ES5_03046. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. FT NON_TER 179 179 SQ SEQUENCE 179 AA; 19065 MW; A278D5D8680C107E CRC64; MTARADRLRA RLADARLYLC IDARRHLDDD ARAQGWTGDF PALRRDVTAA LTGGVDIVQL RDKNSAGDRD LGPLEAGHEL RALAVMREVC DAHGALLSVN DRADVAVAAG ADVLHVGQDD LPVEWARRIV GDDVVIGLSC HATDEVDAAA ANPVVDYFCT GPVWPTPTKP GRDAPGLGL // ID E6JJH4_RIEAN Unreviewed; 205 AA. AC E6JJH4; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=RAYM_05825; OS Riemerella anatipestifer RA-YM. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Riemerella. OX NCBI_TaxID=913239; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RA-YM; RX PubMed=21183670; DOI=10.1128/JB.01445-10; RA Zhou Z., Peng X., Xiao Y., Wang X., Guo Z., Zhu L., Liu M., Jin H., RA Bi D., Li Z., Sun M.; RT "Genome sequence of poultry pathogen Riemerella anatipestifer strain RT RA-YM."; RL J. Bacteriol. 193:1284-1285(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENH01000027; EFT35324.1; -; Genomic_DNA. DR EnsemblBacteria; EFT35324; EFT35324; RAYM_05825. DR PATRIC; 52756198; VBIRieAna180783_1809. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 205 AA; 23492 MW; A21ABFE005B1A37D CRC64; MEIKNGIYLI VNPSMHRDTL LIKLEKIISE GIVAVQIWDN FNDNDNILDI INRIIEICHK ENIPVLINNR WELLREVNID GVHFDVQPND IEAIRRELGR KVIMGITCNN DLEHVQWANK QKMDYISFCS IFPSSTANSC EFVRFDTVRE AKKITQIPIF LAGGITPENV GELTALNCFG IAVVSGIMDA EKPIQEIKKY KRKLK // ID E6JPC7_STAEP Unreviewed; 160 AA. AC E6JPC7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI family protein; GN ORFNames=GSEF_1549; OS Staphylococcus epidermidis FRI909. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=764544; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FRI909; RX PubMed=21317317; DOI=10.1128/JB.00162-10; RA Madhusoodanan J., Seo K.S., Remortel B., Park J.Y., Hwang S.Y., RA Fox L.K., Park Y.H., Deobald C.F., Wang D., Liu S., Daugherty S.C., RA Gill A.L., Bohach G.A., Gill S.R.; RT "An Enterotoxin-Bearing Pathogenicity Island in Staphylococcus RT epidermidis."; RL J. Bacteriol. 193:1854-1862(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENR01000028; EFV88432.1; -; Genomic_DNA. DR EnsemblBacteria; EFV88432; EFV88432; GSEF_1549. DR PATRIC; 52759953; VBIStaEpi161197_1603. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18158 MW; B785D19C532A4689 CRC64; MNNEENKDMI QSLLQLGFSK DKIIIHSDTT LLEELNLKRI HFKSNDTTAF AYKAAHPDIC VSMSTHDVET VKRCYENNLD YVFLGHIFPT ASHPDTPPRS KETIQQALDV PIPIYAIGGI NEHSIQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID E6JRB7_STAEP Unreviewed; 212 AA. AC E6JRB7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GSEF_2257; OS Staphylococcus epidermidis FRI909. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=764544; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FRI909; RX PubMed=21317317; DOI=10.1128/JB.00162-10; RA Madhusoodanan J., Seo K.S., Remortel B., Park J.Y., Hwang S.Y., RA Fox L.K., Park Y.H., Deobald C.F., Wang D., Liu S., Daugherty S.C., RA Gill A.L., Bohach G.A., Gill S.R.; RT "An Enterotoxin-Bearing Pathogenicity Island in Staphylococcus RT epidermidis."; RL J. Bacteriol. 193:1854-1862(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENR01000048; EFV87833.1; -; Genomic_DNA. DR EnsemblBacteria; EFV87833; EFV87833; GSEF_2257. DR PATRIC; 52761464; VBIStaEpi161197_2328. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23573 MW; 6AC85A03F52118E9 CRC64; MFDSKQLSVY FICGTQDIPK NKSIEQVLKE ALEAGITLYQ FREKGPNALK GEKKKQLALK LKQLCHSYHV PMIVNDDVQL AQEINADGIH VGQDDMEIQQ FASQFKNKII GLSVGNLKEY QQSDLSKVDY IGVGPMYTTS SKDDASKPVG PSMISQLRLY IHDVPIVAIG GINETNVQPI VDEGADGISV ISAITRSTNI DKTVKYFLRY FT // ID E6K7G8_9BACT Unreviewed; 202 AA. AC E6K7G8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF6485_1815; OS Prevotella buccae ATCC 33574. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=873513; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33574; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPD01000028; EFU30536.1; -; Genomic_DNA. DR EnsemblBacteria; EFU30536; EFU30536; HMPREF6485_1815. DR PATRIC; 45074637; VBIPreBuc167547_1204. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23378 MW; A0A91043FF850E83 CRC64; MKLVIMTKST FFVEEDKILA TLFEEGMDNL HLNKPDSSPM YSERLLSLLP EETYRKITVH DHFYLKNEYD LAGIHLDDAF QEAPKGYKGK MSATCTETKR LKEAKRKFNY VFLKNIFDCI EYPSEKSSFN LNELEDAAHR GLIDKHVYAL GGMSLENVKL AKQLGFGGVV VCGDLWNRFD IHNETDYLQL INHFNKLRKA VE // ID E6KAT5_9BACT Unreviewed; 214 AA. AC E6KAT5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF6485_2721; OS Prevotella buccae ATCC 33574. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=873513; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33574; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPD01000049; EFU29395.1; -; Genomic_DNA. DR EnsemblBacteria; EFU29395; EFU29395; HMPREF6485_2721. DR PATRIC; 45076383; VBIPreBuc167547_2224. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23064 MW; F18AA4B1D89CF65C CRC64; MTPVQFITHH NARFSYLEGA VQALLGGCRW IQLRMKEASD EEFLEVGRQL VPLCRAHGAR LTVDDRAHLV APLGADGVHL GRDDMPPDEA RRLLGPHALI GGTANTFTDI GRLCTLGVDY IGCGPFRFTA TKQRLSPLLG LDGYRRLTAR MRASGMHVPL VAIGGITLAD IPALMAAGVD GIAVSGAVLG AEHPAEEMRR MVHGTICCRH NQNT // ID E6KAT8_9BACT Unreviewed; 194 AA. AC E6KAT8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-APR-2014, entry version 16. DE SubName: Full=Thiamine monophosphate synthase/TENI; DE EC=2.5.1.3; DE EC=2.7.4.7; GN ORFNames=HMPREF6485_2724; OS Prevotella buccae ATCC 33574. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=873513; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33574; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPD01000049; EFU29398.1; -; Genomic_DNA. DR EnsemblBacteria; EFU29398; EFU29398; HMPREF6485_2724. DR PATRIC; 45076390; VBIPreBuc167547_2227. DR OrthoDB; EOG679THR; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 194 AA; 21179 MW; 163FE0EA532FC5B3 CRC64; MKTIVITSPD HRPGEETVIP RLLEAGVDFV HLRKPAWSEA DCARLLSLVP AWCHGRIVVH DHFVLCRRFA LRGIHLNGRC PEIPVGFEGA VSRSCHSLCE VEEGKPLSSY VFLSPVFDSI SKPGYRAAFT PAELQSAARR GIIDRRVVAL GGVSVDNVAL LRTCGFGGVA LLGEVWRQAA GAHFGDYLRR LAAL // ID E6KM31_STROR Unreviewed; 210 AA. AC E6KM31; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF8578_1098; OS Streptococcus oralis ATCC 49296. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888049; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49296; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPO01000012; EFU62958.1; -; Genomic_DNA. DR EnsemblBacteria; EFU62958; EFU62958; HMPREF8578_1098. DR PATRIC; 45083966; VBIStrSan172127_1679. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; 5EDDAEAEEA0297BB CRC64; MNREVLKLYL VTNRYQDSLE NFLEKVETAC RSGVTIVQLR EKNLTTNQYY HLAKQVKEIT DAYQVPLIID DRLDVCLAVD TAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE EGGANYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLAATGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDDMIS // ID E6L026_9PAST Unreviewed; 220 AA. AC E6L026; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiDE; Synonyms=thiE; ORFNames=HMPREF9064_1758; OS Aggregatibacter segnis ATCC 33393. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=888057; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33393; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPS01000014; EFU66829.1; -; Genomic_DNA. DR EnsemblBacteria; EFU66829; EFU66829; HMPREF9064_1758. DR PATRIC; 45093477; VBIAggSeg171182_0419. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 49 53 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24219 MW; FEDAE9ED22434941 CRC64; MSEAVSHLSE IIPPKAPFAP TEFKLGLYVI VDSYEWIERL IHAGVKTLQI RIKDRSPEQA EEEIARCIAL AKQHQVRLFV DDFWSLAIKY QAYGVHLGQE DLLTADLNAI QQAGLRLGVS THNQEEVDLV LPLRPSYVAL GHIFPTQTKD MPSAPQGITN LAAQVKNLGK MPTVAIGGIS ASHFPDILAT GVGSIAVISA VTKAQDWQRA VKNLQQYFVE // ID E6L277_9PROT Unreviewed; 203 AA. AC E6L277; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF9401_0553; OS Arcobacter butzleri JV22. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=888827; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JV22; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPT01000010; EFU70530.1; -; Genomic_DNA. DR EnsemblBacteria; EFU70530; EFU70530; HMPREF9401_0553. DR PATRIC; 45096984; VBIArcBut170584_1742. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 203 AA; 23082 MW; FE713608BD8BDC7E CRC64; MISNLEKALG FKLEAFNYLY VLCDYETLLK KNISLETFVD LCRKKDVKII QYRDKISSLE EQKINLLYLK SQLNIPIIVN DKIELIDFAD GLHLGQEDLE KIHKDKNLAI KLVRIKIKDK LLGLSTHNEI EILEANELNL DMIGLGAYKQ TNTKDVSSIL GEKISYLAKI SKHPVCAIGG VKIEDKILNV KFNVVGSGFF DEN // ID E6L3Z3_9PROT Unreviewed; 184 AA. AC E6L3Z3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=HMPREF9401_1169; OS Arcobacter butzleri JV22. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=888827; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JV22; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPT01000036; EFU69868.1; -; Genomic_DNA. DR EnsemblBacteria; EFU69868; EFU69868; HMPREF9401_1169. DR PATRIC; 45097814; VBIArcBut170584_1891. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 184 AA; 21393 MW; 7F3C4E2E2BEBDCEA CRC64; MKKYLITDPN YYTNNELIFK QTLSNAFEKH KVDFACFRDK ESNNFEALAK TFIETCHEKN IKNTFLNSDF LLAQKLGFYG VHLTSTQFED IKKAKELNLK IIISCHNIKD IETAREYEVD YITYSPIFDT PNKGKEKGIK DLELVLNIFK DMKIIALGGI IDETQVSKIE KTKAYGFASI RYFI // ID E6L8R5_CAMUP Unreviewed; 207 AA. AC E6L8R5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9400_0460; OS Campylobacter upsaliensis JV21. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=888826; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JV21; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPU01000011; EFU72406.1; -; Genomic_DNA. DR EnsemblBacteria; EFU72406; EFU72406; HMPREF9400_0460. DR PATRIC; 45099719; VBICamUps173175_0161. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22348 MW; FBB7A28044283F57 CRC64; MLDLSLYLVA SRGNLSDEKF LNVLESAIKG GVSLIQLREK NLNARDFFTL GLKAQKLCQK YKIPLIINDR IDLALALDAD GVHLGQEDLP LQIARKILGK DKIIGLSLKS LKQLEGIEGA DYLGCGAIKK TPTKESSVLS LELLSQICQN SSLPVVAIGG IDEAVIKDLR GIKLGGVAVV RAIMNAKNPY QAAKTLKKAV CENLSLK // ID E6L9X2_CAMUP Unreviewed; 201 AA. AC E6L9X2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN ORFNames=HMPREF9400_0867; OS Campylobacter upsaliensis JV21. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=888826; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JV21; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPU01000019; EFU71917.1; -; Genomic_DNA. DR EnsemblBacteria; EFU71917; EFU71917; HMPREF9400_0867. DR PATRIC; 45100539; VBICamUps173175_0564. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23284 MW; 0BB3B7CCCE7C9F5A CRC64; MWVRKIIAIS DRVLVQDDFL RQVEKLAKAK IDAFVLREKD LSEYEYYDLA KEVLKICTKY KITCFLHGYL TPTLKLEHKY FQAPLALLRK ESNIAKYFHI LGTSVHSKEE LLEAINYKVN HAFVGHIFKS SCKPNLKPYG IELLKDLLSF SSIPLYAIGG INAENIKFFK NINIAGVCMR EALMRESNPK KYLALCKKEF L // ID E6LE97_9ENTE Unreviewed; 210 AA. AC E6LE97; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9088_0687; OS Enterococcus italicus DSM 15952. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=888064; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15952; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPV01000026; EFU74386.1; -; Genomic_DNA. DR EnsemblBacteria; EFU74386; EFU74386; HMPREF9088_0687. DR PATRIC; 45103628; VBIEntIta172006_0430. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22773 MW; 4707318AB5F3D30E CRC64; MADYSLYLVT GSYDYDDQTF LQIVEEACQA GVTIVQLREK TGTTQAIYQK ALKVKAITDR YGIPLIIDDR VDICLAVDAT GVHIGDDELP VHVVRGLIGP TKILGVSAKT TARARQAEQE GADYLGTGAM FETQTKQTPV TSFETLQAVI QAVKIPVVAI GGIKEDNLAS FQDIPIAGVA IVSEIMKAID VKEKVQALQK KVAYWRSGNE // ID E6LP96_9FIRM Unreviewed; 204 AA. AC E6LP96; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0381_1781; OS Lachnoanaerobaculum saburreum DSM 3986. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Lachnoanaerobaculum. OX NCBI_TaxID=887325; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3986; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPW01000076; EFU76291.1; -; Genomic_DNA. DR EnsemblBacteria; EFU76291; EFU76291; HMPREF0381_1781. DR PATRIC; 45110484; VBIEubSab170007_1887. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22163 MW; BAB796B2E7D9F3B7 CRC64; MHLYAVTDRA WTGKKTLYEQ INEALKNGVT CVQLREKNLD EISFIEEAKK ISELCKQYSI PFIVNDNVKV AVASNADGVH IGQDDMKLKD VRKLVGENMI IGVSVHTVDE AKSAQEDGAD YIGIGAVFET STKNDVDIIP YEKVKSICEA VDIPKVAIGG INAENILKLK GSKIDGVAVV SAIFGAKDIG KATKELDTLV NELI // ID E6MAX3_STALU Unreviewed; 196 AA. AC E6MAX3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0790_1576; OS Staphylococcus lugdunensis M23590. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525377; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23590; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQA01000013; EFU83818.1; -; Genomic_DNA. DR EnsemblBacteria; EFU83818; EFU83818; HMPREF0790_1576. DR PATRIC; 45125938; VBIStaLug105164_1548. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 22570 MW; 61C3E2794E180F4B CRC64; MFIFIAITEY KFLDNNDLQH FLTIEQDIDF LLFRTSMSQK ELQHFIQQLI YQGFPKSKMM IHSDVKLLNT LGLQNIHFRE NDAQAFHLKS KYPDIHVSMS THHLSSVIRA YEAGLDAIFF GHIFPTPSKP NLPPRSQVEI DSVLEVPIPV YAIGGITTDT IRKLSPNFAG ICAISFFMKS SASVIHQFRK EWHHHA // ID E6MD12_STALU Unreviewed; 212 AA. AC E6MD12; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0790_2315; OS Staphylococcus lugdunensis M23590. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525377; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23590; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQA01000020; EFU83015.1; -; Genomic_DNA. DR ProteinModelPortal; E6MD12; -. DR EnsemblBacteria; EFU83015; EFU83015; HMPREF0790_2315. DR PATRIC; 45127183; VBIStaLug105164_2161. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23243 MW; CD4DB4E493873289 CRC64; MFKSTDLKVY FICGTQDIPE GKSLEQVVTQ ALESGVTMFQ FREKGSKVSQ DKEIEQLALK LKELCHNYQV PFIVNDNVAL ALKVQADGIH VGQDDAKVED FFEQFHDKII GLSVSNLDEL KRSDLTHVDY IGVGPIYQTP SKSDASTPVG PEMILTLRKE IGDFPIVAIG GVTENNAQAV VDAGADGISV ISAIARSQNI DSTVNKFLSY YN // ID E6MHF8_9FIRM Unreviewed; 230 AA. AC E6MHF8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMP0721_1443; OS Pseudoramibacter alactolyticus ATCC 23263. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Pseudoramibacter. OX NCBI_TaxID=887929; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23263; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQN01000018; EFV01460.1; -; Genomic_DNA. DR EnsemblBacteria; EFV01460; EFV01460; HMP0721_1443. DR PATRIC; 45130660; VBIPseAla174371_0924. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 208 209 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 24093 MW; A32D1B160268AEDA CRC64; MSMREALDLS AYLVIGPENT KGRPVKGIIR DVVAAGFTIV QVRSKVASAK ELIGYCRDAA EAIAEAGRAD RVALVADDRL DVVLAAREAG IKVDGIHVGQ SDIPAAVCRK YLGDDAVIGL SARTRELIDY VRTADISDID YFGAGPLHET ATKPEAGRSA SGRVITRSLE EIAELARVSP VPAVIGGGVK LADIPDLKRT GIAGFFVVST VTEADDPGRA AAALTAAWRA // ID E6MZQ9_NEIMH Unreviewed; 205 AA. AC E6MZQ9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NMBH4476_2014; ORFNames=NMH_2075; OS Neisseria meningitidis serogroup B / serotype 15 (strain H44/76). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=909420; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H44/76; RX PubMed=21378179; DOI=10.1128/JB.01331-10; RA Piet J.R., Huis In 't Veld R.A., van Schaik B.D., van Kampen A.H., RA Baas F., van de Beek D., Pannekoek Y., van der Ende A.; RT "Genome sequence of Neisseria meningitidis serogroup B strain RT H44/76."; RL J. Bacteriol. 193:2371-2372(2011). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H44/76; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002420; ADY96572.1; -; Genomic_DNA. DR EMBL; AEQZ01000043; EFV62938.1; -; Genomic_DNA. DR RefSeq; YP_005900627.1; NC_017516.1. DR EnsemblBacteria; ADY96572; ADY96572; NMBH4476_2014. DR EnsemblBacteria; EFV62938; EFV62938; NMH_2075. DR GeneID; 12491178; -. DR KEGG; nmh:NMBH4476_2014; -. DR PATRIC; 47154041; VBINeiMen174185_2710. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR BioCyc; NMEN909420:GLHQ-2013-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21605 MW; 7DAC8AFBD9AD2D26 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKAL HGDELKREIA RCAAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYIASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID E6N704_9ARCH Unreviewed; 209 AA. AC E6N704; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-MAR-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CSUB_C1010, HGMM_F34A01C28; OS Candidatus Caldiarchaeum subterraneum. OC Archaea; Thaumarchaeota; unclassified Thaumarchaeota; OC Candidatus Caldiarchaeum. OX NCBI_TaxID=311458; RN [1] RP NUCLEOTIDE SEQUENCE. RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S., RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.; RT "Genetic and functional properties of uncultivated thermophilic RT crenarchaeotes from a subsurface gold mine as revealed by analysis of RT genome fragments."; RL Environ. Microbiol. 7:1967-1984(2005). RN [2] RP NUCLEOTIDE SEQUENCE. RA Nunoura T., Takaki Y., Kakuta J., Nishi S., Sugahara J., Kazama H., RA Chee G., Hattori M., Kanai A., Atomi H., Takai K., Takami H.; RT "Insights into the evolution of Archaea and eukaryotic protein RT modifier systems revealed by the genome of a novel archaeal group."; RL Nucleic Acids Res. 39:3204-3223(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011853; BAJ48073.1; -; Genomic_DNA. DR EMBL; BA000048; BAJ50863.1; -; Genomic_DNA. DR RefSeq; YP_008797493.1; NC_022786.1. DR GeneID; 17602346; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 134 136 THZ-P binding (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22246 MW; B7CF67AD81FCBCEF CRC64; MQKIPKPPLL VITDSGLAEG RLLAIVEECL AAGCRWFMVR EKNMPLESLI KLTISIAKMA EKYSAAVVVN GYPEIVNQTG AAGVHLPWSM DIKAARRVVG GDKLLGVSTH STEQAVEAEK MGADYVTLSP IFPSVSKPGY QNPAGLQMLK DIVRRLTIPV IALGGIKPGN AKTCIANGAA GVAVLGAMMK AQKPYDVILS IINEIKPTQ // ID E6NDA5_HELPI Unreviewed; 219 AA. AC E6NDA5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPF16_0518; OS Helicobacter pylori (strain F16). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=866344; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F16; RX PubMed=21212362; DOI=10.1073/pnas.1012579108; RA Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T., RA Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I., RA Kobayashi I.; RT "Birth and death of genes linked to chromosomal inversion."; RL Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011940; BAJ55115.1; -; Genomic_DNA. DR RefSeq; YP_005778753.1; NC_017368.1. DR EnsemblBacteria; BAJ55115; BAJ55115; HPF16_0518. DR GeneID; 12358785; -. DR KEGG; hef:HPF16_0518; -. DR KO; K00788; -. DR BioCyc; HPYL866344:GLEC-530-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23802 MW; 9EE02D603410A196 CRC64; MFDANCLRLM FVAGSQDFYH IKGDKNDRIN ALLDALELAL QSKITAFQFR QKGDLALQDP IEIKQLALKC QKLCQKYGAP FIVNDEVQLA LELKADGVHV GQEDMAIGEV MALCKKRQFI GLSVNTLEQA LKAHHLDGVA YLGVGPIFPT QSKKDKQVVG VELLKKIKDS GVKKPLIAIG GITTHNASKL HEYGGIAVIS AIAQAKDKAL AVGKLLKNA // ID E6NII2_HELPK Unreviewed; 219 AA. AC E6NII2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPF30_0488; OS Helicobacter pylori (strain F30). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=866345; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F30; RX PubMed=21212362; DOI=10.1073/pnas.1012579108; RA Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T., RA Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I., RA Kobayashi I.; RT "Birth and death of genes linked to chromosomal inversion."; RL Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011941; BAJ56585.1; -; Genomic_DNA. DR RefSeq; YP_005774233.1; NC_017365.1. DR EnsemblBacteria; BAJ56585; BAJ56585; HPF30_0488. DR GeneID; 12353849; -. DR KEGG; hpf:HPF30_0488; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; HPYL866345:GLED-516-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23945 MW; C5745AC842795573 CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLALQDP IEIKQLALEC QKLCQKYGTP FIVNDEVKLA LELKADGVHV GQEDMAIEEV MTLCKKRQFI GLSVNTLEQA LKARHLDGVA YLGVGPIFPT RSKKDKQAVG VELLKKIKDS GVKKPLVAIG GITTHNASKL REYGGIAVIS AIAQAKDKAL AIEKLLNNA // ID E6NKM5_HELPL Unreviewed; 219 AA. AC E6NKM5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPF32_0810; OS Helicobacter pylori (strain F32). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=102608; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F32; RX PubMed=21212362; DOI=10.1073/pnas.1012579108; RA Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T., RA Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I., RA Kobayashi I.; RT "Birth and death of genes linked to chromosomal inversion."; RL Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011943; BAJ58392.1; -; Genomic_DNA. DR RefSeq; YP_005776034.1; NC_017366.1. DR EnsemblBacteria; BAJ58392; BAJ58392; HPF32_0810. DR GeneID; 12355636; -. DR KEGG; heq:HPF32_0810; -. DR KO; K00788; -. DR BioCyc; HPYL102608:GLEE-832-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23874 MW; 93CED9CD1608D9DB CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLALQDP IEIKQLALKC QKLCQKYGAP FIVNDEVELA LELKADGVHV GQEDMAIEEV ITLCKKRQFI GLSVNTLEQA LKACHLDGVA YLGVGPIFPT QSKKDKQVVG VELLKKIKDS GVKKPLVAIG GITTHNASKL REYGGIAVIS TIAQAKDKAL AVEKLLKNA // ID E6NS23_HELPQ Unreviewed; 219 AA. AC E6NS23; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPF57_0865; OS Helicobacter pylori (strain F57). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=866346; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F57; RX PubMed=21212362; DOI=10.1073/pnas.1012579108; RA Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T., RA Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I., RA Kobayashi I.; RT "Birth and death of genes linked to chromosomal inversion."; RL Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011945; BAJ59939.1; -; Genomic_DNA. DR RefSeq; YP_005777579.1; NC_017367.1. DR EnsemblBacteria; BAJ59939; BAJ59939; HPF57_0865. DR GeneID; 12357570; -. DR KEGG; hex:HPF57_0865; -. DR KO; K00788; -. DR BioCyc; HPYL866346:GLEF-879-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23843 MW; B5A8BAE84B3AD102 CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLALQDP IEIKQLALEC QKLCQKYGAP FIVNDEVQLA LELKADGVHV GQEDMAIEEV MTLCKKRQFI GLSVNTLEQA LKARHLDGVA YLGVGPIFPT QSKKDKQVVG VELLKKIKDS GVKKPLIAIG GITTHNASKL REYGGIAVIS AIAQAKDKAL AVGKLLNNA // ID E6PGJ3_9ZZZZ Unreviewed; 211 AA. AC E6PGJ3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Putative Thiamine-phosphate pyrophosphorylase (TMP pyrophosphorylase) (TMP-PPase) (Thiamine-phosphate synthase) (ThiE); DE EC=2.5.1.3; GN ORFNames=CARN1_2651; OS mine drainage metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=410659; RN [1] RP NUCLEOTIDE SEQUENCE. RA Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F., RA Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C., RA Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O., RA Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N., RA Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P., RA Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., RA Medigue C., Le Paslier D.; RT "Diversity of trophic interactions inside an arsenic-rich microbial RT ecosystem."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CABL01000011; CBH75581.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Transferase. SQ SEQUENCE 211 AA; 21546 MW; DAD45D8E73DF3E37 CRC64; MKREEARPLL CGPYAIVNEA PNARSIAEAV LGAGFRILQY RAKDGIDPAR LREFSDLTRT HGALSIGNDD WRAAQAAGCD GVHLGPGDDG FGDPARVRAA WPEAIIGLSI GSPDEARRID GAAVDYLGVG AIFATASKAD AGAPIALAGL RAVVEATTLP ICAIGGITAE RLAGLRANGA AMAATIAAIA QAADPAEAAR RFHAAWEGVA A // ID E6PLB2_9ZZZZ Unreviewed; 309 AA. AC E6PLB2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE SubName: Full=Putative Phosphomethylpyrimidine kinase ThiD/thiamine-phosphate diphosphorylase fused protein ThiE; DE EC=2.5.1.3; DE EC=2.7.4.7; GN ORFNames=CARN2_1979; OS mine drainage metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=410659; RN [1] RP NUCLEOTIDE SEQUENCE. RA Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F., RA Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C., RA Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O., RA Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N., RA Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P., RA Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., RA Medigue C., Le Paslier D.; RT "Diversity of trophic interactions inside an arsenic-rich microbial RT ecosystem."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CABM01000010; CBH95713.1; -; Genomic_DNA. DR ProteinModelPortal; E6PLB2; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Transferase. SQ SEQUENCE 309 AA; 32325 MW; 2A634AB01DC3F7E3 CRC64; MLTRDGAQSF AVPRLAHGAH GTGCLYAAVL AAMLAQGWSV ADAVVEAQWR THAGIAQAWR AAPEARPLVN PAAVLDSGSF PRRPAPGGLP QTDAPAFAPL TAPPGFYPIL PDADWALRVL DWGARTLQLR IKDLQGAALR ADIARVAEAA RQAGAQLFVN DHWREALDAG AYGVHLGQED LLLADLAALR AAGMRLGVST HTPGEMARAH ALGPSYIALG PVYPTTLKVM PYRPLGLQRL ADWVARCRPR YPTVAIGGIS LERAPGVMAA GADGYAVVSA VTQAADPQAA VRRGLAIAQQ AQDCRAAAG // ID E6Q7G3_9ZZZZ Unreviewed; 211 AA. AC E6Q7G3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Putative Thiamine-phosphate pyrophosphorylase (TMP pyrophosphorylase) (TMP-PPase) (Thiamine-phosphate synthase) (ThiE); DE EC=2.5.1.3; GN ORFNames=CARN4_2794; OS mine drainage metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=410659; RN [1] RP NUCLEOTIDE SEQUENCE. RA Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F., RA Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C., RA Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O., RA Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N., RA Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P., RA Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., RA Medigue C., Le Paslier D.; RT "Diversity of trophic interactions inside an arsenic-rich microbial RT ecosystem."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CABO01000049; CBI03138.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Transferase. SQ SEQUENCE 211 AA; 21617 MW; F3654237E090A844 CRC64; MKRAEGRALL YGPYAIVNEA PNARRIAEAA LGAGFRILQY RAKDGIDPAR LREFSDLARA RGALSIGNDD WRAAQAAGCD GVHLGPGDDG FEDPARVRAA WPEAMIGLSI GSPDEARRVD GAAVDYLGVG AIFATASKAD AGTPIALAGL RAVAEATTLP ICAIGGITAE RLAGLRANGA SMAATIAAIA EAADPAEAAR RFHSAWEGAA P // ID E6QGB9_9ZZZZ Unreviewed; 329 AA. AC E6QGB9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=NUDIX hydrolase; GN ORFNames=CARN5_0227; OS mine drainage metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=410659; RN [1] RP NUCLEOTIDE SEQUENCE. RA Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F., RA Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C., RA Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O., RA Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N., RA Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P., RA Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., RA Medigue C., Le Paslier D.; RT "Diversity of trophic interactions inside an arsenic-rich microbial RT ecosystem."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CABP01000167; CBI06274.1; -; Genomic_DNA. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 329 AA; 35284 MW; 1745BFB7B585D761 CRC64; MPTVPVATGI IEDAFGRLLV ALRPEGKPWP GFWEFPGGKV DPGETPEQAL VRELWEELGV TVTAPEPFRV LEYTYPERTV RVHFYRVRHW TGTAHGREGQ EVRWLFPWEI PALECLPANL RLTADVLAEA LPQPPLCLIA DPGRLPLPDF RRALEAALDA GLRWLVLRCK AVPDGSSADV LAALCAGALA GGVQVYLNHP DPLPGWPRTG RHLTQAQSDA GVKPDEAFGV SCHDAAGLQQ AARLGARYAF LSPIFPTSSH PDTEALGPGV FAAMAAESSL PLIALGGMTA ARVPEALAAG ARGVAVLSGI LEAQDPAAAT RALLRHWER // ID E6QGX4_9ZZZZ Unreviewed; 217 AA. AC E6QGX4; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase (TMP pyrophosphorylase) (TMP-PPase) (Thiamine-phosphate synthase); DE EC=2.5.1.3; GN Name=thiE; ORFNames=CARN5_3293; OS mine drainage metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=410659; RN [1] RP NUCLEOTIDE SEQUENCE. RA Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F., RA Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C., RA Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O., RA Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N., RA Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P., RA Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., RA Medigue C., Le Paslier D.; RT "Diversity of trophic interactions inside an arsenic-rich microbial RT ecosystem."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CABP01000182; CBI06488.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Transferase. SQ SEQUENCE 217 AA; 22630 MW; 1AE888365E0C98A9 CRC64; MAGDDHLISG LYAITDAHLM PEPVFLARAE AALRGGARIL QYRDKGDVVT DARRRRMQAG ALRELCAQYG ALFVVNDDPR LARAVGAPAL HVGAEDAPPA ALRAQFGRAI LIGVSCYGSV PQAQEAAMQG ADYVAFGSFF ASPSKPQAPV VSVDVLTAAR AMIDLPIVAI GGITEANGRA LIAAGADALA VISGVFAAED VEGAARRFTA LFNNRKE // ID E6QSJ8_9ZZZZ Unreviewed; 310 AA. AC E6QSJ8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=NUDIX hydrolase; GN ORFNames=CARN7_0987; OS mine drainage metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=410659; RN [1] RP NUCLEOTIDE SEQUENCE. RA Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F., RA Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C., RA Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O., RA Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N., RA Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P., RA Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., RA Medigue C., Le Paslier D.; RT "Diversity of trophic interactions inside an arsenic-rich microbial RT ecosystem."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CABR01000076; CBI10220.1; -; Genomic_DNA. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 310 AA; 33776 MW; 141ABD4977C4BA9C CRC64; MNQLASLPVI AVSAGILYRP DGTILLASRP ADKPWPGYWE FPGGKIEAGE TSRQALTREL EEELGIQVTH AMPWLTLTHN YPTACVCLNC FLIDAWQGDP TPREGQILSW QHPDAVNVTP LLPANLPLLR ALCLPPIMGI THIENDPVGF LKKLDAALLA GLKLIQLREA ELTQHYAETV IARAHQHGAQ VVINQDVNLA QRTQADGIHL TAKQLADTVM RPDFRLVGAS CHNQLELDHA EHLGCDYALL SPVLPTASHP GATVLGWDKF TELAQGRSLP VYALGGMTQS LLTAARERGA HGIALLRGIW // ID E6RB54_CRYGW Unreviewed; 537 AA. AC E6RB54; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-APR-2014, entry version 18. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative; GN OrderedLocusNames=CGB_H4330W; OS Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071) OS (Filobasidiella gattii) (Cryptococcus bacillisporus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Tremellomycetes; Tremellales; Tremellaceae; Filobasidiella; OC Filobasidiella/Cryptococcus neoformans species complex. OX NCBI_TaxID=367775; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WM276 / ATCC MYA-4071; RX PubMed=21304167; DOI=10.1128/mBio.00342-10; RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G., RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., RA Sawkins J., McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., RA Bartlett K., Li W., Wang X., Heitman J., Stajich J.E., Fraser J.A., RA Meyer W., Carter D., Schein J., Krzywinski M., Kwon-Chung K.J., RA Varma A., Wang J., Brunham R., Fyfe M., Ouellette B.F.F., Siddiqui A., RA Marra M., Jones S., Holt R., Birren B.W., Galagan J.E., Cuomo C.A.; RT "Genome variation in Cryptococcus gattii, an emerging pathogen of RT immunocompetent hosts."; RL MBio 2:E342-E342(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WM276; RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G., RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., RA Sawkins J., McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., RA Bartlett K., Li W., Wang X., Heitman J., Stajich J.E., Fraser J.A., RA Meyer W., Carter D., Schein J., Krzywinski M., Kwong-Chung K.J., RA Varma A., Wang J., Brunham R., Fyfe M., Ouellette B.F.F., Siddiqui A., RA Marra M., Jones S., Holt R., Birren B.W., Galagan J.E., Cuomo C.A.; RT "Genome variation in Cryptococcus gattii, an emerging pathogen of RT immunocompetent hosts."; RL MBio 0:0-0(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000293; ADV24041.1; -; Genomic_DNA. DR RefSeq; XP_003195828.1; XM_003195780.1. DR GeneID; 10185780; -. DR KEGG; cgi:CGB_H4330W; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 537 AA; 57158 MW; 1E266AE18AE13EAA CRC64; MTKPNLDYSL YLVTGRELLP PGKDYYESLE ESLQGGVTLV QVREKDADTG EFIEVARRTK AICDKYNVPV LINDRIDVHL AVGTAGIHVG QTDCPIGLAR SLVGPDAIIG LSVGNVNEAK RAIQQGADYV GIGAVWPTNS KDVTKKNMLG PDGVGEILDL LHGTGVQSVA IGGIHLPNVA QLLHASIAPQ SRNALDGIAI ISDIVASFTP REAAKNLREV VQSFKRARSQ LANLEAVYGA NLFISPRNID DFIKEAVHLT DMIKKVTPLV NQMTNNVVIN DSANVTLAIG ASPIMATHPR DVYDLSPAIG ALLINFGTVT DKAGMLVAGR QANVNRKPIV FDPVAIGATP YRQETSVELL AHWQPTIIKG NAAEIGFMAK STEVASRGVD SVGSGFSDPG AIVKALARKQ AAIIVLTGEH DYISDGSTTL KIFNGHHYLE RITGSGCQLG SVIASFAAAA RLDHLAKYGE WENASQLVQG DMLAAAVTGV LVYTIAAEVA AAREDVKGPG TFRAALIDEL YNLTPEVLQQ RANIEIV // ID E6RJX8_PSEU9 Unreviewed; 508 AA. AC E6RJX8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 26. DE SubName: Full=Phosphomethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN Name=thiDE; OrderedLocusNames=PSM_A0374; OS Pseudoalteromonas sp. (strain SM9913). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=234831; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM9913; RX PubMed=20703316; DOI=10.1038/ismej.2010.103; RA Qin Q.L., Li Y., Zhang Y.J., Zhou Z.M., Zhang W.X., Chen X.L., RA Zhang X.Y., Zhou B.C., Wang L., Zhang Y.Z.; RT "Comparative genomics reveals a deep-sea sediment-adapted life style RT of Pseudoalteromonas sp. SM9913."; RL ISME J. 5:274-284(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001796; ADT67328.1; -; Genomic_DNA. DR RefSeq; YP_004067480.1; NC_014803.1. DR EnsemblBacteria; ADT67328; ADT67328; PSM_A0374. DR GeneID; 10037269; -. DR KEGG; psm:PSM_A0374; -. DR PATRIC; 45328141; VBIPseSp136886_0998. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR BioCyc; PSP234831:GH93-381-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 508 AA; 54958 MW; A3FC561A74DF6A86 CRC64; MTNVVWTIAG SDSGGGAGIQ ADIKAMQSFG VHGCTAITAL TAQNSLGVEA INAVSTDIIE SQLLALEKDM KAKVIKIGML ANVQQIQLIS EHISHYKAKW PTPPVIVYDP VAIASSGDLL TEEDTVSAIK ECLLPLVDVI TPNTHETQLL TGVYLIGPAA IKEAASKLMA WGAKAVVIKG GHWDYPSGYC IDYCTQNGED YWLGNEKIQV PHSHGTGCSM ASVIAACLAK DYPLKDAFIL AKAYINQGLK QSVRYGEGIG PVAQTQFPTN LAHYPQVIEP GSWLGDELDF DVPLDFNMAA DFAACESKKL GLYGVVDSIE WLEKCLQQGI KTAQLRVKNK TQNELDELIA KAVTLGEQYN AQVFINDYWQ LAIKHGAYGV HLGQEDLESA NLVAIKEAGL RLGLSTHGFY EMLRAHNYRP SYMAFGAIYP TTTKDMTGQI QGLEKLTRFV PLMQSYPTVA IGGIDLNRAQ EVAKTGVGSV AVVRAITEAD DYVEAINTLK SVINENAC // ID E6RSD3_CAMJS Unreviewed; 201 AA. AC E6RSD3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=CJS3_1092; OS Campylobacter jejuni subsp. jejuni (strain S3). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=718271; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S3; RX PubMed=21217004; DOI=10.1128/JB.01475-10; RA Cooper K.K., Cooper M.A., Zuccolo A., Law B., Joens L.A.; RT "Complete genome sequence of Campylobacter jejuni strain S3."; RL J. Bacteriol. 193:1491-1492(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001960; ADT72815.1; -; Genomic_DNA. DR RefSeq; YP_005659651.1; NC_017281.1. DR ProteinModelPortal; E6RSD3; -. DR EnsemblBacteria; ADT72815; ADT72815; CJS3_1092. DR GeneID; 12246213; -. DR KEGG; cjs:CJS3_1092; -. DR PATRIC; 45419080; VBICamJej157961_1086. DR KO; K00788; -. DR BioCyc; CJEJ718271:GLAE-1096-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID E6RSG9_CAMJS Unreviewed; 200 AA. AC E6RSG9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CJS3_1128; OS Campylobacter jejuni subsp. jejuni (strain S3). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=718271; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S3; RX PubMed=21217004; DOI=10.1128/JB.01475-10; RA Cooper K.K., Cooper M.A., Zuccolo A., Law B., Joens L.A.; RT "Complete genome sequence of Campylobacter jejuni strain S3."; RL J. Bacteriol. 193:1491-1492(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001960; ADT72851.1; -; Genomic_DNA. DR RefSeq; YP_005659687.1; NC_017281.1. DR EnsemblBacteria; ADT72851; ADT72851; CJS3_1128. DR GeneID; 12246249; -. DR KEGG; cjs:CJS3_1128; -. DR PATRIC; 45419150; VBICamJej157961_1121. DR KO; K00788; -. DR BioCyc; CJEJ718271:GLAE-1132-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 29 33 HMP-PP binding (By similarity). FT REGION 124 126 THZ-P binding (By similarity). FT METAL 62 62 Magnesium (By similarity). FT METAL 81 81 Magnesium (By similarity). FT BINDING 61 61 HMP-PP (By similarity). FT BINDING 100 100 HMP-PP (By similarity). FT BINDING 127 127 HMP-PP (By similarity). FT BINDING 153 153 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 200 AA; 21830 MW; A9F1CC921184020D CRC64; MVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSSIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID E6RY89_CAMJC Unreviewed; 201 AA. AC E6RY89; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-APR-2014, entry version 20. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=ICDCCJ07001_1006; OS Campylobacter jejuni subsp. jejuni serotype HS:41 (strain OS ICDCCJ07001). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=757425; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ICDCCJ07001; RX PubMed=21124772; DOI=10.1371/journal.pone.0015060; RA Zhang M., He L., Li Q., Sun H., Gu Y., You Y., Meng F., Zhang J.; RT "Genomic Characterization of the Guillain-Barre Syndrome-Associated RT Campylobacter jejuni ICDCCJ07001 Isolate."; RL PLoS ONE 5:E15060-E15060(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002029; ADT66346.1; -; Genomic_DNA. DR RefSeq; YP_004066535.1; NC_014802.1. DR ProteinModelPortal; E6RY89; -. DR EnsemblBacteria; ADT66346; ADT66346; ICDCCJ07001_1006. DR GeneID; 10036273; -. DR KEGG; cjn:ICDCCJ_1006; -. DR PATRIC; 45194542; VBICamJej156877_1181. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR BioCyc; CJEJ757425:GJ7N-1007-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 23390 MW; 081449B92607D5F2 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RGCLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID E6RYC2_CAMJC Unreviewed; 210 AA. AC E6RYC2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ICDCCJ07001_1040; OS Campylobacter jejuni subsp. jejuni serotype HS:41 (strain OS ICDCCJ07001). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=757425; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ICDCCJ07001; RX PubMed=21124772; DOI=10.1371/journal.pone.0015060; RA Zhang M., He L., Li Q., Sun H., Gu Y., You Y., Meng F., Zhang J.; RT "Genomic Characterization of the Guillain-Barre Syndrome-Associated RT Campylobacter jejuni ICDCCJ07001 Isolate."; RL PLoS ONE 5:E15060-E15060(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002029; ADT66379.1; -; Genomic_DNA. DR RefSeq; YP_004066568.1; NC_014802.1. DR EnsemblBacteria; ADT66379; ADT66379; ICDCCJ07001_1040. DR GeneID; 10036307; -. DR KEGG; cjn:ICDCCJ_1040; -. DR PATRIC; 45194632; VBICamJej156877_1223. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; CJEJ757425:GJ7N-1041-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23027 MW; 62A5FD22439A7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKKSS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID E6S1H1_HELPF Unreviewed; 219 AA. AC E6S1H1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HMPREF4655_20753; OS Helicobacter pylori (strain 35A). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=585535; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=35A; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RT "Complete genome sequence of Helicobacter pylori 35A."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=35A; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002096; ADU40873.1; -; Genomic_DNA. DR RefSeq; YP_005769865.1; NC_017360.1. DR EnsemblBacteria; ADU40873; ADU40873; HMPREF4655_20753. DR GeneID; 12349364; -. DR KEGG; hpo:HMPREF4655_20753; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; HPYL585535:GLE3-738-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23891 MW; 522AC443FE259158 CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLALQDP IEIKQLALKC QKLCQKYGVP FIVNDEVKLA LELKADGVHV GQEDMAIEEV MTLCKKCQFI GLSVNTLEQA LKARHLDGVA YLGVGPIFLT QSKKDKQVVG VELLKKIKDS GVKKPLVAIG GITTHNASKL REYGGIAVIS AIAQAKDKAL AVEKLLNNA // ID E6S721_INTC7 Unreviewed; 248 AA. AC E6S721; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN OrderedLocusNames=Intca_1400; OS Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / OS NBRC 12989 / 7 KIP). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Intrasporangiaceae; Intrasporangium. OX NCBI_TaxID=710696; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP; RX PubMed=21304734; DOI=10.4056/sigs.1263355; RA Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S., RA Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Complete genome sequence of Intrasporangium calvum type strain (7 RT KIP)."; RL Stand. Genomic Sci. 3:294-303(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002343; ADU47916.1; -; Genomic_DNA. DR RefSeq; YP_004098643.1; NC_014830.1. DR EnsemblBacteria; ADU47916; ADU47916; Intca_1400. DR GeneID; 10084208; -. DR KEGG; ica:Intca_1400; -. DR PATRIC; 45244287; VBIIntCal153415_1423. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; ICAL710696:GH9U-1426-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 248 AA; 25710 MW; 878A361534EDBCB3 CRC64; MVSLREAAGL AIAVTDRSQV PGNRPLLDVV RAVLEGGAHG VLVRERDLAD EERAALVTGV GPLCAEHQAL LLVASPLPHP HLPHPHLPPP QGRCDRSRSA SVDHIESGEG RRLGLHLRRH EGVPADLDRV ATFVGRSCHD LAELRRAADD GLDHVTLSPV AASVSKPGHG PALGPAGLRR LASTVRREHP TPPVIFALGG VDAANAGHWI AAGADGVAVM GAVMRAADPT AAMRAVVDSV RAARAGAS // ID E6S725_INTC7 Unreviewed; 227 AA. AC E6S725; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Intca_1404; OS Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / OS NBRC 12989 / 7 KIP). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Intrasporangiaceae; Intrasporangium. OX NCBI_TaxID=710696; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP; RX PubMed=21304734; DOI=10.4056/sigs.1263355; RA Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S., RA Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Complete genome sequence of Intrasporangium calvum type strain (7 RT KIP)."; RL Stand. Genomic Sci. 3:294-303(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002343; ADU47920.1; -; Genomic_DNA. DR RefSeq; YP_004098647.1; NC_014830.1. DR EnsemblBacteria; ADU47920; ADU47920; Intca_1404. DR GeneID; 10084212; -. DR KEGG; ica:Intca_1404; -. DR PATRIC; 45244295; VBIIntCal153415_1427. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; ICAL710696:GH9U-1430-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 22710 MW; FC19BB0CF65308A0 CRC64; MTQSPRPFPR LHVLTDTRGG RDPLREVRCA IATGRAAVQV RAKDHTDREV LALTTAILGL ARPAGTLVIV DDRVDVALAA GADGVHLGAT DLPVAEVRRV VPAGFVIGAT VRTPDMARAA ESAGATYLGA GPAHATTTKA GLPEPLGPPG LRAVTAATEL PVIAIGGVTP ELVPALLAAG AHGVAVVAAL SEAADPAATA AALTAALVGP SDQCDGEPAD GRIEVRP // ID E6SIE4_THEM7 Unreviewed; 232 AA. AC E6SIE4; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tmar_1855; OS Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM OS 10246 / 7p75a). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XVII. Incertae Sedis; Thermaerobacter. OX NCBI_TaxID=644966; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a; RX DOI=10.4056/sigs.1373474; RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L., RA Pitluck S., Pagani I., Ivanova N., Mavromatis K., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y., RA Jeffries C., Schneider S., Rohde M., Goker M., Pukall R., Woyke T., RA Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., RA Klenk H., Detter J.; RT "Complete genome sequence of Thermaerobacter marianensis type strain RT (7p75aT)."; RL Stand. Genomic Sci. 3:337-345(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002344; ADU51955.1; -; Genomic_DNA. DR RefSeq; YP_004102682.1; NC_014831.1. DR EnsemblBacteria; ADU51955; ADU51955; Tmar_1855. DR GeneID; 10082238; -. DR KEGG; tmr:Tmar_1855; -. DR PATRIC; 45380992; VBITheMar50867_1902. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR BioCyc; TMAR644966:GHKT-1894-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 232 AA; 24041 MW; 6F9285AB1CFB5B72 CRC64; MAGAVVHLIT DRGTAPDLVG AVASALSGGV HWVQLRDKSP AARDLLELAR RIQPLCQDHR AGLLINDRLD VALAAGCHGV HLAKKSLPVK EARRLVPANL LVGVSVHSVE EAVAAAADGA DYVTFGSVFP TRSHPGRPAA GVDLLAQVVH AVNIPVLAIG GITPDNVDAV LATGVAGVAV ISSILAEADP ARAAARLRET MERSQHRPRF PFPPVGPFPD AHRCAGPPPP GR // ID E6SJ40_THEM7 Unreviewed; 241 AA. AC E6SJ40; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tmar_1981; OS Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM OS 10246 / 7p75a). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XVII. Incertae Sedis; Thermaerobacter. OX NCBI_TaxID=644966; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a; RX DOI=10.4056/sigs.1373474; RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L., RA Pitluck S., Pagani I., Ivanova N., Mavromatis K., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y., RA Jeffries C., Schneider S., Rohde M., Goker M., Pukall R., Woyke T., RA Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., RA Klenk H., Detter J.; RT "Complete genome sequence of Thermaerobacter marianensis type strain RT (7p75aT)."; RL Stand. Genomic Sci. 3:337-345(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002344; ADU52064.1; -; Genomic_DNA. DR RefSeq; YP_004102791.1; NC_014831.1. DR EnsemblBacteria; ADU52064; ADU52064; Tmar_1981. DR GeneID; 10082364; -. DR KEGG; tmr:Tmar_1981; -. DR PATRIC; 45381218; VBITheMar50867_2014. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR BioCyc; TMAR644966:GHKT-2020-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 73 77 HMP-PP binding (By similarity). FT REGION 169 171 THZ-P binding (By similarity). FT METAL 106 106 Magnesium (By similarity). FT METAL 125 125 Magnesium (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 HMP-PP (By similarity). FT BINDING 199 199 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 241 AA; 24727 MW; 70A68B6B87A45716 CRC64; MERWTPEGSG GRGGDRREGG GDEPPAVGGR PGGGSPLPQR LAVYFIYDLG LSGEGDPAPL LRPVLEAGIR AVQLRAKEVP DRVAYRVAVA VRDLTARFGA LLIVNDRLDL ALAAAADGVH LGQDDLPAEA ARRLWPEGLL GVSVRTPVEA RAAEAAGADY VGAGALRSTS TKPDSRVIGL EGLAAVVGAT RLPVIAIGGI TVDDLPALRR LGVAGVAVAS AIARAADPRQ AAAAFLRAWT C // ID E6SU56_BACT6 Unreviewed; 224 AA. AC E6SU56; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Bache_2361; OS Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / P OS 36-108). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=693979; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P 36-108; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Bacteroides helcogenes P 36-108."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35417 / DSM 20613 / JCM 6297 / P 36-108; RX DOI=10.4056/sigs.1513795; RA Pati A., Gronow S., Zeytun A., Lapidus A., Nolan M., Hammon N., RA Deshpande S., Cheng J., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Detter J., RA Brambilla E., Rohde M., Goker, M., Woyke T., Bristow J., Eisen J., RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lucas S.; RT "Complete genome sequence of Bacteroides helcogenes type strain (P 36- RT 108)."; RL Stand. Genomic Sci. 4:45-53(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002352; ADV44329.1; -; Genomic_DNA. DR RefSeq; YP_004161915.1; NC_014933.1. DR EnsemblBacteria; ADV44329; ADV44329; Bache_2361. DR GeneID; 10141145; -. DR KEGG; bhl:Bache_2361; -. DR PATRIC; 45175370; VBIBacHel147569_2475. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR BioCyc; BHEL693979:GHID-2422-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24898 MW; C775D097471CA065 CRC64; MKTMEKESLI RKNGNVQFIT HYTECYSYLD AARIALEGGC RWIQLRMKDA PLEEVESTAR QVRQLCQQQG ALFIIDDHVE LAKIYADGVH LGKMDMPIAD ARCILGETYI IGGTANSFED VRQHYEAGAD YIGCGPFRYT TTKKNLSPIL GTDGYADIVR RMEASHISLP IVAIGGIMPD DIKEIMQTGV TGIALSGSVL RAKNPIEEMK RTVAEANRTI NHCK // ID E6SU61_BACT6 Unreviewed; 196 AA. AC E6SU61; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bache_2366; OS Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / P OS 36-108). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=693979; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P 36-108; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Bacteroides helcogenes P 36-108."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35417 / DSM 20613 / JCM 6297 / P 36-108; RX DOI=10.4056/sigs.1513795; RA Pati A., Gronow S., Zeytun A., Lapidus A., Nolan M., Hammon N., RA Deshpande S., Cheng J., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Detter J., RA Brambilla E., Rohde M., Goker, M., Woyke T., Bristow J., Eisen J., RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lucas S.; RT "Complete genome sequence of Bacteroides helcogenes type strain (P 36- RT 108)."; RL Stand. Genomic Sci. 4:45-53(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002352; ADV44334.1; -; Genomic_DNA. DR RefSeq; YP_004161920.1; NC_014933.1. DR EnsemblBacteria; ADV44334; ADV44334; Bache_2366. DR GeneID; 10141150; -. DR KEGG; bhl:Bache_2366; -. DR PATRIC; 45175380; VBIBacHel147569_2480. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR OMA; ANAVENF; -. DR BioCyc; BHEL693979:GHID-2427-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 196 AA; 21905 MW; EBED0DBAFE4A26DD CRC64; MKLIVITTPC FFEGEAKEIT SLFRAGLEVL HLRKPGASAE ETEHLLRQLP EQYMQRIVIH EHFHLASVFN LRGIHLNRRS PDVPHGYVGH VSLSCHSLNE VAKYKSACDY VFLSPIFDSI SKEGYASAFS HRELCEARKV GIIDSKVMAL GGITAGCLRK IEALGFGGAA LLGDIWNREK SDVVSHFLEL RQSYNP // ID E6SVS0_BACT6 Unreviewed; 202 AA. AC E6SVS0; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bache_2548; OS Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / P OS 36-108). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=693979; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P 36-108; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Bacteroides helcogenes P 36-108."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35417 / DSM 20613 / JCM 6297 / P 36-108; RX DOI=10.4056/sigs.1513795; RA Pati A., Gronow S., Zeytun A., Lapidus A., Nolan M., Hammon N., RA Deshpande S., Cheng J., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Detter J., RA Brambilla E., Rohde M., Goker, M., Woyke T., Bristow J., Eisen J., RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lucas S.; RT "Complete genome sequence of Bacteroides helcogenes type strain (P 36- RT 108)."; RL Stand. Genomic Sci. 4:45-53(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002352; ADV44509.1; -; Genomic_DNA. DR RefSeq; YP_004162095.1; NC_014933.1. DR EnsemblBacteria; ADV44509; ADV44509; Bache_2548. DR GeneID; 10141340; -. DR KEGG; bhl:Bache_2548; -. DR PATRIC; 45175780; VBIBacHel147569_2671. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR BioCyc; BHEL693979:GHID-2617-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 23484 MW; 788581A41B06574C CRC64; MKLIVVTAPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHRRIVTH EHFYLQEEFN LMGIHLNARN PNEPHDYSGH ISCTCHSMEE IQSKKHFYDY LFLSPIYNCI TKNGVTSGFT AEELRQAGKN KIVDNRVMAL GGITPDNILE IKDYGFGGAV VMGDLWNKFN TRTDRDYLEI IRHFKKLKEM SD // ID E6SZS8_SHEB6 Unreviewed; 642 AA. AC E6SZS8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 24. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Sbal678_2439; OS Shewanella baltica (strain OS678). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=693973; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS678; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., RA Konstantinidis K., Deng J.I., Hofle M., Brettar I., Tiedje J., RA Auchtung J., Woyke T.; RT "Complete sequence of chromosome of Shewanella baltica OS678."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002383; ADT94591.1; -; Genomic_DNA. DR RefSeq; YP_005273643.1; NC_016901.1. DR ProteinModelPortal; E6SZS8; -. DR EnsemblBacteria; ADT94591; ADT94591; Sbal678_2439. DR GeneID; 11772552; -. DR KEGG; sbt:Sbal678_2439; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR BioCyc; SBAL693973:GJDB-2500-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 642 AA; 67935 MW; ADC00DA2DF19E784 CRC64; MQGIHGGKLP MSTERPAFVW TIAGSDSGGG AGIQADLATI QDLGCHGCSV VTTVTAQSSV AVTLVEPVSA AMLMAQLTTL LSDLPPKAIK IGLLADQTQV ALLADWIASF KIHYPSVPVI VDPVMVASCG DALAVDNCQD IKSAAKSALD FRPFKGLIEL ITPNVLELGR LTHSDVSTKA QFAAAALALS QSLDCSVLAK GGDVSFGSTD ILENTHAKTH DNTYAQTQAN AHNSNGWDLE LAEDYLVCHQ VRASSKLHQN GRFWLASQRV NTRHNHGSGC TLSSAIAAVL AQGFVLQDAV VVAKAYVSQG LSAAIGLGQG PGPLARTGWP NNLSRYAKIN LCDGNFIRHH LNRHLDVRSD LVATVLSATD QATAQVRIAS TPPQNILSHG FKVLDAELGV YPVVSDLTML ESLLAAGVKT VQLRIKTDIS ELTTTTAPAE SDLGKSALGR CESGEPELIG SELEAQIQTA IALGKHFNAQ LFINDHWKLA IKYHAFGVHL GQEDLAVTDL AAIQAAGLAL GISSHSYFEL LLAHQYSPSY IALGHIFPTT TKQMPSAPQG LAKLKHYVAL LQGHYPLVAI GGIDLTNLAK VKATGVGNIA VVRAITKAKE PVAAFAELSQ AWEQCSLCEE LAVKQELDAK HE // ID E6TA16_MYCSR Unreviewed; 224 AA. AC E6TA16; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mspyr1_05790; OS Mycobacterium sp. (strain Spyr1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=278137; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Spyr1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., RA Hauser L., Koukkou A.I., Drainas C., Kyrpides N., Woyke T.; RT "Complete sequence of chromosome of Mycobacterium sp. Spyr1."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002385; ADT97288.1; -; Genomic_DNA. DR RefSeq; YP_004075123.1; NC_014814.1. DR EnsemblBacteria; ADT97288; ADT97288; Mspyr1_05790. DR GeneID; 10044976; -. DR KEGG; msp:Mspyr1_05790; -. DR PATRIC; 45282211; VBIMycSp109077_0812. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; MSP278137:GHD6-575-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23430 MW; F4A2D89EEBA5C4F0 CRC64; MPESPSLQGA RLYLCTDARR ERGDLADFAD AALAGGVDII QLRDKGSPGE KAFGPLEARA EIDALHVLAE AARRHNALVA VNDRADIARA SGADVLHLGQ DDLPLTVARQ IVGDRVVGRS THDLAQAEAA IADGPDAPDY FCVGPCWPTP TKPGRAAPGL DLVREVAALN TAKPWFAIGG IDAQRLPDVL DAGARRVVVV RAITAAEDPR AAAEQLAGML DSAV // ID E6U035_BACCJ Unreviewed; 216 AA. AC E6U035; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Bcell_0758; OS Bacillus cellulosilyticus (strain ATCC 21833 / DSM 2522 / FERM P-1141 OS / JCM 9156 / N-4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=649639; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Brumm P., Mead D., Woyke T.; RT "Complete sequence of Bacillus cellulosilyticus DSM 2522."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002394; ADU29039.1; -; Genomic_DNA. DR RefSeq; YP_004093770.1; NC_014829.1. DR ProteinModelPortal; E6U035; -. DR EnsemblBacteria; ADU29039; ADU29039; Bcell_0758. DR GeneID; 10087295; -. DR KEGG; bco:Bcell_0758; -. DR PATRIC; 45157350; VBIBacCel7049_0789. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; BCEL649639:GHTT-803-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23016 MW; E9AE7DECBAD46DDF CRC64; MARINSDKMK DFLKVYFIAG STNVHGSLPT VLQQAIEGGI SIFQFREKGN GALTGESKIT LARELQQLCQ KASIPFIVND DIDLAIELDA DGVHIGQEDD NIIEVRKKIG DRILGVSAHT LDEAKAALAS GADYLGVGPV FPTSSKADTR EVCGPHFIEE LRHEGIDAPI VAIGGINVEN ATQVVHGKAD GLSVISAISS ANDPSDAVKM LNEAWK // ID E6U039_BACCJ Unreviewed; 199 AA. AC E6U039; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bcell_0762; OS Bacillus cellulosilyticus (strain ATCC 21833 / DSM 2522 / FERM P-1141 OS / JCM 9156 / N-4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=649639; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Brumm P., Mead D., Woyke T.; RT "Complete sequence of Bacillus cellulosilyticus DSM 2522."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002394; ADU29043.1; -; Genomic_DNA. DR RefSeq; YP_004093774.1; NC_014829.1. DR ProteinModelPortal; E6U039; -. DR EnsemblBacteria; ADU29043; ADU29043; Bcell_0762. DR GeneID; 10087299; -. DR KEGG; bco:Bcell_0762; -. DR PATRIC; 45157358; VBIBacCel7049_0793. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR BioCyc; BCEL649639:GHTT-807-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 199 AA; 21780 MW; 7320C3E2B6B93868 CRC64; MTRKEIHVIS NGKQPLEEFA QCARLILSDV DYFHVREKQL SAKQLSDGID ILLQHGIPAE KIVVNDRVDV AAVRNVAGVQ LAYHSLKVNE VKQRFPELKI GKSVHSIEEA IDAERLGADY VLYGHIFTSK SKPDVTPRGI RQLEALVNEV SIPVIAIGGI TPFNVESVMS AGARGVAIMS GILEAEDPLS MIKLYKNGG // ID E6U7L2_ETHHY Unreviewed; 221 AA. AC E6U7L2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ethha_1498; OS Ethanoligenens harbinense (strain DSM 18485 / JCM 12961 / CGMCC 1.5033 OS / YUAN-3). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ethanoligenens. OX NCBI_TaxID=663278; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18485 / JCM 12961 / CGMCC 1.5033 / YUAN-3; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., Wang A., Mouttaki H., He Z., Zhou J., Hemme C.L., RA Woyke T.; RT "Complete sequence of Ethanoligenens harbinense YUAN-3."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002400; ADU27035.1; -; Genomic_DNA. DR RefSeq; YP_004091766.1; NC_014828.1. DR ProteinModelPortal; E6U7L2; -. DR EnsemblBacteria; ADU27035; ADU27035; Ethha_1498. DR GeneID; 10092474; -. DR KEGG; eha:Ethha_1498; -. DR PATRIC; 45210191; VBIEthHar145175_1638. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; EHAR663278:GIWT-1535-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23801 MW; 3E757E263644080D CRC64; MSAQAKRAEK VAAYLNGLYC ITAEPLSCGR ENLDVVRAML VGGAKVVQYR EKDMPMQRQY EQCLKLREMT REANALLIVD DHVHLAMAVG ADGVHIGQTD LPIEAVRALV GAEMLIGLST HDIGQARDAV ARGADYIGVG PIFETHTKSD VVAPVGFAYL DAVVREIRLP FVAIGGIKQH NLPDVLTHGA ACAALVTEIV QAPDISGMVK ELRQIFSAQT T // ID E6UC23_RUMA7 Unreviewed; 201 AA. AC E6UC23; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 11-DEC-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Rumal_2159; OS Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO OS 2250 / 7). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=697329; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7; RX PubMed=21914885; DOI=10.1128/JB.05621-11; RA Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A., RA Cheng J.F., Detter C., Detter J.C., Goodwin L.A., Han C.S., RA Hauser L.J., Ivanova N.N., Kyrpides N.C., Land M.L., Lapidus A., RA Lucas S., Ovchinnikova G., Pitluck S., Tapia R., Woyke T., Boyum J., RA Mead D., Weimer P.J.; RT "Complete genome of the cellulolytic ruminal bacterium Ruminococcus RT albus 7."; RL J. Bacteriol. 193:5574-5575(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002403; ADU22645.1; -; Genomic_DNA. DR RefSeq; YP_004105279.1; NC_014833.1. DR EnsemblBacteria; ADU22645; ADU22645; Rumal_2159. DR GeneID; 10078429; -. DR KEGG; ral:Rumal_2159; -. DR PATRIC; 45360810; VBIRumAlb150544_2924. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; RALB697329:GIWQ-2206-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 22232 MW; D80E81ADB14E4787 CRC64; MCKIICITNR KLCRVDFSVQ LEKIAAAQPD MVILREKDMR EDEYSILAEK SAEICRKYEV PFAVNSFRNT ALKKGIKRIH LPLHILRELT PEDKAVFDII GTSVHSKEDT EEAVALGAGY IIAGHIFETE CKKGLAGRGT DFLKEICNTV KLPVYAIGGI TADNAAECIK AGADGICLMS SFMQAENVSE FMDRLRGVMN G // ID E6UC24_RUMA7 Unreviewed; 210 AA. AC E6UC24; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rumal_2160; OS Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO OS 2250 / 7). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=697329; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7; RX PubMed=21914885; DOI=10.1128/JB.05621-11; RA Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A., RA Cheng J.F., Detter C., Detter J.C., Goodwin L.A., Han C.S., RA Hauser L.J., Ivanova N.N., Kyrpides N.C., Land M.L., Lapidus A., RA Lucas S., Ovchinnikova G., Pitluck S., Tapia R., Woyke T., Boyum J., RA Mead D., Weimer P.J.; RT "Complete genome of the cellulolytic ruminal bacterium Ruminococcus RT albus 7."; RL J. Bacteriol. 193:5574-5575(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002403; ADU22646.1; -; Genomic_DNA. DR RefSeq; YP_004105280.1; NC_014833.1. DR ProteinModelPortal; E6UC24; -. DR EnsemblBacteria; ADU22646; ADU22646; Rumal_2160. DR GeneID; 10078430; -. DR KEGG; ral:Rumal_2160; -. DR PATRIC; 45360812; VBIRumAlb150544_2925. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; RALB697329:GIWQ-2207-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22013 MW; 90B702E50BBA8F7F CRC64; MVNVDVTLYA ITDRGAIGQR DFYEAIEAAL KGGATILQLR EKGLDEVSLI EEAKKVKNIC SRYGVPLIIN DNYKAAIASG ADGVHVGIED APVAEIRSKA GSGFIIGATA KTVEQAKAAQ AAGADYLGVG AVFPSTTKKN AIRITNEQLR EIAASVDIPV TAIGGISKSN MTELKGCGAD GAALVSAIFA AENIETECRE LKKLSQEVFR // ID E6USM7_CLOTL Unreviewed; 356 AA. AC E6USM7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Clo1313_1628; OS Clostridium thermocellum (strain DSM 1313 / LMG 6656 / LQ8). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=637887; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 1313 / LMG 6656 / LQ8; RX PubMed=21460082; DOI=10.1128/JB.00322-11; RA Feinberg L., Foden J., Barrett T., Davenport K.W., Bruce D., RA Detter C., Tapia R., Han C., Lapidus A., Lucas S., Cheng J.F., RA Pitluck S., Woyke T., Ivanova N., Mikhailova N., Land M., Hauser L., RA Argyros D.A., Goodwin L., Hogsett D., Caiazza N.; RT "Complete genome sequence of the cellulolytic thermophile Clostridium RT thermocellum DSM1313."; RL J. Bacteriol. 193:2906-2907(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002416; ADU74689.1; -; Genomic_DNA. DR RefSeq; YP_005688140.1; NC_017304.1. DR ProteinModelPortal; E6USM7; -. DR EnsemblBacteria; ADU74689; ADU74689; Clo1313_1628. DR GeneID; 12421357; -. DR KEGG; ctx:Clo1313_1628; -. DR PATRIC; 45478090; VBICloThe140364_1763. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR BioCyc; CTHE637887:GLBN-1670-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 183 187 HMP-PP binding (By similarity). FT REGION 280 282 THZ-P binding (By similarity). FT REGION 331 332 THZ-P binding (By similarity). FT METAL 216 216 Magnesium (By similarity). FT METAL 235 235 Magnesium (By similarity). FT BINDING 215 215 HMP-PP (By similarity). FT BINDING 254 254 HMP-PP (By similarity). FT BINDING 283 283 HMP-PP (By similarity). FT BINDING 311 311 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 356 AA; 40444 MW; 3C88F277A3F463FC CRC64; MGLDNLYRVL DANVNRTSEG LRVLEDLARF CYNDRLLSKR IKELRHSVRK NIAGLVPNLI SSRDSVNDVG LKTSMEMDID RKASLLDLAR ANFKRVQEAL RTVEESLKVL NENDLSKFYE SCRFETYSIE KEYFKVLTFE NKKGRLNEII TGLYCITSEE HSKGRSNIEV VEKMIKAGVK IIQYREKKKS LLEKYNECKK IREMTLDSGV TFIVNDNIDI AMMVKADGVH IGQDDLPIEK VRELVGDEMI IGISTHSPTQ AEDAVRRGAD YIGVGPLYRT YTKEDVCEPV GLEYLDYVVK NINIPYVAIG GIKEHNMDEV LARGARCIAM VTEIVGADDI EEKISKVKSK FSRGVL // ID E6V1P6_VARPE Unreviewed; 314 AA. AC E6V1P6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Varpa_2602; OS Variovorax paradoxus (strain EPS). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=595537; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EPS; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P., RA Han J.-I.G., Woyke T.; RT "Complete sequence of Variovorax paradoxus EPS."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002417; ADU36802.1; -; Genomic_DNA. DR RefSeq; YP_004154913.1; NC_014931.1. DR EnsemblBacteria; ADU36802; ADU36802; Varpa_2602. DR GeneID; 10129435; -. DR KEGG; vpe:Varpa_2602; -. DR PATRIC; 45391238; VBIVarPar156291_2657. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR BioCyc; VPAR595537:GHGJ-2627-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 314 AA; 32795 MW; 726DF1B11E9B822E CRC64; MSGVSDMNDA RAIAHAIVAA HGLRFGAITA STVGATSFSS NDAVYRGAKQ ACTALGFIEV DAECLALAWH AQTERIGHFD AARWPDAPAD FGMRSFPPAA RDDAFLPCPE RLGLYAVLPD AAWVGRMARA GVPTVQLRFK SDDAAAVERE VQAAVEAVQG TGALLFINDH WQVAIAARAY GIHLGQEDLD ALSPDELQQL RASGLRLGVS THGYAEMVRA DAVSPSYIAM GAVYPTTLKK MATAPQGVAR LAAYARLLRG YPQVGIGGID AVRLPEVLAT GVGSVAVVRA LVTAADPEAT AAQWMAAMGA AIGN // ID E6VD95_RHOPX Unreviewed; 219 AA. AC E6VD95; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Rpdx1_1104; OS Rhodopseudomonas palustris (strain DX-1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=652103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DX-1; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Misra M., Chertkov O., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., RA Logan B., Oda Y., Harwood C., Woyke T.; RT "Complete sequence of Rhodopseudomonas palustris DX-1."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002418; ADU42730.1; -; Genomic_DNA. DR RefSeq; YP_004107463.1; NC_014834.1. DR ProteinModelPortal; E6VD95; -. DR EnsemblBacteria; ADU42730; ADU42730; Rpdx1_1104. DR GeneID; 10063303; -. DR KEGG; rpx:Rpdx1_1104; -. DR PATRIC; 45342433; VBIRhoPal82507_1122. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; RPAL652103:GHQR-1117-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 219 AA; 22618 MW; E1E785BD2035F76D CRC64; MNAKPAPSRP APRLYLATPV TADPAALVAA LPKLLAAADI AAVLLRLEPS DPRTLTSRIK AVAPVVQAGG GALLVEGHAD LVARGGADGA HLSGLQAMQE WLPQLQPSRI AGVGGLETRH DSMIAGEAGA DYVLFGEPGA DGTRPSAEAI AERLDWWAEL FEPPCVGYAT SRDDVHQFAT AGADFVLVGD FIWSADDPTA ALADAGEALR QGFAAAPRQ // ID E6VLN1_RHOPX Unreviewed; 202 AA. AC E6VLN1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Rpdx1_1778; OS Rhodopseudomonas palustris (strain DX-1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=652103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DX-1; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Misra M., Chertkov O., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., RA Logan B., Oda Y., Harwood C., Woyke T.; RT "Complete sequence of Rhodopseudomonas palustris DX-1."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002418; ADU43392.1; -; Genomic_DNA. DR RefSeq; YP_004108125.1; NC_014834.1. DR ProteinModelPortal; E6VLN1; -. DR EnsemblBacteria; ADU43392; ADU43392; Rpdx1_1778. DR GeneID; 10063979; -. DR KEGG; rpx:Rpdx1_1778; -. DR PATRIC; 45343839; VBIRhoPal82507_1815. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; RPAL652103:GHQR-1793-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 202 AA; 21646 MW; 0D1A5860D581BF00 CRC64; MPYPDRFYPV VDSIAWVKRL AALGVGTVQL RAKDLDDGAA LQLVTDALAA VKDTSVKLII NDYWRAAIVA GAQHLHLGQE DLAEADLAEI RSAGLTLGLS THDDAELETA LAAEPDYIAL GPIFPTTLKS MRFAPQGIPK ITEWKKRVGA IPLVAIGGIK LEHAEEIFAA GADSIAVVSD VTQNPDPDAR VRAWLDFVAE KA // ID E6VUP3_DESAO Unreviewed; 221 AA. AC E6VUP3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Daes_1270; OS Desulfovibrio aespoeensis (strain ATCC 700646 / DSM 10631 / Aspo-2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=643562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., RA Pedersen K., Jagevall S., Hazen T., Woyke T.; RT "Complete sequence of Desulfovibrio aespoeensis Aspo-2."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002431; ADU62284.1; -; Genomic_DNA. DR RefSeq; YP_004121030.1; NC_014844.1. DR ProteinModelPortal; E6VUP3; -. DR EnsemblBacteria; ADU62284; ADU62284; Daes_1270. DR GeneID; 10095863; -. DR KEGG; das:Daes_1270; -. DR PATRIC; 45202533; VBIDesAes51796_1294. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; DAES643562:GH9Z-1292-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 24399 MW; 02D1322C5880FC20 CRC64; MGAREITRQS ILDTDIYCLT AEKFSRGRSN VEVVRAMLNH GIRLVQYREK DKKMGSKYEE CLEIRRMTRE AGAAFVVNDD IDLAVLVGAD GVHIGQEDLP VEAVRRLVGE GMAIGLSTHS PEEALAAVQR GADYIGVGPI FRTFTKEDVC DPVGYEYLEY VAREIDIPFV AIGGIKRHNV AEVVRRGARC VALITEIVEA DDIGTAISEL REAMQSAKEQ S // ID E6W3R9_DESIS Unreviewed; 217 AA. AC E6W3R9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Selin_2230; OS Desulfurispirillum indicum (strain ATCC BAA-1389 / S5). OC Bacteria; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae; OC Desulfurispirillum. OX NCBI_TaxID=653733; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1389 / S5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., RA Haggblom M., Rauschenbach I., Bini E., Woyke T.; RT "Complete sequence of Desulfurispirillum indicum S5."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002432; ADU66950.1; -; Genomic_DNA. DR RefSeq; YP_004113506.1; NC_014836.1. DR ProteinModelPortal; E6W3R9; -. DR EnsemblBacteria; ADU66950; ADU66950; Selin_2230. DR GeneID; 10073770; -. DR KEGG; din:Selin_2230; -. DR PATRIC; 45169444; VBIDesInd86994_2259. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; DIND653733:GHGZ-2278-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23034 MW; 4311EAEB9992192B CRC64; MERKGLMFTF CAITAADALG DHCQTAASAL EGGADMIQLR AKELSGDDLL VCAKKIMELK SRFRFTFIVN DSIEAALKSN ADGVHLGQDD DGLEFARDIL GPDAIVGIST HTLQQAKSAV AAGADYIGFG PMFATMTKSS EYEPREVGDL LKVAQGVEVP VCAIGGISVA SVAQLIVAPN VFVASISGFR REDMKAAVGE YVHAVEECRR LKGFDVS // ID E6W5J2_DESIS Unreviewed; 204 AA. AC E6W5J2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Selin_1288; OS Desulfurispirillum indicum (strain ATCC BAA-1389 / S5). OC Bacteria; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae; OC Desulfurispirillum. OX NCBI_TaxID=653733; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1389 / S5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., RA Haggblom M., Rauschenbach I., Bini E., Woyke T.; RT "Complete sequence of Desulfurispirillum indicum S5."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002432; ADU66023.1; -; Genomic_DNA. DR RefSeq; YP_004112579.1; NC_014836.1. DR ProteinModelPortal; E6W5J2; -. DR EnsemblBacteria; ADU66023; ADU66023; Selin_1288. DR GeneID; 10072809; -. DR KEGG; din:Selin_1288; -. DR PATRIC; 45167527; VBIDesInd86994_1317. DR KO; K00788; -. DR BioCyc; DIND653733:GHGZ-1317-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 204 AA; 22663 MW; 4EAF997202732202 CRC64; MSLAIYVITD SRSFETSDAF VDHYRAIACD HRVTGVLLRE PDMASDAYLR LVHRLADCGK LIVHSRNITT PQHAHELYEQ HLCTAIHCAE RDMDFLGAMK LPCSVSCHHP EQAQALLRAY EHLRFVTLSP IFPTPKPYSV TPLGISALMD VDVSLRSRVV ALGGINQQTL SLLQRVEGLG GWAAIGCFLR DSHNILATPF CDNP // ID E6WHM7_PANSA Unreviewed; 211 AA. AC E6WHM7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Pat9b_0214; OS Pantoea sp. (strain At-9b). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=592316; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=At-9b; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., RA Currie C., Woyke T.; RT "Complete sequence chromosome of Pantoea sp. At-9b."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002433; ADU67540.1; -; Genomic_DNA. DR RefSeq; YP_004114096.1; NC_014837.1. DR ProteinModelPortal; E6WHM7; -. DR EnsemblBacteria; ADU67540; ADU67540; Pat9b_0214. DR GeneID; 10067607; -. DR KEGG; pao:Pat9b_0214; -. DR PATRIC; 45314687; VBIPanSp129740_0211. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; PSP592316:GI0L-228-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23032 MW; 8DF02650105D8451 CRC64; MTAPFPSTAP RLGLYPVVDS VEWIARLLEA GVRTIQLRIK DCEDHEVEEA VRDAIALGKK YRARLFINDY WRLAIRYNAY GVHLGQEDLD VADLEAIRQA GLRLGLSTHD DAELDRALAL HPSYIALGHI FPTQTKEMPS EPQGITELKR HLTRLQGIST VAIGGISLAR APEVLATGVG SIAVVSAITQ APDWLAATRE LLALAEPPVT A // ID E6WQQ7_PSEUU Unreviewed; 319 AA. AC E6WQQ7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 21. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=Psesu_0650; OS Pseudoxanthomonas suwonensis (strain 11-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Pseudoxanthomonas. OX NCBI_TaxID=743721; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=11-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Siebers A.K., RA Allgaier M., Thelen M.P., Hugenholtz P., Gladden J., Woyke T.; RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002446; ADV26506.1; -; Genomic_DNA. DR RefSeq; YP_004145737.1; NC_014924.1. DR ProteinModelPortal; E6WQQ7; -. DR EnsemblBacteria; ADV26506; ADV26506; Psesu_0650. DR GeneID; 10122194; -. DR KEGG; psu:Psesu_0650; -. DR PATRIC; 45335081; VBIPseSuw172708_0675. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; PSUW743721:GH68-654-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 319 AA; 34018 MW; D738CCD1EF7D3E90 CRC64; MEAPLRSIHV VAGVITDVRG RILLTQRGKD SDLAGLWEFP GGKREPGESS QAALARELEE ELGIEVEVGD RLVEVPQHYP SKRLRLEVFR IARWKGSPRG REGQAMTWVE PDRLLRYSMP SADLPVVGVL RQPGLYLVTP APGTDLQAWL GALDAALESG VSRVQLRAPG MEGARWRELA GLVLPRCRDA GAELLLNRDI ALARELGTGV HLGSEQLGAL AERPLSPGLP VGASCHTLDE LKAAEALGCD FAVLGPVQAT ATHPGAAPLG WEGFAELRQH VGLPIYAIGG LGPEDVDAAR LQGAQGIAAI RGLWSRVAA // ID E6WVY7_PSEUU Unreviewed; 213 AA. AC E6WVY7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Psesu_2649; OS Pseudoxanthomonas suwonensis (strain 11-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Pseudoxanthomonas. OX NCBI_TaxID=743721; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=11-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Siebers A.K., RA Allgaier M., Thelen M.P., Hugenholtz P., Gladden J., Woyke T.; RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002446; ADV28478.1; -; Genomic_DNA. DR RefSeq; YP_004147709.1; NC_014924.1. DR EnsemblBacteria; ADV28478; ADV28478; Psesu_2649. DR GeneID; 10124242; -. DR KEGG; psu:Psesu_2649; -. DR PATRIC; 45339200; VBIPseSuw172708_2675. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; PSUW743721:GH68-2703-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 21713 MW; 6A4702645DCE8F6E CRC64; MNPASPHAAR GLYLITPDEP DTTRLLARVE PLLGAGVAWL QYRNKTAGPA LKHEQAAALQ VLCTRAGVPL LVNDDAALAS EIGAAGAHLG EEDGALATAR ALLGPRAILG ASCYDSLDLA RAAVAAGASY VAFGAFFPTT TKVVTRRATP GLLREAAALG VPRVAIGGIT PDNGRALVES GADLLAVVGG VFEAPDPLAA VAAYRRCFEP AAR // ID E6X002_NITSE Unreviewed; 195 AA. AC E6X002; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Nitsa_1477; OS Nitratifractor salsuginis (strain DSM 16511 / JCM 12458 / E9I37-1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Nitratifractor. OX NCBI_TaxID=749222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16511 / JCM 12458 / E9I37-1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A., RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Nitratifractor salsuginis DSM 16511."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002452; ADV46725.1; -; Genomic_DNA. DR RefSeq; YP_004168474.1; NC_014935.1. DR EnsemblBacteria; ADV46725; ADV46725; Nitsa_1477. DR GeneID; 10148268; -. DR KEGG; nsa:Nitsa_1477; -. DR PATRIC; 46984515; VBINitSal150288_1474. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; NSAL749222:GHWN-1508-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 195 AA; 21474 MW; C1DD30352DC1F956 CRC64; MPQETEIYAL IDSRLLRRYD LSLARVGRFL EEAKIPIAQY RDKEASDADV ARALEELRIY YSGTLIVNDR LGLAGLADGL HLGQEDLAAI DPDSEAAVSK VRRQIGSKLL GLSTHNREEI ETANALDLDY IGLGAYRSTA TKADAGVSGK ALLELARLSR HPVALIGGVR WEDRFEAPIR YKVLGSALME RIANL // ID E6X1W5_NITSE Unreviewed; 180 AA. AC E6X1W5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Nitsa_0706; OS Nitratifractor salsuginis (strain DSM 16511 / JCM 12458 / E9I37-1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Nitratifractor. OX NCBI_TaxID=749222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16511 / JCM 12458 / E9I37-1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A., RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Nitratifractor salsuginis DSM 16511."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002452; ADV45973.1; -; Genomic_DNA. DR RefSeq; YP_004167722.1; NC_014935.1. DR EnsemblBacteria; ADV45973; ADV45973; Nitsa_0706. DR GeneID; 10147485; -. DR KEGG; nsa:Nitsa_0706; -. DR PATRIC; 46982944; VBINitSal150288_0704. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; NSAL749222:GHWN-727-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 180 AA; 19528 MW; E864DE70FD2E75B1 CRC64; MILYAITDPS ILSFETLSSD LHRIKARGAS MILYRDKKTA EYEKRAERFV EAAKEAGFGK IILHNTPQLA LRLGAWGVHC SSDAYGLISE GKRLGLKTVA STHSLEEIKK AEEAGADMVT LSPLFVSPGK GKPLGEKGFT RIVQEAKVPM IALGGITDKE KIRRAMSCGA SGIASIRYFA // ID E6XB97_CELAD Unreviewed; 198 AA. AC E6XB97; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Celal_2676; OS Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Cellulophaga. OX NCBI_TaxID=688270; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14237 / IC166 / ACAM 630; RX DOI=10.4056/sigs.1543845; RA Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J., Tapia R., Goodwin L., Pitluck S., Liolios K., RA Pagani I., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., RA Detter J., Brambilla E., Rohde M., Tindall B., Goker M., Woyke T., RA Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., RA Klenk H., Lapidus A.; RT "Complete genome sequence of Cellulophaga algicola type strain RT (IC166)."; RL Stand. Genomic Sci. 4:72-80(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002453; ADV49961.1; -; Genomic_DNA. DR RefSeq; YP_004165459.1; NC_014934.1. DR EnsemblBacteria; ADV49961; ADV49961; Celal_2676. DR GeneID; 10145097; -. DR KEGG; cao:Celal_2676; -. DR PATRIC; 46910942; VBICelAlg158510_2715. DR HOGENOM; HOG000274937; -. DR KO; K00788; -. DR BioCyc; CALG688270:GHJ1-2726-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 198 AA; 22797 MW; 55171BECFB47252D CRC64; MIVLIAPEED IANEIEILNQ LFEEGLTCYH FRKPNKSYQE HSDYLNQIAS KYHNRIVVHF HHELVNEFSL KGIHFQEQKR IDHIDNPGQY FKPLDMYGKT ISSSFHDPEV LNACEFEFDY HLLSPVFSSI SKKGYEGKGF DVNHIEKRII GMGGVTKDNI AEMHRLGFKG VGVLGGIWNS VSPVAEFKAM QAYYSKNK // ID E6XB98_CELAD Unreviewed; 217 AA. AC E6XB98; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Celal_2677; OS Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Cellulophaga. OX NCBI_TaxID=688270; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14237 / IC166 / ACAM 630; RX DOI=10.4056/sigs.1543845; RA Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J., Tapia R., Goodwin L., Pitluck S., Liolios K., RA Pagani I., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., RA Detter J., Brambilla E., Rohde M., Tindall B., Goker M., Woyke T., RA Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., RA Klenk H., Lapidus A.; RT "Complete genome sequence of Cellulophaga algicola type strain RT (IC166)."; RL Stand. Genomic Sci. 4:72-80(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002453; ADV49962.1; -; Genomic_DNA. DR RefSeq; YP_004165460.1; NC_014934.1. DR EnsemblBacteria; ADV49962; ADV49962; Celal_2677. DR GeneID; 10145098; -. DR KEGG; cao:Celal_2677; -. DR PATRIC; 46910944; VBICelAlg158510_2716. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; CALG688270:GHJ1-2727-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23930 MW; CED1B9CC4282BAF1 CRC64; MQLPNLHYIS QGETPQEHLK NIKSACTAGA TLVQLRLKNL SPKKVLKFAS EAKEITDHYQ TRLIINDHYR IAKEVKADGV HLGRTDTCPS IARKYLESWQ IIGGTANTIS DCNALIAKNV DYIGVGPYHF TKTKESLSPI LGLEGYAAIL EKLKTTIPII AVGGITVTDV PEILKTGVYG VAVATAITKD FNTITLFKKI LEKSDIEEQV WKPKQTV // ID E6XM05_SHEP2 Unreviewed; 646 AA. AC E6XM05; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Sput200_2067; OS Shewanella putrefaciens (strain 200). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=399804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=200; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., Kolker E., Lawrence C., McCue L.A., DiChristina T., RA Nealson K., Fredrickson J.K., Woyke T.; RT "Complete sequence of Shewanella putrefaciens 200."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002457; ADV54523.1; -; Genomic_DNA. DR RefSeq; YP_006009989.1; NC_017566.1. DR EnsemblBacteria; ADV54523; ADV54523; Sput200_2067. DR GeneID; 12605312; -. DR KEGG; shp:Sput200_2067; -. DR KO; K14153; -. DR BioCyc; SPUT399804:GLK4-2122-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 646 AA; 68391 MW; 03475D4F194F7B3A CRC64; MLGIHGGKLP MNTERPAIVW TIAGSDSGGG AGIQADLATI QDFGCHACSV ITTVTAQSSV AVTLVEPVSA AMLMAQLTTL LSDLPPKAIK IGLLADQTQV ALLADWIASF KIHYPSVPVI VDPVMVASCG DALAVDNCQD IKSTAKSALD FNPFKGLIEL ITPNVPELGR LTHSDVSTKA QFAAAAQALS QSLDCSVLAK GGDVSFGSTD ILDDTHAKTH DNTHAQTQAN VHVSTLDSNG WDHGLAEDYL VCHQVRASSE LHQNGCIWLA SQRVNTRHNH GSGCTLSSAI AAVLAQGFVL QDTVVVAKAY VSQGLSAAIG LGQGPGPLAR TGWPNDLSRY AKIRLCDGNF ISHQLNQHLD VRSDLVATVL SATDQATAQV RIVSTPPQNI LSHGFKILDA DLGVYPVVSD IAMLESLLAA GVKTVQLRIK TDISELSSAA PAESDLGKCE SGKSELVGSE LEVQIQTAIA LGKHFNAQLF INDHWQLAIK YHAFGIHLGQ EDLAVTDLAA IQSAGLALGI SSHSYFELLL AHQYSPSYIA LGHIFPTTTK QMPSAPQGLA KLKHYVALLQ DHYPLVAIGG IDLDNLAKVK ATGVGNIAVV RAITEAQDPL AAFAELSQAW EQCSLSEELA AKHEFDVKHK LDAKYE // ID E6YGU5_BARC7 Unreviewed; 201 AA. AC E6YGU5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BARCL_0402; OS Bartonella clarridgeiae (strain CIP 104772 / 73). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=696125; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 104772 / 73; RA Engel P., Salzburger W., Marius L., Chao-Chin C., Soichi M., RA Christa L., Alexandra C., Aurelie L., Claudine M., Stephan S.C., RA Christoph D.; RT "Genome sequencing of Bartonella species and comparative genomics."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN645454; CBI76083.1; -; Genomic_DNA. DR EnsemblBacteria; CBI76083; CBI76083; BARCL_0402. DR PATRIC; 45178292; VBIBarCla149360_0376. DR HOGENOM; HOG000155781; -. DR OMA; QWIEVTR; -. DR BioCyc; BCLA696125:GC2L-416-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 23079 MW; 737239E49A1153B4 CRC64; MKLDPFYLIV DSADWVERLI PFGVKLIQLR IKDKDTETII QHIKRAKNIC DKFKAQLIIN DYWKIAIDEK CDFIHLGQED LKNTDISAIR KSGIKFGLST HDEHELDISL SISPEYIALG PIYPTILKKM KWAPQGLEKI KQWRKRIDSL PLVGIGGLTP ERAIDVLKVG ANSAAVVTDI ILNKKPEKRV QQWIKVTQAW R // ID E6YJ60_BARC7 Unreviewed; 224 AA. AC E6YJ60; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 22-JAN-2014, entry version 19. DE SubName: Full=Thiamine-phosphate pyrosphorylase; GN Name=thiE; OrderedLocusNames=BARCL_1226; OS Bartonella clarridgeiae (strain CIP 104772 / 73). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=696125; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 104772 / 73; RA Engel P., Salzburger W., Marius L., Chao-Chin C., Soichi M., RA Christa L., Alexandra C., Aurelie L., Claudine M., Stephan S.C., RA Christoph D.; RT "Genome sequencing of Bartonella species and comparative genomics."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN645454; CBI76898.1; -; Genomic_DNA. DR EnsemblBacteria; CBI76898; CBI76898; BARCL_1226. DR PATRIC; 45179971; VBIBarCla149360_1173. DR HOGENOM; HOG000155781; -. DR OMA; FACVILY; -. DR BioCyc; BCLA696125:GC2L-1278-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 224 AA; 25561 MW; 06120CB00E3D615A CRC64; MTKQKNKPIV QCLFPQLILT VDVRRTFNPV LFRQILQTQS FACVILYDLQ GEKMGEEHLQ KSAQRYVHDI QHNGAALIIA EQSRVVGRVK ADGLHVEGDL NIQKSVENLK KEQKIIGCGN LQNRHSAMVV AEAGIDYLLF GKLGADKNPR PHPRNIQLAQ WWAEIMQTPA IIQTGSEYAF FDEALETNCE FIAVEEMIFM HDDPFGVLDM MKEKCQNVPL RTER // ID E6YKU9_9RHIZ Unreviewed; 201 AA. AC E6YKU9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 22-JAN-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BARRO_30068; OS Bartonella rochalimae ATCC BAA-1498. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=685782; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1498; RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296; RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C., RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.; RT "Parallel evolution of a type IV secretion system in radiating RT lineages of the host-restricted bacterial pathogen Bartonella."; RL PLoS Genet. 7:E1001296-E1001296(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN645457; CBI77487.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22975 MW; C268C3EE257DB472 CRC64; MKLDPFYPIV DSADWVERLV PFGIKLIQLR IKDKDTETII QHIKRAKNIC DKFKVQLVIN DYWKIAIDEK CDFIHLGQED LKSADILAIR KSGIKFGLST HDEHELDISL SISPEYIALG PIYPTILKKM KWAPQGLEKI KQWRKKIGSL PLIGIGGLTP ERAISILKIG ANSAAVVTDI ILNKKPEERV QQWIKVTQAW R // ID E6YNC8_9RHIZ Unreviewed; 227 AA. AC E6YNC8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 22-JAN-2014, entry version 13. DE SubName: Full=Thiamine-phosphate pyrosphorylase; GN Name=thiE; ORFNames=BARRO_130010; OS Bartonella rochalimae ATCC BAA-1498. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=685782; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1498; RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296; RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C., RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.; RT "Parallel evolution of a type IV secretion system in radiating RT lineages of the host-restricted bacterial pathogen Bartonella."; RL PLoS Genet. 7:E1001296-E1001296(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN645467; CBI78366.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 227 AA; 25884 MW; 77637FE68CAF085E CRC64; MTKQKSEPIV QCLSPQLILT VDVRRTLNPV LFRQILQTQS FVCVILYDSQ GEKMGEEHLQ KSGHLYAHDI QQNGAALIIA EQSRVVGRIK ADGLHLESHF NLSQVIENLK KEKKIIGCGN FQNRHSAMVI AETGVDYLFF GKLGADKKPR AHPRNIQLAQ WWAEIMNTPA IIQAGSEYAF FDETLETACE FIAVEEMIFM QDDPLRVLDM IKEKCQNVLL RTEREKS // ID E6YQ18_9RHIZ Unreviewed; 201 AA. AC E6YQ18; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 22-JAN-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BAR15_110152; OS Bartonella sp. AR 15-3. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=545617; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AR 15-3; RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296; RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C., RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.; RT "Parallel evolution of a type IV secretion system in radiating RT lineages of the host-restricted bacterial pathogen Bartonella."; RL PLoS Genet. 7:E1001296-E1001296(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN645478; CBI78956.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22992 MW; 76EB92CBB4A26F8F CRC64; MKLDPFYLIV DSADWVERLV PFGIKLIQLR IKDEDTETII QHIKRAKNIC NKFKAQLVIN DYWKIAIDEK CDFIHLGQDD LKNADILAIR KSDIKLGLST HDEHELDISL SISPEYIALG PIYPTIFKKM KWAPQGLEKI KQWRKKIGSL PLVGIGGLTP ERAINILTVG ANSAAVVTDV ILNKKPEERV QQWIKVTQAW R // ID E6YSQ1_9RHIZ Unreviewed; 224 AA. AC E6YSQ1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 22-JAN-2014, entry version 13. DE SubName: Full=Thiamine-phosphate pyrosphorylase; GN Name=thiE; ORFNames=BAR15_180122; OS Bartonella sp. AR 15-3. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=545617; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AR 15-3; RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296; RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C., RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.; RT "Parallel evolution of a type IV secretion system in radiating RT lineages of the host-restricted bacterial pathogen Bartonella."; RL PLoS Genet. 7:E1001296-E1001296(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN645485; CBI79889.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 224 AA; 25495 MW; 2FC51EBE7DAC6422 CRC64; MTKQKSEPIV QCFCPQLILT IDVRRTLNPV LLRQILQTQS FACVILYDSQ GKKMGEEYLQ KSAQLYVHDI QHNGAALIIA EESRVVGRIR ADGLHVEDHF NISKIVENLK KEQKIIGCGN FQNRHSAMVI AEAGVDYLFF GKLGADKKPR SHPRNIQLAQ WWAEIMKTPA IIQAGSEYAF FDEALATACE FIAVEEMIFM HDDPLRVLDM MKEKCQNASL NTER // ID E6YUK9_9RHIZ Unreviewed; 201 AA. AC E6YUK9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 22-JAN-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=B11C_110158; OS Bartonella sp. 1-1C. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=515256; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1-1C; RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296; RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C., RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.; RT "Parallel evolution of a type IV secretion system in radiating RT lineages of the host-restricted bacterial pathogen Bartonella."; RL PLoS Genet. 7:E1001296-E1001296(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN645496; CBI80547.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22979 MW; 65D0F87E257B1818 CRC64; MKLDPFYPIV DSADWVERLV PFGIKLIQLR IKDKDTETII QHIKRAKNIC DKFKVQLVIN DYWKIAIDEK CDFIHLGQED LKSADILAIR KSGIKFGLST HDEHELDISL SISPEYIALG PIYPTILKKM KWAPQGLEKI KQWRKKIGSL PLIGIGGLTP ERAMSILKVG ANSAAVVTDI ILNKKPEERV QQWIKVTQAW R // ID E6YWY9_9RHIZ Unreviewed; 224 AA. AC E6YWY9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 22-JAN-2014, entry version 13. DE SubName: Full=Thiamine-phosphate pyrosphorylase; GN Name=thiE; ORFNames=B11C_190083; OS Bartonella sp. 1-1C. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=515256; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1-1C; RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296; RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C., RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.; RT "Parallel evolution of a type IV secretion system in radiating RT lineages of the host-restricted bacterial pathogen Bartonella."; RL PLoS Genet. 7:E1001296-E1001296(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN645504; CBI81377.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 224 AA; 25318 MW; 4851543E70B4FB5B CRC64; MTKQKSESIV QCLSPQLILT VDVCRTLNPV LFRQILQTQS FACVILYDSQ GEKMGEEHLQ KSGHLYAHDI QQNGAALIIA EQSRVVGRIK ADGLHLESHF NLSTVVESLK KEKKIIGCGN LQTRHSAMVV AEAGVDYLLF GKLGADKKPR SHPRNIQLAQ WWAEIMNTPA IIQAGSEYAF FDEALETACE FIAVEEMIFM HDDPFRVLDM IKEKCQNVFL RTER // ID E6YYA0_BARSR Unreviewed; 201 AA. AC E6YYA0; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 22-JAN-2014, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=B11C_20188; OS Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=687861; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R1; RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296; RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C., RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.; RT "Parallel evolution of a type IV secretion system in radiating RT lineages of the host-restricted bacterial pathogen Bartonella."; RL PLoS Genet. 7:E1001296-E1001296(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN645507; CBI81911.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23030 MW; E353E9B58289D5D7 CRC64; MKLDPFYLIV DNADWVERLV PLGVKLIQLR MKNKNIEIIN HHIKRAKNIC DKFGAQLVIN DYWEIAIDEK CDFIHLGQED LCNADIPAIR KNGIKFGLST HDEHELDISM SFSPEYIALG PIYPTILKKM KWAPQGLEKI KQWKKRIGAL PLVGIGGLTP ERAIDVLEAG ANSAAVVTDI ILHKKPEERT QQWMKVTQKW R // ID E6Z1I1_BARSR Unreviewed; 221 AA. AC E6Z1I1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 22-JAN-2014, entry version 13. DE SubName: Full=Thiamine-phosphate pyrosphorylase; GN Name=thiE; ORFNames=BARSC_190242; OS Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=687861; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R1; RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296; RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C., RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.; RT "Parallel evolution of a type IV secretion system in radiating RT lineages of the host-restricted bacterial pathogen Bartonella."; RL PLoS Genet. 7:E1001296-E1001296(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN645524; CBI82969.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 24695 MW; 0D962335A6AEB1DC CRC64; MVHQKNKPIE HCSFPQLVLT LDVRRVIEPA FLRQIFQTKS FACIILYDSF VDQGDGAFLQ NSAKMYADDI QHNGAALIIA EDSRVAGRIK ADGMHLEGGL DAFDVLENQK KNQKIVGFGN LRTRHCAMSV AEAGVDYVFF GKLGADKKPS SHPRNIALAK WWAEIMEVPA IIQAGSDLAT IDETLETTCE FIAIEEMIFA HDHPFIVLDR VKEKCKNHPL S // ID E7A0I0_SPORE Unreviewed; 563 AA. AC E7A0I0; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE SubName: Full=Related to thiamine-phosphate diphosphorylase / hydroxyethylthiazole kinase; GN ORFNames=sr13653; OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina; OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium. OX NCBI_TaxID=999809; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SRZ2; RX PubMed=21148393; DOI=10.1126/science.1195330; RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K., RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., RA Pester D., Mueller O., Winterberg B., Meyer E., Ghareeb H., RA Wollenberg T., Muensterkoetter M., Wong P., Walter M., Stukenbrock E., RA Gueldener U., Kahmann R.; RT "Pathogenicity determinants in smut fungi revealed by genome RT comparison."; RL Science 330:1546-1548(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ311471; CBQ72987.1; -; Genomic_DNA. DR EnsemblFungi; CBQ72987; CBQ72987; sr13653. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 563 AA; 58190 MW; 89271931A8602904 CRC64; MPPSTLDNSA VDYSVYLVTG RELLPPGVDY YASLELCLSQ HNVSVVQIRE KDAETNEFLD IARRSLEICD RYGVPMLIND NLSVCLSLPE RVGLHIGQED IPVAEARRIL GDKRLLGISV KTVEQARVAR EEGKADYAGV GPCYGTLSKA GITEDKVIGC SGAQRIVAEL NRDGARVPCV LIGGLNQKTA ARTLFGATSA TNAPDGIAVI SAIVSRTDSD KAAQELADIV RTYKAGLAAS ATPTSTHGIA SAFALPSPSP HDASHYKTAA ANLLAFHRQA AHGPPLIQAI TSHVSSTMSA NLALAFSASP IMSHEAAEAA DLSLALGALV LNIGTISPAA RDGMHAAGTA ANRNRKPVVL DPVGGGATQF RRDVVRALLD RTQVTLLKGN AAELASIAGR ADEVSSRGVD SGSGQLSDPV GMVRALAQKE RCLVLLSGKT DYLTDGTTVL TSENGHPLLG AITGSGCALG VTVAAGLAAA CNLVRSQGSA AESLGNTLVA HGHVDLLVGA LTGLLAMTIA SEKAARRDDV KGPGTFIPAL QDELAAVSAE DILQFAKINV VSS // ID E7A7B1_HAEIF Unreviewed; 226 AA. AC E7A7B1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HIBPF_19180; OS Haemophilus influenzae F3031. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=866630; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F3031; RA Aslett M.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F3031; RX PubMed=22377449; DOI=10.3201/eid1803.110728; RA Strouts F.R., Power P., Croucher N.J., Corton N., van Tonder A., RA Quail M.A., Langford P.R., Hudson M.J., Parkhill J., Kroll J.S., RA Bentley S.D.; RT "Lineage-specific Virulence Determinants of Haemophilus influenzae RT Biogroup aegyptius."; RL Emerg. Infect. Dis. 18:449-457(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ670178; CBY81952.1; -; Genomic_DNA. DR RefSeq; YP_004136259.1; NC_014920.1. DR GeneID; 10134421; -. DR KEGG; hif:HIBPF19180; -. DR PATRIC; 45233177; VBIHaeInf165906_1867. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; HINF866630:GJN7-1755-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24663 MW; 5E34364402B94040 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SGEYAK // ID E7AB68_HELFC Unreviewed; 204 AA. AC E7AB68; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Precursor; GN Name=thiE; OrderedLocusNames=HFELIS_15420; OS Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=936155; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49179 / NCTC 12436 / CS1; RA Arnold A., Zigova Z., Lawley T., Falkow S., Bentley S., Aslett M., RA Muller A.; RT "Comparative whole genome analysis of the carcinogenic bacterial RT pathogen Helicobacter felis."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ670179; CBY83626.1; -; Genomic_DNA. DR RefSeq; YP_004074216.1; NC_014810.2. DR EnsemblBacteria; CBY83626; CBY83626; HFELIS_15420. DR GeneID; 10050720; -. DR KEGG; hfe:HFELIS_15420; -. DR PATRIC; 45241031; VBIHelFel178703_1590. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; HFEL936155:GHMC-1547-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21918 MW; D124A40591B8D695 CRC64; MGIELKGLYA ISDPQLTPYD RLLNLAERAI EGGVSFLQLR DKQSSDSELL GLAKELNDLC TKKGVGFVIN DRLSLALECN AWGLHLGEAD IPLSEARALF GGVIGVSCYG DLEKAKQAQA QGADYVAFGA CFRSPSKPSA PCIDLEVLER AKACLTIPVC AIGGISVQNV AQLKHADMIA LISALWQGDV RTNAQKLLEN WHAH // ID E7ADD8_HELFC Unreviewed; 185 AA. AC E7ADD8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 11-DEC-2013, entry version 21. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=HFELIS_11110; OS Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=936155; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49179 / NCTC 12436 / CS1; RA Arnold A., Zigova Z., Lawley T., Falkow S., Bentley S., Aslett M., RA Muller A.; RT "Comparative whole genome analysis of the carcinogenic bacterial RT pathogen Helicobacter felis."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ670179; CBY83195.1; -; Genomic_DNA. DR RefSeq; YP_004073785.1; NC_014810.2. DR EnsemblBacteria; CBY83195; CBY83195; HFELIS_11110. DR GeneID; 10051156; -. DR KEGG; hfe:HFELIS_11110; -. DR PATRIC; 45240143; VBIHelFel178703_1155. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IASTHNT; -. DR BioCyc; HFEL936155:GHMC-1115-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 185 AA; 20404 MW; 5D390F06400750BB CRC64; MIESYCITPP FLSTRNLEDF KTTLFKSFST HRPSRACLRA PCAPPDLLAC FVELCKTFAI TSYLNLPLLS SSIDQALQYG FFGVHAKGHA LAELPSIPPT LSSFYSAHSA QEVQQALDLG AHFCTLSPIF PTPHKSPPLG LDYLDQLTPL QKNRLFALGG IVRIEQVKLI ASKGLRGFAS VRYFL // ID E7AF92_HAEIF Unreviewed; 226 AA. AC E7AF92; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HICON_09970; OS Haemophilus influenzae F3047. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=935897; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F3047; RA Aslett M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F3047; RX PubMed=22377449; DOI=10.3201/eid1803.110728; RA Strouts F.R., Power P., Croucher N.J., Corton N., van Tonder A., RA Quail M.A., Langford P.R., Hudson M.J., Parkhill J., Kroll J.S., RA Bentley S.D.; RT "Lineage-specific Virulence Determinants of Haemophilus influenzae RT Biogroup aegyptius."; RL Emerg. Infect. Dis. 18:449-457(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ670204; CBY86462.1; -; Genomic_DNA. DR RefSeq; YP_004138143.1; NC_014922.1. DR EnsemblBacteria; CBY86462; CBY86462; HICON_09970. DR GeneID; 10111375; -. DR KEGG; hil:HICON_09970; -. DR PATRIC; 45235155; VBIHaeInf177079_0788. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; HINF935897:GJ9O-751-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24739 MW; 4922E65017694043 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMSVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNV GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID E7B6U6_YERE1 Unreviewed; 223 AA. AC E7B6U6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Y11_35011; OS Yersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM OS 13030 / CIP 106945 / Y11). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=930944; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y11; RA Batzilla J., Hoeper D., Heesemann J., Rakin A.; RT "Complete genome sequence of Y. enterocolitica subsp. palearctica RT serogroup O:3."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13030 / CIP 106945 / Y11; RX PubMed=21296963; DOI=10.1128/JB.01484-10; RA Batzilla J., Hoper D., Antonenka U., Heesemann J., Rakin A.; RT "Complete genome sequence of Yersinia enterocolitica subsp. RT palearctica serogroup O:3."; RL J. Bacteriol. 193:2067-2067(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR729477; CBY29029.1; -; Genomic_DNA. DR RefSeq; YP_006007000.1; NC_017564.1. DR EnsemblBacteria; CBY29029; CBY29029; Y11_35011. DR GeneID; 12602208; -. DR KEGG; yey:Y11_35011; -. DR KO; K00788; -. DR BioCyc; YENT930944:GLMU-3571-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24371 MW; 73F1F69E77A483AC CRC64; MKPSDTPIFS AQKGFPTTEQ RLGLYPVVDS VLWIERLLAL GVTTIQLRIK ELDEAQVEQD IVAAIELGKR YQARLFINDY WRLAIKHGAY GVHLGQEDLE STDLAAIQQA GLRLGVSTHD EYELAIAKAV RPSYIAMGHI FPTQTKQMPS SPQGLAVLKQ MVENTPDYPT VAIGGISIER VPAVLATGVG SVAVVSAITQ AEDWQQATAQ LLHLIEGKEL ADE // ID E7BIT6_NEIMW Unreviewed; 205 AA. AC E7BIT6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NMAA_0087; OS Neisseria meningitidis serogroup A (strain WUE 2594). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=942513; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WUE 2594; RX PubMed=21296965; DOI=10.1128/JB.00084-11; RA Schoen C., Weber-Lehmann J., Blom J., Joseph B., Goesmann A., RA Strittmatter A., Frosch M.; RT "Whole-genome sequence of the transformable Neisseria meningitidis RT serogroup A strain WUE2594."; RL J. Bacteriol. 193:2064-2065(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WUE 2594; RA Schoen C., Weber-Lehmann J., Blom J., Joseph B., Goesmann A., RA Strittmatter A., Frosch M.; RT ""Whole-genome sequence of the transformable Neisseria meningitidis RT serogroup A strain WUE2594"."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR774048; CBY89920.1; -; Genomic_DNA. DR RefSeq; YP_005891080.1; NC_017512.1. DR ProteinModelPortal; E7BIT6; -. DR EnsemblBacteria; CBY89920; CBY89920; NMAA_0087. DR GeneID; 12407600; -. DR KEGG; nmw:NMAA_0087; -. DR KO; K00788; -. DR BioCyc; NMEN942513:GLHV-103-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21702 MW; 8FF53D111925A2EC CRC64; MTFLPLKSPL KFYAVVPTAD WVERMVEAGA DTVQLRCKAL HGDELKREIA RCVAACQGSH TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYIASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTKAA NPEAVVKAFQ ALWDG // ID E7C1J5_9GAMM Unreviewed; 184 AA. AC E7C1J5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Putative uncharacterized protein; OS uncultured gamma proteobacterium HF0010_09F21. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=723560; RN [1] RP NUCLEOTIDE SEQUENCE. RA Pham V.D., Delong E.F.; RT "Genome fragments of uncultured bacteria from the North Pacific RT subtropical Gyre."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GU567950; ADI21284.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 184 AA; 21170 MW; 6DAEA1492BF26E06 CRC64; MAENIRDLIK DQETFFLITG EFKKISTLKK KLLNTKRFNK KILILRIKED TDQLDEIILE VKKFCKKENV PLLLNSPNKF SYKAKGYHLT SKEIYEYKNS RNLVLGASCH NEQDIIQAID IGCSYAFLSP VIRKNGIDGM GWDSFFVLKD KYPQITIVPL GGINESNAIV EAFAGISHWW NHQA // ID E7C1L8_9GAMM Unreviewed; 214 AA. AC E7C1L8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase; OS uncultured gamma proteobacterium HF0010_10D20. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=723561; RN [1] RP NUCLEOTIDE SEQUENCE. RA Pham V.D., Delong E.F.; RT "Genome fragments of uncultured bacteria from the North Pacific RT subtropical Gyre."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GU567951; ADI21342.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 214 AA; 24259 MW; F10C9EA0C4A85A07 CRC64; MKGIYAITPD DIEENELIEK SQELIEAKIN FLQIRRKADT LDQIYSVASK IVKFTKNHSC KLIINDHIEI AKDLNADGVH LGMEDYENFL KKPDDLKKVF SSYFREKVIG LSCKNNLGLV KNPPVDLFDW DYLAVGSMFR TTTKTDTVLV NANQRSLLIK NSSKPLVAIG GIDEKNIGVL LKDNYNFFAI SKFLFNNDSP SRALKKIKKI IKGS // ID E7C1P2_9GAMM Unreviewed; 208 AA. AC E7C1P2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase; OS uncultured gamma proteobacterium HF0010_20H22. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=723562; RN [1] RP NUCLEOTIDE SEQUENCE. RA Pham V.D., Delong E.F.; RT "Genome fragments of uncultured bacteria from the North Pacific RT subtropical Gyre."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GU567952; ADI21366.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 208 AA; 23824 MW; 8BFA8BB553BCA960 CRC64; MIQGLYAITP SGWEENDLLS ETEVLLKEGV KLIQYRDKVF DKKTFQEKAK ALLRLTKKYK AKLLINDHVK ICLEIGADGF HLGLEDYSSE ENLELLKKNK DFISKNLISG LSCKWNKELV VNPPENEIKW TYLAVGSFYP SNTKSTIPET NENIKREFLG YTDKPLVAIG GINKKNIREV KSMGYSCFAL SEALFNKPEY VLSEYKKL // ID E7C1U0_9GAMM Unreviewed; 210 AA. AC E7C1U0; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase; OS uncultured gamma proteobacterium HF0010_21A16. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=723563; RN [1] RP NUCLEOTIDE SEQUENCE. RA Pham V.D., Delong E.F.; RT "Genome fragments of uncultured bacteria from the North Pacific RT subtropical Gyre."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GU567953; ADI21414.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 210 AA; 23860 MW; 5E312AD4BDC5AC37 CRC64; MKSIYAITPS GIDFKKLIFE IEKMLSLGIN LFQYREKSLS ERQLKNNASI LLEVIKKNNG KLLINDSPRI AVEIGADGFH LGMEDYLSPQ NLKFIKEHKE TINSDYIKGL TCKWDYELVK NPPEDLITWN YLAVGAFFKS ETKKDVSLLK NKDKSYPLTI SSKPLVAIGG INYQNMDSVL SLGYETIALS KGIFFAKNLE NIIKNLNEEN // ID E7C261_9GAMM Unreviewed; 66 AA. AC E7C261; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Putative uncharacterized protein; OS uncultured gamma proteobacterium HF0070_25G02. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=723566; RN [1] RP NUCLEOTIDE SEQUENCE. RA Pham V.D., Delong E.F.; RT "Genome fragments of uncultured bacteria from the North Pacific RT subtropical Gyre."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GU567958; ADI21535.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 66 AA; 7496 MW; F058F4DDE5ABD05D CRC64; MIQGLYAITP SGLEENDLLT KTEVLLKEGI KLIQYRDKIL DKKTLQEKAH ALLNLTKKYG AKLVIQ // ID E7C2C2_9GAMM Unreviewed; 91 AA. AC E7C2C2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Putative uncharacterized protein; OS uncultured Oceanospirillales bacterium HF0130_06B06. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC environmental samples. OX NCBI_TaxID=723619; RN [1] RP NUCLEOTIDE SEQUENCE. RA Pham V.D., Delong E.F.; RT "Genome fragments of uncultured bacteria from the North Pacific RT subtropical Gyre."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GU567960; ADI21596.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 91 AA; 9812 MW; 333FA31BEC129AAB CRC64; MKPIAFGRFV PFKTNPDAPA AAKSILNEAS KDLSSPIVAV IKIDTQNGRS LVSSGADMLA VVNAAFDSKE VYSNIKSLNK LFQSRERTLI T // ID E7C7B0_9GAMM Unreviewed; 218 AA. AC E7C7B0; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OS uncultured Oceanospirillales bacterium HF0770_27O18. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC environmental samples. OX NCBI_TaxID=723623; RN [1] RP NUCLEOTIDE SEQUENCE. RA Pham V.D., Delong E.F.; RT "Genome fragments of uncultured bacteria from the North Pacific RT subtropical Gyre."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GU568012; ADI23334.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23149 MW; 9FD321C9C2B3BBC2 CRC64; MSQPLQGLYA ITDPQLTPGD RVLSAAEAAL RGGATLLQYR DKPADADTRR HRAARLALLC KDHGARFIVN DDAALAAEVE ADGVHLGQSD GAVSRARMLL GDDKLIGVSC HGRLDLAQKA ADEGADYLAL GRFFESRTKP GAPPASLDTL REARRRFSLP LVAIGGVNPH NARQLIEAGA DLVAVIHALF GHADDADVEA AARRLHAAFP APPFKESQ // ID E7C8I7_9GAMM Unreviewed; 218 AA. AC E7C8I7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OS uncultured Oceanospirillales bacterium HF4000_43P14. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC environmental samples. OX NCBI_TaxID=723620; RN [1] RP NUCLEOTIDE SEQUENCE. RA Pham V.D., Delong E.F.; RT "Genome fragments of uncultured bacteria from the North Pacific RT subtropical Gyre."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GU568023; ADI23761.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23105 MW; 4AF4690BEC26AC4F CRC64; MSQPLQGLYA ISDPQLTPGD RVLSAAEAAL RGGATLLQYR DKPADADTRR HRAARLALLC KDHGARFIVN DDAALAAEVE ADGVHLGQSD GAVGRARMLL GDDKLIGVSC HGRLDLAQKA ADEGADYLAL GRFFESRTKP GAPPASLDTL REARRRFSLP LVAIGGVNPH NARQLIEAGA DLVAVIHALF GHADDADVEA AARRLHAAFP APPFKESQ // ID E7FYD8_9HELI Unreviewed; 207 AA. AC E7FYD8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HSUHS1_0019; OS Helicobacter suis HS1. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=710393; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HS1; RX PubMed=21414191; DOI=10.1186/1297-9716-42-51; RA Vermoote M., Vandekerckhove T.T., Flahou B., Pasmans F., Smet A., RA De Groote D., Van Criekinge W., Ducatelle R., Haesebrouck F.; RT "Genome sequence of Helicobacter suis supports its role in gastric RT pathology."; RL Vet. Res. 42:51-51(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGY01000006; EFX43654.1; -; Genomic_DNA. DR EnsemblBacteria; EFX43654; EFX43654; HSUHS1_0019. DR PATRIC; 46455583; VBIHelSui156523_0034. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22532 MW; 29C8A90B6C0642DC CRC64; MGIELKGLYA ISDEKLTPYH DLPKLLEQAI LGGVKLFQLR DKSHSDQNLR GLVNELSFLC TEKNVGFILN DRLELALECG VWGLHLGAKD TPLQEARSLF RGVIGVSCYG DLQRALKVQQ MGADYVAFGA CFVSQTKPNA PCIDLKILQE ARACLKIPIC AIGGITPFNV DQLGSVDLVA VVASLWVGDV LKNAQSLSLN SRNSKSF // ID E7G569_9HELI Unreviewed; 207 AA. AC E7G569; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HSUHS5_1151; OS Helicobacter suis HS5. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=710394; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HS5; RX PubMed=21414191; DOI=10.1186/1297-9716-42-51; RA Vermoote M., Vandekerckhove T.T., Flahou B., Pasmans F., Smet A., RA De Groote D., Van Criekinge W., Ducatelle R., Haesebrouck F.; RT "Genome sequence of Helicobacter suis supports its role in gastric RT pathology."; RL Vet. Res. 42:51-51(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADHO01000254; EFX41475.1; -; Genomic_DNA. DR EnsemblBacteria; EFX41475; EFX41475; HSUHS5_1151. DR PATRIC; 46462883; VBIHelSui148992_1629. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22532 MW; 29C8A90B6C0642DC CRC64; MGIELKGLYA ISDEKLTPYH DLPKLLEQAI LGGVKLFQLR DKSHSDQNLR GLVNELSFLC TEKNVGFILN DRLELALECG VWGLHLGAKD TPLQEARSLF RGVIGVSCYG DLQRALKVQQ MGADYVAFGA CFVSQTKPNA PCIDLKILQE ARACLKIPIC AIGGITPFNV DQLGSVDLVA VVASLWVGDV LKNAQSLSLN SRNSKSF // ID E7GAN3_9FIRM Unreviewed; 217 AA. AC E7GAN3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9488_01823; OS Coprobacillus sp. 29_1. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Coprobacillus. OX NCBI_TaxID=469596; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=29_1; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., RA Sibley C.D., White A., Strauss J., Allen-Vercoe E., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Coprobacillus sp. strain 29_1."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADKX01000032; EFW04934.1; -; Genomic_DNA. DR EnsemblBacteria; EFW04934; EFW04934; HMPREF9488_01823. DR PATRIC; 46466932; VBICopSp159203_1841. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23707 MW; BFF25DFAAC8EC2F2 CRC64; MKKDKQAIRK AMQLYLVTDR YWLGKHTLCE DVEKAVQAGV TCVQLREKKL NNHEFIREAG YLKYLCIKYA IPFIINDNVD VMLAVDADGV HVGQSDMKAH NVRQLIGENK ILGVSVQSVE QALEAQGAGA DYLGVGAVFH TGTKKDAVDV DIQTLKDICN AVQIPVVAIG GIGYQNILEL KDSGIAGVAV ISAILAQKDI HKATQCLKEI CQGLFND // ID E7GQ01_CLOSY Unreviewed; 213 AA. AC E7GQ01; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9474_02996; OS Clostridium symbiosum WAL-14163. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=742740; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-14163; RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., RA Summanen P.H., Molitoris D.R., Vaisanen M.L., Daigneault M., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J., RA Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium symbiosum strain WAL-14163."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLQ01000067; EGA93261.1; -; Genomic_DNA. DR EnsemblBacteria; EGA93261; EGA93261; HMPREF9474_02996. DR PATRIC; 46477959; VBICloSym155749_3320. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22836 MW; 30EFDBF0EBD7C097 CRC64; MNFDYTLYLV TDRQLMSCDS LTEAVEQAIL GGCTMIQLRE KELPSLEFYN QAVAVKQVTE RYHIPLIIND RIDIAMAVQA AGVHIGQHDL PAATVRKVIG ENMLLGVSAS SIAEAIQAQQ DGADYLGVGA MFPTGTKTDA ESVSMEELQK IRTAVSLPIV VIGGINKGNA GRFKPMGIDG LAVVSAIIAQ SDIKAAAAEL KDLFCGKEKK HGF // ID E7GQI8_CLOSY Unreviewed; 227 AA. AC E7GQI8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9474_03183; OS Clostridium symbiosum WAL-14163. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=742740; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-14163; RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., RA Summanen P.H., Molitoris D.R., Vaisanen M.L., Daigneault M., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J., RA Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium symbiosum strain WAL-14163."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLQ01000071; EGA93035.1; -; Genomic_DNA. DR EnsemblBacteria; EGA93035; EGA93035; HMPREF9474_03183. DR PATRIC; 46478373; VBICloSym155749_3526. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 24054 MW; 7E38C435A61D5E9E CRC64; MKFTKEEIHK SMLLYAVTDR MWLNEGETLI SVAEEVLKNG ATFLQIREKD LNEDDFEAEA EALHTLCAKY RIPFVVNDSV EIALRCNADG VHVGQSDIKG RDIRALIGPD AILGISAGTV QEAEAAEAAG ADYIGVGAVF TTGTKKDARS LTMEQLRAIR NAVSIPIVAI GGINSGNIMR LAGSGVDGVA VVSAIFAAPH PGEATAGMLK LAEEMLSAKT VRGEGNE // ID E7H3G5_9BURK Unreviewed; 216 AA. AC E7H3G5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9464_01253; OS Sutterella wadsworthensis 3_1_45B. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Sutterellaceae; Sutterella. OX NCBI_TaxID=742821; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_45B; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Sutterella wadsworthensis strain 3_1_45B."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMF01000024; EFW01512.1; -; Genomic_DNA. DR EnsemblBacteria; EFW01512; EFW01512; HMPREF9464_01253. DR PATRIC; 46498116; VBISutWad150710_1368. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22367 MW; D419F2BD07563D5C CRC64; MTVKPLNLTL YLVLDPDLCS QSVGIVETAL AAVQAGAGIV QLRAPTWKKR RMTECARSLK SALTPFHVPL IIDDHADVML AANADGLHVG QQDLTPADAR QLIGSNRILG LSLGSLEDCR PDELALVDYV GIGPTFVTQS KPDAGAAIGL TALQSIAAKA QKPSVAIGGI HINNAAQVGA AGVDGIAVIS AICGQPDPYA ASVSLLKAFQ SNRKQS // ID E7HDM0_ECOLX Unreviewed; 211 AA. AC E7HDM0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECEPECA14_2574; OS Escherichia coli EPECa14. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670893; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EPECa14; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUN01000080; EFZ41736.1; -; Genomic_DNA. DR ProteinModelPortal; E7HDM0; -. DR SMR; E7HDM0; 10-208. DR EnsemblBacteria; EFZ41736; EFZ41736; ECEPECA14_2574. DR PATRIC; 48550636; VBIEscCol144007_2475. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E7HV54_ECOLX Unreviewed; 211 AA. AC E7HV54; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECE128010_2475; OS Escherichia coli E128010. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670894; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E128010; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUO01000098; EFZ47195.1; -; Genomic_DNA. DR ProteinModelPortal; E7HV54; -. DR SMR; E7HV54; 10-208. DR EnsemblBacteria; EFZ47195; EFZ47195; ECE128010_2475. DR PATRIC; 47878565; VBIEscCol146042_2445. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E7I620_ECOLX Unreviewed; 211 AA. AC E7I620; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECLT68_0951; OS Escherichia coli LT-68. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670890; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LT-68; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUP01000028; EFZ60120.1; -; Genomic_DNA. DR ProteinModelPortal; E7I620; -. DR SMR; E7I620; 11-208. DR EnsemblBacteria; EFZ60120; EFZ60120; ECLT68_0951. DR PATRIC; 47886876; VBIEscCol138002_0923. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23027 MW; 0AE827392C8C3853 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGVSLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E7IU44_ECOLX Unreviewed; 211 AA. AC E7IU44; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECOK1180_3619; OS Escherichia coli OK1180. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670904; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OK1180; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUQ01000075; EFZ63133.1; -; Genomic_DNA. DR ProteinModelPortal; E7IU44; -. DR SMR; E7IU44; 10-208. DR EnsemblBacteria; EFZ63133; EFZ63133; ECOK1180_3619. DR PATRIC; 47904215; VBIEscCol141306_3515. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E7JBH7_ECOLX Unreviewed; 211 AA. AC E7JBH7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECOK1357_4384; OS Escherichia coli OK1357. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670905; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OK1357; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUR01000081; EFZ67502.1; -; Genomic_DNA. DR ProteinModelPortal; E7JBH7; -. DR SMR; E7JBH7; 20-202. DR EnsemblBacteria; EFZ67502; EFZ67502; ECOK1357_4384. DR PATRIC; 47917959; VBIEscCol138825_4276. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E7JIV4_ECOLX Unreviewed; 211 AA. AC E7JIV4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECRN5871_1946; OS Escherichia coli RN587/1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670899; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RN587/1; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUS01000023; EFZ75428.1; -; Genomic_DNA. DR EnsemblBacteria; EFZ75428; EFZ75428; ECRN5871_1946. DR PATRIC; 47923886; VBIEscCol138077_1916. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22972 MW; CC43678C52B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGAGD E // ID E7JZQ1_SHISO Unreviewed; 211 AA. AC E7JZQ1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SS53G_2403; OS Shigella sonnei 53G. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=216599; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=53G; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUU01000047; EFZ53171.1; -; Genomic_DNA. DR RefSeq; YP_005459300.1; NC_016822.1. DR ProteinModelPortal; E7JZQ1; -. DR EnsemblBacteria; EFZ53171; EFZ53171; SS53G_2403. DR GeneID; 11953567; -. DR KEGG; ssj:SSON53_24085; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23040 MW; 6DF9E5BB3D8C3E64 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRNEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E7KJB9_YEASA Unreviewed; 459 AA. AC E7KJB9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-APR-2014, entry version 11. DE SubName: Full=Thi6p; GN ORFNames=AWRI796_4799; OS Saccharomyces cerevisiae (strain AWRI796) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764097; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AWRI796; RX PubMed=21304888; DOI=10.1371/journal.pgen.1001287; RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H., RA Pretorius I.S., Egholm M., Chambers P.J.; RT "Whole-genome comparison reveals novel genetic elements that RT characterize the genome of industrial strains of Saccharomyces RT cerevisiae."; RL PLoS Genet. 7:E1001287-E1001287(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVS01000048; EGA72556.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 459 AA; 48985 MW; 9EBE466B9A67B2C1 CRC64; MAIDADGVHV GQDDMPIPMV RKLLGPSKIL GWSVGKPSEV ETLAKWGPDM VDYIGVGTLF PTSTKKNPKK SPMGPQGAIA ILDALEEFKA TWCRTVGIGG LHPDNIQRVL CQCVASNGKR SLDGISLVSD IMAAPDACAA TKRLRGLLDA TRYQFVECEL NNTFPTTTSI QNVISQVSNN RPLVQHITNK VHQNFGANVT LALGSSPIMS EIESEVSELA RIPNASLLLN TGSVAPIEML KAAINAYNEV NRPITFDPVG YSATETRLCL NNTLLTYGQF ACIKGNCSEI LSLAKLNNHK MKGVDSSSGK TNIDTLVRAT QIVAFQYRTV AVCTGEFDCV ADGTFGGEYK LSSGTEGITA EDLPCVIIED GPIPIMGDIT ASGCSLGSTI ASFIGGLDST GKLFDAVVGA VLLYKSAGKL ASTRCQGSGS FHVELIDALY QLFHENKPEK WSASLKKFK // ID E7KVB7_YEASL Unreviewed; 540 AA. AC E7KVB7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-APR-2014, entry version 14. DE SubName: Full=Thi6p; GN ORFNames=QA23_4763; OS Saccharomyces cerevisiae (strain Lalvin QA23) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764098; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lalvin QA23; RX PubMed=21304888; DOI=10.1371/journal.pgen.1001287; RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H., RA Pretorius I.S., Egholm M., Chambers P.J.; RT "Whole-genome comparison reveals novel genetic elements that RT characterize the genome of industrial strains of Saccharomyces RT cerevisiae."; RL PLoS Genet. 7:E1001287-E1001287(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVV01000082; EGA80397.1; -; Genomic_DNA. DR ProteinModelPortal; E7KVB7; -. DR SMR; E7KVB7; 3-536. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 58059 MW; F34FA1E0B76E3930 CRC64; MVFTKEEVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDIE TKNFVAEALE VQKICKKYNV PLIINDRIDV AMAIDADGVH VGQDDMPIPM VRKLLGPSKI LGWSVGKPSE VETLAKWGPD MVDYIGVGTL FPTSTKKNPK KSPMGPQGAI AILDALEEFK ATWCRTVGIG GLHPDNIQRV LCQCVASNGK RSLDGISLVS DIMAAPDACA ATKRLRGLLD ATRYQFVECE LNNTFPTTTS IQNVISQVSN NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL ARIPNASLLL NTGSVAPIEM LKAAINAYNE VNRPITFDPV GYSATETRLC LNNTLLTYGQ FACIKGNCSE ILSLAKLNNH KMKGVDSSSG KTNIDTLVRA TQIVAFQYRT VAVCTGEFDC VADGTFGGEY KLSSGTEGIT AEDLPCVIIE DGPIPIMGDI TASGCSLGST IASFIGGLDS TGKLFDAVVG AVLLYKSAGK LASTRCQGSG SFHVELIDAL YQLFHENKPE KWSASLKKFK // ID E7MEY7_STAAU Unreviewed; 213 AA. AC E7MEY7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9529_00869; OS Staphylococcus aureus subsp. aureus MRSA177. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=754026; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MRSA177; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECP01000014; EFW35489.1; -; Genomic_DNA. DR EnsemblBacteria; EFW35489; EFW35489; HMPREF9529_00869. DR PATRIC; 52370001; VBIStaAur152978_0823. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23339 MW; 60A447368EE3958F CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEC AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID E7MU22_STAAU Unreviewed; 213 AA. AC E7MU22; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9528_00992; OS Staphylococcus aureus subsp. aureus MRSA131. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=754025; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MRSA131; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECR01000022; EFW32588.1; -; Genomic_DNA. DR ProteinModelPortal; E7MU22; -. DR SMR; E7MU22; 4-209. DR PRIDE; E7MU22; -. DR EnsemblBacteria; EFW32588; EFW32588; HMPREF9528_00992. DR PATRIC; 52375773; VBIStaAur148469_0952. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID E7N062_9FIRM Unreviewed; 231 AA. AC E7N062; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9555_00355; OS Selenomonas artemidis F0399. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=749551; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0399; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECV01000001; EFW30726.1; -; Genomic_DNA. DR EnsemblBacteria; EFW30726; EFW30726; HMPREF9555_00355. DR PATRIC; 46556277; VBISelArt149184_0348. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 208 209 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 231 AA; 24360 MW; A84D2FB53A13B71C CRC64; MSMRKNFDLS AYLVIGPENT NGRPAARIIA EAVRAGFTFV QIRSKTAEAR ELIDLTRAAA EIIAAQEKSE RVALVVNDRL DVVLAARDAG VKVGGIHVGQ SDIPPEICRK YLGADAIVGL SARTSALIDY VRTCDTSCVD YFGAGPLHPT ATKPDAGRDA AGHVVTRTIE ELAELHRVSP LPVVVGGGVK AADLPALRAT GVEGFFVVST IAGAAHPFAA AEELVHIWRS A // ID E7P9U8_PSESG Unreviewed; 316 AA. AC E7P9U8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Uncharacterized protein; GN ORFNames=PsgB076_20962; OS Pseudomonas syringae pv. glycinea str. B076. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=875329; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B076; RX PubMed=21304594; DOI=10.1371/journal.pone.0016451; RA Qi M., Wang D., Bradley C.A., Zhao Y.; RT "Genome Sequence Analyses of Pseudomonas savastanoi pv. glycinea and RT Subtractive Hybridization-Based Comparative Genomics with Nine RT Pseudomonads."; RL PLoS ONE 6:E16451-E16451(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEGG01000049; EFW78532.1; -; Genomic_DNA. DR ProteinModelPortal; E7P9U8; -. DR EnsemblBacteria; EFW78532; EFW78532; PsgB076_20962. DR PATRIC; 52507761; VBIPseSyr168192_4120. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34062 MW; ABC09200328F7230 CRC64; MKRVHVAAAV IRGADGSVLI ARRADTQHQG GLWEFPGGKV EEGETVQAAL ARELQEELGI QVTAARPLIK VGHDYADKQV LLDVWEVSAF TGEPHGAEGQ PLVWAAPREL PDYDFPAANQ PIVAAARLPG EYLITPDGLD NIELLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPENRWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWQQ AAQLIAGFNK PVFLLGGVGP SERQQAWESG AQGVAGIRAF WPDEIV // ID E7PAI9_PSESG Unreviewed; 205 AA. AC E7PAI9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PsgB076_22182; OS Pseudomonas syringae pv. glycinea str. B076. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=875329; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B076; RX PubMed=21304594; DOI=10.1371/journal.pone.0016451; RA Qi M., Wang D., Bradley C.A., Zhao Y.; RT "Genome Sequence Analyses of Pseudomonas savastanoi pv. glycinea and RT Subtractive Hybridization-Based Comparative Genomics with Nine RT Pseudomonads."; RL PLoS ONE 6:E16451-E16451(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEGG01000049; EFW78773.1; -; Genomic_DNA. DR ProteinModelPortal; E7PAI9; -. DR EnsemblBacteria; EFW78773; EFW78773; PsgB076_22182. DR PATRIC; 52508265; VBIPseSyr168192_4369. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21968 MW; 8D8113EA1D6B9C94 CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKT SDESRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGSL ELAEQAKADG ATYVAFGRFF NSLTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN AQEVTRRAKA FMALL // ID E7PJ26_PSESG Unreviewed; 205 AA. AC E7PJ26; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-MAR-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Pgy4_29475, PsgRace4_08440; OS Pseudomonas syringae pv. glycinea str. race 4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=875330; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Race 4; RX PubMed=21304594; DOI=10.1371/journal.pone.0016451; RA Qi M., Wang D., Bradley C.A., Zhao Y.; RT "Genome Sequence Analyses of Pseudomonas savastanoi pv. glycinea and RT Subtractive Hybridization-Based Comparative Genomics with Nine RT Pseudomonads."; RL PLoS ONE 6:E16451-E16451(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Race 4; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEGH01000044; EFW86514.1; -; Genomic_DNA. DR EMBL; ADWY01001532; EGH17132.1; -; Genomic_DNA. DR EnsemblBacteria; EFW86514; EFW86514; PsgRace4_08440. DR EnsemblBacteria; EGH17132; EGH17132; Pgy4_29475. DR PATRIC; 52514563; VBIPseSyr203741_1638. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21968 MW; 8D8113EA1D6B9C94 CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKT SDESRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGSL ELAEQAKADG ATYVAFGRFF NSLTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN AQEVTRRAKA FMALL // ID E7PKA7_PSESG Unreviewed; 316 AA. AC E7PKA7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Uncharacterized protein; GN ORFNames=PsgRace4_10707; OS Pseudomonas syringae pv. glycinea str. race 4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=875330; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Race 4; RX PubMed=21304594; DOI=10.1371/journal.pone.0016451; RA Qi M., Wang D., Bradley C.A., Zhao Y.; RT "Genome Sequence Analyses of Pseudomonas savastanoi pv. glycinea and RT Subtractive Hybridization-Based Comparative Genomics with Nine RT Pseudomonads."; RL PLoS ONE 6:E16451-E16451(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEGH01000052; EFW86079.1; -; Genomic_DNA. DR ProteinModelPortal; E7PKA7; -. DR EnsemblBacteria; EFW86079; EFW86079; PsgRace4_10707. DR PATRIC; 52515495; VBIPseSyr203741_2085. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34062 MW; ABC09200328F7230 CRC64; MKRVHVAAAV IRGADGSVLI ARRADTQHQG GLWEFPGGKV EEGETVQAAL ARELQEELGI QVTAARPLIK VGHDYADKQV LLDVWEVSAF TGEPHGAEGQ PLVWAAPREL PDYDFPAANQ PIVAAARLPG EYLITPDGLD NIELLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPENRWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWQQ AAQLIAGFNK PVFLLGGVGP SERQQAWESG AQGVAGIRAF WPDEIV // ID E7QLM6_YEASZ Unreviewed; 540 AA. AC E7QLM6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-APR-2014, entry version 14. DE SubName: Full=Thi6p; GN ORFNames=VL3_4771; OS Saccharomyces cerevisiae (strain Zymaflore VL3) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764100; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Zymaflore VL3; RX PubMed=21304888; DOI=10.1371/journal.pgen.1001287; RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H., RA Pretorius I.S., Egholm M., Chambers P.J.; RT "Whole-genome comparison reveals novel genetic elements that RT characterize the genome of industrial strains of Saccharomyces RT cerevisiae."; RL PLoS Genet. 7:E1001287-E1001287(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEJS01000063; EGA84476.1; -; Genomic_DNA. DR ProteinModelPortal; E7QLM6; -. DR SMR; E7QLM6; 3-536. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 58059 MW; F34FA1E0B76E3930 CRC64; MVFTKEEVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDIE TKNFVAEALE VQKICKKYNV PLIINDRIDV AMAIDADGVH VGQDDMPIPM VRKLLGPSKI LGWSVGKPSE VETLAKWGPD MVDYIGVGTL FPTSTKKNPK KSPMGPQGAI AILDALEEFK ATWCRTVGIG GLHPDNIQRV LCQCVASNGK RSLDGISLVS DIMAAPDACA ATKRLRGLLD ATRYQFVECE LNNTFPTTTS IQNVISQVSN NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL ARIPNASLLL NTGSVAPIEM LKAAINAYNE VNRPITFDPV GYSATETRLC LNNTLLTYGQ FACIKGNCSE ILSLAKLNNH KMKGVDSSSG KTNIDTLVRA TQIVAFQYRT VAVCTGEFDC VADGTFGGEY KLSSGTEGIT AEDLPCVIIE DGPIPIMGDI TASGCSLGST IASFIGGLDS TGKLFDAVVG AVLLYKSAGK LASTRCQGSG SFHVELIDAL YQLFHENKPE KWSASLKKFK // ID E7RJE1_9BACL Unreviewed; 217 AA. AC E7RJE1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GPDM_13046; OS Planococcus donghaensis MPA1U2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Planococcus. OX NCBI_TaxID=933115; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MPA1U2; RX PubMed=21994932; DOI=10.1128/JB.05983-11; RA Pearson M.D., Noller H.F.; RT "The Draft Genome of Planococcus donghaensis MPA1U2 Reveals RT Nonsporulation Pathways Controlled by a Conserved Spo0A Regulon."; RL J. Bacteriol. 193:6106-6106(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPB01000044; EGA88783.1; -; Genomic_DNA. DR ProteinModelPortal; E7RJE1; -. DR EnsemblBacteria; EGA88783; EGA88783; GPDM_13046. DR PATRIC; 46589745; VBIPlaDon176822_2535. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23103 MW; 6638CD23F3C2DE2D CRC64; MRFSNKPAIY FVMGSQNLKA KAPLTALEEA LEGGITHFQL REKGTGALTG HALRNFALRC QQLCQSYSVP FIINDDVELA CSIDAAGVHV GQDDETAFQV RQLIGEEKLL GVSVHSVEEA RLAIQAGADY VGMGPVFGTT SKADAKKPAG VAGIIEVKQE YPHLPIVGIG GITPENADQV WRAGASGIAV ISAITNAKDI AEQVKAFQLS CREGIER // ID E7RSX6_9BACT Unreviewed; 204 AA. AC E7RSX6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF0663_12394; OS Prevotella oralis ATCC 33269. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=873533; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33269; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPE02000006; EFZ36327.1; -; Genomic_DNA. DR EnsemblBacteria; EFZ36327; EFZ36327; HMPREF0663_12394. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 204 AA; 23482 MW; C2BA2C61725D41DE CRC64; MTMKLVILTK STFFVEEDNI LATLFNEGME NLHVYKPGAS SLYLERLLSL LPEEHHSKIT IHNHYHLKNE FHLAGIHIDN DKATYPSGYK GSIGRSCTDL TTLKKLKKKS DYVFLGNIFD SIEFKEKKSN FNIKQLEEAS YQGLIDKHVF AFGGMNIEHA KIVRQLGFGG IVICGDLWQH FDIHRQTDFK TILTHFEKLH KTIS // ID E7RU72_9BURK Unreviewed; 226 AA. AC E7RU72; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0551_0038; OS Lautropia mirabilis ATCC 51599. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Lautropia. OX NCBI_TaxID=887898; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51599; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQP01000001; EFV95855.1; -; Genomic_DNA. DR EnsemblBacteria; EFV95855; EFV95855; HMPREF0551_0038. DR PATRIC; 46591249; VBILauMir174490_0037. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 55 59 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT METAL 88 88 Magnesium (By similarity). FT METAL 107 107 Magnesium (By similarity). FT BINDING 87 87 HMP-PP (By similarity). FT BINDING 126 126 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 183 183 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23825 MW; 6BE921C0F042414D CRC64; METAMLPASS PDHPERQARR ALIRGVYAIT ADEGDTTRLL ADVEAALSGG IRILQYRNKH ANRALKRQQL EALKGVCARH QALLIVNDDW QLAAELGIDA VHLGEDDGDI EEARRALGPG SLIGVSCYAS VERARALAPV ADYLAFGALF ASGTKPLARP APLSVFREVQ ALSLARPLVG IGGIDADNIG LVLAARADAA AVIGSLFRQG DIRAAAQRLV AAAARP // ID E7RYN4_9BURK Unreviewed; 342 AA. AC E7RYN4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 13-NOV-2013, entry version 15. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0551_1798; OS Lautropia mirabilis ATCC 51599. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Lautropia. OX NCBI_TaxID=887898; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51599; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQP01000020; EFV94358.1; -; Genomic_DNA. DR ProteinModelPortal; E7RYN4; -. DR EnsemblBacteria; EFV94358; EFV94358; HMPREF0551_1798. DR PATRIC; 46594777; VBILauMir174490_0631. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 342 AA; 37583 MW; EC26DB72830288F1 CRC64; MPIPMSAPKI VNVAVGILMR PDGQVLLGQR PAGKPYEGWW EFPGGKFEPG EDAAQAAVRE LEEELDIHVL ASQPWVVREH VYEHAHVRLH FRRVTAWEGE PRGREGQQLA WRALDAIDVE PLLPASLDPI RWLSLPAVYA ISDASARGID EWLQCLERWL EGKGLESARG SCAAPSRLLL LREPDMGPAS FDRLFNGVLE RVQGRDVRLM VSSRHPETYA QLAAEKTRGG IHLTGDDLHT SARDSRTAIE YLQVNYPMVA ASCHSAEDLR LAGLLKLDLA VCGPVLPTQS HPGRAGLGWE GLARMIEQTP VPVYALGGLN PAHLDDARQA GAQGVAMQRG VW // ID E7S4S5_STRAG Unreviewed; 223 AA. AC E7S4S5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9171_1271; OS Streptococcus agalactiae ATCC 13813. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888745; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 13813; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQQ01000066; EFV97237.1; -; Genomic_DNA. DR EnsemblBacteria; EFV97237; EFV97237; HMPREF9171_1271. DR PATRIC; 52952109; VBIStrAga174344_1232. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24579 MW; BE93BD7D2C0AFCA5 CRC64; MKDTLKLYFV CGTVDCSRKN ILTVVEEALQ AGITLFQFRE KGFTALQGKE KIAMAKQLQI LCKQYQVPFI IDDDIDLVEL IDADGLHIGQ NDLPVDEARR RLPDKIIGLS VSTMAEYQKS QLSVVDYIGI GPFNPTQSKA DAKPAVGNRT TKAVREINQD IPIVAIGGIT SDFVHDIIES GADGIAVISA ISKANHIVDA TRQLRYEVEK ALVNRQKHSD VTK // ID E7SR66_SHIDY Unreviewed; 211 AA. AC E7SR66; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SDB_04715; OS Shigella dysenteriae CDC 74-1112. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=941429; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC 74-1112; RA Mane S.P., Sobral B.W., Cebula T., Kiss H., Munk A.C., Tapia R., RA Green L., Rogers Y., Detter J.C., Bruce D., Brettin T.S.; RT "Shigella flexneri CDC 796-83 whole genome shotgun sequencing RT project."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERM01000241; EFW47979.1; -; Genomic_DNA. DR ProteinModelPortal; E7SR66; -. DR SMR; E7SR66; 10-208. DR EnsemblBacteria; EFW47979; EFW47979; SDB_04715. DR PATRIC; 47309591; VBIAERShi179086_4762. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E7T0M4_SHIBO Unreviewed; 211 AA. AC E7T0M4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SGB_03275; OS Shigella boydii ATCC 9905. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=932676; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 9905; RA Mane S.P., Sobral B.W., Cebula T., Sims D., Munk A.C., Tapia R., RA Green L., Rogers Y., Detter J.C., Bruce D., Brettin T.S.; RT "Shigella boydii ATCC 9905 whole genome shotgun sequencing project."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERN01000069; EFW54495.1; -; Genomic_DNA. DR EnsemblBacteria; EFW54495; EFW54495; SGB_03275. DR PATRIC; 47316871; VBIAERShi181732_3302. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22996 MW; DD2B95245CBC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVEHLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E7TBA9_SHIFL Unreviewed; 211 AA. AC E7TBA9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SGF_01832; OS Shigella flexneri CDC 796-83. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=945360; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC 796-83; RA Mane S.P., Sobral B.W., Cebula T., Chertkov O., Munk A.C., Tapia R., RA Green L., Rogers Y., Detter J.C., Bruce D., Brettin T.S.; RT "Shigella flexneri CDC 796-83 whole genome shotgun sequencing RT project."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERO01000076; EFW60715.1; -; Genomic_DNA. DR ProteinModelPortal; E7TBA9; -. DR EnsemblBacteria; EFW60715; EFW60715; SGF_01832. DR PATRIC; 47325249; VBIAERShi177170_1839. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23055 MW; 0AF6D6D635A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVISAIT QAADWRLATA QLLEIAGVGD E // ID E7TQP2_ECO57 Unreviewed; 211 AA. AC E7TQP2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECoD_02329; OS Escherichia coli O157:H7 str. EC1212. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=941435; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC1212; RA Mane S.P., Sobral B.W., Cebula T., Munk A.C., Tapia R., Green L., RA Rogers Y., Detter J.C., Bruce D., Brettin T.S.; RT "E. coli O157.H7 str. EC1212 Isolate A whole genome shotgun sequencing RT project."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERQ01000011; EFW65560.1; -; Genomic_DNA. DR ProteinModelPortal; E7TQP2; -. DR SMR; E7TQP2; 10-209. DR EnsemblBacteria; EFW65560; EFW65560; ECoD_02329. DR PATRIC; 47348787; VBIAEREsc180439_2340. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E7U214_ECOLX Unreviewed; 211 AA. AC E7U214; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EcoM_00596; OS Escherichia coli WV_060327. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=945433; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WV_060327; RA Mane S.P., Sobral B.W., Cebula T., Mammel M., LeClerc E.J.E., RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S.; RT "Escherichia coli 4142 strain WV_060327 whole genome shotgun RT sequencing project."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERT01000008; EFW71730.1; -; Genomic_DNA. DR ProteinModelPortal; E7U214; -. DR SMR; E7U214; 9-208. DR EnsemblBacteria; EFW71730; EFW71730; EcoM_00596. DR PATRIC; 47368721; VBIAEREsc178877_0586. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E7UL86_ECOLX Unreviewed; 211 AA. AC E7UL86; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECoL_03005; OS Escherichia coli EC4100B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=945434; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC4100B; RA Mane S.P., Sobral B.W., Cebula T., Mammel M., Saunders E., Munk A.C., RA Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., Brettin T.S.; RT "Escherichia coli EC4100B whole genome shotgun sequencing project."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERU01000022; EFW74756.1; -; Genomic_DNA. DR ProteinModelPortal; E7UL86; -. DR SMR; E7UL86; 10-208. DR EnsemblBacteria; EFW74756; EFW74756; ECoL_03005. DR PATRIC; 47383355; VBIAEREsc181802_3037. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E7V258_SALTM Unreviewed; 211 AA. AC E7V258; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEE_03660; OS Salmonella enterica subsp. enterica serovar Typhimurium str. TN061786. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=946034; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TN061786; RA Mane S.P., Sobral B.W., Cebula T., Munk A.C., Tapia R., Green L., RA Rogers Y., Detter J.C., Bruce D., Brettin T.S.; RT "Salmonella enterica subsp. enterica serovar Typhimurium Str. TN061786 RT whole genome shotgun sequencing project."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERV01000018; EFX48430.1; -; Genomic_DNA. DR ProteinModelPortal; E7V258; -. DR EnsemblBacteria; EFX48430; EFX48430; SEE_03660. DR PATRIC; 47395480; VBIAERSal180824_3683. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22983 MW; 803CF861FC550D88 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE SGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID E7V716_SALMO Unreviewed; 211 AA. AC E7V716; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM315_19428; OS Salmonella enterica subsp. enterica serovar Montevideo str. 315996572. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=745015; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=315996572; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=315996572; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESH01000007; EFY13182.1; -; Genomic_DNA. DR EnsemblBacteria; EFY13182; EFY13182; SEEM315_19428. DR PATRIC; 53041644; VBISalEnt184922_1048. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7VTG0_SALMO Unreviewed; 211 AA. AC E7VTG0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM971_08073; OS Salmonella enterica subsp. enterica serovar Montevideo str. 495297-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=745017; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=495297-1; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=495297-1; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESI01000051; EFY14187.1; -; Genomic_DNA. DR EnsemblBacteria; EFY14187; EFY14187; SEEM971_08073. DR PATRIC; 53058453; VBISalEnt183326_4581. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7VU05_SALMO Unreviewed; 211 AA. AC E7VU05; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM973_18793; OS Salmonella enterica subsp. enterica serovar Montevideo str. 495297-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=745018; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=495297-3; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=495297-3; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESJ01000004; EFY22758.1; -; Genomic_DNA. DR EnsemblBacteria; EFY22758; EFY22758; SEEM973_18793. DR PATRIC; 53058885; VBISalEnt185858_0192. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7WEU7_SALMO Unreviewed; 211 AA. AC E7WEU7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM974_07146; OS Salmonella enterica subsp. enterica serovar Montevideo str. 495297-4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=745019; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=495297-4; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=495297-4; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESK01000036; EFY23461.1; -; Genomic_DNA. DR EnsemblBacteria; EFY23461; EFY23461; SEEM974_07146. DR PATRIC; 53076257; VBISalEnt184299_4038. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7WQP9_SALMO Unreviewed; 211 AA. AC E7WQP9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM201_02468; OS Salmonella enterica subsp. enterica serovar Montevideo str. 515920-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=745020; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=515920-1; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=515920-1; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESL01000031; EFY28251.1; -; Genomic_DNA. DR EnsemblBacteria; EFY28251; EFY28251; SEEM201_02468. DR PATRIC; 53084864; VBISalEnt183868_3610. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7X3H0_SALMO Unreviewed; 211 AA. AC E7X3H0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM202_11366; OS Salmonella enterica subsp. enterica serovar Montevideo str. 515920-2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=745021; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=515920-2; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=515920-2; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESM01000027; EFY31925.1; -; Genomic_DNA. DR EnsemblBacteria; EFY31925; EFY31925; SEEM202_11366. DR PATRIC; 53095840; VBISalEnt183434_4332. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7X6T6_SALMO Unreviewed; 211 AA. AC E7X6T6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM954_12975; OS Salmonella enterica subsp. enterica serovar Montevideo str. 531954. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=745022; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=531954; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=531954; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESN01000037; EFY39202.1; -; Genomic_DNA. DR EnsemblBacteria; EFY39202; EFY39202; SEEM954_12975. DR PATRIC; 53098401; VBISalEnt182317_0950. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7XIU7_SALMO Unreviewed; 211 AA. AC E7XIU7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM054_00410; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS NC_MB110209-0054. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=749949; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NC_MB110209-0054; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NC_MB110209-0054; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESO01000036; EFY43303.1; -; Genomic_DNA. DR EnsemblBacteria; EFY43303; EFY43303; SEEM054_00410. DR PATRIC; 53107920; VBISalEnt182355_1263. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7XXK3_SALMO Unreviewed; 211 AA. AC E7XXK3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM675_10692; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS OH_2009072675. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=749950; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OH_2009072675; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OH_2009072675; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESP01000042; EFY47190.1; -; Genomic_DNA. DR EnsemblBacteria; EFY47190; EFY47190; SEEM675_10692. DR PATRIC; 53118669; VBISalEnt183828_1818. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7Y8P3_SALMO Unreviewed; 211 AA. AC E7Y8P3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM965_08162; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS CASC_09SCPH15965. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=749951; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CASC_09SCPH15965; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CASC_09SCPH15965; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESQ01000020; EFY52204.1; -; Genomic_DNA. DR EnsemblBacteria; EFY52204; EFY52204; SEEM965_08162. DR PATRIC; 53127248; VBISalEnt184925_1271. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7YTT7_SALMO Unreviewed; 211 AA. AC E7YTT7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM19N_14147; OS Salmonella enterica subsp. enterica serovar Montevideo str. 19N. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=763919; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=19N; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESV01000059; EFY53581.1; -; Genomic_DNA. DR EnsemblBacteria; EFY53581; EFY53581; SEEM19N_14147. DR PATRIC; 53143568; VBISalEnt184328_4439. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7YVJ7_SALMO Unreviewed; 211 AA. AC E7YVJ7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM801_08542; OS Salmonella enterica subsp. enterica serovar Montevideo str. 81038-01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=766762; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=81038-01; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=81038-01; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESZ01000005; EFY61749.1; -; Genomic_DNA. DR EnsemblBacteria; EFY61749; EFY61749; SEEM801_08542. DR PATRIC; 53144822; VBISalEnt186186_0457. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7Z6W2_SALMO Unreviewed; 211 AA. AC E7Z6W2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM507_22167; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS MD_MDA09249507. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=789332; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MD_MDA09249507; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MD_MDA09249507; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETA01000010; EFY65892.1; -; Genomic_DNA. DR EnsemblBacteria; EFY65892; EFY65892; SEEM507_22167. DR PATRIC; 53154793; VBISalEnt182429_0714. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7ZST1_SALMO Unreviewed; 211 AA. AC E7ZST1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM877_02431; OS Salmonella enterica subsp. enterica serovar Montevideo str. 414877. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=858313; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=414877; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=414877; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETB01000044; EFY67106.1; -; Genomic_DNA. DR EnsemblBacteria; EFY67106; EFY67106; SEEM877_02431. DR PATRIC; 53171211; VBISalEnt183482_4062. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E7ZUJ6_SALMO Unreviewed; 211 AA. AC E7ZUJ6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM867_06681; OS Salmonella enterica subsp. enterica serovar Montevideo str. 366867. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=858314; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=366867; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=366867; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETC01000003; EFY75255.1; -; Genomic_DNA. DR EnsemblBacteria; EFY75255; EFY75255; SEEM867_06681. DR PATRIC; 53172530; VBISalEnt184603_0097. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8AH97_SALMO Unreviewed; 211 AA. AC E8AH97; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM180_01317; OS Salmonella enterica subsp. enterica serovar Montevideo str. 413180. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=858315; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=413180; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=413180; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETD01000036; EFY75407.1; -; Genomic_DNA. DR EnsemblBacteria; EFY75407; EFY75407; SEEM180_01317. DR PATRIC; 53191168; VBISalEnt183898_4548. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8AHG4_SALMO Unreviewed; 211 AA. AC E8AHG4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM600_08609; OS Salmonella enterica subsp. enterica serovar Montevideo str. 446600. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=858316; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=446600; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=446600; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETE01000001; EFY84091.1; -; Genomic_DNA. DR EnsemblBacteria; EFY84091; EFY84091; SEEM600_08609. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8B1V7_SALMO Unreviewed; 211 AA. AC E8B1V7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM581_19943; OS Salmonella enterica subsp. enterica serovar Montevideo str. 609458-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=858317; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=609458-1; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=609458-1; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETF01000054; EFZ78605.1; -; Genomic_DNA. DR EnsemblBacteria; EFZ78605; EFZ78605; SEEM581_19943. DR PATRIC; 53197253; VBISalEnt184257_2882. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8B6L6_SALMO Unreviewed; 211 AA. AC E8B6L6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM501_03292; OS Salmonella enterica subsp. enterica serovar Montevideo str. 556150-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=858318; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=556150-1; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=556150-1; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETG01000001; EFZ85758.1; -; Genomic_DNA. DR EnsemblBacteria; EFZ85758; EFZ85758; SEEM501_03292. DR PATRIC; 53200827; VBISalEnt186463_0017. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8BS62_SALMO Unreviewed; 211 AA. AC E8BS62; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM460_15957; OS Salmonella enterica subsp. enterica serovar Montevideo str. 609460. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=859198; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=609460; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=609460; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETH01000080; EFZ87230.1; -; Genomic_DNA. DR EnsemblBacteria; EFZ87230; EFZ87230; SEEM460_15957. DR PATRIC; 53216667; VBISalEnt182877_3062. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8CF51_SALMO Unreviewed; 211 AA. AC E8CF51; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM6152_01271; OS Salmonella enterica subsp. enterica serovar Montevideo str. 556152. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=871586; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=556152; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=556152; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETJ01000080; EFZ96447.1; -; Genomic_DNA. DR EnsemblBacteria; EFZ96447; EFZ96447; SEEM6152_01271. DR PATRIC; 53234934; VBISalEnt184735_2681. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8CM96_SALMO Unreviewed; 211 AA. AC E8CM96; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM0077_12858; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS MB101509-0077. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=871587; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MB101509-0077; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MB101509-0077; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETK01000008; EGA02765.1; -; Genomic_DNA. DR EnsemblBacteria; EGA02765; EGA02765; SEEM0077_12858. DR PATRIC; 53240369; VBISalEnt185604_0624. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8D3B1_SALMO Unreviewed; 211 AA. AC E8D3B1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM0047_11074; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS MB102109-0047. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=871588; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MB102109-0047; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MB102109-0047; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETL01000095; EGA05763.1; -; Genomic_DNA. DR EnsemblBacteria; EGA05763; EGA05763; SEEM0047_11074. DR PATRIC; 53253142; VBISalEnt185741_2138. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8DGS4_SALMO Unreviewed; 211 AA. AC E8DGS4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM0055_21365; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS MB110209-0055. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=871589; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MB110209-0055; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MB110209-0055; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETM01000089; EGA09953.1; -; Genomic_DNA. DR EnsemblBacteria; EGA09953; EGA09953; SEEM0055_21365. DR PATRIC; 53263481; VBISalEnt183470_2424. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8DS98_SALMO Unreviewed; 211 AA. AC E8DS98; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM0052_01137; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS MB111609-0052. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=871590; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MB111609-0052; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MB111609-0052; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETN01000018; EGA15097.1; -; Genomic_DNA. DR EnsemblBacteria; EGA15097; EGA15097; SEEM0052_01137. DR PATRIC; 53271490; VBISalEnt184909_1598. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8E1Z5_SALMO Unreviewed; 211 AA. AC E8E1Z5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM3312_10231; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS 2009083312. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=871591; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2009083312; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2009083312; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETO01000014; EGA19844.1; -; Genomic_DNA. DR EnsemblBacteria; EGA19844; EGA19844; SEEM3312_10231. DR PATRIC; 53280206; VBISalEnt186300_1246. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8EC55_SALMO Unreviewed; 211 AA. AC E8EC55; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM5258_19487; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS 2009085258. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=871592; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2009085258; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2009085258; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETP01000013; EGA24122.1; -; Genomic_DNA. DR EnsemblBacteria; EGA24122; EGA24122; SEEM5258_19487. DR PATRIC; 53289795; VBISalEnt186256_1305. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8EUL5_SALMO Unreviewed; 211 AA. AC E8EUL5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM1156_11507; OS Salmonella enterica subsp. enterica serovar Montevideo str. 315731156. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=871593; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=315731156; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=315731156; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETQ01000030; EGA26613.1; -; Genomic_DNA. DR EnsemblBacteria; EGA26613; EGA26613; SEEM1156_11507. DR PATRIC; 53303377; VBISalEnt185849_3299. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8EZP8_SALMO Unreviewed; 211 AA. AC E8EZP8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM9199_05861; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS IA_2009159199. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=882863; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2009159199; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2009159199; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETR01000019; EGA33608.1; -; Genomic_DNA. DR EnsemblBacteria; EGA33608; EGA33608; SEEM9199_05861. DR PATRIC; 53307288; VBISalEnt184975_0571. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8FGG7_SALMO Unreviewed; 211 AA. AC E8FGG7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM8282_11520; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS IA_2010008282. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=882864; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2010008282; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2010008282; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETS01000035; EGA36425.1; -; Genomic_DNA. DR EnsemblBacteria; EGA36425; EGA36425; SEEM8282_11520. DR PATRIC; 53320290; VBISalEnt183082_2226. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8FU86_SALMO Unreviewed; 211 AA. AC E8FU86; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM8283_09603; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS IA_2010008283. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=882865; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2010008283; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2010008283; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETT01000072; EGA40634.1; -; Genomic_DNA. DR EnsemblBacteria; EGA40634; EGA40634; SEEM8283_09603. DR PATRIC; 53330440; VBISalEnt185837_2507. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8G5C4_SALMO Unreviewed; 211 AA. AC E8G5C4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM8284_13119; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS IA_2010008284. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=882866; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2010008284; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2010008284; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETU01000048; EGA45619.1; -; Genomic_DNA. DR EnsemblBacteria; EGA45619; EGA45619; SEEM8284_13119. DR PATRIC; 53338878; VBISalEnt185067_1889. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8GPG5_SALMO Unreviewed; 211 AA. AC E8GPG5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM8285_18347; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS IA_2010008285. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=882867; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2010008285; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2010008285; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETV01000041; EGA47453.1; -; Genomic_DNA. DR EnsemblBacteria; EGA47453; EGA47453; SEEM8285_18347. DR PATRIC; 53353965; VBISalEnt184010_4578. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8H1H5_SALMO Unreviewed; 211 AA. AC E8H1H5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM8287_09732; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS IA_2010008287. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=882869; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2010008287; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2010008287; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETW01000068; EGA51918.1; -; Genomic_DNA. DR EnsemblBacteria; EGA51918; EGA51918; SEEM8287_09732. DR PATRIC; 53363337; VBISalEnt182471_4514. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID E8H9Q9_ECO57 Unreviewed; 211 AA. AC E8H9Q9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECO5101_19973; OS Escherichia coli O157:H7 str. G5101. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=926026; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=G5101; RX PubMed=21317333; DOI=10.1128/JB.00118-11; RA Rump L.V., Strain E.A., Cao G., Allard M.W., Fischer M., Brown E.W., RA Gonzalez-Escalona N.; RT "Draft genome sequences of six Escherichia coli isolates from the RT stepwise model of emergence of Escherichia coli O157:H7."; RL J. Bacteriol. 193:2058-2059(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=G5101; RA Gonzaliz-Escalona N.; RT "The complete plasmid sequence of Escherichia coli 0157:H7 str. RT G5101."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETX01000112; EFX08724.1; -; Genomic_DNA. DR ProteinModelPortal; E8H9Q9; -. DR SMR; E8H9Q9; 10-209. DR EnsemblBacteria; EFX08724; EFX08724; ECO5101_19973. DR PATRIC; 48119948; VBIEscCol185374_2837. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E8HNH3_ECOLX Unreviewed; 211 AA. AC E8HNH3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECO9389_00075; OS Escherichia coli O157:H- str. 493-89. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=926027; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=493-89; RX PubMed=21317333; DOI=10.1128/JB.00118-11; RA Rump L.V., Strain E.A., Cao G., Allard M.W., Fischer M., Brown E.W., RA Gonzalez-Escalona N.; RT "Draft genome sequences of six Escherichia coli isolates from the RT stepwise model of emergence of Escherichia coli O157:H7."; RL J. Bacteriol. 193:2058-2059(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETY01000103; EFX13541.1; -; Genomic_DNA. DR ProteinModelPortal; E8HNH3; -. DR SMR; E8HNH3; 10-209. DR EnsemblBacteria; EFX13541; EFX13541; ECO9389_00075. DR PATRIC; 48130337; VBIEscCol183878_2867. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E8I2G2_ECOLX Unreviewed; 211 AA. AC E8I2G2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECO2687_09939; OS Escherichia coli O157:H- str. H 2687. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=926028; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H 2687; RX PubMed=21317333; DOI=10.1128/JB.00118-11; RA Rump L.V., Strain E.A., Cao G., Allard M.W., Fischer M., Brown E.W., RA Gonzalez-Escalona N.; RT "Draft genome sequences of six Escherichia coli isolates from the RT stepwise model of emergence of Escherichia coli O157:H7."; RL J. Bacteriol. 193:2058-2059(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETZ01000109; EFX18318.1; -; Genomic_DNA. DR ProteinModelPortal; E8I2G2; -. DR SMR; E8I2G2; 10-209. DR EnsemblBacteria; EFX18318; EFX18318; ECO2687_09939. DR PATRIC; 48140963; VBIEscCol183164_2931. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E8IGK1_ECOLX Unreviewed; 211 AA. AC E8IGK1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECO7815_21790; OS Escherichia coli O55:H7 str. 3256-97. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=926029; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3256-97 TW 07815; RX PubMed=21317333; DOI=10.1128/JB.00118-11; RA Rump L.V., Strain E.A., Cao G., Allard M.W., Fischer M., Brown E.W., RA Gonzalez-Escalona N.; RT "Draft genome sequences of six Escherichia coli isolates from the RT stepwise model of emergence of Escherichia coli O157:H7."; RL J. Bacteriol. 193:2058-2059(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUA01000085; EFX23086.1; -; Genomic_DNA. DR ProteinModelPortal; E8IGK1; -. DR SMR; E8IGK1; 10-209. DR EnsemblBacteria; EFX23086; EFX23086; ECO7815_21790. DR PATRIC; 48151638; VBIEscCol182397_3039. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E8IUQ3_ECOLX Unreviewed; 211 AA. AC E8IUQ3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECO5905_13202; OS Escherichia coli O55:H7 str. USDA 5905. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=926030; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=USDA 5905; RX PubMed=21317333; DOI=10.1128/JB.00118-11; RA Rump L.V., Strain E.A., Cao G., Allard M.W., Fischer M., Brown E.W., RA Gonzalez-Escalona N.; RT "Draft genome sequences of six Escherichia coli isolates from the RT stepwise model of emergence of Escherichia coli O157:H7."; RL J. Bacteriol. 193:2058-2059(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUB01000057; EFX28228.1; -; Genomic_DNA. DR ProteinModelPortal; E8IUQ3; -. DR SMR; E8IUQ3; 10-209. DR EnsemblBacteria; EFX28228; EFX28228; ECO5905_13202. DR PATRIC; 48161660; VBIEscCol185931_2792. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E8J8Z7_ECO57 Unreviewed; 211 AA. AC E8J8Z7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECOSU61_00085; OS Escherichia coli O157:H7 str. LSU-61. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=926032; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LSU-61; RA Rump L.V., Strain E.A., Cao G., Allard M.W., Fischer M., RA Gonzalez-Escalona N.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUC01000088; EFX32923.1; -; Genomic_DNA. DR ProteinModelPortal; E8J8Z7; -. DR SMR; E8J8Z7; 10-209. DR EnsemblBacteria; EFX32923; EFX32923; ECOSU61_00085. DR PATRIC; 48172505; VBIEscCol185276_2879. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E8JNH6_STREI Unreviewed; 210 AA. AC E8JNH6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0819_0549; OS Streptococcus equinus ATCC 9812. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=525379; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 9812; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVB01000016; EFW89240.1; -; Genomic_DNA. DR EnsemblBacteria; EFW89240; EFW89240; HMPREF0819_0549. DR PATRIC; 46642172; VBIStrEqu32851_0152. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22957 MW; C595F9D053A96A94 CRC64; MNKEELRVYF ICGTPNCPKG MFFKTLEAAL KSGVTCFQLR EKGDGALIGK EKLDLTLKVK ELCHKYHVPF IINDDVDLAL QVDADGIHVR QDDLPVTEAR KLFSNKIIGL SVGDVREYQL SEIDLVDYIG VGPIFPTPSK SDAGEVIELK GLREIRELDK VIPIVAIGGI TIGDVPSICE SGADGVAVIS ALAKSTQVEL DTQRFAEAFH // ID E8KGL9_9PAST Unreviewed; 225 AA. AC E8KGL9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0027_0986; OS Actinobacillus ureae ATCC 25976. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=887324; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25976; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVG01000065; EFX91957.1; -; Genomic_DNA. DR EnsemblBacteria; EFX91957; EFX91957; HMPREF0027_0986. DR PATRIC; 46661832; VBIActUre170509_1245. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT REGION 203 204 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 183 183 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 24719 MW; AF53C0F9EF87D6A0 CRC64; MIMHDIQQML TLYFIAGTQD CPNPTEDRAK NLFLILEQAL QAGITCFQFR DKGNNSLEAQ PQAQKALAIQ CRDLCHRYKV PFIVDDNVAL AIEIDADGVH VGQKDISPIM IRQMTNKPLI IGLSNNTLED LWHSEQMIEV DYCGLGPVFP TNSKEKHNPP IGLDFVKKAR DAGIRKPIVS IGGVKAEHVA ILKQNGANGI AVISAISLAS NVSQAVKALL YGYLN // ID E8LB34_9FIRM Unreviewed; 192 AA. AC E8LB34; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF9443_00042; OS Phascolarctobacterium succinatutens YIT 12067. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Phascolarctobacterium. OX NCBI_TaxID=626939; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12067; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVN01000003; EFY05950.1; -; Genomic_DNA. DR EnsemblBacteria; EFY05950; EFY05950; HMPREF9443_00042. DR PATRIC; 46683262; VBIPhaSp142870_0038. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 192 AA; 20506 MW; 05626D5E2CE0ADCD CRC64; MSELPLIAVT DSATCPRPLA EQIERLAKLT KLRPQAVILR AKSLDKAAYR TLALQAQQSC EAAGIPLILH SDWQLASELG IKKLHLPLAL LRQLPTCERA HFTWLSTSVH SVEEAIEAQA LGATVLIAGH IYTTQCKAGL APRGLGFLQA VCSAVSLLVY AIGGIGFDAA QHAELQANGA RGACVMSAYM RL // ID E8LBI5_9FIRM Unreviewed; 211 AA. AC E8LBI5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9443_00196; OS Phascolarctobacterium succinatutens YIT 12067. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Phascolarctobacterium. OX NCBI_TaxID=626939; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12067; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVN01000007; EFY05757.1; -; Genomic_DNA. DR EnsemblBacteria; EFY05757; EFY05757; HMPREF9443_00196. DR PATRIC; 46683549; VBIPhaSp142870_0177. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21828 MW; 5BC43492A9E07723 CRC64; MKAQPDYSIY LVTDDGCLQG RTLIDCVREA LEGGVTLVQY RAKTASSAEM YAEALQLKAL CDSFNVPLII NDRLDIAMAV GAAGVHLGQD DLPCAAARKI LGEDYLIGVS AHNPAEAKAA LQNGADYLGC GAVFGTATKA DVQKLGTDGL AAICREKGLP VVGIGGVTAD NYREVRAAGA DGAAIVSGIL AQSDIRATVK AIAKVSQEFA K // ID E8LMA4_9GAMM Unreviewed; 498 AA. AC E8LMA4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9444_01889; OS Succinatimonas hippei YIT 12066. OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Succinivibrionaceae; Succinatimonas. OX NCBI_TaxID=762983; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12066; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVO01000131; EFY06376.1; -; Genomic_DNA. DR EnsemblBacteria; EFY06376; EFY06376; HMPREF9444_01889. DR PATRIC; 46691035; VBISucHip160816_1738. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 498 AA; 53526 MW; 3ABE6F90E1796AAE CRC64; MTSKRPLVLI AATVDSGGGA GITADILSIH DHGAWGLPLV NAVSSQSLKR VAGIENISAA MFSNMLDVAL SDWEEISAVK VGLMPDRKTL DIFLTALETK LKGVKVVWDP VLTATAGRLE SADLKSNLSR ILKVTTIFTP NLPEALELAG WDKARLKQDG VFELGRFFVK MGAKNVIIKG GHLGDSVATA DDVFVSERLS FMMRLPKAAG DGAHGGGCAL SSALAALLAK DYAPEDAAVL AKAYVYHGIL DPDLQSDGGR PPVGHHGLIC SLKYFPEIFE EGFPQKAEPF PLCPTQLGLY PVVDSVEWVE TLLAMGVRTI QLRIKDKNDP QLAEKIKRSV FLSKTYKARL FIDDHYDLAI AAGAYGVHLG MEDLRTADLE KIRKSGLRLG VSTHGLYEML KGLQLNPSYI ALGHIFPTKS KVMPSKPQGV EKLAHEAALL ENVVPTVAIG GIKLHNLADV LSTKVGSVAL ITGITQSDDP LLTTQKWLNL CKNGGDEI // ID E8LUG2_9VIBR Unreviewed; 445 AA. AC E8LUG2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VIBR0546_10659; OS Vibrio brasiliensis LMG 20546. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=945543; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 20546; RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0; RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., RA Naum M., McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.; RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge RT Scleritoderma cyanea."; RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVS01000063; EGA65705.1; -; Genomic_DNA. DR EnsemblBacteria; EGA65705; EGA65705; VIBR0546_10659. DR PATRIC; 46707848; VBIVibBra176315_2111. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 445 AA; 49694 MW; 48AB3E7C94511525 CRC64; MTKILLPSSY VELTGDVQQC LLLAKEQGFS IDSIELGVSP TQLIQLVQGQ QITSISTDLN VEERALDLAD YVFVYRSNIL VEHYLQQTRN AIFIGIQDVD STQRDRDYSQ FDIWRHPSTN EVRALSVLLD SCANTAPEYH LCWVLTLLAL DFPLEDSLTL ARAMQASAKS VSRETLSSRA WRIVDAWPAQ YSDFPTPVLE DNRIGIKVGW HAGRDLSPFE TLSESSLGLY PVVDDVDWIE RLLPMGVTTI QLRIKNPDQD DLEQQIKKAI DLGRQHNAQV FINDYWQLAI KHGAFGVHLG QEDIEQSNLS QLNHAGICLG LSTHGYYELL RIVQISPSYI ALGHIFPTTT KQMPSQPQGV VRLALYQKLI DSIPYGDRTG VPTVAIGGID QSNADEVWQC GVTSLAVVRA ITLAKSPQQV IEFFNQLMGS NLIGATEHKE VIEHA // ID E8MC65_9VIBR Unreviewed; 204 AA. AC E8MC65; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VISI1226_08824; OS Vibrio sinaloensis DSM 21326. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=945550; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 21326; RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0; RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., RA Naum M., McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.; RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge RT Scleritoderma cyanea."; RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVT01000107; EGA68370.1; -; Genomic_DNA. DR EnsemblBacteria; EGA68370; EGA68370; VISI1226_08824. DR PATRIC; 46720407; VBIVibSin177761_3951. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22034 MW; 041D0697FF9ADC08 CRC64; MNPYRLYLVT DDQQDLATLK YVVQQAIEGG VTMVQVREKH GDVRAFIERA KAVKTILKQT DVPLIINDRV DVALAVDADG VHLGQSDMPA SVARALIGPD KLLGLSIENE QQLAEADSLP IDYIGLSAIF ATPTKTNTKK HWGIEGLQLA LSRTSLPIVA IGGINQDNIP QLCATGVQGL ALVSAICHAD DPKSAARYLR QLMN // ID E8MCI3_9VIBR Unreviewed; 471 AA. AC E8MCI3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=VISI1226_18796; OS Vibrio sinaloensis DSM 21326. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=945550; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 21326; RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0; RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., RA Naum M., McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.; RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge RT Scleritoderma cyanea."; RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVT01000108; EGA68351.1; -; Genomic_DNA. DR EnsemblBacteria; EGA68351; EGA68351; VISI1226_18796. DR PATRIC; 46720650; VBIVibSin177761_4068. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 471 AA; 52581 MW; 6DFDD9087D16ECC4 CRC64; MSKILIPSSL IELTGLVQHC LLLAKEQGFS IEDIELGVSP TQSIQLVRDQ QTTRITTDLI DGYDSEHESS FVLYYRSALS VEACAKQPSK AIYIGIADTQ VSDEKEKGRQ LDIWRHPISD EVRALSVESK LNAMFDTEHH LAWIVTLTVL DFPIEDALTL ARGMLIQQAN VSRETRLGVK LTDGEHTQWA DQFDDFPTPV LEDSRLGIKV GWSAQGESVS FPTLTKQSLG LYPVVDDVAW IERLLPLGIN TIQLRIKNPQ QADLEQQIIR AIELGRQYQA QVFINDYWQL AIKHGAYGVH LGQEDIEESN LAQLTKAGIR LGLSTHGYYE LLRIVQIHPS YIALGHIFPT TTKQMPSKPQ GLVRLALYQK LIDSIPYTNT EAAFRPAKDE AVSDYVLGFP TVAIGGIDQS NADQVWQTGV SSLAVVRAIT LAESPQSVIE FFAQLMKERQ LTFTDQNSKL AHTKRGEHAH G // ID E8ME72_BIFL2 Unreviewed; 917 AA. AC E8ME72; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE SubName: Full=Thiamine biosynthesis protein; GN OrderedLocusNames=BLLJ_1332; OS Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / OS JCM 1217 / NCTC 11818 / E194b). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=565042; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b; RX PubMed=21270894; DOI=10.1038/nature09646; RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., RA Tobe T., Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., RA Kikuchi J., Morita H., Hattori M., Ohno H.; RT "Bifidobacteria can protect from enteropathogenic infection through RT production of acetate."; RL Nature 469:543-547(2011). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010888; BAJ66999.1; -; Genomic_DNA. DR RefSeq; YP_004221091.1; NC_015067.1. DR ProteinModelPortal; E8ME72; -. DR EnsemblBacteria; BAJ66999; BAJ66999; BLLJ_1332. DR GeneID; 10210095; -. DR KEGG; blm:BLLJ_1332; -. DR PATRIC; 46891115; VBIBifLon48544_1382. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR OMA; INTICSA; -. DR BioCyc; BLON565042:GIWN-1386-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100355 MW; 00000DA28A98E1F6 CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLADTKA AGWFVVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID E8MUS2_BIFL1 Unreviewed; 917 AA. AC E8MUS2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE SubName: Full=Thiamine biosynthesis protein; GN OrderedLocusNames=BLIF_1377; OS Bifidobacterium longum subsp. infantis (strain 157F). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=565040; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=157F; RX PubMed=21270894; DOI=10.1038/nature09646; RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., RA Tobe T., Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., RA Kikuchi J., Morita H., Hattori M., Ohno H.; RT "Bifidobacteria can protect from enteropathogenic infection through RT production of acetate."; RL Nature 469:543-547(2011). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010890; BAJ71516.1; -; Genomic_DNA. DR RefSeq; YP_004209294.1; NC_015052.1. DR EnsemblBacteria; BAJ71516; BAJ71516; BLIF_1377. DR GeneID; 10208063; -. DR KEGG; blf:BLIF_1377; -. DR PATRIC; 46886832; VBIBifLon182273_1411. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR OMA; INTICSA; -. DR BioCyc; BLON565040:GHFW-1413-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100297 MW; 76CDE68E4C1C32F8 CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLAGTKA AGWFVVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID E8NCI6_MICTS Unreviewed; 211 AA. AC E8NCI6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MTES_1891; OS Microbacterium testaceum (strain StLB037). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Microbacteriaceae; Microbacterium. OX NCBI_TaxID=979556; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=StLB037; RX PubMed=21357489; DOI=10.1128/JB.00180-11; RA Morohoshi T., Wang W.-Z., Someya N., Ikeda T.; RT "Genome sequence of Microbacterium testaceum StLB037, an N- RT acylhomoserine lactone-degrading bacterium isolated from potato RT leaves."; RL J. Bacteriol. 193:2072-2073(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=StLB037; RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.; RT "Genome sequence of Microbacterium testaceum StLB037."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012052; BAJ74855.1; -; Genomic_DNA. DR RefSeq; YP_004224735.1; NC_015125.1. DR EnsemblBacteria; BAJ74855; BAJ74855; MTES_1891. DR GeneID; 10218711; -. DR KEGG; mts:MTES_1891; -. DR PATRIC; 46970840; VBIMicTes185510_1865. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; MTES979556:GJFH-2837-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21378 MW; 623579C6E445E586 CRC64; MTDLSLHLVT DHRVPFSRLR DIVDAAVGAG VTVVQLRDKL ASGGELFART LDLADVVAGR CTFVVDDRLD IVLAARDRGA RVDGIHLGQS DLPVDAARAL LGPDALVGWT ANTPAHLAAA AAFPEGTVDY LGVGVIRATA TKPDHPQPLG VDGFAELAAS TALPCVAIGG IGVDDVAALR RAGAAGVAVV SAVCAADDPG AVVRELRAAA A // ID E8NTU8_SALET Unreviewed; 211 AA. AC E8NTU8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SCA50_4320; OS Salmonella enterica subsp. enterica serovar Choleraesuis str. SCSA50. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=904139; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A50; RX PubMed=21478351; DOI=10.1128/JB.00394-11; RA Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S., RA Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.; RT "Genome sequences of Salmonella enterica serovar typhimurium, RT Choleraesuis, Dublin, and Gallinarum strains of well- defined RT virulence in food-producing animals."; RL J. Bacteriol. 193:3162-3163(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001062; EFZ08682.1; -; Genomic_DNA. DR ProteinModelPortal; E8NTU8; -. DR EnsemblBacteria; EFZ08682; EFZ08682; SCA50_4320. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22950 MW; 088AE10486472682 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE VGVRTIQLRI KDKRNEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSVAVVSAIT QAADWREATA QLLAIVGVGD E // ID E8P949_ACIB1 Unreviewed; 203 AA. AC E8P949; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ABK1_2795; OS Acinetobacter baumannii (strain 1656-2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=696749; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1656-2; RA Kim J., Kim S.-H., Kim S.-M., Park J.-Y., Lee H.-W., Shin J.-H.; RT "Complete genome sequence of multidrug-resistant Acinetobacter RT baumannii, a master of both adherence and biofilm formation."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001921; ADX04429.1; -; Genomic_DNA. DR RefSeq; YP_005515367.1; NC_017162.1. DR ProteinModelPortal; E8P949; -. DR EnsemblBacteria; ADX04429; ADX04429; ABK1_2795. DR GeneID; 12102332; -. DR KEGG; abx:ABK1_2795; -. DR PATRIC; 47067548; VBIAciBau150852_2824. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; ABAU696749:GL7T-2846-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21778 MW; F47FCEF0DAC9A9AE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKID KAEQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID E8PGV0_ACIB1 Unreviewed; 299 AA. AC E8PGV0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=ABK1_1203; OS Acinetobacter baumannii (strain 1656-2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=696749; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1656-2; RA Kim J., Kim S.-H., Kim S.-M., Park J.-Y., Lee H.-W., Shin J.-H.; RT "Complete genome sequence of multidrug-resistant Acinetobacter RT baumannii, a master of both adherence and biofilm formation."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001921; ADX02837.1; -; Genomic_DNA. DR RefSeq; YP_005513775.1; NC_017162.1. DR ProteinModelPortal; E8PGV0; -. DR EnsemblBacteria; ADX02837; ADX02837; ABK1_1203. DR GeneID; 12104533; -. DR KEGG; abx:ABK1_1203; -. DR PATRIC; 47064295; VBIAciBau150852_1223. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; ABAU696749:GL7T-1243-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 299 AA; 34203 MW; 49BD9DC168F2FC57 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLNPELK KQIKTVHLKQ SQLMSLHKGD LEVGVRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID E8PQE1_THESS Unreviewed; 206 AA. AC E8PQE1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TSC_c11800; OS Thermus scotoductus (strain ATCC 700910 / SA-01). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=743525; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700910 / SA-01; RA Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R., RA Gottschalk G., van Heerden E., Litthauer D.; RT "The genome sequence of Thermus scotoductus SA-01."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001962; ADW21800.1; -; Genomic_DNA. DR RefSeq; YP_004202349.1; NC_014974.1. DR ProteinModelPortal; E8PQE1; -. DR EnsemblBacteria; ADW21800; ADW21800; TSC_c11800. DR GeneID; 10177301; -. DR KEGG; tsc:TSC_c11800; -. DR PATRIC; 47045208; VBITheSco147128_1141. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; TSCO743525:GCD4-1179-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22710 MW; 0B20C14CE4FB4E19 CRC64; MLGRLYLVVT PRPGWSMAEV LDRTERALAG GVEVVQLRAK DWEARPILDL GKRMLALARR YGVPFFLNDR PDLAALLGAD GVHLGQGDLT PAEARRFFQG MVGRSTHAPE QALRALEEGV DYLSIGPVWE TPTKPGRQAA GLGYVRWARE NLGERPWYAI GGITLENLGE VLEAGARRVV VVRAILDAEN PERAAQAFRE RLYGVA // ID E8QFG5_HELP7 Unreviewed; 219 AA. AC E8QFG5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPIN_02385; OS Helicobacter pylori (strain India7). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=907238; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=India7; RA Kersulyte D., Mukhopadhyay A., Choudhury A., Nair G.B., Berg D.E.; RT "Genome sequence of Helicobacter pylori strain India7."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002331; ADU79727.1; -; Genomic_DNA. DR RefSeq; YP_005781812.1; NC_017372.1. DR EnsemblBacteria; ADU79727; ADU79727; HPIN_02385. DR GeneID; 12361931; -. DR KEGG; hpn:HPIN_02385; -. DR PATRIC; 45421649; VBIHelPyl171055_0475. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; HPYL907238:GLEI-479-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24078 MW; C5609E42EB9A2EFB CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDTLELAL ESQITAFQFR QKGDLALQDP VEIKRLALEC QKLCQKYSVP FIVNDEVQLA LELKADGVHV GQEDMAIEEV VTLCQKRLFI GLSVNTLEQA LKARHLDAVA YFGVGPIFPT QSKKDKQVVG VELLKKIKDS GVKKPLIAIG GITMHNASKL REYGGIAVIS AITQARDKAL VIGKLLNDA // ID E8QHU4_HELP4 Unreviewed; 217 AA. AC E8QHU4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPGAM_04360; OS Helicobacter pylori (strain Gambia94/24). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=907240; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Gambia94/24; RA Kersulyte D., Secka O., Thomas J.E., Adegbola R., Berg D.E.; RT "Genome sequence of Helicobacter pylori strain Gambia94/24."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002332; ADU81691.1; -; Genomic_DNA. DR RefSeq; YP_005780572.1; NC_017371.1. DR EnsemblBacteria; ADU81691; ADU81691; HPGAM_04360. DR GeneID; 12360650; -. DR KEGG; heg:HPGAM_04360; -. DR PATRIC; 45483086; VBIHelPyl173289_0873. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; HPYL907240:GLEG-845-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23807 MW; D64D4E96FA76F17B CRC64; MFDANCLKLM FVAGSQDFYH IKGDRINALL DTLELALQSK ITAFQFRQKG DLALQDPVEI KRLALECQKL CQKYGAPFII NDEVRLALEL KADGVHVGQE DMAIEEIVTL CQKRLFIGLS VNTLEQALKA RRLDSVCYLG VGPIFPTPSK KDAKEVVGVE LLKKIHDSGV KKPLIAIGGI TTDNASKLQK FSGIAVISAI TQAKDKALAV EKLLKNA // ID E8QPX8_HELPR Unreviewed; 220 AA. AC E8QPX8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPLT_04270; OS Helicobacter pylori (strain Lithuania75). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=907237; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lithuania75; RA Kersulyte D., Kupcinskas L., Chalkauskas H., Kiuduliene L., RA Janulaitis A., Berg D.E.; RT "Genome sequence of Helicobacter pylori strain Lithuania75."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002334; ADU83260.1; -; Genomic_DNA. DR RefSeq; YP_005772975.1; NC_017362.1. DR EnsemblBacteria; ADU83260; ADU83260; HPLT_04270. DR GeneID; 12351824; -. DR KEGG; hph:HPLT_04270; -. DR PATRIC; 45454985; VBIHelPyl170489_0858. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; HPYL907237:GLEJ-809-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24025 MW; 95E0848A6E946F1B CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDTLELAL QSQITAFQFR QKGDLALQDP TQIKQLALEC QKLCQKYGAP FIVNDEVRLA LELKADGVHV GQEDMAIEEV ITLCKKRQFI GLSVNTLEQA LKARHLDAVA YLGVGPIFPT PSKKDAKEVV GVELLKKIRD SGVKKPLIAI GGITTHNASK LREYGGIAVI SAITQAKDKA LVIGKLLNNA // ID E8QS45_HELPW Unreviewed; 220 AA. AC E8QS45; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPSA_04100; OS Helicobacter pylori (strain SouthAfrica7). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=907239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SouthAfrica7; RA Kersulyte D., Segal I., Mistry R., Berg D.E.; RT "Genome sequence of Helicobacter pylori strain SouthAfrica7."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002336; ADU84809.1; -; Genomic_DNA. DR RefSeq; YP_005771416.1; NC_017361.1. DR EnsemblBacteria; ADU84809; ADU84809; HPSA_04100. DR GeneID; 12349729; -. DR KEGG; hes:HPSA_04100; -. DR PATRIC; 45399977; VBIHelPyl171460_0833. DR KO; K00788; -. DR BioCyc; HPYL907239:GLES-793-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24178 MW; CD416F1800AEF692 CRC64; MFDANGLKLM FVAGSQDFYH IKGDRINALL DTLKLALQSK ITAFQFRQKG DLALQDPTQI KQLALECQKL CKKYGVPFIV NDEVQLALEL KADGVHVGQE DMAIEKVIAL CKKRLFIGLS VNTLEQALKA RHLDNIAYLG VGPIFPTPSK KDAKQVVGIE LLKKIQDSGV KKPLVAIGGI TTDNASKIQK FSGIAVISAI TQAKDKSLAI ETLLKMREKF // ID E8R1P8_ISOPI Unreviewed; 545 AA. AC E8R1P8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Isop_2901; OS Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Isosphaera. OX NCBI_TaxID=575540; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43644; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders E., RA Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Eisen J.A.; RT "The complete sequence of chromosome of Isophaera pallida ATCC RT 43644."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43644 / DSM 9630 / IS1B; RX PubMed=21475588; DOI=10.4056/sigs.1533840; RG US DOE Joint Genome Institute (JGI-PGF); RA Goker M., Cleland D., Saunders E., Lapidus A., Nolan M., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Detter J.C., Beck B., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Isosphaera pallida type strain (IS1B)."; RL Stand. Genomic Sci. 4:63-71(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002353; ADV63466.1; -; Genomic_DNA. DR RefSeq; YP_004180015.1; NC_014962.1. DR EnsemblBacteria; ADV63466; ADV63466; Isop_2901. DR GeneID; 10157044; -. DR KEGG; ipa:Isop_2901; -. DR PATRIC; 46960542; VBIIsoPal14453_3741. DR KO; K00788; -. DR BioCyc; IPAL575540:GI5T-2945-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0019538; P:protein metabolic process; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.1780.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004176; Clp_N. DR InterPro; IPR023150; Dbl_Clp-N. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02861; Clp_N; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 545 AA; 59475 MW; 3E1293F772B68E11 CRC64; MRDALTPAAQ RLVDQAHRRA QARSSPLTEP GDLLAALADQ PESKAGELLA DHGLRAEELL SALGFSVANS DRVGPDESVA EPNVVPGEPP RDAEAPGKPT NEPPDSLDFR AVLNEARSIA RRWDRNHPVS SEHLLLALVE YSLPLRTLLV RAGVQVEALV EAIRTLIHED IGPIEVEDEP FRLDLGDAAD DHELARILDA SGNRAREALR VIEDYVRFAL DDPMLTRRLK DVRHRLSQAL AGLDDQTLLA ARDTPGDVGT HIMTPEERLR EHPRAVLTAN FKRLGEALRT LEEYCKIRNV WLSGRFEVLR YDVYTLEKMV ATAIRSQRGL GKARLYLLVG GLPTLGDLTW VVGEALEGGV DVVQLREKGV EDRVWLERAR EVRLLTARAG ATFVVNDRCD LARLAGADGV HLGQTDLTVR DARRLLGGAP LIGVSTHDPS QIRRAVLDAA NYLGVGPVFP SGTKSFDSSE IVGLGLVRHA AETTTLPWFA LGGIDESNLD DVLEAGARRV AVSGALLRAG SPRKVARSLK DRLEQAVAIS SDEED // ID E8RE08_DESPD Unreviewed; 218 AA. AC E8RE08; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Despr_1881; OS Desulfobulbus propionicus (strain ATCC 33891 / DSM 2032 / 1pr3). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfobulbus. OX NCBI_TaxID=577650; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33891 / DSM 2032 / 1pr3; RX PubMed=21475592; RA Pagani I., Lapidus A., Nolan M., Lucas S., Hammon N., Deshpande S., RA Cheng J.F., Chertkov O., Davenport K., Tapia R., Han C., Goodwin L., RA Pitluck S., Liolios K., Mavromatis K., Ivanova N., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Detter J.C., Brambilla E., Kannan K.P., Djao O.D., RA Rohde M., Pukall R., Spring S., Goker M., Sikorski J., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Desulfobulbus propionicus type strain RT (1pr3)."; RL Stand. Genomic Sci. 4:100-110(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002364; ADW18029.1; -; Genomic_DNA. DR RefSeq; YP_004195320.1; NC_014972.1. DR ProteinModelPortal; E8RE08; -. DR EnsemblBacteria; ADW18029; ADW18029; Despr_1881. DR GeneID; 10174608; -. DR KEGG; dpr:Despr_1881; -. DR PATRIC; 46937359; VBIDesPro114934_1998. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; DPRO577650:GH80-1909-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 22597 MW; EABA4C06908B7EC5 CRC64; MIDYSLYLVT DRHLSLGRDT VDIVQAAIRG GITCVQLREK HGSTRQFIEE ARQVRNLLDC LASTIPLIIN DRVDVALATG ADGVHLGQRD MDIRDARRLA GSSLLIGISV ESVDDAVRAE AEGADYVGVS PVFATPTKSD TAPPLGLAGI QAIRAAVSLP LVAIGGINAD NAAAIIRAGA DGVAVVSAIV SAACPAQAAR TLKEQISSVK GGGRHGNQ // ID E8REK0_DESPD Unreviewed; 216 AA. AC E8REK0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Despr_1928; OS Desulfobulbus propionicus (strain ATCC 33891 / DSM 2032 / 1pr3). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfobulbus. OX NCBI_TaxID=577650; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33891 / DSM 2032 / 1pr3; RX PubMed=21475592; RA Pagani I., Lapidus A., Nolan M., Lucas S., Hammon N., Deshpande S., RA Cheng J.F., Chertkov O., Davenport K., Tapia R., Han C., Goodwin L., RA Pitluck S., Liolios K., Mavromatis K., Ivanova N., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Detter J.C., Brambilla E., Kannan K.P., Djao O.D., RA Rohde M., Pukall R., Spring S., Goker M., Sikorski J., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Desulfobulbus propionicus type strain RT (1pr3)."; RL Stand. Genomic Sci. 4:100-110(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002364; ADW18076.1; -; Genomic_DNA. DR RefSeq; YP_004195367.1; NC_014972.1. DR EnsemblBacteria; ADW18076; ADW18076; Despr_1928. DR GeneID; 10174656; -. DR KEGG; dpr:Despr_1928; -. DR PATRIC; 46937459; VBIDesPro114934_2048. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR BioCyc; DPRO577650:GH80-1957-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23113 MW; C2D931E0385040D7 CRC64; MKHSKPLFPA GIYGITAEKF SAGRTNIEVA QQMIRGGIRL IQYREKRPHK SFAEMLAECR AIRAMTRDAG VLFIVNDYPD IAQLVDADGV HVGQDDFPVP EVRRLIGPHK LIGLSTHGPE QAAAALAAGA DYIGVGPIFS TQTKEDVCAP VGLGYLEHVV RSCPLPFVAI GGIKEHNLHE VVARGAKTVC LVTEIVGATD IAATARRLQA ACSAPL // ID E8RNK1_ASTEC Unreviewed; 191 AA. AC E8RNK1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Astex_0131; OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / VKM B-1370 / OS CB 48). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Asticcacaulis. OX NCBI_TaxID=573065; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15261 / DSM 4724 / VKM B-1370 / CB 48; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., RA Ovchinnikova G., Brun Y.V., Woyke T.; RT "Complete sequence of chromosome 1 of Asticcacaulis excentricus CB RT 48."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002395; ADU11832.1; -; Genomic_DNA. DR RefSeq; YP_004085983.1; NC_014816.1. DR ProteinModelPortal; E8RNK1; -. DR EnsemblBacteria; ADU11832; ADU11832; Astex_0131. DR GeneID; 10051680; -. DR KEGG; aex:Astex_0131; -. DR PATRIC; 45148226; VBIAstExc23432_0125. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; AEXC573065:GJ7A-131-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 191 AA; 20079 MW; 9B8C94336F9D8868 CRC64; MSSANGRELP ALFYVTDPKR TPHPEEIVAH LPAGAGVIYR HFGDPHATAH ARVLRTLCDD NGLKLLIGQD VALAEDVAAD GVHLPERALS NAPDVRERHR EWLITGACHG CETLDLAEVT ALDGLFISPV FASHSPSAKG VAPLGLKGIQ MFCDLSPVPV LGLGGIGADN AEQLTHSGLA GFGAVEAFQL N // ID E8RR61_ASTEC Unreviewed; 205 AA. AC E8RR61; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Astex_1713; OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / VKM B-1370 / OS CB 48). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Asticcacaulis. OX NCBI_TaxID=573065; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15261 / DSM 4724 / VKM B-1370 / CB 48; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., RA Ovchinnikova G., Brun Y.V., Woyke T.; RT "Complete sequence of chromosome 1 of Asticcacaulis excentricus CB RT 48."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002395; ADU13379.1; -; Genomic_DNA. DR RefSeq; YP_004087530.1; NC_014816.1. DR ProteinModelPortal; E8RR61; -. DR EnsemblBacteria; ADU13379; ADU13379; Astex_1713. DR GeneID; 10053284; -. DR KEGG; aex:Astex_1713; -. DR PATRIC; 45151386; VBIAstExc23432_1682. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; AEXC573065:GJ7A-1735-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21680 MW; 731349BC06BE0906 CRC64; MTSQLYLITP PSITDHAAFA RALDDALSAG PVPALQIRLK DVSLDEIRAL TRLISPIAHR HGTAVLMNDH VDLARELRLD GVHVGQSDMS YKDARKRLGT EAMIGVTCHN SRHLAMEAAE AGADYVAFGA FYPTATKTVE HMAELDTLTI WQETMEVPCV AIGGITAANA AEVSAAGADF IAVSGAVWTH PDGPAAGVRA LLSAI // ID E8SAM4_MICSL Unreviewed; 520 AA. AC E8SAM4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE SubName: Full=Phosphomethylpyrimidine kinase; GN OrderedLocusNames=ML5_0576; OS Micromonospora sp. (strain L5). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Micromonospora. OX NCBI_TaxID=648999; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., RA De Hoff P.L., Hirsch A.M., Woyke T.; RT "Complete sequence of Micromonospora sp. L5."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002399; ADU06126.1; -; Genomic_DNA. DR RefSeq; YP_004080277.1; NC_014815.1. DR ProteinModelPortal; E8SAM4; -. DR EnsemblBacteria; ADU06126; ADU06126; ML5_0576. DR GeneID; 10056059; -. DR KEGG; mil:ML5_0576; -. DR PATRIC; 45268978; VBIMicSp154089_0593. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OMA; YLAQGEP; -. DR BioCyc; MSP648999:GHVN-585-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:InterPro. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 520 AA; 52914 MW; F657EC4F0FFC01A4 CRC64; MTALRVADPG TEAPLEGRPR TRIYTGPTGV VLLTDRRVAK GALVDVVAGA VGGGVRWVVL REKDLPRAER LALAVELRAI LAEAGGTLVV AGPDPLDGDA VHLPAAGPYP PPAVGLVGRS CHDTAELARL TTEHYATLSP VYETRTKPGY GPALRPTGLR ELIAASKVPV LALGGIETTA QVTACVEAGA TGVAVLGAIM RAPDPTETAT TLGRAFEEAA TRVARTHPAR SDQGPHAAAP TATTVGRSRH SNHRRREPVT PKTVLSIAGS DSGAGAGIQA DLKTFAALGA YGTSVLTAVT AQSTRGVDAL LPLPPQTVRD QMDSVLGDFD VRAVKTGMLG TPAVADAVAE AARAGRLPHL VVDPVLVATS GHRLGVVEAV ERLLPYAEVA TPNCAEAAAL TGGPVGTVEE MVAAAEALAA RGPAFVVVTG GDVDADGESV DVLAGGGTTR LLRAPRVDTR HNHGTGCSFS AAVAVRLAAG DAVPVAVAAA KEYVTRALTG ARTWELGAGR GPLDHFGWSA // ID E8SAM8_MICSL Unreviewed; 208 AA. AC E8SAM8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ML5_0580; OS Micromonospora sp. (strain L5). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Micromonospora. OX NCBI_TaxID=648999; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., RA De Hoff P.L., Hirsch A.M., Woyke T.; RT "Complete sequence of Micromonospora sp. L5."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002399; ADU06130.1; -; Genomic_DNA. DR RefSeq; YP_004080281.1; NC_014815.1. DR ProteinModelPortal; E8SAM8; -. DR EnsemblBacteria; ADU06130; ADU06130; ML5_0580. DR GeneID; 10056063; -. DR KEGG; mil:ML5_0580; -. DR PATRIC; 45268987; VBIMicSp154089_0597. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR BioCyc; MSP648999:GHVN-589-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 20826 MW; 29F71EB2306CF80B CRC64; MLSLGRLHLI TDTRPGRDPL AVLRAALPVA GAELVVQVRV EDDATDREAY ELACRVTEAC RPYGAQFLVN DRLHVALAVD AAGGHVGADD LPVAAARRVL GPDAVLGATA RGPVGARTAV DAGASYLGVG PCHVTTTKSG LPDPIGPEGI RAVAEAVSVP VIAIGGVTAA SVPALRAAGA YGVAVVGALS LAADPAHATA ELLRALTC // ID E8SJV6_STAPH Unreviewed; 196 AA. AC E8SJV6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=SPSINT_0375; OS Staphylococcus pseudintermedius (strain HKU10-03). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=937773; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HKU10-03; RA Tse H., Tsoi H.W., Leung S.P., Urquhart I.J., Lau S.K.P., Woo P.C.Y., RA Yuen K.Y.; RT "Complete genome sequence of Staphylococcus pseudintermedius."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HKU10-03; RX PubMed=21278300; DOI=10.1128/JB.00023-11; RA Tse H., Tsoi H.W., Leung S.P., Urquhart I.J., Lau S.K., Woo P.C., RA Yuen K.Y.; RT "Complete genome sequence of the veterinary pathogen Staphylococcus RT pseudintermedius strain HKU10-03, isolated in a case of canine RT pyoderma."; RL J. Bacteriol. 193:1783-1784(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002439; ADV04904.1; -; Genomic_DNA. DR RefSeq; YP_004148540.1; NC_014925.1. DR EnsemblBacteria; ADV04904; ADV04904; SPSINT_0375. DR GeneID; 10135134; -. DR KEGG; ssd:SPSINT_0375; -. DR PATRIC; 45363935; VBIStaPse177932_0374. DR HOGENOM; HOG000090085; -. DR KO; K10810; -. DR BioCyc; SPSE937773:GH0P-395-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 196 AA; 22044 MW; 51AF319353B92774 CRC64; MMIVITPYVV LDDWHIKRLC VIESQIAGVI LRTPMNRHAL KQWLIQLLAN GFPKSKVIIH TDVTLAMELS ISNVHFKEGD HRATLLKQVQ PHYQVSMSTH SAAMVRDAKA QQLDFVLFGH LFPTSSKPDL PPRTQLEVDE VLAIDFPVVA LGGITADTVQ QISSHFTGIA CMSSAFGYEL QSFEKMVDYW SLKKVK // ID E8SKM7_STAPH Unreviewed; 212 AA. AC E8SKM7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPSINT_1754; OS Staphylococcus pseudintermedius (strain HKU10-03). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=937773; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HKU10-03; RA Tse H., Tsoi H.W., Leung S.P., Urquhart I.J., Lau S.K.P., Woo P.C.Y., RA Yuen K.Y.; RT "Complete genome sequence of Staphylococcus pseudintermedius."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HKU10-03; RX PubMed=21278300; DOI=10.1128/JB.00023-11; RA Tse H., Tsoi H.W., Leung S.P., Urquhart I.J., Lau S.K., Woo P.C., RA Yuen K.Y.; RT "Complete genome sequence of the veterinary pathogen Staphylococcus RT pseudintermedius strain HKU10-03, isolated in a case of canine RT pyoderma."; RL J. Bacteriol. 193:1783-1784(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002439; ADV06282.1; -; Genomic_DNA. DR RefSeq; YP_004149918.1; NC_014925.1. DR EnsemblBacteria; ADV06282; ADV06282; SPSINT_1754. DR GeneID; 10136561; -. DR KEGG; ssd:SPSINT_1754; -. DR PATRIC; 45366794; VBIStaPse177932_1753. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; SPSE937773:GH0P-1822-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23640 MW; 619F0627042FA122 CRC64; MTFNRKQLRV YFIAGTQDVK QGSLDGILKE ALEAGITMYQ FREKGSSSLQ GEEKTAMAVR LRDLCRHYQV PFIVNDDVDL AIEIDADGIH VGQEDAKVQS FQHLLEDKII GLSVGSFEEY DQSDLTNVDY IGVGPVYETS SKLDASKPGG IRLIRRMREY DENIPMVAIG GITEENVAPL LKNGADGIAT ISSITHSTDI EKSVKRYLQY FK // ID E8SMR7_NEIGO Unreviewed; 205 AA. AC E8SMR7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NGTW08_1791; OS Neisseria gonorrhoeae TCDC-NG08107. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=940296; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TCDC-NG08107; RA Chen C.-C., Hsia K.-C., Huang C.-T., Wong W.-W., Yen M.-Y., Li L.-H., RA Lin K.-Y., Chen K.-W., Li S.-Y.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TCDC-NG08107; RX PubMed=21257765; DOI=10.1128/JB.00007-11; RA Chen C.C., Hsia K.C., Huang C.T., Wong W.W., Yen M.Y., Li L.H., RA Lin K.Y., Chen K.W., Li S.Y.; RT "Draft genome sequence of a dominant, multidrug-resistant Neisseria RT gonorrhoeae strain, TCDC-NG08107, from a sexual group at high risk of RT acquiring human immunodeficiency virus infection and syphilis."; RL J. Bacteriol. 193:1788-1789(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002440; ADV08746.1; -; Genomic_DNA. DR RefSeq; YP_005890609.1; NC_017511.1. DR ProteinModelPortal; E8SMR7; -. DR EnsemblBacteria; ADV08746; ADV08746; NGTW08_1791. DR GeneID; 12407096; -. DR KEGG; ngt:NGTW08_1791; -. DR PATRIC; 45473449; VBINeiGon174987_2219. DR KO; K00788; -. DR BioCyc; NGON940296:GLHN-1809-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21779 MW; 1353772F6A7897A9 CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP GYIASGAIFQ TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID E8SS81_GEOS2 Unreviewed; 221 AA. AC E8SS81; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GYMC52_1474; OS Geobacillus sp. (strain Y412MC52). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=550542; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y412MC52; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Mead D., Woyke T.; RT "Complete sequence of chromosome of Geobacillus sp. Y412MC52."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002442; ADU93924.1; -; Genomic_DNA. DR RefSeq; YP_004132067.1; NC_014915.1. DR ProteinModelPortal; E8SS81; -. DR EnsemblBacteria; ADU93924; ADU93924; GYMC52_1474. DR GeneID; 10108153; -. DR KEGG; gya:GYMC52_1474; -. DR PATRIC; 45224419; VBIGeoSp94955_1575. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; GSP550542:GH52-1550-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23055 MW; 40DF21614BB8F035 CRC64; MARIASGEMK ERLAVYFIMG SQNSERPAAD VLKEALDGGV TLFQFREKGP GALKGADKEE LARQLQHLCR AYGVPFIVND DVELALAIDA DGVHVGQDDE DARRVREKIG DKILGVSAHN VEEAMAAVEA GADYLGVGPI YPTSSKEDAK EAQGPDVLRR LREAGITIPI VAIGGITAAN AKTVVEAGAD GVSVISAIAS APSPKAAAAA LAEAVRAART R // ID E8SUJ9_GEOS2 Unreviewed; 201 AA. AC E8SUJ9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=GYMC52_0535; OS Geobacillus sp. (strain Y412MC52). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=550542; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y412MC52; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Mead D., Woyke T.; RT "Complete sequence of chromosome of Geobacillus sp. Y412MC52."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002442; ADU93030.1; -; Genomic_DNA. DR RefSeq; YP_004131173.1; NC_014915.1. DR ProteinModelPortal; E8SUJ9; -. DR EnsemblBacteria; ADU93030; ADU93030; GYMC52_0535. DR GeneID; 10107212; -. DR KEGG; gya:GYMC52_0535; -. DR PATRIC; 45222388; VBIGeoSp94955_0571. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR BioCyc; GSP550542:GH52-609-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 21097 MW; FA3CD957E8611004 CRC64; MGVLHFVSTG RQTVDEFAAI CAHTHPYADL IHIREKGKTA REVAAFVAAL LRVGVPPQKI IVNDRVDVAA VYGVKGVQLA YHSLPVRAVR RSFPDLTVGC SVHGSEEAKQ AEQDGAHFCL YGHIFPTDSK PGLPPRGLDS LAEIVAAVSI PVIAIGGIHA GNARRVLEAG AAGVAVLSAV FFAADPVAEA KRLADIVKGR G // ID E8T5Y1_THEA1 Unreviewed; 214 AA. AC E8T5Y1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Theam_0593; OS Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1). OC Bacteria; Aquificae; Aquificales; Desulfurobacteriaceae; Thermovibrio. OX NCBI_TaxID=648996; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15698 / JCM 12110 / HB-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Vetriani C., RA Woyke T.; RT "Complete sequence of chromosome of Thermovibrio ammonificans HB-1."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002444; ADU96565.1; -; Genomic_DNA. DR RefSeq; YP_004151206.1; NC_014926.1. DR EnsemblBacteria; ADU96565; ADU96565; Theam_0593. DR GeneID; 10125630; -. DR KEGG; tam:Theam_0593; -. DR PATRIC; 45383508; VBITheAmm13058_0688. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; TAMM648996:GI3X-612-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23654 MW; 642500EFEE93C4E2 CRC64; MVEFPPETPF LYGITDERFL NPFNIVEAVE RAILGGAKVI QYRAKRKSAR EMYEEALLVR EATRNHDAVF IVNDRLDLAL AVEADGVHLG QSDLPFELVK GIAGEEFIVG LSTHNLEQVR EANEKKEFLD YIGFGPVFPT TTKENPDPVT GVELLCRAVE LSELPVVAIG GINPSNLEDV CRCKPAGVAV VRALFEKGDP FVNAREIKER LSGC // ID E8TMZ1_MESCW Unreviewed; 215 AA. AC E8TMZ1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Mesci_1273; OS Mesorhizobium ciceri bv. biserrulae (strain HAMBI 2942 / LMG 23838 / OS WSM1271). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=765698; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAMBI 2942 / LMG 23838 / WSM1271; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Nandasena K., Reeve W.G., RA Howieson J.G., O'Hara G., Tiwari R.P., Woyke T.; RT "Complete sequence of chromosome of Mesorhizobium ciceri bv. RT biserrulae WSM1271."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002447; ADV10434.1; -; Genomic_DNA. DR RefSeq; YP_004140484.1; NC_014923.1. DR EnsemblBacteria; ADV10434; ADV10434; Mesci_1273. DR GeneID; 10116722; -. DR KEGG; mci:Mesci_1273; -. DR PATRIC; 45252433; VBIMesCic160642_1710. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR BioCyc; MCIC765698:GHQ5-1283-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 215 AA; 22580 MW; 7E0F2F80AE966053 CRC64; MNEATPPNRC RIVLIAPPGV PAARIVTAFD GGDVASLILP ENGMDEASFQ AFAERIVPAA QAAGVAVIIA GDTRIAGRVQ ADGIHVEVSK AELAETIEHF QAKMMVGTGG AKTRDDALEL GETRPDYIFF GRFGYDNKPE PHPRNLSLGA WWADMIQIPC IVMAGSDIAS VEAVGATGAE FVALSSAVFA DGTDPRTAVA TANALLDETA PRFED // ID E8TWL0_ALIDB Unreviewed; 300 AA. AC E8TWL0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 11-DEC-2013, entry version 20. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Alide_1782; OS Alicycliphilus denitrificans (strain DSM 18852 / JCM 14587 / BC). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Alicycliphilus. OX NCBI_TaxID=596153; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 14587 / BC; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Daligault H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Oosterkamp M.J., RA Veuskens T., Weelink S.A., Plugge C.M., Stams A.J.M., Woyke T.; RT "Complete sequence of chromosome of Alicycliphilus denitrificans BC."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002449; ADU99533.1; -; Genomic_DNA. DR RefSeq; YP_004126421.1; NC_014910.1. DR ProteinModelPortal; E8TWL0; -. DR EnsemblBacteria; ADU99533; ADU99533; Alide_1782. DR GeneID; 10103829; -. DR KEGG; adn:Alide_1782; -. DR PATRIC; 45142338; VBIAliDen149934_1868. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; ADEN596153:GHGY-1807-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 300 AA; 31738 MW; EB00599BEE43CB1F CRC64; MHESHEAMVQ AIVHHHGAAY ADFPAQPVPA TATDEPVYRA ALAACSALGF IAHDAGCLAR AWAAQTRRLG SFDAARWPDD PADFGLQPRP HARPFAPCPQ QLGLYAVLPD AAWVGRMARA GVPTVQLRYK SQDGAAIARE VQAAVQAVRG TPALLFINDH WRAAIDAGAY GVHLGQEDLD ALGPDDLRAI REAGLRLGVS THGYAEMVRA DAASPSYIAM GAVFPTTLKK MATVPQGVAR LVAYARLMRG YPQVAIGGIG LEQFPQVLAT GVGSIAVVRA LVNADEPEAS AARLMRAMQA // ID E8U9W2_DEIML Unreviewed; 218 AA. AC E8U9W2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Precursor; GN Name=thiE; OrderedLocusNames=Deima_2211; OS Deinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 OS / LB-34). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=709986; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., RA Gehrich-Schroeter G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Deinococcus maricopensis DSM 21211."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002454; ADV67851.1; -; Genomic_DNA. DR RefSeq; YP_004171516.1; NC_014958.1. DR EnsemblBacteria; ADV67851; ADV67851; Deima_2211. DR GeneID; 10151572; -. DR KEGG; dmr:Deima_2211; -. DR PATRIC; 46925522; VBIDeiMar159729_2224. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; DMAR709986:GHZG-2263-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23171 MW; 39C64D8FA8872E4E CRC64; MTPFPLGRLY LVATPRDGQA EADFLARIAA ALDGGVDTLQ LRCKGWEAVP YIRLAERVRD LAHARRVPLF INDRVDVAVA SGATGVHLGQ ADLPTRWARD LAPALRIGRS THAPDHAEAA LADRPAYFAV GPVYATPTKP GRAPATLDYV RWAAAHAPED HTGVPWYAIG GIDHATAPDV IRAGATRLAV VRAILDAPDP AQAAGDLARL LDRPAVLA // ID E8UEV0_TAYEM Unreviewed; 209 AA. AC E8UEV0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TEQUI_0420; OS Taylorella equigenitalis (strain MCE9). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Taylorella. OX NCBI_TaxID=937774; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCE9; RX PubMed=21278298; DOI=10.1128/JB.01547-10; RA Hebert L., Moumen B., Duquesne F., Breuil M.F., Laugier C., RA Batto J.M., Renault P., Petry S.; RT "Genome sequence of Taylorella equigenitalis MCE9, the causative agent RT of contagious equine metritis."; RL J. Bacteriol. 193:1785-1785(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002456; ADU91364.1; -; Genomic_DNA. DR RefSeq; YP_004129507.1; NC_014914.1. DR EnsemblBacteria; ADU91364; ADU91364; TEQUI_0420. DR GeneID; 10114255; -. DR KEGG; teq:TEQUI_0420; -. DR PATRIC; 45374757; VBITayEqu178523_0403. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FQFRVKG; -. DR BioCyc; TEQU937774:GHXS-420-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23076 MW; 0B0C1AC97E7C39B0 CRC64; MFIPRGLYGI TPDWIEFSKV LQAVEIACDA GLPMLQFRRK IKEPSFERLK QCQAIKNICD KNNCVLIVND NLELARSCEA NGVHLGREDM DLLDAKLGEA LNSNNFIVGM SCYNELELAS KAVELGASYI AFGSMFPSPT KPNAVKANLD LIRRARKLFP VTPIVCIGGI TLDNAPYVIE AGADMLAVIS GLFEKEDIAT TIKEFNKLF // ID E8UFX6_TAYEM Unreviewed; 332 AA. AC E8UFX6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE SubName: Full=Mutator mutT protein; GN OrderedLocusNames=TEQUI_0802; OS Taylorella equigenitalis (strain MCE9). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Taylorella. OX NCBI_TaxID=937774; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCE9; RX PubMed=21278298; DOI=10.1128/JB.01547-10; RA Hebert L., Moumen B., Duquesne F., Breuil M.F., Laugier C., RA Batto J.M., Renault P., Petry S.; RT "Genome sequence of Taylorella equigenitalis MCE9, the causative agent RT of contagious equine metritis."; RL J. Bacteriol. 193:1785-1785(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002456; ADU91740.1; -; Genomic_DNA. DR RefSeq; YP_004129883.1; NC_014914.1. DR ProteinModelPortal; E8UFX6; -. DR EnsemblBacteria; ADU91740; ADU91740; TEQUI_0802. DR GeneID; 10114637; -. DR KEGG; teq:TEQUI_0802; -. DR PATRIC; 45375512; VBITayEqu178523_0774. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR BioCyc; TEQU937774:GHXS-802-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 332 AA; 37462 MW; 4433E684F18EB1F6 CRC64; MSEEKPFFDV SACVLVDSEG RFLMAQRPEG KSWSGWWEFP GGKIEEGETP KDATIRELRE ELGVDLDPES TYPWVTLSYE YPKTEVLLHF FRCYKWTGKL CSLENQAFEW FTEMPTDRDL LPASVEPIEW LGLGNVYLIS NFFEDALEIN SNIKPEETIF WGRLVKAIDA GVKLFQFREP KASRILKNED LKKYFDAMLE YCHLHGTKVL VNSCHPKTWA AQADGIHLRS ADALIMDIED APEKGLLAVS CHNMADLLYA HELGADFVVL GHVLETASHP NSEPLGWKKF EECACESAIP VFAIGGQSKE TLIEAFKHGA QGIAILRGGI IE // ID E8UN35_STREJ Unreviewed; 229 AA. AC E8UN35; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SSUJS14_0823; OS Streptococcus suis (strain JS14). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=945704; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS14; RX PubMed=21398551; DOI=10.1128/JB.00083-11; RA Hu P., Yang M., Zhang A., Wu J., Chen B., Hua Y., Yu J., Xiao J., RA Jin M.; RT "Complete genome sequence of Streptococcus suis serotype 14 strain RT JS14."; RL J. Bacteriol. 193:2375-2376(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JS14; RA Hu P., Yang M., Jin M., Xiao J.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002465; ADV69908.1; -; Genomic_DNA. DR RefSeq; YP_006076179.1; NC_017618.1. DR ProteinModelPortal; E8UN35; -. DR EnsemblBacteria; ADV69908; ADV69908; SSUJS14_0823. DR GeneID; 12722042; -. DR KEGG; sui:SSUJS14_0823; -. DR PATRIC; 45414118; VBIStrSui181850_0791. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SSUI945704:GLLM-866-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 24866 MW; 13EC09C5B3734B31 CRC64; MNRKMLQVYF ICGTSDCPKG KFLDVLEKAL QAGITCFQFR EKGEQGLTGA DKLLLAKQVQ HLCHRYQVPL IINDDVELAR AIDADGIHLG QEDLSVVEAR QLFPGKIIGL SVGTKEEYLN SPIDLVDYIG SGPVFPTLSK DDASPAIGMD GLKQLRKLNS DIPMVAIGGL SAKDCKEVLQ AGADGIAVIS AISHAEDPYK ATKILVDGMQ AMILKFNQVE SNKQILKNP // ID E8UVI7_THEBF Unreviewed; 211 AA. AC E8UVI7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Thebr_1695; OS Thermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389 OS / AKO-1) (Thermoanaerobacter finnii). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=509193; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43586 / DSM 3389 / AKO-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Hemme C.L., Woyke T.; RT "Complete sequence of Thermoanaerobacter brockii finnii Ako-1."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002466; ADV80239.1; -; Genomic_DNA. DR RefSeq; YP_004186622.1; NC_014964.1. DR ProteinModelPortal; E8UVI7; -. DR EnsemblBacteria; ADV80239; ADV80239; Thebr_1695. DR GeneID; 10163967; -. DR KEGG; tbo:Thebr_1695; -. DR PATRIC; 47041426; VBITheBro57020_1742. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; TBRO509193:GHWP-1741-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22990 MW; 437BC9C076A68280 CRC64; MDLTLYAITD RSYIKNMDIA EAVELAIKGG ATVIQLREKD ISSREFYEIA LKVKEVTKRN RIPLIINDRV DIALAVDADG VHVGQEDLPA DIVRKIIGRD KIVGVSARTV EEALKAQRDG ADYLGVGAVF KTPTKPEAEA IGIEGLKKIK EAVTIPVVAI GGITKDNAYE VMLKSGADGI SSVSAVFYGD IENNTRKLLE VIKKAINDRR I // ID E8UXF3_TERSS Unreviewed; 183 AA. AC E8UXF3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-MAR-2014, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=AciPR4_3423; OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Terriglobus. OX NCBI_TaxID=401053; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4; RX PubMed=23450133; DOI=10.4056/sigs.3036810; RA Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., RA Hauser L., Land M., Davenport K.W., Woyke T., Haggblom M.M.; RT "Complete genome sequence of Terriglobus saanensis type strain RT SP1PR4(T), an Acidobacteria from tundra soil."; RL Stand. Genomic Sci. 7:59-69(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002467; ADV84177.1; -; Genomic_DNA. DR RefSeq; YP_004184171.1; NC_014963.1. DR EnsemblBacteria; ADV84177; ADV84177; AciPR4_3423. DR GeneID; 10161355; -. DR KEGG; tsa:AciPR4_3423; -. DR PATRIC; 46832742; VBITerSaa54836_3550. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; TSAA401053:GHYY-3465-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 183 AA; 19228 MW; 047ADDEAA43480B3 CRC64; MIRYAISDRS QYPGDEQDRR AALVQQAERL SKAGVDFYQI REKDLGGSEL ILLLEAVLAA ARGVGKMKVL LNGSEEDARA AGADGVHLSS DRAGETITSG LVVSVACHSL EDVRRANANL RHFALFSPIF GKDSQDGVGL DALRSAAEIG EMSVLALGDV NEANAQACLG AGAAGIAGIR MFL // ID E8V7C9_TERSS Unreviewed; 218 AA. AC E8V7C9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-MAR-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AciPR4_2038; OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Terriglobus. OX NCBI_TaxID=401053; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4; RX PubMed=23450133; DOI=10.4056/sigs.3036810; RA Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., RA Hauser L., Land M., Davenport K.W., Woyke T., Haggblom M.M.; RT "Complete genome sequence of Terriglobus saanensis type strain RT SP1PR4(T), an Acidobacteria from tundra soil."; RL Stand. Genomic Sci. 7:59-69(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002467; ADV82842.1; -; Genomic_DNA. DR RefSeq; YP_004182836.1; NC_014963.1. DR EnsemblBacteria; ADV82842; ADV82842; AciPR4_2038. DR GeneID; 10159951; -. DR KEGG; tsa:AciPR4_2038; -. DR PATRIC; 46829852; VBITerSaa54836_2124. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; TSAA401053:GHYY-2061-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 52 56 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23040 MW; 269535125E1DC26F CRC64; MDEQSALWER VAQGTPIPRL YGVLDLMAVE GRGLDLFDVA KAWRDAGVKL VQYRDKLSPS MVMIAHAVRL AEIFRGTDTL LVLNDSPAMA RDAGLCAAHL GQTDGTVEAA RRAVPYIGVS TNTERQIRTA DGAACTYIAI GPVFETRTKV DAKSAVGLAG VRSARALTKK PLVAIGGIKL ENAASVLEAG ADSVAVISAL LEGGNPVTQA RAFLRIVE // ID E8VEP6_BACST Unreviewed; 222 AA. AC E8VEP6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-APR-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BSn5_10135; OS Bacillus subtilis (strain BSn5). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=936156; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSn5; RX PubMed=21317323; DOI=10.1128/JB.00129-11; RA Deng Y., Zhu Y., Wang P., Zhu L., Zheng J., Li R., Ruan L., Peng D., RA Sun M.; RT "Complete genome sequence of Bacillus subtilis BSn5, an endophytic RT bacterium of Amorphophallus konjac with antimicrobial activity for the RT plant pathogen Erwinia carotovora subsp. carotovora."; RL J. Bacteriol. 193:2070-2071(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSn5; RA Deng Y., Sun M.; RT "Complete Genome Sequence of Bacillus Subtilis BSn5, a Strain of RT Plant-associated Bacterium with Antimicrobial Activity to Soil-borne RT Plant Pathogens."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002468; ADV94647.1; -; Genomic_DNA. DR RefSeq; YP_004205674.1; NC_014976.1. DR ProteinModelPortal; E8VEP6; -. DR SMR; E8VEP6; 1-222. DR EnsemblBacteria; ADV94647; ADV94647; BSn5_10135. DR GeneID; 10182693; -. DR KEGG; bsn:BSn5_10135; -. DR PATRIC; 46871258; VBIBacSub180317_2068. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; BSUB936156:GHCY-2045-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23681 MW; BF09EB73866F4FB4 CRC64; MTRISREMMK ELLSVYFIMG SNNTKADPVT VVQKALKGGA TLYQFREKGG DALTGEARIK FAEKAQAACR EAGVPFIVND DVELALNLKA DGIHIGQEDA NAKEVRAAIG DMILGVSAHT MSEVKQAEED GADYVGLGPI YPTETKKDTR AVQGVSLIEA VRRQGISIPI VGIGGITIDN AAPVIQAGAD GVSMISAISQ AEDPESAARK FREEIQTYKT GR // ID E8VHI8_BACST Unreviewed; 205 AA. AC E8VHI8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-APR-2014, entry version 22. DE SubName: Full=Transcriptional regulator TenI; GN OrderedLocusNames=BSn5_17745; OS Bacillus subtilis (strain BSn5). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=936156; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSn5; RX PubMed=21317323; DOI=10.1128/JB.00129-11; RA Deng Y., Zhu Y., Wang P., Zhu L., Zheng J., Li R., Ruan L., Peng D., RA Sun M.; RT "Complete genome sequence of Bacillus subtilis BSn5, an endophytic RT bacterium of Amorphophallus konjac with antimicrobial activity for the RT plant pathogen Erwinia carotovora subsp. carotovora."; RL J. Bacteriol. 193:2070-2071(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSn5; RA Deng Y., Sun M.; RT "Complete Genome Sequence of Bacillus Subtilis BSn5, a Strain of RT Plant-associated Bacterium with Antimicrobial Activity to Soil-borne RT Plant Pathogens."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002468; ADV96157.1; -; Genomic_DNA. DR RefSeq; YP_004207184.1; NC_014976.1. DR EnsemblBacteria; ADV96157; ADV96157; BSn5_17745. DR GeneID; 10184280; -. DR KEGG; bsn:BSn5_17745; -. DR PATRIC; 46874570; VBIBacSub180317_3624. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR BioCyc; BSUB936156:GHCY-3632-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 22929 MW; 1E4953427153A6E5 CRC64; MELHAITDDS KPVEELARII ITIQNEVDFI HIRERSKSAA DILKLLELIF EGGIDKRKLV MNGRVDIALF STIHRVQLPS GSFSPKQVRA RFPHLHIGRS VHSLEEAVQA EKEDADYVLF GHVFETDCKK GLEGRGVSLL SDIKQRISIP VIAIGGMTPD RLRDVKQAGA DGIAVMSGIF SSAEPLEAAR RYSRKLKEMR YEKAL // ID E8VU61_VIBVM Unreviewed; 444 AA. AC E8VU61; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=VVMO6_02941; OS Vibrio vulnificus (strain MO6-24/O). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=914127; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MO6-24/O; RX PubMed=21317338; DOI=10.1128/JB.00110-11; RA Park J.H., Cho Y.J., Chun J., Seok Y.J., Lee J.K., Kim K.S., Lee K.H., RA Park S.J., Choi S.H.; RT "Complete genome sequence of Vibrio vulnificus MO6-24/O."; RL J. Bacteriol. 193:2062-2063(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002469; ADV87963.1; -; Genomic_DNA. DR RefSeq; YP_004190166.1; NC_014965.1. DR EnsemblBacteria; ADV87963; ADV87963; VVMO6_02941. DR GeneID; 10167755; -. DR KEGG; vvm:VVMO6_02941; -. DR PATRIC; 47053986; VBIVibVul176069_2920. DR KO; K00788; -. DR BioCyc; VVUL914127:GJJH-3060-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 444 AA; 49290 MW; 8913F419D71DF212 CRC64; MRLLIPSAII ELTGEIQQCL FLAKQQGFAI DHIELGVSPT RTLQLISSAK TVVFETDLIH NDSRHLGAHD FALHYHHSLA LTEVSSYLGS ECKAKTLLIN LQGEQGEAFD VWQHPLADET RALRFLSRQN HSQNESVESI YRHLAWVVTL SALDFPIEDC LTLARAMLNV SRETWVSDFA LFPTPVLHLD EFGILPSHNL EGLTKAFPRV IAQQLGLYPV VDDVSWIEKL LPLGIKTVQL RIKDPNQVDL EQQIVRAIQL GRDYGAQVYI NDYWQLAILH QAYGVHLGQE DLQVADLAAL TNAGIALGLS THGYYELLRI VQLQPSYIAL GHIFPTTTKQ MPSLPQGLVR LKLYQQLIDT MPYDETITGV PTVAIGGIDQ SNAATVWQCG VSSLAVVRAI TLAKDVKAVI EHFKQVMTPN TTLVRLDSAS THSLEPISEA NHVG // ID E8VZC4_STRFA Unreviewed; 216 AA. AC E8VZC4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sfla_4713; OS Streptomyces flavogriseus (strain ATCC 33331 / DSM 40990 / IAF-45CD). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=591167; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33331 / DSM 40990 / IAF-45CD; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Brumm P., Mead D., Woyke T.; RT "Complete sequence of chromosome of Streptomyces flavogriseus ATCC RT 33331."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002475; ADW06114.1; -; Genomic_DNA. DR RefSeq; YP_004925631.1; NC_016114.1. DR ProteinModelPortal; E8VZC4; -. DR EnsemblBacteria; ADW06114; ADW06114; Sfla_4713. DR GeneID; 11367714; -. DR KEGG; sfa:Sfla_4713; -. DR KO; K00788; -. DR BioCyc; SFLA591167:GI5Y-4786-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22598 MW; B8C6ACDEED2D4D51 CRC64; MSTPRDQLSG ARLYLCTDAR KRQGDLPEFL DAVLANGVDI VQLRDKGMEA AEELEHLAVL ADACKRHGAL LAVNDRADVA HAIGSDVLHL GQGDLPVPAA RAVLGADVII GRSTHAEAEV DAAVAEAGVD YFCTGPCWPT PTKPGRHAPG LGLVRHAASL GTTRPWFAIG GIDAGNLDEV LDAGARRVVV VRAITEAADP AEAAASLARR VRERAV // ID E8WQ22_GEOS8 Unreviewed; 219 AA. AC E8WQ22; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GM18_3703; OS Geobacter sp. (strain M18). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=443143; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M18; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., RA Pagani I., Holmes D., Aklujkar M., Lovley D., Woyke T.; RT "Complete sequence of Geobacter sp. M18."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002479; ADW15131.1; -; Genomic_DNA. DR RefSeq; YP_004200407.1; NC_014973.1. DR ProteinModelPortal; E8WQ22; -. DR EnsemblBacteria; ADW15131; ADW15131; GM18_3703. DR GeneID; 10199330; -. DR KEGG; geb:GM18_3703; -. DR PATRIC; 46951342; VBIGeoSp68312_3671. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR BioCyc; GSP443143:GHZL-3771-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23891 MW; 3A4F790E30A20212 CRC64; MRELDSPWID FNLYLITGRG ETLGRNLEFV VEEALRGGVR AVQLRDKGVS TKDLYETAQE LRRLTSRYGA KLFINDRADV ALAVDADGVH IGSSSLPLYK VRRLLGERKL IGVSCHNQTQ AITAQEMGAD FITFGPVYHT PSKAEYGEPV GVEKLDKVAQ MLQIPVFALG GVNLDNCSDA VSGGVRGIAL ISAILSAPEP RDAAKRLLAL LPPLEEHHD // ID E8WRU5_GEOS8 Unreviewed; 485 AA. AC E8WRU5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE SubName: Full=Phosphomethylpyrimidine kinase; GN OrderedLocusNames=GM18_0635; OS Geobacter sp. (strain M18). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=443143; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M18; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., RA Pagani I., Holmes D., Aklujkar M., Lovley D., Woyke T.; RT "Complete sequence of Geobacter sp. M18."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002479; ADW12116.1; -; Genomic_DNA. DR RefSeq; YP_004197392.1; NC_014973.1. DR ProteinModelPortal; E8WRU5; -. DR EnsemblBacteria; ADW12116; ADW12116; GM18_0635. DR GeneID; 10196206; -. DR KEGG; geb:GM18_0635; -. DR PATRIC; 46945115; VBIGeoSp68312_0627. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OMA; YLAQGEP; -. DR BioCyc; GSP443143:GHZL-646-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 485 AA; 51148 MW; 05FE86FA97D5457F CRC64; MLKLVVDHSG KERRVAGLYL ITDQGERLVP RVREALASGG VTLLQYRDKL RSYEERLELG HDLKRLCTEF QVQFIINDDL ELALALDADG LHLGQEDGDP AAARAALGSK KLIGISTHSF EEALAAQEAG ADYIGFGSLY PTLTKEVEYI QSPEALAQLK EKVQIPVVAI GGITRDNACA VIDAGADAIA VISAVLTARS PGLAATELSL LFNRNLTHPR GAVLTIAGSD SGGGAGIQAD LKTITLLGSY GASAITALTA QNTRGVTGIH PSPPAFLAEQ IDAVLSDIPI DVIKIGMLCS PENAEIVADK LTAYEMRMVV LDPVMSAKGG VALLEDEALS VLKKRLIPHS YLVTPNIPEA EALTGLTISD TAGMELAARA LHLMGAKHVL VKGGHLTEGV VTDILFDGSG FTRFSAPRVL TRNTHGTGCT LASAIATYLA QGEPLPGAVL RAKLFVTRAI KYSLPLGKGH GPVNHFLAAR DQADN // ID E8X037_ACISM Unreviewed; 234 AA. AC E8X037; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AciX9_1887; OS Acidobacterium sp. (strain MP5ACTX9). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Acidobacterium. OX NCBI_TaxID=696844; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP5ACTX9; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Rawat S.R., Mannisto M., Haggblom M.M., Woyke T.; RT "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002480; ADW68933.1; -; Genomic_DNA. DR RefSeq; YP_004217713.1; NC_015064.1. DR ProteinModelPortal; E8X037; -. DR EnsemblBacteria; ADW68933; ADW68933; AciX9_1887. DR GeneID; 10203886; -. DR KEGG; acm:AciX9_1887; -. DR PATRIC; 46821334; VBIAciSp155132_2566. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 234 AA; 24372 MW; 714B7CF674DAE921 CRC64; MKGLYAIADV GVLARRGMGL RVFAEGLKAA GVGVVQLRDK DGSPEGVLAG ARVLREVFAG TDSLLVMNDR VDLGLLAGFG GVHVGQGDLS VEDAKAVAGQ SESQRAQRKD EEDTERKWVV GGSTHTEDEV RVADVGAADY VAVGPVFATG TKADASPVVG LEGVRRARAL TGKPLVAIGG ITLANARSVV DAGADMVAVI TGLFVPGRTV ESVAWEFGKI CVEVEREKTQ TRIF // ID E8X3Z1_ACISM Unreviewed; 211 AA. AC E8X3Z1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=AciX9_3494; OS Acidobacterium sp. (strain MP5ACTX9). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Acidobacterium. OX NCBI_TaxID=696844; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP5ACTX9; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Rawat S.R., Mannisto M., Haggblom M.M., Woyke T.; RT "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002480; ADW70499.1; -; Genomic_DNA. DR RefSeq; YP_004219279.1; NC_015064.1. DR EnsemblBacteria; ADW70499; ADW70499; AciX9_3494. DR GeneID; 10205515; -. DR KEGG; acm:AciX9_3494; -. DR PATRIC; 46824514; VBIAciSp155132_4131. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 211 AA; 21858 MW; F87DB6514F02C9C2 CRC64; MTQAVHCQRR FIRPKLDSML RYAITDRFLL GKGDTGRLIE RCGALAQTGI DFILVREKDL PAGELVQLCR QIAAAAQGSA TQILVSSRVD VALAAGVAGV HLSSQPGELT PAQVRQLMPS AFISVSCHSL EEIRRARLGG ASAALFAPVF GKTIQGQEVS AAIGLDALRA ACAEAAPMPV FALGGVTNEN AASCGAAGAA GIAGIRIFYA A // ID E8XLA9_SALT4 Unreviewed; 211 AA. AC E8XLA9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=STM474_4349; OS Salmonella typhimurium (strain 4/74). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=909946; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4/74; RX PubMed=21478351; DOI=10.1128/JB.00394-11; RA Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S., RA Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.; RT "Genome sequences of Salmonella enterica serovar typhimurium, RT Choleraesuis, Dublin, and Gallinarum strains of well- defined RT virulence in food-producing animals."; RL J. Bacteriol. 193:3162-3163(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002487; ADX19929.1; -; Genomic_DNA. DR RefSeq; YP_005245128.1; NC_016857.1. DR ProteinModelPortal; E8XLA9; -. DR EnsemblBacteria; ADX19929; ADX19929; STM474_4349. DR PATRIC; 47200479; VBISalEnt171491_4419. DR OMA; AVRPSYI; -. DR BioCyc; SENT909946:GLJU-4319-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22983 MW; 803CF861FC550D88 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE SGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID E8XYC7_RAHSY Unreviewed; 217 AA. AC E8XYC7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rahaq_4127; OS Rahnella sp. (strain Y9602). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Rahnella. OX NCBI_TaxID=741091; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y9602; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Sobecky P.A., RA Martinez R.J., Woyke T.; RT "Complete sequence of chromosome of Rahnella sp. Y9602."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002505; ADW75715.1; -; Genomic_DNA. DR RefSeq; YP_004214842.1; NC_015061.1. DR EnsemblBacteria; ADW75715; ADW75715; Rahaq_4127. DR GeneID; 10215165; -. DR KEGG; rah:Rahaq_4127; -. DR PATRIC; 47406500; VBIRahSp167412_4112. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; RSP741091:GHHP-4207-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23231 MW; 82F0B08770C9E16D CRC64; MNPSSQSFPA VPFHLGLYPV VDTVEWIARL LDAGVKTLQL RVKDLPDEQA EPAIIDAIAL GKKYQARLFI NDYWRLAVKH QAYGVHLGQE DLDTADLEAI RQAGLRLGVS THDDAEMARA VAVNPSYIAL GHIFPTQTKD MPSAPQGLAE LTRHVKKLDG SFPTVAIGGI SIDRAASVLD CGVGSIAVVS AITQAADWRA ATAQLLALCA SKVPQDA // ID E8Y694_ECOKO Unreviewed; 211 AA. AC E8Y694; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-MAY-2014, entry version 29. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EKO11_4328; ORFNames=KO11_02405; OS Escherichia coli (strain ATCC 55124 / KO11). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=595495; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55124 / KO11, and KO11; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Keating D., Landick R., Woyke T.; RT "Complete sequence of chromosome of Escherichia coli KO11."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KO11FL; RX PubMed=22075923; DOI=10.1007/s10295-011-1052-2; RA Turner P.C., Yomano L.P., Jarboe L.R., York S.W., Baggett C.L., RA Moritz B.E., Zentz E.B., Shanmugam K.T., Ingram L.O.; RT "Optical mapping and sequencing of the Escherichia coli KO11 genome RT reveal extensive chromosomal rearrangements, and multiple tandem RT copies of the Zymomonas mobilis pdc and adhB genes."; RL J. Ind. Microbiol. Biotechnol. 39:629-639(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002516; ADX52886.1; -; Genomic_DNA. DR EMBL; CP002970; AFH15469.1; -; Genomic_DNA. DR RefSeq; YP_005279950.1; NC_016902.1. DR RefSeq; YP_006162821.1; NC_017660.1. DR SMR; E8Y694; 10-208. DR EnsemblBacteria; ADX52886; ADX52886; EKO11_4328. DR EnsemblBacteria; AFH15469; AFH15469; KO11_02405. DR GeneID; 11778935; -. DR GeneID; 12759993; -. DR KEGG; ekf:KO11_02405; -. DR KEGG; eko:EKO11_4328; -. DR PATRIC; 48648845; VBIEscCol13896_4400. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; ECOL595495:GI1Q-4415-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E8YGN2_9BURK Unreviewed; 370 AA. AC E8YGN2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BC1001_3211; OS Burkholderia sp. CCGE1001. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=640510; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCGE1001; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Saunders E., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J., Woyke T.; RT "Complete sequence of chromosome1 of Burkholderia sp. CCGE1001."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002519; ADX56625.1; -; Genomic_DNA. DR RefSeq; YP_004229685.1; NC_015136.1. DR ProteinModelPortal; E8YGN2; -. DR EnsemblBacteria; ADX56625; ADX56625; BC1001_3211. DR GeneID; 10224791; -. DR KEGG; bug:BC1001_3211; -. DR PATRIC; 46899335; VBIBurSp1058_3362. DR KO; K00788; -. DR BioCyc; BSP640510:GI28-3269-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 370 AA; 39922 MW; 4B4DC78EDFAE1676 CRC64; MTQTLALKDR DLFWPPADEL VEATERIRAR LGDWPPTHAP WRICLTAPDE PNGGDLIVVA DTARHDEQMA RWLVQGAAVV EAAEHKATLH LGGEKYQLEG HLAEDWIPAL AAFLDCGFDP HDALVLALAW RDGDETCTHA AGDSFPCDLA SFPRVAGLPP APAEAFPRCP ERLGLYPVLP SAEWVERVLD FGVKTVQLRR KSAHPADELQ REIARCVAAG RQHDAQVFIN DHWRAALEAG AYGVHLGQED VHTADLSALA TAGIRLGLST HGFYEILKAL HFRPSYIALG AVFPTTTKVM PTAPQGLKRL ARYVRLLDGV VPLVAIGGID LQVLPDVLAT GVGCAAVVRA VTEAADPAAA VSALQQAFTQ // ID E8ZTA8_CLOB0 Unreviewed; 205 AA. AC E8ZTA8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=H04402_00468; OS Clostridium botulinum (strain H04402 065 / Type A5). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=941968; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H04402 065 / Type A5; RX PubMed=21378191; DOI=10.1128/JB.00072-11; RA Carter A.T., Pearson B.M., Crossman L.C., Drou N., Heavens D., RA Baker D., Febrer M., Caccamo M., Grant K.A., Peck M.W.; RT "Complete genome sequence of proteolytic Clostridium botulinum type A5 RT (B3') strain H04402 065."; RL J. Bacteriol. 193:2351-2352(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR773526; CBZ02283.1; -; Genomic_DNA. DR RefSeq; YP_005677034.1; NC_017299.1. DR ProteinModelPortal; E8ZTA8; -. DR EnsemblBacteria; CBZ02283; CBZ02283; H04402_00468. DR GeneID; 12916503; -. DR KEGG; cbj:H04402_00468; -. DR KO; K00788; -. DR BioCyc; CBOT941968:GLBI-496-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22407 MW; 33B89532CE505327 CRC64; MEINYELYLI TDRRFLKGRQ LKKVVEDAIL GGVTIVQVRE KDVSTREFYN VAKEVKEVTD YYKVPIIIND RLDIAQAIDA SGVHLGQKDM HLNIAREILG KDKIIGISVG NVKEALEAQN NGADYLGIGT IFPTGSKKDV DAIIGIDGLS KIKDSISIPS VAIGGINKTN FKDVLKTGIE GISVISAILD EDDIKLAANN LLINK // ID E9A9D9_SALET Unreviewed; 211 AA. AC E9A9D9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SENTW_4271; OS Salmonella enterica subsp. enterica serovar Weltevreden str. OS 2007-60-3289-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=936157; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2007-60-3289-1; RA Brankatschk K., Blom J., Goesmann A., Smits T.H., Duffy B.; RT "Genome of a European Fresh-Vegetable Food Safety Outbreak Strain of RT Salmonella enterica subsp. enterica Serovar Weltevreden."; RL J. Bacteriol. 193:2066-2066(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR775245; CBY98352.1; -; Genomic_DNA. DR RefSeq; YP_006888552.1; NT_187126.1. DR ProteinModelPortal; E9A9D9; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22859 MW; DF93565F60864431 CRC64; MYQPDFPTVP FCLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVES DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSVAVVSAIT QAADWRAATA QLLDIAGVGD E // ID E9CMK6_9ENTR Unreviewed; 216 AA. AC E9CMK6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSYM_1559; OS Serratia symbiotica str. Tucson. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia; Serratia symbiotica. OX NCBI_TaxID=914128; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tucson; RA Burke G.R., Moran N.A.; RT "Massive genomic decay in Serratia symbiotica, a recently evolved RT symbiont of aphids."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL636113; EFW12220.1; -; Genomic_DNA. DR PATRIC; 46581007; VBISerSym177930_1403. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23302 MW; 9811EA7DF484BAA0 CRC64; MTDITTPFPD TPHKLGLYPV VNSVEWIARL LDAGVTTLQL RIKDLPSEQV EEDTATAIAL GKQYGARLFI NDYWQLAIKH RAYGVHLGQE DLDSADLLAI HRAGLRLGVS THDDTELARA IALKPSYIAL GHIFATQTKN MPSAPQGLSA LKRHIARLPG YPTVAIGGIN LDRVPAVLAC GVGSVAVVSA ITKAPDWRAA TAELLRLIEG EVWSDA // ID E9DD51_COCPS Unreviewed; 529 AA. AC E9DD51; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-APR-2014, entry version 12. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme; GN ORFNames=CPSG_08013; OS Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever OS fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; mitosporic Onygenales; Coccidioides. OX NCBI_TaxID=443226; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RMSCC 757 / Silveira; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., RA Gardner M.J., Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Howarth C., Jen D., Larson L., RA Mehta T., Neiman D., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Coccidioides posadasii strain Silveira."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL636500; EFW15576.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 529 AA; 56093 MW; C481486F4DBCA285 CRC64; MPIDLSLYLV TDSTPNILGD RDLCTVVEQA IQGGVTIVQY RDKHADTGVL IETASRLHTI TKAHGVPLVI NDRVDVALAV GAEGVHLGQD DMDIETARKL LPKNCFIGAT VSSVEEARIA VEKGANYLGI GTVFATPTKT NTKSIIGTAG VRQILDFLST LPRKVGTVAI GGINLSNTQR VIYQSAAATK GLDGVAIVSA IVAAEDPYKA AALLARAIIK SPSFATIPPD PREDEFSYLL NNAISVARKV AVRMPLVHSM INYVVANFAA NVSLQIGASP IMSPYGPEAT DLSKAGGSLL INMGTLNADS LNNYTQAVQA YNQRGSPVVF DPVGGGATEV RQNAIRTLMA GGYFDLIKGN ESEIKVIYGQ SSSRQIGVDS GPSTLTLQEK VAMVRDLATR ERNIVLMTGP VDFLSDGIRT VAIKNGHRYL GQITGTGCVI GLVAAAFLAV ERTDKLLAVL AGVLMFEIAA ENAALKEYVR GPGTFMPAFL DELYALREDT KASPENNWIK QRAQITVFTA ESDGAASSS // ID E9DNQ6_9STRE Unreviewed; 210 AA. AC E9DNQ6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0848_00880; OS Streptococcus sp. C150. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=435842; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C150; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Sibley C.D., Field T.R., Grinwis M., RA Eshaghurshan C.S., Surette M.G., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Streptococcus sp. C150."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL698449; EFX55283.1; -; Genomic_DNA. DR EnsemblBacteria; EFX55283; EFX55283; HMPREF0848_00880. DR PATRIC; 46428158; VBIStrSp126103_0437. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23162 MW; 4876384D56BE7A54 CRC64; MLKETLRLYL VTNRYQDSLE TFLKKVEQAC QSGVTMVQLR EKNLTTNQYY ELAKIVKQTT DTYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GTEKILGVTA KTVKRALEAE ESGADYLGTG AIFPTTTKEN APITLISTLK DICQTVNIPV VAIGGLTCEN IHQLSGTDIA GIAVVRDLMQ ARDIEKRTQE FLIKLDQIIP // ID E9DSK6_METAQ Unreviewed; 477 AA. AC E9DSK6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-APR-2014, entry version 15. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative; GN ORFNames=MAC_00604; OS Metarhizium acridum (strain CQMa 102). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae; OC mitosporic Clavicipitaceae; Metarhizium. OX NCBI_TaxID=655827; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CQMa 102; RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264; RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., RA Hu X., Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., RA Fang W., Wang S., Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., RA Pei Y., Feng M.-G., Xia Y., Wang C.; RT "Genome sequencing and comparative transcriptomics of the model RT entomopathogenic fungi Metarhizium anisopliae and M. acridum."; RL PLoS Genet. 7:E1001264-E1001264(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL698471; EFY93366.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 477 AA; 49052 MW; 8CD23BB00B244CCA CRC64; MAVDYSVYLV TDSTPAILGD KDLISVVEAS LRGGVTVVQY RDKHSAREDV VAVAKKLHQL TKGYGVPLLI NDRVDVAVEI GCEGVHIGQD DMGDKKDTKS IIGPSGVADI LAALDAAGHS STPAVCIGGV NASNASAVLA GSASPRKALD GIAVVSAIIA ADDPAAASRD LLGKVITAKI PNVVAAVARK TPLSHNMTNL ACPPTPSPLS KPRGRAETDL TNATPIMSNY AEEAADLAKL GGALVLNMGT VTPEGLKNYA QALEAYNEAG RPVVLDPVGN LAASNASHAS SAGATSVRRE AVKTLLASGT FAVIKGNQSE IQTVHGAGVT QRGVDSSSSL TVPQRAQLVR SLARRRRCVV LLTGPTDLIS DGRRTLRVDN GHGYLGMITG TGCTLGTTVS AMAAAYEEDA LVATVAGTVM FGVAAEMAAQ REDVRGPGSF VPAFLDELFG IRKATMEGDS KWLALAKVAA VDVADDE // ID E9F0Y6_METAR Unreviewed; 457 AA. AC E9F0Y6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-APR-2014, entry version 17. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative; GN ORFNames=MAA_05935; OS Metarhizium anisopliae (strain ARSEF 23 / ATCC MYA-3075). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae; OC mitosporic Clavicipitaceae; Metarhizium. OX NCBI_TaxID=655844; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ARSEF 23 / ATCC MYA-3075; RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264; RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., RA Hu X., Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., RA Fang W., Wang S., Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., RA Pei Y., Feng M.-G., Xia Y., Wang C.; RT "Genome sequencing and comparative transcriptomics of the model RT entomopathogenic fungi Metarhizium anisopliae and M. acridum."; RL PLoS Genet. 7:E1001264-E1001264(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL698718; EFY98796.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 457 AA; 47042 MW; D253A4C623E64CE8 CRC64; MAVDYSVYLV TDSTPAILGD KDLISVVEAS LRGGVTVVQY RDKHSAKEDA VAVAKKLHQL TQSHGVPLLI NDRVDVAVEI GCEGVHIGQD DMGDKKDTKS IIGPSGVADI LAALDAAGHS SIPAVCIGGV NASNASAVLA GSASPHKALD GLAVVSAIIA AADPAAASRD LLGKVITAKI PDVVAAVGRK TPLSHNMTNL VVQNFAANVA LCVGASPIMS NYAEEAADLA RLGGALVLNM GTVTPEGLNN YAQALKAYNQ ARRPVVLDPV GAGATSVRRE AVQTLLASGT FAVIKGNQSE IQTVHGASVT QRGVDSSSSL TIPQRARLVR SLARQRRCVV LLTGPTDLIS DGRRTLRVDN GHGYLGMVTG TGCTLGTTVS AMAAAYEQDA LVATVAGTVM FGLAAEMAAQ RDHVRGPGSF VPAFLDELFG IRKATMEGDS TWLALAKVAA VDVADDE // ID E9FGA7_9STRE Unreviewed; 210 AA. AC E9FGA7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0849_00383; OS Streptococcus sp. C300. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=563036; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C300; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Sibley C.D., Field T.R., Grinwis M., RA Eshaghurshan C.S., Surette M.G., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Streptococcus sp. C300."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL732466; EFX57206.1; -; Genomic_DNA. DR EnsemblBacteria; EFX57206; EFX57206; HMPREF0849_00383. DR PATRIC; 46431246; VBIStrSp73906_0196. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22751 MW; B098C03F8A2FACE7 CRC64; MNREALRLYL VTNRYQDSLE SFLEKVETAC RSGVTIIQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGITA KTVKRALEAE TSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLSGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDDIIS // ID E9RNA9_LACRE Unreviewed; 215 AA. AC E9RNA9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0536_10618; OS Lactobacillus reuteri MM4-1A. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=548485; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MM4-1A; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGX02000006; EGC14970.1; -; Genomic_DNA. DR ProteinModelPortal; E9RNA9; -. DR EnsemblBacteria; EGC14970; EGC14970; HMPREF0536_10618. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23849 MW; BE51CB250D92566D CRC64; MIFDPKMLQV YLVGGTQDVH NDVVKFLEKV ELAMKSGITA FQYREKGNSK LRPNERVDLG LELRTLCTHY GIPLIVDDDY ELAQQINADG VHVGQNDTKI EQVSVAVGHQ MFIGYSCNTP EQVERANTMD FIDYIGCGPV FPTKSKSDAD TAIGINRLER LNMISERPVV AIGGIDEENM KVVHDTGVAG LAVISLVFDS KDLVATVKKM KNLYK // ID E9RRV7_9FIRM Unreviewed; 217 AA. AC E9RRV7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0490_00186; OS Lachnospiraceae bacterium 6_1_37FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658656; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_37FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 6_1_37FAA."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADCR01000004; EGC76110.1; -; Genomic_DNA. DR EnsemblBacteria; EGC76110; EGC76110; HMPREF0490_00186. DR PATRIC; 46449387; VBILacBac17921_0897. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23224 MW; 1ECF0F86AAC9625D CRC64; MRTGNQVDLT LYLVTDSTYH TTESLLRTVE EACKGGVTLV QLREKEAGGK EYLEKAILVK KITDRYGVPL IIDDRVDVAI ACDAAGVHVG ASDLPVAVAR KLLGPEKIVG ATAKTVEAAK KAWEEGADYL GVGAIYPTTT KVITILTKPE TLKAICETVP IPVTAIGGLN AENLEILRGC KMDGVAVVSA IMKADDPKRA AEYLKEKICK LKDTEGK // ID E9SHX8_RUMAL Unreviewed; 409 AA. AC E9SHX8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CUS_6956; OS Ruminococcus albus 8. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=246199; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=8; RA Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D., RA Montgomery R., Ziemer C., Klaassens E., Ocuiv P., Morrison M.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADKM02000134; EGC01151.1; -; Genomic_DNA. DR ProteinModelPortal; E9SHX8; -. DR EnsemblBacteria; EGC01151; EGC01151; CUS_6956. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 409 AA; 42710 MW; ADCEF7C222D08898 CRC64; MCKVVCVTAL TLCENAHKQL EKIAESGADM LVLRAKELTE DEYKKLAARV MEMFAESSTK VVLHNFVGAA LELGAECIHL PLGVLRGLDD DTKSKFRLIG ASCHSTEDAL EAQTLGAGYV TAGHVFKTDC KKGLAGRGLD FVRKVSGAVD IPVYGIGGIS PENAGKVIRA GADGVCVMSG FMSGEPHMLT EKLREVMNMR ITGDKLRLYA ITDPALVKER GIVSCVESAL KGGANIIQLR DKQCGHEGLV AQARELLPVC HKYGAPLIVN DDWQAAIEAG ADGVHVGIED APVDEIRAKA GGGFMIGATA KTVAQAQNAQ AAGADYLGVG ALFPSPTKTN AIPVSKALFS EIAGAVSIPC VAIGGISLEN IGTLAGMGAE GFAVVSAVFG ADDIESRTAR LKELISGMF // ID E9SNZ8_CLOSY Unreviewed; 227 AA. AC E9SNZ8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9475_02044; OS Clostridium symbiosum WAL-14673. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=742741; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-14673; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., RA Summanen P.H., Molitoris D.R., Vaisanen M.L., Daigneault M., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J., RA Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium symbiosum strain WAL-14673."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLR01000074; EGB18802.1; -; Genomic_DNA. DR EnsemblBacteria; EGB18802; EGB18802; HMPREF9475_02044. DR PATRIC; 46486479; VBICloSym148390_2440. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 24073 MW; 5D934F07AF877292 CRC64; MKFTKEEIRK SMLLYAVTDR MWLNEGETLI SVAEEVLKNG ATFLQIREKD LNEDDFEAEA EALHALCTKY RIPFVVNDSV EIALRCNADG VHVGQSDIKG RDIRALIGPD AILGISAGTV QEAEAAEAAG ADYIGVGAVF TTGTKKDARS LTMEQLRAIR NAVSIPIVAI GGINSGNIMR LAGSGVDGVA VVSAIFAAPH PGEATAGMLK LAEEMLSAKT VRGEGNE // ID E9SZB6_COREQ Unreviewed; 230 AA. AC E9SZB6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0724_11408; OS Rhodococcus equi ATCC 33707. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=525370; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33707; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNW02000007; EGD24873.1; -; Genomic_DNA. DR ProteinModelPortal; E9SZB6; -. DR EnsemblBacteria; EGD24873; EGD24873; HMPREF0724_11408. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 157 159 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 160 160 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 24305 MW; 71FC2F09591C7920 CRC64; MHASQSVKHL TPRERLADAR LYLCTDARRD KGDLAQFVDA ALAGGVDIVQ LRDKGSAGER EFGPMEVKEE LAALAVIGAA ARRHGALLAV NDRADVALAA GADVLHLGQN DLPVHYARQI VGPDVVIGRS TNNRAQASLA AIEEDVDYFC TGPVWATPTK PGRAASGIEL VRSTAEAQPS RPWFAIGGVD HERLPEILEA GATRIVVVRA ITAADDPKAA ARALSDALRG // ID E9TJL6_ECOLX Unreviewed; 211 AA. AC E9TJL6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9542_04009; OS Escherichia coli MS 117-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749539; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 117-3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTS01000327; EGB86573.1; -; Genomic_DNA. DR ProteinModelPortal; E9TJL6; -. DR SMR; E9TJL6; 10-208. DR EnsemblBacteria; EGB86573; EGB86573; HMPREF9542_04009. DR PATRIC; 47817568; VBIEscCol157132_3531. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9TQJ2_ECOLX Unreviewed; 211 AA. AC E9TQJ2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9533_00657; OS Escherichia coli MS 60-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749530; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 60-1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUF01000059; EGB84485.1; -; Genomic_DNA. DR ProteinModelPortal; E9TQJ2; -. DR SMR; E9TQJ2; 10-208. DR EnsemblBacteria; EGB84485; EGB84485; HMPREF9533_00657. DR PATRIC; 47842365; VBIEscCol156146_0564. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23086 MW; 1A8F52AF19C8B3F0 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ERPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9U723_ECOLX Unreviewed; 211 AA. AC E9U723; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9532_00786; OS Escherichia coli MS 57-2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749529; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 57-2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADUG01000054; EGB78706.1; -; Genomic_DNA. DR ProteinModelPortal; E9U723; -. DR SMR; E9U723; 9-208. DR EnsemblBacteria; EGB78706; EGB78706; HMPREF9532_00786. DR PATRIC; 47853567; VBIEscCol147009_0721. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23030 MW; D9436839F2B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSTIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9UUN2_9ACTO Unreviewed; 210 AA. AC E9UUN2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 14. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=NBCG_02468; OS Nocardioidaceae bacterium Broad-1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Nocardioidaceae. OX NCBI_TaxID=408672; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Broad-1; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Orbach M.J., Henn M.R., Cole G.T., Galgiani J.N., RA Gardner M.J., Kirkland T.N., Taylor J.W., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Howarth C., Jen D., Larson L., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., RA Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C., RA Haas B., Nusbaum C., Birren B.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Broad-1; RA Neafsey D., Orbach M.J., Henn M.R., Cole G.T., Galgiani J.N., RA Gardner M.J., Kirkland T.N., Taylor J.W., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D.I., Howarth C., Jen D., Larson L., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., RA Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C., RA Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Nocardioidaceae bacterium Broad-1."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVI01000042; EGD43284.1; -; Genomic_DNA. DR EnsemblBacteria; EGD43284; EGD43284; NBCG_02468. DR PATRIC; 46518512; VBINocBac160729_2561. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 210 AA; 21483 MW; 7D3A2B88F0CCA7CA CRC64; MTVLPRLLVL TDRSQLPLGR SLLATMAACA EAGLTHVVLR ELDEPLEHRA KLAELLAGLG LNVIAAHIPL PAAVGVQLPA SASGNTSFVE LLALSERPDS RCNSVLHLGR SCHSATEVAT AAEEGFDYAM LSPYALTESK PGYGPPLGPG AFGDLPLPTY ALGGITPDNA ADAVAGGAYG VAVMGAVMRA DEPGQVVRDL LAALAAGVTR // ID E9VHE7_ECOLX Unreviewed; 211 AA. AC E9VHE7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ERKG_04754; OS Escherichia coli H252. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656388; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H252; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli strain H252."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEFI01000033; EGB44733.1; -; Genomic_DNA. DR ProteinModelPortal; E9VHE7; -. DR SMR; E9VHE7; 9-208. DR EnsemblBacteria; EGB44733; EGB44733; ERKG_04754. DR PATRIC; 47961572; VBIEscCol162925_4997. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9VX74_ECOLX Unreviewed; 211 AA. AC E9VX74; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ERLG_04911; OS Escherichia coli H263. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656390; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H263; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli strain H263."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEFJ01000109; EGB49602.1; -; Genomic_DNA. DR ProteinModelPortal; E9VX74; -. DR SMR; E9VX74; 9-208. DR EnsemblBacteria; EGB49602; EGB49602; ERLG_04911. DR PATRIC; 47972813; VBIEscCol160927_5069. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9WAP1_ECOLX Unreviewed; 211 AA. AC E9WAP1; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ERBG_04603; OS Escherichia coli E1167. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656372; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E1167; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli strain E1167."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEHS01000070; EGC09370.1; -; Genomic_DNA. DR ProteinModelPortal; E9WAP1; -. DR SMR; E9WAP1; 10-208. DR EnsemblBacteria; EGC09370; EGC09370; ERBG_04603. DR PATRIC; 47982942; VBIEscCol163352_4743. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9WNZ7_ECOLX Unreviewed; 211 AA. AC E9WNZ7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ERCG_04627; OS Escherichia coli E1520. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656374; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E1520; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli strain E1520."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEHT01000099; EGB30439.1; -; Genomic_DNA. DR ProteinModelPortal; E9WNZ7; -. DR SMR; E9WNZ7; 11-208. DR EnsemblBacteria; EGB30439; EGB30439; ERCG_04627. DR PATRIC; 47993082; VBIEscCol161400_4786. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23027 MW; 0AE827392C8C3853 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGVSLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9X1Y2_ECOLX Unreviewed; 211 AA. AC E9X1Y2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ERDG_04498; OS Escherichia coli E482. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=550687; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E482; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli strain E482."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEHU01000070; EGB35110.1; -; Genomic_DNA. DR ProteinModelPortal; E9X1Y2; -. DR SMR; E9X1Y2; 20-202. DR EnsemblBacteria; EGB35110; EGB35110; ERDG_04498. DR PATRIC; 48003070; VBIEscCol163141_4702. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9XFN8_ECOLX Unreviewed; 211 AA. AC E9XFN8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EREG_04759; OS Escherichia coli H120. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656383; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H120; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli strain H120."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEHV01000132; EGB39699.1; -; Genomic_DNA. DR EnsemblBacteria; EGB39699; EGB39699; EREG_04759. DR PATRIC; 48013543; VBIEscCol162867_4914. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23069 MW; 886F5E43FE4A8ADE CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEV DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9XV34_ECOLX Unreviewed; 211 AA. AC E9XV34; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ERFG_04938; OS Escherichia coli TW10509. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656449; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TW10509; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli strain TW10509."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEHW01000055; EGB69325.1; -; Genomic_DNA. DR EnsemblBacteria; EGB69325; EGB69325; ERFG_04938. DR PATRIC; 48024586; VBIEscCol161062_5176. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23183 MW; DC88F14F423B5D21 CRC64; MYQPDFPHVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLP RAPAVMATGV GSIAVVSAIT QAADWRLATE QLLEIAGVGD E // ID E9Y8E4_ECOLX Unreviewed; 211 AA. AC E9Y8E4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ERGG_04550; OS Escherichia coli H489. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656404; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H489; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli strain H489."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEHX01000119; EGB54595.1; -; Genomic_DNA. DR ProteinModelPortal; E9Y8E4; -. DR SMR; E9Y8E4; 20-202. DR EnsemblBacteria; EGB54595; EGB54595; ERGG_04550. DR PATRIC; 48034744; VBIEscCol163998_4722. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9YMG9_ECOLX Unreviewed; 211 AA. AC E9YMG9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ERHG_04851; OS Escherichia coli TA007. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656429; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA007; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli strain TA007."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEHY01000138; EGB64375.1; -; Genomic_DNA. DR ProteinModelPortal; E9YMG9; -. DR SMR; E9YMG9; 20-202. DR EnsemblBacteria; EGB64375; EGB64375; ERHG_04851. DR PATRIC; 48045737; VBIEscCol162956_5104. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9Z205_ECOLX Unreviewed; 211 AA. AC E9Z205; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ERJG_04820; OS Escherichia coli M863. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656420; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M863; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli strain M863."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEHZ01000096; EGB59287.1; -; Genomic_DNA. DR EnsemblBacteria; EGB59287; EGB59287; ERJG_04820. DR PATRIC; 48056959; VBIEscCol163215_5038. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23095 MW; 4EF760EE698C9D2C CRC64; MYQPDFPHVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWQLAIKHQA YGVHLGQEDL QSTDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLP RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9ZF37_ESCFE Unreviewed; 211 AA. AC E9ZF37; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ERIG_04442; OS Escherichia fergusonii B253. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=550694; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B253; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia fergusonii strain B253."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEIA01000029; EGC04897.1; -; Genomic_DNA. DR EnsemblBacteria; EGC04897; EGC04897; ERIG_04442. DR PATRIC; 52545617; VBIEscFer76022_4607. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23213 MW; EBCF93C6FA5A69F8 CRC64; MYQPDFPHVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVTAIALGR RYNARLFIND YWRLAIKHQA YGIHLGQEDL QTTDLDAIRT AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLP RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID E9ZFK3_MYCTX Unreviewed; 222 AA. AC E9ZFK3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TMMG_03172; OS Mycobacterium tuberculosis CDC1551A. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=911237; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC1551A; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Galagan J., Gagneux S., Young S.K., Zeng Q., Gargeya S., Alvarado L., RA Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C., RA Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain CDC1551A."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AELF01000014; EGB30147.1; -; Genomic_DNA. DR ProteinModelPortal; E9ZFK3; -. DR SMR; E9ZFK3; 1-221. DR EnsemblBacteria; EGB30147; EGB30147; TMMG_03172. DR PATRIC; 52614064; VBIMycTub171704_0148. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID E9ZX09_NEIME Unreviewed; 205 AA. AC E9ZX09; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NMXN1568_1937; OS Neisseria meningitidis N1568. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=562020; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=N1568; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQD01000092; EGC50281.1; -; Genomic_DNA. DR EnsemblBacteria; EGC50281; EGC50281; NMXN1568_1937. DR PATRIC; 52901479; VBINeiMen71257_2665. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21705 MW; 6D6EF39936BD6D5C CRC64; MTFLPLKSPL KFYAVVPTAD WVERMVEAGA DTVQLRCKAL HSDELKREIA RCAAACQGSH TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYIASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID F0A2K2_NEIME Unreviewed; 205 AA. AC F0A2K2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NMBOX9930304_1892; OS Neisseria meningitidis OX99.30304. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935592; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OX99.30304; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQE01000123; EGC52155.1; -; Genomic_DNA. DR EnsemblBacteria; EGC52155; EGC52155; NMBOX9930304_1892. DR PATRIC; 52907322; VBINeiMen177978_2519. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21664 MW; 8CCB8C4953833D3E CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKAL HGDELKREIA RCAAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYIASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAE EVLATGVSSL AVVRAVTEAA NPEAVVKAFQ ALWDG // ID F0A882_NEIME Unreviewed; 205 AA. AC F0A882; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NMBM6190_1991; OS Neisseria meningitidis M6190. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935587; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M6190; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQF01000044; EGC54023.1; -; Genomic_DNA. DR ProteinModelPortal; F0A882; -. DR EnsemblBacteria; EGC54023; EGC54023; NMBM6190_1991. DR PATRIC; 52913200; VBINeiMen176114_2655. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21654 MW; 28E6A2E0137A5C49 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGDELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAE NPEAVVKAFQ ALWDG // ID F0ADX7_NEIME Unreviewed; 205 AA. AC F0ADX7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NMBM13399_2064; OS Neisseria meningitidis M13399. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935594; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M13399; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQG01000044; EGC55913.1; -; Genomic_DNA. DR ProteinModelPortal; F0ADX7; -. DR EnsemblBacteria; EGC55913; EGC55913; NMBM13399_2064. DR PATRIC; 52919310; VBINeiMen176386_2748. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21561 MW; 8A9C7F4164DC2A47 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKAL HGDELKREIA RCVAACQGSH TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYIASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID F0AJI3_NEIME Unreviewed; 205 AA. AC F0AJI3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NMBM0579_1963; OS Neisseria meningitidis M0579. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935590; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M0579; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQH01000030; EGC57921.1; -; Genomic_DNA. DR EnsemblBacteria; EGC57921; EGC57921; NMBM0579_1963. DR PATRIC; 52925174; VBINeiMen181207_2663. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21547 MW; 6D36E0F3FF4972FA CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKAL HGDELKREIA RCVAACQGSR TQLFINDHWH EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAQ AVLATGVSSL AVVRAVTEAA NPEAVVKAFQ ALWDG // ID F0AQ53_NEIME Unreviewed; 205 AA. AC F0AQ53; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NMBES14902_1968; OS Neisseria meningitidis ES14902. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935586; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ES14902; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQI01000045; EGC59929.1; -; Genomic_DNA. DR ProteinModelPortal; F0AQ53; -. DR EnsemblBacteria; EGC59929; EGC59929; NMBES14902_1968. DR PATRIC; 52931118; VBINeiMen179918_2654. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21654 MW; 28E6A2E0137A5C49 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGDELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAE NPEAVVKAFQ ALWDG // ID F0AV81_NEIME Unreviewed; 205 AA. AC F0AV81; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NMBCU385_1803; OS Neisseria meningitidis CU385. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935597; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CU385; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQJ01000045; EGC61932.1; -; Genomic_DNA. DR ProteinModelPortal; F0AV81; -. DR EnsemblBacteria; EGC61932; EGC61932; NMBCU385_1803. DR PATRIC; 52936520; VBINeiMen175349_2405. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21605 MW; 7DAC8AFBD9AD2D26 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKAL HGDELKREIA RCAAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYIASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID F0B1F2_NEIME Unreviewed; 205 AA. AC F0B1F2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NMB9615945_2008; OS Neisseria meningitidis 961-5945. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935598; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=961-5945; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQK01000154; EGC63864.1; -; Genomic_DNA. DR EnsemblBacteria; EGC63864; EGC63864; NMB9615945_2008. DR PATRIC; 52943232; VBINeiMen178209_2720. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21708 MW; C441B54399455D54 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGDELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAE EVLATGVSSL AVVRAVTEAA NPEAVVKAFQ ALWDG // ID F0B729_NEIME Unreviewed; 205 AA. AC F0B729; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NMBM01240013_2021; OS Neisseria meningitidis M01-240013. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935595; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M01-240013; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQL01000052; EGC65804.1; -; Genomic_DNA. DR EnsemblBacteria; EGC65804; EGC65804; NMBM01240013_2021. DR PATRIC; 52949182; VBINeiMen176729_2695. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21708 MW; C441B54399455D54 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGDELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAE EVLATGVSSL AVVRAVTEAA NPEAVVKAFQ ALWDG // ID F0BCJ8_9XANT Unreviewed; 315 AA. AC F0BCJ8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 13-NOV-2013, entry version 16. DE SubName: Full=Mutator mutT protein; DE Flags: Precursor; GN ORFNames=XVE_1826; OS Xanthomonas vesicatoria ATCC 35937. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925775; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35937; RX PubMed=21396108; DOI=10.1186/1471-2164-12-146; RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P., RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., RA Preston J.F., Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., RA Staskawicz B.J., Jones J.B.; RT "Comparative genomics reveals diversity among xanthomonads infecting RT tomato and pepper."; RL BMC Genomics 12:146-146(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQV01000052; EGD09871.1; -; Genomic_DNA. DR ProteinModelPortal; F0BCJ8; -. DR PATRIC; 46604326; VBIXanVes179409_1757. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34988 MW; E316BA205B8AD0D0 CRC64; MPDSLRSIHV VAGVITDPRG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELHE ELGIEAQVGE WVMDVPQLYP DKRLRLEVRH IVSWKGSPRG REGQAMTWVA ADKLTRYSMP PADVPVVGVL RQPDRYLITP EPEDDTRWLE GLERALQDGV TRIQLRGRQV APARWQALLH QVMNLRGRVR AQLLLNRDIV LAAELGIGVH LGSEQLAGLQ ERPLPAEQLV AASCHGLEEL RHAQRLGCDF AVLGPVRATA SHPGATPLGW DGFETLREQV SLPIYALGGM QAADLREARA HGAQGIAAIR SLWPQ // ID F0BG84_9XANT Unreviewed; 207 AA. AC F0BG84; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=XVE_3248; OS Xanthomonas vesicatoria ATCC 35937. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925775; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35937; RX PubMed=21396108; DOI=10.1186/1471-2164-12-146; RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P., RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., RA Preston J.F., Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., RA Staskawicz B.J., Jones J.B.; RT "Comparative genomics reveals diversity among xanthomonads infecting RT tomato and pepper."; RL BMC Genomics 12:146-146(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQV01000121; EGD08537.1; -; Genomic_DNA. DR PATRIC; 46607135; VBIXanVes179409_3083. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21499 MW; 20BD172BC2FD10D3 CRC64; MPQLQDARGV YLITPDDADT QRLLARTAPL LSSITWLQYR NKQADTALRR RQATALREAC AAQGVPLIIN DDAQLAVQVG AHGVHLGEDD GDVGVARAVL GPQAIIGVSC YDDIARARAA VARGASYVAF GAFFQTTTKV TTRRATPALL QQAADLGVPR VAIGGIAPAQ VAGLVTAGAD LIAVVSGVYA APDPVAALQA YRAGFAR // ID F0BNQ0_9XANT Unreviewed; 315 AA. AC F0BNQ0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Mutator mutT protein; GN ORFNames=XPE_0847; OS Xanthomonas perforans 91-118. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925776; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=91-118; RX PubMed=21396108; DOI=10.1186/1471-2164-12-146; RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P., RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., RA Preston J.F., Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., RA Staskawicz B.J., Jones J.B.; RT "Comparative genomics reveals diversity among xanthomonads infecting RT tomato and pepper."; RL BMC Genomics 12:146-146(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQW01000050; EGD15466.1; -; Genomic_DNA. DR ProteinModelPortal; F0BNQ0; -. DR EnsemblBacteria; EGD15466; EGD15466; XPE_0847. DR PATRIC; 46612639; VBIXanPer180062_0804. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34949 MW; 1F053438483BAD82 CRC64; MPDSLRSIHV VAGVITDPRG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIEAQVGD WVMEVPQLYP DKRLRLEVRH ITSWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGAL RQPDRYLITP EPEDEARWLE GLELALHNGI TRIQLRARQL APARWQALLQ QVMRLRGRAR AQLLLNRDIA LAADLGIGVH LGSEQLAGLQ ERPLPADRLV AASCHGLDDL RHAQRIGCDF AVLGPVQATA SHPGATPIGW DGFETLREQV WLPIYALGGM QGEDVRQARS HGAQGIAAIR ALWPQ // ID F0BUW6_9XANT Unreviewed; 207 AA. AC F0BUW6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=XPE_3141; OS Xanthomonas perforans 91-118. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925776; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=91-118; RX PubMed=21396108; DOI=10.1186/1471-2164-12-146; RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P., RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., RA Preston J.F., Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., RA Staskawicz B.J., Jones J.B.; RT "Comparative genomics reveals diversity among xanthomonads infecting RT tomato and pepper."; RL BMC Genomics 12:146-146(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQW01000174; EGD13235.1; -; Genomic_DNA. DR EnsemblBacteria; EGD13235; EGD13235; XPE_3141. DR PATRIC; 46617420; VBIXanPer180062_3040. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21586 MW; AB1ECC2CB4464668 CRC64; MPNRLDVRGV YLITPDEPNT QRLLLRTAPL LGSITWLQYR NKQADAALRL RQAGALREAC AAHGVPLIIN DDAQLAAQVG AQGVHLGEDD GDVAAARALL GEQAIIGVSC YDDIERARAA AEAGASYVAF GAFFPTTTKQ TTRRATPALL QQAAELNLPR VAIGGIAPAQ VTALVTAGAD LIAVVSGVYA APDPVAAVQE YRAGFGC // ID F0C1B3_9XANT Unreviewed; 315 AA. AC F0C1B3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Mutator mutT protein; DE Flags: Precursor; GN ORFNames=XGA_0623; OS Xanthomonas gardneri ATCC 19865. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925777; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19865; RX PubMed=21396108; DOI=10.1186/1471-2164-12-146; RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P., RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., RA Preston J.F., Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., RA Staskawicz B.J., Jones J.B.; RT "Comparative genomics reveals diversity among xanthomonads infecting RT tomato and pepper."; RL BMC Genomics 12:146-146(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQX01000060; EGD20695.1; -; Genomic_DNA. DR ProteinModelPortal; F0C1B3; -. DR EnsemblBacteria; EGD20695; EGD20695; XGA_0623. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34989 MW; A1671CAA32F173EB CRC64; MPDSLRSIHV VAGVITDARG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIEAQVGE WLMDVPQLYP DKRLRLEVRH ITAWKGSPRG REGQAMTWVA ADKLTRYSMP PADVPVVGAL RQPDRYLITP EPDDEMLWLE GLERALQEGV TRIQLRARQA EPARWQALLQ QVMRVRGRAR AQLLLNRDIA LAGELGIGVH LGSEQLAALQ QRPLPAEQLV AASCHGLEDL HHAQRLGCDF AVLGPVQTTT SHPGAAPLGW DGFETLREQV SLPIYALGGM QIDDLREARS HGAQGIAAIR SLWPQ // ID F0C842_9XANT Unreviewed; 207 AA. AC F0C842; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=XGA_3109; OS Xanthomonas gardneri ATCC 19865. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925777; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19865; RX PubMed=21396108; DOI=10.1186/1471-2164-12-146; RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P., RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., RA Preston J.F., Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., RA Staskawicz B.J., Jones J.B.; RT "Comparative genomics reveals diversity among xanthomonads infecting RT tomato and pepper."; RL BMC Genomics 12:146-146(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQX01000282; EGD18329.1; -; Genomic_DNA. DR EnsemblBacteria; EGD18329; EGD18329; XGA_3109. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21295 MW; 16611CA48519B105 CRC64; MPDLHNARGV YLITPDEPDT ARLLARTRPL LPVVTWLQYR NKQATAPLRL EQASALREAC AAHGVPLIIN DDAQLALQVG AQGVHLGEDD GEVAAARALL GAQAIIGVSC YDEIARAQAA VAAGASYVAF GAFFPTTTKV TTRRASPALL QQAAALGVPR VAIGGIAAAQ VPELVAAGAE LIAVVSGVYA APDPVAAVQA YRAGFAQ // ID F0CCC9_9XANT Unreviewed; 90 AA. AC F0CCC9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; Fragment; GN ORFNames=XGA_4627, XGA_4629; OS Xanthomonas gardneri ATCC 19865. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925777; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19865; RX PubMed=21396108; DOI=10.1186/1471-2164-12-146; RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P., RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., RA Preston J.F., Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., RA Staskawicz B.J., Jones J.B.; RT "Comparative genomics reveals diversity among xanthomonads infecting RT tomato and pepper."; RL BMC Genomics 12:146-146(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQX01000477; EGD16800.1; -; Genomic_DNA. DR EMBL; AEQX01000476; EGD16801.1; -; Genomic_DNA. DR EnsemblBacteria; EGD16800; EGD16800; XGA_4629. DR EnsemblBacteria; EGD16801; EGD16801; XGA_4627. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Signal. FT SIGNAL <1 21 Potential. FT CHAIN 22 90 Potential. FT /FTId=PRO_5000712671. FT NON_TER 1 1 SQ SEQUENCE 90 AA; 8811 MW; BE942A2B7E70A359 CRC64; QAAVAAGASY VAFGAFFPTT TKVTTRRASP ALLQQAAALG VPRVAIGGIA AAQVPELVAA GAELIAVVSG VYAAPDPVAA VQAYRAGFAQ // ID F0D6N0_STAAU Unreviewed; 171 AA. AC F0D6N0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-MAR-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN Name=thiE; ORFNames=SAO11_1861; OS Staphylococcus aureus O11. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=948561; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=O11; RX PubMed=21398544; DOI=10.1128/JB.00045-11; RA Le Marechal C., Hernandez D., Schrenzel J., Even S., Berkova N., RA Thiery R., Vautor E., Fitzgerald J.R., Francois P., Le Loir Y.; RT "Genome sequences of two Staphylococcus aureus ovine strains that RT induce severe (strain O11) and mild (strain O46) mastitis."; RL J. Bacteriol. 193:2353-2354(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUQ01000018; EGA97085.1; -; Genomic_DNA. DR EnsemblBacteria; EGA97085; EGA97085; SAO11_1861. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT NON_TER 171 171 SQ SEQUENCE 171 AA; 18867 MW; CAAD719787143DD8 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG G // ID F0D6W5_STAAU Unreviewed; 49 AA. AC F0D6W5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN Name=thiE; ORFNames=SAO11_1946; OS Staphylococcus aureus O11. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=948561; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=O11; RX PubMed=21398544; DOI=10.1128/JB.00045-11; RA Le Marechal C., Hernandez D., Schrenzel J., Even S., Berkova N., RA Thiery R., Vautor E., Fitzgerald J.R., Francois P., Le Loir Y.; RT "Genome sequences of two Staphylococcus aureus ovine strains that RT induce severe (strain O11) and mild (strain O46) mastitis."; RL J. Bacteriol. 193:2353-2354(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUQ01000021; EGA96919.1; -; Genomic_DNA. DR EnsemblBacteria; EGA96919; EGA96919; SAO11_1946. DR PATRIC; 53394084; VBIStaAur179325_1852. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; FT NON_TER 1 1 SQ SEQUENCE 49 AA; 5118 MW; B07BFCE261BC9C4C CRC64; PIVAIGGINT SNVAPIVEAG ANGISVISAI SKSENIEKTV NRFKDFFNN // ID F0DDT7_STAAU Unreviewed; 213 AA. AC F0DDT7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-MAR-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAO46_1603; OS Staphylococcus aureus O46. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=948563; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=O46; RX PubMed=21398544; DOI=10.1128/JB.00045-11; RA Le Marechal C., Hernandez D., Schrenzel J., Even S., Berkova N., RA Thiery R., Vautor E., Fitzgerald J.R., Francois P., Le Loir Y.; RT "Genome sequences of two Staphylococcus aureus ovine strains that RT induce severe (strain O11) and mild (strain O46) mastitis."; RL J. Bacteriol. 193:2353-2354(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUR01000019; EGB00059.1; -; Genomic_DNA. DR EnsemblBacteria; EGB00059; EGB00059; SAO46_1603. DR PATRIC; 53398889; VBIStaAur179520_1532. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23359 MW; 8756A27C9EE9DE8A CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F0E789_PSEDT Unreviewed; 314 AA. AC F0E789; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE SubName: Full=Uncharacterized protein; GN ORFNames=G1E_17018; OS Pseudomonas sp. (strain TJI-51). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=985010; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TJI-51; RA Asif H., Azim M.Kamran., Khan Aullah.; RT "A draft genome sequence and comparative analysis of Pseudomonas RT putida TJI-51."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEWE01000565; EGB97714.1; -; Genomic_DNA. DR ProteinModelPortal; F0E789; -. DR EnsemblBacteria; EGB97714; EGB97714; G1E_17018. DR PATRIC; 46727955; VBIPseSp184914_2831. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 314 AA; 34064 MW; 32B04CEE05D58A75 CRC64; MKRIHVVAAV IRGADGRILI ARRAATQHQG GLWEFPGGKV EAGESVEAAL ARELREELGI EVSRSRALIK VSHDYPDKQV LLDVREVQAF TGEAHGAEGQ PLAWVAPRDL PQYEFPEANQ PIVAAARLPD QYLITPDGLE VPQLLKGIQK AVASGIRLIQ LRAPDMYDPK YRDVAVDAVG LCAGKAQLML KGPLEWLGDF PSAGWHLTAA QLRKYAAKGR PFPRERWLAA SCHCAEELAL AEQMGVDFVT LSPVQATQTH PEAAPLGWDE AGRLLAGFSK PVYLLGGVGP GERERAWEAG AQGVAGIRAF WPEA // ID F0EA70_PSEDT Unreviewed; 54 AA. AC F0EA70; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE Flags: Fragment; GN Name=thiE; ORFNames=G1E_22325; OS Pseudomonas sp. (strain TJI-51). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=985010; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TJI-51; RA Asif H., Azim M.Kamran., Khan Aullah.; RT "A draft genome sequence and comparative analysis of Pseudomonas RT putida TJI-51."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEWE01000763; EGB96700.1; -; Genomic_DNA. DR EnsemblBacteria; EGB96700; EGB96700; G1E_22325. DR PATRIC; 46729938; VBIPseSp184914_3711. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. FT NON_TER 1 1 SQ SEQUENCE 54 AA; 5470 MW; BAD52DB0E9A51278 CRC64; SLPIAVIGGI TLDNAAPLVA HGADLLAVIH GLFGADSAQE VTRRARAFNA LFAS // ID F0EA71_PSEDT Unreviewed; 134 AA. AC F0EA71; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE Flags: Fragment; GN Name=thiE; ORFNames=G1E_22330; OS Pseudomonas sp. (strain TJI-51). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=985010; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TJI-51; RA Asif H., Azim M.Kamran., Khan Aullah.; RT "A draft genome sequence and comparative analysis of Pseudomonas RT putida TJI-51."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEWE01000764; EGB96687.1; -; Genomic_DNA. DR EnsemblBacteria; EGB96687; EGB96687; G1E_22330. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. FT NON_TER 134 134 SQ SEQUENCE 134 AA; 14404 MW; 98343D71C5961F4F CRC64; MKLRGLYAIT DSQLLASRFL SYVEAALEGG VCLLQYRDKS DDAARRLREA EALMKLCERY GTRLLINDDA ELAARLGVGV HLGQTDGPLT PARALLGRQA IIGSTCHASL ALAAQAAEEG ASYVAFGRFF NSVT // ID F0EQ89_HAEPA Unreviewed; 225 AA. AC F0EQ89; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9417_0033; OS Haemophilus parainfluenzae ATCC 33392. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=888828; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33392; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEWU01000002; EGC73252.1; -; Genomic_DNA. DR EnsemblBacteria; EGC73252; EGC73252; HMPREF9417_0033. DR PATRIC; 46748147; VBIHaePar172879_1132. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 24757 MW; A8ACD8FDCE907C39 CRC64; MKNIQEILPL YFVAGTQDCR HLGDNPADNL LSVLRQALEG GITCFQFRDK GKFSLENSPT EQRALAIKCR DLCRRYNVPF IVDDNVDLAL EIEADGIHVG QSDTPVKTIR ARTHKPFIIG WSVNRLDEAK IGEELSEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRKA GITKPLVAIG GVKLEHVKTL RKYGADGIAV ITAISQAKDI KASTKALKEA SGCNH // ID F0GEM0_9BURK Unreviewed; 100 AA. AC F0GEM0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 22-JAN-2014, entry version 13. DE SubName: Full=Uncharacterized protein; DE Flags: Fragment; GN ORFNames=B1M_33472; OS Burkholderia sp. TJI49. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=987057; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TJI49; RA Khan A.U., Asif H., Azim M.K.; RT "Draft Genome sequence of Burkholderia sp. TJI49 isolated from mango RT (Mangifera indica) tree."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TJI49; RX PubMed=23653265; DOI=10.1007/s11274-013-1366-5; RA Khan A., Asif H., Studholme D.J., Khan I.A., Azim M.K.; RT "Genome characterization of a novel Burkholderia cepacia complex RT genomovar isolated from dieback affected mango orchards."; RL World J. Microbiol. Biotechnol. 29:2033-2044(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXE01002063; EGD00062.1; -; Genomic_DNA. DR EnsemblBacteria; EGD00062; EGD00062; B1M_33472. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; FT NON_TER 1 1 SQ SEQUENCE 100 AA; 10569 MW; F57500BA4760BF6E CRC64; AALRATAQRP LPADRWLSAA CHSLDDLQLA ARAGADFVTL SPVLPTLSHP GAPTLGWAQF GAWAAQAAMP VYALGGMTPA HLDDARRHHA YGIAGIRSFW // ID F0GIE9_9BURK Unreviewed; 71 AA. AC F0GIE9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 22-JAN-2014, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN ORFNames=B1M_40143; OS Burkholderia sp. TJI49. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=987057; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TJI49; RA Khan A.U., Asif H., Azim M.K.; RT "Draft Genome sequence of Burkholderia sp. TJI49 isolated from mango RT (Mangifera indica) tree."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TJI49; RX PubMed=23653265; DOI=10.1007/s11274-013-1366-5; RA Khan A., Asif H., Studholme D.J., Khan I.A., Azim M.K.; RT "Genome characterization of a novel Burkholderia cepacia complex RT genomovar isolated from dieback affected mango orchards."; RL World J. Microbiol. Biotechnol. 29:2033-2044(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXE01002603; EGC98728.1; -; Genomic_DNA. DR EnsemblBacteria; EGC98728; EGC98728; B1M_40143. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; FT NON_TER 1 1 SQ SEQUENCE 71 AA; 7117 MW; 75B3F235A8AF281F CRC64; QGLARIARYA RFASARAPLV AIGGVGLEAL PAVLATGVGS VAVVSAVTGA ADYRAAIVAL QQCFAGEFDN R // ID F0GV99_9FIRM Unreviewed; 142 AA. AC F0GV99; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF9290_1192; OS Anaerococcus prevotii ACS-065-V-Col13. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Anaerococcus. OX NCBI_TaxID=879305; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-065-V-Col13; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXM01000013; EGC82309.1; -; Genomic_DNA. DR EnsemblBacteria; EGC82309; EGC82309; HMPREF9290_1192. DR PATRIC; 53483698; VBIAnaPre174396_0732. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 142 AA; 15250 MW; 031A1B4D8C463285 CRC64; MLIDDKAHLA WALGVGLHLG ADDMPVSLAR KLLGDKAIIG ATAKSVEAAT LSQNEGADYL GVGAIFETKT HVKTKITSVE TLKEIKKNVG IDVYAIGGLN IDNVDVLENS HVDGICVVRA IMDSDDVEND TRRLKEKINK IL // ID F0GVA0_9FIRM Unreviewed; 51 AA. AC F0GVA0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine-phosphate diphosphorylase domain protein; GN ORFNames=HMPREF9290_1193; OS Anaerococcus prevotii ACS-065-V-Col13. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Anaerococcus. OX NCBI_TaxID=879305; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-065-V-Col13; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXM01000013; EGC82227.1; -; Genomic_DNA. DR EnsemblBacteria; EGC82227; EGC82227; HMPREF9290_1193. DR PATRIC; 53483700; VBIAnaPre174396_0733. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 51 AA; 5957 MW; 7357A39536D686AE CRC64; MKKLYLVTNS DKYSEEEFLQ RVESALKGGV DILQLREKEK TDIEILELGK K // ID F0H1C6_9FIRM Unreviewed; 203 AA. AC F0H1C6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9246_0417; OS Anaerococcus hydrogenalis ACS-025-V-Sch4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Anaerococcus. OX NCBI_TaxID=879306; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-025-V-Sch4; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXN01000030; EGC83716.1; -; Genomic_DNA. DR EnsemblBacteria; EGC83716; EGC83716; HMPREF9246_0417. DR PATRIC; 46770663; VBIAnaHyd174097_1222. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 22541 MW; 9677BCC4708192C9 CRC64; MKKLYLVTNS DKYTEEEFLK RIEDAIKGGV DILQLREKEK TDLEILNLGK KVKKICDEYN IPMLIDDKPH LAWTLGCGLH VGADDMPISL CRKLLGEKAL IGATAKSVEA AKKAQEDGAN YLGVGAIFET KTHVKTKRTS VETFKKIKEA VDIDVYAIGG LNIENVEILK GSNTDGICVV RAIMDANDVY QTSLDLKEKI QEL // ID F0HE37_9FIRM Unreviewed; 209 AA. AC F0HE37; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9402_0559; OS Turicibacter sp. HGF1. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Turicibacter. OX NCBI_TaxID=910310; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGF1; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXQ01000051; EGC92469.1; -; Genomic_DNA. DR ProteinModelPortal; F0HE37; -. DR EnsemblBacteria; EGC92469; EGC92469; HMPREF9402_0559. DR PATRIC; 46780055; VBITurSp170039_1003. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22869 MW; DFBA31C800E4F83C CRC64; MKLNKQDLSL YLVTDRHWTK DQSLVEQVEA GLKGGVTMVQ LREKNLSDEE FLLKALELKE LTTTYKVPFM INDNVWVAIQ SDADGIHIGQ DDLPADEVRK LVGEEKILGV SVQTVEQAQI AKRQGADYLG VGAVFSTDTK KDAKHVPLQV LKEICEAVNL PVVAIGGIDE DNVDELTGSG ICGVAVVSAI LASDDIMQAA KNLKRDWVL // ID F0HJM3_9ACTN Unreviewed; 216 AA. AC F0HJM3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9404_3750; OS Eggerthella sp. HGA1. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Eggerthella. OX NCBI_TaxID=910311; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGA1; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXR01000007; EGC90518.1; -; Genomic_DNA. DR ProteinModelPortal; F0HJM3; -. DR EnsemblBacteria; EGC90518; EGC90518; HMPREF9404_3750. DR PATRIC; 46784373; VBIEggSp172060_0301. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22147 MW; 474E0E7B75D894D0 CRC64; MYPRENLRRA MALYAVTDRA WLGERTLSAC VEEALAGGAT FVQLREKDAP QAEVVLRARA LAPLCREAGV PFVVDDDVEA ARIAGVDGVH VGQDDAACVE AREKLGPDAI VGVSVQTVEQ ALVAQADGAD YLGVGAVFGT PTKPDAADVG TDGLAAICAA VDIPVVAIGG LNERTIPELA GTGADGAAVV SAIFAAEDIE EETRRLRAAV QAALGA // ID F0HNK7_9ACTN Unreviewed; 211 AA. AC F0HNK7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF9404_5021; OS Eggerthella sp. HGA1. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Eggerthella. OX NCBI_TaxID=910311; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGA1; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXR01000018; EGC89040.1; -; Genomic_DNA. DR EnsemblBacteria; EGC89040; EGC89040; HMPREF9404_5021. DR PATRIC; 46786704; VBIEggSp172060_1428. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 211 AA; 22505 MW; 5E8E6D6EB3961841 CRC64; MFACEPSAAD PTFRRVFVTD RLRCALPLPQ QTAFLAESGA IDAVILREKD LDDAAYELLA AEMAAVCARC GIAFVAHAHV EAARRLGCAA VHLPLPLLRA QGRPDGFAWV GTNVHEADEV AEAEVLGADV LVASPVFAPS CKPASTARGL PFLRAVLDRA HAPVFALGGI TDENERLIRE AGAAGACRMA DYARRRGVRQ AAPCKYERSR G // ID F0J0V8_ACIMA Unreviewed; 200 AA. AC F0J0V8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=ACMV_22970; OS Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / AIU301). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=926570; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11245 / JCM 8867 / AIU301; RA Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., RA Nakazawa H., Hosoyama A., Yamada R., Fujita N.; RT "Whole genome sequence of Acidiphilium multivorum AIU301."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012035; BAJ81644.1; -; Genomic_DNA. DR RefSeq; YP_004284526.1; NC_015186.1. DR EnsemblBacteria; BAJ81644; BAJ81644; ACMV_22970. DR GeneID; 10319509; -. DR KEGG; amv:ACMV_22970; -. DR PATRIC; 46813496; VBIAciMul178205_2698. DR KO; K00788; -. DR BioCyc; AMUL926570:GI8V-2336-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 200 AA; 21112 MW; 7946104C30CFD04C CRC64; MDEQLIAAAR AVKRRRRCRH PTLWLFTDRA RLPDPLGAIA RLPPGLSGVV LRDDAAPDRA ALAAAVAKLC RRRRIALVVA GDARLAARLH AGLHLRRGRV APGRKPGLVT ASAHGRQELV RARRAGAGLV FLSPAFPTAS HPGAPALGPV RWAALARLAG GVQVVALGGI EGRRMRALGP ACRGVAAIGA LSNQCHTVWR // ID F0J3G3_ACIMA Unreviewed; 206 AA. AC F0J3G3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ACMV_04720; OS Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / AIU301). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=926570; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11245 / JCM 8867 / AIU301; RA Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., RA Nakazawa H., Hosoyama A., Yamada R., Fujita N.; RT "Whole genome sequence of Acidiphilium multivorum AIU301."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012035; BAJ79819.1; -; Genomic_DNA. DR RefSeq; YP_004282701.1; NC_015186.1. DR EnsemblBacteria; BAJ79819; BAJ79819; ACMV_04720. DR GeneID; 10320658; -. DR KEGG; amv:ACMV_04720; -. DR PATRIC; 46809664; VBIAciMul178205_0826. DR KO; K00788; -. DR BioCyc; AMUL926570:GI8V-481-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21659 MW; 39F5FAED8554DEC5 CRC64; MTELYLITPP RLGPDFADAL AAALDAGPVA CIQLRLKEAG ADEMRRAIDA LRPVAQSRGV AFLLNDDPRL AVETGCDGAH LGQDDLAAHG GLARVRRVLD GLSLGITCHD SRHLAMEAAE QGADYVAFGA FYPTGTKEPK ARADVEILRW WSELMEVPCV AIGGITPGNA APLVEAGADF LAVVGAVWQH PDGPAAGVRA FRAELA // ID F0JGA4_DESDE Unreviewed; 212 AA. AC F0JGA4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DND132_0636; OS Desulfovibrio desulfuricans ND132. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=641491; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ND132; RX PubMed=21357488; DOI=10.1128/JB.00170-11; RA Brown S.D., Gilmour C.C., Kucken A.M., Wall J.D., Elias D.A., RA Brandt C.C., Podar M., Chertkov O., Held B., Bruce D.C., Detter J.C., RA Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Woyke T., RA Mikhailova N., Ivanova N.N., Han J., Lucas S., Lapidus A.L., RA Land M.L., Hauser L.J., Palumbo A.V.; RT "Genome sequence of the mercury-methylating strain Desulfovibrio RT desulfuricans ND132."; RL J. Bacteriol. 193:2078-2079(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003220; EGB13852.1; -; Genomic_DNA. DR RefSeq; YP_005166656.1; NC_016803.1. DR EnsemblBacteria; EGB13852; EGB13852; DND132_0636. DR GeneID; 11740554; -. DR KEGG; ddn:DND132_0636; -. DR PATRIC; 46635161; VBIDesSp116210_0650. DR KO; K00788; -. DR BioCyc; DDES641491:GH21-654-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22401 MW; 62F92EBEADEF6A4A CRC64; MRTEDLLVYL VTDRSLCRGR SLEEVVAQAA EGGCTMVQLR EKEADTGEFV ELARALHRLL KPLSIPLLIN DRVDVALAAG VEGVHVGQSD MLPEDVRRII GPDAILGLSV DTEAELLDAQ NRPVDYLGIG PAYPTLTKKD VKGTPWGPEG LRRAVGQSAI PLVAIGGVQR DNVRAVAGSG VAGIAVVSAI CSAPSPAEAA RELAYAMKEG TR // ID F0JHL9_DESDE Unreviewed; 216 AA. AC F0JHL9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DND132_0864; OS Desulfovibrio desulfuricans ND132. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=641491; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ND132; RX PubMed=21357488; DOI=10.1128/JB.00170-11; RA Brown S.D., Gilmour C.C., Kucken A.M., Wall J.D., Elias D.A., RA Brandt C.C., Podar M., Chertkov O., Held B., Bruce D.C., Detter J.C., RA Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Woyke T., RA Mikhailova N., Ivanova N.N., Han J., Lucas S., Lapidus A.L., RA Land M.L., Hauser L.J., Palumbo A.V.; RT "Genome sequence of the mercury-methylating strain Desulfovibrio RT desulfuricans ND132."; RL J. Bacteriol. 193:2078-2079(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003220; EGB14079.1; -; Genomic_DNA. DR RefSeq; YP_005166883.1; NC_016803.1. DR EnsemblBacteria; EGB14079; EGB14079; DND132_0864. DR GeneID; 11743043; -. DR KEGG; ddn:DND132_0864; -. DR PATRIC; 46635656; VBIDesSp116210_0889. DR KO; K00788; -. DR BioCyc; DDES641491:GH21-890-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23594 MW; D07B880F2A18A65D CRC64; MTITRHNILD TDLYCLTAEK FSLGRSNVEV VRQMLDAGIK LVQYREKEKK AGAKLEECRA IREMTREAGA AFIVNDDIDI AILVGADGVH VGQEDLPVEC VRRLVGPDMA IGLSTHSPEQ AREAVRCGAD YIGVGPIFRT YTKDDVVDPV GFEYLDWVVA HLDIPFVAIG GIKEHNLGEV VRHGARCAAL VTEIVGGANI ADTITALRHQ MDAAKE // ID F0JWW7_ESCFE Unreviewed; 193 AA. AC F0JWW7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECD227_3372; OS Escherichia fergusonii ECD227. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=981367; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ECD227; RA Forgetta V., Rempel H., Malouin F., Vaillancourt R.Jr., Dewar K., RA Diarra M.S.; RT "Genomic Characterization of a Multi-drug Resistant E. fergusonii RT Isolate from a Healthy Broiler Chicken."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001142; EGC97134.1; -; Genomic_DNA. DR EnsemblBacteria; EGC97134; EGC97134; ECD227_3372. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 19 23 HMP-PP binding (By similarity). FT REGION 116 118 THZ-P binding (By similarity). FT REGION 168 169 THZ-P binding (By similarity). FT METAL 52 52 Magnesium (By similarity). FT METAL 71 71 Magnesium (By similarity). FT BINDING 51 51 HMP-PP (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 193 AA; 21088 MW; 7216D7940EEED950 CRC64; MDSVQWIERL LDAGVRTLQL RIKDRRDEEV EADVVAAIAL GRRYNARLFI NDYWRLAIKH QAYGVHLGQE DLQATDLSAI RAAGLRLGVS THDDMEIDVA LAARPSYIAL GHVFPTQTKQ MPSAPQGLEQ LARHIERLAD YPTVAIGGIS LPRAPAVMAT GVGSIAVVSA ITQDADWRLA TEQLLEIAGV GDE // ID F0K5I5_CLOAE Unreviewed; 195 AA. AC F0K5I5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine monophosphate synthase; GN Name=tenI; OrderedLocusNames=CEA_G2927; OS Clostridium acetobutylicum (strain EA 2018). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=863638; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EA 2018; RX PubMed=21284892; DOI=10.1186/1471-2164-12-93; RA Hu S., Zheng H., Gu Y., Zhao J., Zhang W., Yang Y., Wang S., Zhao G., RA Yang S., Jiang W.; RT "Comparative genomic and transcriptomic analysis revealed genetic RT characteristics related to solvent formation and xylose utilization in RT Clostridium acetobutylicum EA 2018."; RL BMC Genomics 12:93-93(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002118; ADZ21964.1; -; Genomic_DNA. DR RefSeq; YP_005672059.1; NC_017295.1. DR ProteinModelPortal; F0K5I5; -. DR EnsemblBacteria; ADZ21964; ADZ21964; CEA_G2927. DR GeneID; 12233675; -. DR KEGG; cay:CEA_G2927; -. DR PATRIC; 47112847; VBICloAce167171_2956. DR KO; K00788; -. DR OMA; AGHIFET; -. DR BioCyc; CACE863638:GLBA-3003-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 195 AA; 21204 MW; A665BB197818F6B9 CRC64; MIYVVTNRKL AKNKDLLGCV EKVLKYGACS VILREKDLGY DELYEIAKKI KFITDKHSAK LIVNGSLRVA EEVKAYAYHS SFVNFINNGG SKIIKNGVSI HSLEEAKRAE ENGADYVLAG NIYETACKPG LKGRGLEFVN SISKNITIPE IAIGGISEEN VQELINSGAN GAAVMSSAMK NPAVIKKIIG KLNKK // ID F0K5T4_CLOAE Unreviewed; 211 AA. AC F0K5T4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CEA_G0506; OS Clostridium acetobutylicum (strain EA 2018). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=863638; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EA 2018; RX PubMed=21284892; DOI=10.1186/1471-2164-12-93; RA Hu S., Zheng H., Gu Y., Zhao J., Zhang W., Yang Y., Wang S., Zhao G., RA Yang S., Jiang W.; RT "Comparative genomic and transcriptomic analysis revealed genetic RT characteristics related to solvent formation and xylose utilization in RT Clostridium acetobutylicum EA 2018."; RL BMC Genomics 12:93-93(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002118; ADZ19545.1; -; Genomic_DNA. DR RefSeq; YP_005669640.1; NC_017295.1. DR ProteinModelPortal; F0K5T4; -. DR EnsemblBacteria; ADZ19545; ADZ19545; CEA_G0506. DR GeneID; 12234465; -. DR KEGG; cay:CEA_G0506; -. DR PATRIC; 47107867; VBICloAce167171_0519. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; CACE863638:GLBA-542-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23159 MW; 8857F93D17AAFCA6 CRC64; MKNVDYKLYL VTDRKVLKER DLYKSIEEAI KGGVTLVQLR EKEMSTLDFY ESALKLKKIT ETYKIPLIIN DRIDIALAIN ADGVHIGQSD MPLIKARELL GKDKIIGVSA HSIEEALEAE RNGATYLGVG AIYNTSTKGD AQAVSLEELK NIKNSVKIPV VGIGGINEEN ANKVIETGVD GISVISGILS AQKIKDKARV MFDIVKKNST K // ID F0KJ37_ACICP Unreviewed; 299 AA. AC F0KJ37; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Putative bifunctional protein; GN OrderedLocusNames=BDGL_001778; OS Acinetobacter calcoaceticus (strain PHEA-2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=871585; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PHEA-2; RA Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.; RT "The genome sequence of a nonpathogenic wastewater-adapted bacterium RT Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights RT into environmental adaptation."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PHEA-2; RX PubMed=21441526; DOI=10.1128/JB.00261-11; RA Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z., RA Yuan M., Zhou Z., Elmerich C., Lin M.; RT "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from RT industry wastewater."; RL J. Bacteriol. 193:2672-2673(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002177; ADY82364.1; -; Genomic_DNA. DR RefSeq; YP_004996046.1; NC_016603.1. DR ProteinModelPortal; F0KJ37; -. DR EnsemblBacteria; ADY82364; ADY82364; BDGL_001778. DR GeneID; 11639965; -. DR KEGG; acc:BDGL_001778; -. DR PATRIC; 47081652; VBIAciCal168233_1773. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; ACAL871585:GH86-1796-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 299 AA; 34282 MW; 839EFDE13C857B8A CRC64; MLKPIVDVAI AILIHRGKIL VGWREEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWAWYTREQL LHLNFPKANK DIIKRLYWPH LIKISNTLSM VESSEALLYW RIENEAEQQY IEQLTALDEG QRSSLIINVD IWWQLSPELQ KQIKTVHLKQ SQLMNLHKGD LTVGVRYIAA CHDAVSLKQA QQIGCDAVFI SPVKSTTTHP EAVALGWERF SDLAQNSQIP VFALGGVHPD DLATAQQHGA YGLAGIRNF // ID F0KKF6_ACICP Unreviewed; 203 AA. AC F0KKF6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BDGL_001933; OS Acinetobacter calcoaceticus (strain PHEA-2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=871585; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PHEA-2; RA Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.; RT "The genome sequence of a nonpathogenic wastewater-adapted bacterium RT Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights RT into environmental adaptation."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PHEA-2; RX PubMed=21441526; DOI=10.1128/JB.00261-11; RA Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z., RA Yuan M., Zhou Z., Elmerich C., Lin M.; RT "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from RT industry wastewater."; RL J. Bacteriol. 193:2672-2673(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002177; ADY82519.1; -; Genomic_DNA. DR RefSeq; YP_004996201.1; NC_016603.1. DR EnsemblBacteria; ADY82519; ADY82519; BDGL_001933. DR GeneID; 11640125; -. DR KEGG; acc:BDGL_001933; -. DR PATRIC; 47081985; VBIAciCal168233_1932. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; ACAL871585:GH86-1956-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21755 MW; 7DDE5FF7EC2C635C CRC64; MRGLYLITND DPIQLLLEKL DAALATRQVA ILQYRRKKID KADQPAEVEQ IKLLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YIAFGAVYAT STKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKSVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID F0KXZ4_YERE3 Unreviewed; 223 AA. AC F0KXZ4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=YE105_C0294; OS Yersinia enterocolitica subsp. palearctica serotype O:9 / biotype 3 OS (strain 105.5R(r)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=994476; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=105.5R(r); RX PubMed=21325549; DOI=10.1128/JCM.01921-10; RA Wang X., Li Y., Jing H., Ren Y., Zhou Z., Wang S., Kan B., Xu J., RA Wang L.; RT "Complete genome sequence of a Yersinia enterocolitica "Old World" RT (3/O:9) strain and comparison with the "New World" (1B/O:8) strain."; RL J. Clin. Microbiol. 49:1251-1259(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002246; ADZ40792.1; -; Genomic_DNA. DR RefSeq; YP_004296495.1; NC_015224.1. DR EnsemblBacteria; ADZ40792; ADZ40792; YE105_C0294. DR GeneID; 10300130; -. DR KEGG; yep:YE105_C0294; -. DR PATRIC; 47212105; VBIYerEnt184081_0311. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; YENT994476:GHRB-320-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24371 MW; 73F1F69E77A483AC CRC64; MKPSDTPIFS AQKGFPTTEQ RLGLYPVVDS VLWIERLLAL GVTTIQLRIK ELDEAQVEQD IVAAIELGKR YQARLFINDY WRLAIKHGAY GVHLGQEDLE STDLAAIQQA GLRLGVSTHD EYELAIAKAV RPSYIAMGHI FPTQTKQMPS SPQGLAVLKQ MVENTPDYPT VAIGGISIER VPAVLATGVG SVAVVSAITQ AEDWQQATAQ LLHLIEGKEL ADE // ID F0LBE6_AGRSH Unreviewed; 220 AA. AC F0LBE6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AGROH133_11114; OS Agrobacterium sp. (strain H13-3) (Rhizobium lupini (strain H13-3)). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=861208; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H13-3; RX PubMed=21329740; DOI=10.1016/j.jbiotec.2011.01.010; RA Wibberg D., Blom J., Jaenicke S., Kollin F., Rupp O., Scharf B., RA Schneiker-Bekel S., Sczcepanowski R., Goesmann A., Setubal J.C., RA Schmitt R., Puhler A., Schluter A.; RT "Complete genome sequencing of Agrobacterium sp. H13-3, the former RT Rhizobium lupini H13-3, reveals a tripartite genome consisting of a RT circular and a linear chromosome and an accessory plasmid but lacking RT a tumor-inducing Ti-plasmid."; RL J. Biotechnol. 155:50-62(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002249; ADY66454.1; -; Genomic_DNA. DR RefSeq; YP_004443545.1; NC_015508.1. DR EnsemblBacteria; ADY66454; ADY66454; AGROH133_11114. DR GeneID; 10582430; -. DR KEGG; agr:AGROH133_11114; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; ASP861208:GH59-3504-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22743 MW; 2CCACEEF56D1A352 CRC64; MNKVDYRLNA LVDASLGDVA PLGELALAAA LNGATILQYR DKHASTREMI ENASAIREAI AGTGVPLVIN DRVDVALASG ADGVHLGADD MDAKTARRIL GDKAIIGLTV KNRADGERAA SMPADYACIG GVFETVSKVN PDKPVGLDGF TTLRTLLREL RPGMPVGAIA GIDLARVPNV IAAGADGVAV ISAIFRAGDI ASTTRDFRAA VDAALKARQS // ID F0LCP8_AGRSH Unreviewed; 221 AA. AC F0LCP8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 20. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=AGROH133_12107; OS Agrobacterium sp. (strain H13-3) (Rhizobium lupini (strain H13-3)). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=861208; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H13-3; RX PubMed=21329740; DOI=10.1016/j.jbiotec.2011.01.010; RA Wibberg D., Blom J., Jaenicke S., Kollin F., Rupp O., Scharf B., RA Schneiker-Bekel S., Sczcepanowski R., Goesmann A., Setubal J.C., RA Schmitt R., Puhler A., Schluter A.; RT "Complete genome sequencing of Agrobacterium sp. H13-3, the former RT Rhizobium lupini H13-3, reveals a tripartite genome consisting of a RT circular and a linear chromosome and an accessory plasmid but lacking RT a tumor-inducing Ti-plasmid."; RL J. Biotechnol. 155:50-62(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002249; ADY66858.1; -; Genomic_DNA. DR RefSeq; YP_004443949.1; NC_015508.1. DR EnsemblBacteria; ADY66858; ADY66858; AGROH133_12107. DR GeneID; 10582836; -. DR KEGG; agr:AGROH133_12107; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR BioCyc; ASP861208:GH59-3911-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23398 MW; 1B629D1250FF8F13 CRC64; MDEPMTKVDN RCRLVLIVPQ LDDAQKQATE LQEALRGGDV ASVIIPQYDL DDATFQKRAE LIVPMVQEAG AAALIAGDSR VASRVKADGL HVAGNAEALA EAVENFAPKL IVGGGNADDR HKALEMGESN PDYVFFGKLE GDIKPEAHPK NLALGEWWAS MIEIPSIVMG GTDISSVVAV AEAGVEFVAM RSGVFDNASG AAQAVSEINA LLDEKAPRFD G // ID F0LJU7_THEBM Unreviewed; 209 AA. AC F0LJU7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TERMP_00507; OS Thermococcus barophilus (strain DSM 11836 / MP). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=391623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11836 / MP; RX PubMed=21217005; DOI=10.1128/JB.01490-10; RA Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.; RT "Complete genome sequence of the hyperthermophilic, piezophilic, RT heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus RT MP."; RL J. Bacteriol. 193:1481-1482(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002372; ADT83484.1; -; Genomic_DNA. DR RefSeq; YP_004070707.1; NC_014804.1. DR ProteinModelPortal; F0LJU7; -. DR EnsemblBacteria; ADT83484; ADT83484; TERMP_00507. DR GeneID; 10040825; -. DR KEGG; tba:TERMP_00507; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GLGPICH; -. DR BioCyc; TBAR391623:GH3I-521-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22830 MW; 939440A88FF3933D CRC64; MNLKKRLRLY VITDRRLRDE IETTKAALEG GATAIQMRIK NAPTGEMVRV GKELRKITKE YGALFFVDDR LDVALAVDAD GVQLGPEDMP VYIARELAPN LIIGASVYSL EEALKAEREK ADYLGAGSVF PTKTKKDARV LGLEGLKKVV ESVKIPVVAI GGINHENVRK VLEIGVDGIA VISAIVGAED VKKAAEEMRR IIDEYLGGE // ID F0LQJ7_VIBFN Unreviewed; 400 AA. AC F0LQJ7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=vfu_A00369; OS Vibrio furnissii (strain DSM 14383 / NCTC 11218). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=903510; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14383 / NCTC 11218; RX PubMed=21217006; DOI=10.1128/JB.01512-10; RA Lux T.M., Lee R., Love J.; RT "Complete genome sequence of a free-living Vibrio furnissii sp. nov. RT strain (NCTC 11218)."; RL J. Bacteriol. 193:1487-1488(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002377; ADT85591.1; -; Genomic_DNA. DR RefSeq; YP_004991603.1; NC_016602.1. DR EnsemblBacteria; ADT85591; ADT85591; vfu_A00369. DR GeneID; 11636262; -. DR KEGG; vfu:vfu_A00369; -. DR PATRIC; 45424921; VBIVibFur169925_0347. DR KO; K00788; -. DR BioCyc; VFUR903510:GHFS-384-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 400 AA; 44481 MW; 0BC40CD15149BAE0 CRC64; MKLLIPSQCI ELTGDVQRVL LLAEQQGFAI GHIELGVSPT PDLQLVGDTT LRLSCNWFPH VQPDADWVLY YGGVADDCAS TAMHDRWIFI GDEHQGRVTD HWQHSDEVRY LLQVTPLEPR DYGRHLAWVL ACLSLDFPIE DALVLSRAAL NVSRETWPSD YRHFPQPRTQ AEFSAFPTLK SASLGVYPVV DDVRWIAQLL PLGITTIQLR IKDSHQADLE QQVMEAIRLG REFGAQVFIN DYWQLAVKHG AYGVHLGQED LQTVDLKMLS DNNLRLGLST HGYFELLRIH QLAPSYIALG HIFPTTTKQM PSKPQGLVRL ALYQRLLDSM PYGDTTGVPS VAIGGIDALN AEHVLACGVT SIAVVRAITE AKDVAVATHT LQHILALSLA STKERNHVVG // ID F0LRN3_VIBFN Unreviewed; 215 AA. AC F0LRN3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=vfu_A01489; OS Vibrio furnissii (strain DSM 14383 / NCTC 11218). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=903510; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14383 / NCTC 11218; RX PubMed=21217006; DOI=10.1128/JB.01512-10; RA Lux T.M., Lee R., Love J.; RT "Complete genome sequence of a free-living Vibrio furnissii sp. nov. RT strain (NCTC 11218)."; RL J. Bacteriol. 193:1487-1488(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002377; ADT86662.1; -; Genomic_DNA. DR RefSeq; YP_004992674.1; NC_016602.1. DR EnsemblBacteria; ADT86662; ADT86662; vfu_A01489. DR GeneID; 11635444; -. DR KEGG; vfu:vfu_A01489; -. DR PATRIC; 45427199; VBIVibFur169925_1431. DR KO; K00788; -. DR BioCyc; VFUR903510:GHFS-1494-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23033 MW; 279B2FB1AE3ADAE8 CRC64; MTPYTLYLVT DDQQDLSTLC HVVQQAIAGG VSLVQVREKQ GDVRTFIERA AAVKAMLSGS GVPLIINDRV DVALAVDADG VHLGQSDMPA TLARQLLGPD KLIGLSVENE QQFEQAQSLP VDYLGLSAIF ATPTKTNTVK HWGLDGLNWA MARSRLPMVA IGGLNTSNIA AVAQTGVQGI ALVSAISHAR DPQQAARDLR LLIEQNRPAS LVRNY // ID F0M8A2_ARTPP Unreviewed; 246 AA. AC F0M8A2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Asphe3_26450; OS Arthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG OS 23796 / Sphe3). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=930171; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3; RX PubMed=21677849; DOI=10.4056/sigs.1393494; RA Kallimanis A., Labutti K.M., Lapidus A., Clum A., Lykidis A., RA Mavromatis K., Pagani I., Liolios K., Ivanova N., Goodwin L., RA Pitluck S., Chen A., Palaniappan K., Markowitz V., Bristow J., RA Velentzas A.D., Perisynakis A., Ouzounis C.C., Kyrpides N.C., RA Koukkou A.I., Drainas C.; RT "Complete genome sequence of Arthrobacter phenanthrenivorans type RT strain (Sphe3)."; RL Stand. Genomic Sci. 4:123-130(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002379; ADX73765.1; -; Genomic_DNA. DR RefSeq; YP_004241899.1; NC_015145.1. DR EnsemblBacteria; ADX73765; ADX73765; Asphe3_26450. DR GeneID; 10286012; -. DR KEGG; apn:Asphe3_26450; -. DR PATRIC; 46863658; VBIArtPhe178037_2620. DR KO; K00788; -. DR BioCyc; APHE930171:GJHZ-2637-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 61 65 HMP-PP binding (By similarity). FT REGION 163 165 THZ-P binding (By similarity). FT METAL 94 94 Magnesium (By similarity). FT METAL 113 113 Magnesium (By similarity). FT BINDING 93 93 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 166 166 HMP-PP (By similarity). FT BINDING 201 201 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 246 AA; 25258 MW; E84224382EDDFD53 CRC64; MNVSPSPAAS HVPGTDAFIN AEGSAGLQAA RLYLCTDARR DRGDFEQFVD AAFAGGVDII QLRDKSIEAA EELELLALLK EAAVRHGRLW AVNDRADIAV LSGAPVFHIG QKDLPLNAAR TLLNGNAAIG LSSHSPEQVD AALAAAAGPA ALDYFCVGPL WATPTKPGRA AVGLDLVKYA AAAAGRQEES DGGVPWFAIG GIDHGNVEQV VEAGASRIVV VRAITEADEP AAAAASLLAA LDAARP // ID F0MGL3_NEIMG Unreviewed; 205 AA. AC F0MGL3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NMBG2136_1970; OS Neisseria meningitidis serogroup B (strain G2136). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935599; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G2136; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002419; ADY94616.1; -; Genomic_DNA. DR RefSeq; YP_005894788.1; NC_017513.1. DR ProteinModelPortal; F0MGL3; -. DR EnsemblBacteria; ADY94616; ADY94616; NMBG2136_1970. DR GeneID; 12411610; -. DR KEGG; nmd:NMBG2136_1970; -. DR PATRIC; 47148136; VBINeiMen175532_2647. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21654 MW; 28E6A2E0137A5C49 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGDELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAE NPEAVVKAFQ ALWDG // ID F0MT96_NEIMM Unreviewed; 205 AA. AC F0MT96; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NMBM01240149_0112; OS Neisseria meningitidis serogroup B (strain M01-240149). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M01-240149; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002421; ADY96747.1; -; Genomic_DNA. DR RefSeq; YP_005894958.1; NC_017514.1. DR EnsemblBacteria; ADY96747; ADY96747; NMBM01240149_0112. DR GeneID; 12411793; -. DR KEGG; nmm:NMBM01240149_0112; -. DR PATRIC; 47154579; VBINeiMen175098_0144. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; NMEN935591:GLHR-112-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21547 MW; 259C693BD81A50FB CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKAL HGDELKREIA RCVAACQGSH TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID F0MW16_NEIMP Unreviewed; 205 AA. AC F0MW16; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NMBM01240355_2004; OS Neisseria meningitidis serogroup B (strain M01-240355). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935588; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M01-240355; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002422; ADZ00472.1; -; Genomic_DNA. DR RefSeq; YP_005902590.1; NC_017517.1. DR EnsemblBacteria; ADZ00472; ADZ00472; NMBM01240355_2004. DR GeneID; 12493267; -. DR KEGG; nms:NMBM01240355_2004; -. DR PATRIC; 47165818; VBINeiMen181352_2743. DR KO; K00788; -. DR BioCyc; NMEN935588:GLHS-2004-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21752 MW; 157E6726F1A9AE5C CRC64; MTFLPLKSPL KFYAVVPTAD WVERMVEAGA DTVQLRCKAL HGDELKREIA RCAAACRGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLEKLREYV KQAGSTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID F0N0U8_NEIMO Unreviewed; 205 AA. AC F0N0U8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NMBM04240196_2011; OS Neisseria meningitidis serogroup B (strain M04-240196). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935593; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M04-240196; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002423; ADZ02426.1; -; Genomic_DNA. DR RefSeq; YP_005898665.1; NC_017515.1. DR EnsemblBacteria; ADZ02426; ADZ02426; NMBM04240196_2011. DR GeneID; 12489080; -. DR KEGG; nmq:NMBM04240196_2011; -. DR PATRIC; 47171697; VBINeiMen179694_2683. DR KO; K00788; -. DR BioCyc; NMEN935593:GLHT-2010-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21708 MW; C441B54399455D54 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGDELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAE EVLATGVSSL AVVRAVTEAA NPEAVVKAFQ ALWDG // ID F0NB55_NEIMN Unreviewed; 205 AA. AC F0NB55; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NMBNZ0533_2002; OS Neisseria meningitidis serogroup B (strain NZ-05/33). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=935589; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NZ-05/33; RX PubMed=21368196; DOI=10.1073/pnas.1019751108; RA Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., RA Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., RA Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.; RT "Neisseria meningitidis is structured in clades associated with RT restriction modification systems that modulate homologous RT recombination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002424; ADZ04373.1; -; Genomic_DNA. DR RefSeq; YP_005904544.1; NC_017518.1. DR EnsemblBacteria; ADZ04373; ADZ04373; NMBNZ0533_2002. DR GeneID; 12495359; -. DR KEGG; nmz:NMBNZ0533_2002; -. DR PATRIC; 47177543; VBINeiMen179262_2671. DR KO; K00788; -. DR BioCyc; NMEN935589:GLHU-2001-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21547 MW; 259C693BD81A50FB CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKAL HGDELKREIA RCVAACQGSH TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLCEYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID F0NY94_WEEVC Unreviewed; 219 AA. AC F0NY94; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Weevi_1390; OS Weeksella virosa (strain ATCC 43766 / DSM 16922 / JCM 21250 / NBRC OS 16016 / NCTC 11634 / CL345/78). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Weeksella. OX NCBI_TaxID=865938; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 / RC CL345/78; RX DOI=10.4056/sigs.1603927; RA Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S., RA Nolan M., Cheng J., Pitluck S., Liolios K., Pagani I., Mikhailova N., RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., RA Brambilla E., Kopitz M., Rohde M., Goker M., Tindall B., Detter J., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Klenk H., RA Kyrpides N.; RT "Complete genome sequence of Weeksella virosa type strain (9751T)."; RL Stand. Genomic Sci. 4:81-90(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002455; ADX68091.1; -; Genomic_DNA. DR RefSeq; YP_004238669.1; NC_015144.1. DR EnsemblBacteria; ADX68091; ADX68091; Weevi_1390. DR GeneID; 10282632; -. DR KEGG; wvi:Weevi_1390; -. DR PATRIC; 47060211; VBIWeeVir165365_1414. DR KO; K00788; -. DR BioCyc; WVIR865938:GHXX-1441-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24253 MW; 676765D92FD9180C CRC64; MKINPTFPYP LYLVISEKDC KYLHWLDVAE QAIIGGVDII QLREKNCSVG EYISKATLLK NITDHYNIPL IINDSLEVAT AVDSWGIHVG QADISPSKIK KNTQALKHIG WSLENIKQLD DDEMKYVHHL GVSPIFSTPT KTNTITEWGF DGLKFLKTKT SKPLIAIGGI NESNIAKIIQ AGADSVAIVS AICGSKNPKK STQILKQIIN NNEYHAKTL // ID F0P4E4_STAPE Unreviewed; 212 AA. AC F0P4E4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPSE_0735; OS Staphylococcus pseudintermedius (strain ED99). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=984892; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ED99; RX PubMed=21398539; DOI=10.1128/JB.00137-11; RA Zakour N.L., Bannoehr J., van den Broek A.H., Thoday K.L., RA Fitzgerald J.R.; RT "Complete Genome Sequence of the Canine Pathogen Staphylococcus RT pseudintermedius."; RL J. Bacteriol. 193:2363-2364(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002478; ADX76055.1; -; Genomic_DNA. DR RefSeq; YP_006014894.1; NC_017568.1. DR EnsemblBacteria; ADX76055; ADX76055; SPSE_0735. DR GeneID; 12610497; -. DR KEGG; sdt:SPSE_0735; -. DR PATRIC; 47203368; VBIStaPse182428_0694. DR KO; K00788; -. DR BioCyc; SPSE984892:GLKW-722-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23640 MW; 619F0627042FA122 CRC64; MTFNRKQLRV YFIAGTQDVK QGSLDGILKE ALEAGITMYQ FREKGSSSLQ GEEKTAMAVR LRDLCRHYQV PFIVNDDVDL AIEIDADGIH VGQEDAKVQS FQHLLEDKII GLSVGSFEEY DQSDLTNVDY IGVGPVYETS SKLDASKPGG IRLIRRMREY DENIPMVAIG GITEENVAPL LKNGADGIAT ISSITHSTDI EKSVKRYLQY FK // ID F0P9C4_STAPE Unreviewed; 195 AA. AC F0P9C4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 23. DE SubName: Full=Thiamine monophosphate synthase, putative; GN OrderedLocusNames=SPSE_2079; OS Staphylococcus pseudintermedius (strain ED99). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=984892; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ED99; RX PubMed=21398539; DOI=10.1128/JB.00137-11; RA Zakour N.L., Bannoehr J., van den Broek A.H., Thoday K.L., RA Fitzgerald J.R.; RT "Complete Genome Sequence of the Canine Pathogen Staphylococcus RT pseudintermedius."; RL J. Bacteriol. 193:2363-2364(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002478; ADX77318.1; -; Genomic_DNA. DR RefSeq; YP_006016157.1; NC_017568.1. DR EnsemblBacteria; ADX77318; ADX77318; SPSE_2079. DR GeneID; 12611820; -. DR KEGG; sdt:SPSE_2079; -. DR PATRIC; 47205979; VBIStaPse182428_1951. DR KO; K10810; -. DR BioCyc; SPSE984892:GLKW-2045-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 195 AA; 21913 MW; B6A66E93FC70B174 CRC64; MIVITPYVVL DDWHIKRLCV IESQIAGVIL RTPMNRHALK QWLIQLLANG FPKSKVIIHT DVTLAMELSI SNVHFKEGDH RATLLKQVQP HYQVSMSTHS AAMVRDAKAQ QLDFVLFGHL FPTSSKPDLP PRTQLEVDEV LAIDFPVVAL GGITADTVQQ ISSHFTGIAC MSSAFGYELQ SFEKMVDYWS LKKVK // ID F0PDG3_ENTF6 Unreviewed; 207 AA. AC F0PDG3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EF62_2928; OS Enterococcus faecalis (strain 62). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=936153; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=62; RX PubMed=21398545; DOI=10.1128/JB.00183-11; RA Brede D.A., Snipen L.G., Ussery D.W., Nederbragt A.J., Nes I.F.; RT "Complete genome sequence of the commensal Enterococcus faecalis 62, RT isolated from a healthy Norwegian infant."; RL J. Bacteriol. 193:2377-2378(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002491; ADX81136.1; -; Genomic_DNA. DR RefSeq; YP_005706869.1; NC_017312.1. DR EnsemblBacteria; ADX81136; ADX81136; EF62_2928. DR GeneID; 12292051; -. DR KEGG; efl:EF62_2928; -. DR PATRIC; 47120843; VBIEntFae176554_2867. DR KO; K00788; -. DR BioCyc; EFAE936153:GLCR-2915-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 179 180 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 159 159 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22340 MW; 828430709C77D05B CRC64; MKVYLVTGRY DFSDTEFLNR IETACRSGVT LVQLREKEVS TRRFYELAVK VKAVTDAYQI PLIINDRVDI CLAVDAAGVH IGDDELPVAL VRKLVGSTKI VGVSAKTVAR GVEAENEGAD YLGVGAIFPT TTKDSPLTSL QTLSEIAAAV TIPVVAIGGI KEENIEQLMG TGVAGVSLVS EIMLAEQITE KVQGLMRVTE RMLEARK // ID F0PJN0_BACT0 Unreviewed; 206 AA. AC F0PJN0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Transcriptional regulator TenI; GN OrderedLocusNames=YBT020_03925; OS Bacillus thuringiensis subsp. finitimus (strain YBT-020). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=930170; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YBT-020; RX PubMed=21398543; DOI=10.1128/JB.00267-11; RA Zhu Y., Shang H., Zhu Q., Ji F., Wang P., Fu J., Deng Y., Xu C., RA Ye W., Zheng J., Zhu L., Ruan L., Peng D., Sun M.; RT "Complete genome sequence of Bacillus thuringiensis serovar finitimus RT strain YBT-020."; RL J. Bacteriol. 193:2379-2380(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002508; ADY20031.1; -; Genomic_DNA. DR RefSeq; YP_005564449.1; NC_017200.1. DR EnsemblBacteria; ADY20031; ADY20031; YBT020_03925. DR GeneID; 12184190; -. DR KEGG; btf:YBT020_03925; -. DR PATRIC; 47087239; VBIBacThu177620_0769. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR BioCyc; BTHU930170:GL8S-890-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22749 MW; 767D7D620CB3BB67 CRC64; MKNELHVISN GHMSFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK IVINDRIDIA ILLNIPRVQL GYRSADVRSV KEKFSYLHVG YSVHSLEEAI DAFKNGADSL VYGHVFPTDC KKGVPARGLE EISDIAKCLS IPITAIGGIT PENTGDVLTN GVSGIAVMSG IISSSNPYSK AKSYKESIRK WAEKHV // ID F0PWJ8_BACT0 Unreviewed; 219 AA. AC F0PWJ8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=YBT020_02410; OS Bacillus thuringiensis subsp. finitimus (strain YBT-020). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=930170; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YBT-020; RX PubMed=21398543; DOI=10.1128/JB.00267-11; RA Zhu Y., Shang H., Zhu Q., Ji F., Wang P., Fu J., Deng Y., Xu C., RA Ye W., Zheng J., Zhu L., Ruan L., Peng D., Sun M.; RT "Complete genome sequence of Bacillus thuringiensis serovar finitimus RT strain YBT-020."; RL J. Bacteriol. 193:2379-2380(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002508; ADY19732.1; -; Genomic_DNA. DR RefSeq; YP_005564150.1; NC_017200.1. DR EnsemblBacteria; ADY19732; ADY19732; YBT020_02410. DR GeneID; 12183849; -. DR KEGG; btf:YBT020_02410; -. DR PATRIC; 47086539; VBIBacThu177620_0465. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; BTHU930170:GL8S-549-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23554 MW; 5672A9167EE9511A CRC64; MSRISKSEMS RLLSVYFIMG SNNCTKDPLQ ILKDALEGGI TIFQFREKGE GALTEEKRIC FAKELQAICK EYGVPFIVND DVELALKLDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKR LVEEVSNSL // ID F0QBF8_ACIAP Unreviewed; 302 AA. AC F0QBF8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Acav_2211; OS Acidovorax avenae (strain ATCC 19860 / DSM 7227 / JCM 20985 / NCPPB OS 1011). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=643561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19860 / DSM 7227 / JCM 20985 / NCPPB 1011; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., RA Pagani I., Gordon S., Woyke T.; RT "Complete sequence of Acidovorax avenae subsp. avenae ATCC 19860."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002521; ADX46123.1; -; Genomic_DNA. DR RefSeq; YP_004234690.1; NC_015138.1. DR ProteinModelPortal; F0QBF8; -. DR EnsemblBacteria; ADX46123; ADX46123; Acav_2211. DR GeneID; 10307144; -. DR KEGG; aaa:Acav_2211; -. DR PATRIC; 46839187; VBIAciAve68977_2248. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; AAVE643561:GHRD-2243-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 302 AA; 31736 MW; 2A34ECB78B589953 CRC64; MAEDSTLQAM ADAIVQAHAA AFAGFPAQPM PAPAHGGAAY AAALRACSQL GFIAVDADCL ARAWQARTDR TGHFDAAQWP GEPVDFGLQP RPHARPFAHC PDRLGLYAVL PDAHWVGRMA RAGVPTVQLR FKSEDGAAVE REVRAAVEAV RGTPALLFIN DHWQAAIEAG AYGVHLGQED LDALAPGSLE TLRTSGLRLG VSTHGYAEMV RADAAAPSYV AMGAVFPTTL KKMATVPQGL ARLAGYARLM RGYPQVAIGG IGAEQFAEVL ATGVGSIAVV RALVNAPDPE AAARDLMRRM GR // ID F0QLG3_ACIBD Unreviewed; 299 AA. AC F0QLG3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 25. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=ABTW07_2676; OS Acinetobacter baumannii (strain TCDC-AB0715). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=980514; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TCDC-AB0715; RX PubMed=21398540; DOI=10.1128/JB.00244-11; RA Chen C.C., Lin Y.C., Sheng W.H., Chen Y.C., Chang S.C., Hsia K.C., RA Liao M.H., Li S.Y.; RT "Genome sequence of a dominant, multidrug-resistant Acinetobacter RT baumannii strain, TCDC-AB0715."; RL J. Bacteriol. 193:2361-2362(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TCDC-AB0715; RA Chen C.-C., Hsia K.-C., Lin Y.-C., Sheng W.-H., Chen Y.-C., RA Chang S.-C., Liao M.-H., Li S.-Y.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002522; ADX93100.1; -; Genomic_DNA. DR RefSeq; YP_005799558.1; NC_017387.1. DR ProteinModelPortal; F0QLG3; -. DR EnsemblBacteria; ADX93100; ADX93100; ABTW07_2676. DR GeneID; 12378725; -. DR KEGG; abd:ABTW07_2676; -. DR PATRIC; 47075298; VBIAciBau182139_2755. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; ABAU980514:GL7M-2696-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 299 AA; 34203 MW; 49BD9DC168F2FC57 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLNPELK KQIKTVHLKQ SQLMSLHKGD LEVGVRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID F0QNJ4_ACIBD Unreviewed; 203 AA. AC F0QNJ4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ABTW07_2918; OS Acinetobacter baumannii (strain TCDC-AB0715). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=980514; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TCDC-AB0715; RX PubMed=21398540; DOI=10.1128/JB.00244-11; RA Chen C.C., Lin Y.C., Sheng W.H., Chen Y.C., Chang S.C., Hsia K.C., RA Liao M.H., Li S.Y.; RT "Genome sequence of a dominant, multidrug-resistant Acinetobacter RT baumannii strain, TCDC-AB0715."; RL J. Bacteriol. 193:2361-2362(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TCDC-AB0715; RA Chen C.-C., Hsia K.-C., Lin Y.-C., Sheng W.-H., Chen Y.-C., RA Chang S.-C., Liao M.-H., Li S.-Y.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002522; ADX93341.1; -; Genomic_DNA. DR RefSeq; YP_005799798.1; NC_017387.1. DR ProteinModelPortal; F0QNJ4; -. DR EnsemblBacteria; ADX93341; ADX93341; ABTW07_2918. DR GeneID; 12378970; -. DR KEGG; abd:ABTW07_2918; -. DR PATRIC; 47075809; VBIAciBau182139_3003. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; ABAU980514:GL7M-2941-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21778 MW; F47FCEF0DAC9A9AE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKID KAEQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID F0QWN3_VULM7 Unreviewed; 205 AA. AC F0QWN3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 26. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=VMUT_2053; OS Vulcanisaeta moutnovskia (strain 768-28). OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Vulcanisaeta. OX NCBI_TaxID=985053; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=768-28; RX PubMed=21398550; DOI=10.1128/JB.00237-11; RA Gumerov V.M., Mardanov A.V., Beletsky A.V., Prokofeva M.I., RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.; RT "Complete genome sequence of "Vulcanisaeta moutnovskia" strain 768-28, RT a novel member of the hyperthermophilic crenarchaeal genus RT Vulcanisaeta."; RL J. Bacteriol. 193:2355-2356(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002529; ADY02250.1; -; Genomic_DNA. DR RefSeq; YP_004245752.1; NC_015151.1. DR EnsemblBacteria; ADY02250; ADY02250; VMUT_2053. DR GeneID; 10289705; -. DR KEGG; vmo:VMUT_2053; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; VMOU985053:GHEG-2092-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21911 MW; FD68C683DF718CB1 CRC64; MRLPRGIYGI TDTSYTVKSH VDAARAFLEG GVRIIQYRRK EGSIRILLEE ARAIRRLCNE YGAVFIVDDR IDIAILSDAD GVHVGLDDAP VDEIRRRFSG LVIGASASTV DEAIQGENAG ANYIGAGSVF PSPTRPDYRV TGLVGLRNIV QSVSIPVYAI GGITLESIPA IKATGAWGAA VISGILAAKD PVKMARAFVE AWENA // ID F0R8E3_BACSH Unreviewed; 202 AA. AC F0R8E3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bacsa_3605; OS Bacteroides salanitronis (strain DSM 18170 / JCM 13567 / BL78). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=667015; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18170 / JCM 13567 / BL78; RX PubMed=21677856; DOI=10.4056/sigs.1704212; RA Gronow S., Held B., Lucas S., Lapidus A., Del Rio T.G., Nolan M., RA Tice H., Deshpande S., Cheng J.F., Pitluck S., Liolios K., Pagani I., RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Brambilla E.M., Rohde M., Goker M., Detter J.C., RA Woyke T., Bristow J., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Eisen J.A.; RT "Complete genome sequence of Bacteroides salanitronis type strain RT (BL78)."; RL Stand. Genomic Sci. 4:191-199(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002530; ADY38127.1; -; Genomic_DNA. DR RefSeq; YP_004260600.1; NC_015164.1. DR EnsemblBacteria; ADY38127; ADY38127; Bacsa_3605. DR GeneID; 10261580; -. DR KEGG; bsa:Bacsa_3605; -. DR PATRIC; 46883627; VBIBacSal140776_3774. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR BioCyc; BSAL667015:GHA0-3788-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 23196 MW; 2CCECF97365226A3 CRC64; MKLIVITRPT YFVEEDKIIT ALFDEGLDIL HLRKVDSIPV YAERLLTLIP EKYRKRIVVH DNFYLKEEYK LKGIHLNSRN PFIPDNYSGS VTTSCHTLEE VKEKKPHCEY VFLSPIFDSI SKEGYQAAFT PEQIRTAAKS NIIDKKVIAL GGIDESNILQ VKDYGFGGAA ILGGLWNQFD AGHDYNYSQL LEHFRKLKRL AD // ID F0R912_BACSH Unreviewed; 203 AA. AC F0R912; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Bacsa_3611; OS Bacteroides salanitronis (strain DSM 18170 / JCM 13567 / BL78). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=667015; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18170 / JCM 13567 / BL78; RX PubMed=21677856; DOI=10.4056/sigs.1704212; RA Gronow S., Held B., Lucas S., Lapidus A., Del Rio T.G., Nolan M., RA Tice H., Deshpande S., Cheng J.F., Pitluck S., Liolios K., Pagani I., RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Brambilla E.M., Rohde M., Goker M., Detter J.C., RA Woyke T., Bristow J., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Eisen J.A.; RT "Complete genome sequence of Bacteroides salanitronis type strain RT (BL78)."; RL Stand. Genomic Sci. 4:191-199(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002530; ADY38133.1; -; Genomic_DNA. DR RefSeq; YP_004260606.1; NC_015164.1. DR EnsemblBacteria; ADY38133; ADY38133; Bacsa_3611. DR GeneID; 10261586; -. DR KEGG; bsa:Bacsa_3611; -. DR PATRIC; 46883639; VBIBacSal140776_3780. DR KO; K00788; -. DR OMA; AICHAED; -. DR BioCyc; BSAL667015:GHA0-3794-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 31 35 HMP-PP binding (By similarity). FT REGION 128 130 THZ-P binding (By similarity). FT METAL 64 64 Magnesium (By similarity). FT METAL 83 83 Magnesium (By similarity). FT BINDING 63 63 HMP-PP (By similarity). FT BINDING 102 102 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 22499 MW; 67CE004614745505 CRC64; MELQFITHYT DRYTYFDSAR MALEGGCRWI QLRMKEATEE EVEKEAIRVQ DLCRQYGATF IIDDHVALAK KLHADGVHLG KKDMPIAEAR KLLGKDFIIG GTANTFEDVQ MHYAAGADYI GCGPFRFTTT KKNLSPVLGL EGYRNIVSRM KETGINLPIV AIGGIAFEDI PAIMQTGVSG IALSGSILRA DDPIAETRRI INS // ID F0RCJ5_CELLC Unreviewed; 220 AA. AC F0RCJ5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Celly_1869; OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC OS 14961 / NCIMB 1423 / VKM B-1433 / Cy l20). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Cellulophaga. OX NCBI_TaxID=867900; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 / RC VKM B-1433 / Cy l20; RX PubMed=21677859; DOI=10.4056/sigs.1774329; RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., RA Pitluck S., Liolios K., Pagani I., Mavromatis K., Ovchinikova G., RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., RA Detter J.C., Brambilla E.M., Kannan K.P., Rohde M., Spring S., RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Ivanova N.; RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- RT 21)."; RL Stand. Genomic Sci. 4:221-232(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002534; ADY29692.1; -; Genomic_DNA. DR RefSeq; YP_004262563.1; NC_015167.1. DR EnsemblBacteria; ADY29692; ADY29692; Celly_1869. DR GeneID; 10263888; -. DR KEGG; cly:Celly_1869; -. DR PATRIC; 46918021; VBICelLyt164863_1863. DR KO; K00788; -. DR BioCyc; CLYT867900:GHJM-1904-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24258 MW; 03CA9D54BB656ACA CRC64; MISKLHYISQ GKTPEVHLAN IQKACSSGAD WVQLRLKNVD EESLLQVALK AREITSHFQT RLIINDHYKI AKKVNADGVH LGKTDACPLE AREHLGKWIS IGGTANTLED CENLLKKEVD YIGLGPFRFT QTKKNLSPTL GLQGYQAILD ELQTTTPIIA IGGITIADVP ELLKTGIYGI AASTEITANF NSIATLNKVL NTPATQEQVY KFDKSKNDER // ID F0RCJ6_CELLC Unreviewed; 204 AA. AC F0RCJ6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase; GN OrderedLocusNames=Celly_1870; OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC OS 14961 / NCIMB 1423 / VKM B-1433 / Cy l20). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Cellulophaga. OX NCBI_TaxID=867900; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 / RC VKM B-1433 / Cy l20; RX PubMed=21677859; DOI=10.4056/sigs.1774329; RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., RA Pitluck S., Liolios K., Pagani I., Mavromatis K., Ovchinikova G., RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., RA Detter J.C., Brambilla E.M., Kannan K.P., Rohde M., Spring S., RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Ivanova N.; RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- RT 21)."; RL Stand. Genomic Sci. 4:221-232(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002534; ADY29693.1; -; Genomic_DNA. DR RefSeq; YP_004262564.1; NC_015167.1. DR EnsemblBacteria; ADY29693; ADY29693; Celly_1870. DR GeneID; 10263889; -. DR KEGG; cly:Celly_1870; -. DR PATRIC; 46918023; VBICelLyt164863_1864. DR KO; K00788; -. DR BioCyc; CLYT867900:GHJM-1905-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 204 AA; 23884 MW; 2FC03260F5180778 CRC64; MIVLIAPEKD VPNEIEILHQ LFNAGLQYYH LRKPFKDLDQ HTNYLNKIES QYHNRIVVHY YHELINSFNL KGIHFQEQKR RDTIDNPTRY FKNLNMFGKT ISSSFHNQEE LNNCYFEFDY HLLSPVFNSI SKKDYKGRGF NVNHINKTIV GMGGVTAENL SKFNTLGYKG VGVLGGVWSA EKPVEAFKRI DETFYLVQKT KNND // ID F0RQ05_DEIPM Unreviewed; 247 AA. AC F0RQ05; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Deipr_2076; OS Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / OS NBRC 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703). OG Plasmid pDEIPR01. OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=693977; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / RC VKM Ac-1939 / CCM 2703; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete sequence of plasmid1 of Deinococcus proteolyticus DSM RT 20540."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002537; ADY27207.1; -; Genomic_DNA. DR RefSeq; YP_004264067.1; NC_015169.1. DR EnsemblBacteria; ADY27207; ADY27207; Deipr_2076. DR GeneID; 10265396; -. DR KEGG; dpt:Deipr_2076; -. DR PATRIC; 46932630; VBIDeiPro159979_2375. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; DPRO693977:GCFA-2133-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Plasmid; KW Thiamine biosynthesis; Transferase. FT REGION 63 67 HMP-PP binding (By similarity). FT REGION 164 166 THZ-P binding (By similarity). FT METAL 101 101 Magnesium (By similarity). FT METAL 120 120 Magnesium (By similarity). FT BINDING 100 100 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 HMP-PP (By similarity). FT BINDING 195 195 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 247 AA; 25961 MW; 084D45DBA65673C1 CRC64; MTESQQRAES REQRAVQTSP LPSALCQQLG YLYLVATPRP GQSEAEFLAR IGAALDGGVD TLQLRCKADD SRYGEARPYI ALAEKVRDLA HAHQVPFFVN DRVDVALAAG ADGVHLGQND LPVRWARALA LSLLIGRSTH APEQAAAALA EAPAYFACGP VHATPTKPGR AAVGLDYIRA VAAMQPACPW YAIGGIDVQT IHAALDAGAR RVAVVRAVLD AADPAAAAAE LRSCLRVQGS KGLGEPT // ID F0S2U0_DESTD Unreviewed; 214 AA. AC F0S2U0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dester_0510; OS Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA). OC Bacteria; Aquificae; Aquificales; Desulfurobacteriaceae; OC Desulfurobacterium. OX NCBI_TaxID=868864; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11699 / BSA; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., RA Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Desulfurobacterium thermolithotrophum DSM RT 11699."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002543; ADY73162.1; -; Genomic_DNA. DR RefSeq; YP_004281221.1; NC_015185.1. DR EnsemblBacteria; ADY73162; ADY73162; Dester_0510. DR GeneID; 10269738; -. DR KEGG; dte:Dester_0510; -. DR PATRIC; 46941645; VBIDesThe167085_0530. DR KO; K00788; -. DR BioCyc; DTHE868864:GHGF-530-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23653 MW; 2DEF473224D7F5CB CRC64; MGIDFSLYVI TDERFLNISN IAESVEKAIL GGATIIQYRA KKKNTKEMYE EALVVREITK RYNIPFIVND RLDLALAVKA DGVHVGQEDL PVNAIKAIVG NDFIVGLSTH NLNQVKRANE EMLADYIGFG PVFPTTTKEN PDPVTGTDLL CKAVRISKIP VVATGGINEK NVDDVLKCKP AGVAVVRAAF EKGDPYKNVL KLKRKAKELN WKKL // ID F0SEQ8_PEDSD Unreviewed; 205 AA. AC F0SEQ8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Pedsa_1382; OS Pedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / LMG OS 10337 / NBRC 100064 / NCIMB 13643). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=762903; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / RC NCIMB 13643; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Lu M., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Pedobacter saltans DSM 12145."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002545; ADY51948.1; -; Genomic_DNA. DR RefSeq; YP_004273770.1; NC_015177.1. DR EnsemblBacteria; ADY51948; ADY51948; Pedsa_1382. DR GeneID; 10230939; -. DR KEGG; psn:Pedsa_1382; -. DR PATRIC; 47003499; VBIPedSal163994_1446. DR KO; K00788; -. DR OMA; AICHAED; -. DR BioCyc; PSAL762903:GHB2-1409-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22586 MW; B2F6C028DBAB0D26 CRC64; MISKIQYISQ PDSRGSHITN VQKALDAGCT WIQLRIKNKP LDWVYREAES AKVLCKSYQS RLIINDFIQL AKDLDSDGVH LGLQDGSVTV AREILGWDKI IGGTANTFDD VVKRSGEQVD YIGLGPYAFT QTKEKLSPIL GLLSYEQILA QMKVSGINIP IIAIGGIQIK DMRALSKLGI YGFAISGLLN SLSNPEDIFG MLLKQ // ID F0SER0_PEDSD Unreviewed; 195 AA. AC F0SER0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN OrderedLocusNames=Pedsa_1384; OS Pedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / LMG OS 10337 / NBRC 100064 / NCIMB 13643). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=762903; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / RC NCIMB 13643; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Lu M., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Pedobacter saltans DSM 12145."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002545; ADY51950.1; -; Genomic_DNA. DR RefSeq; YP_004273772.1; NC_015177.1. DR EnsemblBacteria; ADY51950; ADY51950; Pedsa_1384. DR GeneID; 10230941; -. DR KEGG; psn:Pedsa_1384; -. DR PATRIC; 47003503; VBIPedSal163994_1448. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR BioCyc; PSAL762903:GHB2-1411-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 195 AA; 22559 MW; 5C026AF1F0164489 CRC64; MKIIVISSPE LFTGESDIVN ALFDEGLELF HFRKPGLQQN KVGAFFEKIR PQYLSRIVLH EQHELAVHFE IKRLHFPEKN RRVLCRETLL KLKADGFTLS SSLHQLKDIE EIATFHYALF GPVFNSISKP DYLTEFNYSR SLNNVINQFN IIGLGGLSSC NYKTLEQYGF KGAAFLGYIW QEPKQALNAF KNLWK // ID F0SGN3_PLABD Unreviewed; 352 AA. AC F0SGN3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Plabr_4061; OS Planctomyces brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / OS NBRC 103401 / IFAM 1448). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Planctomyces. OX NCBI_TaxID=756272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Lu M., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Planctomyces brasiliensis DSM 5305."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002546; ADY61638.1; -; Genomic_DNA. DR RefSeq; YP_004271660.1; NC_015174.1. DR EnsemblBacteria; ADY61638; ADY61638; Plabr_4061. DR GeneID; 10241484; -. DR KEGG; pbs:Plabr_4061; -. DR PATRIC; 47017562; VBIPlaBra152897_4388. DR KO; K00788; -. DR BioCyc; PBRA756272:GH5Q-4106-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 176 180 HMP-PP binding (By similarity). FT REGION 273 275 THZ-P binding (By similarity). FT METAL 209 209 Magnesium (By similarity). FT METAL 228 228 Magnesium (By similarity). FT BINDING 208 208 HMP-PP (By similarity). FT BINDING 247 247 HMP-PP (By similarity). FT BINDING 276 276 HMP-PP (By similarity). FT BINDING 303 303 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 352 AA; 39355 MW; B291CE7655D7EC52 CRC64; MNRQEQRAAY RILDASANRC REGLRVLEEQ VRFRDNDAEM TGQLKTLRHE LTAALGQLRL EEHLDCRDTP GDVGTAISTD SERTRSDWAG VRRANMKRVQ ESLRTLEEYS KLVEPSASAR FEAARYRSYE IEKQLERSEN PRSIRLSKSR LYLLVQGDEP DQFFREVAAG GVNVFQIRDK QADDRELLER GRRLRTLTRE TDTLFIFNDR VDLALLCEAD GVHVGQEELP VAAVRYLAGN DLLVGVSTHS LQQAKTAVVD GADYIGVGPV FPSGTKDFAE FVGPDLVRQV EQEVKLPVFA IGGIDSQNLQ QVCEAGGRRI AVTRAINAAD QPGRAAADLR KNLENSGTLN SN // ID F0SUV9_SYNGF Unreviewed; 207 AA. AC F0SUV9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sgly_2388; OS Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Syntrophobotulus. OX NCBI_TaxID=645991; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8271 / FlGlyR; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., RA Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Syntrophobotulus glycolicus DSM 8271."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002547; ADY56675.1; -; Genomic_DNA. DR RefSeq; YP_004266676.1; NC_015172.1. DR EnsemblBacteria; ADY56675; ADY56675; Sgly_2388. DR GeneID; 10249598; -. DR KEGG; sgy:Sgly_2388; -. DR PATRIC; 47035727; VBISynGly105927_2558. DR KO; K00788; -. DR OMA; MEASHIS; -. DR BioCyc; SGLY645991:GHJ4-2443-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22431 MW; 4403692C28722370 CRC64; MLKWDYTLYL VTDRSYIGDR NLEDCVEEAI LGGATMVQLR EKTASSLDFY HLAVKIKGVT RKYQVPLMIN DRLDIALAID ADGLHLGQDD LPIEIARRYF GREKVIGISV STVEEALLAE KSGADYLGAG AVFPTGTKTD AKLVSLPELS LIKKAVKIPV VAIGGINETN ACDVFHTGID GLSVVSAILA RKDPRKASAE IKARITG // ID F0SYB8_SYNGF Unreviewed; 216 AA. AC F0SYB8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sgly_1655; OS Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Syntrophobotulus. OX NCBI_TaxID=645991; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8271 / FlGlyR; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., RA Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Syntrophobotulus glycolicus DSM 8271."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002547; ADY55953.1; -; Genomic_DNA. DR RefSeq; YP_004265954.1; NC_015172.1. DR EnsemblBacteria; ADY55953; ADY55953; Sgly_1655. DR GeneID; 10248836; -. DR KEGG; sgy:Sgly_1655; -. DR PATRIC; 47034131; VBISynGly105927_1792. DR KO; K00788; -. DR OMA; FQFRVKG; -. DR BioCyc; SGLY645991:GHJ4-1681-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23804 MW; 24CDCFFAC0DB3219 CRC64; MTSRTRPVFP DTDIYGITAE EHSRGRDNVE VVARMLDAGI KLFQYREKDK SMLEKYRQCI KLREMTAERG ATLIVNDHID LAISVEADGV HVGQDDLPLP AVRRLVGEGM LIGLSTHSPQ QAQKAVLDGA DYIGVGPLFQ TFTKKDVCQP VGLEYLEYAV QNIHIPMVAI GGIKLHNLAQ VKAKGAKCIS LVTEIVGAEN IEERVNAIRN ILKGES // ID F0T394_CHLP6 Unreviewed; 212 AA. AC F0T394; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CPSIT_0229; OS Chlamydophila psittaci (strain ATCC VR-125 / 6BC) (Chlamydia OS psittaci). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=331636; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-125 / 6BC; RX PubMed=21441521; DOI=10.1128/JB.00236-11; RA Voigt A., Schofl G., Heidrich A., Sachse K., Saluz H.P.; RT "Full-length de novo sequence of the Chlamydophila psittaci type RT strain, 6BC."; RL J. Bacteriol. 193:2662-2663(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6BC; RA Voigt A., Schofl G., Heidrich A., Sachse K., Saluz H.P.; RT "Full length de novo sequence of the Chlamydophyla psittaci reference RT strain 6BC."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002549; ADZ18225.1; -; Genomic_DNA. DR RefSeq; YP_004422057.1; NC_015470.1. DR EnsemblBacteria; ADZ18225; ADZ18225; CPSIT_0229. DR GeneID; 10601913; -. DR KEGG; chp:CPSIT_0229; -. DR PATRIC; 47105059; VBIChlPsi52874_0215. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22829 MW; 3D460DE4B76332CC CRC64; MEENFFKLIL ITNKQNISVE EYLDFVCACV HSGVTSVQLR EKELSYRELL GFGEALKSML DPLEIPLIVS DSVSVCLDLD ATGVHLGQTD GDVIEARELL GSDKIIGWNV NTLDQLLNAN TLPIDYLGLS AMFATQNKPD ATNLWGFSGL EQAVSLCEHP IVAIGGIDES NAAEVIEAGA AGIAAIGVFH SAQNPGLVTK TLREIVDRGL RC // ID F0TNX1_RIEAR Unreviewed; 207 AA. AC F0TNX1; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=RIA_1783; OS Riemerella anatipestifer (strain RA-GD). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Riemerella. OX NCBI_TaxID=992406; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RA-GD; RX PubMed=21441509; DOI=10.1128/JB.00301-11; RA Yuan J., Liu W., Sun M., Song S., Cai J., Hu S.; RT "Complete genome sequence of the pathogenic bacterium Riemerella RT anatipestifer strain RA-GD."; RL J. Bacteriol. 193:2896-2897(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RA-GD; RA Yuan J., Liu W., Sun M., Song S., Cai J., Hu S.; RT "Complete Genome Sequence of Pathogenic Bacterium Riemerella RT anatipestifer Strain RA-GD."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002562; ADZ12851.1; -; Genomic_DNA. DR RefSeq; YP_006018196.1; NC_017569.1. DR EnsemblBacteria; ADZ12851; ADZ12851; RIA_1783. DR GeneID; 12613970; -. DR KEGG; rar:RIA_1783; -. DR PATRIC; 47190568; VBIRieAna184287_1744. DR KO; K00788; -. DR OMA; YLVIDPS; -. DR BioCyc; RANA992406:GLJP-1733-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 207 AA; 23726 MW; BAAF6760ABA260BC CRC64; MEIKNGIYLI VNPSMHRDTL LIKLEKIISE GIVAVQIWDN FNDNDNILDI INRIIEICHK ENIPVLINNR WELLREVNID GVHFDVQPND IEAIRRELGR KVIMGITCNN DLEHVQWANK QKMDYISFCS IFPSSTANSC EFVRFDTVRE AQKITQIPIF LAGGITPENV GELTYLNCSG IAVVSGIMDS EQPIQEIKKY KLKLKKT // ID F0U8J2_AJEC8 Unreviewed; 536 AA. AC F0U8J2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HCEG_01104; OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) OS (Histoplasma capsulatum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Ajellomyces. OX NCBI_TaxID=544711; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H88; RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Walk T., White J., Yandava C., Klein B., McEwen J.G., Puccia R., RA Goldman G.H., Felipe M.S., Nino-Vega G., San-Blas G., Taylor J., RA Mendoza L., Galagan J., Nusbaum C., Birren B.; RT "Annotation of Ajellomyces capsulatus strain H88."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990636; EGC41742.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 536 AA; 56859 MW; 66413C7AE5E5F7FC CRC64; MDLSVYLVTD STPAILRGRD LCEVVQDAIQ GGVTVVQYRD KHSDSGVMIA TAKRLHEITK KHNVPLIIND RVDVALAVGA EGVHLGQDDM NAKKLLPPNA YIGASVSSNK EALKVVQDGA DYLGIGTVFA TPTKTNTKSI IGPAGTREIL AFLSTMPRRV GTVAIGGINL ANVQRVIYQS QAPLKSLDGA AIVSAIMAAE NPREAAALFC KLVKQIPALA TIPLPPRENE VTLLLDQVPD IVNLVATRRP LCHNMINFVV ANFAANVAIA IGASPIMSGY GPEAVDLAKN GGSLLINMGT LNNESIDNYL QALQAYNAEG NPVVFDPVGA GATDVRRKAA KQLMAGGYFD LIKGNESELI QVYGKVRGHQ VGVDSGPSTL NCKEKARLVM DLAKRERNIV LLTGAVDYLS DGERTLAIGN GHSLLGHITG TGCIIGTIAA SFLAVHRSDK LLAVLASLLL LEIAAERAAV KDGVHGPGHL SPSIYRWTLR GEDVGLVRGK MAAPVLAEAS KTSNWEAATV DENIFEKMAK VHLIHL // ID F0VXZ3_STRG2 Unreviewed; 210 AA. AC F0VXZ3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SGGBAA2069_c11680; OS Streptococcus gallolyticus (strain ATCC BAA-2069). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=990317; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-2069; RX PubMed=21824414; DOI=10.1186/1471-2164-12-400; RA Hinse D., Vollmer T., Rueckert C., Blom J., Kalinowski J., Knabbe C., RA Dreier J.; RT "Complete genome and comparative analysis of Streptococcus RT gallolyticus subsp. gallolyticus, an emerging pathogen of infective RT endocarditis."; RL BMC Genomics 12:400-400(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR824043; CBZ48340.1; -; Genomic_DNA. DR RefSeq; YP_004288084.1; NC_015215.1. DR ProteinModelPortal; F0VXZ3; -. DR EnsemblBacteria; CBZ48340; CBZ48340; SGGBAA2069_c11680. DR GeneID; 10295557; -. DR KEGG; sgg:SGGBAA2069_c11680; -. DR PATRIC; 47028142; VBIStrGal182109_1161. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SGAL990317:GI5F-1260-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22695 MW; B32CAC167AC003AB CRC64; MDKEILQVYF ICGTANCPEG KFLEILEAAF KSGVTCFQFR EKGANALKGG EKVVLARKVK ELCRKYQIPL IINDDVDLAL ELDADGIHLG QDDLPITKAR QLFPNKIIGL SVGSTIEYQR SAVELVDYIG VGPIFPTSSK NDAGEVIGLK GLNDVRDYDK EIPIVAIGGI TFGDVAAIKQ SGADGVAVIS AIAQSKQVEV DTQRLSSFFD // ID F0XPT8_GROCL Unreviewed; 1599 AA. AC F0XPT8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 15. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme; GN ORFNames=CMQ_7749; OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus) OS (Graphiocladiella clavigera). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Ophiostomatales; Ophiostomataceae; OC Grosmannia. OX NCBI_TaxID=655863; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=kw1407 / UAMH 11150; RX PubMed=21262841; DOI=10.1073/pnas.1011289108; RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N., RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M., RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., RA Holt R.A., Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., RA Bohlmann J., Breuil C.; RT "Genome and transcriptome analyses of the mountain pine beetle-fungal RT symbiont Grosmannia clavigera, a lodgepole pine pathogen."; RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL629801; EFX00747.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0005634; C:nucleus; IEA:InterPro. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0000981; F:sequence-specific DNA binding RNA polymerase II transcription factor activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SMART; SM00066; GAL4; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF57701; SSF57701; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 1599 AA; 170286 MW; FBFDCC56A7367499 CRC64; MLAPNKPKGP RACLTCAKAK SRCVPGPVAN VCERCQRLGK PCGSQTPAPQ RRRRLEGSTG GTDAATAATV SSAVGVASTV AQRPRTTKPT RVSELERRLE VLTSRLETVG RQQKQQQQPT TATSPQDDAG QGDESAAAAA AALSTSHFVK NQPMPYYPMT HIFEPSRQTT TAAADATTAE AEASSPSVSS NNNQSGSVSG LSSSTAVSAP DLDTDDLRPC HFFPPCQLRQ PHTPPTGATD TADAAGDVWP QAEEAEMLLQ EFRSHLMPLL PFVVVPDGVS SGQLLAAQPL TWRGVMMTAC HLDGPRQMLM GNQLLGEATG AALLQPRRSV DVLQALLLLL SWFHYNINSF QLNNLLFLAR GITVSLGLGE PHPPSSSPDV PDGYTSEVLQ KMRCFSGTFY LATVATTNKK ADTMMNSPYL DTCCQVLERR MEQPSDRFLV QLVRIQQLSQ AIVVAFSLRN AGIQMDLSTS FMVENLSQRI AQYKAQLPVH FRNDVSINCH MHLAEVLLYE VGLQDSNGLN NGLSLPVAER LNLLSACMRA TRDYMQSRFA EPVQDQPRFV CLTAFDFIYA FLTALKLMTF QMPGWDPRLA REELAFDYVV SRQIFDMQQL ARRRGMRSHK ARGSEAGAAA GRKAGSSERR DPFQRLATRL VELKAMISRE LDQLPSKSTG EVAMSANEEM LSAVAEAAKA PTPTPAPAPV PVAESTNAAM ADAELMTDLA GDFDIGMIDA APAIFSFADA TMDYMQNMDG SSWPDLFNTP GLDSYMDVNL GTPPFDWDIT PLLKKHTITP SSSPPFSIMA VQVRPVVDYS VYLVTDGTAA ILGDGRTVEG VVQAALTSRQ ASEGSQSRES SRSSVGIVQL RDKQSDARGL LASLAALHEH TAAAVVPLVI NDRVDVAAAA MTGGFCEGVH LGQDDVDVAT ARRLLGPAAL IGVTASTAAE AVAACRDGAD YLGLGTVFAT ATKTDTKHVV GTAGLRRMLA AIARAGFGHV PAVCIGGIGA ANARRVVFQG AWEGDDVQQL PPKRVDGIAV VSAIMSAPDP AAAADQLARQ VRLGQTCGPT AFWAAPTTTT TRSKTTTRSI QPILAAMHRL TPLSHNMTNL VVQNLAANVA LAVGASPIMA NSGAEAADLA RLPASALLVN TGSVTPESVA AYVQAIAAYN AAGRPIVYDP VGAGATDVRR AAVRTVMAAG YIDVIKGNEG EMQAVYAAGS NPDDGDCPDS SSAQQQRGVD GSSRLDGTAR ARLVRRLAAR ERCVVVLTGP VDYVAEPTGC HVLAVAHGHP LLGQVTGTGC TLGTAISAAV AAAGVLREEA TDPSAASVFS TFHAVVAALV LYERAAELAA QSATVAGPGS FVPAFLDCLA SCRHRAAAGD MAWVQDNYRI TDTNPPFASY CPYCQIASAA SPAQHLLPPG LKPPPPYRPG RAPASSDAPP PYTAVPLTKQ TIVDDTPILH HLDHDRDSIA SLSLRYNVPA DVLRRTNRLA VDHLLLGRRV VEIPRLSSSS SPVSLSPNPV EGEVEALRKS QIRRFMVACK VADYDLAVLY LDQAAYDLAP AIAAYQADEL WERQNPQVRN KIKTKTKTYN RTSLLSLVRP RPPPETDKH // ID F0YYM2_9CLOT Unreviewed; 257 AA. AC F0YYM2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0240_01941; OS Clostridium sp. D5. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=556261; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D5; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Sibley C.D., White A.P., Crowley S., RA Surette M.G., Strauss J.C., Ambrose C.E., Allen-Vercoe E., Haas B., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium sp. D5."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL870811; EGB93324.1; -; Genomic_DNA. DR EnsemblBacteria; EGB93324; EGB93324; HMPREF0240_01941. DR PATRIC; 46443152; VBICloSp105178_1846. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 257 AA; 27227 MW; B41CE556CAA56101 CRC64; MKCSKEELLL YAVTDRSWLG DSTLYKQVEE ALEGGATFIQ LREKNLETEV FMEEAREIKE LCKRYRVPFV INDSVEIALD VDADGVHVGQ SDMEAGDVRR RLGEDKIIGV SAQTVEQALL AQEHGADYLG VGAVFPTGSK ADATEVDMDT VKAICRAVDI PVIAIGGIGA GNVMELAGSG ICGIAVISAL FAQPDIKAAA RDLKALTKKM VNVSPEESRN TCPAGGTAVS PQNKVYPGAS RNTCPAGGSA VSPQNKV // ID F0YZ24_9CLOT Unreviewed; 203 AA. AC F0YZ24; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Regulatory protein TenI; GN ORFNames=HMPREF0240_02356; OS Clostridium sp. D5. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=556261; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D5; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Sibley C.D., White A.P., Crowley S., RA Surette M.G., Strauss J.C., Ambrose C.E., Allen-Vercoe E., Haas B., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium sp. D5."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL870812; EGB93030.1; -; Genomic_DNA. DR EnsemblBacteria; EGB93030; EGB93030; HMPREF0240_02356. DR PATRIC; 46444045; VBICloSp105178_2280. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 203 AA; 22205 MW; 8F80A4C39D2EC9BB CRC64; MYSGEIMEQS GGELYKHIIA VTNRHLCRRP FMEQIECVCQ RHPGAVLLRE KDLTEEDYGA LFDQVQEICR RYEVPCIPHT FIEAARRQGS GSIHLPLHIL EERPEVGAMF DTVGTSIHAV QEALDAEKAG AAYLTAGHIF STDCKPGLAP RGKKFLREVC AAVAIPVYAI GGMSASGECV EEMKECGAAG ICVMSECMGW GTV // ID F1LLP7_HETGL Unreviewed; 224 AA. AC F1LLP7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 11. DE SubName: Full=Thiamine phosphate diphosphorylase; GN Name=thiE; OS Heterodera glycines (Soybean cyst nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Tylenchida; OC Tylenchina; Tylenchoidea; Heteroderidae; Heteroderinae; Heterodera. OX NCBI_TaxID=51029; RN [1] RP NUCLEOTIDE SEQUENCE. RA Craig J.P., Bekal S., Niblack T., Domier L., Lambert K.N.; RT "Discovery of horizontally transferred genes involved in the RT biosynthesis of vitamin B1, B5, and B7 in Heterodera glycines."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GQ890687; ACZ34278.1; -; mRNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 224 AA; 23780 MW; 57A93646A2B744BF CRC64; MLPKDLFSLY LIVDPILCGG HSHSVKLLNA VIPCGVKIVQ LRAPNWHKGA ILALAKDLLT ITRSKGIPLI INDHVDVCLA SGADGVHLGA NDLPVESARE LLGPDAILGY SVNNEKALEH AIRLGHKIDY LGVGPVFPTA TKSDHAPPLG IERQRLICSR SIHPTVAVGG INAQNAAEVM AIGAPDALAV ISAICAADEP TKTARELCQE IERGRKMKKP MANN // ID F1T7H7_9CLOT Unreviewed; 227 AA. AC F1T7H7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Cpap_3859; OS Clostridium papyrosolvens DSM 2782. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=588581; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2782; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Misra M., Chertkov O., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mouttaki H., RA He Z., Zhou J., Hemme C.L., Woyke T.; RT "The Non-contiguous Finished genome of Clostridium papyrosolvens."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACXX02000001; EGD49425.1; -; Genomic_DNA. DR ProteinModelPortal; F1T7H7; -. DR EnsemblBacteria; EGD49425; EGD49425; Cpap_3859. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 227 AA; 25092 MW; 759024123C697807 CRC64; MVIYVTNRNL CRDDFLKRIE YLASGKPHAI ILREKDLSTE DYQALAEKVK PITDSAGVQL IVNKFIETAK NLGIATVHVS MGDLVKYQDA LQCFSQVWVS VHSAKEAQEA YNSGASALIA GHIYETDCKK DLSPRGLNFL REVCSSVSIP VFGIGGITRD RVKEVTEAGA EGVCIMSEAM TSLSPSSLTS QMLSFTLKDS CYTVNDYNYN KNSSKYHKPP LPKQCHL // ID F1TAC6_9CLOT Unreviewed; 210 AA. AC F1TAC6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Cpap_2890; OS Clostridium papyrosolvens DSM 2782. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=588581; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2782; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Misra M., Chertkov O., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mouttaki H., RA He Z., Zhou J., Hemme C.L., Woyke T.; RT "The Non-contiguous Finished genome of Clostridium papyrosolvens."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACXX02000003; EGD48469.1; -; Genomic_DNA. DR ProteinModelPortal; F1TAC6; -. DR EnsemblBacteria; EGD48469; EGD48469; Cpap_2890. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22582 MW; F94B6AA47573C9AA CRC64; MKTKVDYTLY LVTDRELMST KTLEEAVEQA IMGGCTLVQL REKTASSREF YQTALNIKAI TDKYKVPLII NDRVDIALAI DADGVHVGQS DLPATIVRKI IGKDKILGVS AGCAEKAIEA QREGADYIGV GALFSTSTKT DAKSVSKETL IKIVKEVSIP VVGIGGINEQ NVAQLKNTGI DGIAVVSAII AQKDIKLSAE KMLEIFVEKA // ID F1TKV1_PROAA Unreviewed; 217 AA. AC F1TKV1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9337_00304; OS Propionibacterium acnes HL096PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765057; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL096PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWB01000003; EGE75514.1; -; Genomic_DNA. DR ProteinModelPortal; F1TKV1; -. DR EnsemblBacteria; EGE75514; EGE75514; HMPREF9337_00304. DR PATRIC; 51940568; VBIProAcn164072_0284. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F1TMZ8_PROAA Unreviewed; 216 AA. AC F1TMZ8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9337_01293; OS Propionibacterium acnes HL096PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765057; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL096PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWB01000010; EGE73826.1; -; Genomic_DNA. DR ProteinModelPortal; F1TMZ8; -. DR EnsemblBacteria; EGE73826; EGE73826; HMPREF9337_01293. DR PATRIC; 51942525; VBIProAcn164072_1228. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F1TU29_PROAA Unreviewed; 217 AA. AC F1TU29; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9338_00508; OS Propionibacterium acnes HL096PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765058; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL096PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWC01000002; EGE74356.1; -; Genomic_DNA. DR ProteinModelPortal; F1TU29; -. DR EnsemblBacteria; EGE74356; EGE74356; HMPREF9338_00508. DR PATRIC; 51946224; VBIProAcn162237_0487. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F1TXN1_PROAA Unreviewed; 216 AA. AC F1TXN1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9338_01952; OS Propionibacterium acnes HL096PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765058; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL096PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWC01000021; EGE67829.1; -; Genomic_DNA. DR EnsemblBacteria; EGE67829; EGE67829; HMPREF9338_01952. DR PATRIC; 51949090; VBIProAcn162237_1861. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22628 MW; CC3F100B367E1034 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALYG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F1U1X7_PROAA Unreviewed; 217 AA. AC F1U1X7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9341_00535; OS Propionibacterium acnes HL103PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765061; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL103PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWF01000001; EGE70824.1; -; Genomic_DNA. DR ProteinModelPortal; F1U1X7; -. DR EnsemblBacteria; EGE70824; EGE70824; HMPREF9341_00535. DR PATRIC; 51951510; VBIProAcn163665_0502. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F1U3T1_PROAA Unreviewed; 216 AA. AC F1U3T1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9341_01850; OS Propionibacterium acnes HL103PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765061; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL103PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWF01000003; EGE69517.1; -; Genomic_DNA. DR EnsemblBacteria; EGE69517; EGE69517; HMPREF9341_01850. DR PATRIC; 51954093; VBIProAcn163665_1747. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). SQ SEQUENCE 216 AA; 22620 MW; EE6AAF1B366DB4A9 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAGMRDVVN ASPWPVCVIG EVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F1U8J6_PROAA Unreviewed; 217 AA. AC F1U8J6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9344_00539; OS Propionibacterium acnes HL097PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765064; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL097PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWI01000003; EGE76387.1; -; Genomic_DNA. DR ProteinModelPortal; F1U8J6; -. DR EnsemblBacteria; EGE76387; EGE76387; HMPREF9344_00539. DR PATRIC; 51961876; VBIProAcn164186_0503. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F1UCP9_PROAA Unreviewed; 216 AA. AC F1UCP9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9344_02072; OS Propionibacterium acnes HL097PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765064; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL097PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWI01000019; EGE72491.1; -; Genomic_DNA. DR EnsemblBacteria; EGE72491; EGE72491; HMPREF9344_02072. DR PATRIC; 51964864; VBIProAcn164186_1937. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22574 MW; D45F136331631F39 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETAR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F1UFR2_PROAA Unreviewed; 217 AA. AC F1UFR2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9570_00523; OS Propionibacterium acnes HL043PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765072; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL043PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXP01000001; EGE95612.1; -; Genomic_DNA. DR ProteinModelPortal; F1UFR2; -. DR EnsemblBacteria; EGE95612; EGE95612; HMPREF9570_00523. DR PATRIC; 51977406; VBIProAcn163840_0490. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F1UGZ9_PROAA Unreviewed; 216 AA. AC F1UGZ9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9570_00773; OS Propionibacterium acnes HL043PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765072; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL043PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXP01000002; EGE94594.1; -; Genomic_DNA. DR EnsemblBacteria; EGE94594; EGE94594; HMPREF9570_00773. DR PATRIC; 51977897; VBIProAcn163840_0728. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22628 MW; CC3F100B367E1034 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALYG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F1UNI8_PROAA Unreviewed; 217 AA. AC F1UNI8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9586_00816; OS Propionibacterium acnes HL083PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765088; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL083PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXT01000007; EGF03094.1; -; Genomic_DNA. DR ProteinModelPortal; F1UNI8; -. DR EnsemblBacteria; EGF03094; EGF03094; HMPREF9586_00816. DR PATRIC; 51993317; VBIProAcn162340_0746. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F1USA2_PROAA Unreviewed; 216 AA. AC F1USA2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9586_01675; OS Propionibacterium acnes HL083PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765088; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL083PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXT01000011; EGF00372.1; -; Genomic_DNA. DR ProteinModelPortal; F1USA2; -. DR EnsemblBacteria; EGF00372; EGF00372; HMPREF9586_01675. DR PATRIC; 51994929; VBIProAcn162340_1527. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F1UVL8_PROAA Unreviewed; 217 AA. AC F1UVL8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9584_00488; OS Propionibacterium acnes HL092PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765086; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL092PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXU01000001; EGF03945.1; -; Genomic_DNA. DR EnsemblBacteria; EGF03945; EGF03945; HMPREF9584_00488. DR PATRIC; 51997716; VBIProAcn160697_0459. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22395 MW; B564C189E7C2A32B CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVN // ID F1UZL6_PROAA Unreviewed; 216 AA. AC F1UZL6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9584_01412; OS Propionibacterium acnes HL092PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765086; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL092PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXU01000007; EGE99643.1; -; Genomic_DNA. DR ProteinModelPortal; F1UZL6; -. DR EnsemblBacteria; EGE99643; EGE99643; HMPREF9584_01412. DR PATRIC; 51999518; VBIProAcn160697_1331. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F1V376_PROAA Unreviewed; 217 AA. AC F1V376; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9581_00546; OS Propionibacterium acnes HL087PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765083; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL087PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYA01000006; EGF01028.1; -; Genomic_DNA. DR ProteinModelPortal; F1V376; -. DR EnsemblBacteria; EGF01028; EGF01028; HMPREF9581_00546. DR PATRIC; 52013146; VBIProAcn164350_0512. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F1V847_PROAA Unreviewed; 216 AA. AC F1V847; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9581_02265; OS Propionibacterium acnes HL087PA3. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765083; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL087PA3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYA01000027; EGE97586.1; -; Genomic_DNA. DR ProteinModelPortal; F1V847; -. DR EnsemblBacteria; EGE97586; EGE97586; HMPREF9581_02265. DR PATRIC; 52016503; VBIProAcn164350_2120. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F1VC61_PROAA Unreviewed; 217 AA. AC F1VC61; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9571_01165; OS Propionibacterium acnes HL043PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765073; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL043PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYM01000026; EGE93253.1; -; Genomic_DNA. DR ProteinModelPortal; F1VC61; -. DR EnsemblBacteria; EGE93253; EGE93253; HMPREF9571_01165. DR PATRIC; 52076099; VBIProAcn161999_1073. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F1VDL1_PROAA Unreviewed; 216 AA. AC F1VDL1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9571_01821; OS Propionibacterium acnes HL043PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765073; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL043PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYM01000031; EGE92733.1; -; Genomic_DNA. DR EnsemblBacteria; EGE92733; EGE92733; HMPREF9571_01821. DR PATRIC; 52077374; VBIProAcn161999_1690. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22628 MW; CC3F100B367E1034 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALYG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F1VKX7_PROAA Unreviewed; 217 AA. AC F1VKX7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9568_01607; OS Propionibacterium acnes HL013PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765070; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL013PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYN01000027; EGE91393.1; -; Genomic_DNA. DR ProteinModelPortal; F1VKX7; -. DR EnsemblBacteria; EGE91393; EGE91393; HMPREF9568_01607. DR PATRIC; 52082183; VBIProAcn162435_1499. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F1VN72_PROAA Unreviewed; 216 AA. AC F1VN72; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9568_02415; OS Propionibacterium acnes HL013PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765070; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL013PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYN01000036; EGE89948.1; -; Genomic_DNA. DR ProteinModelPortal; F1VN72; -. DR EnsemblBacteria; EGE89948; EGE89948; HMPREF9568_02415. DR PATRIC; 52083738; VBIProAcn162435_2250. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F1VSA7_MORCA Unreviewed; 346 AA. AC F1VSA7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 13-NOV-2013, entry version 15. DE SubName: Full=NUDIX hydrolase; GN ORFNames=E9Y_06184; OS Moraxella catarrhalis 101P30B1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857572; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=101P30B1; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPC01000019; EGE24031.1; -; Genomic_DNA. DR EnsemblBacteria; EGE24031; EGE24031; E9Y_06184. DR PATRIC; 52833960; VBIMorCat163620_1278. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 346 AA; 39416 MW; 391A827411B39D41 CRC64; MQVNCIHNHN IVSVAVAVLR YTDKFLVAKR HMHQHQGGKW EFIGGKIDAN ESAKQALMRE VNEEIGLSLN TDQLVFMGKV YHDYQDKKVY LYTYEVYLTK KQYHDFLYCQ KGLENQALRW LDMDEMIAKV NQFPVANARI MDWIGLPNLL YISHAVDYFG DFDGFVNYYS NQLPKSAYFY CRPCVGTDDA IRLLTLLKSK RPDINFVVSW SVCQAAQDMM KVLGGVMVKL TCDELEYFSA NFDKLPTDLP LWVGVHDKKE AMMANQLAKS HRIVAALISP VHKTKTHPKA HALGWQGFKS LAKLCDMPSM ALGGMTYFDM NCAKNHGAKG IAGIRGLILS HNSQHY // ID F1VTG8_MORCA Unreviewed; 220 AA. AC F1VTG8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=E9Y_08736; OS Moraxella catarrhalis 101P30B1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857572; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=101P30B1; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPC01000024; EGE23294.1; -; Genomic_DNA. DR EnsemblBacteria; EGE23294; EGE23294; E9Y_08736. DR PATRIC; 52835064; VBIMorCat163620_1809. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 220 AA; 24404 MW; 51463759F5F74067 CRC64; MTLQSIDKVP KLYLLTNDDE LTTLLDKLER VFDTGAVSLL QVRRKSTLKL YDLATVYREA EMIVSLANDY DIKVVMNDNL ELASHFGTGL HLGQRDGSVR VAREILGDHV VIGRTCHTDL ALFKEAKREG ATYGAMGTAF ASITKPRAKI ISKDILKKAC ELDFPLCVIG GITLENIHQL RDKLNGAAID YIAVTADIMG HSVDTIADKC LAWQQKLNTW // ID F1W3Q4_9BURK Unreviewed; 202 AA. AC F1W3Q4; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-MAR-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IMCC9480_1314; OS Oxalobacteraceae bacterium IMCC9480. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae. OX NCBI_TaxID=937450; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IMCC9480; RX PubMed=21572000; DOI=10.1128/JB.05088-11; RA Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., RA Cho J.C.; RT "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing RT betaproteobacterium isolated from the Arctic Ocean."; RL J. Bacteriol. 193:3421-3421(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPR01000695; EGF30518.1; -; Genomic_DNA. DR EnsemblBacteria; EGF30518; EGF30518; IMCC9480_1314. DR PATRIC; 54953811; VBIOxaBac176977_3455. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 202 AA; 21319 MW; 14DEB41CB6BC6687 CRC64; MNGLYLVTPD WDDTERLLHV TEQALLGGAA LVQYRHKTAT AAQRLEQATA LLALCRRHAR PLIINDHADL CIALDADGLH VGGTDASVAQ MRALLGPDKL IGASCYGDLQ LALSAQRSGA SYIAFGGFYP SRVKQYPVTT APDILAQARA VIDLPVVVIG GMTVDNARPL VALGAQMVAA ISSVYGADAP QLAAREIATL FD // ID F1W3Q6_9BURK Unreviewed; 69 AA. AC F1W3Q6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-MAR-2014, entry version 15. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; GN ORFNames=IMCC9480_1316; OS Oxalobacteraceae bacterium IMCC9480. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae. OX NCBI_TaxID=937450; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IMCC9480; RX PubMed=21572000; DOI=10.1128/JB.05088-11; RA Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., RA Cho J.C.; RT "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing RT betaproteobacterium isolated from the Arctic Ocean."; RL J. Bacteriol. 193:3421-3421(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPR01000697; EGF30511.1; -; Genomic_DNA. DR EnsemblBacteria; EGF30511; EGF30511; IMCC9480_1316. DR PATRIC; 54953817; VBIOxaBac176977_3457. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 69 AA; 7361 MW; CFD2F5BC6D18E97B CRC64; MRALLGPDKH IGASCYGDLQ LALSALRSGA SYVAFGCFYR SWLKQYPVAT ASDTIAQARA VIDLPVADV // ID F1W3Q7_9BURK Unreviewed; 39 AA. AC F1W3Q7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-MAR-2014, entry version 11. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; GN ORFNames=IMCC9480_1317; OS Oxalobacteraceae bacterium IMCC9480. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae. OX NCBI_TaxID=937450; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IMCC9480; RX PubMed=21572000; DOI=10.1128/JB.05088-11; RA Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., RA Cho J.C.; RT "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing RT betaproteobacterium isolated from the Arctic Ocean."; RL J. Bacteriol. 193:3421-3421(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPR01000697; EGF30512.1; -; Genomic_DNA. DR EnsemblBacteria; EGF30512; EGF30512; IMCC9480_1317. DR PATRIC; 54953819; VBIOxaBac176977_3458. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 39 AA; 3906 MW; 17AB875EC1F395A2 CRC64; MSALCSCYPQ LLIINDHADL CIALGADGIN VGGTDASVA // ID F1W971_MORCA Unreviewed; 220 AA. AC F1W971; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=E9G_06404; OS Moraxella catarrhalis 7169. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857581; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7169; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERC01000025; EGE10585.1; -; Genomic_DNA. DR ProteinModelPortal; F1W971; -. DR EnsemblBacteria; EGE10585; EGE10585; E9G_06404. DR PATRIC; 52976080; VBIMorCat162371_1301. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 220 AA; 24377 MW; 6B76374C2FC8B34D CRC64; MTLQSIDKVP KLYLLTNDDE LTTLLDKLER VFDTGAVSLL QVRRKSTLKL YDLATVYREA EMIVSLANDY DIKVVMNDSL ELASHFGTGL HLGQRDGSVR VAREILGDHV VIGRTCHTDL ALFKEAKREG ATYGAMGTAF ASITKPRAKI ISKDILKKAC ELDFPLCVIG GITLENIHQL RDKLNGAAID YIAVTADIMG HSVDTIADKC LAWQQKLNTW // ID F1W9U3_MORCA Unreviewed; 346 AA. AC F1W9U3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=NUDIX hydrolase; GN ORFNames=E9G_07820; OS Moraxella catarrhalis 7169. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857581; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7169; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERC01000030; EGE10125.1; -; Genomic_DNA. DR ProteinModelPortal; F1W9U3; -. DR EnsemblBacteria; EGE10125; EGE10125; E9G_07820. DR PATRIC; 52976667; VBIMorCat162371_1586. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 346 AA; 39417 MW; 691A88D411B39D4C CRC64; MQVNCIHNHN IVSVAVAVLR YTDKFLVAKR HMHQHQGGKW EFIGGKIDAN ESAKQALMRE VNEEIGLSLN TDQLVFMGKV YHDYQDKKVY LYTYEVYLTK KQYHDFLYCQ KGLENQALRW LDMDEMIAKV NQFPVANARI MDWIGLPNLL YISHAVDYFG DFDGFVNYYS NQLPKSAYFY CRPCVGTDDA IRLLTLLKSK RPDINFVVSW SVCQAAQDMM KVLGGVMVKL TCDELEYFSA NFDKLPTDLP LWVGVHDKKE AMMANQLAKS HRIVAALISP VHKTKTHPKA HALGWQGFES LAKLCDMPSM ALGGMTYFDM NCAKNHGAKG IAGIRGLILS HNSQHY // ID F1WCV0_MORCA Unreviewed; 346 AA. AC F1WCV0; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=NUDIX hydrolase; GN ORFNames=E9K_03731; OS Moraxella catarrhalis 103P14B1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857579; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=103P14B1; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERE01000027; EGE15181.1; -; Genomic_DNA. DR ProteinModelPortal; F1WCV0; -. DR EnsemblBacteria; EGE15181; EGE15181; E9K_03731. DR PATRIC; 52979075; VBIMorCat162178_0767. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 346 AA; 39417 MW; 691A88D411B39D4C CRC64; MQVNCIHNHN IVSVAVAVLR YTDKFLVAKR HMHQHQGGKW EFIGGKIDAN ESAKQALMRE VNEEIGLSLN TDQLVFMGKV YHDYQDKKVY LYTYEVYLTK KQYHDFLYCQ KGLENQALRW LDMDEMIAKV NQFPVANARI MDWIGLPNLL YISHAVDYFG DFDGFVNYYS NQLPKSAYFY CRPCVGTDDA IRLLTLLKSK RPDINFVVSW SVCQAAQDMM KVLGGVMVKL TCDELEYFSA NFDKLPTDLP LWVGVHDKKE AMMANQLAKS HRIVAALISP VHKTKTHPKA HALGWQGFES LAKLCDMPSM ALGGMTYFDM NCAKNHGAKG IAGIRGLILS HNSQHY // ID F1WGB8_MORCA Unreviewed; 220 AA. AC F1WGB8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=E9K_10128; OS Moraxella catarrhalis 103P14B1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857579; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=103P14B1; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERE01000098; EGE09698.1; -; Genomic_DNA. DR EnsemblBacteria; EGE09698; EGE09698; E9K_10128. DR PATRIC; 52981768; VBIMorCat162178_2042. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 220 AA; 24404 MW; 51463759F5F74067 CRC64; MTLQSIDKVP KLYLLTNDDE LTTLLDKLER VFDTGAVSLL QVRRKSTLKL YDLATVYREA EMIVSLANDY DIKVVMNDNL ELASHFGTGL HLGQRDGSVR VAREILGDHV VIGRTCHTDL ALFKEAKREG ATYGAMGTAF ASITKPRAKI ISKDILKKAC ELDFPLCVIG GITLENIHQL RDKLNGAAID YIAVTADIMG HSVDTIADKC LAWQQKLNTW // ID F1WGI8_MORCA Unreviewed; 220 AA. AC F1WGI8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=E9M_00271; OS Moraxella catarrhalis 46P47B1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857578; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=46P47B1; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERF01000004; EGE15138.1; -; Genomic_DNA. DR ProteinModelPortal; F1WGI8; -. DR EnsemblBacteria; EGE15138; EGE15138; E9M_00271. DR PATRIC; 52981932; VBIMorCat162577_0050. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 220 AA; 24377 MW; 6B76374C2FC8B34D CRC64; MTLQSIDKVP KLYLLTNDDE LTTLLDKLER VFDTGAVSLL QVRRKSTLKL YDLATVYREA EMIVSLANDY DIKVVMNDSL ELASHFGTGL HLGQRDGSVR VAREILGDHV VIGRTCHTDL ALFKEAKREG ATYGAMGTAF ASITKPRAKI ISKDILKKAC ELDFPLCVIG GITLENIHQL RDKLNGAAID YIAVTADIMG HSVDTIADKC LAWQQKLNTW // ID F1WLD3_MORCA Unreviewed; 346 AA. AC F1WLD3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=NUDIX hydrolase; GN ORFNames=E9M_09140; OS Moraxella catarrhalis 46P47B1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857578; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=46P47B1; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERF01000068; EGE09855.1; -; Genomic_DNA. DR ProteinModelPortal; F1WLD3; -. DR EnsemblBacteria; EGE09855; EGE09855; E9M_09140. DR PATRIC; 52985678; VBIMorCat162577_1845. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 346 AA; 39417 MW; 691A88D411B39D4C CRC64; MQVNCIHNHN IVSVAVAVLR YTDKFLVAKR HMHQHQGGKW EFIGGKIDAN ESAKQALMRE VNEEIGLSLN TDQLVFMGKV YHDYQDKKVY LYTYEVYLTK KQYHDFLYCQ KGLENQALRW LDMDEMIAKV NQFPVANARI MDWIGLPNLL YISHAVDYFG DFDGFVNYYS NQLPKSAYFY CRPCVGTDDA IRLLTLLKSK RPDINFVVSW SVCQAAQDMM KVLGGVMVKL TCDELEYFSA NFDKLPTDLP LWVGVHDKKE AMMANQLAKS HRIVAALISP VHKTKTHPKA HALGWQGFES LAKLCDMPSM ALGGMTYFDM NCAKNHGAKG IAGIRGLILS HNSQHY // ID F1WLL5_MORCA Unreviewed; 220 AA. AC F1WLL5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=E9O_00050; OS Moraxella catarrhalis 12P80B1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857577; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=12P80B1; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERG01000001; EGE17967.1; -; Genomic_DNA. DR ProteinModelPortal; F1WLL5; -. DR EnsemblBacteria; EGE17967; EGE17967; E9O_00050. DR PATRIC; 52985845; VBIMorCat189290_0009. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 220 AA; 24377 MW; 6B76374C2FC8B34D CRC64; MTLQSIDKVP KLYLLTNDDE LTTLLDKLER VFDTGAVSLL QVRRKSTLKL YDLATVYREA EMIVSLANDY DIKVVMNDSL ELASHFGTGL HLGQRDGSVR VAREILGDHV VIGRTCHTDL ALFKEAKREG ATYGAMGTAF ASITKPRAKI ISKDILKKAC ELDFPLCVIG GITLENIHQL RDKLNGAAID YIAVTADIMG HSVDTIADKC LAWQQKLNTW // ID F1WN76_MORCA Unreviewed; 346 AA. AC F1WN76; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=NUDIX hydrolase; GN ORFNames=E9O_03073; OS Moraxella catarrhalis 12P80B1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857577; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=12P80B1; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERG01000020; EGE16230.1; -; Genomic_DNA. DR ProteinModelPortal; F1WN76; -. DR EnsemblBacteria; EGE16230; EGE16230; E9O_03073. DR PATRIC; 52987136; VBIMorCat189290_0614. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 346 AA; 39417 MW; 691A88D411B39D4C CRC64; MQVNCIHNHN IVSVAVAVLR YTDKFLVAKR HMHQHQGGKW EFIGGKIDAN ESAKQALMRE VNEEIGLSLN TDQLVFMGKV YHDYQDKKVY LYTYEVYLTK KQYHDFLYCQ KGLENQALRW LDMDEMIAKV NQFPVANARI MDWIGLPNLL YISHAVDYFG DFDGFVNYYS NQLPKSAYFY CRPCVGTDDA IRLLTLLKSK RPDINFVVSW SVCQAAQDMM KVLGGVMVKL TCDELEYFSA NFDKLPTDLP LWVGVHDKKE AMMANQLAKS HRIVAALISP VHKTKTHPKA HALGWQGFES LAKLCDMPSM ALGGMTYFDM NCAKNHGAKG IAGIRGLILS HNSQHY // ID F1WTP3_MORCA Unreviewed; 346 AA. AC F1WTP3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=NUDIX hydrolase; GN ORFNames=E9Q_03983; OS Moraxella catarrhalis BC1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857576; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BC1; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERH01000018; EGE18637.1; -; Genomic_DNA. DR ProteinModelPortal; F1WTP3; -. DR EnsemblBacteria; EGE18637; EGE18637; E9Q_03983. DR PATRIC; 52991695; VBIMorCat160656_0808. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 346 AA; 39417 MW; 691A88D411B39D4C CRC64; MQVNCIHNHN IVSVAVAVLR YTDKFLVAKR HMHQHQGGKW EFIGGKIDAN ESAKQALMRE VNEEIGLSLN TDQLVFMGKV YHDYQDKKVY LYTYEVYLTK KQYHDFLYCQ KGLENQALRW LDMDEMIAKV NQFPVANARI MDWIGLPNLL YISHAVDYFG DFDGFVNYYS NQLPKSAYFY CRPCVGTDDA IRLLTLLKSK RPDINFVVSW SVCQAAQDMM KVLGGVMVKL TCDELEYFSA NFDKLPTDLP LWVGVHDKKE AMMANQLAKS HRIVAALISP VHKTKTHPKA HALGWQGFES LAKLCDMPSM ALGGMTYFDM NCAKNHGAKG IAGIRGLILS HNSQHY // ID F1WVR0_MORCA Unreviewed; 220 AA. AC F1WVR0; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=E9Q_07819; OS Moraxella catarrhalis BC1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857576; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BC1; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERH01000036; EGE16768.1; -; Genomic_DNA. DR ProteinModelPortal; F1WVR0; -. DR EnsemblBacteria; EGE16768; EGE16768; E9Q_07819. DR PATRIC; 52993303; VBIMorCat160656_1576. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 220 AA; 24377 MW; 6B76374C2FC8B34D CRC64; MTLQSIDKVP KLYLLTNDDE LTTLLDKLER VFDTGAVSLL QVRRKSTLKL YDLATVYREA EMIVSLANDY DIKVVMNDSL ELASHFGTGL HLGQRDGSVR VAREILGDHV VIGRTCHTDL ALFKEAKREG ATYGAMGTAF ASITKPRAKI ISKDILKKAC ELDFPLCVIG GITLENIHQL RDKLNGAAID YIAVTADIMG HSVDTIADKC LAWQQKLNTW // ID F1WZG9_MORCA Unreviewed; 220 AA. AC F1WZG9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=E9S_04842; OS Moraxella catarrhalis BC7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857575; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BC7; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERI01000014; EGE21053.1; -; Genomic_DNA. DR EnsemblBacteria; EGE21053; EGE21053; E9S_04842. DR PATRIC; 52996298; VBIMorCat162813_0997. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 220 AA; 24405 MW; 6B6E98AB6767541D CRC64; MTLQSIDKVP KLYLLTNDDE LTTLLDKLER VFDTGAVSLL QVRRKSTLKL YDLATVYREA EMIVSLANDY DIKVVMNDSL ELASHFGTGL HLGQRDGSVR VAREILGDHV VIGRTCHTDL ALFKEAKREG ATYGAMGTVF ASITKPRAKI ISKDILKKAC ELDFPLCVIG GITLENIHQL RDKLNGAAID YIAVTADIMG HSVDTIADKC LAWQQKLNTW // ID F1X1Z2_MORCA Unreviewed; 346 AA. AC F1X1Z2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=NUDIX hydrolase; GN ORFNames=E9S_09319; OS Moraxella catarrhalis BC7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857575; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BC7; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERI01000027; EGE18231.1; -; Genomic_DNA. DR ProteinModelPortal; F1X1Z2; -. DR EnsemblBacteria; EGE18231; EGE18231; E9S_09319. DR PATRIC; 52998214; VBIMorCat162813_1912. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 346 AA; 39417 MW; 691A88D411B39D4C CRC64; MQVNCIHNHN IVSVAVAVLR YTDKFLVAKR HMHQHQGGKW EFIGGKIDAN ESAKQALMRE VNEEIGLSLN TDQLVFMGKV YHDYQDKKVY LYTYEVYLTK KQYHDFLYCQ KGLENQALRW LDMDEMIAKV NQFPVANARI MDWIGLPNLL YISHAVDYFG DFDGFVNYYS NQLPKSAYFY CRPCVGTDDA IRLLTLLKSK RPDINFVVSW SVCQAAQDMM KVLGGVMVKL TCDELEYFSA NFDKLPTDLP LWVGVHDKKE AMMANQLAKS HRIVAALISP VHKTKTHPKA HALGWQGFES LAKLCDMPSM ALGGMTYFDM NCAKNHGAKG IAGIRGLILS HNSQHY // ID F1X2G7_MORCA Unreviewed; 346 AA. AC F1X2G7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=NUDIX hydrolase; GN ORFNames=E9U_00455; OS Moraxella catarrhalis BC8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857574; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BC8; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERJ01000002; EGE22457.1; -; Genomic_DNA. DR ProteinModelPortal; F1X2G7; -. DR EnsemblBacteria; EGE22457; EGE22457; E9U_00455. DR PATRIC; 52998623; VBIMorCat163231_0098. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 346 AA; 39417 MW; 691A88D411B39D4C CRC64; MQVNCIHNHN IVSVAVAVLR YTDKFLVAKR HMHQHQGGKW EFIGGKIDAN ESAKQALMRE VNEEIGLSLN TDQLVFMGKV YHDYQDKKVY LYTYEVYLTK KQYHDFLYCQ KGLENQALRW LDMDEMIAKV NQFPVANARI MDWIGLPNLL YISHAVDYFG DFDGFVNYYS NQLPKSAYFY CRPCVGTDDA IRLLTLLKSK RPDINFVVSW SVCQAAQDMM KVLGGVMVKL TCDELEYFSA NFDKLPTDLP LWVGVHDKKE AMMANQLAKS HRIVAALISP VHKTKTHPKA HALGWQGFES LAKLCDMPSM ALGGMTYFDM NCAKNHGAKG IAGIRGLILS HNSQHY // ID F1X4P1_MORCA Unreviewed; 220 AA. AC F1X4P1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=E9U_05335; OS Moraxella catarrhalis BC8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857574; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BC8; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERJ01000019; EGE20337.1; -; Genomic_DNA. DR ProteinModelPortal; F1X4P1; -. DR EnsemblBacteria; EGE20337; EGE20337; E9U_05335. DR PATRIC; 53000673; VBIMorCat163231_1089. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 220 AA; 24377 MW; 6B76374C2FC8B34D CRC64; MTLQSIDKVP KLYLLTNDDE LTTLLDKLER VFDTGAVSLL QVRRKSTLKL YDLATVYREA EMIVSLANDY DIKVVMNDSL ELASHFGTGL HLGQRDGSVR VAREILGDHV VIGRTCHTDL ALFKEAKREG ATYGAMGTAF ASITKPRAKI ISKDILKKAC ELDFPLCVIG GITLENIHQL RDKLNGAAID YIAVTADIMG HSVDTIADKC LAWQQKLNTW // ID F1X8S8_MORCA Unreviewed; 220 AA. AC F1X8S8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=E9W_02370; OS Moraxella catarrhalis CO72. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857573; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CO72; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERK01000004; EGE25699.1; -; Genomic_DNA. DR ProteinModelPortal; F1X8S8; -. DR EnsemblBacteria; EGE25699; EGE25699; E9W_02370. DR PATRIC; 53003544; VBIMorCat160331_0493. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 220 AA; 24377 MW; 6B76374C2FC8B34D CRC64; MTLQSIDKVP KLYLLTNDDE LTTLLDKLER VFDTGAVSLL QVRRKSTLKL YDLATVYREA EMIVSLANDY DIKVVMNDSL ELASHFGTGL HLGQRDGSVR VAREILGDHV VIGRTCHTDL ALFKEAKREG ATYGAMGTAF ASITKPRAKI ISKDILKKAC ELDFPLCVIG GITLENIHQL RDKLNGAAID YIAVTADIMG HSVDTIADKC LAWQQKLNTW // ID F1XC74_MORCA Unreviewed; 346 AA. AC F1XC74; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=NUDIX hydrolase; GN ORFNames=E9W_08612; OS Moraxella catarrhalis CO72. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857573; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CO72; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERK01000023; EGE22477.1; -; Genomic_DNA. DR ProteinModelPortal; F1XC74; -. DR EnsemblBacteria; EGE22477; EGE22477; E9W_08612. DR PATRIC; 53006203; VBIMorCat160331_1771. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 346 AA; 39417 MW; 691A88D411B39D4C CRC64; MQVNCIHNHN IVSVAVAVLR YTDKFLVAKR HMHQHQGGKW EFIGGKIDAN ESAKQALMRE VNEEIGLSLN TDQLVFMGKV YHDYQDKKVY LYTYEVYLTK KQYHDFLYCQ KGLENQALRW LDMDEMIAKV NQFPVANARI MDWIGLPNLL YISHAVDYFG DFDGFVNYYS NQLPKSAYFY CRPCVGTDDA IRLLTLLKSK RPDINFVVSW SVCQAAQDMM KVLGGVMVKL TCDELEYFSA NFDKLPTDLP LWVGVHDKKE AMMANQLAKS HRIVAALISP VHKTKTHPKA HALGWQGFES LAKLCDMPSM ALGGMTYFDM NCAKNHGAKG IAGIRGLILS HNSQHY // ID F1XFQ2_MORCA Unreviewed; 220 AA. AC F1XFQ2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=EA1_04742; OS Moraxella catarrhalis O35E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857571; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=O35E; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERL01000027; EGE26764.1; -; Genomic_DNA. DR ProteinModelPortal; F1XFQ2; -. DR EnsemblBacteria; EGE26764; EGE26764; EA1_04742. DR PATRIC; 53008723; VBIMorCat162853_0954. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 220 AA; 24377 MW; 6B76374C2FC8B34D CRC64; MTLQSIDKVP KLYLLTNDDE LTTLLDKLER VFDTGAVSLL QVRRKSTLKL YDLATVYREA EMIVSLANDY DIKVVMNDSL ELASHFGTGL HLGQRDGSVR VAREILGDHV VIGRTCHTDL ALFKEAKREG ATYGAMGTAF ASITKPRAKI ISKDILKKAC ELDFPLCVIG GITLENIHQL RDKLNGAAID YIAVTADIMG HSVDTIADKC LAWQQKLNTW // ID F1XG63_MORCA Unreviewed; 346 AA. AC F1XG63; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=NUDIX hydrolase; GN ORFNames=EA1_05883; OS Moraxella catarrhalis O35E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=857571; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=O35E; RX PubMed=21269504; DOI=10.1186/1471-2164-12-70; RA Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J., RA Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P., RA Campagnari A.A.; RT "Comparative analysis and supragenome modeling of twelve Moraxella RT catarrhalis clinical isolates."; RL BMC Genomics 12:70-70(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERL01000031; EGE25966.1; -; Genomic_DNA. DR ProteinModelPortal; F1XG63; -. DR EnsemblBacteria; EGE25966; EGE25966; EA1_05883. DR PATRIC; 53009202; VBIMorCat162853_1185. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 346 AA; 39417 MW; 691A88D411B39D4C CRC64; MQVNCIHNHN IVSVAVAVLR YTDKFLVAKR HMHQHQGGKW EFIGGKIDAN ESAKQALMRE VNEEIGLSLN TDQLVFMGKV YHDYQDKKVY LYTYEVYLTK KQYHDFLYCQ KGLENQALRW LDMDEMIAKV NQFPVANARI MDWIGLPNLL YISHAVDYFG DFDGFVNYYS NQLPKSAYFY CRPCVGTDDA IRLLTLLKSK RPDINFVVSW SVCQAAQDMM KVLGGVMVKL TCDELEYFSA NFDKLPTDLP LWVGVHDKKE AMMANQLAKS HRIVAALISP VHKTKTHPKA HALGWQGFES LAKLCDMPSM ALGGMTYFDM NCAKNHGAKG IAGIRGLILS HNSQHY // ID F1XJ60_ECO57 Unreviewed; 211 AA. AC F1XJ60; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECoA_00538; OS Escherichia coli O157:H7 str. 1044. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=997824; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1044; RA Mane S.P., Sobral B.W., Cebula T., Munk A.C., Tapia R., Green L., RA Rogers Y., Detter J.C., Bruce D., Brettin T.S.; RT "Escherichia coli O157.H7 #1044 Isolate A whole genome shotgun RT sequencing project."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERP01000013; EGD71315.1; -; Genomic_DNA. DR ProteinModelPortal; F1XJ60; -. DR SMR; F1XJ60; 10-209. DR EnsemblBacteria; EGD71315; EGD71315; ECoA_00538. DR PATRIC; 47333315; VBIAEREsc186197_0513. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F1XYH0_ECO57 Unreviewed; 211 AA. AC F1XYH0; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECF_00129; OS Escherichia coli O157:H7 str. 1125. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=997825; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1125; RA Mane S.P., Sobral B.W., Cebula T., Munk A.C., Tapia R., Green L., RA Rogers Y., Detter J.C., Bruce D., Brettin T.S.; RT "E. coli O157.H7 #1125 Isolate A whole genome shotgun sequencing RT project."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERR01000006; EGD70886.1; -; Genomic_DNA. DR ProteinModelPortal; F1XYH0; -. DR SMR; F1XYH0; 10-209. DR EnsemblBacteria; EGD70886; EGD70886; ECF_00129. DR PATRIC; 47355884; VBIAEREsc185309_0131. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F1YN81_9ACTO Unreviewed; 225 AA. AC F1YN81; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-MAR-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SCNU_16888; OS Gordonia neofelifaecis NRRL B-59395. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=644548; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL B-59395; RX PubMed=21742880; DOI=10.1128/JB.05531-11; RA Ge F., Li W., Chen G., Liu Y., Zhang G., Yong B., Wang Q., Wang N., RA Huang Z., Li W., Wang J., Wu C., Xie Q., Liu G.; RT "Draft Genome Sequence of Gordonia neofelifaecis NRRL B-59395, a RT Cholesterol-Degrading Actinomycete."; RL J. Bacteriol. 193:5045-5046(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUD01000017; EGD53792.1; -; Genomic_DNA. DR ProteinModelPortal; F1YN81; -. DR EnsemblBacteria; EGD53792; EGD53792; SCNU_16888. DR PATRIC; 46627813; VBIGorNeo97515_3384. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 23532 MW; 3414999414B72F46 CRC64; MNARTRLDTA RLYLCTDARR ELGDLVEFVR AAVDGGVDIV QLRDKNSPGE REFGELTVAE ELDLLGRLRE LTQAAGALLA VNDRADIAVA AGADVLHIGQ DDLPPSHARR IVGPDVVIGR STHSVEQALE AAADDDVDYF CTGPCWTTPT KPGRAATGLG LVASTADARP SKPWFAIGGI DLPRVAEVTA AGAERIVVVR ALTGAADPAG AARDLKAACL SDGSE // ID F1YQG8_9PROT Unreviewed; 201 AA. AC F1YQG8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=APO_0133; OS Acetobacter pomorum DM001. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=945681; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DM001; RX PubMed=22053049; DOI=10.1126/science.1212782; RA Shin S.C., Kim S.H., You H., Kim B., Kim A.C., Lee K.A., Yoon J.H., RA Ryu J.H., Lee W.J.; RT "Drosophila microbiome modulates host developmental and metabolic RT homeostasis via insulin signaling."; RL Science 334:670-674(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DM001; RA Shin S.-C., Lee W.-J.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUP01000004; EGE48853.1; -; Genomic_DNA. DR EnsemblBacteria; EGE48853; EGE48853; APO_0133. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 21980 MW; 7FBB85BB1C7DF812 CRC64; MTALPQKIYP VVDSAIWVDR LGGAGARFIQ LRLKDMDEDA LRAEIRQGHA YAKQHGVCLV LNDYWQIALD EGIDYIHLGQ EDLDTADLAA IRKGGIRLGI STHCHEELDR ALGCTPDYVA LGPIWETKLK KMAFGPQGPL KLTEWRKLIG NLPLVAIGGI TLERAWACIE AGADSVSAVS AFIRQPDPEG QVKAWLAAVE G // ID F1YUY3_9PROT Unreviewed; 190 AA. AC F1YUY3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=APO_1765; OS Acetobacter pomorum DM001. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=945681; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DM001; RX PubMed=22053049; DOI=10.1126/science.1212782; RA Shin S.C., Kim S.H., You H., Kim B., Kim A.C., Lee K.A., Yoon J.H., RA Ryu J.H., Lee W.J.; RT "Drosophila microbiome modulates host developmental and metabolic RT homeostasis via insulin signaling."; RL Science 334:670-674(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DM001; RA Shin S.-C., Lee W.-J.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUP01000030; EGE47088.1; -; Genomic_DNA. DR EnsemblBacteria; EGE47088; EGE47088; APO_1765. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 190 AA; 20132 MW; 9D71DC5B7B91B182 CRC64; MSDLYLVTPA VSDAQAFLPV LEAGLATHQP AALLLRLVDM PVAAARQAVL LLKPVIQARD IALMLENAPT LAQETGCDGV HLSPSYTAAS VKDVRRIIGP DLQLGVAVGE SRDAAMCAGE DGADYICFGA EDGASLETVS ALTRWWSLMM ELPVVAQAQT PADLAVLSAS GADFVMPSEQ WWQQPDTWQG // ID F1Z1X9_9STRE Unreviewed; 65 AA. AC F1Z1X9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE SubName: Full=Uncharacterized protein; GN ORFNames=SPB_0930; OS Streptococcus parauberis NCFD 2020. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=873447; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCFD 2020; RA Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I., RA Town C.D.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUT02000001; EGE55154.1; -; Genomic_DNA. DR EnsemblBacteria; EGE55154; EGE55154; SPB_0930. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 65 AA; 7057 MW; B92E32BB32997C4A CRC64; MQLVDNFIKS RQIVAIGGIG QNDIEPIIKA GANGIAVISA IARSKEIEQT CKSFRSRLDL TLKSE // ID F1Z9U1_9SPHN Unreviewed; 216 AA. AC F1Z9U1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Y88_0708; OS Novosphingobium nitrogenifigens DSM 19370. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=983920; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 19370; RX PubMed=22156397; DOI=10.1128/JB.06381-11; RA Strabala T.J., Macdonald L., Liu V., Smit A.M.; RT "Draft Genome Sequence of Novosphingobium nitrogenifigens Y88T."; RL J. Bacteriol. 194:201-201(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEWJ01000041; EGD58651.1; -; Genomic_DNA. DR EnsemblBacteria; EGD58651; EGD58651; Y88_0708. DR PATRIC; 46734775; VBINovNit182528_0767. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23071 MW; D188FEB846DDA728 CRC64; MTIPDCQLYL ISPLDVSGDF PERLARALDA GPVAAFQFRV KNIDDHEAAR LAAPLRDICA QRDVAFVVND SIGLAKRLNA DGVHLGQEDG DVADARERLG RDVQIGVTCH DSRHLAMAAG EAGADYVAFG AFFPSTTKET KHQADLDLLR WWSSVFELPV VAIGGITPEN CVPLVEAGAD FLAVSNAVWG GDEVAAVQAF ARAMAEGSRL RAAQAE // ID F1ZCM6_9SPHN Unreviewed; 158 AA. AC F1ZCM6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Y88_2961; OS Novosphingobium nitrogenifigens DSM 19370. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=983920; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 19370; RX PubMed=22156397; DOI=10.1128/JB.06381-11; RA Strabala T.J., Macdonald L., Liu V., Smit A.M.; RT "Draft Genome Sequence of Novosphingobium nitrogenifigens Y88T."; RL J. Bacteriol. 194:201-201(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEWJ01000054; EGD57636.1; -; Genomic_DNA. DR EnsemblBacteria; EGD57636; EGD57636; Y88_2961. DR PATRIC; 46739909; VBINovNit182528_3278. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 158 AA; 16847 MW; BF72AE9379AD941C CRC64; MSDARNDAVL DRALARLPAG SALVFRHYHL DPAARAKRMK GLARLARLYG VAFVLSGVGY GPARHLSRWG KGAGGLRLAT AHDMGELAGA ARARVDAVLL SPVFPTRSHP GAKGLGPLRF ALMARQCPLP VLALGGMDRR RAERLRAYGF AAIDGLSR // ID F1ZQA7_ECOLX Unreviewed; 211 AA. AC F1ZQA7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECSTEC7V_4726; OS Escherichia coli STEC_7v. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754082; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STEC_7v; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXD01000025; EGE62174.1; -; Genomic_DNA. DR EnsemblBacteria; EGE62174; EGE62174; ECSTEC7V_4726. DR PATRIC; 48186416; VBIEscCol149628_4581. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23095 MW; 4EF760EE698C9D2C CRC64; MYQPDFPHVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWQLAIKHQA YGVHLGQEDL QSTDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLP RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F1ZWV3_THEET Unreviewed; 213 AA. AC F1ZWV3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TheetDRAFT_1792; OS Thermoanaerobacter ethanolicus JW 200. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=509192; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JW 200; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Land M.L., Hauser L., Hemme C., Woyke T.J.; RT "The draft genome of Thermoanaerobacter ethanolicus JW 200."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYS01000020; EGD51391.1; -; Genomic_DNA. DR EnsemblBacteria; EGD51391; EGD51391; TheetDRAFT_1792. DR PATRIC; 46798764; VBITheEth54201_1889. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23143 MW; 657E833897CEA345 CRC64; MDLTLYAITD RSYIKDMDIA DAVELAIKGG ATVIQLREKD ISSREFYEIA LKVKEVTKRN RIPLIINDRV DIALAVDADG VHVGQEDLPA DVVRKVIGHD KIVGVSARTV EEALKAQRDG ADYLGVGAVF KTPTKPEAEA IGIEGLKKIK EAVTIPVVAI GGITKDNAYE VMLKSGVDGI SSVSAVFYGD IENNTRKLLE VIAKAINDRR NLK // ID F2A6Q0_RHIET Unreviewed; 211 AA. AC F2A6Q0; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RHECNPAF_183002; OS Rhizobium etli CNPAF512. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=993047; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNPAF512; RX PubMed=21515775; DOI=10.1128/JB.00310-11; RA Fauvart M., Sanchez-Rodriguez A., Beullens S., Marchal K., RA Michiels J.; RT "Genome sequence of Rhizobium etli CNPAF512, a nitrogen-fixing RT symbiont isolated from bean root nodules in Brazil."; RL J. Bacteriol. 193:3158-3159(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYZ01000089; EGE59830.1; -; Genomic_DNA. DR EnsemblBacteria; EGE59830; EGE59830; RHECNPAF_183002. DR PATRIC; 53538997; VBIRhiEtl185341_1805. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21692 MW; E7FAF60289CFE7BA CRC64; MKAFDLSLYL VLDPDLCARI GMVETARLAV AGGATMVQLR DKQAGTARMI ETGRALKQAL GGTGARLIVN DDVEAAIAIS ADGLHIGQED MDARTARGMI GPDMILGLSV ETEALAAAVD RDLVDYTGVG PVFATPTKAD HKQPIGFDGL ARLVQVSPVP SVAIGGLKAE HVAEVFAAGA KGLAVVSAVC GTPDPVAATR RIAAEIRKVP A // ID F2AEU5_RHIET Unreviewed; 204 AA. AC F2AEU5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-MAR-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=RHECNPAF_520012; OS Rhizobium etli CNPAF512. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=993047; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNPAF512; RX PubMed=21515775; DOI=10.1128/JB.00310-11; RA Fauvart M., Sanchez-Rodriguez A., Beullens S., Marchal K., RA Michiels J.; RT "Genome sequence of Rhizobium etli CNPAF512, a nitrogen-fixing RT symbiont isolated from bean root nodules in Brazil."; RL J. Bacteriol. 193:3158-3159(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYZ01000305; EGE56988.1; -; Genomic_DNA. DR EnsemblBacteria; EGE56988; EGE56988; RHECNPAF_520012. DR PATRIC; 53545108; VBIRhiEtl185341_4697. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 204 AA; 22486 MW; 047E91E25DFBEE47 CRC64; MKLDPFYLIV DSAEWIERLV PLGVKLVQLR IKDRPEPVLR EEIRRSKAAC AAAACQLIIN DYWKLAIDEG CDFIHLGQED LAAADLAAIR RAGLKLGLST HDPSELETAL AAAPDYVALG PVWPTILKEM KWAPQGVERL ADWRRRVGPM PLVAIGGITA ERAPLVLENG ANSAAVVTDI TRNPDPEART RQWLAATAPW RSVK // ID F2AHN7_RHIET Unreviewed; 217 AA. AC F2AHN7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-MAR-2014, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase protein; GN ORFNames=RHECNPAF_770037; OS Rhizobium etli CNPAF512. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=993047; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNPAF512; RX PubMed=21515775; DOI=10.1128/JB.00310-11; RA Fauvart M., Sanchez-Rodriguez A., Beullens S., Marchal K., RA Michiels J.; RT "Genome sequence of Rhizobium etli CNPAF512, a nitrogen-fixing RT symbiont isolated from bean root nodules in Brazil."; RL J. Bacteriol. 193:3158-3159(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYZ01000364; EGE55998.1; -; Genomic_DNA. DR EnsemblBacteria; EGE55998; EGE55998; RHECNPAF_770037. DR PATRIC; 53547222; VBIRhiEtl185341_5708. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 217 AA; 22775 MW; 2D84FDFC437E6590 CRC64; MTEPENRCRL VLIAPDIADA DEQARIVADA LKGGDVASVI VPQYGLDDGT FQKHAEKLVP VIQDAGAAAL IAGDSRVAGR AKADGLHLSG NAEALSEAID KHAPKLIVGG GNAADRHNAL EIGEVRPDYI FFGKLDGDIK PEAHPKNLAL GEWWASMIEI PCIVMGGTDP ASALTVAETG AEFVALRLAV FGDPARAPSV IAEINALLDE KAPRFED // ID F2AVS5_RHOBT Unreviewed; 375 AA. AC F2AVS5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=RBWH47_01992; OS Rhodopirellula baltica WH47. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Rhodopirellula. OX NCBI_TaxID=991778; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH47; RX PubMed=23273849; RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., RA Richter M., Achstetter T., Glockner F.O., Harder J.; RT "Expression of sulfatases in Rhodopirellula baltica and the diversity RT of sulfatases in the genus Rhodopirellula."; RL Mar. Genomics 0:0-0(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFAR01000190; EGF26274.1; -; Genomic_DNA. DR EnsemblBacteria; EGF26274; EGF26274; RBWH47_01992. DR PATRIC; 53608880; VBIRhoBal184597_4067. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 375 AA; 40795 MW; 453A2589EC797226 CRC64; MTNAESRIVL RILDANANRA GEGLRTLEES ARFILNDLSL TERLKTHRHD LAVAMRRWNR FQLISSRDTP GDVGTGVRTA SEQSRADLSS VIAAATTRTQ QALRCLEEYG KTADSEFAAC IESIRYQCYA TFRELELKMA GLNERSRKLV EARLYALIAC EPNADCLKAR IAELVDAGVD VIQLRDSSVD DRTLFEQAKL GAAIAAERDV LWIINDRADI AVASGADGVH VGQEELPVDA VREVVGPERL IGLSTHSIEQ VRLATRTTAN YIGCGPTFPG KTKSFDRFPG CEFLTQVRDA ERSGELTLPA FAIGGIGLGN VEQVAQSGIG RVAVTGALAP HDGLHQTAMG MREILERVPL RIAPDSSDVC PLPND // ID F2B4B9_STREE Unreviewed; 209 AA. AC F2B4B9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR5_0682; OS Streptococcus pneumoniae GA04375. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760746; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA04375; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA04375."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFAX01000004; EGE88419.1; -; Genomic_DNA. DR ProteinModelPortal; F2B4B9; -. DR EnsemblBacteria; EGE88419; EGE88419; SPAR5_0682. DR PATRIC; 53615480; VBIStrPne179389_0700. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID F2B4C6_STREE Unreviewed; 210 AA. AC F2B4C6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR5_0689; OS Streptococcus pneumoniae GA04375. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760746; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA04375; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA04375."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFAX01000004; EGE88426.1; -; Genomic_DNA. DR ProteinModelPortal; F2B4C6; -. DR EnsemblBacteria; EGE88426; EGE88426; SPAR5_0689. DR PATRIC; 53615494; VBIStrPne179389_0707. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID F2BG16_9NEIS Unreviewed; 204 AA. AC F2BG16; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9123_2673; OS Neisseria bacilliformis ATCC BAA-1200. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=888742; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1200; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFAY01000053; EGF07137.1; -; Genomic_DNA. DR ProteinModelPortal; F2BG16; -. DR EnsemblBacteria; EGF07137; EGF07137; HMPREF9123_2673. DR PATRIC; 54998922; VBINeiBac171574_2636. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21504 MW; 0E60FC344445C509 CRC64; MTFPPLKSPL KFYAVVSTAE WVARMVKAGA DTVQLRCKTL SGEALRREIA ECVAACAGSK TQLFINDHWR EAIAAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVD ELARALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV RQAGSTPVVA IGGIDLGNAA QVLQTGVSSL AVVRAVTEAE NPEAVVKAFQ ALWE // ID F2BYH0_9FIRM Unreviewed; 212 AA. AC F2BYH0; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9083_1238; OS Dialister micraerophilus DSM 19965. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Dialister. OX NCBI_TaxID=888062; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 19965; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBB01000026; EGF12330.1; -; Genomic_DNA. DR EnsemblBacteria; EGF12330; EGF12330; HMPREF9083_1238. DR PATRIC; 55002120; VBIDiaMic173032_1216. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23570 MW; 0C9AC285E203D725 CRC64; MKNNIDYTLY LVTYNHVSDF EKFCYKIEKA ICNGVTTVQL REKKLETNLF YKKALKVKEL TDKYNVPLII NDRIDIMLAI DAAGVHLGQS DMPADIARKI IGQNKILGIS ASNLTEAKKA YEDGADYLGV GAMFATQTKP DADVTSMKEL KKIRENVDIP IVVIGGINCK TISLFSKIKV DGFAVVSAIM SEKDSGKASK DLIEEIQKVK IR // ID F2BYS4_HAEAE Unreviewed; 226 AA. AC F2BYS4; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9095_0098; OS Haemophilus aegyptius ATCC 11116. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=888728; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11116; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBC01000005; EGF19270.1; -; Genomic_DNA. DR EnsemblBacteria; EGF19270; EGF19270; HMPREF9095_0098. DR PATRIC; 55002342; VBIHaeAeg171656_0096. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24663 MW; 5E34364402B94040 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SGEYAK // ID F2DL69_HORVD Unreviewed; 525 AA. AC F2DL69; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 15. DE SubName: Full=Predicted protein; DE Flags: Fragment; OS Hordeum vulgare var. distichum (Two-rowed barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Pooideae; Triticeae; Hordeum. OX NCBI_TaxID=112509; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Shoot and root; RX PubMed=21415278; DOI=10.1104/pp.110.171579; RA Matsumoto T., Tanaka T., Sakai H., Amano N., Kanamori H., Kurita K., RA Kikuta A., Kamiya K., Yamamoto M., Ikawa H., Fujii N., Hori K., RA Itoh T., Sato K.; RT "Comprehensive sequence analysis of 24,783 barley full-length cDNAs RT derived from 12 clone libraries."; RL Plant Physiol. 156:20-28(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK364637; BAJ95840.1; -; mRNA. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 2: Evidence at transcript level; FT NON_TER 1 1 SQ SEQUENCE 525 AA; 55873 MW; 3A0405FBE8E85698 CRC64; HSSISSFSSP RLPHLSPRTR PWRLAAAREM PWPHVLTVAG SDSSAGAGIQ ADVKACAALG AYCSSVITAV TAQNTAGVQG VHLVPEELIR EQLKSVLSDM SVDVVKTGML PSAGIIQILC ESLRKFPVKA LVVDPVMVST SGDSLSDPST LTNYRDELFA MADIVTPNVK EASKLLGGVS LHTISDMRDA AESIYKLGPR YVLVKGGDMP DSSEAIDVLY DGKEFVELRG HRIKTRNTHG TGCTLASSIA AELAKGSSML NAVQVAKNFV ESALHHSKDL VIGNGPQGPF DHLFRLKRPP YNIGSQQRFN PDSLFLYAVT DSRMNKKWGH SIEDAVKAAI EGGATIVQLR EKDIESRAFL EAAKACMEIC KSSGVSLLIN DRVDIALACN ADGVHVGQSD ISAREVRELL GPGKIIGVSC KTPAQAEQAW RDGADYLGCG GVFPTTTKAN NPTLGFEGLK AVCLASKLPV VAIGGINTTN AGSVMELRLP NLKGVAVVSA LFDRECVSTE TRNLRSILTS VRCLA // ID F2ER66_PANAA Unreviewed; 108 AA. AC F2ER66; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Thiamine-phosphate pyrophosphorylase ThiE; GN Name=thiE; OrderedLocusNames=PAJ_3379; OS Pantoea ananatis (strain AJ13355). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=932677; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AJ13355; RA Hara Y.; RT "Genome sequence of Pantoea ananatis AJ13355."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012032; BAK13459.1; -; Genomic_DNA. DR RefSeq; YP_005936255.1; NC_017531.1. DR EnsemblBacteria; BAK13459; BAK13459; PAJ_3379. DR GeneID; 12526721; -. DR KEGG; paj:PAJ_3379; -. DR PATRIC; 54228084; VBIPanAna188453_3895. DR KO; K00788; -. DR BioCyc; PANA932677:GLI8-3442-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 108 AA; 12242 MW; 4B69D86FADA5D7BB CRC64; MDAFPATASR LGLYPVVDSV EWIERLLEAG VRTLQLRIKD QPDEVVEPMI IRAIAAGKRY QARLFINDYW QLAIKHQAYG VHLGQEDLEV ANLQQILHAG LRLGTFNS // ID F2F0I5_SOLSS Unreviewed; 205 AA. AC F2F0I5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SSIL_1337; OS Solibacillus silvestris (strain StLB046) (Bacillus silvestris). OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Solibacillus. OX NCBI_TaxID=1002809; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=StLB046; RA Morohoshi T., Someya N., Ikeda T.; RT "Genome sequence of Solibacillus silvestris StLB046."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012157; BAK15760.1; -; Genomic_DNA. DR RefSeq; YP_006461906.1; NC_018065.1. DR EnsemblBacteria; BAK15760; BAK15760; SSIL_1337. DR GeneID; 13226291; -. DR KEGG; siv:SSIL_1337; -. DR KO; K00788; -. DR BioCyc; SSIL1002809:GLKA-2376-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22335 MW; B093F0EB40192933 CRC64; MSMSFDLNKY FVMGTANCKR EPLLVLEEAL QAGITMFQLR EKGKNALKGD AYAEFARQCQ KLCQTYKVPF IINDDVELAL TLNADGIHVG QEDTGIEQFR FLAKNKIIGV SVHTIEQLEM AIANGADYAG IGPIYETSTK DDARAPVGLT LLEEAKSQYT QFPIVAIGGI SVENSFIVRQ TGVNGVAVIS AISHSDNIKE AVNSL // ID F2FHZ7_SALDU Unreviewed; 211 AA. AC F2FHZ7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SD3246_4427; OS Salmonella enterica subsp. enterica serovar Dublin str. SD3246. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=909945; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3246; RX PubMed=21478351; DOI=10.1128/JB.00394-11; RA Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S., RA Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.; RT "Genome sequences of Salmonella enterica serovar typhimurium, RT Choleraesuis, Dublin, and Gallinarum strains of well- defined RT virulence in food-producing animals."; RL J. Bacteriol. 193:3162-3163(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001151; EGE32217.1; -; Genomic_DNA. DR ProteinModelPortal; F2FHZ7; -. DR EnsemblBacteria; EGE32217; EGE32217; SD3246_4427. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22898 MW; B8C829313371011C CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RATAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID F2FRI2_SALGL Unreviewed; 211 AA. AC F2FRI2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SG9_3501; OS Salmonella enterica subsp. enterica serovar Gallinarum str. SG9. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=909947; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=9; RX PubMed=21478351; DOI=10.1128/JB.00394-11; RA Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S., RA Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.; RT "Genome sequences of Salmonella enterica serovar typhimurium, RT Choleraesuis, Dublin, and Gallinarum strains of well- defined RT virulence in food-producing animals."; RL J. Bacteriol. 193:3162-3163(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001153; EGE35910.1; -; Genomic_DNA. DR ProteinModelPortal; F2FRI2; -. DR EnsemblBacteria; EGE35910; EGE35910; SG9_3501. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22898 MW; B8C829313371011C CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RATAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID F2G2T2_ALTMD Unreviewed; 526 AA. AC F2G2T2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=MADE_1000715; OS Alteromonas macleodii (strain DSM 17117 / Deep ecotype). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alteromonas. OX NCBI_TaxID=314275; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17117 / Deep ecotype; RX PubMed=18670397; DOI=10.1038/ismej.2008.74; RA Ivars-Martinez E., Martin-Cuadrado A.B., D'Auria G., Mira A., RA Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.; RT "Comparative genomics of two ecotypes of the marine planktonic RT copiotroph Alteromonas macleodii suggests alternative lifestyles RT associated with different kinds of particulate organic matter."; RL ISME J. 2:1194-1212(2008). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001103; AEA96292.1; -; Genomic_DNA. DR RefSeq; YP_004425290.1; NC_011138.3. DR ProteinModelPortal; F2G2T2; -. DR EnsemblBacteria; AEA96292; AEA96292; MADE_1000715. DR GeneID; 6775273; -. DR KEGG; amc:MADE_1000715; -. DR PATRIC; 20871559; VBIAltMac49397_0148. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR BioCyc; AMAC314275:GHA7-149-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 526 AA; 56888 MW; BB42AE1A63F695FA CRC64; MTENALQQPA VKQPVVWCIG GIDSSGGAGI TRDAITLADL NVHACVITTQ ATVQSNSIML SKESMTASAL NQQWQVLSES TPASAIKIGA IANDEQALLL CARIRSMDKP RPFVLWDPVI RTSSGGKLSE LSEPVVEELL NTVDLVTPNT QELSWLTRLS IKSEDSLLTA AHQLITKGAH AIYIKGGHAN WQAHVCDTFI SPTQTIQFSQ PRKETSKLRG TGCMLASAIA AFVVNDYCIE DALTLANAYV SQVRHASCAN TAYTLTSQTS SPAFGHCIGF PNNPLCFPSV KFYQREHAPS QPSLLSAKQV SHVQSQAIER PFPALTQTDL GLYPVVDSVD WIARLLPTGV NIIQLRVKHG TQEEIRQQIK EAIALTKNTH CQLFINDYWE LAIALGAYGV HLGQEDIDTA NLEAIRQAGL RLGISTHGFA EIQRVRALHP SYIALGHIFP TNTKDMPSKP QGVERLRKYV ALCEGIPTVA IGGINLARIA DVAKTGVNSI AVVSAITQAD EPLNAFCKLS KEAGFA // ID F2GMD1_MYCTX Unreviewed; 222 AA. AC F2GMD1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TBSG_00418; OS Mycobacterium tuberculosis KZN 4207. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=478433; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KZN 4207; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center.; RA Murray M., Pillay M., Borowsky M.L., Young S.K., Kodira C., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain KZN 4207."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001662; AEB02547.1; -; Genomic_DNA. DR RefSeq; YP_005098886.1; NC_016768.1. DR ProteinModelPortal; F2GMD1; -. DR SMR; F2GMD1; 1-221. DR EnsemblBacteria; AEB02547; AEB02547; TBSG_00418. DR GeneID; 11694302; -. DR KEGG; mtk:TBSG_00418; -. DR KO; K00788; -. DR OMA; YEVINRS; -. DR BioCyc; MTUB478433:GH4Y-422-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID F2GQH3_BRUM5 Unreviewed; 203 AA. AC F2GQH3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BM590_A0222; OS Brucella melitensis (strain M5-90). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=703352; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M5-90; RX PubMed=21478357; DOI=10.1128/JB.00357-11; RA Wang F., Hu S., Gao Y., Qiao Z., Liu W., Bu Z.; RT "Complete genome sequences of Brucella melitensis strains M28 and M5- RT 90, with different virulence backgrounds."; RL J. Bacteriol. 193:2904-2905(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001851; ADZ86166.1; -; Genomic_DNA. DR RefSeq; YP_005599670.1; NC_017246.1. DR ProteinModelPortal; F2GQH3; -. DR EnsemblBacteria; ADZ86166; ADZ86166; BM590_A0222. DR GeneID; 12153095; -. DR KEGG; bmg:BM590_A0222; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; BMEL703352:GL9P-224-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID F2GS10_BRUM5 Unreviewed; 221 AA. AC F2GS10; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=BM590_A1698; OS Brucella melitensis (strain M5-90). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=703352; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M5-90; RX PubMed=21478357; DOI=10.1128/JB.00357-11; RA Wang F., Hu S., Gao Y., Qiao Z., Liu W., Bu Z.; RT "Complete genome sequences of Brucella melitensis strains M28 and M5- RT 90, with different virulence backgrounds."; RL J. Bacteriol. 193:2904-2905(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001851; ADZ87642.1; -; Genomic_DNA. DR RefSeq; YP_005601146.1; NC_017246.1. DR ProteinModelPortal; F2GS10; -. DR EnsemblBacteria; ADZ87642; ADZ87642; BM590_A1698. DR GeneID; 12154183; -. DR KEGG; bmg:BM590_A1698; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR BioCyc; BMEL703352:GL9P-1734-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23242 MW; 9838EBF5FD9C7A47 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAIEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID F2H503_BACTU Unreviewed; 219 AA. AC F2H503; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CT43_CH0363; OS Bacillus thuringiensis serovar chinensis CT-43. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=541229; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CT-43; RX PubMed=21551307; DOI=10.1128/JB.05085-11; RA He J., Wang J., Yin W., Shao X., Zheng H., Li M., Zhao Y., Sun M., RA Wang S., Yu Z.; RT "Complete genome sequence of Bacillus thuringiensis subsp. chinensis RT strain CT-43."; RL J. Bacteriol. 193:3407-3408(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001907; AEA14055.1; -; Genomic_DNA. DR RefSeq; YP_005570346.1; NC_017208.1. DR ProteinModelPortal; F2H503; -. DR EnsemblBacteria; AEA14055; AEA14055; CT43_CH0363. DR GeneID; 12179654; -. DR KEGG; btc:CT43_CH0363; -. DR PATRIC; 54153243; VBIBacThu155232_0368. DR KO; K00788; -. DR BioCyc; BTHU541229:GL8T-419-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23594 MW; 7794A889CDD6A89F CRC64; MMRIETKKMS KLLQVYFIMG SNNCTRDPLA VLKEALDGGV TLFQFREKGE GSLIGGDRVR FAKELQTLCK EYSVPFIVND DVELAIELDA DGVHVGQDDE GITSVREKMG DKIIGVSAHT IEEARFAIEN GADYLGVGPI FTTSTKKDTK AVQGTKGLAY FREQGITVPI VGIGGITIEN TAAVIEAGAD GVSVISAISL AESAYESTRK LAEEVKRSL // ID F2H9Q3_BACTU Unreviewed; 206 AA. AC F2H9Q3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 22-JAN-2014, entry version 20. DE SubName: Full=Transcriptional regulator TenI; GN Name=tenI; ORFNames=CT43_CH0707; OS Bacillus thuringiensis serovar chinensis CT-43. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=541229; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CT-43; RX PubMed=21551307; DOI=10.1128/JB.05085-11; RA He J., Wang J., Yin W., Shao X., Zheng H., Li M., Zhao Y., Sun M., RA Wang S., Yu Z.; RT "Complete genome sequence of Bacillus thuringiensis subsp. chinensis RT strain CT-43."; RL J. Bacteriol. 193:3407-3408(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001907; AEA14398.1; -; Genomic_DNA. DR RefSeq; YP_005570689.1; NC_017208.1. DR EnsemblBacteria; AEA14398; AEA14398; CT43_CH0707. DR GeneID; 12181319; -. DR KEGG; btc:CT43_CH0707; -. DR PATRIC; 54154046; VBIBacThu155232_0724. DR KO; K10810; -. DR BioCyc; BTHU541229:GL8T-804-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22762 MW; F39BC50677FBDD08 CRC64; MKNELHVISN GHMPFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLMEGFPASK IVINDRIDIA ILLNIPRVQL GYRSTDVKSV KEKFSYLHVG YSVHSLDEAI VAFKNGADSL VYGHVFPTDC KKGVPARGLE EISDIARCLS IPITAIGGIT PENAVDVLTN GVSGIAVMSG IVSSSDPYSK AKSYKESIRK WAEKHV // ID F2HLU7_LACLV Unreviewed; 215 AA. AC F2HLU7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 23. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CVCAS_1229; OS Lactococcus lactis subsp. lactis (strain CV56). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=929102; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CV56; RX PubMed=21460077; DOI=10.1128/JB.00358-11; RA Gao Y., Lu Y., Teng K.L., Chen M.L., Zheng H.J., Zhu Y.Q., Zhong J.; RT "Complete genome sequence of Lactococcus lactis subsp. lactis CV56, a RT probiotic strain isolated from the vaginas of healthy women."; RL J. Bacteriol. 193:2886-2887(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002365; ADZ63872.1; -; Genomic_DNA. DR RefSeq; YP_005868606.1; NC_017486.1. DR ProteinModelPortal; F2HLU7; -. DR EnsemblBacteria; ADZ63872; ADZ63872; CVCAS_1229. DR GeneID; 12477331; -. DR KEGG; llt:CVCAS_1229; -. DR PATRIC; 47139885; VBILacLac178659_1274. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; LLAC929102:GLFG-1268-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23657 MW; 824D01C7F484806A CRC64; MKNKILDLRA YFIAGPQDFP KLSIDDAIDK ISVIIKSGVT VYQFRDKGTI YKNKNQRLEV AKRLQEVAQK AAVSFIVNDD VELARELSAD GIHVGQDDDS VSKIRELIGQ EMWVGLSVSN DMELESAQKS GADYLGIGPI YPTNSKSDAA EPIGVDHLRK MLEHNQLPTV GIGGITENSL TELSKIGLGG VAVISLLTES ENYKNMVQKI KQNIR // ID F2HVG4_BRUMM Unreviewed; 203 AA. AC F2HVG4; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BM28_A0224; OS Brucella melitensis (strain M28). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=941967; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M28; RX PubMed=21478357; DOI=10.1128/JB.00357-11; RA Wang F., Hu S., Gao Y., Qiao Z., Liu W., Bu Z.; RT "Complete genome sequences of Brucella melitensis strains M28 and M5- RT 90, with different virulence backgrounds."; RL J. Bacteriol. 193:2904-2905(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002459; ADZ65300.1; -; Genomic_DNA. DR RefSeq; YP_005596309.1; NC_017244.1. DR ProteinModelPortal; F2HVG4; -. DR EnsemblBacteria; ADZ65300; ADZ65300; BM28_A0224. DR GeneID; 12282947; -. DR KEGG; bmz:BM28_A0224; -. DR PATRIC; 47097951; VBIBruMel176544_0222. DR KO; K00788; -. DR BioCyc; BMEL941967:GL9M-226-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID F2HWK0_BRUMM Unreviewed; 221 AA. AC F2HWK0; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BM28_A1709; OS Brucella melitensis (strain M28). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=941967; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M28; RX PubMed=21478357; DOI=10.1128/JB.00357-11; RA Wang F., Hu S., Gao Y., Qiao Z., Liu W., Bu Z.; RT "Complete genome sequences of Brucella melitensis strains M28 and M5- RT 90, with different virulence backgrounds."; RL J. Bacteriol. 193:2904-2905(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002459; ADZ66785.1; -; Genomic_DNA. DR RefSeq; YP_005597794.1; NC_017244.1. DR ProteinModelPortal; F2HWK0; -. DR EnsemblBacteria; ADZ66785; ADZ66785; BM28_A1709. DR GeneID; 12284228; -. DR KEGG; bmz:BM28_A1709; -. DR PATRIC; 47101085; VBIBruMel176544_1706. DR KO; K00788; -. DR BioCyc; BMEL941967:GL9M-1746-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23242 MW; 9838EBF5FD9C7A47 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAIEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID F2I2Z5_PELSM Unreviewed; 201 AA. AC F2I2Z5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=SAR11G3_00425; OS Pelagibacter sp. (strain IMCC9063). OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=1002672; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC9063; RX PubMed=21515764; DOI=10.1128/JB.05033-11; RA Oh H.M., Kang I., Lee K., Jang Y., Lim S.I., Cho J.C.; RT "Complete genome sequence of strain IMCC9063, belonging to SAR11 RT subgroup 3, isolated from the Arctic Ocean."; RL J. Bacteriol. 193:3379-3380(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002511; AEA80900.1; -; Genomic_DNA. DR RefSeq; YP_004357639.1; NC_015380.1. DR EnsemblBacteria; AEA80900; AEA80900; SAR11G3_00425. DR GeneID; 10475420; -. DR KEGG; pel:SAR11G3_00425; -. DR PATRIC; 54520406; VBICanPel201843_0423. DR BioCyc; CPEL1002672:GHAA-434-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 23019 MW; 73DD54F8AB12ECDB CRC64; MRKTQIYFFL EELNSINIPL LKKLKNVSII YRNYSKQDYI ARALKIKKFV KKQGHSLFIS NDLLLATKLS ANLYIPNFNK QLRYLNHSCQ KKISVIGSAH NHLEVRIKKA QGCSQVFVSP LYPTSSHPEK KSMGIVKFNL LKNNFTSKIN ICALGGVNES NIHKARSLNI FGFALKSYLN KKQTQKSLGF LNLIARSNVM R // ID F2I369_PELSM Unreviewed; 201 AA. AC F2I369; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=SAR11G3_01434; OS Pelagibacter sp. (strain IMCC9063). OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=1002672; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC9063; RX PubMed=21515764; DOI=10.1128/JB.05033-11; RA Oh H.M., Kang I., Lee K., Jang Y., Lim S.I., Cho J.C.; RT "Complete genome sequence of strain IMCC9063, belonging to SAR11 RT subgroup 3, isolated from the Arctic Ocean."; RL J. Bacteriol. 193:3379-3380(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002511; AEA81909.1; -; Genomic_DNA. DR RefSeq; YP_004358648.1; NC_015380.1. DR EnsemblBacteria; AEA81909; AEA81909; SAR11G3_01434. DR GeneID; 10476455; -. DR KEGG; pel:SAR11G3_01434; -. DR PATRIC; 54522493; VBICanPel201843_1423. DR KO; K00788; -. DR BioCyc; CPEL1002672:GHAA-1469-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 201 AA; 23129 MW; 5D249494C7551B92 CRC64; MLKRNIYLIT PNTLNKSFYY FLPKLLKTKR IRYLQIRLKR LSKKKLVQEI KKIKKIVNKK TKIIINDFPE IASLLNCDGY HLGQKDKEIS LVKKKFKTLK IVGVTCHNSK KIALSSVKKG ASYVAFGSFY KTSTKKTKFN ATVALLRWAK DKIKVPVVAI GGINEHNYQP LLKNGANLIA CSSFVWKNKK YNPLQALNRL K // ID F2I5M7_AERUA Unreviewed; 482 AA. AC F2I5M7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.7.4.7; GN Name=thiD; OrderedLocusNames=HMPREF9243_0074; OS Aerococcus urinae (strain ACS-120-V-Col10a). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Aerococcus. OX NCBI_TaxID=866775; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACS-120-V-Col10a; RA Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., RA Gillis M., Methe B., Sutton G., Nelson K.E.; RT "Complete genome sequence of Aerococcus urinae strain ACS-120-V- RT Col10a."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002512; AEA00453.1; -; Genomic_DNA. DR RefSeq; YP_004320488.1; NC_015278.1. DR EnsemblBacteria; AEA00453; AEA00453; HMPREF9243_0074. DR GeneID; 10344630; -. DR KEGG; aur:HMPREF9243_0074; -. DR PATRIC; 47220633; VBIAerUri166521_0061. DR KO; K14153; -. DR BioCyc; AURI866775:GI3R-73-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 482 AA; 50991 MW; 7F4B056FE857A908 CRC64; MTFNKNDLLV YAITPDRFDH DELIQQVKEV LAGGATILQL RLKDHPFKDQ EDKLALTKKI KALCQEAGVP FIIDDDYELA LAVDADGLHV GEDDLPVDQA RQLLGPEKII GASAKTLDTA LKAQAAGADY LGVGALYPTQ SKANAQGTSL TTLRTIAQGV NIPIVGIGGI SLDNMANLRD QGLAGVALIS ALFKAEDPYR TTQAVRQAAE RLFKLQAVLT IAGSDSSGGA GIQADLKTMQ ANGVFGMSAI TSVTAQNTRG VTGVYDLSPE ALASQLQAVF EDIPPASVKI GMVSQVELVE EIAKALKTYQ AKNVVVDPVM VATSGSNLIQ DQAVQVLADQ VFPLACLITP NIPESQVLAG QDIHSAADME AVAKTISQTY QVAVLCKGGH RVNDANDVLV TPEGEVHWFR GERVDNPNTH GTGCTLSSAI ASNLAKGDDL VTAIARAKTY LSLTLKDQLD LGQGSGPLNH GFGLLTYYPT DH // ID F2IH03_FLUTR Unreviewed; 207 AA. AC F2IH03; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Fluta_2804; OS Fluviicola taffensis (strain DSM 16823 / RW262 / RW262). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Cryomorphaceae; Fluviicola. OX NCBI_TaxID=755732; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16823 / RW262 / RW262; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I., RA Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Fluviicola taffensis DSM 16823."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002542; AEA44784.1; -; Genomic_DNA. DR RefSeq; YP_004345622.1; NC_015321.1. DR EnsemblBacteria; AEA44784; AEA44784; Fluta_2804. DR GeneID; 10398172; -. DR KEGG; fte:Fluta_2804; -. DR PATRIC; 54420009; VBIFluTaf147081_2839. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR BioCyc; FTAF755732:GHMH-2847-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 207 AA; 23724 MW; 736B420F1A8538A3 CRC64; MLIVISDSDF RPDEAVIVNE LFQAGLDLFH IRKYGASEEA LLKLVDSIDA KNYSKLVLHH DHEWGKSIGL NRFHYSEKDR KTWYEEDWKG MNSECIYSTS VHSVEEYNEL ANHFSYAFLS PVFDSISKSD YKAVKFDFSK RQNKETKLIG LGGIQADNVN QAIQMGFDGA ALLGAIWNNP NPINEWKLCR DVISQFPLRR GIKGEEV // ID F2IH05_FLUTR Unreviewed; 209 AA. AC F2IH05; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Fluta_2806; OS Fluviicola taffensis (strain DSM 16823 / RW262 / RW262). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Cryomorphaceae; Fluviicola. OX NCBI_TaxID=755732; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16823 / RW262 / RW262; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I., RA Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Fluviicola taffensis DSM 16823."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002542; AEA44786.1; -; Genomic_DNA. DR RefSeq; YP_004345624.1; NC_015321.1. DR EnsemblBacteria; AEA44786; AEA44786; Fluta_2806. DR GeneID; 10398174; -. DR KEGG; fte:Fluta_2806; -. DR PATRIC; 54420013; VBIFluTaf147081_2841. DR KO; K00788; -. DR OMA; MLARYFI; -. DR BioCyc; FTAF755732:GHMH-2849-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22939 MW; 7648EFD034BCC917 CRC64; MLSRIHYISH GETVEEQKKN ILDALEAGCK MIQVRFKNGS RTQILDVARQ VRVWCTYGNA LLIINDSIEI AREVNADGVH LGLTDTSVAD ARKLLGPTKI IGGTANTLED VLQRINEKCD YVGLGPLRFT STKEKLSPLL GFEGYQRVAK ELEMLGLSIP IYAIGGIVRN DVELLKKIGV YGIAVSGMIS NSADKMTLVS EIEQTLSYA // ID F2IQ28_VIBCL Unreviewed; 440 AA. AC F2IQ28; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCLMA_A0058; OS Vibrio cholerae LMA3984-4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=935297; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=21871929; DOI=10.1016/j.mimet.2011.08.003; RA Perez Chaparro P.J., McCulloch J.A., Cerdeira L.T., Al-Dilaimi A., RA Canto de Sa L.L., de Oliveira R., Tauch A., de Carvalho Azevedo V.A., RA Cruz Schneider M.P., da Silva A.L.; RT "Whole genome sequencing of environmental Vibrio cholerae O1 from 10 RT nanograms of DNA using short reads."; RL J. Microbiol. Methods 87:208-212(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMA3984-4; RA Chaparro J., Cerdeira L., Al-Dilaimi A., Barbosa M.S., RA de Oliveira R.S., Ranieri A., Garcia B., Coimbra N., Sa L.L.C., RA Tauch A., Schneider M.P., McCulloch J., Silva A.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002555; AEA77378.1; -; Genomic_DNA. DR RefSeq; YP_005632776.1; NC_017270.1. DR EnsemblBacteria; AEA77378; AEA77378; VCLMA_A0058. DR GeneID; 12267267; -. DR KEGG; vcl:VCLMA_A0058; -. DR PATRIC; 54229840; VBIVibCho179000_0062. DR KO; K00788; -. DR BioCyc; VCHO935297:GLMO-64-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48927 MW; 2A90133D1902DEB6 CRC64; MVRLVFPRHL SALIGHVQCA LLQAKEQGFA IQHIRLDVGS EAQFILEKSD ESLRIGSSLC SQEEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGNAAEQLII YSSETHRLNS KLNQHLAWVL ATLTLDFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPA MQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CSNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSVFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID F2IV12_POLGS Unreviewed; 201 AA. AC F2IV12; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 16. DE SubName: Full=Thiamine-phosphate pyrophosphorylase ThiE1; GN Name=thiE; OrderedLocusNames=SL003B_1814; OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Polymorphum. OX NCBI_TaxID=991905; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1; RX PubMed=21478361; DOI=10.1128/JB.00333-11; RA Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.; RT "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude RT oil-degrading bacterium from oil-polluted saline soil."; RL J. Bacteriol. 193:2894-2895(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002568; ADZ70241.1; -; Genomic_DNA. DR RefSeq; YP_004303542.1; NC_015259.1. DR EnsemblBacteria; ADZ70241; ADZ70241; SL003B_1814. DR GeneID; 10419151; -. DR KEGG; pgv:SL003B_1814; -. DR PATRIC; 47181548; VBIPolGil182274_1860. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; PGIL991905:GJ0L-1841-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 21670 MW; B6E7F07B3CBF6733 CRC64; MLDRFYLIVD SAEWLVRLLP AGLKLAQLRL KDKTPAEIEA EVRASLTLAS TFGCQLVIND HWRTAIDAGA AWIHLGQEDL DGADLAAIRR AGLRLGISTH TEAELDRALG FDPDYVALGP IYEPGGKKVD FAPQGLARIG AWKARIACPL VAIGGLTLER APAVYAAGAD SLCVITDVLA AADPEGRCRA WLEARQTWTR G // ID F2IX41_POLGS Unreviewed; 224 AA. AC F2IX41; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=SL003B_0903; OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Polymorphum. OX NCBI_TaxID=991905; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1; RX PubMed=21478361; DOI=10.1128/JB.00333-11; RA Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.; RT "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude RT oil-degrading bacterium from oil-polluted saline soil."; RL J. Bacteriol. 193:2894-2895(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002568; ADZ69332.1; -; Genomic_DNA. DR RefSeq; YP_004302632.1; NC_015259.1. DR EnsemblBacteria; ADZ69332; ADZ69332; SL003B_0903. DR GeneID; 10418242; -. DR KEGG; pgv:SL003B_0903; -. DR PATRIC; 47179641; VBIPolGil182274_0917. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR BioCyc; PGIL991905:GJ0L-920-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 224 AA; 23553 MW; 209B75F6B677D7BD CRC64; MTLSAASTDT ALNRPRLFLV TPPDPVPADF LGPLEQALGG GDVACVLIYC PTSESRALQA TAEALVPSIQ AAGAAALVYR DTQAAGRSGA DGVHVDTSLE DIKLAVESLR PTRIVGAGGT KLKHEDMEIA ETGVDYLFYG RLDLDERPEP HPKTIERAAW WAELFQTPCV ALAGNTADSI EAAAATGADF VAIKDAVWQH PDGPAAAVRA ANAILERHPF EEAS // ID F2J875_HELP9 Unreviewed; 217 AA. AC F2J875; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=hp2017_0825; OS Helicobacter pylori 2017. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=985081; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2017; RX PubMed=21515762; DOI=10.1128/JB.05006-11; RA Avasthi T.S., Devi S.H., Taylor T.D., Kumar N., Baddam R., Kondo S., RA Suzuki Y., Lamouliatte H., Megraud F., Ahmed N.; RT "Genomes of two chronological isolates (Helicobacter pylori 2017 and RT 2018) of the West African Helicobacter pylori strain 908 obtained from RT a single patient."; RL J. Bacteriol. 193:3385-3386(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002571; ADZ49927.1; -; Genomic_DNA. DR RefSeq; YP_005783823.1; NC_017374.1. DR EnsemblBacteria; ADZ49927; ADZ49927; hp2017_0825. DR GeneID; 12363995; -. DR KEGG; hpq:hp2017_0825; -. DR PATRIC; 47122994; VBIHelPyl182737_0853. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; HPYL985081:GLE0-870-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23884 MW; 4447CB36BDB0720C CRC64; MFDADCLKLM FVAGSQDFYH IKGDRTNALL DTLELALQSK ITAFQFRQKG DLVLQDPVEI KRLALECQKL CKKYGAPFII NDEVRLALEL KADGVHVGQE DMAIEEVVTL CQKRLFIGLS VNTLEQALKA RHLDHVSYLG VGPIFPTPSK KDAKEVVGVN LLKKIHDSGV EKPLIAIGGI TTDNASKLWE YGGIAVISAI TQAKDKALAV ERLLKNA // ID F2JC07_HELP9 Unreviewed; 217 AA. AC F2JC07; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=hp2018_0826; OS Helicobacter pylori 2018. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=985080; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2018; RX PubMed=21515762; DOI=10.1128/JB.05006-11; RA Avasthi T.S., Devi S.H., Taylor T.D., Kumar N., Baddam R., Kondo S., RA Suzuki Y., Lamouliatte H., Megraud F., Ahmed N.; RT "Genomes of two chronological isolates (Helicobacter pylori 2017 and RT 2018) of the West African Helicobacter pylori strain 908 obtained from RT a single patient."; RL J. Bacteriol. 193:3385-3386(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002572; ADZ51528.1; -; Genomic_DNA. DR RefSeq; YP_005791665.1; NC_017381.1. DR EnsemblBacteria; ADZ51528; ADZ51528; hp2018_0826. DR GeneID; 12372047; -. DR KEGG; hpw:hp2018_0826; -. DR PATRIC; 47126356; VBIHelPyl183925_0852. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; HPYL985080:GLE1-875-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23884 MW; 4447CB36BDB0720C CRC64; MFDADCLKLM FVAGSQDFYH IKGDRTNALL DTLELALQSK ITAFQFRQKG DLVLQDPVEI KRLALECQKL CKKYGAPFII NDEVRLALEL KADGVHVGQE DMAIEEVVTL CQKRLFIGLS VNTLEQALKA RHLDHVSYLG VGPIFPTPSK KDAKEVVGVN LLKKIHDSGV EKPLIAIGGI TTDNASKLWE YGGIAVISAI TQAKDKALAV ERLLKNA // ID F2JPA3_CELLD Unreviewed; 213 AA. AC F2JPA3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Clole_3147; OS Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB OS 11756 / RHM5) (Clostridium lentocellum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Cellulosilyticum. OX NCBI_TaxID=642492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5; RX PubMed=21398547; DOI=10.1128/JB.00239-11; RG US DOE Joint Genome Institute; RA Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C., RA Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S., RA Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G., RA Angert E.R., Currie C.R.; RT "Complete genome sequence of the cellulose-degrading bacterium RT Cellulosilyticum lentocellum."; RL J. Bacteriol. 193:2357-2358(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002582; ADZ84842.1; -; Genomic_DNA. DR RefSeq; YP_004310040.1; NC_015275.1. DR ProteinModelPortal; F2JPA3; -. DR EnsemblBacteria; ADZ84842; ADZ84842; Clole_3147. DR GeneID; 10332883; -. DR KEGG; cle:Clole_3147; -. DR KO; K00788; -. DR BioCyc; CCLO642492:GIWK-3272-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22955 MW; A0374AFC3C75D118 CRC64; MKCDKKDLLL YAVTDRSWVG KVSLEEQVKE ALEAGVTFLQ LREKELSKEA FIEEAKRIKK LTDIYHIPFI INDEVEVALA VNADGVHVGQ KDMEVGDVRA LIGPDKILGV SAQTVEQAIC AEARGADYLG VGAVFSTSTK QDAKGVSFET LKAICNAVHI PVIAIGGITK DNMVQLKDSG IVGVAVVSAI FASQNIREAT CALKEKAEQV IGR // ID F2K276_MARM1 Unreviewed; 540 AA. AC F2K276; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Marme_1903; OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 OS / MMB-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=717774; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Lucas-Elio P., Johnston A.W.B., Sanchez-Amat A., Woyke T.; RT "Complete sequence of Marinomonas mediterranea MMB-1."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002583; ADZ91154.1; -; Genomic_DNA. DR RefSeq; YP_004312990.1; NC_015276.1. DR EnsemblBacteria; ADZ91154; ADZ91154; Marme_1903. DR GeneID; 10335978; -. DR KEGG; mme:Marme_1903; -. DR PATRIC; 47228610; VBIMarMed159599_1962. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR BioCyc; MMED717774:GCPW-1954-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 540 AA; 58446 MW; CDFFD176A7797055 CRC64; MKNVEKEKAG GVAVSASRMP VVWCVGGSDS SAHAGLQADL RTGQDLGCHV QTIVTSVTAQ NSKQVDLVEP VSLEVFNQQW ITLLDDVIPD AIKVSLLPTE NLISECGHWL RAVREKFPTV PVIFDPVMAA STNKGNQLQE SGVVGALLRE IFPNVTLVTP NLHEAEVLLG NTVNSTSPSE LYARVSPWLK DFNTQWFVKG GHDKTQDVSC DWLLSNEQQA IGFSAPRLTA HNDRGTGCTL STAIASFMAH GYELLDALTL AKAYISEALS LGVEIGAGAG PLGPPSWPST LSYFPTICSS VSSLKTRVAM EDEFALVQTS KMSLYPVLDS IEWLERTLKQ GVKTAQLRIK NPNDPDLDEH IRQAIALGRA YDAQVFINDY WEKAIEYGAF GVHLGQEDLE IADLQQIKEA GLRLGISTHG YFEIAKVLSI KPSYVALGHI FPTQTKDMPS SPQGTKRLKR YVALLKGHYS TVAIGGISES RVAAVKQTGV DSIALVTAIT LSPEPELAIK RILLACKKPS DHESTSSTAS VIDSAKQEEG // ID F2K512_PSEBN Unreviewed; 314 AA. AC F2K512; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 13-NOV-2013, entry version 20. DE SubName: Full=Uncharacterized protein; GN ORFNames=PSEBR_a4456; OS Pseudomonas brassicacearum (strain NFM421). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=994484; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NFM421; RX PubMed=21515771; DOI=10.1128/JB.00411-11; RA Ortet P., Barakat M., Lalaouna D., Fochesato S., Barbe V., RA Vacherie B., Santaella C., Heulin T., Achouak W.; RT "Complete genome sequence of a beneficial plant root-associated RT bacterium, Pseudomonas brassicacearum."; RL J. Bacteriol. 193:3146-3146(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NFM421; RA Ortet P., Barakat M., Lalaouna D., Fochesato S., Barbe V., RA Santaella C., Heulin T., Achouak W.; RT "Complete Genome Sequence of a beneficial plant roots-associated RT bacterium Pseudomonas brassicacearum."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002585; AEA70867.1; -; Genomic_DNA. DR RefSeq; YP_004355871.1; NC_015379.1. DR ProteinModelPortal; F2K512; -. DR EnsemblBacteria; AEA70867; AEA70867; PSEBR_a4456. DR GeneID; 10473621; -. DR KEGG; pba:PSEBR_a4456; -. DR PATRIC; 54516866; VBIPseBra188168_4744. DR KO; K03574; -. DR BioCyc; PBRA994484:GJWC-4812-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 33842 MW; 6305F68AF18AC2BA CRC64; MKRVHVAAAV IRDAAGKILI ARRADTQHQG GLWEFPGGKV EADESVETAL ARELHEELGI VVDAARPLIK VRHDYPDKQV LLDVWEVSAF TGEPHGAEGQ PLAWVTARDL TNYEFPAANQ PIVAAARLPG QYLITPDGLE TPALLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPFEWLGDF PSAGWHITAA QLRKHAAAGR PFGKDRWLAA SCHSAEELSL AQQMDVDFVT LSPVQPTQTH PDAQPLGWAE AARLIEGFNR PVYLLGGVGP GERQKAWEAG AQGVAGIRAF WPEA // ID F2K5S3_PSEBN Unreviewed; 208 AA. AC F2K5S3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSEBR_a4940; OS Pseudomonas brassicacearum (strain NFM421). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=994484; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NFM421; RX PubMed=21515771; DOI=10.1128/JB.00411-11; RA Ortet P., Barakat M., Lalaouna D., Fochesato S., Barbe V., RA Vacherie B., Santaella C., Heulin T., Achouak W.; RT "Complete genome sequence of a beneficial plant root-associated RT bacterium, Pseudomonas brassicacearum."; RL J. Bacteriol. 193:3146-3146(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NFM421; RA Ortet P., Barakat M., Lalaouna D., Fochesato S., Barbe V., RA Santaella C., Heulin T., Achouak W.; RT "Complete Genome Sequence of a beneficial plant roots-associated RT bacterium Pseudomonas brassicacearum."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002585; AEA71362.1; -; Genomic_DNA. DR RefSeq; YP_004356366.1; NC_015379.1. DR EnsemblBacteria; AEA71362; AEA71362; PSEBR_a4940. DR GeneID; 10474127; -. DR KEGG; pba:PSEBR_a4940; -. DR PATRIC; 54517933; VBIPseBra188168_5261. DR KO; K00788; -. DR BioCyc; PBRA994484:GJWC-5318-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22120 MW; 52D010739E8566F4 CRC64; MKLRGLYAIT DSQLLAGKFL AYVEAALEGG VTLLQYRDKS SDEARRLREA EALRNLCERY KTQLIINDDA ELAARLGVGV HLGQTDGPLA PVRALLGHKA IVGATCHASL ALAEQAASEG ASYVAFGRFF NSNTKPGAPS ANLELLEQAH LKLHVPVCAI GGITLDNAAP LVAHGVDLLA VVHGLFGADS TTEVTRRARA FNDLLQIK // ID F2KMT3_ARCVS Unreviewed; 206 AA. AC F2KMT3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Arcve_0066; OS Archaeoglobus veneficus (strain DSM 11195 / SNP6). OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; OC Archaeoglobaceae; Archaeoglobus. OX NCBI_TaxID=693661; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SNP6; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., RA Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Archaeoglobus veneficus SNP6."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002588; AEA46107.1; -; Genomic_DNA. DR RefSeq; YP_004340822.1; NC_015320.1. DR EnsemblBacteria; AEA46107; AEA46107; Arcve_0066. DR GeneID; 10393157; -. DR KEGG; ave:Arcve_0066; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; AVEN693661:GHD5-68-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR023795; Serpin_CS. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS00284; SERPIN; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 179 180 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 159 159 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22136 MW; 37BA2AC8588345E2 CRC64; MLKIDKPFLY VITSGKRWKH EEVAKAALKA GVRIIQYREK EAPARVMVGE ARRIRKLCDE YDAMLIVNDR VDIAIACNAD GVHVGQDDIP AEIVAEIFDG IIGMSVKTVE QAKQAEEYAD YLGAGSAFPT GTKESKVIGV EGIRRIVEAV SIPVVAIGGI TRENVLEVLK TGVAGVAVVS AVSMADDPED AARKLLGILS TFNGGR // ID F2LHY1_BURGS Unreviewed; 373 AA. AC F2LHY1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=bgla_1g03640; OS Burkholderia gladioli (strain BSR3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=999541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSR3; RX PubMed=21478339; DOI=10.1128/JB.00420-11; RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., RA Choi I.Y., Moon J.S., Kim J., Hwang I.; RT "Complete genome sequence of Burkholderia gladioli BSR3."; RL J. Bacteriol. 193:3149-3149(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002599; AEA59058.1; -; Genomic_DNA. DR RefSeq; YP_004359014.1; NC_015381.1. DR EnsemblBacteria; AEA59058; AEA59058; bgla_1g03640. DR GeneID; 10476841; -. DR KEGG; bgd:bgla_1g03640; -. DR PATRIC; 54498704; VBIBurGla188977_3881. DR KO; K00788; -. DR OMA; INDHWQI; -. DR BioCyc; BGLA999541:GHSQ-372-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 373 AA; 38170 MW; 290750281F526C68 CRC64; MSRGASTPAH FAELFWPPAD ELAAAAERIR ARLGDWPARA APMRICVAAP EHPAAGDLLI VTAGDAEAEA ARAAGVIAAG GAVIAIDERH ATLVSGTARH ALTAAAQLAD DWIAALAAFL DCGFEPHDAL VLALAWRDGD EAAAGDPWPV DPARFPSIAG APAAPEPAFA PCPARLGLYP VVPSADWVER VLDYGARAVQ LRLKGVPAGQ LADEVARAVA AGRRHPDARV FINDHWRLAI EAGAYGVHLG QEDLQTADLG AIAAAGLRLG LSSHGYYEML VALRLRPSYL ALGPVYATTT KAVAAPPQGL ARIARYARLA GRRAPLVAIG GVTAATLPAV IATGVGSVAV VSAVTAAADP RAAVASLGAC FEA // ID F2LQ89_BURGS Unreviewed; 215 AA. AC F2LQ89; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=bgla_2g21580; OS Burkholderia gladioli (strain BSR3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=999541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSR3; RX PubMed=21478339; DOI=10.1128/JB.00420-11; RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., RA Choi I.Y., Moon J.S., Kim J., Hwang I.; RT "Complete genome sequence of Burkholderia gladioli BSR3."; RL J. Bacteriol. 193:3149-3149(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002600; AEA64592.1; -; Genomic_DNA. DR RefSeq; YP_004350104.1; NC_015376.1. DR EnsemblBacteria; AEA64592; AEA64592; bgla_2g21580. DR GeneID; 10467762; -. DR KEGG; bgd:bgla_2g21580; -. DR PATRIC; 54495654; VBIBurGla188977_2385. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR BioCyc; BGLA999541:GHSQ-6133-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 215 AA; 21559 MW; 48FAAE03AE4B919E CRC64; MSSSETAARP ALPAVYLITP EPASASGDAL DAFVARLEAA FASGIALLQL RVKSLDAGAY AALAARVIEL AHAAGARVIC NGAITPAAAL ALGADGVHLS EAALLATSSR PVAPMVLLSA ACHDATSLRQ AQQIDVDLVT LSPVKPTLTH PGTPALGWHG FAQCIAQAGP AIEPAAALPA RPAIYALGGM TREDLPDARA HGAHGVAGIR GFGVF // ID F2LU18_HIPMA Unreviewed; 199 AA. AC F2LU18; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Hipma_0445; OS Hippea maritima (strain ATCC 700847 / DSM 10411 / MH2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfurellales; OC Desulfurellaceae; Hippea. OX NCBI_TaxID=760142; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700847 / DSM 10411 / MH2; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., RA Mikhailova N., Lu M., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Hippea maritima DSM 10411."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002606; AEA33417.1; -; Genomic_DNA. DR RefSeq; YP_004339476.1; NC_015318.1. DR EnsemblBacteria; AEA33417; AEA33417; Hipma_0445. DR GeneID; 10391771; -. DR KEGG; hmr:Hipma_0445; -. DR PATRIC; 54411549; VBIHipMar155866_0450. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR BioCyc; HMAR760142:GHVE-463-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 128 130 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 159 159 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 199 AA; 22117 MW; 50985702B526DBD0 CRC64; MDLPKGFYGI IDERFGCIDS AKKLIDFGAK IIQYRCKNKT DRQMLEEAET IRRLTLNAGA VFIIDDRVDL ALLVGADGVH VGDKDFPPCR IRKLAPKGFI IGLSTHSIDD VRNASCCDYI GVGPVFATTT KDKPHPTLGV ELAEEMVRQS PYPAFLIGGI ALDNIETIKH IPAWGFVSVR DVLANDKAHF ERMLEIWNS // ID F2M426_LACCC Unreviewed; 213 AA. AC F2M426; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LC2W_0309; OS Lactobacillus casei (strain LC2W). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=999378; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LC2W; RX PubMed=21515769; DOI=10.1128/JB.05017-11; RA Chen C., Ai L., Zhou F., Wang L., Zhang H., Chen W., Guo B.; RT "Complete genome sequence of the probiotic bacterium Lactobacillus RT casei LC2W."; RL J. Bacteriol. 193:3419-3420(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002616; AEA52644.1; -; Genomic_DNA. DR RefSeq; YP_005855228.1; NC_017473.1. DR ProteinModelPortal; F2M426; -. DR EnsemblBacteria; AEA52644; AEA52644; LC2W_0309. DR GeneID; 12463400; -. DR KEGG; lce:LC2W_0309; -. DR PATRIC; 54297824; VBILacCas186771_0315. DR KO; K00788; -. DR BioCyc; LCAS999378:GLF5-318-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Magnesium; Metal-binding; KW Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22633 MW; 09637BD33C906AD5 CRC64; MNATDLKLYL VTHRYDDNEA TFLAKIAAAC ENGVTMVQLR EKMLSTRAYF ELAQRVKLIT DRYQIPLIID DRVDICLAVD AAGVHIGDDE LPVAMTRQLI GPDKVLGVST KTVETAVAAV AAGADYLGVG AIFPTQTKAN APVTPIATLK AITAQVAVPV VAIGGVKEAN LGTFKETGIA GVAIVSEIMQ APDIAHKVQA LRTKLKAVLP NDR // ID F2MLH5_LACCD Unreviewed; 213 AA. AC F2MLH5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LCBD_0317; OS Lactobacillus casei (strain BD-II). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=998820; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BD-II; RX PubMed=21478345; DOI=10.1128/JB.00421-11; RA Ai L., Chen C., Zhou F., Wang L., Zhang H., Chen W., Guo B.; RT "Complete genome sequence of the probiotic strain Lactobacillus casei RT BD-II."; RL J. Bacteriol. 193:3160-3161(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002618; AEA55817.1; -; Genomic_DNA. DR RefSeq; YP_005858358.1; NC_017474.1. DR ProteinModelPortal; F2MLH5; -. DR EnsemblBacteria; AEA55817; AEA55817; LCBD_0317. DR GeneID; 12466624; -. DR KEGG; lcs:LCBD_0317; -. DR PATRIC; 54291254; VBILacCas184581_0311. DR KO; K00788; -. DR OMA; AICHAED; -. DR BioCyc; LCAS998820:GLF4-320-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Magnesium; Metal-binding; KW Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22633 MW; 09637BD33C906AD5 CRC64; MNATDLKLYL VTHRYDDNEA TFLAKIAAAC ENGVTMVQLR EKMLSTRAYF ELAQRVKLIT DRYQIPLIID DRVDICLAVD AAGVHIGDDE LPVAMTRQLI GPDKVLGVST KTVETAVAAV AAGADYLGVG AIFPTQTKAN APVTPIATLK AITAQVAVPV VAIGGVKEAN LGTFKETGIA GVAIVSEIMQ APDIAHKVQA LRTKLKAVLP NDR // ID F2MUD2_ENTFO Unreviewed; 211 AA. AC F2MUD2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=OG1RF_12136; OS Enterococcus faecalis (strain ATCC 47077 / OG1RF). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=474186; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 47077 / OG1RF; RX PubMed=18611278; DOI=10.1186/gb-2008-9-7-r110; RA Bourgogne A., Garsin D.A., Qin X., Singh K.V., Sillanpaa J., RA Yerrapragada S., Ding Y., Dugan-Rocha S., Buhay C., Shen H., Chen G., RA Williams G., Muzny D., Maadani A., Fox K.A., Gioia J., Chen L., RA Shang Y., Arias C.A., Nallapareddy S.R., Zhao M., Prakash V.P., RA Chowdhury S., Jiang H., Gibbs R.A., Murray B.E., Highlander S.K., RA Weinstock G.M.; RT "Large scale variation in Enterococcus faecalis illustrated by the RT genome analysis of strain OG1RF."; RL Genome Biol. 9:R110.1-R110.16(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002621; AEA94823.1; -; Genomic_DNA. DR RefSeq; YP_005709193.1; NC_017316.1. DR EnsemblBacteria; AEA94823; AEA94823; OG1RF_12136. DR GeneID; 12288878; -. DR KEGG; efi:OG1RF_12136; -. DR KO; K00788; -. DR BioCyc; EFAE474186:GLCT-2196-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22879 MW; EF37A91BF45C1754 CRC64; MREQLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKVVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVAIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID F2N162_PSEU6 Unreviewed; 312 AA. AC F2N162; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 20. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=PSTAA_3329; OS Pseudomonas stutzeri (strain DSM 4166 / CMT.9.A). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=996285; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4166 / CMT.9.A; RX PubMed=21515765; DOI=10.1128/JB.05039-11; RA Yu H., Yuan M., Lu W., Yang J., Dai S., Li Q., Yang Z., Dong J., RA Sun L., Deng Z., Zhang W., Chen M., Ping S., Han Y., Zhan Y., Yan Y., RA Jin Q., Lin M.; RT "Complete genome sequence of the nitrogen-fixing and rhizosphere- RT associated bacterium Pseudomonas stutzeri strain DSM4166."; RL J. Bacteriol. 193:3422-3423(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 4166; RA Yu H., Yuan M., Yang J., Yan Y., Jin Q., Lin M.; RT "Complete genome sequence of Pseudomonas stutzeri DSM4166."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002622; AEA85198.1; -; Genomic_DNA. DR RefSeq; YP_005939940.1; NC_017532.1. DR ProteinModelPortal; F2N162; -. DR EnsemblBacteria; AEA85198; AEA85198; PSTAA_3329. DR GeneID; 12530472; -. DR KEGG; psr:PSTAA_3329; -. DR PATRIC; 54288468; VBIPseStu183391_3334. DR KO; K03574; -. DR BioCyc; PSTU996285:GLIZ-3331-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 312 AA; 33691 MW; FC66D520E4BE0753 CRC64; MKRIHVAAAV IRGPESSVLI AKRPLDKHQG GLWEFPGGKV EDGESVESAL ARELQEELGI EVTQAQPLIQ VRHDYPDKQV LLDVWEVLAF AGEPHGAEGQ PLAWVAPEEL VDYSFPAANR PIVTAARLPQ HYLITPDGLA MPRLLEGIAR ALDGGIRLIQ LRAPSLPPAD YRALAERVMA LCAGRAQLML KGPLEWVEDF PGAGWHLTAE QLRRAGSGRP VQAQRWLAAS CHGAEELALA AALEVDFVTL SPVQSTATHP GAPTLGWQRA ADLLSGFDRP VFLLGGLQVG DMGRARQIGA QGIAAIRAFW PD // ID F2N322_PSEU6 Unreviewed; 213 AA. AC F2N322; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PSTAA_3840; OS Pseudomonas stutzeri (strain DSM 4166 / CMT.9.A). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=996285; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4166 / CMT.9.A; RX PubMed=21515765; DOI=10.1128/JB.05039-11; RA Yu H., Yuan M., Lu W., Yang J., Dai S., Li Q., Yang Z., Dong J., RA Sun L., Deng Z., Zhang W., Chen M., Ping S., Han Y., Zhan Y., Yan Y., RA Jin Q., Lin M.; RT "Complete genome sequence of the nitrogen-fixing and rhizosphere- RT associated bacterium Pseudomonas stutzeri strain DSM4166."; RL J. Bacteriol. 193:3422-3423(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 4166; RA Yu H., Yuan M., Yang J., Yan Y., Jin Q., Lin M.; RT "Complete genome sequence of Pseudomonas stutzeri DSM4166."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002622; AEA85696.1; -; Genomic_DNA. DR RefSeq; YP_005940438.1; NC_017532.1. DR ProteinModelPortal; F2N322; -. DR EnsemblBacteria; AEA85696; AEA85696; PSTAA_3840. DR GeneID; 12530991; -. DR KEGG; psr:PSTAA_3840; -. DR PATRIC; 54289526; VBIPseStu183391_3846. DR KO; K00788; -. DR BioCyc; PSTU996285:GLIZ-3843-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22683 MW; 99A5EB7B84E94725 CRC64; MKESSRLRGL YAITDSKLLA DGRLLPYVEA ALKGGARLLQ YRDKTSDEAR RLREADALQE LCARHGAQLI INDDAELAAR LGVGLHLGQE DGSLAAARAL LGRQAIIGAT CHAQLPLAEQ AARDGASYVA FGRFFQSHTK PGAPAANHEL LREARARIGL PIVAIGGITL DTAPSLIAEG VQMIAVIHAL FAADSAAEVE RRAQAFSQLF NTP // ID F2N7A5_CORGP Unreviewed; 206 AA. AC F2N7A5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Corgl_0462; OS Coriobacterium glomerans (strain ATCC 49209 / DSM 20642 / JCM 10262 / OS PW2). OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Coriobacterium. OX NCBI_TaxID=700015; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49209 / DSM 20642 / JCM 10262 / PW2; RX PubMed=23961308; DOI=10.4056/sigs.3507020; RA Stackebrandt E., Zeytun A., Lapidus A., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Mikhailova N., RA Huntemann M., Pati A., Chen A., Palaniappan K., Chang Y.J., Land M., RA Hauser L., Rohde M., Pukall R., Goker M., Detter J.C., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Coriobacterium glomerans type strain RT (PW2(T)) from the midgut of Pyrrhocoris apterus L. (red soldier RT bug)."; RL Stand. Genomic Sci. 8:15-25(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002628; AEB06580.1; -; Genomic_DNA. DR RefSeq; YP_004372395.1; NC_015389.1. DR EnsemblBacteria; AEB06580; AEB06580; Corgl_0462. DR GeneID; 10438680; -. DR KEGG; cgo:Corgl_0462; -. DR PATRIC; 54444439; VBICorGlo157054_0503. DR KO; K00788; -. DR OMA; MEEAVIA; -. DR BioCyc; CGLO700015:GH6A-474-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 21798 MW; CB6D958B3CDCEF7A CRC64; MTSIAATATC QLGEPARSDP PFASGFARVA LTDRVHCARP LPEQVLRIAG RIDAIVVRER DLDDDAYERL ARAVAAACDE AGVALIVHGR PAVARRMGLN AVHLPLPQLV EQGRPAGIAW VGTNVHEPDE VELAQRSGAD YLMASPIFKP SCKPLAAARG LEFLERVLAC ARLPVLALGG IDDAAERAVR STGAAGACRM SGYMLL // ID F2N8E6_CORGP Unreviewed; 233 AA. AC F2N8E6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Corgl_1227; OS Coriobacterium glomerans (strain ATCC 49209 / DSM 20642 / JCM 10262 / OS PW2). OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Coriobacterium. OX NCBI_TaxID=700015; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49209 / DSM 20642 / JCM 10262 / PW2; RX PubMed=23961308; DOI=10.4056/sigs.3507020; RA Stackebrandt E., Zeytun A., Lapidus A., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Mikhailova N., RA Huntemann M., Pati A., Chen A., Palaniappan K., Chang Y.J., Land M., RA Hauser L., Rohde M., Pukall R., Goker M., Detter J.C., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Coriobacterium glomerans type strain RT (PW2(T)) from the midgut of Pyrrhocoris apterus L. (red soldier RT bug)."; RL Stand. Genomic Sci. 8:15-25(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002628; AEB07329.1; -; Genomic_DNA. DR RefSeq; YP_004373144.1; NC_015389.1. DR EnsemblBacteria; AEB07329; AEB07329; Corgl_1227. DR GeneID; 10439470; -. DR KEGG; cgo:Corgl_1227; -. DR PATRIC; 54446120; VBICorGlo157054_1319. DR KO; K00788; -. DR OMA; AICHAED; -. DR BioCyc; CGLO700015:GH6A-1264-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 56 60 HMP-PP binding (By similarity). FT REGION 153 155 THZ-P binding (By similarity). FT REGION 203 204 THZ-P binding (By similarity). FT METAL 89 89 Magnesium (By similarity). FT METAL 108 108 Magnesium (By similarity). FT BINDING 88 88 HMP-PP (By similarity). FT BINDING 127 127 HMP-PP (By similarity). FT BINDING 156 156 HMP-PP (By similarity). FT BINDING 183 183 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 24568 MW; 43D028FCD7A8C3DD CRC64; MERFAAQDPR RRGMWSRERI RASMLIYAVT DRSWLAGRTL EACVLQAIEG GATCVQLREK DRPTAEVAAI AERLVPCCRA HGIPLIIDDD VEAAARSGAD GVHVGQTDTA CREARARLGD DAIIGVSART VAEALAAEEA GADYLGVGAM FSTQTKADAT PVTRETLSGI CRAVSIPVTA IGGLSERTIP LLFGTGADGA AIVSAIFAAA DIEAATRALR MCAVRAFHRD GMK // ID F2NDP7_DESAR Unreviewed; 200 AA. AC F2NDP7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Desac_2576; OS Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophaceae; Desulfobacca. OX NCBI_TaxID=880072; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Desulfobacca acetoxidans DSM 11109."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002629; AEB10394.1; -; Genomic_DNA. DR RefSeq; YP_004371575.1; NC_015388.1. DR EnsemblBacteria; AEB10394; AEB10394; Desac_2576. DR GeneID; 10437801; -. DR KEGG; dao:Desac_2576; -. DR PATRIC; 54442540; VBIDesAce170587_2752. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; DACE880072:GHK9-2620-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 128 130 THZ-P binding (By similarity). FT REGION 179 180 THZ-P binding (By similarity). FT METAL 64 64 Magnesium (By similarity). FT METAL 83 83 Magnesium (By similarity). FT BINDING 63 63 HMP-PP (By similarity). FT BINDING 102 102 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 159 159 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 200 AA; 21249 MW; 367695D16C5AF6A1 CRC64; MKGYYFITDA RLSRAGNVSD VQSALAAGVR VVQYRDKWAD DAALIAEARL LRRLCQGAFF LINDRVEVAL AVGADGVHLG QKDLSCREAR RWLGAGKIIG ITVNTMEQAL EAARQGADYL GVAPIFATHT KPDAGAPAGL RLLREVRRRV NLPLIAIGGI NQDNAPAVIA AGADGICAIS AVVTRPDVQA AISGFQRLFG // ID F2NMU2_MARHT Unreviewed; 209 AA. AC F2NMU2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Marky_1741; OS Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Marinithermus. OX NCBI_TaxID=869210; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14884 / JCM 11576 / T1; RX PubMed=22675595; DOI=10.4056/sigs.2435521; RA Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S., RA Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., RA Palaniappan K., Land M., Pan C., Brambilla E.M., Rohde M., RA Tindall B.J., Sikorski J., Goker M., Detter J.C., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Woyke T.; RT "Complete genome sequence of the aerobic, heterotroph Marinithermus RT hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent RT chimney."; RL Stand. Genomic Sci. 6:21-30(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002630; AEB12476.1; -; Genomic_DNA. DR RefSeq; YP_004368586.1; NC_015387.1. DR ProteinModelPortal; F2NMU2; -. DR EnsemblBacteria; AEB12476; AEB12476; Marky_1741. DR GeneID; 10434659; -. DR KEGG; mhd:Marky_1741; -. DR PATRIC; 54435885; VBIMarHyd166763_1729. DR KO; K00788; -. DR BioCyc; MHYD869210:GHEE-1789-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23008 MW; 4C4567387E0B42B0 CRC64; MLGRLYLVAT PRPHWDAAEF TARVEAALAG GVEVLQLRVK DAEAQAYLGL ARRIRPLARR YGVPFFLNDR PDLAALAEAD GVHLGQGDLT PHEARRFFSG RIGRSTHRPE EARNALEEGV DYLSIGPVWP TPTKPGRPAA GLEYVRWAAR HLPADAVWYA IGGITLENLP EVLEAGARRV AVVRAILDAP DPERAAARFR EVLDGARER // ID F2NXC3_TRES6 Unreviewed; 223 AA. AC F2NXC3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tresu_0808; OS Treponema succinifaciens (strain ATCC 33096 / DSM 2489 / 6091). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=869209; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33096 / DSM 2489 / 6091; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Treponema succinifaciens DSM RT 2489."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002631; AEB13736.1; -; Genomic_DNA. DR RefSeq; YP_004365033.1; NC_015385.1. DR EnsemblBacteria; AEB13736; AEB13736; Tresu_0808. DR GeneID; 10430902; -. DR KEGG; tsu:Tresu_0808; -. DR PATRIC; 54428195; VBITreSuc166698_0850. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; TSUC869209:GHSS-816-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23955 MW; 6C136E23EFA88643 CRC64; MKSVELKTSL LLYAVTDRAW LGKNFCCETL SDAVFQAIEG GATLIQLREK ELSEKEFLDE AFSIKEICAS KKIPLIINDN VKIAKETDVC GVHIGQSDME LKEARKILGA DKIIGVSCQT VEQALQAEKN GADYLGVGAV FSTSTKTDAD NVPLSTLKEI CSSVKIPVVA IGGISLQNMS QLKGSGIAGV SVISAIFAQQ DIRSSTKELK SSAEKLFLSF IDC // ID F2P555_PHOMO Unreviewed; 405 AA. AC F2P555; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PMSV_4119; OS Photobacterium leiognathi subsp. mandapamensis svers.1.1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=1001530; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Svers.1.1.; RA Urbanczyk H., Ogura Y., Hendry T.A., Gould A.L., Kiwaki N., RA Atkinson J.T., Hayashi T., Dunlap P.V.; RT "Genome Sequence of Photobacterium mandapamensis svers.1.1., the RT Bioluminescent Symbiont of the Cardinalfish Siphamia versicolor."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF093593; GAA03076.1; -; Genomic_DNA. DR EnsemblBacteria; GAA03076; GAA03076; PMSV_4119. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 405 AA; 44540 MW; 038B319DE52ACF86 CRC64; MSTLSLPKAL SPLVMHIEPL LAAAADYQLG EQVTLMPSSL DWAEVSTPSS IKRVGFEQAC SIELIDYEIQ DQWGSIDAKL SSLKAQVLKC PELVVCGLPV KGGYLDIWHH DGEVRGCFSV ERGNQTQQRA MLLAALALNY PLEDALVLAR AYAQSTQMGI WPTERDAFPD IVCANFSKLS DIGWQSEYQP VEAFAPVDSE KLTLYPVVDS VQWVKQLLEL DVKTTQLRIK DPNAQGLEQD VAHAIALGQQ ANAQVFINDY WQLAIEHGAF GVHLGQEDLA VADLNAIQQA TLRLGISTHG YYEILRAMAF NPSYIALGHI YPTTTKQMPS LPQGVHRLKL YQQLIGNAFP TVAIGGIDLS RVPVVWDTGV SSVAVVRAIT QSSEPAIAVE QLNKCLVQRE VMYDN // ID F2PLW6_TRIEC Unreviewed; 517 AA. AC F2PLW6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE SubName: Full=Hydroxyethylthiazole kinase; GN ORFNames=TEQG_01922; OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse OS ringworm fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; OC mitosporic Arthrodermataceae; Trichophyton. OX NCBI_TaxID=559882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4606 / CBS 127.97; RX PubMed=22951933; DOI=10.1128/mBio.00259-12; RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W., RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E., RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I., RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., RA Summerbell R.C., Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., RA White T.C.; RT "Comparative genome analysis of Trichophyton rubrum and related RT dermatophytes reveals candidate genes involved in infection."; RL MBio 3:E259-E259(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995724; EGE02884.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 517 AA; 54470 MW; D6A3C4B0BDFEE72B CRC64; MPMNLSLYLV TDSTPKILGD RDLCSVVEQA VQGGVTIVQY RDKHSDTKEL IKTAAKLHDI TLNYGIPLII NDRVDVALAV GAEGVHLGQD DMNIAVARNM LPKGTIIGVT VSSVEEAQAA VESGADYLGI GTVYATPTKT NTKSIIGTAG VKRILNCVAS LNPRVGTVAI GGINLDNVQR IIYQSQDTKK GLEGVAIVSA IMAAENPRAT AALFLDKVSK NPAFATIPTP PRENEEELLL SKVDGLVRKV ATVHPLCHNM INYVVANFAA NVALAVGASP IMSGYGLEAP DLAKNKGSLL INMGTLNSES LNNYLQAIRA YNEAGNPVVL DPVGAAATQI RRQSVKTLMQ GGYFDLIKGN ESEIGHIYGH TGNQVGVDSG PSALDAKEKA MLLIISPGCI VLLTGPTDYL SDGARTIAIH NGHPLLGQVT GTGCVIGTVT SAFLAVERQD KLLAVLSALL MFEVAAERAV ISGVKGPGSF VPALLDELYS LRTQATESKS ASIDTLKKAA KVNFIHF // ID F2QEI7_STROU Unreviewed; 210 AA. AC F2QEI7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SOR_1402; OS Streptococcus oralis (strain Uo5). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=927666; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Uo5; RX PubMed=21460080; DOI=10.1128/JB.00321-11; RA Reichmann P., Nuhn M., Denapaite D., Bruckner R., Henrich B., RA Maurer P., Rieger M., Klages S., Reinhard R., Hakenbeck R.; RT "Genome of Streptococcus oralis strain Uo5."; RL J. Bacteriol. 193:2888-2889(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR720602; CBZ01056.1; -; Genomic_DNA. DR RefSeq; YP_004326396.1; NC_015291.1. DR EnsemblBacteria; CBZ01056; CBZ01056; SOR_1402. DR GeneID; 10416287; -. DR KEGG; sor:SOR_1402; -. DR PATRIC; 54425332; VBIStrOra177080_1289. DR KO; K00788; -. DR BioCyc; SORA927666:GH8G-1402-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22907 MW; AFC307978674535A CRC64; MNREALRLYL VTNRYQDSLE NFLEKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE TWGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLAATGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDDIIF // ID F2QV82_PICP7 Unreviewed; 560 AA. AC F2QV82; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 19. DE SubName: Full=Putative uncharacterized protein; GN OrderedLocusNames=PP7435_Chr3-0341; OS Komagataella pastoris (strain ATCC 76273 / CBS 7435 / CECT 11047 / OS NRRL Y-11430 / Wegner 21-1) (Yeast) (Pichia pastoris). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Komagataella. OX NCBI_TaxID=981350; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner RC 21-1; RX PubMed=21575661; DOI=10.1016/j.jbiotec.2011.04.014; RA Kuberl A., Schneider J., Thallinger G.G., Anderl I., Wibberg D., RA Hajek T., Jaenicke S., Brinkrolf K., Goesmann A., Szczepanowski R., RA Puhler A., Schwab H., Glieder A., Pichler H.; RT "High-quality genome sequence of Pichia pastoris CBS7435."; RL J. Biotechnol. 154:312-320(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS 7435; RA Kueberl A., Schneider J., Thallinger G.G., Anderl I., Wibberg D., RA Hajek T., Jaenicke S., Brinkrolf K., Goesmann A., Szczepanowski R., RA Puehler A., Schwab H., Glieder A., Pichler H.; RT "High-quality genome sequence of Pichia pastoris CBS 7435."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR839630; CCA39310.1; -; Genomic_DNA. DR ProteinModelPortal; F2QV82; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 560 AA; 60335 MW; 4B3FC58A6A014908 CRC64; MNRTDFDLSI YLVTNAEMVP EGLSFLDQVR KAIDNGVTTI QLREKNIETR DFIERASQVH ELTKAAGIPL IINDRVDVAL AVDAEGVHVG QTDMPVPLVR KLVGEDKIIG VSTGKVEEAR QAIKDGADYV GIGIVYDTKT KDHKKIPFGT LGIREILTVL LNEGGAGIKT CAIGGVNQTN VQKVLYQGSI PGKKLDGVAI VSCIMAQEDA AEATRVLVEK FHSHAPWLSD DHRADNDFFN NVTEKAKKVA DTNPMIHHIT NAVVKNFSAN VTLAVGASPI MSESYQEFEE FARLPTTGLV LNTGTQSAEN FVQMVIAAAK AYNATGNPIV FDPVGCGASE MRKHRTRLFL DAGYYTVIKG NVSEILTVAG EANQMRGVDT GDLSNLTEEA IVAAAKRAAL NNRCIVVVTG AVDYIVDGIL DGANYYESQP TQRVFKVQGG SSIMGDVTGT GCSLGSAIAA YITTFPATPL EATIAAVHHY KYVGAVAARR STTPNGISDS GPRPGSFMSN FLDDLYGFRT QESKVGHKIL LGPNPDKTFY TKLESSENGR YPAEVEEIFI // ID F2RI67_STRVP Unreviewed; 227 AA. AC F2RI67; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SVEN_1763; OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / OS JCM 4526 / NBRC 13096 / PD 04745). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=953739; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / RC PD 04745; RX PubMed=21463507; DOI=10.1186/1471-2164-12-175; RA Pullan S.T., Chandra G., Bibb M.J., Merrick M.; RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae RT provides new insights into global nitrogen regulation in RT actinomycetes."; RL BMC Genomics 12:175-175(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR845719; CCA55050.1; -; Genomic_DNA. DR RefSeq; YP_006877309.1; NC_018750.1. DR ProteinModelPortal; F2RI67; -. DR EnsemblBacteria; CCA55050; CCA55050; SVEN_1763. DR GeneID; 13820887; -. DR KEGG; sve:SVEN_1763; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 23919 MW; BEBA3BD47A0424FB CRC64; MTPTGEPVMS TPREQLADAR LYLCTDARKR QGDLPAFLDA VLSSGVDIVQ LRDKGMEAGE ELEHLAVFAE AARRHGRLLA VNDRADVAHA IGSDVLHLGQ GDLPVPAARA ILGGPDGVLI GRSCHAEAEV AAAAAEPGVD YFCTGPCWPT PTKPGRYAPG LDLVRYAAGL AQDRPWFAIG GIDESNLDEV LDAGARRIVV VRAITEADDP AAATAALAKR VRERAGE // ID F2RQL0_TRIT1 Unreviewed; 520 AA. AC F2RQL0; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 16. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=TESG_01151; OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; OC mitosporic Arthrodermataceae; Trichophyton. OX NCBI_TaxID=647933; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 112818; RX PubMed=22951933; DOI=10.1128/mBio.00259-12; RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W., RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E., RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I., RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., RA Summerbell R.C., Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., RA White T.C.; RT "Comparative genome analysis of Trichophyton rubrum and related RT dermatophytes reveals candidate genes involved in infection."; RL MBio 3:E259-E259(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG698480; EGD93609.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 520 AA; 54999 MW; 13AFB2F1B3FA87FE CRC64; MPMNLSLYLV TDSTPKILGD RDLCSVVEQA VQGGVTIVQY RDKHSDTKEL IKTAAKLHDI TLNYGIPLII NDRVDVALAV GAEGVHLGQD DMNIAVARNM LPKGTIIGVT VSSVEEAQAA VESGADYLGI GTVYATPTKT NTKSIIGTAG VKRILNCVAS LNPRVGTVAI GGINLDNVQR IIYQSQDTKK GLEGVAIVSA IMAAENPRAT AALFLDKVSK NPAFATIPIS PRENEEELLL SKVDGLVRKV ATVHPLCHNM INYVVANFAA NVALAVGASP IMSGYGLEAP DLAKNKGSLL INMGTLNSES LNNYLQAIRA YNEAGNPVVL DPVGAAATQI RRQSVKTLMQ GGYFDLIKGN ESEIGHIYGH TGNQVGVDSG PSALDAKEKA MLVRDLALRE RCIVLLTGPT DYLSDGARTI AIHNGHPLLG QVTGTGCVIG TVTSAFLAVE RQDKLLAVLS ALLMFEVAAE RAVISGVKGP GSFVPALLDK LYSLRTQATE SKSASIDTLK KAAKVNFIHF // ID F2SKA1_TRIRC Unreviewed; 520 AA. AC F2SKA1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 16. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=TERG_03454; OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's OS foot fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; OC mitosporic Arthrodermataceae; Trichophyton. OX NCBI_TaxID=559305; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4607 / CBS 118892; RX PubMed=22951933; DOI=10.1128/mBio.00259-12; RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W., RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E., RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I., RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., RA Summerbell R.C., Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., RA White T.C.; RT "Comparative genome analysis of Trichophyton rubrum and related RT dermatophytes reveals candidate genes involved in infection."; RL MBio 3:E259-E259(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG700650; EGD87204.1; -; Genomic_DNA. DR RefSeq; XP_003236409.1; XM_003236361.1. DR GeneID; 10373226; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 520 AA; 55057 MW; DFA2BF2CACCB778C CRC64; MPVNLSLYLV TDSTPKILGD RDLCSVVEQA VQGGVTIVQY RDKHSDTKEL IKTAAKLHDI TLNHGIPLII NDRVDVALAV GAEGVHLGQD DMNIAVARKI LPKGTIIGVT VSSVEEAQVA VESGADYLGI GTVYATPTKT NTKSIIGTAG VKRILSCVAS LNPRVGTVAI GGINLDNVQR IIYQSQDTKK GLEGVAIVSA IMAAENPRAT AALFLDKVSK NPTFATIPIS PRENEEELLL GKVDGLVRKV ATVHPLCHNM INYVVANFAA NVALAIGASP IMSGYGLEAP DLAKNKGSLL INMGTLNSES LDNYMQAIRA YNEAGNPVVL DPVGAAATQL RRQSVKTLMH GGYFDLIKGN ESEIGHIYGH TGNQVGVDSG PSTLDTKEKA MLVRDLALRE RCIVLLTGPT DYLSDGARTI AIHNGHPLLG QVTGTGCVIG TVTSAFLAVE RQDKLLAVLS ALLMFEVAAE RAVVSGVKGP GSFVPALLDE LYSLRTQATE SKSASIDTLK KTAKVNFIHF // ID F2TFF5_AJEDA Unreviewed; 540 AA. AC F2TFF5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-APR-2014, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BDDG_04911; OS Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces OS dermatitidis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Ajellomyces. OX NCBI_TaxID=653446; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 18188 / CBS 674.68; RA Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., RA Gargeya S., Alvarado L., Berlin A.M., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Blastomyces dermatitidis strain ATCC 18188."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG749429; EGE81968.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 57190 MW; 8C29D99521914511 CRC64; MDLSVYLVTD STPAILGNRD LCEVVQDALE GGVTVVQYRD KHSDTGVMID MAKRLHGITK KYNVPLIIND RVDVALAVGA EGVHLGQDDM KITEAKKLLP PNTYIGVSVR SNEEAFRAVQ DGADYVGIGT VFATPTKTDT KSIIGTAGTR DILAFLSTMP RKVGAVAIGG INLTNVQRVI YQSQAPLKSL DGAAIVSAIM AAESPREAAA SFCRLVKQIP ASATLPVPAR ENEVSLLLDQ VPDIVSLVAT KRPLCHNMIN FVVANFAANV AIAIGASPIM SGYGPEAPDL AKNGGSLLIN MGTLNNESLD NYLQALRAYN AEGNPVVFDP VGAGATDIRR KATKQLLAGG YFDLIKGNES ELIQVYGKAR GNQVGVDSGP STLNPEEKAK LVKDLARRER NIVLLTGSVD YLSDGERTLA IGNGHQFLGH ITGTGCIIGT MAASFLAVHR SDKLLAVFAS LLLLEIAAER AAMKDGVHGP GTFLPAFIDE LFTLRQWAVD WKSGDAAGGT GAGAKTSNGD ASAVDENIFR KMAKVHLINM // ID F2UZM6_ACTVI Unreviewed; 220 AA. AC F2UZM6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0059_01901; OS Actinomyces viscosus C505. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Actinomycineae; Actinomycetaceae; Actinomyces. OX NCBI_TaxID=562973; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C505; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., RA White J., Yandava C., Sibley C.D., Field T.R., Grinwis M., RA Eshaghurshan C.S., Surette M.G., Haas B., Nusbaum C., Birren B.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C505; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R., RA Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Actinomyces viscosus C505."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACRE02000007; EGE37630.1; -; Genomic_DNA. DR EnsemblBacteria; EGE37630; EGE37630; HMPREF0059_01901. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22559 MW; EBFD8E761BA76108 CRC64; MRAAPDLSVY LVTDEGQCRS RGRDVLATVE AAVDGGVTCV QLRAKGTDGG LFLTQVLEVA EVIGDQVPVI VNDRVDIFLA ARDQGAPVAG VHLGQSDLPA RIARRLVGEE AYLGLSAATP DELRTAQEQG ACDHVGIGVV HPTATKADAP KSLGVNGVAR MAALIDLPAV AIGGITASDL PALRAGGLAG AAVVSAICTA EDPRSVAADL HRAWDEGCRR // ID F2V249_MYCTX Unreviewed; 222 AA. AC F2V249; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TBPG_00079; OS Mycobacterium tuberculosis W-148. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=659019; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=W-148; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease.; RA Galagan J., Murray M., Pillay M., Borowsky M.L., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D., Larson L., RA Mehta T., Neiman D., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain W-148."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL877853; EGE49172.1; -; Genomic_DNA. DR ProteinModelPortal; F2V249; -. DR SMR; F2V249; 1-221. DR EnsemblBacteria; EGE49172; EGE49172; TBPG_00079. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID F2ZIH6_9PSED Unreviewed; 219 AA. AC F2ZIH6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 13. DE SubName: Full=Uncharacterized protein; DE Flags: Fragment; GN ORFNames=POR16_10756; OS Pseudomonas syringae pv. oryzae str. 1_6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas coronafaciens. OX NCBI_TaxID=563797; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_6; RX PubMed=19015323; DOI=10.1101/gr.083311.108; RA Reinhardt J.A., Baltrus D.A., Nishimura M.T., Jeck W.R., Jones C.D., RA Dangl J.L.; RT "Dynamic Evolution of Pathogenicity Revealed by Sequencing and RT Comparative Genomics of 19 Pseudomonas syringae Isolates."; RL Genome Res. 19:294-305(2009). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_6; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Muhktar M.S., Cherkis K., RA Roach J., Grant S., Jones C.D., Dangl J.L.; RT "Dynamic Evolution of Pathogenicity Revealed by Sequencing and RT Comparative Genomics of 19 Pseudomonas syringae Isolates."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABZR01000269; EGI02216.1; -; Genomic_DNA. DR ProteinModelPortal; F2ZIH6; -. DR EnsemblBacteria; EGI02216; EGI02216; POR16_10756. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; FT NON_TER 1 1 SQ SEQUENCE 219 AA; 23667 MW; 437E5AA0C45816F0 CRC64; EGQPLVWATS RELPDYEFPA ANQPIVAAAC LPGEYLITPE GLDNIELLRG MQKAVAGGIK LVQLRAPGGY DPKYRDLAVD AAGLCAGKAQ LMLKGPLEWL GDFPSAGWHL TSEQLRKYAS RGRPFPENRW LAASCHDAEE LALAEQMGVD FVTLSPLQPT LTHPDAQPLG WDQATRLIAG FNKPVFLLGG VGPAELKQAW ESGAQGVAGI RAFWPDEIL // ID F2ZLR1_9PSED Unreviewed; 205 AA. AC F2ZLR1; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=POR16_16529; OS Pseudomonas syringae pv. oryzae str. 1_6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas coronafaciens. OX NCBI_TaxID=563797; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_6; RX PubMed=19015323; DOI=10.1101/gr.083311.108; RA Reinhardt J.A., Baltrus D.A., Nishimura M.T., Jeck W.R., Jones C.D., RA Dangl J.L.; RT "Dynamic Evolution of Pathogenicity Revealed by Sequencing and RT Comparative Genomics of 19 Pseudomonas syringae Isolates."; RL Genome Res. 19:294-305(2009). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_6; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Muhktar M.S., Cherkis K., RA Roach J., Grant S., Jones C.D., Dangl J.L.; RT "Dynamic Evolution of Pathogenicity Revealed by Sequencing and RT Comparative Genomics of 19 Pseudomonas syringae Isolates."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABZR01000451; EGI03351.1; -; Genomic_DNA. DR ProteinModelPortal; F2ZLR1; -. DR EnsemblBacteria; EGI03351; EGI03351; POR16_16529. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22106 MW; 7A8B34FD8EDB5E89 CRC64; MKLRGLYAIT DSQLLTGRFL SYVEAALEGG VTLLQYRDKT HDESRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGSL DLAERAKADG ATYVAFGRFF NSQTKPGAPA VPLDLIAQVR TKVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAET SREVTRRAKA FTALL // ID F3A1T9_9BACL Unreviewed; 210 AA. AC F3A1T9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0428_00697; OS Gemella haemolysans M341. OC Bacteria; Firmicutes; Bacilli; Bacillales; OC Bacillales Family XI. Incertae Sedis; Gemella. OX NCBI_TaxID=562981; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M341; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R., RA Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Gemella haemolysans M341."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACRO01000007; EGF85640.1; -; Genomic_DNA. DR EnsemblBacteria; EGF85640; EGF85640; HMPREF0428_00697. DR PATRIC; 54842728; VBIGemHae124407_0689. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23283 MW; 551ABD7D9CD916F0 CRC64; MFNKELLKLY FICGTTTCLG KDLYTVVEDA LVGGITLFQF REKGKGALEG KEKLELAIKL QNLCKKYNVP FIVNDDIELA LEIDADGVHV GQDDLGVDEI RKLMPNKIIG LSIGNEEEFK QSKVEYVDYV GVGPVYVTQS KDDAGGAIGY EGLELMRKLL PEMPLVAIGG IQTQHIKDIM KTNVDGVSII SAISYSDNIE KTVREMNEQF // ID F3A5X1_9BACL Unreviewed; 211 AA. AC F3A5X1; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0433_00196; OS Gemella sanguinis M325. OC Bacteria; Firmicutes; Bacilli; Bacillales; OC Bacillales Family XI. Incertae Sedis; Gemella. OX NCBI_TaxID=562983; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M325; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R., RA Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Wortman J., RA Nusbaum C., Birren B.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M325; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R., RA Grinwis M., Eshaghurshan C.S., Surette M.G., Walker B., Young S., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Gemella sanguinis M325."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACRY02000002; EGF89077.1; -; Genomic_DNA. DR EnsemblBacteria; EGF89077; EGF89077; HMPREF0433_00196. DR PATRIC; 54845670; VBIGemSan95479_0188. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23161 MW; F71D7B0F3D742A8B CRC64; MFNPESLKLY FICGTTTCNG RNLLEVVEKA LAGGITLFQF REKGKDALEG KEKEDLAREI QKLCKNYNVP FIVNDDVELA IKLNADGVHV GQEDSDVELI REKMPDAILG LSIGDELEYK SSNLSVVDYI GVGPIFSTIS KDDAGKAIGY TGLKQIRELD RSLPIVAIGG ISRDKIKPIM DTGIEGVSII SAISYADDIE KEVSLMLKQF N // ID F3AAE1_9FIRM Unreviewed; 218 AA. AC F3AAE1; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0992_00036; OS Lachnospiraceae bacterium 6_1_63FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658083; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_63FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 6_1_63FAA."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTV01000001; EGG85109.1; -; Genomic_DNA. DR EnsemblBacteria; EGG85109; EGG85109; HMPREF0992_00036. DR PATRIC; 54848914; VBILacBac91825_0036. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 24057 MW; CE1958B4851BCD3C CRC64; MRLERKNMCL YAVTDRSWIG EKSFLEQIED SLKGGVTLLQ LREKNLSREE FLKEAQEVKK LTDKYGVPFI INDDVEIALQ VDAAGVHVGQ KDMEAGEARQ KLGADKILGV SCRTVEDAKK AEQMGADYLG VGAMFATSTK TEAEVITTER LRSICQAVAI PVVAIGGIKE ENITKLRDCG ISGVAVISGI YAQKDIESAC QRFLKLSKEI TQQEVKEK // ID F3ACL4_9FIRM Unreviewed; 195 AA. AC F3ACL4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF0992_00809; OS Lachnospiraceae bacterium 6_1_63FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658083; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_63FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 6_1_63FAA."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTV01000005; EGG80023.1; -; Genomic_DNA. DR ProteinModelPortal; F3ACL4; -. DR EnsemblBacteria; EGG80023; EGG80023; HMPREF0992_00809. DR PATRIC; 54850514; VBILacBac91825_0819. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 195 AA; 22220 MW; 9C3F27611EC5F2E9 CRC64; MCREEIFQNV IAVSNRKLCT RPFPEQIEIV CRHRPQSLIL REKDLNESEY GKLGQEVKEI CKKYQVTCIY HTFYEEAKKA GVRNIHLPLW KLEELNEEDG QRDFDLIGAS IHSVEEAKKA EKLGATYLTA GHIYETGCKP DLPPRGLNFL KEVCQVVDIP VYAIGGIRLE KQQIAEIQKA GARGACIMSE LMKIS // ID F3AK59_9FIRM Unreviewed; 217 AA. AC F3AK59; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0987_00833; OS Lachnospiraceae bacterium 9_1_43BFAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658088; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=9_1_43BFAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 9_1_43BFAA."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTX01000004; EGG87181.1; -; Genomic_DNA. DR EnsemblBacteria; EGG87181; EGG87181; HMPREF0987_00833. DR PATRIC; 54856052; VBILacBac68115_0851. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23212 MW; F379C3F763F8FD60 CRC64; MRTGNQVDLT LYLVTDSTYH TTESLLRTVE EACKGGVTLV QLREKEAGGK EYLEKAILVK KITDRYGVPL IIDDRVDVAI ACDAAGVHVG ASDLPVAVAR KLLGPEKIIG ATAKTVEAAK KAWEEGADYL GVGAIYPTTT KVITILTKPE TLKAICETVP IPVTAIGGLN AENLEILRGC KMDGVAVVSA IMKADDPKRA AEHLKEKICK LKDTEGK // ID F3B0Q0_9FIRM Unreviewed; 211 AA. AC F3B0Q0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0491_00516; OS Lachnospiraceae oral taxon 107 str. F0167. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=575593; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0167; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V., RA Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium oral taxon 107 RT strain F0167."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADDS01000005; EGG90645.1; -; Genomic_DNA. DR EnsemblBacteria; EGG90645; EGG90645; HMPREF0491_00516. DR PATRIC; 54867446; VBILacOra53760_0515. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23108 MW; C879FDB617039960 CRC64; MKLDKKYMHL YAITDRSWTG EKSLYEQIEE ALKNGVSCLQ LREKNLDEDE FIKEAKKTAA LCKKYSIPFI VNDNVNVAIA SNADGIHIGQ DDMDIKKVRS LVGEKMIIGV SAHTVKEAIA AEKNGADYIG IGAVFNTSTK NDVMQVSYEK LKSICEAVSI PKVAIGGINR DNILKLKGSK IDGVAVISAI FGAKDIGSAI KELDILIKEL F // ID F3BL19_PSEHA Unreviewed; 511 AA. AC F3BL19; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE SubName: Full=Phosphomethylpyrimidine kinase / thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN ORFNames=PH505_bf00020; OS Pseudoalteromonas haloplanktis ANT/505. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=722419; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ANT/505; RA Troung L.V., Kabisch J., Thuermer A., Lehmann R., Liesegang H., RA Welsch N., Daniel R., Schweder T.; RT "Pectinolytic activity of the psychrophilic marine bacterium RT Pseudoalteromonas haloplanktis ANT/505."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADOP01000032; EGI72687.1; -; Genomic_DNA. DR EnsemblBacteria; EGI72687; EGI72687; PH505_bf00020. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 511 AA; 55088 MW; 47DD8486CF533099 CRC64; MNNVVWTIAG SDSGGGAGIQ ADIKAMQSFG VHGCTAITAL TAQNSLGVEA INAVSTDIIE SQLLALEKDM KAKVIKIGML ANVQQIQLIS EHISHYKAKW TVPPVIVYDP VAIASSGDLL TEEDTVSAIK ECLLPLVDVI TPNTHETQLL TGVYLIGPAA IKEAASKLLS WGAKAVVIKG GHWDYPSGYC IDYCIDSNTQ NGEEYWLGNQ KIQTPHNHGT GCSMASVIAA CLAKDYPLKD AFILAKAYIN QGLKQSVRYG EGIGPVAQTS FPTNLADYPQ VIEPGSWLGD ELDFDVPLDF NMAADFAPCE SKSLGLYAVV DSADWLEKCL QQGIKTAQLR VKNKTQDELD ELIKQAVELG KQYNAQVFIN DYWQLAIKHG AYGVHLGQED LDIANLAAIK DAGLRLGLST HGFYEMLRAH NYRPSYMAFG AIYPTTTKDM TGQIQGLEKL IKFVPLMQSY PTVAIGGIDL SRAEQVAKTG VGSVAVVRAI TEADNYVEAI SALQVAISSA N // ID F3BV70_PROAA Unreviewed; 216 AA. AC F3BV70; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9343_01739; OS Propionibacterium acnes HL099PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765063; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL099PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWH01000082; EGF74028.1; -; Genomic_DNA. DR EnsemblBacteria; EGF74028; EGF74028; HMPREF9343_01739. DR PATRIC; 51958893; VBIProAcn164029_1596. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22628 MW; CC3F100B367E1034 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALYG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F3BXK8_PROAA Unreviewed; 217 AA. AC F3BXK8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9343_02568; OS Propionibacterium acnes HL099PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765063; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL099PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWH01000111; EGF73302.1; -; Genomic_DNA. DR ProteinModelPortal; F3BXK8; -. DR EnsemblBacteria; EGF73302; EGF73302; HMPREF9343_02568. DR PATRIC; 51960512; VBIProAcn164029_2370. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F3C1V3_PSESG Unreviewed; 189 AA. AC F3C1V3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Uncharacterized protein; GN ORFNames=Pgy4_07464; OS Pseudomonas syringae pv. glycinea str. race 4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=875330; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Race 4; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWY01000299; EGH09097.1; -; Genomic_DNA. DR EnsemblBacteria; EGH09097; EGH09097; Pgy4_07464. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 189 AA; 20372 MW; C045A1734170007D CRC64; MGGNYLITPD GLDNIELLRG MQKAIAGGIK LVQLRAPGGY DPKYRDLAVD AAGLCAGKAQ LMLKGPLEWL GDFPSAGWHL TAEQLRKYAS RGRPFPENRW LAASCHNAEE LALAEQMGVD FVTLSPVQPT LTHPDAQPLG WQQAAQLIAG FNKPVFLLGG VGPSERQQAW ESGAQGVAGI RAFWPDEIV // ID F3CMQ8_PROAA Unreviewed; 217 AA. AC F3CMQ8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9579_00619; OS Propionibacterium acnes HL087PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765081; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL087PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXQ01000005; EGF69748.1; -; Genomic_DNA. DR ProteinModelPortal; F3CMQ8; -. DR EnsemblBacteria; EGF69748; EGF69748; HMPREF9579_00619. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F3CQS4_PROAA Unreviewed; 216 AA. AC F3CQS4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9579_02022; OS Propionibacterium acnes HL087PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765081; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL087PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADXQ01000015; EGF67970.1; -; Genomic_DNA. DR ProteinModelPortal; F3CQS4; -. DR EnsemblBacteria; EGF67970; EGF67970; HMPREF9579_02022. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F3CUL3_PROAA Unreviewed; 217 AA. AC F3CUL3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9563_00486; OS Propionibacterium acnes HL020PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765065; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL020PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYO01000004; EGF71468.1; -; Genomic_DNA. DR ProteinModelPortal; F3CUL3; -. DR EnsemblBacteria; EGF71468; EGF71468; HMPREF9563_00486. DR PATRIC; 52085006; VBIProAcn162044_0454. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F3CY66_PROAA Unreviewed; 216 AA. AC F3CY66; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9563_01961; OS Propionibacterium acnes HL020PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765065; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL020PA1; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADYO01000024; EGF67236.1; -; Genomic_DNA. DR ProteinModelPortal; F3CY66; -. DR EnsemblBacteria; EGF67236; EGF67236; HMPREF9563_01961. DR PATRIC; 52087922; VBIProAcn162044_1848. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F3D2F0_PROAA Unreviewed; 217 AA. AC F3D2F0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9588_00729; OS Propionibacterium acnes HL025PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765090; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL025PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZO01000018; EGF72128.1; -; Genomic_DNA. DR ProteinModelPortal; F3D2F0; -. DR EnsemblBacteria; EGF72128; EGF72128; HMPREF9588_00729. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F3D5M7_PROAA Unreviewed; 216 AA. AC F3D5M7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9588_01873; OS Propionibacterium acnes HL025PA2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765090; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL025PA2; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZO01000040; EGF68532.1; -; Genomic_DNA. DR ProteinModelPortal; F3D5M7; -. DR EnsemblBacteria; EGF68532; EGF68532; HMPREF9588_01873. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F3DC62_9PSED Unreviewed; 205 AA. AC F3DC62; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSYAE_08047, PSYAE_28288; OS Pseudomonas syringae pv. aesculi str. 0893_23. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629258; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=0893_23; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAD01000143; EGH01906.1; -; Genomic_DNA. DR EMBL; AEAD01000896; EGH05794.1; -; Genomic_DNA. DR EnsemblBacteria; EGH01906; EGH01906; PSYAE_08047. DR EnsemblBacteria; EGH05794; EGH05794; PSYAE_28288. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21968 MW; 8D8113EA1D6B9C94 CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKT SDESRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGSL ELAEQAKADG ATYVAFGRFF NSLTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN AQEVTRRAKA FMALL // ID F3DGJ0_9PSED Unreviewed; 316 AA. AC F3DGJ0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 17. DE SubName: Full=Uncharacterized protein; GN ORFNames=PSYAE_16026; OS Pseudomonas syringae pv. aesculi str. 0893_23. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629258; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=0893_23; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAD01000270; EGH03434.1; -; Genomic_DNA. DR ProteinModelPortal; F3DGJ0; -. DR EnsemblBacteria; EGH03434; EGH03434; PSYAE_16026. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34047 MW; 86C092002609A949 CRC64; MKRVHVAAAV IRGADGSVLI ARRADTQHQG GLWEFPGGKV EEGETVQAAL ARELQEELGI QVTAARPLIK VGHDYADKQV LLDVWEVSAF TGEPHGAEGQ PLVWAAPREL PDYDFPAANQ PIVAAARLPG EYLITPDGLD NIELLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPENRWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDALPLGWQQ AAQLIAGFNK PVFLLGGVGP SERQQAWESG AQGVAGIRAF WPDEIV // ID F3DRC4_9PSED Unreviewed; 205 AA. AC F3DRC4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSYMP_04125; OS Pseudomonas syringae pv. morsprunorum str. M302280. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629259; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302280; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAE01000064; EGH07704.1; -; Genomic_DNA. DR EnsemblBacteria; EGH07704; EGH07704; PSYMP_04125. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21982 MW; 85A9B3080867D129 CRC64; MKLRGLYAIT DSQLLTGKFL SYVEAALDGG VTLLQYRDKT GDDSRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGQL ELAEQAKADG ATYVAFGRFF NSQTKPGAPA VPLDLIAQVR AKVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGADN TQEVTRRAKA FMALL // ID F3DYG2_9PSED Unreviewed; 316 AA. AC F3DYG2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Uncharacterized protein; GN ORFNames=PSYMP_16721; OS Pseudomonas syringae pv. morsprunorum str. M302280. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629259; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302280; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAE01000321; EGH11266.1; -; Genomic_DNA. DR ProteinModelPortal; F3DYG2; -. DR EnsemblBacteria; EGH11266; EGH11266; PSYMP_16721. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34065 MW; AF8985EB5E3F3EC4 CRC64; MKRVHVAAAV IRGTDGRVLI ARRADSQHQG GLWEFPGGKV EAGETVEMAL ARELQEELGI VVTAARPLIK VCHDYPDKQV LLDVWEVSAF TGEPHGAEGQ PLVWASPREL ANYDFPAANQ PIVAAARLPG EYLITPEGLD NIELLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAQ QLRKYASNGR PFPENRWLAA SCHSAEELAL AEQMGVDFVT LSPVQPTLTH PDAHPLGWEQ AAQLIAGFNK PVFLLGGVGP AQCQQAWESG AQGVAGIRAF WPDKIV // ID F3EGE2_PSESL Unreviewed; 316 AA. AC F3EGE2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE SubName: Full=Uncharacterized protein; GN ORFNames=PLA107_19104; OS Pseudomonas syringae pv. lachrymans str. M301315. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629260; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M301315; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAF01000221; EGH85248.1; -; Genomic_DNA. DR ProteinModelPortal; F3EGE2; -. DR EnsemblBacteria; EGH85248; EGH85248; PLA107_19104. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 316 AA; 34047 MW; 86C092002609A949 CRC64; MKRVHVAAAV IRGADGSVLI ARRADTQHQG GLWEFPGGKV EEGETVQAAL ARELQEELGI QVTAARPLIK VGHDYADKQV LLDVWEVSAF TGEPHGAEGQ PLVWAAPREL PDYDFPAANQ PIVAAARLPG EYLITPDGLD NIELLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPENRWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDALPLGWQQ AAQLIAGFNK PVFLLGGVGP SERQQAWESG AQGVAGIRAF WPDEIV // ID F3EHS1_PSESL Unreviewed; 205 AA. AC F3EHS1; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PLA107_21553; OS Pseudomonas syringae pv. lachrymans str. M301315. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629260; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M301315; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAF01000271; EGH85727.1; -; Genomic_DNA. DR EnsemblBacteria; EGH85727; EGH85727; PLA107_21553. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21938 MW; 8D6F125A1D709D2F CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKT SDESRRLREA TELLKLCERY KARLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGSL ELAEQAKADG ATYVAFGRFF NSLTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN AQEVTRRAKA FMALL // ID F3ERK3_9PSED Unreviewed; 205 AA. AC F3ERK3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSYMO_03423; OS Pseudomonas syringae pv. mori str. 301020. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629261; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=301020; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAG01000137; EGH20585.1; -; Genomic_DNA. DR EnsemblBacteria; EGH20585; EGH20585; PSYMO_03423. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21996 MW; 8D8210EA1E689C94 CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKT SDESRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGSL ELAEQAKADG ATYVAFGRFF NSLTKPGAPA VPLDLIARVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN AQEVTRRAKA FMALL // ID F3FBG5_PSESX Unreviewed; 316 AA. AC F3FBG5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 13-NOV-2013, entry version 18. DE SubName: Full=Uncharacterized protein; GN ORFNames=PSYJA_00315; OS Pseudomonas syringae pv. japonica str. M301072. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629262; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M301072; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAH01000016; EGH27551.1; -; Genomic_DNA. DR ProteinModelPortal; F3FBG5; -. DR EnsemblBacteria; EGH27551; EGH27551; PSYJA_00315. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34221 MW; 5E1B13D52266C8AF CRC64; MKRVHVAAAV IRGADGSVLI ARRADTQHQG GLWEFPGGKV EEGETVQAAL ARELQEELGI LVTAARPLIK VCHDYPDKQV LLDVWEVSAF TGQAHGAEGQ PLVWASPREL ANYDFPAANQ PIVAAARLPG EYLITPEGLD NIELLRGMQK AIADGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPENRWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWPQ ATQLIADFNR PVFLLGGVGP AERQQAWKSG AQGVAGIRAF WPDEIV // ID F3FCD4_PSESX Unreviewed; 205 AA. AC F3FCD4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSYJA_02104; OS Pseudomonas syringae pv. japonica str. M301072. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629262; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M301072; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAH01000089; EGH27870.1; -; Genomic_DNA. DR ProteinModelPortal; F3FCD4; -. DR EnsemblBacteria; EGH27870; EGH27870; PSYJA_02104. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22037 MW; BC6FE11ACCA29092 CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKN SDESRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQSDGSLP DARALLGHKA IVGATCHGRV ELAEQAKADG ATYVAFGRFF NSQTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN TQEVTRRAKA FTALL // ID F3G427_PSESJ Unreviewed; 184 AA. AC F3G427; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 17. DE SubName: Full=Uncharacterized protein; DE Flags: Fragment; GN ORFNames=PSYPI_05103; OS Pseudomonas syringae pv. pisi str. 1704B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629263; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1704B; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAI01000241; EGH41827.1; -; Genomic_DNA. DR EnsemblBacteria; EGH41827; EGH41827; PSYPI_05103. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. FT NON_TER 184 184 SQ SEQUENCE 184 AA; 19778 MW; B239CB3C64ACE3D6 CRC64; MKRVHVAAAV IRGADGSVLI ARRADTQHQG GLWEFPGGKV EEGETVQAAL ARELQEELGI LVTAARPLIK VCHDYPDKQV LLDVWEVSAF TGQAHGAEGQ PLVWASPREL ANYDFPAANQ PIVAAARLPG EYLITPEGLD NIELLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG HCAR // ID F3GJ31_PSESJ Unreviewed; 205 AA. AC F3GJ31; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSYPI_34385; OS Pseudomonas syringae pv. pisi str. 1704B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629263; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1704B; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAI01001974; EGH47084.1; -; Genomic_DNA. DR EnsemblBacteria; EGH47084; EGH47084; PSYPI_34385. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22079 MW; 7F7D711ACCB017AF CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKN SDESRRLREA TELLKLCERY KTRLIINDDA ELAARLGIGV HLGQSDGSLP DARALLGHKA IVGATCHGRV ELAEQAKADG ATYVAFGRFF NSQTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN TQEVTRRARA FTALL // ID F3GLM7_PSESJ Unreviewed; 123 AA. AC F3GLM7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 15. DE SubName: Full=Uncharacterized protein; GN ORFNames=PSYPI_39159; OS Pseudomonas syringae pv. pisi str. 1704B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629263; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1704B; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAI01002688; EGH47980.1; -; Genomic_DNA. DR EnsemblBacteria; EGH47980; EGH47980; PSYPI_39159. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 123 AA; 13548 MW; D682B6E8FEE95F4C CRC64; MERLGDFPSA GWHLTAEQLR KYASRGRPFP ENRWLAASCH NAEELALAEQ MGVDFVTLSP VQPTLTHPDA QPLGWPQATQ LIADFNRPVF LLGGVGPAER QQAWESGAQG VAGIRAFWPD EIV // ID F3GTR8_PSESX Unreviewed; 316 AA. AC F3GTR8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE SubName: Full=Uncharacterized protein; GN ORFNames=PSYCIT7_02147; OS Pseudomonas syringae Cit 7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629264; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cit 7; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAJ01000072; EGH50471.1; -; Genomic_DNA. DR ProteinModelPortal; F3GTR8; -. DR EnsemblBacteria; EGH50471; EGH50471; PSYCIT7_02147. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34155 MW; 6AD683F0F92836CF CRC64; MKRVHVAAAV IRDADGSVLI ARRADTQHQG GLWEFPGGKV EEGETVQDAL ARELQEELGI LVTAARPLIK VCHDYPDKQV LLDVWEVSAF TGLAHGAEGQ PLVWASPREL ANYDFPAANQ PIVAAARLPG EYLITPEGLD NIELLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPENRWLAA SCHNAEELAL AEQMGVDFVT LSPVQSTLTH PDAQPLGWPQ ATQLIAGFNK PVFLLGGVGP AERQQAWESG AQGVAGIRAF WPDEIV // ID F3H1P8_PSESX Unreviewed; 205 AA. AC F3H1P8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSYCIT7_16824; OS Pseudomonas syringae Cit 7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629264; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cit 7; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAJ01000584; EGH53261.1; -; Genomic_DNA. DR ProteinModelPortal; F3H1P8; -. DR EnsemblBacteria; EGH53261; EGH53261; PSYCIT7_16824. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22022 MW; A65CC800FF8B9092 CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKN SDESRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQSDGSLP DARALLGHKA IVGATCHGRV ELAEQAKADG ATYVAFGRFF NSLTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN TQEVTRRAKA FTALL // ID F3HFV3_PSEYM Unreviewed; 316 AA. AC F3HFV3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE SubName: Full=Uncharacterized protein; GN ORFNames=PMA4326_05191; OS Pseudomonas syringae pv. maculicola str. ES4326. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=629265; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ES4326; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAK01000088; EGH58216.1; -; Genomic_DNA. DR ProteinModelPortal; F3HFV3; -. DR EnsemblBacteria; EGH58216; EGH58216; PMA4326_05191. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34060 MW; C61A1F25D6FCE5B8 CRC64; MKRVHVAAAV IRGADDKVLI ARRADSQHQG GLWEFPGGKV EAGETVEAAL ARELQEELGI VVAAARPLIK VCHDYPDKQV LLDVWEVSAF TGEPHGAEGQ PLAWVTPREL AGYEFPAANQ PIVAAARLSA EYLITPDGLD SIELLRGVQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPEHRWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWEQ ATQLIAGFNK PVFLLGGVGP AERQKAWESG AQGVAGIRAF WPDEII // ID F3HM33_PSEYM Unreviewed; 205 AA. AC F3HM33; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PMA4326_16426; OS Pseudomonas syringae pv. maculicola str. ES4326. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=629265; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ES4326; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAK01000283; EGH60403.1; -; Genomic_DNA. DR EnsemblBacteria; EGH60403; EGH60403; PMA4326_16426. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22012 MW; 45A6C024754D2E44 CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKT GDDSRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLA DARALLGHKA IVGATCHGQL ELAERAKADG ATYVAFGRFF NSRTKPGAPA VPLDLIAQVR AKVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN TQEVTRRAKA FMALL // ID F3HWM8_PSESF Unreviewed; 205 AA. AC F3HWM8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSYAC_02332; OS Pseudomonas syringae pv. actinidiae str. M302091. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629266; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302091; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAL01000049; EGH63748.1; -; Genomic_DNA. DR EnsemblBacteria; EGH63748; EGH63748; PSYAC_02332. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21996 MW; 8472C3080867D129 CRC64; MKLRGLYAIT DSQLLTGKFL SYVEAALDGG VTLLQYRDKT GDDSRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGQL ELAEQAKADG ATYVAFGRFF NSQTKPGAPA VPLDLIAQVR AKVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN TQEVTRRAKA FMALL // ID F3HY78_PSESF Unreviewed; 316 AA. AC F3HY78; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 13-NOV-2013, entry version 17. DE SubName: Full=Uncharacterized protein; GN ORFNames=PSYAC_05370; OS Pseudomonas syringae pv. actinidiae str. M302091. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629266; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302091; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAL01000094; EGH64328.1; -; Genomic_DNA. DR ProteinModelPortal; F3HY78; -. DR EnsemblBacteria; EGH64328; EGH64328; PSYAC_05370. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34071 MW; 24198DCB4DA2880C CRC64; MKRVHVAAAV IRGTDGRVLI ARRADSQHQG GLWEFPGGKV EAGETVEMAL ARELQEELGI VVTAARPLIK VCHDYPDKQV LLDVWEVSAF TGEPHGAEGQ PLVWASPREL ANYDFPAANQ PIVAAARLPG EYLITPEGLD NIELLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAQ QLRKYASNGR PFPENRWLAA SCHSAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWEQ AAQLIAGFNK PVFLLGGVGP AQCQQAWESG AQGVAGIRAF WPDEII // ID F3ICV6_PSESL Unreviewed; 205 AA. AC F3ICV6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PLA106_02605; OS Pseudomonas syringae pv. lachrymans str. M302278. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629267; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302278; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAM01000052; EGH94820.1; -; Genomic_DNA. DR ProteinModelPortal; F3ICV6; -. DR EnsemblBacteria; EGH94820; EGH94820; PLA106_02605. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22007 MW; A70BC30808744997 CRC64; MKLRGLYAIT DSQLLTGKFL SYVEAALDGG VTLLQYRDKT GDDSRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGQL ELAEQAKADG ATYVAFGRFF NSQTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAET PQEVTRRAKA FMALL // ID F3II39_PSESL Unreviewed; 316 AA. AC F3II39; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Uncharacterized protein; GN ORFNames=PLA106_11945; OS Pseudomonas syringae pv. lachrymans str. M302278. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629267; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302278; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAM01000217; EGH96801.1; -; Genomic_DNA. DR ProteinModelPortal; F3II39; -. DR EnsemblBacteria; EGH96801; EGH96801; PLA106_11945. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34190 MW; CB509F95F7ED2E29 CRC64; MKRVHVAAAV IRGTDGRVLI ARRAESQHQG GLWEFPGGKV EAGETVEIAL ARELQEELGI VVTATRPLIK VCHDYPDKQV LLDVWEVSAF TGEPHGAEGQ PLVWASPREL ANYDFPAANQ PIVAAARLPG EYLITPEGLD NIELLRGLQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAQ QLRKYASNGR PFPENRWLAA SCHSAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWEQ ATRLIAGFNK PVFLLGGVGP AQRQQAWESG AQGVAGIRAF WPDEII // ID F3IXL6_PSEAP Unreviewed; 173 AA. AC F3IXL6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSYAP_09395; OS Pseudomonas syringae pv. aptata str. DSM 50252. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629268; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 50252; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAN01000370; EGH76888.1; -; Genomic_DNA. DR EnsemblBacteria; EGH76888; EGH76888; PSYAP_09395. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 173 AA; 18655 MW; 84D504E7A7B670F2 CRC64; MLQYRDKNSD ESRRLREATE LLKLCERYKT RLIINDDAEL AARLGVGVHL GQSDGSLPDA RALLGHKAIV GATCHGRVEL AEQAKADGAT YVAFGRFFNS QTKPGAPAVP LDLIAQVRAR VHLPIAVIGG ITLENAPQLV EHGADLLAVV HGLFGAENTQ EVTRRAKAFT ALL // ID F3J8A6_PSEAP Unreviewed; 316 AA. AC F3J8A6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE SubName: Full=Uncharacterized protein; GN ORFNames=PSYAP_28908; OS Pseudomonas syringae pv. aptata str. DSM 50252. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629268; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 50252; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAN01001280; EGH80632.1; -; Genomic_DNA. DR ProteinModelPortal; F3J8A6; -. DR EnsemblBacteria; EGH80632; EGH80632; PSYAP_28908. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34109 MW; 068D12BC64743C4C CRC64; MKRVHVAAAV IRGADGSVLI ARRADTLHQG GLWEFPGGKV EEGETVQAAL ARELQEELGI LVTAARPLIK VCHDYPDKQV LLDVWEVSAF TGQAHGAEGQ PLVWASPREL ANYDFPAANQ PIVAAARLPG EYLITPDGLD NIELLRGMQK AIAGGSKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPENRWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWPQ ATQLIADFNR PVFLLGGVGP AERQQAWESG AQGVAGIRAF WPDEIV // ID F3JCF3_PSESX Unreviewed; 205 AA. AC F3JCF3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSYAR_03074; OS Pseudomonas syringae pv. aceris str. M302273. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629270; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302273; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAO01000063; EGH69526.1; -; Genomic_DNA. DR ProteinModelPortal; F3JCF3; -. DR EnsemblBacteria; EGH69526; EGH69526; PSYAR_03074. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22022 MW; A65CC800FF8B9092 CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKN SDESRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQSDGSLP DARALLGHKA IVGATCHGRV ELAEQAKADG ATYVAFGRFF NSLTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN TQEVTRRAKA FTALL // ID F3JNL8_PSESX Unreviewed; 316 AA. AC F3JNL8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Uncharacterized protein; GN ORFNames=PSYAR_23084; OS Pseudomonas syringae pv. aceris str. M302273. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629270; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302273; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAO01000552; EGH73441.1; -; Genomic_DNA. DR ProteinModelPortal; F3JNL8; -. DR EnsemblBacteria; EGH73441; EGH73441; PSYAR_23084. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34054 MW; ED2EB464B3540105 CRC64; MKRVHVAAAV IRGADGSVLI ARRADTQHQG GLWEFPGGKV EEGETVQAAL ARELQEELGI LVTAARPLIK VCHDYPDKQV LLDVWEVSAF TGQAHGAEGQ PLAWATPREL ANYDFPAANQ PIVAAARLPG EYLITPDGLD TIELLRGMQK AIAGGVKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPENRWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWQQ ATQLIAGFNK PVFLLGGVGP AERQQAWESG AQGVAGIRAF WPDEIV // ID F3K2J9_PSESZ Unreviewed; 205 AA. AC F3K2J9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSYTB_17000; OS Pseudomonas syringae pv. tabaci str. ATCC 11528. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=573066; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11528; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAP01000312; EGH91390.1; -; Genomic_DNA. DR ProteinModelPortal; F3K2J9; -. DR EnsemblBacteria; EGH91390; EGH91390; PSYTB_17000. DR PATRIC; 25610019; VBIPseSyr56650_0473. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22006 MW; 1E4C21080C474C96 CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKT SDEPRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGSL ELAEQAKADG ATYVAFGRFF NSLTKPGAPA VPLDLIARVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN AQEVTRRAKA FMALL // ID F3K3A3_PSESZ Unreviewed; 316 AA. AC F3K3A3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE SubName: Full=Uncharacterized protein; GN ORFNames=PSYTB_18304; OS Pseudomonas syringae pv. tabaci str. ATCC 11528. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=573066; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11528; RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132; RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S., RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.; RT "Dynamic evolution of pathogenicity revealed by sequencing and RT comparative genomics of 19 Pseudomonas syringae isolates."; RL PLoS Pathog. 7:E1002132-E1002132(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEAP01000337; EGH91644.1; -; Genomic_DNA. DR ProteinModelPortal; F3K3A3; -. DR EnsemblBacteria; EGH91644; EGH91644; PSYTB_18304. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 316 AA; 34047 MW; 86C092002609A949 CRC64; MKRVHVAAAV IRGADGSVLI ARRADTQHQG GLWEFPGGKV EEGETVQAAL ARELQEELGI QVTAARPLIK VGHDYADKQV LLDVWEVSAF TGEPHGAEGQ PLVWAAPREL PDYDFPAANQ PIVAAARLPG EYLITPDGLD NIELLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPENRWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDALPLGWQQ AAQLIAGFNK PVFLLGGVGP SERQQAWESG AQGVAGIRAF WPDEIV // ID F3KR68_9BURK Unreviewed; 317 AA. AC F3KR68; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HGR_04718; OS Hylemonella gracilis ATCC 19624. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Hylemonella. OX NCBI_TaxID=887062; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19624; RX PubMed=21673657; DOI=10.1038/emboj.2011.186; RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R., RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J., RA Jensen G.J.; RT "Structural diversity of bacterial flagellar motors."; RL EMBO J. 30:2972-2981(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEGR01000042; EGI77769.1; -; Genomic_DNA. DR EnsemblBacteria; EGI77769; EGI77769; HGR_04718. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 317 AA; 33744 MW; 14302B8E503414E8 CRC64; MTTLTTNARA IVAAHPDKAI PVVGQPQPRY SLDDPIYRAA VQAALALGFI EIDAECLALA WLAQSRRTGR FDPDIWPVEA VDFGLRPRGD GAGAFAACPS RLGVYAVLPD ARWVGRMAHA GVPTLQLRFK SHDPQAVRRE VRAAIETVSA AHRQRGARSL LFINDHWRET LEVLASDASH LEFLGVHLGQ EDMDAAAMVE GFEAIRAAGL RLGLSTHGYA EMRRAAALQP SYIAMGAVYP TTLKQMATAP QGPGRLAAYA RLLHHAGYPG VAIGGISAAE LPVIKATGVG SLAVVRAITA EANPEAAAAR LMAAWDL // ID F3LIC8_9GAMM Unreviewed; 497 AA. AC F3LIC8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 19. DE SubName: Full=Phosphomethylpyrimidine kinase; GN ORFNames=IMCC1989_1308; OS gamma proteobacterium IMCC1989. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales. OX NCBI_TaxID=937772; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IMCC1989; RX PubMed=21602334; DOI=10.1128/JB.05202-11; RA Jang Y., Oh H.M., Kim H., Kang I., Cho J.C.; RT "Genome sequence of strain IMCC1989, a novel member of the marine RT gammaproteobacteria."; RL J. Bacteriol. 193:3672-3673(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVK01000219; EGG93355.1; -; Genomic_DNA. DR EnsemblBacteria; EGG93355; EGG93355; IMCC1989_1308. DR PATRIC; 54960092; VBIGamPro175983_2271. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 497 AA; 53200 MW; 189C13BE363B831D CRC64; MKNVSNNTPP PIVWAIAASD SGGGAGVQAD IKTIFDLGAH ACTAITGITA QNSQGVHHID ICNDDIFEKQ LLALAQDLPP VAIKIGVLLS VSQVHIVTNI IRSLKNVCVI FDPVLAPTAG LNFVTEETRD AFNQLLPLVD LLTPNIPEAE MLSGLSINDT HSQHLAAQYF IGKGVTAVLI KGGHGALNGN ASYCQDVFVS ATQQFWLTQK KQNTPHSHGT GCTLSSAATA FVAEGKALCD AVVLANTYIS KGLRLAITFD EAGYKRGAVA QTGWPQSLSD FPQVSLQPEA IEQTAFPSCD TQRLGLYPVV DSLDWLSKLC ATGVKTLQLR VKDKSAAELD ELVKAAVAIG KHYQARLFIN DYWQLAIKHQ AYGVHLGQED MVDADVDAMR AAGLHLGIST HSEYEFAYAA TFKPSYLAIG AIFPTDTKEV VEVGLDNLYR WADTLNGHYP LVAIGGINLH NIQSVLQSGV GSIAVVSAIT KADDYISATK QLTKIIQ // ID F3LK18_9BURK Unreviewed; 221 AA. AC F3LK18; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RBXJA2T_00065; OS Rubrivivax benzoatilyticus JA2 = ATCC BAA-35. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Rubrivivax. OX NCBI_TaxID=987059; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JA2; RX PubMed=21478355; DOI=10.1128/JB.00379-11; RA Mohammed M., Isukapatla A., Mekala L.P., Eedara Veera Venkata R.P., RA Chintalapati S., Chintalapati V.R.; RT "Genome sequence of the phototrophic betaproteobacterium Rubrivivax RT benzoatilyticus strain JA2T."; RL J. Bacteriol. 193:2898-2899(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEWG01000002; EGJ08686.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ08686; EGJ08686; RBXJA2T_00065. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23054 MW; 41EF36C110D36403 CRC64; MTERRTPMQG WGVEALRLML VTDEALCAGR PLEQVVAAAV RGGVRCVQLR EKQLGTRAFV ERARALKSLL APLRVPLVVN DRVDVALACG ADGVHLGQSD MPVEDARRLL PPEVFIGWSV ESFDDLRRAA SLPLDYLGTS PVFATATKTD AAPPWGLAGL RAARDATALP LVAIGGLHAG NAALAIAHGA DSVAVVSAIC AAADPEAAAR ELARAVGEGA R // ID F3M8N7_9BACL Unreviewed; 224 AA. AC F3M8N7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9412_3788; OS Paenibacillus sp. HGF5. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=908341; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGF5; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXS01000068; EGG36284.1; -; Genomic_DNA. DR ProteinModelPortal; F3M8N7; -. DR EnsemblBacteria; EGG36284; EGG36284; HMPREF9412_3788. DR PATRIC; 54969097; VBIPaeSp172377_2417. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23825 MW; 5A21C26D8D07A926 CRC64; MTGRVAPKIM RRHLRMYLVL GSVNCSVEPS LVVQEALAGG ATMVQFREKG QAALAGEPMI RLARRIQAEC RLAGVPFIVN DDVELALKLD ADGVHVGQDD ESAASVRERI GNRILGVSAH TVEEARRAIL HGADYLGIGP IYPTRSKDDA KTAKGPAILR ELREAGIHLP IVGIGGITVE RVEEVIGAGA DGLAVISAVT GAESAREVVE AIVDKIRRAT EEIS // ID F3MU72_LACRH Unreviewed; 209 AA. AC F3MU72; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AAULR_02804; OS Lactobacillus rhamnosus MTCC 5462. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=947828; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MTCC 5462; RX PubMed=22328760; DOI=10.1128/JB.06644-11; RA Prajapati J.B., Khedkar C.D., Chitra J., Suja S., Mishra V., RA Sreeja V., Patel R.K., Ahir V.B., Bhatt V.D., Sajnani M.R., RA Jakhesara S.J., Koringa P.G., Joshi C.G.; RT "Whole-Genome Shotgun Sequencing of Lactobacillus rhamnosus MTCC 5462, RT a Strain with Probiotic Potential."; RL J. Bacteriol. 194:1264-1265(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYM01000757; EGF48249.1; -; Genomic_DNA. DR ProteinModelPortal; F3MU72; -. DR EnsemblBacteria; EGF48249; EGF48249; AAULR_02804. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21836 MW; FDF458E872FD9638 CRC64; MNAEALQLYL VTNRYADSPE VFLAKIAAAC ENGVTMVQLR EKSLTTRDYY ALAKQVKLIT DRYRIPLIID DRVDVCLAVD AAGVHIGDDE LPVAVTRQLL GPDKILGVST KTVATATAAV AAGADYLGVG AIFPTQTKAA APLTSLATLK AITAAVSVPV VAIGGIKADN LDTFKATGIA GVAIVSEIMQ APDTAQKVQT LSAKLKEVL // ID F3NRH1_9ACTO Unreviewed; 216 AA. AC F3NRH1; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SGM_5735; OS Streptomyces griseoaurantiacus M045. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=996637; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M045; RX PubMed=21551298; DOI=10.1128/JB.05053-11; RA Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.; RT "Draft genome sequence of the marine bacterium Streptomyces RT griseoaurantiacus M045, which produces novel manumycin-type RT antibiotics with a pABA core component."; RL J. Bacteriol. 193:3417-3418(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYX01000044; EGG44155.1; -; Genomic_DNA. DR ProteinModelPortal; F3NRH1; -. DR EnsemblBacteria; EGG44155; EGG44155; SGM_5735. DR PATRIC; 54989476; VBIStrGri184913_5959. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22644 MW; F76A4DE1503CA116 CRC64; MPDTARARLD EALLYLCTDA RTRQGDLPEF LDAVLAAGVD IVQLRDKGIE AAEELAHLEV FAEACARHGR LLAVNDRADV AHAAGADVLH LGQGDLPVPA ARAILGEGVL VGRSTHSPAE AGAAAVQDGV DYFCTGPCWP TPTKPGRPAP GLDLVRHTAA LGTERPWFAI GGIDLGNLDE VIEAGARRVV VVRALTEAED PGAAAAEFAR RLRAAR // ID F3NUP5_CHLPS Unreviewed; 212 AA. AC F3NUP5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=G5Q_0221; OS Chlamydia psittaci Cal10. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=984894; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cal10; RX PubMed=21622741; DOI=10.1128/JB.05277-11; RA Grinblat-Huse V., Drabek E.F., Creasy H.H., Daugherty S.C., RA Jones K.M., Santana-Cruz I., Tallon L.J., Read T.D., Hatch T.P., RA Bavoil P., Myers G.S.; RT "Genome sequences of the zoonotic pathogens Chlamydia psittaci 6BC and RT Cal10."; RL J. Bacteriol. 193:4039-4040(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cal10; RA Huse V., Drabek E.F., Huot Creasy H., Daugherty S., Jones K.M., RA Santana-Cruz I., Tallon L.J., Read T.D., Hatch T.P., Bavoil P., RA Myers G.S.A.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEZD01000001; EGF85422.1; -; Genomic_DNA. DR EnsemblBacteria; EGF85422; EGF85422; G5Q_0221. DR PATRIC; 54991746; VBIChlPsi186351_0219. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22829 MW; 3D460DE4B76332CC CRC64; MEENFFKLIL ITNKQNISVE EYLDFVCACV HSGVTSVQLR EKELSYRELL GFGEALKSML DPLEIPLIVS DSVSVCLDLD ATGVHLGQTD GDVIEARELL GSDKIIGWNV NTLDQLLNAN TLPIDYLGLS AMFATQNKPD ATNLWGFSGL EQAVSLCEHP IVAIGGIDES NAAEVIEAGA AGIAAIGVFH SAQNPGLVTK TLREIVDRGL RC // ID F3NZZ5_9ACTO Unreviewed; 226 AA. AC F3NZZ5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PA08_1118; OS Propionibacterium humerusii P08. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=999892; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P08; RX PubMed=21571999; DOI=10.1128/JB.05036-11; RA Butler-Wu S.M., Sengupta D.J., Kittichotirat W., Matsen F.A.III., RA Bumgarner R.E.; RT "Genome sequence of a novel species, Propionibacterium humerusii."; RL J. Bacteriol. 193:3678-3678(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P08; RA Matsen F., Hoffman N., Butler-Wu S., Kittichotirat W., Bumgarner R.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFAM01000008; EGG26881.1; -; Genomic_DNA. DR EnsemblBacteria; EGG26881; EGG26881; PA08_1118. DR PATRIC; 53596992; VBIProSp187533_1078. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 151 153 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23534 MW; D9305CDB7DA17FDE CRC64; MKSARGEGFA MSRPEFDLSV YLVTDTAQCG GPDGVVETVR RAIVGGVTLV QFRDHDLSDD EFVTLGRRVR DACISGGVPL IIDDRVHLVA EIGADGAHVG QSDMPVDQAR AVLGDDLLIG LSAQAPVHVK AALSHGRDVI DYLGVGALHG TGTKPEAEEL GLAGICDVVN ASPWPVCVIG GVSASDAPYV SRMGCDGLSV VSAICGSTDP ESSARELAEA WRRAKE // ID F3P4B4_9ACTO Unreviewed; 214 AA. AC F3P4B4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PA08_2630; OS Propionibacterium humerusii P08. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=999892; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P08; RX PubMed=21571999; DOI=10.1128/JB.05036-11; RA Butler-Wu S.M., Sengupta D.J., Kittichotirat W., Matsen F.A.III., RA Bumgarner R.E.; RT "Genome sequence of a novel species, Propionibacterium humerusii."; RL J. Bacteriol. 193:3678-3678(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P08; RA Matsen F., Hoffman N., Butler-Wu S., Kittichotirat W., Bumgarner R.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFAM01000018; EGG25679.1; -; Genomic_DNA. DR EnsemblBacteria; EGG25679; EGG25679; PA08_2630. DR PATRIC; 53600138; VBIProSp187533_2573. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 214 AA; 22005 MW; B66EC551F31299E4 CRC64; MTLDLRCYLV TSGTDHRTVE TAASAAAAGA GMVQVRAKDV STRDSLGLVL QVGEAVRRAN SATRVVVDDR ADVAWAAMRA HGNVHGVHVG SADLPVRDAR AILGPDAIVG YTTGTLDLVR SVEPFADALD YVGAGPFRPT PTKDSGRVPL GVQGYPELVA ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVIQA FDRV // ID F3PB63_9ACTO Unreviewed; 220 AA. AC F3PB63; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9056_02197; OS Actinomyces sp. oral taxon 170 str. F0386. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Actinomycineae; Actinomycetaceae; Actinomyces. OX NCBI_TaxID=762963; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0386; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBL01000053; EGF53705.1; -; Genomic_DNA. DR EnsemblBacteria; EGF53705; EGF53705; HMPREF9056_02197. DR PATRIC; 55010129; VBIActSp161325_1825. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22465 MW; 8B8DC19F9FBBE645 CRC64; MRAVPDLSVY LITDEGQCRS RGRDVLATVE AAVDGGVTCV QLRAKGADGG LFLTQVLEVA EVVGDQVPVI VNDRVDIFLA ARDQGASVAG VHLGQSDLPA RIARRLVGED AYLGLSAATP DELCTAQEQG ACDHVGIGVV HLTATKADAP KSLGVNGVAR MAALTDLPAV AIGGITVSDL PALRAGGLAG AAVVSAICTA EDPRSVAADL HRAWDEGGRR // ID F3PFL9_9BACE Unreviewed; 215 AA. AC F3PFL9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9445_00789; OS Bacteroides clarus YIT 12056. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=762984; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12056; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBM01000007; EGF54048.1; -; Genomic_DNA. DR EnsemblBacteria; EGF54048; EGF54048; HMPREF9445_00789. DR PATRIC; 55013236; VBIBacCla162388_0742. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 24152 MW; 91C9C66088BA6EAD CRC64; MKSLQFITHY TERYSYLDSA RMALEGGCRW IQLRMKDAGK EEILPIATEI RKLCNDCGAI FIIDDHVELV REIRADGVHL GKNDMPVAEA RRILGDEYII GGTANTYEDI KKHWLDGVNY IGCGPFRYTT TKQKLSPILG LEGYKEIIRQ MRAENINLPI VAIGGITFAD IPSVMQTGIT GIALSGTVLR ADNPAEEMWR ILAAINQTDN HRTNK // ID F3PFM4_9BACE Unreviewed; 197 AA. AC F3PFM4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF9445_00794; OS Bacteroides clarus YIT 12056. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=762984; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12056; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBM01000007; EGF54053.1; -; Genomic_DNA. DR EnsemblBacteria; EGF54053; EGF54053; HMPREF9445_00794. DR PATRIC; 55013246; VBIBacCla162388_0747. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 197 AA; 21752 MW; 2FB59EC38E6C3977 CRC64; MKLITITLPV FFEEEAEAIT SLFDAGLEIL HLRKPGASYE DMEKLLNKLP SEYLERIVTH EHFQLASFLN LKGIHLNGRN PVAPAGFTGH ISRSCHSLEE VSKYKTTCDY VFLSPIYDSI SKKGYSSAYT PDTLQKARQA GIIDAKVMAL GGVTAAHFPE ISSSGFGGAV LLGDIWKRTG TDFIGHFKEL LRLASLF // ID F3PTQ4_9BACE Unreviewed; 206 AA. AC F3PTQ4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF9446_02122; OS Bacteroides fluxus YIT 12057. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=763034; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12057; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBN01000037; EGF56702.1; -; Genomic_DNA. DR EnsemblBacteria; EGF56702; EGF56702; HMPREF9446_02122. DR PATRIC; 55022162; VBIBacFlu160465_1966. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22595 MW; BA3EEE36CB1A1832 CRC64; MKLIVITAPQ FFEGEVAAIV SLFRAGLETM HLRKPKASIE ETENLLRQLP AEYMQRIVTH DHFQLASAFG LKGIHLNGRN PHVPAGYTGH ISCSCHSLHE VVKRKSACDY VFLSPIYDSI SKEGYSPVYS CKELQEACRA GIIDSKVMAL GGISREHLPE IAALGFGGAA LLGDIWNRAA SSIPFHFREL LSHTCNACPP PLIINS // ID F3PTQ9_9BACE Unreviewed; 217 AA. AC F3PTQ9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9446_02127; OS Bacteroides fluxus YIT 12057. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=763034; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12057; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBN01000037; EGF56707.1; -; Genomic_DNA. DR EnsemblBacteria; EGF56707; EGF56707; HMPREF9446_02127. DR PATRIC; 55022172; VBIBacFlu160465_1971. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23977 MW; 75F6D79649A88698 CRC64; MMKDEKLKNG KLQFITHYTE RYSYLDAAHM ALEGGCRWVQ LRMKDTSMED IEPVALEMQS LCRQYGATFI IDDHVELAGK LHADGVHLGK KDMPIADARR ILGKEYIIGG TANTLEDVLQ HYEAGADYIG CGPFRYTTTK KNLSPILGLE GYTAIIRRMQ EADIHLPVVA IGGITIADIP AVMQAGVSGI ALSGTVLHAD NPTKEMRRII SLMENGE // ID F3PXE7_9BACE Unreviewed; 202 AA. AC F3PXE7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF9446_03439; OS Bacteroides fluxus YIT 12057. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=763034; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12057; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBN01000098; EGF51719.1; -; Genomic_DNA. DR EnsemblBacteria; EGF51719; EGF51719; HMPREF9446_03439. DR PATRIC; 55024649; VBIBacFlu160465_3150. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23175 MW; BD18BF6250B4B6B8 CRC64; MKLIVVTAPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHKRIVTH EHFYLQEEFS LMGIHLNARN PKEPHDYSGH VSCTCHSMEE VQNKKHFYDY LFLSPVYDCI TKSGVASGFT AEELRQAGKS KIVDGRVMAL GGITPDNILE IKDYGFGGAV VMGDLWNKFN ACTDRDYLEI IRHFKKLKDM AD // ID F3Q6R6_9ENTR Unreviewed; 211 AA. AC F3Q6R6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9538_02780; OS Klebsiella sp. MS 92-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=749535; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 92-3; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBO01000355; EGF62773.1; -; Genomic_DNA. DR ProteinModelPortal; F3Q6R6; -. DR EnsemblBacteria; EGF62773; EGF62773; HMPREF9538_02780. DR PATRIC; 55030941; VBIKleSp165603_2375. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 21B54D01518D3CB0 CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIERLLE AGVRTLQLRI KDRRDSEVED DVIAAIALGR RYHARLFIND YWQLAIKHQA YGVHLGQEDL ETTDLSAIRQ AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIQRLADYP TVAIGGISLE KAPGVLATGV GSIAVVSAIT QAADWRAATD QLLALAGAGD E // ID F3QHQ8_9BURK Unreviewed; 215 AA. AC F3QHQ8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9439_00455; OS Parasutterella excrementihominis YIT 11859. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Sutterellaceae; Parasutterella. OX NCBI_TaxID=762966; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11859; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBP01000010; EGG57040.1; -; Genomic_DNA. DR EnsemblBacteria; EGG57040; EGG57040; HMPREF9439_00455. DR PATRIC; 55038281; VBIParExc164098_0421. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22433 MW; 9DD9DE1380E81E8C CRC64; MKSGKKLDLS LYLVLDANLC KTPEGMAETA RKAVEGGCTV VQLRAPEWKK KKQLRAAFLL KELLKDTDVL FIVDDHIDIA LLSGADGVHV GQEDIDPKYV RQFLGPDAVI GLSVGSIKEL NTIGPDVDYI GIGPVFSTKT KVDAGAAVGL GLLEYISKEA GLPNVAIGGI NQSNAADCIR HGADGVAVVS AICGAEDPKA AAAAIKKAVN DALSI // ID F3QPB6_9BACT Unreviewed; 210 AA. AC F3QPB6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9442_00003; OS Paraprevotella xylaniphila YIT 11841. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Paraprevotella. OX NCBI_TaxID=762982; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11841; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBR01000001; EGG58110.1; -; Genomic_DNA. DR EnsemblBacteria; EGG58110; EGG58110; HMPREF9442_00003. DR PATRIC; 55042720; VBIParXyl161988_0002. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23242 MW; 80C0CCAEA5ACDF5E CRC64; MQNLQFITHY TEQYGYADAA RLALEGGCRW IQLRMKDASP EEWMRTGAEV EALCRRYGAT FILDDHVEWV DVLHADGIHL GKSDMPIDEA RRLLGQDRII GGTANTLEDV MLHAARGADY IGCGPFRFTT TKEKLAPTLG LEGYRRILDG MKKKSISLPL IAIGGITKED IPALMETGVD GIALSGTILR AGNPTEETQN ILRILNIQQS // ID F3QPB8_9BACT Unreviewed; 202 AA. AC F3QPB8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF9442_00005; OS Paraprevotella xylaniphila YIT 11841. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Paraprevotella. OX NCBI_TaxID=762982; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11841; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBR01000001; EGG58112.1; -; Genomic_DNA. DR EnsemblBacteria; EGG58112; EGG58112; HMPREF9442_00005. DR PATRIC; 55042724; VBIParXyl161988_0004. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23185 MW; FFC3E7F86DD51221 CRC64; MKLILLTPPD FFVEEDKILT ALFEEGLDLL HLRKPDTEPV YSERLLTLLP ESHHNQIVVH DHFYLKEEFN LRGIHLNGRN PEPPVGYKGH ISKSFHHIDE LKAEKKNFNY VFLSPIFDSI SKSNYTSAFD MEVLKQASAH GIIDKRVMAL GGITTENMAV AKDFGFGGVV VLGDLWNRFN IHSTLDYKEL INHFRKLRKA AD // ID F3R5C3_ENTFL Unreviewed; 211 AA. AC F3R5C3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9520_02213; OS Enterococcus faecalis TX1467. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=749517; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX1467; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBS01000146; EGG54533.1; -; Genomic_DNA. DR ProteinModelPortal; F3R5C3; -. DR EnsemblBacteria; EGG54533; EGG54533; HMPREF9520_02213. DR PATRIC; 53667681; VBIEntFae154052_2024. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22936 MW; A6E424940A930223 CRC64; MREQLKVYLV TGRYDFSDTE FLNRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKAVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTRVAGV SLVSEIMLAE QIAEKVQGLM RVTERMLEAR K // ID F3RB01_LISMN Unreviewed; 214 AA. AC F3RB01; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LM1816_05398; OS Listeria monocytogenes J1816. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=930781; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J1816; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006046; EGF38820.1; -; Genomic_DNA. DR RefSeq; YP_008286385.1; NC_021829.1. DR ProteinModelPortal; F3RB01; -. DR GeneID; 16801905; -. DR KEGG; lmoz:LM1816_05398; -. DR PATRIC; 53672049; VBILisMon188815_0763. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22624 MW; 10F8C1830CF46A06 CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAE EAERLGAVDY IGVGPIFPTI SKADAEPVSG TTILKEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GYPS // ID F3RVZ3_VIBPH Unreviewed; 444 AA. AC F3RVZ3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=VP10329_13005; OS Vibrio parahaemolyticus 10329. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=745023; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=10329; RX PubMed=21551294; DOI=10.1128/JB.05044-11; RA Gonzalez-Escalona N., Strain E.A., De Jesus A.J., Jones J.L., RA Depaola A.; RT "Genome Sequence of the Clinical O4:K12 Serotype Vibrio RT parahaemolyticus Strain 10329."; RL J. Bacteriol. 193:3405-3406(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBW01000021; EGF42201.1; -; Genomic_DNA. DR EnsemblBacteria; EGF42201; EGF42201; VP10329_13005. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 444 AA; 49318 MW; ECB7C97D1A4C4776 CRC64; MTKILIPSPL IPLTGSVQQS LLLAKEQGFN IDEIELGVSP TQFIQLVLGQ NTFRVSTDLI DVCEEAENAD FVLYYQSGLS VSECRQQPSS AIFIGIEDVE SKHDDSVETT SADVLDIWRH PVNDEIRALS VASTSRTTTL QTDQHLAWIV TLLALDFPIE DALTLARPMT NVSRETLING ETMVKQEWAS QFADFPTPVL EDCRLGIKVG WSSHGQSVNF PHLSKQSLGL YPVVDDVSWI ERLLPLGINT IQLRIKDPYQ PDLEQQIARA IELGRQYDAQ VFINDYWQLA IKHGAFGVHL GQEDIEDSNL SQLSTAGICL GLSTHGYYEL LRIVQINPSY IALGHIFPTT TKQMPSKPQG LVRLALYQKL IDSIPYGESV GYPTVAIGGI DQSNAEQVWQ CGVSSLAVVR AITLSESPKQ VIEFFDQLMS TTSTSLVMED YRAY // ID F3RZQ5_VIBPH Unreviewed; 204 AA. AC F3RZQ5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VP10329_04212; OS Vibrio parahaemolyticus 10329. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=745023; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=10329; RX PubMed=21551294; DOI=10.1128/JB.05044-11; RA Gonzalez-Escalona N., Strain E.A., De Jesus A.J., Jones J.L., RA Depaola A.; RT "Genome Sequence of the Clinical O4:K12 Serotype Vibrio RT parahaemolyticus Strain 10329."; RL J. Bacteriol. 193:3405-3406(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBW01000024; EGF40883.1; -; Genomic_DNA. DR EnsemblBacteria; EGF40883; EGF40883; VP10329_04212. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21738 MW; 0D952EB615F08C0E CRC64; MNAYRLYLVT DDQQDLPTLK HVVRKAVEGG VTMVQVREKH GDVRAFIERA QAVKTILEGT GVPLIINDRV DVALAVDADG VHLGQSDMPA EIARQLIGPN KILGLSIETE DQLAEADSLP IDYIGLSAIF ATPTKTNTKK HWGIGGLKMA LNTTSLPIVA IGGINETNIP ALSATGVHGL ALVSAICHAE NPTKAAEYLL SLMD // ID F3S4E4_9PROT Unreviewed; 211 AA. AC F3S4E4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SXCC_00915; OS Gluconacetobacter sp. SXCC-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconacetobacter. OX NCBI_TaxID=1004836; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SXCC-1; RX PubMed=21551293; DOI=10.1128/JB.05147-11; RA Du X.J., Jia S.R., Yang Y., Wang S.; RT "Genome sequence of Gluconacetobacter sp. strain SXCC-1, isolated from RT Chinese vinegar fermentation starter."; RL J. Bacteriol. 193:3395-3396(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SXCC-1; RA Du X., Jia S., Yang Y., Wang S.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCH01000029; EGG78318.1; -; Genomic_DNA. DR ProteinModelPortal; F3S4E4; -. DR EnsemblBacteria; EGG78318; EGG78318; SXCC_00915. DR PATRIC; 55057133; VBIGluSp188091_0630. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21993 MW; 064658761E46E226 CRC64; MNDCQLYLIT PESLDPAAFA PRLAEALDAG PVAAVQLRLK NVPDDAIRHA VDVLQPIAHA RNVAFILNDR PDLAVACGCD GAHVGMDDGD VATARRILGA DLQLGVSCYD SRDMALRAGE AGADYVAFGA FFPSPSKETE VRADPALLTW WSSMIELPVV AIGGITPDNC GTLVRAGADF LSVISAVWSH PDGPGAGVRA MNTAIAAAED A // ID F3SDF6_9PROT Unreviewed; 206 AA. AC F3SDF6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=SXCC_04167; OS Gluconacetobacter sp. SXCC-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconacetobacter. OX NCBI_TaxID=1004836; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SXCC-1; RX PubMed=21551293; DOI=10.1128/JB.05147-11; RA Du X.J., Jia S.R., Yang Y., Wang S.; RT "Genome sequence of Gluconacetobacter sp. strain SXCC-1, isolated from RT Chinese vinegar fermentation starter."; RL J. Bacteriol. 193:3395-3396(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SXCC-1; RA Du X., Jia S., Yang Y., Wang S.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCH01000055; EGG75257.1; -; Genomic_DNA. DR EnsemblBacteria; EGG75257; EGG75257; SXCC_04167. DR PATRIC; 55062853; VBIGluSp188091_3403. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22311 MW; 84308F22FBE2B079 CRC64; MNTPLPSRIY PVVDTAQWVA RLGQAGARLI QLRLKDMADE ALHHEIREGI RQARAHGVTL VLNDYWRIAI AEGVDYIHLG QEDLDTADLS AIRAAGIRLG VSTHSDSELE RALSVAPDYV ALGPVWPTKL KKMPWAPQGT GKLTRWKQRI GTIPLVAIGG ITLERAPLCL AAGADCVSAV SDFIRMPDPQ AQVKAWLAAT AVPAGM // ID F3SRY0_STAWA Unreviewed; 213 AA. AC F3SRY0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU121_0753; OS Staphylococcus warneri VCU121. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904338; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU121; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFEC01000100; EGG96470.1; -; Genomic_DNA. DR EnsemblBacteria; EGG96470; EGG96470; SEVCU121_0753. DR PATRIC; 55743023; VBIStaWar171498_1527. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23342 MW; 60C38750C043E223 CRC64; MSFKASELKI YFICGTQDIP ENQTIQDILT QALEAGITMF QFREKGDKAL SGLNKEKLAK ELQALCNTYS VPFIVNDDVS LAKRINADGI HVGQDDEAVR AFSNDFQDKI IGLSVGNLYE YEKSDLTNVD YIGIGPMFET PSKSDANAPV GPDMIKQLRQ KMGKFPMVAI GGITEDNVGL IANAGADGIS VISAISRSNN IDNTVNEFKK YFK // ID F3SSG6_STAWA Unreviewed; 196 AA. AC F3SSG6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU121_1063; OS Staphylococcus warneri VCU121. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904338; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU121; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFEC01000114; EGG96318.1; -; Genomic_DNA. DR EnsemblBacteria; EGG96318; EGG96318; SEVCU121_1063. DR PATRIC; 55743437; VBIStaWar171498_1705. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 22577 MW; C57E887585698614 CRC64; MYIFIAITFY KELSQQDLRH FLTIEPAIDG LLFRTPMSAF ELQGFIVQLI EAGFPKDKII IHSHFKLLKA LNLQCIHFKE NDEEAFLIKQ QHPELVVGMS THNIEMVKQC HEWQLDYVFF GHIFPTSSHP DEHPRTIQEI HDVLEIDIPI YAIGGISPST ISQLPTAFDG LCSISFFMTS TVSEINSLKR KWHAHA // ID F3SXU2_STAEP Unreviewed; 199 AA. AC F3SXU2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU144_2102; OS Staphylococcus epidermidis VCU144. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904347; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU144; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFED01000051; EGG62973.1; -; Genomic_DNA. DR EnsemblBacteria; EGG62973; EGG62973; SEVCU144_2102. DR PATRIC; 53723737; VBIStaEpi171049_1180. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 22765 MW; 0E8D0A09FE2AC9AA CRC64; MGGIFIFIAI TYHKQLTRDD LQHYKHIEEA IDGLLFRTSM NKEETKDIIQ SLLQLGFSKD KIIIHSDVTL LEDLHLKRIH FKENDTTAFT YKEAHPDICV SMSTHDVETV KRCYENSLDS VFFGHIFPTS SHPNVPPRSK EAIQQALNVP IPIYAIGGIN EHSLQKMPPG FKGICAISYF NNASLEEIKQ LRKEWSTHA // ID F3SYK1_STAEP Unreviewed; 213 AA. AC F3SYK1; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU144_0603; OS Staphylococcus epidermidis VCU144. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904347; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU144; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFED01000053; EGG62622.1; -; Genomic_DNA. DR ProteinModelPortal; F3SYK1; -. DR EnsemblBacteria; EGG62622; EGG62622; SEVCU144_0603. DR PATRIC; 53724295; VBIStaEpi171049_1441. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID F3T877_STAAU Unreviewed; 213 AA. AC F3T877; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21189_2639; OS Staphylococcus aureus subsp. aureus 21189. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904725; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21189; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFEE01000059; EGG60574.1; -; Genomic_DNA. DR ProteinModelPortal; F3T877; -. DR SMR; F3T877; 4-209. DR PRIDE; F3T877; -. DR EnsemblBacteria; EGG60574; EGG60574; SA21189_2639. DR PATRIC; 53731351; VBIStaAur174504_2467. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F3TBN8_STAAU Unreviewed; 213 AA. AC F3TBN8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21172_1991; OS Staphylococcus aureus subsp. aureus 21172. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904723; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21172; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFEF01000009; EGG62771.1; -; Genomic_DNA. DR ProteinModelPortal; F3TBN8; -. DR SMR; F3TBN8; 4-209. DR PRIDE; F3TBN8; -. DR EnsemblBacteria; EGG62771; EGG62771; SA21172_1991. DR PATRIC; 53733890; VBIStaAur172269_1033. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F3TM99_STAAU Unreviewed; 213 AA. AC F3TM99; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21193_0035; OS Staphylococcus aureus subsp. aureus 21193. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904726; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21193; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFEG01000024; EGG65677.1; -; Genomic_DNA. DR ProteinModelPortal; F3TM99; -. DR SMR; F3TM99; 4-209. DR PRIDE; F3TM99; -. DR EnsemblBacteria; EGG65677; EGG65677; SA21193_0035. DR PATRIC; 53741661; VBIStaAur171098_2249. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F3TRL5_STAEP Unreviewed; 215 AA. AC F3TRL5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU028_1425; OS Staphylococcus epidermidis VCU028. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904317; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU028; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFEH01000030; EGG71924.1; -; Genomic_DNA. DR ProteinModelPortal; F3TRL5; -. DR EnsemblBacteria; EGG71924; EGG71924; SEVCU028_1425. DR PATRIC; 53744855; VBIStaEpi171852_1164. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23998 MW; 87DCB45162513A97 CRC64; MNMMFDSKQL SVYFICGTQD IPKNKSIEQV LKEALEAGIT LYQFREKGPN ALKGEKKKQL ALKLKQLCHS YHVPMIVNDD VQLAQEINAD GIHVGQDDME IQQFASQFKN KIIGLSVGNL KEYQQSDLSK VDYIGVGPMY TTSSKDDASK PVGPSMISQL RLYIHDFPIV AIGGINETNV QPIVDEGADG ISVISAITRS TNIDKTVKYF LRYFT // ID F3TSG4_STAEP Unreviewed; 160 AA. AC F3TSG4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU028_1643; OS Staphylococcus epidermidis VCU028. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904317; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU028; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFEH01000038; EGG71300.1; -; Genomic_DNA. DR EnsemblBacteria; EGG71300; EGG71300; SEVCU028_1643. DR PATRIC; 53745473; VBIStaEpi171852_1457. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18169 MW; 1CFC64416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTNA // ID F3U0F9_STAEP Unreviewed; 160 AA. AC F3U0F9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU045_0150; OS Staphylococcus epidermidis VCU045. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904321; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU045; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFEI01000053; EGG70896.1; -; Genomic_DNA. DR ProteinModelPortal; F3U0F9; -. DR EnsemblBacteria; EGG70896; EGG70896; SEVCU045_0150. DR PATRIC; 53751269; VBIStaEpi170106_1909. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID F3U0W3_STAEP Unreviewed; 213 AA. AC F3U0W3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU045_2057; OS Staphylococcus epidermidis VCU045. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904321; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU045; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFEI01000056; EGG70505.1; -; Genomic_DNA. DR ProteinModelPortal; F3U0W3; -. DR EnsemblBacteria; EGG70505; EGG70505; SEVCU045_2057. DR PATRIC; 53751653; VBIStaEpi170106_2063. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID F3U3D6_RHOSH Unreviewed; 206 AA. AC F3U3D6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=RSWS8N_16239; OS Rhodobacter sphaeroides WS8N. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=992186; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WS8N; RX PubMed=21622735; DOI=10.1128/JB.05257-11; RA Porter S.L., Wilkinson D.A., Byles E.D., Wadhams G.H., Taylor S., RA Saunders N.J., Armitage J.P.; RT "Genome sequence of Rhodobacter sphaeroides Strain WS8N."; RL J. Bacteriol. 193:4027-4028(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFER01000002; EGJ19726.1; -; Genomic_DNA. DR ProteinModelPortal; F3U3D6; -. DR EnsemblBacteria; EGJ19726; EGJ19726; RSWS8N_16239. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22171 MW; 11DDB967817BEAEA CRC64; MAEVERPQLY LVTPPEIDLE IFPDRLAAVL DSTEVACLRL ALAGKDEDRI ARTGDALREV AHARDVALVI ENHVLMVERL GLDGVHLTDG ARLVRKLRKD LGPDAILGAF CGRTRHEGIN AAEAGADYVA FGPVGTTALG DGSLAEAELF GWWSEMIEVP VVAEGALTPE KVAELAPLTD FFAVGEEIWR EEDAAAALRR LLAPLG // ID F3VCL3_SHIDY Unreviewed; 211 AA. AC F3VCL3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SD15574_4432; OS Shigella dysenteriae 155-74. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766142; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=155-74; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFFZ01000096; EGI90561.1; -; Genomic_DNA. DR ProteinModelPortal; F3VCL3; -. DR SMR; F3VCL3; 20-202. DR EnsemblBacteria; EGI90561; EGI90561; SD15574_4432. DR PATRIC; 53815505; VBIShiDys163707_4404. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F3VHA5_STREE Unreviewed; 209 AA. AC F3VHA5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR148_0667; OS Streptococcus pneumoniae GA17545. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=886289; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17545; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA17545."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGA01000001; EGI87596.1; -; Genomic_DNA. DR EnsemblBacteria; EGI87596; EGI87596; SPAR148_0667. DR PATRIC; 53819054; VBIStrPne178990_0679. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23302 MW; 094F9E0E007A2FA0 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGESALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID F3VHB2_STREE Unreviewed; 210 AA. AC F3VHB2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR148_0674; OS Streptococcus pneumoniae GA17545. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=886289; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17545; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA17545."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGA01000001; EGI87603.1; -; Genomic_DNA. DR ProteinModelPortal; F3VHB2; -. DR EnsemblBacteria; EGI87603; EGI87603; SPAR148_0674. DR PATRIC; 53819068; VBIStrPne178990_0686. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID F3VNJ1_STREE Unreviewed; 209 AA. AC F3VNJ1; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR50_0694; OS Streptococcus pneumoniae GA17570. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760791; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17570; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA17570."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGB01000004; EGI84989.1; -; Genomic_DNA. DR ProteinModelPortal; F3VNJ1; -. DR EnsemblBacteria; EGI84989; EGI84989; SPAR50_0694. DR PATRIC; 53823792; VBIStrPne181904_0688. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23247 MW; 9D63833774B28637 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID F3VNJ8_STREE Unreviewed; 210 AA. AC F3VNJ8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR50_0701; OS Streptococcus pneumoniae GA17570. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760791; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17570; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA17570."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGB01000004; EGI84996.1; -; Genomic_DNA. DR ProteinModelPortal; F3VNJ8; -. DR EnsemblBacteria; EGI84996; EGI84996; SPAR50_0701. DR PATRIC; 53823806; VBIStrPne181904_0695. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID F3W0T5_SHIBO Unreviewed; 211 AA. AC F3W0T5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SB359474_3040; OS Shigella boydii 3594-74. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766139; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3594-74; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGC01000044; EGI97392.1; -; Genomic_DNA. DR ProteinModelPortal; F3W0T5; -. DR EnsemblBacteria; EGI97392; EGI97392; SB359474_3040. DR PATRIC; 53833773; VBIShiBoy161087_2996. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23055 MW; 0AF6D6D635A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVISAIT QAADWRLATA QLLEIAGVGD E // ID F3W8W7_STREE Unreviewed; 209 AA. AC F3W8W7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR68_0720; OS Streptococcus pneumoniae GA41301. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760809; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41301; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA41301."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGD01000006; EGI86465.1; -; Genomic_DNA. DR EnsemblBacteria; EGI86465; EGI86465; SPAR68_0720. DR PATRIC; 53840073; VBIStrPne178929_0744. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23271 MW; B351214742E856CB CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVKYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID F3W8X4_STREE Unreviewed; 210 AA. AC F3W8X4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR68_0727; OS Streptococcus pneumoniae GA41301. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760809; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41301; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA41301."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGD01000006; EGI86472.1; -; Genomic_DNA. DR EnsemblBacteria; EGI86472; EGI86472; SPAR68_0727. DR PATRIC; 53840087; VBIStrPne178929_0751. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22740 MW; E8E4874C9DBCC48E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID F3WQV3_SHIBO Unreviewed; 211 AA. AC F3WQV3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SB521682_4778; OS Shigella boydii 5216-82. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766141; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5216-82; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGE01000070; EGI89095.1; -; Genomic_DNA. DR ProteinModelPortal; F3WQV3; -. DR SMR; F3WQV3; 20-202. DR EnsemblBacteria; EGI89095; EGI89095; SB521682_4778. DR PATRIC; 53853417; VBIShiBoy163146_4660. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F3WUP6_9SPHN Unreviewed; 228 AA. AC F3WUP6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SUS17_868; OS Sphingomonas sp. S17. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1007104; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S17; RX PubMed=21602338; DOI=10.1128/JB.05225-11; RA Farias M.E., Revale S., Mancini E., Ordonez O., Turjanski A., RA Cortez N., Vazquez M.P.; RT "Genome sequence of Sphingomonas sp. S17, isolated from an alkaline, RT hyperarsenic, and hypersaline volcano-associated lake at high altitude RT in the Argentinean Puna."; RL J. Bacteriol. 193:3686-3687(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGG01000003; EGI56297.1; -; Genomic_DNA. DR EnsemblBacteria; EGI56297; EGI56297; SUS17_868. DR PATRIC; 53856188; VBISphSp187231_0840. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 59 63 HMP-PP binding (By similarity). FT REGION 157 159 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 160 160 HMP-PP (By similarity). FT BINDING 187 187 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 24312 MW; A66E04A2FD94DD34 CRC64; MTLDDDPLGP LDPQFADAFV RDMRRPPCQL YLISPLEVGG DFPDRLARAL DAGPVAAFQF RVKDMDQHAA AKLAEPLQRI CADREVAFIV NDSISLAKRL GADGVHLGQE DGDAREARDV LGPSVQIGVT CHDSRHLAME AGEAGADYVA FGAFYPTTTK ETKHRAEPVV LSWWSTLFEL PCVAIGGITP ANAAPLVKAG ADFLAASGAV WNGDEAAAVK AFAEVLKV // ID F3X0A0_9SPHN Unreviewed; 160 AA. AC F3X0A0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Thiamine monophosphate synthase/TENI family protein; GN ORFNames=SUS17_2868; OS Sphingomonas sp. S17. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1007104; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S17; RX PubMed=21602338; DOI=10.1128/JB.05225-11; RA Farias M.E., Revale S., Mancini E., Ordonez O., Turjanski A., RA Cortez N., Vazquez M.P.; RT "Genome sequence of Sphingomonas sp. S17, isolated from an alkaline, RT hyperarsenic, and hypersaline volcano-associated lake at high altitude RT in the Argentinean Puna."; RL J. Bacteriol. 193:3686-3687(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGG01000015; EGI54321.1; -; Genomic_DNA. DR EnsemblBacteria; EGI54321; EGI54321; SUS17_2868. DR PATRIC; 53860130; VBISphSp187231_2765. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 17161 MW; 3DFD517962DCFCC0 CRC64; MTDERLGDGL WAALRRLPPG SGVVFRHHAT PPGKRRAIHR RVWRIARARG LVLLVAGGGL PGDGVHKWGG RKGLRSWPAH DRAEAIAGWK AGADLLFVSP LFPTRSHPGA PSIKPARAAR IGRGLGLAQI ALGGMNAERF RRLRGRFDGW AAIDAWGGAG // ID F3X5X0_STREE Unreviewed; 209 AA. AC F3X5X0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR120_0695; OS Streptococcus pneumoniae GA47901. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760861; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47901; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA47901."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGR01000001; EGJ18795.1; -; Genomic_DNA. DR ProteinModelPortal; F3X5X0; -. DR EnsemblBacteria; EGJ18795; EGJ18795; SPAR120_0695. DR PATRIC; 53870338; VBIStrPne180632_0716. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID F3X5X7_STREE Unreviewed; 210 AA. AC F3X5X7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR120_0702; OS Streptococcus pneumoniae GA47901. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760861; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47901; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA47901."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGR01000001; EGJ18802.1; -; Genomic_DNA. DR ProteinModelPortal; F3X5X7; -. DR EnsemblBacteria; EGJ18802; EGJ18802; SPAR120_0702. DR PATRIC; 53870352; VBIStrPne180632_0723. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22744 MW; A3239DF7871A7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID F3XC09_STREE Unreviewed; 209 AA. AC F3XC09; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR93_0746; OS Streptococcus pneumoniae GA47368. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760834; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47368; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA47368."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGS01000003; EGJ17942.1; -; Genomic_DNA. DR ProteinModelPortal; F3XC09; -. DR EnsemblBacteria; EGJ17942; EGJ17942; SPAR93_0746. DR PATRIC; 53875175; VBIStrPne180912_0745. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID F3XC16_STREE Unreviewed; 210 AA. AC F3XC16; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR93_0753; OS Streptococcus pneumoniae GA47368. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760834; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47368; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA47368."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGS01000003; EGJ17949.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ17949; EGJ17949; SPAR93_0753. DR PATRIC; 53875189; VBIStrPne180912_0752. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22728 MW; E8F9319141D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGAGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID F3XGW5_STREE Unreviewed; 209 AA. AC F3XGW5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR69_0696; OS Streptococcus pneumoniae GA41317. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760810; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41317; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA41317."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGT01000001; EGJ16654.1; -; Genomic_DNA. DR ProteinModelPortal; F3XGW5; -. DR EnsemblBacteria; EGJ16654; EGJ16654; SPAR69_0696. DR PATRIC; 53880090; VBIStrPne181959_0720. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID F3XGX2_STREE Unreviewed; 210 AA. AC F3XGX2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR69_0703; OS Streptococcus pneumoniae GA41317. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760810; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41317; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic sequence of Streptococcus pneumoniae GA41317."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGT01000001; EGJ16661.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ16661; EGJ16661; SPAR69_0703. DR PATRIC; 53880104; VBIStrPne181959_0727. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22728 MW; E8F9319141D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGAGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID F3XVZ1_9FLAO Unreviewed; 210 AA. AC F3XVZ1; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9074_02920; OS Capnocytophaga sp. oral taxon 329 str. F0087. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=706436; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0087; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHP01000069; EGJ55340.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ55340; EGJ55340; HMPREF9074_02920. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23213 MW; 9ADBFAD6FE61DDC3 CRC64; MQNLQFITHY TEQYGYADAA RLALEGGCRW IQLRMKDASP EEWMRTGAEV EALCRRYGAT FILDDHVEWV DVLHADGVHL GKSDMPIDEA RRLLGQDRII GGTANTLEDV MLHAVRGADY IGCGPFRFTT TKEKLAPTLG LEGYRRILDG MKKKGISLPL IAIGGITKED IPALMETGVD GIALSGTILR AGSPTEETRN ILRILNVQQS // ID F3XVZ3_9FLAO Unreviewed; 202 AA. AC F3XVZ3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF9074_02922; OS Capnocytophaga sp. oral taxon 329 str. F0087. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=706436; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0087; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHP01000069; EGJ55342.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ55342; EGJ55342; HMPREF9074_02922. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23165 MW; 9C04F2F86DD51C2E CRC64; MKLILLTPPD FFVEEDKILT ALFEEGLDLL HLRKPDTEPV YSERLLTLLP ESHHNQIVVH DHFYLKEEFN LRGIHLNGRN PEPPVGYKGH ISKSFHHIDE LKAEKKNFNY VFLSPIFDSI SKSNYTSAFD MEVLKQASAH GIIDKRVMAL GGITTENMAV AKELGFGGVV VLGDLWNRFN IHSTLDYKEL INHFRKLRKA AD // ID F3YAB2_MELPT Unreviewed; 216 AA. AC F3YAB2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MPTP_0981; OS Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 / OS NCIMB 702443). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Melissococcus. OX NCBI_TaxID=940190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443; RX PubMed=21622755; DOI=10.1128/JB.05151-11; RA Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M., RA Miyoshi-Akiyama T.; RT "Complete genome sequence of Melissococcus plutonius ATCC 35311."; RL J. Bacteriol. 193:4029-4030(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35311; RA Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D., RA Akiyama T.; RT "Whole genome sequence of Melissococcus plutonius ATCC 35311."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012200; BAK21440.1; -; Genomic_DNA. DR RefSeq; YP_004456249.1; NC_015516.1. DR EnsemblBacteria; BAK21440; BAK21440; MPTP_0981. DR GeneID; 10595807; -. DR KEGG; mps:MPTP_0981; -. DR PATRIC; 54620710; VBIMelPlu182073_0971. DR KO; K00788; -. DR BioCyc; MPLU940190:GH20-981-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23733 MW; A6C985FCDA819F5A CRC64; MLTSQQLKKA LQIYFIAGTQ DTNGSSLQLL NVLDKALTAG ITCFQYREKG ANSLKKSLER KRMARACQRL CRKHQVPFII NDDIELALEI DADGIHVGQN DEAISKVIQK NPNKIIGLSC HNVTEITYAN TFKEISYYGI GPIFPTSSKL DADKPLGLDQ LKTMVAVAKK PTVAIGGISI KNAVDIWQSN ADGLAIISAI TQAENLEETI ELLKFN // ID F3YPH2_LISMN Unreviewed; 208 AA. AC F3YPH2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMOSA_12210; OS Listeria monocytogenes str. Scott A. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1027396; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Scott A; RX PubMed=21685277; DOI=10.1128/JB.05328-11; RA Briers Y., Klumpp J., Schuppler M., Loessner M.J.; RT "Genome Sequence of Listeria monocytogenes Scott A, a Clinical Isolate RT from a Food-Borne Listeriosis Outbreak."; RL J. Bacteriol. 193:4284-4285(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001159; EGJ23830.1; -; Genomic_DNA. DR ProteinModelPortal; F3YPH2; -. DR EnsemblBacteria; EGJ23830; EGJ23830; LMOSA_12210. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21913 MW; 91665D070EBAFD9D CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAE EAERLGAVDY IGVGPIFPTI SKADAEPVSG TTILKEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC QLVIANLI // ID F3YWF5_DESAF Unreviewed; 213 AA. AC F3YWF5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Desaf_0993; OS Desulfovibrio africanus str. Walvis Bay. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=690850; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Walvis Bay; RX PubMed=21642452; DOI=10.1128/JB.05223-11; RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., RA Brandt C.C., Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., RA Han J., Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., RA Palumbo A.V., Elias D.A.; RT "Genome sequence of the mercury-methylating and pleomorphic RT Desulfovibrio africanus Strain Walvis Bay."; RL J. Bacteriol. 193:4037-4038(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003221; EGJ49341.1; -; Genomic_DNA. DR RefSeq; YP_005051000.1; NC_016629.1. DR EnsemblBacteria; EGJ49341; EGJ49341; Desaf_0993. DR GeneID; 11568440; -. DR KEGG; daf:Desaf_0993; -. DR KO; K00788; -. DR BioCyc; DAFR690850:GHYW-1006-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22598 MW; FA9160767C005B90 CRC64; MPARLDLRLY LVTDPVGCMG RDLAWVVAEA LAGGVTMVQL REKQATTREF LERAWRIKPI CDAAGAPFII NDRVDVALAV GAAGVHLGRQ DMPYADARRL LGPRAIIGLT VHNMAELEEA KATDADYFGL GPAFPTRTKP DAPAPWGMDE YARACVLAGR PVVAIGGIGP HNARTVLAAG AHGLAVSSAI CSADSPKWAA MELAALHARL WPS // ID F3Z463_DESAF Unreviewed; 214 AA. AC F3Z463; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Desaf_3315; OS Desulfovibrio africanus str. Walvis Bay. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=690850; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Walvis Bay; RX PubMed=21642452; DOI=10.1128/JB.05223-11; RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., RA Brandt C.C., Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., RA Han J., Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., RA Palumbo A.V., Elias D.A.; RT "Genome sequence of the mercury-methylating and pleomorphic RT Desulfovibrio africanus Strain Walvis Bay."; RL J. Bacteriol. 193:4037-4038(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003221; EGJ51605.1; -; Genomic_DNA. DR RefSeq; YP_005053264.1; NC_016629.1. DR EnsemblBacteria; EGJ51605; EGJ51605; Desaf_3315. DR GeneID; 11567688; -. DR KEGG; daf:Desaf_3315; -. DR KO; K00788; -. DR BioCyc; DAFR690850:GHYW-3376-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22516 MW; 557EB54384934180 CRC64; MSRSFDLSVY LVTDRPLCQG RDLLDIVGQA VRGGVSMVQL REKMADTREF VELARALKAM LAPQGVPLLI NDRVDVALAA GADGVHVGQG DMHVLDVRRI LGPRAILGLS TDTLEQVLEA EGLPVDYYGV GPVFPTSTKT DFSHQPWGIE GLRRLRPRIS RPMVGIGGVD VGNAARIVSA GAEGVAVVSA ICSAPSPKDA ARALAKAVAV GRGS // ID F3Z5N3_9ACTO Unreviewed; 211 AA. AC F3Z5N3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=STTU_0619; OS Streptomyces sp. Tu6071. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=355249; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tu6071; RA Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., RA Bechthold A., Gunther S.; RT "Genome sequence of Streptomyces sp. Tu6071."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001165; EGJ73408.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ73408; EGJ73408; STTU_0619. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 20903 MW; F8E0410C0B244FD2 CRC64; MYLVTDTAQC AARGRTVPET VAAAVAGGVT AVQVREKDAG GRAFLEQVRA VADVLPAHVT LLVNDRVDVY LAARAAGARV HGVHVGQSDL PVAAVRDLVG ADALLGLSAA TPGELAEAAA ARVDHVGVGA LHATTTKADA PPALGIEGFA RLLAPAGLPP AVAIGGVVPA DLPALRRAGA AGAAIVSGIC AAADPETAAR RYVAAWERGV G // ID F3ZJ60_9ACTO Unreviewed; 235 AA. AC F3ZJ60; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=STTU_5271; OS Streptomyces sp. Tu6071. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=355249; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tu6071; RA Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., RA Bechthold A., Gunther S.; RT "Genome sequence of Streptomyces sp. Tu6071."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001165; EGJ78060.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ78060; EGJ78060; STTU_5271. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 235 AA; 24955 MW; 9B9BA94AA8E06486 CRC64; MPDRTPHAAA RTVLADARLY LCTDARKHRN DLPAFLDAVL SGGVDIVQLR DKSLEAAEEL ELLQVFADAC RRHGKLLAVN DRADVAHAAR ADVLHLGQGD LPVPAARALI GPDALIGRST HSEAEAAAAA VQDGVDYFCT GPCWPTPTKP GRPAPGLPLV RYAAALGTTR PWFAIGGIDA ARLDEVLDAG ARRVVVVRAL TEAEDPEHAA RELARRLRAL PLGTPSVQSV DKKSA // ID F3ZQ58_9BACE Unreviewed; 202 AA. AC F3ZQ58; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Bcop_1530; OS Bacteroides coprosuis DSM 18011. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=679937; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18011; RX PubMed=21677860; DOI=10.4056/sigs.1784330; RA Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M., RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., RA Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L., RA Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., RA Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Non-contiguous finished genome sequence of Bacteroides coprosuis type RT strain (PC139)."; RL Stand. Genomic Sci. 4:233-243(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001167; EGJ71724.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ71724; EGJ71724; Bcop_1530. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 22833 MW; F1EC8A16FF226099 CRC64; MKLILITPPH FFPQEADALN YLLENTSFRL HIRKPKASKD ALAKLIQQID AKFYSRVVLH DAHSLALKYL LGGIHLNKRN PTAPDKYAGT ISSSCHSWNE VLSYRNTVNY LFISPLYDSI SKQGYSQAFT ESQLQQAQEK GWIDQRVIGL GGIAPDKIPL LKSYGFGGVA VLGYVWKDFI ETLDYSSLQA RLRACEDQIQ LE // ID F3ZQ59_9BACE Unreviewed; 214 AA. AC F3ZQ59; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Bcop_1531; OS Bacteroides coprosuis DSM 18011. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=679937; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18011; RX PubMed=21677860; DOI=10.4056/sigs.1784330; RA Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M., RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., RA Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L., RA Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., RA Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Non-contiguous finished genome sequence of Bacteroides coprosuis type RT strain (PC139)."; RL Stand. Genomic Sci. 4:233-243(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001167; EGJ71725.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ71725; EGJ71725; Bcop_1531. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23460 MW; F91927326BFB3B56 CRC64; MIQYKLPRLL FITHQTPQCS YLQSITRALA GGCKFIQLRM KGAGYHEIKE VVHQALPLCK EQGALLTIDD HAELCLEWNL EGVHLGLNDM KASEARKLLG PDVLIGGTAN TFEDIQYQIA EGVDYIGLGP YQYTSTKTNL STTLGLNGYL SIIQECRFNN IDIPIYAIGG INQADIPAIL STGVWGISLS SAILNAPNPI KETTNIIQTI DKSL // ID F3ZUB9_9BACE Unreviewed; 214 AA. AC F3ZUB9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Bcop_1160; OS Bacteroides coprosuis DSM 18011. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=679937; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18011; RX PubMed=21677860; DOI=10.4056/sigs.1784330; RA Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M., RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., RA Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L., RA Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., RA Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Non-contiguous finished genome sequence of Bacteroides coprosuis type RT strain (PC139)."; RL Stand. Genomic Sci. 4:233-243(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001167; EGJ71364.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ71364; EGJ71364; Bcop_1160. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23054 MW; 8579050381E90738 CRC64; MKKSLDLSLY LVTDPQVAEG NSFLEVIEDA VKGGVTLVQL REKDCSSREF YDKALAIKHL LSSYDVPLII NDRLDIALAV DADGLHIGQE DIPYDVARKI LGPDKIIGLS VENKTDALRA NKLDIDYIGI SPVFSTPTKI DTAPALGLEG SRLINSISKH PSVGIGGIHL QNAASIIASG SDGISVVSAI MMAKDPFRAA QELKQIILKA KDYE // ID F4A2F3_MAHA5 Unreviewed; 207 AA. AC F4A2F3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mahau_2043; OS Mahella australiensis (strain DSM 15567 / CIP 107919 / 50-1 BON). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family IV. Incertae Sedis; Mahella. OX NCBI_TaxID=697281; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Teshima H., RA Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Pukall R., Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Mahella australiensis DSM 15567."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002360; AEE97219.1; -; Genomic_DNA. DR RefSeq; YP_004464041.1; NC_015520.1. DR ProteinModelPortal; F4A2F3; -. DR EnsemblBacteria; AEE97219; AEE97219; Mahau_2043. DR GeneID; 10608806; -. DR KEGG; mas:Mahau_2043; -. DR PATRIC; 54632795; VBIMahAus157719_2085. DR KO; K00788; -. DR BioCyc; MAUS697281:GH33-2090-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21769 MW; 286FEE929C16F2EA CRC64; MNISGLYAIA GSYRNDKPVE RMVEAAIKGG ASIIQLREKN TSAKQYIERA TRVKAITDRY GVPLIIDDRA DIALASGATG VHLGQNDLPI EFARQILGSS AVIGISVQTP QQAIMAQRQG ADYIGAGPVF PTISKDDAEP PIGIADLYDI CHAVTIPVIA IGGIYSYNAT EVMGAGAAGI AVISAIFNAR DIAAATAELI QAMRRNT // ID F4A425_CLOBO Unreviewed; 216 AA. AC F4A425; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 22-JAN-2014, entry version 17. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=CbC4_0679; OS Clostridium botulinum BKT015925. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=929506; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BKT015925; RX PubMed=21486474; DOI=10.1186/1471-2164-12-185; RA Skarin H., Hafstrom T., Westerberg J., Segerman B.; RT "Clostridium botulinum group III: a group with dual identity shaped by RT plasmids, phages and mobile elements."; RL BMC Genomics 12:185-185(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002410; AEB75359.1; -; Genomic_DNA. DR RefSeq; YP_004395356.1; NC_015425.1. DR EnsemblBacteria; AEB75359; AEB75359; CbC4_0679. DR GeneID; 10463595; -. DR KEGG; cbn:CbC4_0679; -. DR PATRIC; 54456643; VBICloBot178872_0998. DR KO; K00788; -. DR BioCyc; CBOT929506:GHKW-703-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 216 AA; 24285 MW; 77CF5FB9207B3E2A CRC64; MLFLRIGREF KEVIKIIFVV TNRRLVQDED FYTVIERVAK NKIDYLILRE KDLDYDELIS VTKDIKLITD KYNVPLIING NLEVAEEVQA YGCQLGYETL NNSKEKCLKS KLKIGASVHS VEEAKNAEKI GVDYIIAGHV FETDCKKGLK GRGIGFIKNI SNFVKIPVIA IGGINKENVT KVMESGARGI AIMSSAMKKN NVETIKCIKN LINNKS // ID F4A5C5_CLOBO Unreviewed; 204 AA. AC F4A5C5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CbC4_2000; OS Clostridium botulinum BKT015925. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=929506; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BKT015925; RX PubMed=21486474; DOI=10.1186/1471-2164-12-185; RA Skarin H., Hafstrom T., Westerberg J., Segerman B.; RT "Clostridium botulinum group III: a group with dual identity shaped by RT plasmids, phages and mobile elements."; RL BMC Genomics 12:185-185(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002410; AEB76672.1; -; Genomic_DNA. DR RefSeq; YP_004396669.1; NC_015425.1. DR EnsemblBacteria; AEB76672; AEB76672; CbC4_2000. DR GeneID; 10464925; -. DR KEGG; cbn:CbC4_2000; -. DR PATRIC; 54459328; VBICloBot178872_2318. DR KO; K00788; -. DR BioCyc; CBOT929506:GHKW-2033-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21996 MW; D71C2A1043EA6846 CRC64; MDLNYKLYLI TDRSFLNGRS LADCVEDAIK GGATMVQVRE KNISTRKFFN IAKEVQNVTS KYNIPLLIND RIDIALAINA DGVHLGQSDM SIDIARKILG PNKIIGISAG NINEAKEAEN NGADYVGLGA VFFTGTKRDI DEPIGLKGLN EITKNINIPS VAIGGINKEN AKSVLETGVN GISVISAILN KDNIKQAAEE LLNI // ID F4AS53_GLAS4 Unreviewed; 571 AA. AC F4AS53; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 11-DEC-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=Glaag_2310; OS Glaciecola sp. (strain 4H-3-7+YE-5). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Glaciecola. OX NCBI_TaxID=983545; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7+YE-5; RX PubMed=21705587; DOI=10.1128/JB.05468-11; RG US DOE Joint Genome Institute; RA Klippel B., Lochner A., Bruce D.C., Davenport K.W., Detter C., RA Goodwin L.A., Han J., Han S., Land M.L., Mikhailova N., Nolan M., RA Pennacchio L., Pitluck S., Tapia R., Woyke T., Wiebusch S., Basner A., RA Abe F., Horikoshi K., Keller M., Antranikian G.; RT "Complete genome sequence of the marine, cellulose and xylan degrading RT bacterium Glaciecola sp. 4H-3-7+YE-5."; RL J. Bacteriol. 193:4547-4548(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4H-3-7+YE-5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Piela B., Lochner A., Antranikian F.I., Woyke T.; RT "Complete sequence of chromosome of Glaciecola sp. 4H-3-7+YE-5."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002526; AEE23255.1; -; Genomic_DNA. DR RefSeq; YP_004434523.1; NC_015497.1. DR EnsemblBacteria; AEE23255; AEE23255; Glaag_2310. DR GeneID; 10572455; -. DR KEGG; gag:Glaag_2310; -. DR PATRIC; 54578319; VBIGlaSp182133_2452. DR KO; K14153; -. DR BioCyc; GSP983545:GH3Q-2364-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 571 AA; 61694 MW; 6F96738DDC4338B3 CRC64; MIDRDALVSD PQSTDHGIKP TVLTFSGSDS AGLAGMQMDI KVQHAFNIHC LSVLTAVTAQ NNQQVLAVHA VEQTMFDAQI KAVSAFKPGA IKTGLIAQHA QAKSIIDAKQ ALGIPFICDP VGAATSGNPL IARGSEDSDG HFTDVLLPHC TLITPNIPEA ERLVGFSILS SQDIKNAAKI LLDKGASAVL IKGGHGPCAK RFSQDYYCNP TEQFWLESQW IDTQHTRGTG CALASAIASC IALGYCLKDA VVIAKMAITQ GLIDAKALLS NPQGYMDTQG YMDTHDKGAE NCKDTHAKQS YMDTHGKGTG NYKDTNYEDT HDKGAVDIRS FPSAQQILPS LRDDDGGAGC GEPHSFLTPV EPFPDIGDSP LGLYPIVDRA DWLEMLLPLG VTTIQLRIKD LSDRCLEDEI SRAVQIARRY SCRLFINDHW QLAIKHRAYG VHLGQEDLIA TQSDASNPIQ QLRSAGLRLG ISTHCHYEVA RAHSFKPSYI AYGPVFATSS KDMPWVPQGL TGLDYWQNLL AYPLVAIGGI NLERAQAIHA LGVSGIAMIS EITQADSPLE KTRALLAALR T // ID F4AWN4_KROS4 Unreviewed; 213 AA. AC F4AWN4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Krodi_2641; OS Krokinobacter sp. (strain 4H-3-7-5) (Krokinobacter diaphorus (strain OS 4H-3-7-5)). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Krokinobacter. OX NCBI_TaxID=983548; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7-5; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Piela B., Lochner A., Antranikian F.I., Woyke T.; RT "Complete sequence of Krokinobacter diaphorus 4H-3-7-5."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4H-3-7-5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Piela B., Lochner A., Antranikian F.I., Woyke T.; RT "Complete sequence of Krokinobacter sp. 4H-3-7-5."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002528; AEE20617.1; -; Genomic_DNA. DR RefSeq; YP_004431885.1; NC_015496.1. DR EnsemblBacteria; AEE20617; AEE20617; Krodi_2641. DR GeneID; 10569718; -. DR KEGG; kdi:Krodi_2641; -. DR PATRIC; 54572563; VBIKroSp190710_2723. DR BioCyc; KSP983548:GHAF-2694-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23239 MW; C8F2278BFC1316D2 CRC64; MIPKLHYISQ GSSLKEHIEH IQKACNAGAE LVQLRVKDCS QKKLLAIAQE AREITAHFQT RLIINDDYKI AKEVKADGVH LGSADACPIT ARKHLYTWQI IGGTAHTLQD CEALIEKQVD YISLGPYSTT TTKETTAKTL GTSGYKAIID ELATTTPMLA VGGITLNDVK NILEAGIDGI AVSQAITTEF NSIRSFNELL GASSTQEQRH SFE // ID F4AWP4_KROS4 Unreviewed; 215 AA. AC F4AWP4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Krodi_2651; OS Krokinobacter sp. (strain 4H-3-7-5) (Krokinobacter diaphorus (strain OS 4H-3-7-5)). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Krokinobacter. OX NCBI_TaxID=983548; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7-5; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Piela B., Lochner A., Antranikian F.I., Woyke T.; RT "Complete sequence of Krokinobacter diaphorus 4H-3-7-5."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4H-3-7-5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Piela B., Lochner A., Antranikian F.I., Woyke T.; RT "Complete sequence of Krokinobacter sp. 4H-3-7-5."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002528; AEE20627.1; -; Genomic_DNA. DR RefSeq; YP_004431895.1; NC_015496.1. DR EnsemblBacteria; AEE20627; AEE20627; Krodi_2651. DR GeneID; 10569728; -. DR KEGG; kdi:Krodi_2651; -. DR PATRIC; 54572583; VBIKroSp190710_2733. DR KO; K00788; -. DR BioCyc; KSP983548:GHAF-2704-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23590 MW; B947BE9A9601D1CE CRC64; MIPKLHYISQ GNTPEAHLDN LQKACSHGAT LVQLRLKNVP LDQVLIIARE ARTITAQYDT KLIINDHYEV AKEVKADGVH LGKTDSCPTV ARAHLYSWQI IGGTANTLED CLSLRDKGVD YIGLGPLRFT TTKKNLSPVL GYNGYHLITE TLKTKTPIIA IGGITVDDVT DLLETGIHGI AVSGEITHDF TKIEAFQKSL GASFNKEQHH TLNNI // ID F4AWP6_KROS4 Unreviewed; 195 AA. AC F4AWP6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Krodi_2653; OS Krokinobacter sp. (strain 4H-3-7-5) (Krokinobacter diaphorus (strain OS 4H-3-7-5)). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Krokinobacter. OX NCBI_TaxID=983548; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7-5; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Piela B., Lochner A., Antranikian F.I., Woyke T.; RT "Complete sequence of Krokinobacter diaphorus 4H-3-7-5."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4H-3-7-5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Piela B., Lochner A., Antranikian F.I., Woyke T.; RT "Complete sequence of Krokinobacter sp. 4H-3-7-5."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002528; AEE20629.1; -; Genomic_DNA. DR RefSeq; YP_004431897.1; NC_015496.1. DR EnsemblBacteria; AEE20629; AEE20629; Krodi_2653. DR GeneID; 10569730; -. DR KEGG; kdi:Krodi_2653; -. DR PATRIC; 54572587; VBIKroSp190710_2735. DR KO; K00788; -. DR BioCyc; KSP983548:GHAF-2706-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 195 AA; 22386 MW; 3090E608A4688078 CRC64; MIIVLSPENN ISNEVEILPQ LFKQGLACYH LRKPHKSYEE YCAYIQQIDT AFHDKIVVHD HHMIINEFNL KGIHFKEQHR MDHINNPGKY FKGLNMFGKT ISSSFHDLQN LEDCYFEFDY HFLSPVFDSI SKEGYKGRGF DVNNSDKTII ALGGICPENV AQVNELGYNG IAVLGSIWKA ENPLQSFKKI KAVFG // ID F4B1Z9_KROS4 Unreviewed; 200 AA. AC F4B1Z9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Krodi_0897; OS Krokinobacter sp. (strain 4H-3-7-5) (Krokinobacter diaphorus (strain OS 4H-3-7-5)). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Krokinobacter. OX NCBI_TaxID=983548; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7-5; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Piela B., Lochner A., Antranikian F.I., Woyke T.; RT "Complete sequence of Krokinobacter diaphorus 4H-3-7-5."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4H-3-7-5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Piela B., Lochner A., Antranikian F.I., Woyke T.; RT "Complete sequence of Krokinobacter sp. 4H-3-7-5."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002528; AEE18881.1; -; Genomic_DNA. DR RefSeq; YP_004430149.1; NC_015496.1. DR EnsemblBacteria; AEE18881; AEE18881; Krodi_0897. DR GeneID; 10567935; -. DR KEGG; kdi:Krodi_0897; -. DR PATRIC; 54568886; VBIKroSp190710_0931. DR BioCyc; KSP983548:GHAF-911-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 200 AA; 22170 MW; A435356ED2DBF5F8 CRC64; MIILISPEET SENEIATLHQ LFEAGLSHFH LRKPNASLDD HIAYLNMVNA TYHNRIMTHN FHKELCNQFN IMGVHLEEAM WRAQGDRLEA YVNSFTSKDN SVSSSYHEPE DLASQAVRFA YTLLSPVFSA ISKSDMQGRG FDVRHINKDI VGMGGINATT TPEALKLGFK GVGALGGVWN ADNPVAAFIE MKNAFAKANT // ID F4BGC2_FRACN Unreviewed; 494 AA. AC F4BGC2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Phosphomethylpyrimidine kinase / Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=FN3523_1213; OS Francisella cf. novicida (strain 3523). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=676032; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3523; RX PubMed=21666011; DOI=10.1128/AEM.00337-11; RA Siddaramappa S., Challacombe J.F., Petersen J.M., Pillai S., Hogg G., RA Kuske C.R.; RT "Common ancestry and novel genetic traits of Francisella novicida-like RT isolates from North America and Australia as revealed by comparative RT genomic analyses."; RL Appl. Environ. Microbiol. 77:5110-5122(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002558; AEE26516.1; -; Genomic_DNA. DR RefSeq; YP_005824267.1; NC_017449.1. DR EnsemblBacteria; AEE26516; AEE26516; FN3523_1213. DR GeneID; 12924973; -. DR KEGG; fcn:FN3523_1213; -. DR PATRIC; 54259769; VBIFraCf142222_1221. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR BioCyc; FNOV676032:GLDF-1227-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 494 AA; 54806 MW; A06B97FB7568CE57 CRC64; MASVLRDSIM RDIFLTIGGS DSSSGAGIQA DIKTANNIGV HVCTVISCVT AQNSTSILNI EKVYKDSFKE QIQAISSDFK IKVIKTSVLS SIEQIDIVVD LLNDLKDVFY ICDPVMVSTT GYSLVDYKLV EYSKRKLYPL ANILVPNLDE AKTLLDEYDS SNMEVVEIAK AIQKKYNCKS VLLKGGHDSY KNISLDYYYS PEVNYKLIST RHKLDEKVRG TGCTFSSAIA SFLTLGFDIN NSIVLAKSYI SNAIKSSQKI ASHGCLIVGA EYINKQGLFP KVSMHGKDLN IKFRSINKIG FYPIVDNASK IPGLANLGIK TIQLRIKSND NKHIQKHIVE AVEYQNKYGL QLFINDYYDL AIKYKAFGIH LGHDDLLSID KKTLLKIKNT DMALGLSTHD YYELAIALGV NPSYVALGPI YTTTTKKMKF APQGIARIHE WLNITDTPLV TIGGIKKRHI QSLASIGVDG VAVVTLIDEI SNHEIQNIVK LLEK // ID F4BKS8_CARS1 Unreviewed; 200 AA. AC F4BKS8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-APR-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CAR_c00200; OS Carnobacterium sp. (strain 17-4). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Carnobacterium. OX NCBI_TaxID=208596; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17-4; RX PubMed=21551290; DOI=10.1128/JB.05113-11; RA Voget S., Klippel B., Daniel R., Antranikian G.; RT "Complete genome sequence of Carnobacterium sp. 17-4."; RL J. Bacteriol. 193:3403-3404(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002563; AEB28771.1; -; Genomic_DNA. DR RefSeq; YP_004373787.1; NC_015391.1. DR EnsemblBacteria; AEB28771; AEB28771; CAR_c00200. DR GeneID; 10440140; -. DR KEGG; crn:CAR_c00200; -. DR PATRIC; 54447546; VBICarSp108130_0074. DR KO; K00788; -. DR BioCyc; CSP208596:GHHT-20-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 26 30 HMP-PP binding (By similarity). FT REGION 125 127 THZ-P binding (By similarity). FT REGION 177 178 THZ-P binding (By similarity). FT METAL 62 62 Magnesium (By similarity). FT METAL 81 81 Magnesium (By similarity). FT BINDING 61 61 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 200 AA; 21599 MW; 31A217CBCB0604D2 CRC64; MGTMNCTKDP LKILEEALEA GITCFQLREK GEGALTGSVY EEFARACQKM CLAYQVPFII NDDVELALKL DADGIHIGQE DLALSTFRKQ AKGKIIGVSV HNSREMEQAI LSGADYVGIG PIYKTQSKKD AKPPAGLHFL KAMRKQCSNF PIVGIGGITE ENASEVRSSG ADGVSVISVI CHSKDIGQTV KNLLLTKKIN // ID F4BVK6_METCG Unreviewed; 199 AA. AC F4BVK6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MCON_3369; OS Methanosaeta concilii (strain ATCC 5969 / DSM 3671 / JCM 10134 / NBRC OS 103675 / OCM 69 / GP-6) (Methanothrix concilii). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosaetaceae; Methanosaeta. OX NCBI_TaxID=990316; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 5969 / DSM 3671 / JCM 10134 / NBRC 103675 / OCM 69 / GP-6; RX PubMed=21571998; DOI=10.1128/JB.05031-11; RA Barber R.D., Zhang L., Harnack M., Olson M.V., Kaul R., RA Ingram-Smith C., Smith K.S.; RT "Complete genome sequence of Methanosaeta concilii, a specialist in RT aceticlastic methanogenesis."; RL J. Bacteriol. 193:3668-3669(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002565; AEB69619.1; -; Genomic_DNA. DR RefSeq; YP_004385437.1; NC_015416.1. DR EnsemblBacteria; AEB69619; AEB69619; MCON_3369. DR GeneID; 10462583; -. DR KEGG; mcj:MCON_3369; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR BioCyc; MCON990316:GHHN-2765-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 128 130 THZ-P binding (By similarity). FT REGION 179 180 THZ-P binding (By similarity). FT METAL 64 64 Magnesium (By similarity). FT METAL 83 83 Magnesium (By similarity). FT BINDING 63 63 HMP-PP (By similarity). FT BINDING 102 102 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 159 159 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 199 AA; 21596 MW; 5D6281574C29B1DC CRC64; MKGYYFITDS RLSRAGNISD VMEAASCKVD AVQYRNKNAE TREMYEEALH LREICRDLTF LINDRIDIAL AVGADGVHLG QTDMPCKTAR EMLGEEMIIG VTVHSLFEAL VAKRDGADYL GVSPIFQTAT KSDAGKPAGI ALIEEIRRKI DIPLIAIGGI NLSNAPEVIG AGADGLCAIS CVVESDDVSA QIKRFQDLF // ID F4CFD2_SPHS2 Unreviewed; 220 AA. AC F4CFD2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sph21_1385; OS Sphingobacterium sp. (strain 21). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=743722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=21; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Siebers A.K., Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.; RT "Complete sequence of Sphingobacterium sp. 21."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002584; ADZ77948.1; -; Genomic_DNA. DR RefSeq; YP_004316618.1; NC_015277.1. DR EnsemblBacteria; ADZ77948; ADZ77948; Sph21_1385. DR GeneID; 10347129; -. DR KEGG; shg:Sph21_1385; -. DR PATRIC; 47236585; VBISphSp165585_1482. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR BioCyc; SSP743722:GH04-1402-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24386 MW; E11D4FADAED6C80B CRC64; MNRIKKHIER LQYITHATKD KSIIDQVHIA VDAGIKWVQF RLKNADDDTF KQQAMACLEI AKRHRCTFVI NDRVHVAKEI DADGIHIGKE DMSPRTAREI LGPDKIIGCT ANTIDDIIQL SNLPIDYIGL GPFRFTRTKE KLSPILGLAG YDKIIKKAVA HNLSVPIIAI GGIQVEDVGP LFQTGVHGIA VSGIISNSNH PRKDCQNLLK QIEAQSCPTV // ID F4CFD3_SPHS2 Unreviewed; 216 AA. AC F4CFD3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Sph21_1386; OS Sphingobacterium sp. (strain 21). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=743722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=21; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Siebers A.K., Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.; RT "Complete sequence of Sphingobacterium sp. 21."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002584; ADZ77949.1; -; Genomic_DNA. DR RefSeq; YP_004316619.1; NC_015277.1. DR EnsemblBacteria; ADZ77949; ADZ77949; Sph21_1386. DR GeneID; 10347130; -. DR KEGG; shg:Sph21_1386; -. DR PATRIC; 47236587; VBISphSp165585_1483. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR BioCyc; SSP743722:GH04-1403-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 216 AA; 24654 MW; 207CF3146006EFDC CRC64; MKKQRSFAKI TLNFILDTYN MKLVIISPET FIRNESKTVN QLFDHGLEVF HVRKPNADIK SIRKFIQSID PFFHHRLIVH GDCNLLQEFN LAGIHLKAGE FEVLKEQRGV ISSSAHSIAE FIAMDRPWTQ IFISPVFDSI SKTGYRKAPH LLEMGSITRQ GQLIALGGIS DRNIGLIKRK GFDGAGLLGY IWLTTNPLSN YINLKHLVEE RTYESN // ID F4CI21_CHLP6 Unreviewed; 205 AA. AC F4CI21; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=G5O_0233; OS Chlamydophila psittaci (strain ATCC VR-125 / 6BC) (Chlamydia OS psittaci). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=331636; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-125 / 6BC; RX PubMed=21622741; DOI=10.1128/JB.05277-11; RA Grinblat-Huse V., Drabek E.F., Creasy H.H., Daugherty S.C., RA Jones K.M., Santana-Cruz I., Tallon L.J., Read T.D., Hatch T.P., RA Bavoil P., Myers G.S.; RT "Genome sequences of the zoonotic pathogens Chlamydia psittaci 6BC and RT Cal10."; RL J. Bacteriol. 193:4039-4040(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002586; AEB55234.1; -; Genomic_DNA. DR RefSeq; YP_005662907.1; NC_017287.1. DR EnsemblBacteria; AEB55234; AEB55234; G5O_0233. DR GeneID; 12242492; -. DR KEGG; chb:G5O_0233; -. DR PATRIC; 54261583; VBIChlPsi203718_0216. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 31 35 HMP-PP binding (By similarity). FT METAL 64 64 Magnesium (By similarity). FT METAL 83 83 Magnesium (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 159 159 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21921 MW; 2DDC45E55B59A64C CRC64; MILITNKQNI SVEEYLDFVC ACVHSGVTSV QLREKELSYR ELLGFGEALK SMLDPLEIPL IVSDSVSVCL DLDATGVHLG QTDGDVIEAR ELLGSDKIIG WNVNTLDQLL NANTLPIDYL GLSAMFATQN KPDATNLWGF SGLEQAVSLC EHPIVAIGGI DESNAAEVIE AGAAGIAAIG VFHSAQNPGL VTKTLREIVD RGLRC // ID F4D0S3_PSEUX Unreviewed; 221 AA. AC F4D0S3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Psed_5745; OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM OS 13855 / CB1190). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Pseudonocardia. OX NCBI_TaxID=675635; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190; RX PubMed=21725009; DOI=10.1128/JB.00415-11; RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., RA Woyke T., Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., RA Sczyrba A., Alvarez-Cohen L.; RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia RT dioxanivorans strain CB1190."; RL J. Bacteriol. 193:4549-4550(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002593; AEA27872.1; -; Genomic_DNA. DR RefSeq; YP_004335725.1; NC_015312.1. DR EnsemblBacteria; AEA27872; AEA27872; Psed_5745. DR GeneID; 10367600; -. DR KEGG; pdx:Psed_5745; -. DR PATRIC; 54403141; VBIPseDio141225_5825. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; PDIO675635:GHMF-5799-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23375 MW; 6C82C4779D535B12 CRC64; MSSDGDSRRA RLADARLYLC TDARRERGDL AEFADAVLSG GVDVIQLRDK GSDGPLEARE ELAALEILAD ACARHGALLA VNDRADVALA AGADVLHLGQ DDLPVEWARR VVGDDVVVGR SAHSADETAT AAAEPGVDYF CAGPCWPTPT KPGRPAPGLG LVRTVADRKP ERPWFAIGGI DHDRLDEVLA AGAERIVVVR VLTEAEDPRA AAQSLSSRLR G // ID F4D594_HELPX Unreviewed; 223 AA. AC F4D594; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0462_0564; OS Helicobacter pylori 83. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=585538; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=83; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002605; AEE70169.1; -; Genomic_DNA. DR RefSeq; YP_005785131.1; NC_017375.1. DR EnsemblBacteria; AEE70169; AEE70169; HMPREF0462_0564. DR GeneID; 12365350; -. DR KEGG; hpx:HMPREF0462_0564; -. DR PATRIC; 54110309; VBIHelPyl75410_0578. DR KO; K00788; -. DR BioCyc; HPYL585538:GLE6-577-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 52 56 HMP-PP binding (By similarity). FT REGION 154 156 THZ-P binding (By similarity). FT REGION 203 204 THZ-P binding (By similarity). FT METAL 89 89 Magnesium (By similarity). FT METAL 108 108 Magnesium (By similarity). FT BINDING 88 88 HMP-PP (By similarity). FT BINDING 127 127 HMP-PP (By similarity). FT BINDING 157 157 HMP-PP (By similarity). FT BINDING 185 185 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24479 MW; F360DC8069C90E7B CRC64; MLKSLFDANC LKLMFVAGSQ DFYHIKGGKN DRINALLDAL ELALQSKITA FQFRQKGDLA LQDPIEIKQL ALKCQKLCQK YGTPFIVNDE VQLALELKAD GVHVGQEDMA IEEVMILCKK RFFIGLSVNT LEQALKVRHL DGVAYFGVGP IFPTQSKKDK QVVGVELLKK IKDSGVKKPL VAIGGITTHN ASKLREYGGI AVISAIAQAK DKALAVEKLL KNA // ID F4DE00_AERVB Unreviewed; 520 AA. AC F4DE00; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=B565_3624; OS Aeromonas veronii (strain B565). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=998088; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B565; RX PubMed=21551296; DOI=10.1128/JB.00347-11; RA Li Y., Liu Y., Zhou Z., Huang H., Ren Y., Zhang Y., Li G., Zhou Z., RA Wang L.; RT "Complete genome sequence of Aeromonas veronii strain B565."; RL J. Bacteriol. 193:3389-3390(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002607; AEB51659.1; -; Genomic_DNA. DR RefSeq; YP_004394276.1; NC_015424.1. DR EnsemblBacteria; AEB51659; AEB51659; B565_3624. DR GeneID; 10489541; -. DR KEGG; avr:B565_3624; -. DR PATRIC; 54540123; VBIAerVer186715_3662. DR KO; K14153; -. DR BioCyc; AVER998088:GHKF-3738-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 520 AA; 55312 MW; AA5B4F7F7F1A71F2 CRC64; MTDSRPVVWT IAGSDSGGGA GIQADLHTLH DLGVHGCSVI SAITAQNSVA VKMVDPVLMQ TFTAQIDALG VDLPPAAIKI GLLPTRLHVE VLARRLAAIE APFVVYDPVA IASTGTPMAE PNMLEAVREQ LLQRLSLITP NGPELEALTG IPATSPVLVR FAAQRLRELG ARAVLVKGGH LAWSGELCLD YYQDETREFW LAAPRLNTRH GHGTGCCYAS AIAAVVAQDY PVEDAITLAR AYLQQGLAAA QGVGAGPGPI AHLGWPADLA HFPRAVLAGS TLDRRFGLYE PSSARLPEGP FAATEQHLGL YPVVDSVKWL RRLLGQGVKT IQLRIKNLPA AEVAPAIRDA VALGRRHGAR LFINDYWQQA IEAGAWGVHL GQEDMETADL AAIQGAGLRL GISTHGYFEL MRARELAPSY MALGHIFPTN TKAMPSRPQG LVRLHRYRAL MCDWPTVAIG GISEDRVAAV KASGVGSIAL VSAITASDDW QGATERLLAA VGAGDEPRSA TVIREAEHAL // ID F4DS32_PSEMN Unreviewed; 312 AA. AC F4DS32; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 13-NOV-2013, entry version 19. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=MDS_1022; OS Pseudomonas mendocina (strain NK-01). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1001585; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NK-01; RX PubMed=21551299; DOI=10.1128/JB.05068-11; RA Guo W., Wang Y., Song C., Yang C., Li Q., Li B., Su W., Sun X., RA Song D., Yang X., Wang S.; RT "Complete genome of Pseudomonas mendocina NK-01, which synthesizes RT medium-chain-length polyhydroxyalkanoates and alginate RT oligosaccharides."; RL J. Bacteriol. 193:3413-3414(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002620; AEB57053.1; -; Genomic_DNA. DR RefSeq; YP_004378805.1; NC_015410.1. DR ProteinModelPortal; F4DS32; -. DR EnsemblBacteria; AEB57053; AEB57053; MDS_1022. DR GeneID; 10455804; -. DR KEGG; pmk:MDS_1022; -. DR PATRIC; 54482601; VBIPseMen187712_1042. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; PMEN1001585:GIWS-1028-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 312 AA; 34090 MW; C963C7352AE20B60 CRC64; MKRVHVAAAV IRGVDGRILI ARRPEDKHQG GLWEFPGGKV EEGEAVRVAL DRELQEELGI RPQAARALIQ IRHDYPDKQV LLDVWEVLTF SGEPHGAEGQ PLAWVSERQL PEYEFPAANK PIVAAARLPD RYLITPDGLE PSELLAGIRS ALAQGGRLIQ LRAPNMFDPQ YRDLAVDVQG LCAGKAQLML KGPLEWLGDF PAAGWHLTAE QLRKHAAGGR PFPEHRWLAA SCHSAEELAL AAQMGVDFVT LSPVQATATH PEALPLGWEA ASEMLTHFNL PAYLLGGIGP ADIERAWQIG AQGVAGIRAF WP // ID F4DXP7_PSEMN Unreviewed; 208 AA. AC F4DXP7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MDS_4078; OS Pseudomonas mendocina (strain NK-01). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1001585; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NK-01; RX PubMed=21551299; DOI=10.1128/JB.05068-11; RA Guo W., Wang Y., Song C., Yang C., Li Q., Li B., Su W., Sun X., RA Song D., Yang X., Wang S.; RT "Complete genome of Pseudomonas mendocina NK-01, which synthesizes RT medium-chain-length polyhydroxyalkanoates and alginate RT oligosaccharides."; RL J. Bacteriol. 193:3413-3414(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002620; AEB60109.1; -; Genomic_DNA. DR RefSeq; YP_004381861.1; NC_015410.1. DR EnsemblBacteria; AEB60109; AEB60109; MDS_4078. DR GeneID; 10458860; -. DR KEGG; pmk:MDS_4078; -. DR PATRIC; 54488971; VBIPseMen187712_4146. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR BioCyc; PMEN1001585:GIWS-4138-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21711 MW; 3FF50FA7CD29D95F CRC64; MTSLRGLYAI TDTPLLAGGK LLPYAEAALI GGARLLQYRD KSGDAVRRFD EAQALAELCR RHGATLIIND DLELAARLGV GLHLGQTDGS LAAARARLGS EAVIGGTCHA QLELAERAVA EGASYIAFGR FFNSNTKPGA PAATVELLDQ ARTRFAQPIV AIGGVTLETA PGLIARGASM IAVIHALFAA DSALEVQDRA RAFAALFD // ID F4E6F6_BACAM Unreviewed; 205 AA. AC F4E6F6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-APR-2014, entry version 19. DE SubName: Full=Transcriptional regulator TenI; GN Name=tenI; ORFNames=BAMTA208_11770; OS Bacillus amyloliquefaciens TA208. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=999891; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA208; RX PubMed=21515778; DOI=10.1128/JB.00440-11; RA Zhang G., Deng A., Xu Q., Liang Y., Chen N., Wen T.; RT "Complete genome sequence of Bacillus amyloliquefaciens TA208, a RT strain for industrial production of guanosine and ribavirin."; RL J. Bacteriol. 193:3142-3143(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002627; AEB24519.1; -; Genomic_DNA. DR RefSeq; YP_005542012.1; NC_017188.1. DR EnsemblBacteria; AEB24519; AEB24519; BAMTA208_11770. DR GeneID; 12130616; -. DR KEGG; baz:BAMTA208_11770; -. DR PATRIC; 54308440; VBIBacAmy189468_2339. DR KO; K10810; -. DR BioCyc; BAMY999891:GL8G-2382-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 22628 MW; 4FAA6755F0DD266E CRC64; MELHAVTDNR KPVAELAEDI LSIQHEVSFI HIRERDKTAG EIMQLLALLK KGGADKDKLV INDRADVALF ANIHRVQLPA RSFSVKQVRN RFPHLHIGRS VHSLKEAVQA EKEDADYVVF GHVFETECKQ GLEARGISLL SDIKSTLSIP VIAIGGVTLQ TIGKAKQAKP DGIAVMSGIF SAENPEEAAK RYARAIREAD YEEAL // ID F4EAZ3_BACAM Unreviewed; 222 AA. AC F4EAZ3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-APR-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BAMTA208_19395; OS Bacillus amyloliquefaciens TA208. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=999891; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA208; RX PubMed=21515778; DOI=10.1128/JB.00440-11; RA Zhang G., Deng A., Xu Q., Liang Y., Chen N., Wen T.; RT "Complete genome sequence of Bacillus amyloliquefaciens TA208, a RT strain for industrial production of guanosine and ribavirin."; RL J. Bacteriol. 193:3142-3143(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002627; AEB26027.1; -; Genomic_DNA. DR RefSeq; YP_005543520.1; NC_017188.1. DR EnsemblBacteria; AEB26027; AEB26027; BAMTA208_19395. DR GeneID; 12133058; -. DR KEGG; baz:BAMTA208_19395; -. DR PATRIC; 54311594; VBIBacAmy189468_3872. DR KO; K00788; -. DR BioCyc; BAMY999891:GL8G-3919-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23553 MW; 3A14191D1C159089 CRC64; MTRISREMMK DILSVYFIMG SNNTSADPVS VVKKAIEGGA TLFQFREKGS GSLTGEDLVL FAKQVQDVCR RAGIPFIIND DVELALRLEA DGVHIGQDDA DAEETRAAIG DMILGVSAHN VSEVKLAEAA GADYVGMGPV YPTETKKDAE AVQGVTLIEE VRRQGITIPI VGIGGITADN AAPVIEAGAD GVSMISAISQ AEDPKAAARR FFEEVRRSKA KS // ID F4EQD7_BACAM Unreviewed; 205 AA. AC F4EQD7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-APR-2014, entry version 20. DE SubName: Full=Inhibitor of thiaminase TenA; GN Name=tenI; ORFNames=LL3_01247; OS Bacillus amyloliquefaciens LL3. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1001582; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LL3; RX PubMed=21551302; DOI=10.1128/JB.05058-11; RA Geng W., Cao M., Song C., Xie H., Liu L., Yang C., Feng J., Zhang W., RA Jin Y., Du Y., Wang S.; RT "Complete Genome Sequence of Bacillus amyloliquefaciens LL3, Which RT Exhibits Glutamic Acid-Independent Production of Poly-{gamma}-Glutamic RT Acid."; RL J. Bacteriol. 193:3393-3394(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002634; AEB62789.1; -; Genomic_DNA. DR RefSeq; YP_005545017.1; NC_017190.1. DR EnsemblBacteria; AEB62789; AEB62789; LL3_01247. DR GeneID; 12201629; -. DR KEGG; bql:LL3_01247; -. DR PATRIC; 54314744; VBIBacAmy188832_1231. DR KO; K10810; -. DR BioCyc; BAMY1001582:GL8C-1305-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 22628 MW; 4FAA6755F0DD266E CRC64; MELHAVTDNR KPVAELAEDI LSIQHEVSFI HIRERDKTAG EIMQLLALLK KGGADKDKLV INDRADVALF ANIHRVQLPA RSFSVKQVRN RFPHLHIGRS VHSLKEAVQA EKEDADYVVF GHVFETECKQ GLEARGISLL SDIKSTLSIP VIAIGGVTLQ TIGKAKQAKP DGIAVMSGIF SAENPEEAAK RYARAIREAD YEEAL // ID F4ESQ6_BACAM Unreviewed; 222 AA. AC F4ESQ6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-APR-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LL3_03979; OS Bacillus amyloliquefaciens LL3. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1001582; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LL3; RX PubMed=21551302; DOI=10.1128/JB.05058-11; RA Geng W., Cao M., Song C., Xie H., Liu L., Yang C., Feng J., Zhang W., RA Jin Y., Du Y., Wang S.; RT "Complete Genome Sequence of Bacillus amyloliquefaciens LL3, Which RT Exhibits Glutamic Acid-Independent Production of Poly-{gamma}-Glutamic RT Acid."; RL J. Bacteriol. 193:3393-3394(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002634; AEB65504.1; -; Genomic_DNA. DR RefSeq; YP_005547732.1; NC_017190.1. DR EnsemblBacteria; AEB65504; AEB65504; LL3_03979. DR GeneID; 12203713; -. DR KEGG; bql:LL3_03979; -. DR PATRIC; 54320249; VBIBacAmy188832_3920. DR KO; K00788; -. DR BioCyc; BAMY1001582:GL8C-4069-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23553 MW; 3A14191D1C159089 CRC64; MTRISREMMK DILSVYFIMG SNNTSADPVS VVKKAIEGGA TLFQFREKGS GSLTGEDLVL FAKQVQDVCR RAGIPFIIND DVELALRLEA DGVHIGQDDA DAEETRAAIG DMILGVSAHN VSEVKLAEAA GADYVGMGPV YPTETKKDAE AVQGVTLIEE VRRQGITIPI VGIGGITADN AAPVIEAGAD GVSMISAISQ AEDPKAAARR FFEEVRRSKA KS // ID F4EVH4_SELS3 Unreviewed; 240 AA. AC F4EVH4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Selsp_2085; OS Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=546271; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35185 / DSM 20758 / VPI D19B-28; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., RA Wellnitz S., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Selenomonas sputigena DSM 20758."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002637; AEC01032.1; -; Genomic_DNA. DR RefSeq; YP_004414491.1; NC_015437.1. DR EnsemblBacteria; AEC01032; AEC01032; Selsp_2085. DR GeneID; 10498351; -. DR KEGG; ssg:Selsp_2085; -. DR PATRIC; 54553796; VBISelSpu203744_2154. DR BioCyc; SSPU546271:GCBU-2151-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 156 158 THZ-P binding (By similarity). FT REGION 214 215 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 109 109 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 159 159 HMP-PP (By similarity). FT BINDING 194 194 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 240 AA; 24575 MW; 2D54C6FC16EBA958 CRC64; MGFSVSDMTL RSHLAVTAYL VIGPRDTKGR RVGEIVKAAV CAGFTAVQLR AKEESAREQI ALLGEAARAI EAAGAAASVP LLVDDRLDVA LAAREMGVAV AGVHVGQKDV PAHICRRLLG EAAIVGLSAH PQDLPRLAPE DLAAADYIGT GPLHATASKP DAGIEADGSF RTRSLAEIAA FAQKSPVPVI VGGGVKAADL PAIKATGAAG FFVISAVAAA ADAEGAAREM VARWRDEVIF // ID F4FC94_VERMA Unreviewed; 208 AA. AC F4FC94; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=VAB18032_00945; OS Verrucosispora maris (strain AB-18-032). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Verrucosispora. OX NCBI_TaxID=263358; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB-18-032; RX PubMed=21551311; DOI=10.1128/JB.05041-11; RA Roh H., Uguru G.C., Ko H.J., Kim S., Kim B.Y., Goodfellow M., RA Bull A.T., Kim K.H., Bibb M.J., Choi I.G., Stach J.E.; RT "Genome sequence of the abyssomicin- and proximicin-producing marine RT actinomycete Verrucosispora maris AB-18-032."; RL J. Bacteriol. 193:3391-3392(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002638; AEB47273.1; -; Genomic_DNA. DR RefSeq; YP_004407873.1; NC_015434.1. DR EnsemblBacteria; AEB47273; AEB47273; VAB18032_00945. DR GeneID; 10454056; -. DR KEGG; vma:VAB18032_00945; -. DR PATRIC; 54479027; VBIVerMar92278_5352. DR KO; K00788; -. DR BioCyc; VMAR263358:GI1P-5293-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 21672 MW; D30529A3AF53DF23 CRC64; MLLTDRRAAR GDLVGVVAGA VAGGVRWVVL REKDLLREER RALADELQPI LAEAGGNLIV AGPDPLLAIP VPAAGRPLVA LHLSAADPYP PPEADLVGRS CHDEGELSRL TTEDYVTLSP VFPTRSKPGY GPPLRPVGLA RLIRLSPLPA LALGGIEIPA QVRACVQAGA VGVAVLGAIM RSPDPQQTAA ELTSAFEAAP TATVEEDR // ID F4FC98_VERMA Unreviewed; 208 AA. AC F4FC98; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=VAB18032_00965; OS Verrucosispora maris (strain AB-18-032). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Verrucosispora. OX NCBI_TaxID=263358; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB-18-032; RX PubMed=21551311; DOI=10.1128/JB.05041-11; RA Roh H., Uguru G.C., Ko H.J., Kim S., Kim B.Y., Goodfellow M., RA Bull A.T., Kim K.H., Bibb M.J., Choi I.G., Stach J.E.; RT "Genome sequence of the abyssomicin- and proximicin-producing marine RT actinomycete Verrucosispora maris AB-18-032."; RL J. Bacteriol. 193:3391-3392(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002638; AEB47277.1; -; Genomic_DNA. DR RefSeq; YP_004407877.1; NC_015434.1. DR EnsemblBacteria; AEB47277; AEB47277; VAB18032_00965. DR GeneID; 10454060; -. DR KEGG; vma:VAB18032_00965; -. DR PATRIC; 54479035; VBIVerMar92278_5356. DR KO; K00788; -. DR BioCyc; VMAR263358:GI1P-5297-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 20771 MW; CF1A1F916FA1284C CRC64; MPSLGRLHLI TDTRPGRDAL AVLAAALPVA HTELVVQVRV EDTTTDREAY ELTRQVLVLC RPYGVTCLVN DRLHVALAAG ASGGHVGADD LPVATARRVL GPDAVLGATA REPVSAAEAV AAGASYLGVG PCHATTTKDG LPPAIGVAGV RAVVEAVTVP VIAIGGVTAE DVPVLRSAGV YGVAVVGALS GAADPAHAAA EFVDALAC // ID F4FIX2_STAAU Unreviewed; 213 AA. AC F4FIX2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAT0131_02250; OS Staphylococcus aureus subsp. aureus T0131. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1006543; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T0131; RX PubMed=21551295; DOI=10.1128/JB.05135-11; RA Li Y., Cao B., Zhang Y., Zhou J., Yang B., Wang L.; RT "Complete genome sequence of Staphylococcus aureus T0131, an ST239- RT MRSA-SCCmec type III clone isolated in China."; RL J. Bacteriol. 193:3411-3412(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002643; AEB89189.1; -; Genomic_DNA. DR RefSeq; YP_005753355.1; NC_017347.1. DR ProteinModelPortal; F4FIX2; -. DR SMR; F4FIX2; 4-209. DR PRIDE; F4FIX2; -. DR EnsemblBacteria; AEB89189; AEB89189; SAT0131_02250. DR GeneID; 12338159; -. DR KEGG; sut:SAT0131_02250; -. DR PATRIC; 54325152; VBIStaAur188048_2071. DR KO; K00788; -. DR BioCyc; SAUR1006543:GLKS-2125-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F4FRV9_LACBN Unreviewed; 218 AA. AC F4FRV9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Lbuc_0527; OS Lactobacillus buchneri (strain NRRL B-30929). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=511437; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-30929; RX PubMed=21622751; DOI=10.1128/JB.05180-11; RG US DOE Joint Genome Institute; RA Liu S., Leathers T.D., Copeland A., Chertkov O., Goodwin L., RA Mills D.A.; RT "Complete genome sequence of Lactobacillus buchneri NRRL B-30929, a RT novel strain from a commercial ethanol plant."; RL J. Bacteriol. 193:4019-4020(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002652; AEB72793.1; -; Genomic_DNA. DR RefSeq; YP_004397856.1; NC_015428.1. DR EnsemblBacteria; AEB72793; AEB72793; Lbuc_0527. DR GeneID; 10524639; -. DR KEGG; lbh:Lbuc_0527; -. DR PATRIC; 54462105; VBILacBuc105504_0608. DR KO; K00788; -. DR BioCyc; LBUC511437:GJNY-530-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23334 MW; C36E661F3E0DC5BA CRC64; MGMQFEPGML RAYFIAGTQD VKDQTKTLQE IAKQAMEAGI TAFQYREKGP GSLSGAKRDE MAADLREMCS DYEIPFIVDD DVELAVKTNA DGVHVGQKDE RVTKVIEAVG QSMFVGLSCD TKEQVNIANH IDGISYLGSG PVFPTGSKAD ADPVIGVDGL ATLVKASQLP VVAIGGITEQ NIVELPQTGV AGVSVISMIA QSDDIFRTVK VMNETFEK // ID F4FV47_LACBN Unreviewed; 210 AA. AC F4FV47; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Lbuc_2166; OS Lactobacillus buchneri (strain NRRL B-30929). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=511437; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-30929; RX PubMed=21622751; DOI=10.1128/JB.05180-11; RG US DOE Joint Genome Institute; RA Liu S., Leathers T.D., Copeland A., Chertkov O., Goodwin L., RA Mills D.A.; RT "Complete genome sequence of Lactobacillus buchneri NRRL B-30929, a RT novel strain from a commercial ethanol plant."; RL J. Bacteriol. 193:4019-4020(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002652; AEB74409.1; -; Genomic_DNA. DR RefSeq; YP_004399472.1; NC_015428.1. DR ProteinModelPortal; F4FV47; -. DR EnsemblBacteria; AEB74409; AEB74409; Lbuc_2166. DR GeneID; 10526352; -. DR KEGG; lbh:Lbuc_2166; -. DR PATRIC; 54465581; VBILacBuc105504_2264. DR KO; K00788; -. DR BioCyc; LBUC511437:GJNY-2243-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22331 MW; E9F9BE8B47D29FDA CRC64; MKLTNRPLYL VTDHTGLTDE QFFGAIEAGV QNGVGLVQLR QKEGSSREIF ELALKVKAIT DRYKIPLIID DRLDIAQAVD AAGVHLGQSD LPVDIARRIL GPKKIIGATA KTLKQAKAAE EMGADYLGTG AIFPTTTHVK TVHTTVETLG KIKRLVDIPV YAIGGLKADN VEAIDGAHVD GVAVVSAIMK AADPASATRE LRDAVEEAIG // ID F4G7C2_ALIDK Unreviewed; 300 AA. AC F4G7C2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Alide2_3110; OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Alicycliphilus. OX NCBI_TaxID=596154; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14773 / CIP 107495 / K601; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Oosterkamp M., Pieper D., van Berkel W., Langenhoff A., Smidt H., RA Stams A., Woyke T.; RT "Complete sequence of chromosome of Alicycliphilus denitrificans RT K601."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002657; AEB85452.1; -; Genomic_DNA. DR RefSeq; YP_004388968.1; NC_015422.1. DR ProteinModelPortal; F4G7C2; -. DR EnsemblBacteria; AEB85452; AEB85452; Alide2_3110. DR GeneID; 10484161; -. DR KEGG; adk:Alide2_3110; -. DR PATRIC; 54528923; VBIAliDen79014_3137. DR KO; K00788; -. DR BioCyc; ADEN596154:GHU6-3145-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 300 AA; 31738 MW; EB00599BEE43CB1F CRC64; MHESHEAMVQ AIVHHHGAAY ADFPAQPVPA TATDEPVYRA ALAACSALGF IAHDAGCLAR AWAAQTRRLG SFDAARWPDD PADFGLQPRP HARPFAPCPQ QLGLYAVLPD AAWVGRMARA GVPTVQLRYK SQDGAAIARE VQAAVQAVRG TPALLFINDH WRAAIDAGAY GVHLGQEDLD ALGPDDLRAI REAGLRLGVS THGYAEMVRA DAASPSYIAM GAVFPTTLKK MATVPQGVAR LVAYARLMRG YPQVAIGGIG LEQFPQVLAT GVGSIAVVRA LVNADEPEAS AARLMRAMQA // ID F4GR63_PUSST Unreviewed; 323 AA. AC F4GR63; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 19. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=PT7_3413; OS Pusillimonas sp. (strain T7-7). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Pusillimonas. OX NCBI_TaxID=1007105; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T7-7; RX PubMed=21622753; DOI=10.1128/JB.05242-11; RA Cao B., Ma T., Ren Y., Ren Y., Li G., Li P., Guo X., Ding P., Feng L.; RT "Complete genome sequence of Pusillimonas sp. T7-7, a cold-tolerant RT diesel oil-degrading bacterium isolated from the Bohai Sea in China."; RL J. Bacteriol. 193:4021-4022(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T7-7; RA Cao B., Ma T., Li P., Jiang L., Li Y., Guo X., Feng L.; RT "Genome Announcement Complete Genome Sequence of Pusillimonas sp. T7- RT 7, a novel species isolated from the Bohai Sea, China."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002663; AEC21953.1; -; Genomic_DNA. DR RefSeq; YP_004418577.1; NC_015458.1. DR ProteinModelPortal; F4GR63; -. DR EnsemblBacteria; AEC21953; AEC21953; PT7_3413. DR GeneID; 10603665; -. DR KEGG; put:PT7_3413; -. DR PATRIC; 54561100; VBIPusSp189076_3365. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; PSP1007105:GJAF-3463-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 323 AA; 34965 MW; A7BE1D731C7877B3 CRC64; MSKPFIEVAA GLIMQPDGSL LLAQRPADKP WPGWWELPGG KIEPGETTLQ ALARELKEEL DIDVTVATPW VTYTHEYPKN IVRLAFCRVT GWEGEPTGVE GQQLSWVKLD GPLSVGPLLP ATEPPLRWIR LPDRYLLTSI GSNNELSNYL AKLTRALQDG LKLVQFREPG WNAESEQDVY TAFKQIVELC HEYGARCLIN SCHPEAWWTQ ADGVHLRAAD VRNLAAAGAA IKEKAPGLLA VSAHTVADLD AARTLDADFA VLGHVLSTPS HPGEPGMGWA QFASLITDAG LPVFAIGGQS AATLEAARQH GAHGIAGIRQ LLT // ID F4GRV6_PUSST Unreviewed; 216 AA. AC F4GRV6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PT7_3497; OS Pusillimonas sp. (strain T7-7). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Pusillimonas. OX NCBI_TaxID=1007105; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T7-7; RX PubMed=21622753; DOI=10.1128/JB.05242-11; RA Cao B., Ma T., Ren Y., Ren Y., Li G., Li P., Guo X., Ding P., Feng L.; RT "Complete genome sequence of Pusillimonas sp. T7-7, a cold-tolerant RT diesel oil-degrading bacterium isolated from the Bohai Sea in China."; RL J. Bacteriol. 193:4021-4022(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T7-7; RA Cao B., Ma T., Li P., Jiang L., Li Y., Guo X., Feng L.; RT "Genome Announcement Complete Genome Sequence of Pusillimonas sp. T7- RT 7, a novel species isolated from the Bohai Sea, China."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002663; AEC22037.1; -; Genomic_DNA. DR RefSeq; YP_004418661.1; NC_015458.1. DR EnsemblBacteria; AEC22037; AEC22037; PT7_3497. DR GeneID; 10603076; -. DR KEGG; put:PT7_3497; -. DR PATRIC; 54561269; VBIPusSp189076_3448. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; PSP1007105:GJAF-3548-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22861 MW; A3E65692BD692EAF CRC64; MSSSLRFPQG LYGVTPEWDD TDKLIEAITA AANGGMTALQ WRRKTASPEA GLVQARQVVD VCRQLKVVSI VNDDWRLAAL LDADGVHLGR DDGNLAEARL ALGPQKIIGC SCYNQPALAV PALAAGVDYI AFGAMYPSRV KPDAARATLE HIEQGRMLVE NRKERPRAAV VAIGGITADN AGPIIHAGAD SVALISGLFE SGNIQAAATR CKALFD // ID F4H7V4_CELFA Unreviewed; 230 AA. AC F4H7V4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Celf_1656; OS Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 OS / NCIMB 8980 / NCTC 7547). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Cellulomonadaceae; Cellulomonas. OX NCBI_TaxID=590998; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / RC NCTC 7547; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Mead D., Brumm P., Woyke T.; RT "Complete sequence of Cellulomonas fimi ATCC 484."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002666; AEE45788.1; -; Genomic_DNA. DR RefSeq; YP_004453175.1; NC_015514.1. DR EnsemblBacteria; AEE45788; AEE45788; Celf_1656. DR GeneID; 10592433; -. DR KEGG; cfi:Celf_1656; -. DR PATRIC; 54614223; VBICelFim18861_1657. DR KO; K00788; -. DR OMA; AICHAED; -. DR BioCyc; CFIM590998:GJFK-1673-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 22611 MW; 797C500B0EC15D30 CRC64; MSALPGGAYL VLDADTCAAA ARRPADVARA AVDAGVRVLQ VRAKRAPVRD LVALTVEVAQ AVRGSGATLL VDDRVDVALV VRARGVEVDG VHVGQSDLDV ADVRRLLGPD AVVGVSAATP AELARVDAGL VDYVGSGPVR GTPTKPDAGP PLGLDGLRAA VAATTLPVVA IGGLGVADAG AVRQTGAHGL AVVSAVCAAA DPTRAAQDLV DAWGPTPAPV VGAVATGASR // ID F4HD57_GALAU Unreviewed; 221 AA. AC F4HD57; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=UMN179_01807; OS Gallibacterium anatis (strain UMN179) (Pasteurella anatis). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Gallibacterium. OX NCBI_TaxID=1005058; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMN179; RX PubMed=21602325; DOI=10.1128/JB.05177-11; RA Johnson T.J., Fernandez-Alarcon C., Bojesen A.M., Nolan L.K., RA Trampel D.W., Seemann T.; RT "Complete genome sequence of Gallibacterium anatis strain UMN179, RT isolated from a laying hen with peritonitis."; RL J. Bacteriol. 193:3676-3677(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002667; AEC17822.1; -; Genomic_DNA. DR RefSeq; YP_004420719.1; NC_015460.1. DR EnsemblBacteria; AEC17822; AEC17822; UMN179_01807. DR GeneID; 10565072; -. DR KEGG; gan:UMN179_01807; -. DR PATRIC; 54565542; VBIGalAna187837_1798. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; GANA1005058:GHKG-1860-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 202 203 THZ-P binding (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 24286 MW; 83A9D0A35844F21F CRC64; MDKSILRCYL VAGTQDCRHL SQYDASQPQQ TLLDRLEQAL KAGITCYQFR EKGQFSLQDP QQIEQLAHQC QHLCQQYNVP FIINNDVQLA EKLHADGIHV GQKDFAVDKL AQQIQGKMLI GLSVNTLPQA KQHNAFNGVD YYGCGPIFPT FSKADAAPDV GINFVQFLRE QGINKPLVAI GGIRTEHVPA LLQAGADGVA VISTIMQSAN ITATVKQILN A // ID F4HKS0_PYRSN Unreviewed; 207 AA. AC F4HKS0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PNA2_1765; OS Pyrococcus sp. (strain NA2). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=342949; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NA2; RX PubMed=21602357; DOI=10.1128/JB.05150-11; RA Lee H.S., Bae S.S., Kim M.S., Kwon K.K., Kang S.G., Lee J.H.; RT "Complete genome sequence of hyperthermophilic Pyrococcus sp. strain RT NA2, isolated from a deep-sea hydrothermal vent area."; RL J. Bacteriol. 193:3666-3667(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002670; AEC52680.1; -; Genomic_DNA. DR RefSeq; YP_004424684.1; NC_015474.1. DR EnsemblBacteria; AEC52680; AEC52680; PNA2_1765. DR GeneID; 10555255; -. DR KEGG; pyn:PNA2_1765; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; PSP342949:GI74-1802-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22459 MW; 1D7E7D989A60730A CRC64; MGLREKLKLY TITDRRLKPE IESVKQALEG GATAIQLRIK DASTREMYEI GKEIRKLTNE YDALFFVDDR IDVALAVNAD GVQLGPEDMP IEIAREIAPN LIIGASVYSL EEALKAERMG ADYLGAGSVF PTKTKRDVKV IGLDGLKEIV RAVRIPVVAI GGINAGNARD VLLTGVSGIA VISAVMGAED VRRATQELRK IVEEVLG // ID F4KKL6_PORAD Unreviewed; 673 AA. AC F4KKL6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Poras_0998; OS Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / VPI OS 4198) (Bacteroides asaccharolyticus). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=879243; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25260 / DSM 20707 / VPI 4198; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Pagani I., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Porphyromonas asaccharolytica DSM 20707."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002689; AEE12941.1; -; Genomic_DNA. DR RefSeq; YP_004442109.1; NC_015501.1. DR EnsemblBacteria; AEE12941; AEE12941; Poras_0998. DR GeneID; 10575484; -. DR KEGG; pah:Poras_0998; -. DR PATRIC; 54589102; VBIPorAsa172508_0969. DR OMA; WINAIRS; -. DR BioCyc; PASA879243:GJ3V-1031-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 673 AA; 74531 MW; 883440BBF76C8594 CRC64; MIVITPPERQ YIEGLASDII DVASNCICKV HLRIPGASET DFRKVLDSLE PAYHQHIVLC DHYALLAEYD VAGVYLPYRR VAEWRDIPLA PHQTIAVGAH SLQELQELPF TPDYALLSPL FDSISKEGYQ GNSALLSCRE ELLKLPYPVY ALGGITPERQ ETVAKAGYAG VAVLGDIWSQ PQERRQERLD QYQTPAILTV AGHDPTSGAG IGVDTRIAND LSVQCYSVIS TLTAQSLRRF VCATATPSDQ LQTSLTTLLT DHPVTVAKIG MGQNLQQAVQ IVAQMKALGV KRIIWDPILQ PTAAEETQPH LWTEEQDKLA TLLHEVSLVT PNKPETQALF GTDDPTELQR IAQEHGVAIL LKGGHDTTSP HLVVNQLITR DGIYPFYTHR YDKSIHGTGC MLSAAIASYW AMEYSLVNSV QRACHYLTTI FAGQPNRPGR QLLCPKIFRE DRKKQHLYAH FALQYVTNES DPDRLYNKVS QYLEAGGRWV QLRLKEATTE ERIEMGLRLR TLTDRYNACL LINDDIIATI AVDADGVHLG KRDCPPQEAR RTLGNKYIIG YTVNSRDDLP RALAANIDYI GVGPYRDTQT KALLAPILGL EGISQIAQQV QETDRSYTTP LIVAIGGIQP EDAETLLSKE DIDGIAVSGA IEHATDMAHT VSQLQCGTSN YPR // ID F4L9V8_BORPC Unreviewed; 217 AA. AC F4L9V8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BPTD_0311; OS Bordetella pertussis (strain CS). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=1017264; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CS; RX PubMed=21622744; DOI=10.1128/JB.05184-11; RA Zhang S., Xu Y., Zhou Z., Wang S., Yang R., Wang J., Wang L.; RT "Complete genome sequence of B. pertussis CS, Chinese pertussis RT vaccine strain."; RL J. Bacteriol. 193:4017-4018(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CS; RA Zhang S., Xu Y., Zhou Z., Wang S., Yang R., Wang J., Wang L.; RT "Complete genome sequence of B. pertussis CS, Chinese pertussis RT vaccine strain."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002695; AEE65794.1; -; Genomic_DNA. DR RefSeq; YP_005588572.1; NC_017223.1. DR ProteinModelPortal; F4L9V8; -. DR EnsemblBacteria; AEE65794; AEE65794; BPTD_0311. DR GeneID; 12161055; -. DR KEGG; bpc:BPTD_0311; -. DR PATRIC; 54327225; VBIBorPer192275_0334. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; BPER1017264:GL9D-317-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22343 MW; 71DD7E5C67E57EB1 CRC64; MKTLRFPAGL YGITPEWDDT DRLLAAVRAA AAGGMTALQL RRKLADERLR AAQARALAPL CRELGVVFLV NDHWKLALDV GADGAHLGRD DADPATVRAQ AGAGLLLGVS CYNDLRRADA LLAAGADYVA FGTVFASPTK PEAVHAPLQT LTEARARVLA CPAPRPAVVA IGGITPANVS QVAQAGADSA AVISGLFEAP DIQAAARACA AAFSVNP // ID F4LGN5_BORPC Unreviewed; 320 AA. AC F4LGN5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=BPTD_3752; OS Bordetella pertussis (strain CS). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=1017264; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CS; RX PubMed=21622744; DOI=10.1128/JB.05184-11; RA Zhang S., Xu Y., Zhou Z., Wang S., Yang R., Wang J., Wang L.; RT "Complete genome sequence of B. pertussis CS, Chinese pertussis RT vaccine strain."; RL J. Bacteriol. 193:4017-4018(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CS; RA Zhang S., Xu Y., Zhou Z., Wang S., Yang R., Wang J., Wang L.; RT "Complete genome sequence of B. pertussis CS, Chinese pertussis RT vaccine strain."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002695; AEE68921.1; -; Genomic_DNA. DR RefSeq; YP_005591699.1; NC_017223.1. DR ProteinModelPortal; F4LGN5; -. DR EnsemblBacteria; AEE68921; AEE68921; BPTD_3752. DR GeneID; 12162614; -. DR KEGG; bpc:BPTD_3752; -. DR PATRIC; 54334905; VBIBorPer192275_4020. DR KO; K03574; -. DR OMA; CGASCHN; -. DR BioCyc; BPER1017264:GL9D-3811-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 320 AA; 34128 MW; 760C8F90EDF29237 CRC64; MSEKIVDVAA GLILRPDGQL LLGQRPEGKP WAGWWELPGG KLEPGETVLQ ALARELHEEL GIRVTEAHPW VTYVHVYPHT TVRLAFCHVT GWEGEPRGLE NQRLEWVDPA RAHEVGDLLP AALPPLRWLQ LPTAYAISAI GAPAALADFT ARLRQALDGG LKLVLLREPD WPGGADAASL RDAMQAILAQ CRAAGARLLV SSRHPQAWWR EADGVHLTAR DAQALKQRPA LPEGALVGVS AHGHAEIVHA RDLGADFAVL GPVLATASHP EQAPLGWPGF AAGIRDAGMP VYALGGQSPA TLAEARLHGA HGIAGIRGLL // ID F4MC90_ECOLX Unreviewed; 211 AA. AC F4MC90; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=UMNK88_4834; OS Escherichia coli UMNK88. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=696406; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UMNK88; RA Johnson T.J., Shepard S.M., Isaacson R.E.; RT "Genome structure of porcine enterotoxigenic Escherichia coli."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002729; AEE59317.1; -; Genomic_DNA. DR RefSeq; YP_006136480.1; NC_017641.1. DR ProteinModelPortal; F4MC90; -. DR SMR; F4MC90; 20-202. DR EnsemblBacteria; AEE59317; AEE59317; UMNK88_4834. DR GeneID; 12688085; -. DR KEGG; eun:UMNK88_4834; -. DR PATRIC; 48577469; VBIEscCol159162_4723. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; ECOL696406:GJE4-4782-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F4N540_YEREN Unreviewed; 223 AA. AC F4N540; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YEW_AB00210; OS Yersinia enterocolitica W22703. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=913028; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=21453472; DOI=10.1186/1471-2164-12-168; RA Fuchs T.M., Brandt K., Starke M., Rattei T.; RT "Shotgun sequencing of Yersinia enterocolitica strain W22703 (biotype RT 2, serotype O:9): genomic evidence for oscillation between RT invertebrates and mammals."; RL BMC Genomics 12:168-168(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR718720; CBX73198.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24371 MW; 73F1F69E77A483AC CRC64; MKPSDTPIFS AQKGFPTTEQ RLGLYPVVDS VLWIERLLAL GVTTIQLRIK ELDEAQVEQD IVAAIELGKR YQARLFINDY WRLAIKHGAY GVHLGQEDLE STDLAAIQQA GLRLGVSTHD EYELAIAKAV RPSYIAMGHI FPTQTKQMPS SPQGLAVLKQ MVENTPDYPT VAIGGISIER VPAVLATGVG SVAVVSAITQ AEDWQQATAQ LLHLIEGKEL ADE // ID F4NR46_9ENTR Unreviewed; 211 AA. AC F4NR46; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSJG_04678; OS Shigella sp. D9. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=556266; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D9; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Sibley C., White A., Ambrose C., Lander E., Nusbaum C., RA Galagan J., Birren B.; RT "The Genome Sequence of Shigella sp. D9."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657395; EGJ08627.1; -; Genomic_DNA. DR ProteinModelPortal; F4NR46; -. DR SMR; F4NR46; 10-208. DR EnsemblBacteria; EGJ08627; EGJ08627; SSJG_04678. DR PATRIC; 30985221; VBIShiSp107483_4544. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F4PFK0_BATDJ Unreviewed; 193 AA. AC F4PFK0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=BATDEDRAFT_93141; OS Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog OS chytrid fungus). OC Eukaryota; Fungi; Chytridiomycota; Chytridiomycetes; Rhizophydiales; OC Rhizophydiales incertae sedis; Batrachochytrium. OX NCBI_TaxID=684364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JAM81 / FGSC 10211; RG US DOE Joint Genome Institute (JGI-PGF); RA Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E., RA Stajich J., Eisen M., Grigoriev I.V.; RT "The draft genome of Batrachochytrium dendrobatidis."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL882937; EGF75996.1; -; Genomic_DNA. DR RefSeq; XP_006683383.1; XM_006683320.1. DR ProteinModelPortal; F4PFK0; -. DR GeneID; 18244926; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 193 AA; 20658 MW; 609C923930ACDB27 CRC64; MGSQNCKRNP VEIMEEAVKA GINAFQFREK GNGCLTEEAK VELGRQLRAI CHRADIPFIV NDDVKLVKIL DADGIHVGQD DLPVESLRKI FPNKIIGLSV SNESEVANSP IALVDYIGAG PIFDTTTKLD AKATVGLEWI TTLRREFPDL PIVGIGGITI ENAASVIEAG ADGVSVISAI TAAPDIKRAV KLL // ID F4QK01_9CAUL Unreviewed; 215 AA. AC F4QK01; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase/TENI family protein; GN ORFNames=ABI_04610; OS Asticcacaulis biprosthecum C19. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Asticcacaulis. OX NCBI_TaxID=715226; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C19; RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL883077; EGF92028.1; -; Genomic_DNA. DR EnsemblBacteria; EGF92028; EGF92028; ABI_04610. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 215 AA; 23205 MW; B7F5773AB9A05023 CRC64; MTYRTRFQYL FDKATDITQE ARAFLPSDRR LPPLFFVTDP ARTPHPEDIA ALMPAGTGII YRHFGDSHAL QRARLLRRIA DDHGLVLLIG EDDALAIEVG ADGVHLAQKS LPRVAHLHRD HPELKLSIAC HDLDTLMHLA DDAPLQAVFV SPVFASRSTS AQNVAALGAK GVHDYTAATG LPVYGLGGIT CDTIGELRDC GLAGIGAVDA FHIAD // ID F4QP88_9CAUL Unreviewed; 206 AA. AC F4QP88; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ABI_25600; OS Asticcacaulis biprosthecum C19. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Asticcacaulis. OX NCBI_TaxID=715226; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C19; RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL883078; EGF91146.1; -; Genomic_DNA. DR ProteinModelPortal; F4QP88; -. DR EnsemblBacteria; EGF91146; EGF91146; ABI_25600. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21704 MW; 4F9EC1A9586F6F59 CRC64; MDCRLYLITP PQIADAQAFA RDLEAALSAG EVAALQIRLK DTPPDYIRAV TRVLTPIAHA HGVAVLMNDH ADLAKELGLD GVHIGQSDIA FKEARRILGP KAMIGVTCHN SRHLAMDAAD AGADYVAFGA FYPTQTKTVE HMAELETLTI WQESMEAPCV AIGGITADNA REVAEAGADF IAVSGAVWNH PDGPAAGVKA LLAAIA // ID F4R2F3_BREDI Unreviewed; 219 AA. AC F4R2F3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BDIM_20510; OS Brevundimonas diminuta ATCC 11568. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=751586; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11568; RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.; RT "Draft genome sequence of Brevundimonas diminuta."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL883086; EGF95215.1; -; Genomic_DNA. DR ProteinModelPortal; F4R2F3; -. DR EnsemblBacteria; EGF95215; EGF95215; BDIM_20510. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22947 MW; 78534AE796816EE7 CRC64; MARQPQIPAR PACRLYLITP TAIPDLEAFA AELEAALAAG DCAALQIRLK AASDEEIRAA VARLKPICQA HDVALILNDR PDLARATGCD GVHVGQEDAS LAEARRIMGE GAMIGVTCHD SRHLAMEAAE GGADYVAFGA FFPTQTKDVA HHAEPEILTI WQETMEVPCV AIGGVTVENA GAIAAAGADF VAVSAGVWRH PDGPAAAVRA FDEALRTAY // ID F4RNQ6_MELLP Unreviewed; 579 AA. AC F4RNQ6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-APR-2014, entry version 15. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=MELLADRAFT_63716; OS Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar OS leaf rust fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; OC Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora. OX NCBI_TaxID=747676; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=98AG31 / pathotype 3-4-7; RX PubMed=21536894; DOI=10.1073/pnas.1019315108; RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E., RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., RA Cantarel B.L., Chiu R., Coutinho P.M., Feau N., Field M., Frey P., RA Gelhaye E., Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., RA Kuees U., Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., RA Murat C., Pangilinan J.L., Park R., Pearson M., Quesneville H., RA Rouhier N., Sakthikumar S., Salamov A.A., Schmutz J., Selles B., RA Shapiro H., Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., RA Rouze P., Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C., RA Grigoriev I.V., Szabo L.J., Martin F.; RT "Obligate biotrophy features unraveled by the genomic analysis of rust RT fungi."; RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL883110; EGG06030.1; -; Genomic_DNA. DR EnsemblFungi; EGG06030; EGG06030; MELLADRAFT_63716. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 579 AA; 62894 MW; 633627B7D371007F CRC64; MSKQKTRPQL DLTLYLVTSS DNLAPGSTIE STVQSAILGG VTIVQLREKE LGTREFLKLA ISLRNICHQA IPKVTFIVND RIDIALASDA DGVHLGQDDM PIEEARKWLG PNAVIGISTN TIEEAIDAVE RKADYLGIGT CWPTGTKVIP DHKIIGEHYH QEATLDRFDY KTLMTFFDTR STGPRGVKKI RDELTLRGLK IPAVTIGGIK WENVTRTLYG CVSTAPSGAL DPIEGIAVVS AIMSSDQPQV EARRLRQTLD KHNIALESFS SRQSKPSILS SQGTDSYSEY LSSVIAFKCA HDCRQLIHHI TNTVVQNDCA NLTLALRCSP MMSSSIEEVE ELVETCSDSL VINLGTLDQT QIMAMKLAGR QANLAYKPVV FDPVGVGASQ FRQKVTDELL NYVQMSYIKG NEGEIASLAN HSAASSHGVD SKGSLPDPAR VVRDLARKER CVVIMTGKVD YVSDGMHVIK LENGVKMLAS ITGSGCMVGT AIGCFASITN AMRKGKLAVP FTNLIDFETR MLDAAICGVS SVNIAAELAI SHSNVTGPNS FRAALIDEVY HLTPEKIKSM IKISEVVVD // ID F4SS49_ECOLX Unreviewed; 212 AA. AC F4SS49; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECHG_04637; OS Escherichia coli H736. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656414; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H736; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli H736."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL883799; EGI08266.1; -; Genomic_DNA. DR EnsemblBacteria; EGI08266; EGI08266; ECHG_04637. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23146 MW; 1A81B1DDC0972FAF CRC64; MMYQPDFPPV PFRSGLYPVV DSVQWIERLL DAGVRTLQLR IKDRRDEEVE ADVVAAIALG RRYNARLFIN DYWRLAIKHQ AYGVHLGQED LQATDLNAIR AAGLRLGVST HDDMEIDVAL AARPSYIALG HVFPTQTKQM PSAPQGLEQL ARHVERLADY PTVAIGGISL ARAPAVIATG VGSIAVVSAI TQAADWRLAT AQLLEIAGVG DE // ID F4T6M6_ECOLX Unreviewed; 212 AA. AC F4T6M6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECIG_05407; OS Escherichia coli M605. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656417; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M605; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli M605."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL883926; EGI13464.1; -; Genomic_DNA. DR EnsemblBacteria; EGI13464; EGI13464; ECIG_05407. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23139 MW; 5CD2B0AB56C15E92 CRC64; MMYQPEFPPV PFRLGLYPVV DSVQWIERLL DAGVRTLQLR IKDQRDEEVE ADVVAAIALG RRYNARLFIN DYWRLAIKHQ AYGVHLGQED LQATDLNAIR AAGLRLGVST HDDMEIDVAL AARPSYIALG HVFPTQTKQM PSAPQGLEQL ARHVERLADY PTVAIGGISL AHAPAVIATG VGSIAVVSAI TQAADWRLAT AQLLEIAGVG DE // ID F4TN35_ECOLX Unreviewed; 212 AA. AC F4TN35; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECJG_05293; OS Escherichia coli M718. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656419; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M718; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli M718."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL884140; EGI18705.1; -; Genomic_DNA. DR ProteinModelPortal; F4TN35; -. DR EnsemblBacteria; EGI18705; EGI18705; ECJG_05293. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23173 MW; D75803DAB38F868E CRC64; MMYQPDFPPV PFRLGLYPVV DSVQWIERLL DAGVRTLQLR IKDRRDEEVE ADVVAAIALG RRYNARLFIN DYWRLAIKHQ AYGVHLGQED LQATDLNAIR AAGLRLGVST HDDMEIDVAL AARPSYIALG HVFPTQTKQM PSAPQGLEQL ARHVERLADY PTVAIGGISL ARAPAVIATG VGSIAVVSAI TQAADWRLAT AQLLEIAGVG DE // ID F4U1T8_ECOLX Unreviewed; 211 AA. AC F4U1T8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECKG_05011; OS Escherichia coli TA206. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656440; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA206; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli TA206."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL884197; EGI24374.1; -; Genomic_DNA. DR ProteinModelPortal; F4U1T8; -. DR SMR; F4U1T8; 9-208. DR EnsemblBacteria; EGI24374; EGI24374; ECKG_05011. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F4UG96_ECOLX Unreviewed; 211 AA. AC F4UG96; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECMG_04652; OS Escherichia coli TA143. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656437; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA143; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli TA143."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL884234; EGI29158.1; -; Genomic_DNA. DR EnsemblBacteria; EGI29158; EGI29158; ECMG_04652. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23034 MW; 4EC571B19EAAAE13 CRC64; MYQPDFPPVP FRLGLYPVVD SAQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAITLGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVMATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F4UVY4_ECOLX Unreviewed; 211 AA. AC F4UVY4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECLG_04913; OS Escherichia coli TA271. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656443; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA271; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli TA271."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL884295; EGI33859.1; -; Genomic_DNA. DR ProteinModelPortal; F4UVY4; -. DR SMR; F4UVY4; 11-208. DR EnsemblBacteria; EGI33859; EGI33859; ECLG_04913. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23027 MW; 0AE827392C8C3853 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGVSLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F4V8Y0_ECOLX Unreviewed; 212 AA. AC F4V8Y0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECNG_05142; OS Escherichia coli TA280. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656444; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA280; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli TA280."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL884381; EGI38763.1; -; Genomic_DNA. DR EnsemblBacteria; EGI38763; EGI38763; ECNG_05142. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23055 MW; 26C0545C12322AF6 CRC64; MMYQPDFPPV PFHLGLYPVV DSVQWIERLL DAGVLTLQLR IKDRRDEEAE ADVVAAIALG RRYNARLFIN DYWRLAIKHQ AYGVHLGQED LQATDLSAIR AAGLRLGVST HDDMEIDVAL AARPSYIALG HVFPTQTKQM PSAPQGLEQL ARHVERLADY PTVAIGGISL ARAPAVIATG VGSIAVVSAI TQAADWRLAT AQLLEIAGVG DE // ID F4VLX9_ECOLX Unreviewed; 212 AA. AC F4VLX9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECPG_04922; OS Escherichia coli H591. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656408; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H591; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli H591."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL884469; EGI43605.1; -; Genomic_DNA. DR EnsemblBacteria; EGI43605; EGI43605; ECPG_04922. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23132 MW; 1A81B1DDD9BF8D3C CRC64; MMYQPDFPPV PFRSGLYPVV DSVQWIERLL DAGVRTLQLR IKDRRDEEVE ADVVAAIALG RRYNARLFIN DYWRLAIKHQ AYGVHLGQED LQATDLNAIR AAGLRLGVST HDDMEIDVAL AARPSYIALG HVFPTQTKQM PSAPQGLEQL ARHVERLADY PTVAIGGVSL ARAPAVIATG VGSIAVVSAI TQAADWRLAT AQLLEIAGVG DE // ID F4W2R9_ECOLX Unreviewed; 211 AA. AC F4W2R9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECOG_05364; OS Escherichia coli H299. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656393; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H299; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli H299."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL884548; EGI48261.1; -; Genomic_DNA. DR EnsemblBacteria; EGI48261; EGI48261; ECOG_05364. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23058 MW; 5AE162224E93EC1B CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLP RAPAVMATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F4XQJ3_9CYAN Unreviewed; 360 AA. AC F4XQJ3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LYNGBM3L_52270; OS Moorea producens 3L. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Moorea. OX NCBI_TaxID=489825; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3L; RA Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., RA Esquenazi E., Niessen S., Hoover H., Rothmann M., Lasken R.S., RA Yates J.R.III., Reinhardt R., Kube M., Burkart M.D., Allen E.E., RA Dorrestein P.C., Gerwick W.H., Gerwick L.; RT "Genomic insights into the physiology and ecology of the marine RT filamentous cyanobacterium Lyngbya majuscula."; RL Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL890871; EGJ33117.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ33117; EGJ33117; LYNGBM3L_52270. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 129 Unknown (By similarity). FT REGION 130 360 Thiamine-phosphate synthase (By FT similarity). FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 360 AA; 40431 MW; 2E302807F0112789 CRC64; MDDQHSGIMG QKSAICRILD ANLDRAREGL RIIEEWCRFG LNSAQMAGEC KEMRQELARW HSSEIRIFRD TSGDPGTGLT HPQEERRSSI QQLLQANLCR VQEALRVLEE YGKLYDAQMG IAFKQMRYRV YSLESHLLGY QRHQLLERSH LYLITSLSDQ WFAKVEAALQ GGLTLVQYRE KQADDGDRLA DAQKLCQLCH HYGALFIMND RVDLALAVEA DGVHIGQQDV PISLARQLLG SQRIIGCSTT NPDELHRAIA EGADYIGVGP VYETPTKPSK PAAGLDYVKY AKEHATIPWF AIGGIDPNNL NYVLDAGAQR VAVVRGIMEA EQPTLVTQYF LSQLKREHTL RSLEAGVSKP // ID F5HHV1_CRYNB Unreviewed; 555 AA. AC F5HHV1; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 16-APR-2014, entry version 15. DE SubName: Full=Putative uncharacterized protein; GN OrderedLocusNames=CNBH3540; OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OS (Filobasidiella neoformans). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Tremellomycetes; Tremellales; Tremellaceae; Filobasidiella; OC Filobasidiella/Cryptococcus neoformans species complex. OX NCBI_TaxID=283643; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B-3501A; RX PubMed=15653466; DOI=10.1126/science.1103773; RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., RA D'Souza C.A., Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., RA Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., RA Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., RA Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., RA Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., RA Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., RA Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., RA Fraser C.M., Hyman R.W.; RT "The genome of the basidiomycetous yeast and human pathogen RT Cryptococcus neoformans."; RL Science 307:1321-1324(2005). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEY01000042; EAL19255.1; -; Genomic_DNA. DR RefSeq; XP_773902.1; XM_768809.1. DR ProteinModelPortal; F5HHV1; -. DR GeneID; 4937881; -. DR KEGG; cnb:CNBH3540; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 555 AA; 59219 MW; 012F5FD0ECE906DF CRC64; MPKPTLDYSL YLVTGRELLP PGKDYYESLE ESLQGGVTLV QVREKYADTG EFIEVARRTK AICDKYNVPV LINDRIDVHL AVGTAGIHVG QTDCPIGLAR SLVGPDAIIG LSVSNVNEAK RAIQQGADYV GIGAVWPTNS KDVANKKMLG PDGVGEILDL LHGTGVQSVA IGGIHLPNVA QLLHASIAPQ SRNALDGIAI ISDIVASLTP REAATNLREV VQSFKRARSQ LSNLEAVYGT NLFSGPRGVD GFIKEAVHLM DVIKRETPLI NQMTNNVVIN DSANVTLAIG ASPIMATHPR DVHDLSPAIG ALLINFGYDS YQCSFKSLML MLESSTITDK AGMLVAGRQA NINRKPIIFD PVAIGATPYR QETSVELLSH WQPTIIKGNA GEIGFMARST EVASRGVDSV GSGFSRPGAV VKALARKQAA IIVLTGEHDY ISDGSTTLKI SNGHHYLERI TGSGCQLGSV IASFAATARL EHLAKHGEWE NASQLVQGDM LAAAVTGVLV YTIAAEVAAA REDVKGPGTF RAALIDELYN LTPEVLQQRA KVEIL // ID F5HUB2_ACIBA Unreviewed; 299 AA. AC F5HUB2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0021_00329; OS Acinetobacter baumannii 6013150. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=525243; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6013150; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYQ02000007; EGJ62021.1; -; Genomic_DNA. DR ProteinModelPortal; F5HUB2; -. DR EnsemblBacteria; EGJ62021; EGJ62021; HMPREF0021_00329. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 299 AA; 34203 MW; F41A81BC493DC0A4 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLNPELK KKIKTVHLKQ SQLMSLHKGD LEVGVRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID F5I4P2_ACIBA Unreviewed; 203 AA. AC F5I4P2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0021_03939; OS Acinetobacter baumannii 6013150. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=525243; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6013150; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYQ02000210; EGJ58367.1; -; Genomic_DNA. DR ProteinModelPortal; F5I4P2; -. DR EnsemblBacteria; EGJ58367; EGJ58367; HMPREF0021_03939. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21750 MW; C30389C3887A22BE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKVD KADQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAK LFS // ID F5IC49_ACIBA Unreviewed; 203 AA. AC F5IC49; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0020_02596; OS Acinetobacter baumannii 6013113. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=592014; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6013113; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYR02000178; EGJ63726.1; -; Genomic_DNA. DR ProteinModelPortal; F5IC49; -. DR EnsemblBacteria; EGJ63726; EGJ63726; HMPREF0020_02596. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21750 MW; C30389C3887A22BE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKVD KADQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAK LFS // ID F5IFZ9_ACIBA Unreviewed; 299 AA. AC F5IFZ9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0020_03959; OS Acinetobacter baumannii 6013113. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=592014; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6013113; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYR02000228; EGJ62404.1; -; Genomic_DNA. DR ProteinModelPortal; F5IFZ9; -. DR EnsemblBacteria; EGJ62404; EGJ62404; HMPREF0020_03959. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 299 AA; 34203 MW; F41A81BC493DC0A4 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLNPELK KKIKTVHLKQ SQLMSLHKGD LEVGVRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID F5IMP1_ACIBA Unreviewed; 203 AA. AC F5IMP1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0022_02264; OS Acinetobacter baumannii 6014059. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=525242; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6014059; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYS02000104; EGJ67991.1; -; Genomic_DNA. DR ProteinModelPortal; F5IMP1; -. DR EnsemblBacteria; EGJ67991; EGJ67991; HMPREF0022_02264. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21778 MW; F47FCEF0DAC9A9AE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKID KAEQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID F5INQ5_ACIBA Unreviewed; 299 AA. AC F5INQ5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0022_02639; OS Acinetobacter baumannii 6014059. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=525242; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6014059; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYS02000141; EGJ67612.1; -; Genomic_DNA. DR ProteinModelPortal; F5INQ5; -. DR EnsemblBacteria; EGJ67612; EGJ67612; HMPREF0022_02639. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 299 AA; 34203 MW; 49BD9DC168F2FC57 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLNPELK KQIKTVHLKQ SQLMSLHKGD LEVGVRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID F5IZX1_9PORP Unreviewed; 212 AA. AC F5IZX1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9455_02638; OS Dysgonomonas gadei ATCC BAA-286. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Dysgonomonas. OX NCBI_TaxID=742766; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-286; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Dysgonomonas gadei ATCC BAA-286."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLV01000031; EGK01116.1; -; Genomic_DNA. DR ProteinModelPortal; F5IZX1; -. DR EnsemblBacteria; EGK01116; EGK01116; HMPREF9455_02638. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22536 MW; E19EE8026F55623E CRC64; MAAFDLSLYL VTDRSLSLGR PLETVVEEAV RGGVTMVQLR EKDASTLDFY NLAMKLKSIL KSYNVPLIIN DRLDIALACD AGGLHIGQSD MPYSVARKLL GKDKIIGLSV ESIQDAIDAN NLDVDYIGIS PVFGTQTKTD TAPALGLEGI GEITRISGHP SVGIGGINLT NAQDIIQAGA DGISVVSAIM SAPDPQQSAR QLKEIINKSK NK // ID F5JFU5_9RHIZ Unreviewed; 221 AA. AC F5JFU5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AGRO_4043; OS Agrobacterium sp. ATCC 31749. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=82789; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 31749; RX PubMed=21685288; DOI=10.1128/JB.05302-11; RA Ruffing A.M., Castro-Melchor M., Hu W.S., Chen R.R.; RT "Genome sequence of the curdlan-producing Agrobacterium sp. strain RT ATCC 31749."; RL J. Bacteriol. 193:4294-4295(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECL01000053; EGL63234.1; -; Genomic_DNA. DR EnsemblBacteria; EGL63234; EGL63234; AGRO_4043. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23276 MW; 775526AE2B7ABFFC CRC64; MDETMSIVED RCRLVLIVPQ RDDAQKQVTE VEDALRGGDV ASVIIPQYGL DDAAFQKWAE LIVPIVQAAG AAALIAGDSR TASRVKADGL HVGGNAEALA EAVENFTPKL IVGGGNADDR HKALEMGESN PDYVFFGKLE GDIKPEAHPK NLALGEWWAS MIEIPAIVMG GTDTSSVVAV SETGVEFVAM RSGVFDNASG AAQAVSEINA LLDEKAPRFG G // ID F5JG79_9RHIZ Unreviewed; 225 AA. AC F5JG79; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AGRO_4181; OS Agrobacterium sp. ATCC 31749. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=82789; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 31749; RX PubMed=21685288; DOI=10.1128/JB.05302-11; RA Ruffing A.M., Castro-Melchor M., Hu W.S., Chen R.R.; RT "Genome sequence of the curdlan-producing Agrobacterium sp. strain RT ATCC 31749."; RL J. Bacteriol. 193:4294-4295(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECL01000057; EGL63213.1; -; Genomic_DNA. DR ProteinModelPortal; F5JG79; -. DR EnsemblBacteria; EGL63213; EGL63213; AGRO_4181. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 23399 MW; 5295B1F1EA24A429 CRC64; MRGSSMNKVD YRLNALVDAS LADVAPLPEL ALAAALNGAT ILQYRDKHGS TREMIENARA IREAIGGTGV PLVINDRVDV ALASGADGVH LGADDMDAKT ARRILGEKAI IGLTVKNRAD AERAASMPAD YACIGGVFET VSKVNPDKPV GIEGFTTLRA LLKEWQPDMP VGAIAGIDLD RVPAVIAAGA DGVAVISAIF RAANIASATS DFRSAIDAAL KARQP // ID F5JKC0_ACIBA Unreviewed; 203 AA. AC F5JKC0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AB210_0109; OS Acinetobacter baumannii AB210. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=886886; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB210; RX PubMed=21565804; DOI=10.1093/jac/dkr168; RA Hornsey M., Loman N., Wareham D.W., Ellington M.J., Pallen M.J., RA Turton J.F., Underwood A., Gaulton T., Thomas C.P., Doumith M., RA Livermore D.M., Woodford N.; RT "Whole-genome comparison of two Acinetobacter baumannii isolates from RT a single patient, where resistance developed during tigecycline RT therapy."; RL J. Antimicrob. Chemother. 66:1499-1503(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEOX01000001; EGK49136.1; -; Genomic_DNA. DR ProteinModelPortal; F5JKC0; -. DR EnsemblBacteria; EGK49136; EGK49136; AB210_0109. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21778 MW; F47FCEF0DAC9A9AE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKID KAEQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID F5JQ58_ACIBA Unreviewed; 299 AA. AC F5JQ58; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=AB210_1795; OS Acinetobacter baumannii AB210. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=886886; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB210; RX PubMed=21565804; DOI=10.1093/jac/dkr168; RA Hornsey M., Loman N., Wareham D.W., Ellington M.J., Pallen M.J., RA Turton J.F., Underwood A., Gaulton T., Thomas C.P., Doumith M., RA Livermore D.M., Woodford N.; RT "Whole-genome comparison of two Acinetobacter baumannii isolates from RT a single patient, where resistance developed during tigecycline RT therapy."; RL J. Antimicrob. Chemother. 66:1499-1503(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEOX01000010; EGK47618.1; -; Genomic_DNA. DR ProteinModelPortal; F5JQ58; -. DR EnsemblBacteria; EGK47618; EGK47618; AB210_1795. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 299 AA; 34203 MW; 49BD9DC168F2FC57 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLNPELK KQIKTVHLKQ SQLMSLHKGD LEVGVRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID F5L0H5_9FIRM Unreviewed; 506 AA. AC F5L0H5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF9323_0011; OS Veillonella parvula ACS-068-V-Sch12. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=768727; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-068-V-Sch12; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXI01000012; EGL77277.1; -; Genomic_DNA. DR EnsemblBacteria; EGL77277; EGL77277; HMPREF9323_0011. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 506 AA; 54282 MW; 1B1596DBDC147CDF CRC64; MTYNNPNING SNWSELNILE SLRKKNPLVI CITNDVVRTF TANGLLAIGA SPVMSECSED LKDLIVHASA LLINIGTVTP DKVTYYKEAV KLAKAHEVPI ILDPVGCHSG AYRLSVVLDL IKTGAISLLR GNQSEIKAIY DALNTNHKID SSLSGKGVDG EQVEDSAIIT YRLARQINCP VVATGEEDYV SDGTRVFAVP HGHSIMTAVT GTGCLLGAVL AAFFSSYYPF MDNLSIGEFL AYALAYYGLA GESAVKVSGV KPGIFSVAFM DALYEFDDAM LLSKNRIRPV VVPDQLKVYF ISGTQDVGFN ERHLLDTVEA ACRGGVTCFQ FREKGIGTLE GQQKLELAQQ LKEICAMYNV LYIINDDVDL AVAVNADGVH VGQEDMRLED VRNLVGNKVV GISIHSVEEL HKTDVVYADC VGVGPMYATS SKPDAQEPCG PDCITELRAE GLTLPCVGIG GITLANATPV LQAGASGVAV ISAIAHADNP YEAAEEFKNL VDKIKI // ID F5L1X0_9FIRM Unreviewed; 215 AA. AC F5L1X0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9323_0931; OS Veillonella parvula ACS-068-V-Sch12. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=768727; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-068-V-Sch12; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXI01000018; EGL76856.1; -; Genomic_DNA. DR ProteinModelPortal; F5L1X0; -. DR EnsemblBacteria; EGL76856; EGL76856; HMPREF9323_0931. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23894 MW; 32DD1D56B30782C4 CRC64; MNRKDKLTEV MNACPIYGIT GGTRDVVPLV KDMLSAGIRI IQYREKGKTP ILRYQEAMIL RRLTSNYHAL LIIDDYVDLA LAVHADGVHI GQADLPPNTV RRIVGPNMLI GWSTHSISDL KVANRYTGVI DYIGVGPIFS TQTKPNANPV GISYIYWAKQ FSKAPIVAIG GIKTTNADTV WQAHPDFICA VSEITESDNI QNTIYELMMG YSRVR // ID F5LAE5_9BACI Unreviewed; 208 AA. AC F5LAE5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CathTA2_2880; OS Caldalkalibacillus thermarum TA2.A1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Caldalkalibacillus. OX NCBI_TaxID=986075; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA2.A1; RX PubMed=21685297; DOI=10.1128/JB.05035-11; RA Kalamorz F., Keis S., McMillan D.G., Olsson K., Stanton J.A., RA Stockwell P., Black M.A., Klingeman D.M., Land M.L., Han C.S., RA Martin S.L., Becher S.A., Peddie C.J., Morgan H.W., Matthies D., RA Preiss L., Meier T., Brown S.D., Cook G.M.; RT "Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus RT thermarum strain TA2.A1."; RL J. Bacteriol. 193:4290-4291(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCE01000163; EGL81694.1; -; Genomic_DNA. DR EnsemblBacteria; EGL81694; EGL81694; CathTA2_2880. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 23093 MW; 2BA3BD2474EF4332 CRC64; MKDFSLYVIT GEQFYPHRHY LEVIEEAIQG GADMVQLREK KKTKRELLDM ARQLKALCDR YKVPFIVNDH VDIALAVDAD GVHLGQDDLP LEEARKILGP DKIIGISTHN LEEAKRAEEG GADYIGVGPV FPTNTKEDVV DPVGLEYVRQ VVEHIRIPFV AIGGIKLHNV DQVLKAGAKR ICIVSAIVGA ENVKEAACAF ARKLETVR // ID F5LE99_9BACL Unreviewed; 230 AA. AC F5LE99; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9413_2717; OS Paenibacillus sp. HGF7. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=944559; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGF7; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDH01000026; EGL19307.1; -; Genomic_DNA. DR ProteinModelPortal; F5LE99; -. DR EnsemblBacteria; EGL19307; EGL19307; HMPREF9413_2717. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 53 57 HMP-PP binding (By similarity). FT REGION 155 157 THZ-P binding (By similarity). FT REGION 207 208 THZ-P binding (By similarity). FT METAL 89 89 Magnesium (By similarity). FT METAL 108 108 Magnesium (By similarity). FT BINDING 88 88 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 HMP-PP (By similarity). FT BINDING 187 187 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 23880 MW; 12DFF15696C064F1 CRC64; MAAMTKTASE TRYTGNLREA LKVYLVMGSP NCGGRDPAAV LQAAIEGGVT LFQFREKGPG ALQGQERTEL GSRLLGVCRQ AGIPFIVNDD LRLAEELEAD GVHVGQEDLA QWDREGLRHR FKGRILGISA HDPAEAREAV RCGADYLGAG PMYATATKPD ARAVQGPGIL AAMRADGISL PLAGIGGITP EGAGAVLAAG ADGVAVISAI SGADDPREAA RRFSRLFTGG // ID F5LEA4_9BACL Unreviewed; 218 AA. AC F5LEA4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF9413_2722; OS Paenibacillus sp. HGF7. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=944559; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGF7; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDH01000026; EGL19302.1; -; Genomic_DNA. DR ProteinModelPortal; F5LEA4; -. DR EnsemblBacteria; EGL19302; EGL19302; HMPREF9413_2722. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 218 AA; 22434 MW; F88C10AE283221DB CRC64; MTPYPAGPEL HAISTGRQKP EVLIRIASAI HPYVTAIHVR EKKQSPRELW ALLSGLAACG VPPGKIIVND RADAARLSGA AGVQLPGSGL PASAVKKGFP GLRVGVSVHG PEEGGRAAKE GADYVIFGHV FATGSKPGAA PRGAEALRET VLACGGLPVI AIGGIIPENC AEVIRAGAAG VAVMSGIWEA ENPAEAAERY RHELELALQP EKTGGELR // ID F5LWC0_GARVA Unreviewed; 484 AA. AC F5LWC0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF9435_0002; OS Gardnerella vaginalis 315-A. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=879307; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=315-A; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDI01000009; EGL13434.1; -; Genomic_DNA. DR EnsemblBacteria; EGL13434; EGL13434; HMPREF9435_0002. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 484 AA; 51321 MW; B50C38F2C63F998D CRC64; MQDVRECIET LRAKNPLTHC VTNNVVQEIT ANVLLAAGAS PAMVVDAEEA EVFAQIASGV LVNIGTYRPV DKESMDAAIR GAVKAHTPWV LDPVAVGGLA PRTQYAREIV KSHPAVIRAN ASEILGLAGE ESGGKGVDAG DSVDSAVAAA KKLVKRYGSV VAISGEKDAI YGHGCSARVS GGHEIMTKVV GTGCSLGALV AAYVGANRNR PFAATVAAHV HAAAAGTWAA QRSTLPGSFR KLWMDALMDL SADEMLKLAN IEFELDPVDW SLYFITDPKM SDRAEEDIAV DCVKGGASVV QLRDKYANSE TFNNKAQSLR DKMLANGCGD VPIFVDDRID CAKNLGFNLH VGQTDTPYIE ARKSIPAEWM VGLSIEKLEQ LDYVYNECAK ENVALPDVIG IGPIWPTATK PDAAPALGVE GVEKIAKRAK ELGISTLGIG GVNENTVFPI KSTSIDGLCV VSALMLAQNP CEEAHKLRDA ITKE // ID F5LWM5_GARVA Unreviewed; 872 AA. AC F5LWM5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; ORFNames=HMPREF9435_0281; OS Gardnerella vaginalis 315-A. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=879307; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=315-A; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDI01000010; EGL13357.1; -; Genomic_DNA. DR EnsemblBacteria; EGL13357; EGL13357; HMPREF9435_0281. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 872 AA; 97175 MW; 4360FC5C5062AE9A CRC64; MRDQFNLNTC FIANPKLCKS RALTDIVDDS LRAGSTFIRL NCADESAKEI TSIARDIAQI IEDNDKCDSV TFVIDGRVDV VWQARNQGIK VDGVHLAQSD MEPKEARALL GEDTIIGLSV ETESLVKIIN ELPDGCIDYI CVTAMHNPED GCENTTPTYE LEPNHTILDE AKINTICSAS NFPVLVGGRT SLEDVEMIAR SKAAGLFVSE ALYASETPES TMSEFVERFT QIRGNQKHGY AKRVIIQEKA DDKANNTPKF INAKEAKDAA KLAKQQRVDI ASRGCTQRDK AHIRKTTPVH FEYEYGSYDL EVPYTEIKLS DTPGVGPNPP FKDYNTEGPK CDPKEGLAPL RLDWIRDRGD IVEYEGRSRN LQDDGKRAIK RGKASKEWRG RTHKPMKAAD HPITQMWYAR HGIITPEMQY VATRENCDVE LVRSEVASGR AVIPCNINHP EAEPMIIGSR FLTKLNANMG NSAVTSSIDE EVEKLTWATK WGADTVMDLS TGNDIHTTRE WILRNSPVPI GTVPMYQALE KVEDDASKLS WELFRDTVIE QCEQGVDYMT IHAGVLLRYV PLTANRVTGI VSRGGSIMAE WCLQHHQESF LYTHFEELCE IFAKYDVAFS LGDGLRPGSL ADANDAAQLS ELMTLGELTK IAWQHDVQVM IEGPGHVPFD TVRMNIEMEK AICQNAPFYT LGPLTTDTAP GYDHITSAIG GVEIARYGTA MLCYVTPKEH LGLPNKDDVK QGVIAYKIAC HAADLAKHHP HAMDRDNAIS KARFEFRWLD QFNLSYDPDT AIAFHDETLP AEPAKMAHFC SMCGPKFCSM AISQNIRKRF GGADQQEQLV EEARSQAIAE GMKEMSKKFQ EAGSTLYQSA KA // ID F5M5D4_RHOSH Unreviewed; 203 AA. AC F5M5D4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RSWS8N_08635; OS Rhodobacter sphaeroides WS8N. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=992186; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WS8N; RX PubMed=21622735; DOI=10.1128/JB.05257-11; RA Porter S.L., Wilkinson D.A., Byles E.D., Wadhams G.H., Taylor S., RA Saunders N.J., Armitage J.P.; RT "Genome sequence of Rhodobacter sphaeroides Strain WS8N."; RL J. Bacteriol. 193:4027-4028(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFER01000001; EGJ22135.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ22135; EGJ22135; RSWS8N_08635. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 20305 MW; 1AA20B896A35C60D CRC64; MNLSLYFVTP DGAEGLEQLV AAAVRGGATL VQLRDKQRSD AELIPLARRL VAALDAQGVP LIVNDRIEVV LASGAAGLHV GQGDLGVAEA RRRIGPDRLL GLSVEAPEHL EALPLGIVDY VGAGPVRATA SKPDHAPPIG FEGLARLVAA APVPAVAIGG LGAGDAHAVK AAGAAGMAIV SAIGAAADPE AAARALALEW GRA // ID F5MT88_SHIFL Unreviewed; 211 AA. AC F5MT88; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SFK218_4480; OS Shigella flexneri K-218. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766146; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K-218; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGV01000065; EGK18574.1; -; Genomic_DNA. DR ProteinModelPortal; F5MT88; -. DR SMR; F5MT88; 10-208. DR EnsemblBacteria; EGK18574; EGK18574; SFK218_4480. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F5MW26_SHIFL Unreviewed; 211 AA. AC F5MW26; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SFVA6_5219; OS Shigella flexneri VA-6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766145; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VA-6; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGW01000006; EGK30154.1; -; Genomic_DNA. DR ProteinModelPortal; F5MW26; -. DR SMR; F5MW26; 10-208. DR EnsemblBacteria; EGK30154; EGK30154; SFVA6_5219. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F5NM68_SHIFL Unreviewed; 211 AA. AC F5NM68; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SFK272_4234; OS Shigella flexneri K-272. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766148; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K-272; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGX01000057; EGK18454.1; -; Genomic_DNA. DR EnsemblBacteria; EGK18454; EGK18454; SFK272_4234. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23013 MW; 2C3103AAC598690F CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLQLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F5P0W8_SHIFL Unreviewed; 211 AA. AC F5P0W8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SFK227_4105; OS Shigella flexneri K-227. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766147; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K-227; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGY01000053; EGK33673.1; -; Genomic_DNA. DR EnsemblBacteria; EGK33673; EGK33673; SFK227_4105. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23013 MW; 2C3103AAC598690F CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLQLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F5PGU8_SHIFL Unreviewed; 211 AA. AC F5PGU8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SFK304_4176; OS Shigella flexneri K-304. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766149; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K-304; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGZ01000063; EGK33715.1; -; Genomic_DNA. DR ProteinModelPortal; F5PGU8; -. DR SMR; F5PGU8; 10-208. DR EnsemblBacteria; EGK33715; EGK33715; SFK304_4176. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F5PKD4_SHIFL Unreviewed; 211 AA. AC F5PKD4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SFK671_5278; OS Shigella flexneri K-671. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766152; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K-671; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHA01000001; EGJ95769.1; -; Genomic_DNA. DR ProteinModelPortal; F5PKD4; -. DR SMR; F5PKD4; 10-208. DR EnsemblBacteria; EGJ95769; EGJ95769; SFK671_5278. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F5QEL3_SHIFL Unreviewed; 211 AA. AC F5QEL3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SF274771_5259; OS Shigella flexneri 2747-71. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766157; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2747-71; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHB01000047; EGJ79611.1; -; Genomic_DNA. DR ProteinModelPortal; F5QEL3; -. DR SMR; F5QEL3; 10-208. DR EnsemblBacteria; EGJ79611; EGJ79611; SF274771_5259. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F5QQA6_SHIFL Unreviewed; 193 AA. AC F5QQA6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SF434370_3827; OS Shigella flexneri 4343-70. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766160; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4343-70; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHC01000056; EGJ81855.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ81855; EGJ81855; SF434370_3827. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 19 23 HMP-PP binding (By similarity). FT REGION 116 118 THZ-P binding (By similarity). FT REGION 168 169 THZ-P binding (By similarity). FT METAL 52 52 Magnesium (By similarity). FT METAL 71 71 Magnesium (By similarity). FT BINDING 51 51 HMP-PP (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 193 AA; 20955 MW; 221F8D93D776B08B CRC64; MDSVQWIERL LDAGVRTLQL RIKDRRDEEV EADVVAAIAL GRRYNARLFI NDYWRLAIKH QAYGVHLGQE DLQATDLNAI RAAGLRLGVS THDDMEIDVA LAARPSYIAL GHVFPTQTKQ MPSAPQGLEQ LARHVERLAD YPTVAIGGIS LARAPAVIAT GVGSIAVVSA ITQAADWRLA TAQLLEIAGV GDE // ID F5R724_SHIFL Unreviewed; 193 AA. AC F5R724; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SF293071_5091; OS Shigella flexneri 2930-71. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766159; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2930-71; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHD01000050; EGJ93091.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ93091; EGJ93091; SF293071_5091. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 19 23 HMP-PP binding (By similarity). FT REGION 116 118 THZ-P binding (By similarity). FT REGION 168 169 THZ-P binding (By similarity). FT METAL 52 52 Magnesium (By similarity). FT METAL 71 71 Magnesium (By similarity). FT BINDING 51 51 HMP-PP (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 193 AA; 20955 MW; 221F8D93D776B08B CRC64; MDSVQWIERL LDAGVRTLQL RIKDRRDEEV EADVVAAIAL GRRYNARLFI NDYWRLAIKH QAYGVHLGQE DLQATDLNAI RAAGLRLGVS THDDMEIDVA LAARPSYIAL GHVFPTQTKQ MPSAPQGLEQ LARHVERLAD YPTVAIGGIS LARAPAVIAT GVGSIAVVSA ITQAADWRLA TAQLLEIAGV GDE // ID F5RCK4_9RHOO Unreviewed; 320 AA. AC F5RCK4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE SubName: Full=NUDIX hydrolase; GN ORFNames=METUNv1_02008; OS Methyloversatilis universalis FAM5. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Methyloversatilis. OX NCBI_TaxID=1000565; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FAM5; RX PubMed=21725020; DOI=10.1128/JB.05331-11; RA Kittichotirat W., Good N.M., Hall R., Bringel F., Lajus A., RA Medigue C., Smalley N.E., Beck D., Bumgarner R., Vuilleumier S., RA Kalyuzhnaya M.G.; RT "Genome sequence of Methyloversatilis universalis FAM5T, a RT methylotrophic representative of the order Rhodocyclales."; RL J. Bacteriol. 193:4541-4542(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHG01000048; EGK71784.1; -; Genomic_DNA. DR ProteinModelPortal; F5RCK4; -. DR EnsemblBacteria; EGK71784; EGK71784; METUNv1_02008. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 320 AA; 34282 MW; 38F7383B8603E784 CRC64; MSERKQVAVA AAVIFRDGAH GRAGAREFLL GQRAPGTFYP GYWEFPGGKV EKGEAPVDAL KRELDEELGI RVEHCTPWIT LSHAYEHAHV RLHFFRVERW SGRVHDHVHS ALAWQTADAL TVSPMLPANG PVMKSLRLPT RMAVTHAFRI GAAAQLDALR QACRRGRLML QIREPVLDAA ALDFAREAIR IARDHGCPVV LNGPVEVAQA LGADGVHLKA AQLAGLTARP DFEWVGASCH SVDELAQATR LGLDYAVAGS VLPTATHPGG DTLGWDGFTA LVAGSPLPVF AIGGLDDSHL AQAQTCGAHG IAAIRGAWVL // ID F5RGL1_9RHOO Unreviewed; 205 AA. AC F5RGL1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=METUNv1_03304; OS Methyloversatilis universalis FAM5. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Methyloversatilis. OX NCBI_TaxID=1000565; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FAM5; RX PubMed=21725020; DOI=10.1128/JB.05331-11; RA Kittichotirat W., Good N.M., Hall R., Bringel F., Lajus A., RA Medigue C., Smalley N.E., Beck D., Bumgarner R., Vuilleumier S., RA Kalyuzhnaya M.G.; RT "Genome sequence of Methyloversatilis universalis FAM5T, a RT methylotrophic representative of the order Rhodocyclales."; RL J. Bacteriol. 193:4541-4542(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHG01000057; EGK70399.1; -; Genomic_DNA. DR EnsemblBacteria; EGK70399; EGK70399; METUNv1_03304. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21083 MW; 85572E0F232E8BDF CRC64; MTRKPLRGLY AVTPEALSGG ALYRAAEAAC GGGAVVLQYR NKSTDAAQRR TDADALRAIT TVCGTLFVIN DDIELARACG ADGVHIGRDD GDPARARARL GKDALLGVSC YDDPALARAA AAAGADYIAF GSMYASGTKP QAPPAAITRF AEVADLGLPR CAIGGITLAR APELIAAGAD LLAVVSDLFD ADDIAARARA YARLF // ID F5RLM7_9FIRM Unreviewed; 228 AA. AC F5RLM7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9081_1163; OS Centipeda periodontii DSM 2778. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Centipeda. OX NCBI_TaxID=888060; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2778; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHQ01000030; EGK60150.1; -; Genomic_DNA. DR EnsemblBacteria; EGK60150; EGK60150; HMPREF9081_1163. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 206 207 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 186 186 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 24180 MW; E32B24D71CC9C6ED CRC64; MRNKFDLSAY LVIGPENTNG RPIARVIAEA VCAGFTFVQI RAKHTDAREI IDLTRAAADV IAAQEKSAVV TLVVNDRLDV VLAAREQGVK VDGVHVGQTD IPPDVCRKHL GADAIIGLSA RTSELLDYVS HCDTSCIDYF GAGPLHATPT KPEAGRTASG EIVTRSLEEL TQLHRISPVP VVVGGGVKAA DLPALKATGV EGFFVVSAVA GAMHPYAAAE ELVRIWHE // ID F5RX52_9ENTR Unreviewed; 213 AA. AC F5RX52; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9086_2210; OS Enterobacter hormaechei ATCC 49162. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=888063; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49162; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHR01000040; EGK60832.1; -; Genomic_DNA. DR EnsemblBacteria; EGK60832; EGK60832; HMPREF9086_2210. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23194 MW; F8425B6EDB600DFB CRC64; MYQPDFPPVP FRLGLYPVVD SVEWIARLLE AGVRTLQLRI KDKRDEEVEA DVVAAIALGR RYDARLFIND YWRLAVKHQA YGVHLGQEDL ETTDLNAIRD AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLTQLA SHVKRLADYP TVAIGGISLE RAPAVLETGV GSIAVVSAIT QAADWQAATA QLLQLAGAGD ERS // ID F5SA76_9BACL Unreviewed; 236 AA. AC F5SA76; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9374_0007; OS Desmospora sp. 8437. OC Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae; OC Desmospora. OX NCBI_TaxID=997346; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=8437; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHT01000001; EGK14920.1; -; Genomic_DNA. DR ProteinModelPortal; F5SA76; -. DR EnsemblBacteria; EGK14920; EGK14920; HMPREF9374_0007. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 153 155 THZ-P binding (By similarity). FT REGION 206 207 THZ-P binding (By similarity). FT METAL 89 89 Magnesium (By similarity). FT METAL 108 108 Magnesium (By similarity). FT BINDING 88 88 HMP-PP (By similarity). FT BINDING 127 127 HMP-PP (By similarity). FT BINDING 156 156 HMP-PP (By similarity). FT BINDING 186 186 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 236 AA; 25323 MW; 2AEFF989966CA7FC CRC64; MLQSTIIKYK GSDHMPVSPA SLRLYFVMGS QDCKGRDPVW VLREAIHGGI TMFQFREKKS SLTLSQRVFL GKKLRDLCAR QGIPFIVNDR TDLAMVLNAD GVHVGQEDLP AVQVRRLLGP KPMLGVSCGN PEEADKATQA GADYIGVGSM YATRSKPDAG EPIGPSAIRQ IARMDNSSLP IVGIGGIHHH NAKAVIQAGA EGIAVISAIA GASSPRQAAA ELRETVERTL MEQQAI // ID F5SDW9_9BACL Unreviewed; 214 AA. AC F5SDW9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN ORFNames=HMPREF9374_1300; OS Desmospora sp. 8437. OC Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae; OC Desmospora. OX NCBI_TaxID=997346; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=8437; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHT01000069; EGK12809.1; -; Genomic_DNA. DR EnsemblBacteria; EGK12809; EGK12809; HMPREF9374_1300. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 214 AA; 23210 MW; E86A704EE4A0FD90 CRC64; MDGAGRKGMN ELHFVTDPRK SVKEWVSVCR KAGEWLDWIH LRKPGASTAE LQDWGLTLIR EVGVDPKRLT VNGNVEVAEN LGCGGVHLPE RHPVDTIFTG GGNRRRVGCS VHSRDSAREK EQQGADYLFF GHVFASDSKP GRKPRGIRQL RQVTAAVNIP VIAIGGITPE RLPQLSTTGC AGVAVISAIA DAPDPAAAAR RLKQALQLEW VKQG // ID F5SN74_9GAMM Unreviewed; 253 AA. AC F5SN74; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9373_0507; OS Psychrobacter sp. 1501(2011). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=1002339; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1501; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHU01000047; EGK15020.1; -; Genomic_DNA. DR EnsemblBacteria; EGK15020; EGK15020; HMPREF9373_0507. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 78 82 HMP-PP binding (By similarity). FT REGION 177 179 THZ-P binding (By similarity). FT REGION 228 229 THZ-P binding (By similarity). FT METAL 110 110 Magnesium (By similarity). FT METAL 129 129 Magnesium (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 180 180 HMP-PP (By similarity). FT BINDING 208 208 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 253 AA; 26897 MW; B862AA1CB6869134 CRC64; MNSKTNAYNP TPDTENLPSF SSPQGLSSSQ SLSSSQRFLN KEGSSLKLYL VTDSIMCQRL GLIETVCKAI EGGVSFVQLR DKQANDDQLY KIACELKEAI AGRVPLIIND RVTIAKKANL DGAHIGQGDI SVSEARQILG PEAWLGLSIN TLTQLEHAHN NHLSELDYFG LGPVFATSTK PDHASPIGIK GLNVLAQASH LPTVAIGGIN LTNAPQVYDT SCDGIAVVSA ICAAENPKLA AQLLLAEHKG ALR // ID F5SS09_9GAMM Unreviewed; 393 AA. AC F5SS09; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=NUDIX hydrolase; GN ORFNames=HMPREF9373_1864; OS Psychrobacter sp. 1501(2011). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=1002339; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1501; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHU01000153; EGK10961.1; -; Genomic_DNA. DR ProteinModelPortal; F5SS09; -. DR EnsemblBacteria; EGK10961; EGK10961; HMPREF9373_1864. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 393 AA; 44724 MW; 12A51E68611D534A CRC64; MTINIRRKKT VINIDVAVAV IHYGDQYLLG FRKPEQHQGN RYEFVGGKIE DNETAEQALI REVLEEIGLD ISARCLINPL GILRHHYANI ETPHKSKRVC LHIFRVELTE QHYLECRDQQ QGCEGQQLQW VSLEDLVANK YRLPEANKTI LQWLKLPDLI SITQDVDSDL ELKTEAKSRA AADNGIDMNT NVDTNTTDDS RRQQWLHWYQ QKLPLQACVY LRLKNSDLPQ REQLLSSLLA NRPDIMLIID CQLANYLYSK NILPPQVIAQ HLTQKVIDET YQEANLTDVC NNLLAGLPLT VSSHNQETVL KVNQLAQYRL KHDLSPVIGV FVSPVQQTAT HPEAVPLGWE GFQRIASVSE VPVIALGGMS SEDLQQVRHH QGDKVAGIRN FLT // ID F5T036_9GAMM Unreviewed; 491 AA. AC F5T036; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-MAR-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=MAMP_01987; OS Methylophaga aminisulfidivorans MP. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Methylophaga. OX NCBI_TaxID=1026882; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MP; RX PubMed=21685284; DOI=10.1128/JB.05403-11; RA Han G.H., Kim W., Chun J., Kim S.W.; RT "Draft genome sequence of Methylophaga aminisulfidivorans MP T."; RL J. Bacteriol. 193:4265-4265(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFIG01000001; EGL54993.1; -; Genomic_DNA. DR EnsemblBacteria; EGL54993; EGL54993; MAMP_01987. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 491 AA; 53439 MW; 3A20963795C1626D CRC64; MDNPVQKPAV LLIGGLDPQG CAGISADIMT VQNHGCHPLP LITALTEQSS QGLTELGLVS PSKMMAQYEN CINDFDIKAI KIGLIPHIIT AQYIKEMLLD FSGPVILDPV LASTSGGVTV PDEVKAFIRD EIIPLVTIVT PNLPELAALT RTNLSVEEGA KSLRQKGVSA CLIKGGHAES ALAIDYFSSE LADFYLYNDK TVSQVRGTGC VLASALASQL ACGQDLRDAV VLAKAYVSRG IRLSAKAGPY QVIRHSQQDI ALVDFPKLCY QPELIGQTFN FPNCPELGIY PVVDNADWVE KLIDEGIHTI QLRVKDSDDE STKQQIVSAL AYLNDKSVQF FVNDHWQTAI ELGAYGVHLG QEDLHDANLK TLAEAGLRLG ISTHSYWELA RALAVNPSYI ALGPIYETTS KQMPFSPQGI ERLQQWVDLL KSHYPVVAIG GITLERAEQL KATGVGSVAM ITAITQANDY KTVTRQLLDL WQEISSYPDQ V // ID F5TIF4_9FIRM Unreviewed; 202 AA. AC F5TIF4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF1039_0929; OS Megasphaera sp. UPII 199-6. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=1000568; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UPII 199-6; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFIJ01000038; EGL39378.1; -; Genomic_DNA. DR ProteinModelPortal; F5TIF4; -. DR EnsemblBacteria; EGL39378; EGL39378; HMPREF1039_0929. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 22522 MW; 54A069CD474A9285 CRC64; MVLKIIAITN HDLVSTNYWE RLEQIATAPI DAVVLREKNL TEDEYAEYAR RMLKLCNLHD QTCILHNFGK AAVRLHVPRF QCSLKYLEDH SSLLYYMTTL GVSVHTVKEA VRAEELGATY IIAGHIFPTA CKKTEPPVGV DILKEICQAV SVPVYALGGV NTTTITQLRN IPIAGIALMS GIMTCKNVTD YIAELKNKYV GK // ID F5TJ80_9FIRM Unreviewed; 215 AA. AC F5TJ80; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1039_0647; OS Megasphaera sp. UPII 199-6. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=1000568; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UPII 199-6; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFIJ01000045; EGL35092.1; -; Genomic_DNA. DR EnsemblBacteria; EGL35092; EGL35092; HMPREF1039_0647. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23522 MW; A8D71D76866CAF06 CRC64; MTKEQHLQRL RDDPLYVILG EALSCGRTNV QTAADVLAAG VRIIQYREKH KTWREKYAEA KEIRRLCRKY DATFIMNDAV DLAVACKADG IHVGQDDAPV SFVRQWAGPQ MLIGVSTHTE EEMTEAVRDG ADYVGLGPFY PTQSKRDVHA PVTPKVRQFA LQLSIPVVAI GGIGKANIGA LYAEGFRSFA MISAVVGQVQ IAAAVQALRQ AVAVD // ID F5TNI5_9ACTO Unreviewed; 216 AA. AC F5TNI5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9947_0773; OS Propionibacterium sp. 409-HC1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=936047; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=409-HC1; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFIK01000066; EGL42970.1; -; Genomic_DNA. DR ProteinModelPortal; F5TNI5; -. DR EnsemblBacteria; EGL42970; EGL42970; HMPREF9947_0773. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F5TQM9_9ACTO Unreviewed; 126 AA. AC F5TQM9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF9947_1358; OS Propionibacterium sp. 409-HC1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=936047; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=409-HC1; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFIK01000094; EGL40649.1; -; Genomic_DNA. DR EnsemblBacteria; EGL40649; EGL40649; HMPREF9947_1358. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 126 AA; 13324 MW; D849408A1FEB3130 CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGDLGPRE IGRTVR // ID F5TQN0_9ACTO Unreviewed; 102 AA. AC F5TQN0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF9947_1359; OS Propionibacterium sp. 409-HC1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=936047; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=409-HC1; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFIK01000094; EGL40636.1; -; Genomic_DNA. DR EnsemblBacteria; EGL40636; EGL40636; HMPREF9947_1359. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 102 AA; 10351 MW; C4C0354A30039B4B CRC64; MDLVRSAEPF ADALDYVGAG PFRPTPTKES GRSPLGVQGY PALVGASSLP VVAIGDVQVA DVPALAATGV AGVAMVRAIM ASDDPAAVVR QVVQSFDEVR VS // ID F5TSB8_9ACTO Unreviewed; 216 AA. AC F5TSB8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9948_1517; OS Propionibacterium sp. 434-HC2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=936048; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=434-HC2; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFIL01000016; EGL44705.1; -; Genomic_DNA. DR EnsemblBacteria; EGL44705; EGL44705; HMPREF9948_1517. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22504 MW; D68C19AB366F1623 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAGMRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTAP KSSARELAEA WRTAKE // ID F5TX31_9ACTO Unreviewed; 217 AA. AC F5TX31; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9948_0740; OS Propionibacterium sp. 434-HC2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=936048; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=434-HC2; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFIL01000065; EGL40763.1; -; Genomic_DNA. DR ProteinModelPortal; F5TX31; -. DR EnsemblBacteria; EGL40763; EGL40763; HMPREF9948_0740. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F5UM33_9CYAN Unreviewed; 360 AA. AC F5UM33; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MicvaDRAFT_2335; OS Microcoleus vaginatus FGP-2. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Microcoleus. OX NCBI_TaxID=756067; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FGP-2; RX PubMed=21705610; DOI=10.1128/JB.05138-11; RA Starkenburg S.R., Reitenga K.G., Freitas T., Johnson S., Chain P.S., RA Garcia-Pichel F., Kuske C.R.; RT "Genome of the cyanobacterium Microcoleus vaginatus FGP-2, a RT photosynthetic ecosystem engineer of arid land soil biocrusts RT worldwide."; RL J. Bacteriol. 193:4569-4570(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FGP-2; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Pagani I., Land M.L., Hauser L., Garcia-Pichel F., Kuske C.R., RA Woyke T.J.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFJC01000013; EGK85160.1; -; Genomic_DNA. DR EnsemblBacteria; EGK85160; EGK85160; MicvaDRAFT_2335. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 129 Unknown (By similarity). FT REGION 130 360 Thiamine-phosphate synthase (By FT similarity). FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 360 AA; 40244 MW; 071402AB876F9C68 CRC64; MTDKQNRTLP AQPALCRILD ANLDRSREGL RIIEEWCRFG LNNADLAGEC KQLRQELAAW HVAELRSARD TPADPGTELT HPQEEQRSSI QQLLEANFCR VEEALRVLEE YGKIYDRNMG AAFKQMRYRV YTLESNLLAY RRYQQLLRSQ LYLVTSPRDN LLGVVEAALQ GGLTLVQYRD KSSDDGAKLA NARKLCELCH RYDALLIVND RVDFAIAADA DGVHLGQQDL PVAEARKLLG PGRIIGRSTT NGEEMQRAIE EGADYIGVGP VYSTPTKPDK QAAGLDYVRY AADKSSIPWF AIGGIDINNL DEVLNAGAQR VAAVRAIMEA EQPTLVTQFF ISQLIRMENL KAQKALHGKS // ID F5VQA4_CROSK Unreviewed; 210 AA. AC F5VQA4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CSE899_17782; OS Cronobacter sakazakii E899. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=930780; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E899; RX PubMed=21952538; DOI=10.1128/JB.05913-11; RA Chen Y., Strain E.A., Allard M., Brown E.W.; RT "Genome Sequence of Cronobacter sakazakii E899, a Strain Associated RT with Human Illness."; RL J. Bacteriol. 193:5861-5861(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFMO01000316; EGL71450.1; -; Genomic_DNA. DR EnsemblBacteria; EGL71450; EGL71450; CSE899_17782. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22700 MW; 9E016695B53AB23E CRC64; MTPLFAPVPR RLGLYPVVDS VEWVTRLLDA GVRTVQLRIK DKTEAEAEAD VAAAIALGQR YHARLFINDY WRLAIKHQAY GVHLGQEDLQ TADPDAIRRA GLRLGVSTHD DMEIDVALAV RPSYIALGHV FPTQTKQMPS APQGLAQLAA HVKRLGDYPT VAIGGISLER APAVLETGVG SIAVVSAITQ APDWRGATQR LLELAGVGDE // ID F5VT70_STROR Unreviewed; 210 AA. AC F5VT70; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9968_0766; OS Streptococcus oralis SK255. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1005704; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK255; RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., RA Methe B., Sutton G., Nelson K.E.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFNM01000016; EGL91134.1; -; Genomic_DNA. DR EnsemblBacteria; EGL91134; EGL91134; HMPREF9968_0766. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22777 MW; A5C6873030CCC88B CRC64; MNRKILKLYL VTNRYQDSLE NFLEKVETAC RSGVTIIQLR EKILTTNQYY QLAKRVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE TSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLIQ AEDIEAKAHA FLTKLDDIVS // ID F5W3S2_STAAU Unreviewed; 213 AA. AC F5W3S2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21305_0034; OS Staphylococcus aureus subsp. aureus 21305. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904759; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21305; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFNO01000007; EGL89293.1; -; Genomic_DNA. DR ProteinModelPortal; F5W3S2; -. DR SMR; F5W3S2; 4-209. DR PRIDE; F5W3S2; -. DR EnsemblBacteria; EGL89293; EGL89293; SA21305_0034. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F5WES4_STAAU Unreviewed; 213 AA. AC F5WES4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21310_2680; OS Staphylococcus aureus subsp. aureus 21310. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904760; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21310; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFNP01000048; EGL92099.1; -; Genomic_DNA. DR ProteinModelPortal; F5WES4; -. DR SMR; F5WES4; 4-209. DR PRIDE; F5WES4; -. DR EnsemblBacteria; EGL92099; EGL92099; SA21310_2680. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F5WML5_STAAU Unreviewed; 213 AA. AC F5WML5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21318_2527; OS Staphylococcus aureus subsp. aureus 21318. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904763; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21318; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFNQ01000052; EGL93312.1; -; Genomic_DNA. DR ProteinModelPortal; F5WML5; -. DR SMR; F5WML5; 4-209. DR PRIDE; F5WML5; -. DR EnsemblBacteria; EGL93312; EGL93312; SA21318_2527. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F5X173_STRG1 Unreviewed; 210 AA. AC F5X173; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SGGB_1172; OS Streptococcus gallolyticus (strain ATCC 43143 / F-1867). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=981539; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43143 / F-1867; RX PubMed=21633709; DOI=10.1371/journal.pone.0020519; RA Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M., RA Chang C.-H., Hsu M.-T.; RT "Sequencing and comparative genome analysis of two pathogenic RT Streptococcus gallolyticus subspecies: genome plasticity, adaptation RT and virulence."; RL PLoS ONE 6:E20519-E20519(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012053; BAK28034.1; -; Genomic_DNA. DR RefSeq; YP_006033993.1; NC_017576.1. DR ProteinModelPortal; F5X173; -. DR EnsemblBacteria; BAK28034; BAK28034; SGGB_1172. DR GeneID; 12630373; -. DR KEGG; sgt:SGGB_1172; -. DR KO; K00788; -. DR BioCyc; SGAL981539:GLL2-1239-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22695 MW; B32CAC167AC003AB CRC64; MDKEILQVYF ICGTANCPEG KFLEILEAAF KSGVTCFQFR EKGANALKGG EKVVLARKVK ELCRKYQIPL IINDDVDLAL ELDADGIHLG QDDLPITKAR QLFPNKIIGL SVGSTIEYQR SAVELVDYIG VGPIFPTSSK NDAGEVIGLK GLNDVRDYDK EIPIVAIGGI TFGDVAAIKQ SGADGVAVIS AIAQSKQVEV DTQRLSSFFD // ID F5X6R1_STRPX Unreviewed; 210 AA. AC F5X6R1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SGPB_1036; OS Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC OS 1723-81). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=981540; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81; RX PubMed=21633709; DOI=10.1371/journal.pone.0020519; RA Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M., RA Chang C.-H., Hsu M.-T.; RT "Sequencing and comparative genome analysis of two pathogenic RT Streptococcus gallolyticus subspecies: genome plasticity, adaptation RT and virulence."; RL PLoS ONE 6:E20519-E20519(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012054; BAK30101.1; -; Genomic_DNA. DR RefSeq; YP_004559187.1; NC_015600.1. DR EnsemblBacteria; BAK30101; BAK30101; SGPB_1036. DR GeneID; 10752640; -. DR KEGG; stb:SGPB_1036; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR BioCyc; SPAS981540:GJYA-1103-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22609 MW; D0ED6845742031E0 CRC64; MDKEILQVYF ICGTANCPEG KFLEILEAAF KSGVTCFQFR EKGANALKGD EKVVLARKVK ELCRKYQIPL IINDDVDLAL ELDADGIHLG QDDLPITKAR QLFPNKIIGL SVGSTIEYQQ SAVGLVDYIG VGPIFPTSSK NDAGEVIGLK GLNDVRDYDK EIPIVAIGGI TFGDVAAIKQ SGADGVAVIS AIAQSKQVEV DTQRLSSCFD // ID F5XAY3_PORGT Unreviewed; 647 AA. AC F5XAY3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PGTDC60_1311; OS Porphyromonas gingivalis (strain TDC60). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=1030843; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TDC60; RX PubMed=21705612; DOI=10.1128/JB.05269-11; RA Watanabe T., Maruyama F., Nozawa T., Aoki A., Okano S., Shibata Y., RA Oshima K., Kurokawa K., Hattori M., Nakagawa I., Abiko Y.; RT "Complete genome sequence of the bacterium Porphyromonas gingivalis RT TDC60, which causes periodontal disease."; RL J. Bacteriol. 193:4259-4260(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012203; BAK25465.1; -; Genomic_DNA. DR RefSeq; YP_004510031.1; NC_015571.1. DR EnsemblBacteria; BAK25465; BAK25465; PGTDC60_1311. DR GeneID; 10722754; -. DR KEGG; pgt:PGTDC60_1311; -. DR KO; K00788; -. DR BioCyc; PGIN1030843:GJTB-1347-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 647 AA; 70893 MW; DA3CD7F47136F4A7 CRC64; MKPWLITPEK LTSGQIGLLD HLFDRGLERL HLRLPGAGEE EYSQVIEAVA ACYRRRIVVH DHPRLIGRYR LCGLHLPERI WKGMTDRPQL PDGCTVSASC HAIEDIESFP FRLDYCFLSP VFDSLCKVGY AGRFSPDSLG DRLQRLHLPV VALGGITPDR LPQLRRAGFA SAAALGYVWL AKGRELMRWQ ELCTPAVICV GGVDPSAGAG ITADVRTAEN MGVRAYTVAT AITFQGSGSY RGERWVDSAD IIRQIESLSA EMEPAVAKIG LIRDSDTLSL VVDCLKKVFP SIRIVWDPVL RASADSSAGQ ADRFNLEDIT ALSRIDFITP NLPEARHLLG CEPDDETLLD FYRRSGVGLV LKGGHAGESV VTDRIVYDGR CEALRLLRGG TGKHGTGCAH STAFAAALAL EQEPFTAAGM AQLYVSRLRE RASGLLAMHK DLPVDPVVRL MSEIDLQFIT HRQPDLSELE EAEAVCRIGV HWVQLRMKEA SDEEMLHTAC AVKAVCRHHG ALFVVNDRVE IARQVDADGV HLGKEDMAIV EARRILGSNK IIGRTCNTME DVRRAYAEGA DYVGIGPYRY TETKQRLAPV LGLEGYKAIA ACMQTEGIRL PAFAVGGIED ADIPLIRDCG IGGIAVSGSL IRKIKKN // ID F5XRV3_MICPN Unreviewed; 244 AA. AC F5XRV3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MLP_41520; OS Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / OS NBRC 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Microlunatus. OX NCBI_TaxID=1032480; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414 RC / VKM Ac-1990 / NM-1; RA Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., RA Sasagawa M., Fukada J., Nakamura S., Katano Y., Hanada S., RA Kamagata Y., Nakamura N., Yamazaki S., Fujita N.; RT "Whole genome sequence of Microlunatus phosphovorus NM-1."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012204; BAK37166.1; -; Genomic_DNA. DR RefSeq; YP_004574569.1; NC_015635.1. DR ProteinModelPortal; F5XRV3; -. DR EnsemblBacteria; BAK37166; BAK37166; MLP_41520. DR GeneID; 10770082; -. DR KEGG; mph:MLP_41520; -. DR KO; K00788; -. DR BioCyc; MPHO1032480:GHBY-4180-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 244 AA; 26524 MW; A8FC2AB512C82689 CRC64; MTALMGLQAR LRLARLYLCT DARTERGDLA EFCEAAFAGG VDILQIRQKE MDPAEELDAL EIARRAAERH QALICVNDSP RLAGRFAADV LHLGQTDGSS REARRQLPRW ALIGRSTHEP KQADRAIEDG DADYFCVGPV YATPTKPDYR PAGLDLVQYA AEVAPPSDIA AKPWFAIGGI DLGNLDQVLA AGARRVCVVR AITQADDPEA GARELSDRLR EAWRSDPAMK PYALAAAGFT GPAR // ID F5Y0G2_RAMTT Unreviewed; 347 AA. AC F5Y0G2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine-phosphate synthase; GN Name=thiE; OrderedLocusNames=Rta_22700; OS Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 OS / TTB310). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Ramlibacter. OX NCBI_TaxID=365046; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310; RA Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., RA Py B., Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., RA Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., RA Mejean V., DuBow M., Barras F., Heulin T.; RT "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000245; AEG93368.1; -; Genomic_DNA. DR RefSeq; YP_004619387.1; NC_015677.1. DR EnsemblBacteria; AEG93368; AEG93368; Rta_22700. DR GeneID; 10832886; -. DR KEGG; rta:Rta_22700; -. DR KO; K00788; -. DR OMA; VEWRICL; -. DR BioCyc; RTAT365046:GHCU-2335-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 347 AA; 36604 MW; 487E5085EB0CCE3F CRC64; MSNTMRRQEC RVELAGQANQ DTWPATSRGL RERGAAAVLM YGGPGQDLHW LDSVHATGWV RGRSNLAAGE LAAAWDGARG QGFVAADAVL LALAGSDPLR LPLLSWDAWP PAAVAPPAAV PAPLGLYAIV DSVPALRQVL AAGIATVQLR IKQPGDADAA WQAGLRAQLR EGIAATRAAG ATLFVNDHWR LAAELGAQAV HLGQEDLAAL SDEGRAALRA TGLQLGVSSH AVWELCCAIG LAPRYVACGP VWPTVTKDMP WRPQGLDNLA WWCRAAGRPV VAIGGILTPR QVRSAARSGA DGVCVLRGLW PDPRQTVPAL KEAFELGRQE RDGLAPAWPH PTLEPAA // ID F5YA24_TREAZ Unreviewed; 226 AA. AC F5YA24; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 15. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=TREAZ_2037; OS Treponema azotonutricium (strain ATCC BAA-888 / DSM 13862 / ZAS-9). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=545695; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-888 / DSM 13862 / ZAS-9; RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A., RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., RA Lucey K., Ballor N.R., Ottesen E., Rosenthal R., Allen A., RA Leadbetter J.R., Paulsen I.T.; RT "Complete sequence of Treponema azotonutricium strain ZAS-9."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001841; AEF81566.1; -; Genomic_DNA. DR RefSeq; YP_004525895.1; NC_015577.1. DR EnsemblBacteria; AEF81566; AEF81566; TREAZ_2037. DR GeneID; 10675448; -. DR KEGG; taz:TREAZ_2037; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR BioCyc; TAZO545695:GHPL-303-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 226 AA; 23840 MW; 60FC925C0BFC22B9 CRC64; MRIVGVTNRL LCGGENGFLA QVKKIAVSGI DAFVLREKDL SLGRYEDLAR KVLDICRPGN VELILHTQVE AAIDLNAKSI QLPWAVFKTG AFISADLARL RDRGIAFGVS VHSAEEAAEA ERSGAAWLIA GHVFVTDCKK GLEPRGLEFI GSVCRAVKIP VYAIGGISEY TIAGVEKCGT EGVCIMSSLM ESPDPPALIA GLRSRLGAAC FPNPCAGQGS GLKEGA // ID F5YB60_TREAZ Unreviewed; 208 AA. AC F5YB60; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TREAZ_3009; OS Treponema azotonutricium (strain ATCC BAA-888 / DSM 13862 / ZAS-9). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=545695; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-888 / DSM 13862 / ZAS-9; RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A., RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., RA Lucey K., Ballor N.R., Ottesen E., Rosenthal R., Allen A., RA Leadbetter J.R., Paulsen I.T.; RT "Complete sequence of Treponema azotonutricium strain ZAS-9."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001841; AEF83389.1; -; Genomic_DNA. DR RefSeq; YP_004528438.1; NC_015577.1. DR EnsemblBacteria; AEF83389; AEF83389; TREAZ_3009. DR GeneID; 10677308; -. DR KEGG; taz:TREAZ_3009; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; TAZO545695:GHPL-2994-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21618 MW; B87CE0DCB9B6D723 CRC64; MLNIEDLKLY LCTDRGLSLG RPLVETVEDA IAGGVTMVQI REKDIPSREF YDLALQALRV TRAHHIPLII NDRLDIALAI GAEGVHLGQS DLPCIEARRV GGEDFIIGVS AHTPAEAVRA ERDGADYIGA GAVFPTGSKA DVSAIIGLDG LKAAAASVKI PVIGIGGIGP KNAAEVIASG AAGIAVISAI LSQPDIREAA MILRRCLG // ID F5YZV9_MYCSD Unreviewed; 225 AA. AC F5YZV9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=JDM601_0385; OS Mycobacterium sp. (strain JDM601). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=875328; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JDM601; RX PubMed=21685274; DOI=10.1128/JB.05291-11; RA Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., RA Song Y.Z., Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.; RT "Complete genome sequence of a novel clinical isolate, the RT nontuberculous Mycobacterium strain JDM601."; RL J. Bacteriol. 193:4300-4301(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002329; AEF34385.1; -; Genomic_DNA. DR RefSeq; YP_004521639.1; NC_015576.1. DR EnsemblBacteria; AEF34385; AEF34385; JDM601_0385. DR GeneID; 10682379; -. DR KEGG; mjd:JDM601_0385; -. DR KO; K00788; -. DR BioCyc; MSP875328:GHLX-390-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT METAL 87 87 Magnesium (By similarity). FT METAL 106 106 Magnesium (By similarity). FT BINDING 86 86 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 23855 MW; 5FBE0F6F16BF47E4 CRC64; MHERSDRLTR LVDARLYLCT DARREKGDLA EFAEAALAGG VDVIQLRDKG SPGEQQFGPL EARDELAALE ILSAAARRHG ALLAVNDRAD IARAAEVDVL HLGQDDLPLP IAREIVGPDV LIGRSTHDGQ QVRAALTEPV DYFCVGPCWP TPTKPGRPAP GLELLRFAVD QRADKPWFAI GGIDAERLPQ VVAAGAGRVV VVRAITAADD PQAAASALLA ALTGA // ID F5Z5V0_ALTSS Unreviewed; 541 AA. AC F5Z5V0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=ambt_18450; OS Alteromonas sp. (strain SN2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alteromonas. OX NCBI_TaxID=715451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SN2; RX PubMed=21705606; DOI=10.1128/JB.05252-11; RA Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O., RA Oh T.K., Kim J.F.; RT "Complete genome sequence of the polycyclic aromatic hydrocarbon- RT degrading bacterium Alteromonas sp. strain SN2."; RL J. Bacteriol. 193:4292-4293(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002339; AEF05183.1; -; Genomic_DNA. DR RefSeq; YP_004468985.1; NC_015554.1. DR EnsemblBacteria; AEF05183; AEF05183; ambt_18450. DR GeneID; 10650593; -. DR KEGG; alt:ambt_18450; -. DR KO; K14153; -. DR BioCyc; ASP715451:GHV1-3693-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 541 AA; 58047 MW; CD412EAB556CE14C CRC64; MIETTRGLFK ATQAMSEEPV VWAIGGIDTS GGAGITRDAI TLADINVHAC VLTTQVANQS HSIMRSASAL SIDTLNEQWQ ALESDLPPRA IKIGAIANSA QALFLCEHVV KIKQYKTANC FVVWDPVLVS SSGGVLGELS QHSIDTLIAT VDVVTPNVKE LAQLTGWPVH CEKSLLAAAQ ALIARGAQAV YVKGGHAHWQ STAIDTFVSA QAIRIFQQPR DNMGNLRGTG CMFSSALAGF VASDYDIQDA LTLANAYLHK VRNASVFSSS SVCSADQIHC AGLVGFPLTP VHYPSVRYGE NDPISHKTPM QFPKLTNTSL GIYPVVSDVS QLEVLVKAGA VIIQLRIKFG TEDFKSTQIA KAVEVVKNTP CQLFINDDWE LAIKHGAYGV HLGQEDLETA NLQAISRAGL RLGVSTHGYC ELQRIKRLSP SYIALGHIFP TTTKDMPSKP QGLDRLSRYV RLCADIPTVA IGGINLSRIN TVASTGVSSI AVVRAVTQAA DPAAAFHDLL RRMNDAEDNG EDMVDRITEP GALVQHGLSY G // ID F5ZJJ1_STRPW Unreviewed; 212 AA. AC F5ZJJ1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=STP_1065; OS Streptococcus parauberis (strain KCTC 11537). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=936154; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 11537; RX PubMed=21531805; DOI=10.1128/JB.00182-11; RA Nho S.W., Hikima J.I., Cha I.S., Park S.B., Jang H.B., RA Del Castillo C.S., Kondo H., Hirono I., Aoki T., Jung T.S.; RT "Complete genome sequence and immunoproteomic analyses of the RT bacterial fish pathogen Streptococcus parauberis."; RL J. Bacteriol. 193:3356-3366(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002471; AEF25513.1; -; Genomic_DNA. DR RefSeq; YP_004479185.1; NC_015558.1. DR EnsemblBacteria; AEF25513; AEF25513; STP_1065. DR GeneID; 10662050; -. DR KEGG; stk:STP_1065; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; SPAR936154:GHCN-1103-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23147 MW; B4231215D5E79193 CRC64; MLSLYFVCGT SNCPNGDLIR TLENALKGGV NCFQFREKGP NAMVGQEKEE LAKQLHLLCQ TYHVPFIIDD DIDLVKKLDA DGLHIGQKDI SVQEARQQIG NKILGLSVNN LEEYEKSEID LLDYIGVGPY HPTQSKVDAQ EAVGTSSIQA IRQVNQSLPI VAIGGIGQND IEPIIKAGAN GIAVISAIAR SKEIEQTCKS FRSRLDLALK SE // ID F5ZWR4_SALTU Unreviewed; 211 AA. AC F5ZWR4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-APR-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=STMUK_4147; OS Salmonella typhimurium (strain ATCC 68169 / UK-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=990282; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 68169 / UK-1; RX PubMed=21622747; DOI=10.1128/JB.05224-11; RA Luo Y., Kong Q., Yang J., Golden G., Wanda S.Y., Jensen R.V., RA Ernst P.B., Curtiss R.III.; RT "Complete genome sequence of the universal killer Salmonella enterica RT serovar typhimurium UK-1 (ATCC 68169)."; RL J. Bacteriol. 193:4035-4036(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002614; AEF09965.1; -; Genomic_DNA. DR RefSeq; YP_005254599.1; NC_016863.1. DR ProteinModelPortal; F5ZWR4; -. DR EnsemblBacteria; AEF09965; AEF09965; STMUK_4147. DR BioCyc; SENT990282:GHYP-4146-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22983 MW; 803CF861FC550D88 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE SGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID F6A0M3_GARVH Unreviewed; 484 AA. AC F6A0M3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=HMPREF9231_0090; OS Gardnerella vaginalis (strain HMP9231). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=1009464; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMP9231; RA Durkin A.S., Kim M.K., Hostetler J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RT "Complete sequence of Gardnerella vaginalis HMP9231."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002725; AEF31547.1; -; Genomic_DNA. DR RefSeq; YP_005837469.1; NC_017456.1. DR EnsemblBacteria; AEF31547; AEF31547; HMPREF9231_0090. DR GeneID; 12444200; -. DR KEGG; gvh:HMPREF9231_0090; -. DR OrthoDB; EOG628F8M; -. DR BioCyc; GVAG1009464:GLDL-89-MONOMER; -. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Thiamine biosynthesis; Transferase. SQ SEQUENCE 484 AA; 51321 MW; B50C38F2C63F998D CRC64; MQDVRECIET LRAKNPLTHC VTNNVVQEIT ANVLLAAGAS PAMVVDAEEA EVFAQIASGV LVNIGTYRPV DKESMDAAIR GAVKAHTPWV LDPVAVGGLA PRTQYAREIV KSHPAVIRAN ASEILGLAGE ESGGKGVDAG DSVDSAVAAA KKLVKRYGSV VAISGEKDAI YGHGCSARVS GGHEIMTKVV GTGCSLGALV AAYVGANRNR PFAATVAAHV HAAAAGTWAA QRSTLPGSFR KLWMDALMDL SADEMLKLAN IEFELDPVDW SLYFITDPKM SDRAEEDIAV DCVKGGASVV QLRDKYANSE TFNNKAQSLR DKMLANGCGD VPIFVDDRID CAKNLGFNLH VGQTDTPYIE ARKSIPAEWM VGLSIEKLEQ LDYVYNECAK ENVALPDVIG IGPIWPTATK PDAAPALGVE GVEKIAKRAK ELGISTLGIG GVNENTVFPI KSTSIDGLCV VSALMLAQNP CEEAHKLRDA ITKE // ID F6A2W0_GARVH Unreviewed; 872 AA. AC F6A2W0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 22. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; OrderedLocusNames=HMPREF9231_0926; OS Gardnerella vaginalis (strain HMP9231). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=1009464; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMP9231; RA Durkin A.S., Kim M.K., Hostetler J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RT "Complete sequence of Gardnerella vaginalis HMP9231."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002725; AEF31152.1; -; Genomic_DNA. DR RefSeq; YP_005838256.1; NC_017456.1. DR EnsemblBacteria; AEF31152; AEF31152; HMPREF9231_0926. DR GeneID; 12445031; -. DR KEGG; gvh:HMPREF9231_0926; -. DR KO; K03147; -. DR OrthoDB; EOG6NWBM5; -. DR BioCyc; GVAG1009464:GLDL-920-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 872 AA; 97175 MW; 4360FC5C5062AE9A CRC64; MRDQFNLNTC FIANPKLCKS RALTDIVDDS LRAGSTFIRL NCADESAKEI TSIARDIAQI IEDNDKCDSV TFVIDGRVDV VWQARNQGIK VDGVHLAQSD MEPKEARALL GEDTIIGLSV ETESLVKIIN ELPDGCIDYI CVTAMHNPED GCENTTPTYE LEPNHTILDE AKINTICSAS NFPVLVGGRT SLEDVEMIAR SKAAGLFVSE ALYASETPES TMSEFVERFT QIRGNQKHGY AKRVIIQEKA DDKANNTPKF INAKEAKDAA KLAKQQRVDI ASRGCTQRDK AHIRKTTPVH FEYEYGSYDL EVPYTEIKLS DTPGVGPNPP FKDYNTEGPK CDPKEGLAPL RLDWIRDRGD IVEYEGRSRN LQDDGKRAIK RGKASKEWRG RTHKPMKAAD HPITQMWYAR HGIITPEMQY VATRENCDVE LVRSEVASGR AVIPCNINHP EAEPMIIGSR FLTKLNANMG NSAVTSSIDE EVEKLTWATK WGADTVMDLS TGNDIHTTRE WILRNSPVPI GTVPMYQALE KVEDDASKLS WELFRDTVIE QCEQGVDYMT IHAGVLLRYV PLTANRVTGI VSRGGSIMAE WCLQHHQESF LYTHFEELCE IFAKYDVAFS LGDGLRPGSL ADANDAAQLS ELMTLGELTK IAWQHDVQVM IEGPGHVPFD TVRMNIEMEK AICQNAPFYT LGPLTTDTAP GYDHITSAIG GVEIARYGTA MLCYVTPKEH LGLPNKDDVK QGVIAYKIAC HAADLAKHHP HAMDRDNAIS KARFEFRWLD QFNLSYDPDT AIAFHDETLP AEPAKMAHFC SMCGPKFCSM AISQNIRKRF GGADQQEQLV EEARSQAIAE GMKEMSKKFQ EAGSTLYQSA KA // ID F6A3A4_GARVH Unreviewed; 535 AA. AC F6A3A4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=HMPREF9231_0999; OS Gardnerella vaginalis (strain HMP9231). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=1009464; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMP9231; RA Durkin A.S., Kim M.K., Hostetler J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RT "Complete sequence of Gardnerella vaginalis HMP9231."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002725; AEF30774.1; -; Genomic_DNA. DR RefSeq; YP_005838323.1; NC_017456.1. DR EnsemblBacteria; AEF30774; AEF30774; HMPREF9231_0999. DR GeneID; 12445102; -. DR KEGG; gvh:HMPREF9231_0999; -. DR KO; K00878; -. DR OrthoDB; EOG628F8M; -. DR BioCyc; GVAG1009464:GLDL-991-MONOMER; -. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Thiamine biosynthesis; Transferase. SQ SEQUENCE 535 AA; 57465 MW; 0EC5747B29BC5179 CRC64; MRKNAEITPV KPDLGSASEG KIMEELNELN ANIDTNIDTS FSVRARRRMF LNDVRSCIER VRAKKPLTHC ITNNIVQEIT ANVLLSAGAT PIMVCDPDEA AGIAKIASGV LVNVGTFEEI KGKAIRKAIE TCEETQTTWV LDPVGVGVDE LTTRTKFVRE IVKRNPTVIR ANASEILALV GQNSQMKGVD AQDPVNSALE AAKKLAKEYG SVISISGEKD AVYGHGCLVR ITGGHKAMTK VVGTGCALGS LVAAYVGANP ERPVAATVAA HVHAAAAGTF AARQTTAPGT FKTLWIDALQ TLSVNNMFEL TNIEFSIEPT DWTLYLVTDP RMGNRSEEQV AVESIDGGVT IVQLRDKYSN DTEISEKAIK LRKTLIKAKH GDIPIFIDDH VDTAAKLGFN LHIGQKDTPF VTARKSMPAE WMIGLSCARV DLMEKAYKEC KENDTPLPDV IGIGAAFATN TKAHDVPPLG IEGVNEVAKV AHSMGVKTLA IGGIHENTVF PIKDLSIDGV CTVSALMCAE DPKKVASDLK SVITR // ID F6ACG4_PSEF1 Unreviewed; 213 AA. AC F6ACG4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Psefu_3448; OS Pseudomonas fulva (strain 12-X). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=743720; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12-X; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I., RA Woyke T.; RT "Complete sequence of Pseudomonas fulva 12-X."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002727; AEF23410.1; -; Genomic_DNA. DR RefSeq; YP_004475504.1; NC_015556.1. DR EnsemblBacteria; AEF23410; AEF23410; Psefu_3448. DR GeneID; 10659157; -. DR KEGG; pfv:Psefu_3448; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; PFUL743720:GHQV-3518-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22135 MW; 30EFD2D963AD7C56 CRC64; MAAPGKLRGL YAITDSELLA GGKLLPYVEA ALAGGARLLQ YRDKSTDEAR RLREAEALRT LCENHGAELI INDDAELAAR LGVGLHLGQE DGSLAAARAL LGRQAIIGGT CHAQLALAEQ AAGEGASYVA FGRFFNSLTK PGAPAATLDL LETAKARVAL PIVAIGGVDL HNAAPLIERG ASMIAVIHAL FAADSAAEVE RRARAFSALF ESN // ID F6AE03_PSEF1 Unreviewed; 316 AA. AC F6AE03; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=Psefu_3553; OS Pseudomonas fulva (strain 12-X). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=743720; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12-X; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I., RA Woyke T.; RT "Complete sequence of Pseudomonas fulva 12-X."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002727; AEF23515.1; -; Genomic_DNA. DR RefSeq; YP_004475609.1; NC_015556.1. DR ProteinModelPortal; F6AE03; -. DR EnsemblBacteria; AEF23515; AEF23515; Psefu_3553. DR GeneID; 10656009; -. DR KEGG; pfv:Psefu_3553; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; PFUL743720:GHQV-3623-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 316 AA; 34651 MW; 55F69BDE3BAF3E63 CRC64; MKRVHVAAAV IRGDDGRILI AKRPDDKHQG GLWEFPGGKV EEGEAVLAAL SRELHEELGI RVEAARPLIQ VRHDYSDKQV LLDVWEVSQF TGEPHGAEGQ PLAWVSPRQL GDYDFLAANR PIVAAARLPE HYLITPEGLD GPELLAGVRV AVANGIRLIQ LRAPAMFDAQ YRDLAVDVQG LCAGKAQLML KGPLEWLGDF PAAGWHLTAE QLRKYASKGR PLPEGRWLAA SCHSAEELEL ATQIGADFVT LSPLQATQTH PEAQPLGWQR ASEWLQGFNQ PCYLLGGVGP QDCQQAWQVG AQGVAGIRAF WPEQQR // ID F6AX73_DELSC Unreviewed; 307 AA. AC F6AX73; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=DelCs14_3479; OS Delftia sp. (strain Cs1-4). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Delftia. OX NCBI_TaxID=742013; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Cs1-4; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Bradfield C., RA Sheety A., Cheng S., Chain P., Denef V., Hickey W., Woyke T.; RT "Complete sequence of Delftia sp. Cs1-4."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002735; AEF90471.1; -; Genomic_DNA. DR RefSeq; YP_004488826.1; NC_015563.1. DR EnsemblBacteria; AEF90471; AEF90471; DelCs14_3479. DR GeneID; 10640337; -. DR KEGG; del:DelCs14_3479; -. DR KO; K00788; -. DR BioCyc; DSP742013:GH2F-3532-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 307 AA; 32412 MW; 2B4462B49C36A40C CRC64; MSNDSIQSWA DAIVRLHGAT FAPEGSALPS QPVPQAQRQE PAYLAALQAC SALGFIAIDA ETLACAWQAQ TLRRGRFEAT LWPDDPRDFG LEGADPALAF PECPRSLGLY GVLPDAQWVG RMARAGVPTV QLRFKSEDRD AIAREVRAAV AAVEGTGALL FINDHWREAI DAGAYGVHVG QEDLDALAGA DLQAIHASGL RLGVSTHGYA EMVRAHAVQP SYIALGAVFP TTLKKMATAP QGLARLGAYV RLMQRYPLVA IGGISADQFP AVRATGVGSV AVVRALVNAE DPEAAAQQLL ASMHAAD // ID F6B413_DESCC Unreviewed; 201 AA. AC F6B413; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Desca_1207; OS Desulfotomaculum carboxydivorans (strain DSM 14880 / VKM B-2319 / OS CO-1-SRB). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=868595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G., RA Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.; RT "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002736; AEF94068.1; -; Genomic_DNA. DR RefSeq; YP_004496980.1; NC_015565.1. DR EnsemblBacteria; AEF94068; AEF94068; Desca_1207. DR GeneID; 10630607; -. DR KEGG; dca:Desca_1207; -. DR KO; K00788; -. DR BioCyc; DCAR868595:GHXC-1264-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 159 159 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 201 AA; 21115 MW; 05F810CFCBD3C30F CRC64; MQLYLVTNRK QCLLPLPEVV RQAAGAGVNG IILREKDLTS RELYELALPI RKITGETGTT LIVADRLEVA MAVQADGVLL GYSSLPPGVV KQTIGYRGEI WASVHSPAEA RQAQQNGATA LVAGHIFTTD CKPGLNPKGI SFLKEILAQV TIPVIAIGGI TSSTAPSLIG SGAAGVAVMS YINNAQEPSL ATRKLLAVCT R // ID F6B7A2_DESCC Unreviewed; 216 AA. AC F6B7A2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Desca_0459; OS Desulfotomaculum carboxydivorans (strain DSM 14880 / VKM B-2319 / OS CO-1-SRB). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=868595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G., RA Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.; RT "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002736; AEF93352.1; -; Genomic_DNA. DR RefSeq; YP_004496264.1; NC_015565.1. DR EnsemblBacteria; AEF93352; AEF93352; Desca_0459. DR GeneID; 10629836; -. DR KEGG; dca:Desca_0459; -. DR KO; K00788; -. DR BioCyc; DCAR868595:GHXC-493-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22580 MW; 09DF7A81FC6D1D84 CRC64; MPKPIPDYSL YVITGESFSK GRSTEDVIRQ AILGGATVIQ LREKEYCGKE LIRVGKLLRD MTREMGVTFI VNDRVDVAFA VDADGVHLGQ DDLPIEVARQ ILGPDKIVGI SAGNMDEVLA AQARGADYVG LGPVFATGTK SDAGEAVGLD LVKQVCARAT IPVVGIGGIK ANNAAQVIEA GAAGVSVITA VVSADDVTEA ARQLRHQIDL AKGLKG // ID F6BK43_THEXL Unreviewed; 209 AA. AC F6BK43; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Thexy_1005; OS Thermoanaerobacterium xylanolyticum (strain ATCC 49914 / DSM 7097 / OS LX-11). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Thermoanaerobacterium. OX NCBI_TaxID=858215; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Pagani I., Hemme C., Woyke T.; RT "Complete sequence of Thermoanaerobacterium xylanolyticum LX-11."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002739; AEF17038.1; -; Genomic_DNA. DR RefSeq; YP_004470710.1; NC_015555.1. DR EnsemblBacteria; AEF17038; AEF17038; Thexy_1005. DR GeneID; 10661298; -. DR KEGG; txy:Thexy_1005; -. DR KO; K00788; -. DR BioCyc; TXYL858215:GHCH-1064-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22782 MW; 824D65E8BE939288 CRC64; MKDFDVSLYL VTDRNLLKAG RDFYDAVEES LQNGVTMLQL REKDISSREF YEIAKRLKDI AGKYNVPFII NDRIDIALSV DADGVHLGQE DLPCSIARKI MSDNKIIGIS AGCVDEAVEA ERDGADYIGA GAVFYTGTKK DIGEAIGLLD LKKIKEAVKI PVVAIGGIKY SNALDVMRTG VDGISVVSEI MASDDIGFAT RRLKDAISK // ID F6BUQ3_SINMB Unreviewed; 217 AA. AC F6BUQ3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=SinmeB_2611; OS Sinorhizobium meliloti (strain BL225C). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=698936; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BL225C; RX PubMed=21569405; DOI=10.1186/1471-2164-12-235; RG US DOE Joint Genome Institute; RA Galardini M., Mengoni A., Brilli M., Pini F., Fioravanti A., Lucas S., RA Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Land M., Hauser L., RA Woyke T., Mikhailova N., Ivanova N., Daligault H., Bruce D., RA Detter C., Tapia R., Han C., Teshima H., Mocali S., Bazzicalupo M., RA Biondi E.G.; RT "Exploring the symbiotic pangenome of the nitrogen-fixing bacterium RT Sinorhizobium meliloti."; RL BMC Genomics 12:235-235(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002740; AEG05508.1; -; Genomic_DNA. DR RefSeq; YP_005714751.1; NC_017322.1. DR ProteinModelPortal; F6BUQ3; -. DR EnsemblBacteria; AEG05508; AEG05508; SinmeB_2611. DR GeneID; 12302848; -. DR KEGG; smq:SinmeB_2611; -. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 217 AA; 22682 MW; 219C4A7B75DEEA83 CRC64; MSNIEDRCRL VLVVPDIADS AERARLVGEA LKGGDVASVI VPQYALSDAD FQKHAEALVP VIQQAGAAAL IEGDTRVAGR AKADGLHIAG GPDALADAIE RHAPKLIVGG GNATDRHHAL EIGELRPDYV FFGRTDGDIK PEAHPKNLAL AEWWASMIEI PCIVMGGTDP QSALAVAETG AEFVALRLAV FGEAGQAPSV VAAVNALLDE KAPRFEG // ID F6C1H4_SINMB Unreviewed; 201 AA. AC F6C1H4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 22-JAN-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=SinmeB_4703; OS Sinorhizobium meliloti (strain BL225C). OG Plasmid pSINMEB02. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=698936; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BL225C; RX PubMed=21569405; DOI=10.1186/1471-2164-12-235; RG US DOE Joint Genome Institute; RA Galardini M., Mengoni A., Brilli M., Pini F., Fioravanti A., Lucas S., RA Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Land M., Hauser L., RA Woyke T., Mikhailova N., Ivanova N., Daligault H., Bruce D., RA Detter C., Tapia R., Han C., Teshima H., Mocali S., Bazzicalupo M., RA Biondi E.G.; RT "Exploring the symbiotic pangenome of the nitrogen-fixing bacterium RT Sinorhizobium meliloti."; RL BMC Genomics 12:235-235(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002742; AEG08978.1; -; Genomic_DNA. DR RefSeq; YP_005716799.1; NC_017323.1. DR EnsemblBacteria; AEG08978; AEG08978; SinmeB_4703. DR GeneID; 12306689; -. DR KEGG; smq:SinmeB_4703; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Plasmid; Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22635 MW; 9D793C87865C3637 CRC64; MKLDPFYLIV DSAQWIERLV PLGVKLVQLR IKDRSKEDIR HQIRVARAVC SAHECQLIVN DYWQLTIEEA CDFIHLGQED LADADVAAIR AAGLKLGVST HDEAELAKAL AAEPDYVALG PIYPTILKKM KWAPQGLERL SWWRERVHPL PLVAIGGLNT ERIEGVFAHG ADSAAVVTDI TLNADPEGRT REWIRKTEAW R // ID F6C891_BIFBA Unreviewed; 918 AA. AC F6C891; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE SubName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiC; OrderedLocusNames=HMPREF9228_0557; OS Bifidobacterium breve (strain ACS-071-V-Sch8b). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=866777; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACS-071-V-Sch8b; RA Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M., RA Methe B., Sutton G., Nelson K.E.; RT "Complete sequence of Bifidobacterium breves ACS-071-V-Sch8b."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002743; AEF27869.1; -; Genomic_DNA. DR RefSeq; YP_005582445.1; NC_017218.1. DR EnsemblBacteria; AEF27869; AEF27869; HMPREF9228_0557. DR GeneID; 12169213; -. DR KEGG; bbv:HMPREF9228_0557; -. DR KO; K03147; -. DR OMA; INTICSA; -. DR OrthoDB; EOG6NWBM5; -. DR BioCyc; BBRE866777:GL99-554-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 918 AA; 100024 MW; C834C4CCDD603563 CRC64; MSNEYPYASM RDSFDLSAYF VVGPDDCKGR PLTDVVDQAL RGGATFIQLR AKKADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPRETRALLG DEAIVGLSAE TESLVQLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLAGTKA AGWFAVSAIA GAENPEEATR AMVEGWKAVR GDKKHGYAPR IVAHAPAADT QAAQEGTAAA GSEATEKKFT NAKQAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCKGAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGVSADA LTTAAKAAAD SGVVSANVLS PEEILAGMDA MSEKYTAQGG KLYSTAQE // ID F6CM17_DESK7 Unreviewed; 362 AA. AC F6CM17; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Desku_0543; OS Desulfotomaculum kuznetsovii (strain DSM 6115 / VKM B-1805 / 17). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=760568; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6115 / VKM B-1805 / 17; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Lu M., Saunders E., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Nazina T., RA Ivanova A., Parshina S., Kuever J., Muyzer G., Plugge C., Stams A., RA Woyke T.; RT "Complete sequence of Desulfotomaculum kuznetsovii DSM 6115."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002770; AEG14160.1; -; Genomic_DNA. DR RefSeq; YP_004515961.1; NC_015573.1. DR EnsemblBacteria; AEG14160; AEG14160; Desku_0543. DR GeneID; 10664405; -. DR KEGG; dku:Desku_0543; -. DR KO; K00788; -. DR OMA; NFNRARE; -. DR BioCyc; DKUZ760568:GHV4-556-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 362 AA; 39239 MW; EE5C73C5B354B6A3 CRC64; MGDLYRVLDA NFNRAREGLR VVEEVARFVL DDAGMTIRIR DMRHRLGILQ EGFPGRGAVL VQARDVEGDV AAPAPPAAGE EKTNLIQLVM ANFKRVQEAT RVLEEYARLL PLTAPFKEIR YAAYLVEKEM VSRLVQLDAS EAPSCKPGAR KVDYSLYVIT GDKFSRGRPV VEVARAAIEG GATVLQLREK DFTARQLIDA GHQLRRLTRE KGVTFIVNDR VDVALAVGAD GVHLGQDDLP IGMARRILGP GKIIGISTHS VEQALEAQRQ GADYIGVGPV YETRTKDDVQ APVGVDLVRQ VASVVSIPKV AIGGIKAHNV EEVIAAGADG VAVITAVVAA EDVSGAAREL RSRIDNARRY LP // ID F6CSD6_MARPP Unreviewed; 506 AA. AC F6CSD6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Mar181_1952; OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=491952; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181; RX PubMed=23458837; DOI=10.4056/sigs.2976373; RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., RA Kyrpides N.C., Detter J.C., Copeland A., Lu M., Bruce D., Detter C., RA Tapia R., Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W., RA Sanchez-Amat A.; RT "Complete genome sequence of Marinomonas posidonica type strain (IVIA- RT Po-181(T))."; RL Stand. Genomic Sci. 7:31-43(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002771; AEF54990.1; -; Genomic_DNA. DR RefSeq; YP_004481909.1; NC_015559.1. DR EnsemblBacteria; AEF54990; AEF54990; Mar181_1952. DR GeneID; 10646824; -. DR KEGG; mpc:Mar181_1952; -. DR KO; K14153; -. DR BioCyc; MPOS491952:GI6N-2023-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 506 AA; 55441 MW; D7F5A7D70D939AE7 CRC64; MSKPPVIWCV GGSDSSAHAG LQADLRTGQD LGCHMQSIVT CVTAQNSKVV ELVEPVSVAM FDAQWQVLLD DVYPQAIKVS LLPNHELVVA CSKWLEKIKR QRPEINIVFD PVMAASSETG NRLQQSEAAV DLLTLMLPYV DYITPNLLEF EALTQISAHQ AVNQIAFQII EKYGVSQVSW LLKGGHYADA AATDWWFKGE RVCGFSTEKL SVHNTRGTGC TLSTALSCFL GYDYFADDAI TMAKAYITGA LKTGVQIGQG AGPLGRPGWP EQIENLPEIL MANMRLGQPL PFPMVDVDLM GVYPVVDSIA WLELVLRQGV RMAQLRIKDT DAVGLDEQIQ QAILLGKTHQ AQVFINDHWE KAIKYGAYGV HLGQEDLQVA DLTHIQQAGL RLGVSTHGYF EIARALAFNP SYIALGHIYP TQTKQMPSQP QGLKRLQHYV NLLKGHYPTV AIGGINCERF AAVAATGVNS VALVTAITLA EAPERVTRFL IGEFEQSKEV GNEDIS // ID F6D9D3_THICA Unreviewed; 232 AA. AC F6D9D3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Thicy_1296; OS Thioalkalimicrobium cyclicum (strain DSM 14477 / JCM 11371 / ALM1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Thioalkalimicrobium. OX NCBI_TaxID=717773; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14477 / JCM 11371 / ALM1; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Davenport K., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Kappler U., Woyke T.; RT "Complete sequence of Thioalkalimicrobium cyclicum ALM1."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002776; AEG32060.1; -; Genomic_DNA. DR RefSeq; YP_004537539.1; NC_015581.1. DR EnsemblBacteria; AEG32060; AEG32060; Thicy_1296. DR GeneID; 10720127; -. DR KEGG; tcy:Thicy_1296; -. DR KO; K00788; -. DR OMA; IGISCHT; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 232 AA; 24232 MW; 5B3EF7D2B5644563 CRC64; MHNSQLDLSL YLILDPAQCR LAPLEVALAA ARGGISLIQL RDKRADQQAC LDLAHQLQHR LAALKVPLII NDSVVIAKAV GAAGVHLGQG DGDLATAREI LGADVIIGRT APNAQALQAD ELRFADYVGH GPVYATATKQ NHLPPIGWSG ATAGVALSRK PVVLIGGLRL IDVAQVYQTG AQGLAVASAI CGASDPESIT RQFRQAWSLA VQGLSHPHTG HKPSAANRGS LK // ID F6D9M6_THICA Unreviewed; 319 AA. AC F6D9M6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Thicy_0207; OS Thioalkalimicrobium cyclicum (strain DSM 14477 / JCM 11371 / ALM1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Thioalkalimicrobium. OX NCBI_TaxID=717773; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14477 / JCM 11371 / ALM1; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Davenport K., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Kappler U., Woyke T.; RT "Complete sequence of Thioalkalimicrobium cyclicum ALM1."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002776; AEG30983.1; -; Genomic_DNA. DR RefSeq; YP_004536462.1; NC_015581.1. DR ProteinModelPortal; F6D9M6; -. DR EnsemblBacteria; AEG30983; AEG30983; Thicy_0207. DR GeneID; 10719001; -. DR KEGG; tcy:Thicy_0207; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 319 AA; 34737 MW; 08BC1F3943F9FC12 CRC64; MSGVVPVAVG CLIRNGEVLI GQRLARQSFA GEWEFPGGKL EANETPIEAL VREFKEETGL TTSDWQPLIS YPWTHQLPNG SVQVQLHVYI TEQASGQLSA PEGHLFAWCP LSMLDQRHLL RANKGIVRAL QLPSAYMITG GFHDQQDALS RLEEALKQEV KLVQLRAKHL DKQAYIALAN EMVKHCHGHG AKLIVNTSVA WFDEMPAVDG LQLASSELAA LTHRPIAANK WLGVSTHNAF ELAKATELEA DFALLSPVKA TQTHPDSTPL GWAKFELMTQ ALPIPVYALG GLSLDDLLQA KATGAQGIAA INGLWPQAI // ID F6DFD9_THETG Unreviewed; 206 AA. AC F6DFD9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ththe16_0676; OS Thermus thermophilus (strain SG0.5JP17-16). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=762633; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG0.5JP17-16; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Allgaier M., RA Hugenholtz P., Singer S., Gladden J., Woyke T.; RT "Complete sequence of chromosome of Thermus thermophilus SG0.5JP17- RT 16."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002777; AEG33097.1; -; Genomic_DNA. DR RefSeq; YP_005640224.1; NC_017272.1. DR ProteinModelPortal; F6DFD9; -. DR EnsemblBacteria; AEG33097; AEG33097; Ththe16_0676. DR GeneID; 12260030; -. DR KEGG; tts:Ththe16_0676; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; TTHE762633:GLMG-707-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22689 MW; 77A4FC79F25CD7B2 CRC64; MQGRLYLVVT PRPHWSMGET LDRTERALGG GVEVLQLRAK DWEARPILEL GERMLALARR YGVPFFLNDR PDLAALLGAD GVHLGQGDLT PLEARRFFSG LVGRSTHAPE QALKALEEGA DYLSVGPVWE TPTKPGRKAA GLGYVRWAAE NLKEKPWFAI GGIDLENLDQ VLEAGARRIV VVRAILDAPD PEKAAKAFRE RLYGVA // ID F6DMN1_DESRL Unreviewed; 209 AA. AC F6DMN1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Desru_0138; OS Desulfotomaculum ruminis (strain ATCC 23193 / DSM 2154 / NCIB 8452 / OS DL). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=696281; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Stams A.J.M., RA Plugge C.M., Muyzer G., Kuever J., Parshina S.N., Ivanova A.E., RA Nazina T.N., Brambilla E., Spring S., Klenk H.-P., Woyke T.; RT "Complete sequence of Desulfotomaculum ruminis DSM 2154."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002780; AEG58439.1; -; Genomic_DNA. DR RefSeq; YP_004543725.1; NC_015589.1. DR EnsemblBacteria; AEG58439; AEG58439; Desru_0138. DR GeneID; 10736490; -. DR KEGG; dru:Desru_0138; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22876 MW; 2F3F4BAD337010A6 CRC64; MHHLLTADLY GITAEEYSLG RSNLQVVEKM IEAGIQVIQY REKEKKTREK YLECLKIREL TRQAGVTFIV NDHIDLALLV GADGVHIGQD DLPPEKVREL VGKEMLIGLS THSPEEARAA LGAGVDYLGV GPIFATKTKK DVCDPVGLEY LEYVARNIPL PFVAIGGIKE YNIHQVTARG ARCVALVAEI VGSPDIAAKV QALRQAMMG // ID F6E1M0_SINMK Unreviewed; 217 AA. AC F6E1M0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Sinme_2835; OS Sinorhizobium meliloti (strain AK83). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=693982; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK83; RX PubMed=21569405; DOI=10.1186/1471-2164-12-235; RG US DOE Joint Genome Institute; RA Galardini M., Mengoni A., Brilli M., Pini F., Fioravanti A., Lucas S., RA Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Land M., Hauser L., RA Woyke T., Mikhailova N., Ivanova N., Daligault H., Bruce D., RA Detter C., Tapia R., Han C., Teshima H., Mocali S., Bazzicalupo M., RA Biondi E.G.; RT "Exploring the symbiotic pangenome of the nitrogen-fixing bacterium RT Sinorhizobium meliloti."; RL BMC Genomics 12:235-235(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002781; AEG54542.1; -; Genomic_DNA. DR RefSeq; YP_004550156.1; NC_015590.1. DR ProteinModelPortal; F6E1M0; -. DR EnsemblBacteria; AEG54542; AEG54542; Sinme_2835. DR GeneID; 10727438; -. DR KEGG; smk:Sinme_2835; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR BioCyc; SMEL693982:GJDT-2880-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 217 AA; 22682 MW; 219C4A7B75DEEA83 CRC64; MSNIEDRCRL VLVVPDIADS AERARLVGEA LKGGDVASVI VPQYALSDAD FQKHAEALVP VIQQAGAAAL IEGDTRVAGR AKADGLHIAG GPDALADAIE RHAPKLIVGG GNATDRHHAL EIGELRPDYV FFGRTDGDIK PEAHPKNLAL AEWWASMIEI PCIVMGGTDP QSALAVAETG AEFVALRLAV FGEAGQAPSV VAAVNALLDE KAPRFEG // ID F6E6S5_SINMK Unreviewed; 201 AA. AC F6E6S5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Sinme_4212; OS Sinorhizobium meliloti (strain AK83). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=693982; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK83; RX PubMed=21569405; DOI=10.1186/1471-2164-12-235; RG US DOE Joint Genome Institute; RA Galardini M., Mengoni A., Brilli M., Pini F., Fioravanti A., Lucas S., RA Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Land M., Hauser L., RA Woyke T., Mikhailova N., Ivanova N., Daligault H., Bruce D., RA Detter C., Tapia R., Han C., Teshima H., Mocali S., Bazzicalupo M., RA Biondi E.G.; RT "Exploring the symbiotic pangenome of the nitrogen-fixing bacterium RT Sinorhizobium meliloti."; RL BMC Genomics 12:235-235(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002782; AEG55903.1; -; Genomic_DNA. DR RefSeq; YP_004556783.1; NC_015596.1. DR EnsemblBacteria; AEG55903; AEG55903; Sinme_4212. DR GeneID; 10730252; -. DR KEGG; smk:Sinme_4212; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; SMEL693982:GJDT-4277-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22730 MW; 3F061599E5223593 CRC64; MKLDPFYLIV DSAQWIERLV PLGVRLVQLR IKDRNEEDIR HQIRVARAVC SAHACQLIVN DYWQLAIEEA CDFIHLGQED LAEADLAAIR AARLKLGVST HDEAELAKAL AAEPDYVALG PIYPTILKKM KWAPQGLERL SWWRERVHPL PLVAIGGLNT ERIEGVFAHG ADSAAVVTDI TLNADPEGRT REWIRKTEAW R // ID F6EIR6_AMYSD Unreviewed; 222 AA. AC F6EIR6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AS9A_0536; OS Amycolicicoccus subflavus (strain DSM 45089 / DQS3-9A1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Amycolicicoccus. OX NCBI_TaxID=443218; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45089 / DQS3-9A1; RX PubMed=21725023; DOI=10.1128/JB.05388-11; RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y., RA Wu X.L.; RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an RT actinomycete isolated from crude oil-polluted soil."; RL J. Bacteriol. 193:4538-4539(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002786; AEF38991.1; -; Genomic_DNA. DR RefSeq; YP_004491791.1; NC_015564.1. DR ProteinModelPortal; F6EIR6; -. DR EnsemblBacteria; AEF38991; AEF38991; AS9A_0536. DR GeneID; 10632713; -. DR KEGG; asd:AS9A_0536; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; ASUB443218:GH9R-547-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23575 MW; 7A1DE9481430D8E4 CRC64; MESPRERLRT AQLYLCTDAR RDKDDLAEFA EAALSGGVDI IQLRDKGSPG EKQYGPLEAQ HEIAALAILG AAAKRHGALL AVNDRADIAL AAGADILHLG QDDLPVHYAR KILGERPLIG RSTHNAEQAR DAAIEEGVDY FCVGPCWTTP TKPGRSAAGL GLVRSTADHA PARPWFAIGG IDEERLPEAV ASGAQRIVVV RAITEATDPH AAAQRIKAAL TG // ID F6EVP5_SPHCR Unreviewed; 230 AA. AC F6EVP5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Sphch_1191; OS Sphingobium chlorophenolicum L-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=690566; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L-1; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Pagani I., Turner P., Copley S., Woyke T.; RT "Complete sequence of chromosome 1 of Sphingobium chlorophenolicum L- RT 1."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002798; AEG48881.1; -; Genomic_DNA. DR RefSeq; YP_004553387.1; NC_015593.1. DR EnsemblBacteria; AEG48881; AEG48881; Sphch_1191. DR GeneID; 10741508; -. DR KEGG; sch:Sphch_1191; -. DR KO; K00788; -. DR BioCyc; SCHL690566:GJJA-1213-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 58 62 HMP-PP binding (By similarity). FT REGION 156 158 THZ-P binding (By similarity). FT METAL 91 91 Magnesium (By similarity). FT METAL 110 110 Magnesium (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 159 159 HMP-PP (By similarity). FT BINDING 186 186 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 24256 MW; 0EF1064FC9652CFC CRC64; MTDFTDEELA LDPNFADRFE QGFRPACQLY LISPPAIGAD FADSLAAAFD GGGVAAFQLR LKGLDEDAIA RAAEPLQKLC GERNVAFIVN DSMALAKRLG ADGVHLGQGD GDPKEARRLL GPSVQIGVTC HDSRHLAMEA GEAGADYVAF GAFYPTTTKE THYRPDPSIL GWWTALFELP CVAIGGITAD NAAPLVKAGA DFLAVSGAVW NHPEGPRAGV AAFEGVLARK // ID F6EX79_SPHCR Unreviewed; 188 AA. AC F6EX79; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 22-JAN-2014, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Sphch_2239; OS Sphingobium chlorophenolicum L-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=690566; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L-1; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Pagani I., Turner P., Copley S., Woyke T.; RT "Complete sequence of chromosome 1 of Sphingobium chlorophenolicum L- RT 1."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002798; AEG49900.1; -; Genomic_DNA. DR RefSeq; YP_004554406.1; NC_015593.1. DR EnsemblBacteria; AEG49900; AEG49900; Sphch_2239. DR GeneID; 10742527; -. DR KEGG; sch:Sphch_2239; -. DR KO; K00788; -. DR BioCyc; SCHL690566:GJJA-2281-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 188 AA; 20590 MW; FC5A581E4B744C21 CRC64; MQRRHRKKLP MIWLMTDERV GEADLLAAVA KLPRGKAGII FRHYRTAAKE RRTLFDRVAR IAGKRRLALM LGGTAAQAQA WRADGWHGVD RRRGGKTLIH SMPAHNGREM AAASRCGADL LFLSPLFPTR SHPGAPMLGR VRFAALARLA DMPVIALGGV RPAHRPMLKG LGASGWAAID GLSVQARQ // ID F6F4W9_CHLPS Unreviewed; 212 AA. AC F6F4W9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-APR-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CPS0C_0233; OS Chlamydia psittaci C19/98. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=1112250; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C19/98; RX PubMed=21705611; DOI=10.1128/JB.05382-11; RA Schofl G., Voigt A., Litsche K., Sachse K., Saluz H.P.; RT "Complete genome sequences of four mammalian isolates of Chlamydophila RT psittaci."; RL J. Bacteriol. 193:4258-4258(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002804; AEG85259.1; -; Genomic_DNA. DR RefSeq; YP_005665855.1; NC_017291.1. DR EnsemblBacteria; AEG85259; AEG85259; CPS0C_0233. DR GeneID; 16798467; -. DR KEGG; chc:CPS0C_0233; -. DR KO; K00788; -. DR BioCyc; CPSI1027844:GLAW-217-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22829 MW; 3D460DE4B76332CC CRC64; MEENFFKLIL ITNKQNISVE EYLDFVCACV HSGVTSVQLR EKELSYRELL GFGEALKSML DPLEIPLIVS DSVSVCLDLD ATGVHLGQTD GDVIEARELL GSDKIIGWNV NTLDQLLNAN TLPIDYLGLS AMFATQNKPD ATNLWGFSGL EQAVSLCEHP IVAIGGIDES NAAEVIEAGA AGIAAIGVFH SAQNPGLVTK TLREIVDRGL RC // ID F6F7K4_CHLPS Unreviewed; 212 AA. AC F6F7K4; S4LBY0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-APR-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CP01DC11_0998, CPS0A_0235; OS Chlamydia psittaci 01DC11. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=1112252; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=01DC11; RX PubMed=21705611; DOI=10.1128/JB.05382-11; RA Schofl G., Voigt A., Litsche K., Sachse K., Saluz H.P.; RT "Complete genome sequences of four mammalian isolates of Chlamydophila RT psittaci."; RL J. Bacteriol. 193:4258-4258(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=01DC11; RA Huot-Creasy H., McCracken C.L., Humphries M., Sachse K., Laroucau K., RA Bavoil P., Myers G.S.A.; RT "Genome sequence of Chlamydia psittaci 01DC11."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002805; AEG86237.1; -; Genomic_DNA. DR EMBL; ATKP01000010; EPJ18315.1; -; Genomic_DNA. DR RefSeq; YP_005663907.1; NC_017289.1. DR EnsemblBacteria; AEG86237; AEG86237; CPS0A_0235. DR GeneID; 16798853; -. DR KEGG; chs:CPS0A_0235; -. DR KO; K00788; -. DR BioCyc; CPSI1027846:GLB6-217-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22829 MW; 3D460DE4B76332CC CRC64; MEENFFKLIL ITNKQNISVE EYLDFVCACV HSGVTSVQLR EKELSYRELL GFGEALKSML DPLEIPLIVS DSVSVCLDLD ATGVHLGQTD GDVIEARELL GSDKIIGWNV NTLDQLLNAN TLPIDYLGLS AMFATQNKPD ATNLWGFSGL EQAVSLCEHP IVAIGGIDES NAAEVIEAGA AGIAAIGVFH SAQNPGLVTK TLREIVDRGL RC // ID F6FA20_CHLPS Unreviewed; 212 AA. AC F6FA20; S4L6E5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-APR-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CP02DC15_1008, CPS0B_0231; OS Chlamydia psittaci 02DC15. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=1112254; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=02DC15; RX PubMed=21705611; DOI=10.1128/JB.05382-11; RA Schofl G., Voigt A., Litsche K., Sachse K., Saluz H.P.; RT "Complete genome sequences of four mammalian isolates of Chlamydophila RT psittaci."; RL J. Bacteriol. 193:4258-4258(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=02DC15; RA Huot-Creasy H., McCracken C.L., Humphries M., Sachse K., Laroucau K., RA Bavoil P., Myers G.S.; RT "Genome sequence of Chlamydia psittaci 02DC15."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002806; AEG87211.1; -; Genomic_DNA. DR EMBL; ATKQ01000014; EPJ13639.1; -; Genomic_DNA. DR RefSeq; YP_005666832.1; NC_017292.1. DR EnsemblBacteria; AEG87211; AEG87211; CPS0B_0231. DR GeneID; 12238394; -. DR KEGG; chi:CPS0B_0231; -. DR KO; K00788; -. DR BioCyc; CPSI1027845:GLB8-217-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22829 MW; 3D460DE4B76332CC CRC64; MEENFFKLIL ITNKQNISVE EYLDFVCACV HSGVTSVQLR EKELSYRELL GFGEALKSML DPLEIPLIVS DSVSVCLDLD ATGVHLGQTD GDVIEARELL GSDKIIGWNV NTLDQLLNAN TLPIDYLGLS AMFATQNKPD ATNLWGFSGL EQAVSLCEHP IVAIGGIDES NAAEVIEAGA AGIAAIGVFH SAQNPGLVTK TLREIVDRGL RC // ID F6FFB6_CHLPS Unreviewed; 212 AA. AC F6FFB6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-APR-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CP08DC60_0135, CPS0D_0232; OS Chlamydia psittaci 08DC60. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=1112267; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=08DC60; RX PubMed=21705611; DOI=10.1128/JB.05382-11; RA Schofl G., Voigt A., Litsche K., Sachse K., Saluz H.P.; RT "Complete genome sequences of four mammalian isolates of Chlamydophila RT psittaci."; RL J. Bacteriol. 193:4258-4258(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=08DC60; RA Huot-Creasy H., McCracken C.L., Humphries M., Sachse K., Laroucau K., RA Bavoil P., Myers G.S.; RT "Genome sequence of Chlamydia psittaci 08DC60."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002807; AEG88190.1; -; Genomic_DNA. DR EMBL; ATKY01000010; EPJ25939.1; -; Genomic_DNA. DR RefSeq; YP_005664882.1; NC_017290.1. DR EnsemblBacteria; AEG88190; AEG88190; CPS0D_0232. DR GeneID; 16799893; -. DR KEGG; cht:CPS0D_0232; -. DR KO; K00788; -. DR BioCyc; CPSI1027843:GLB9-217-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22829 MW; 3D460DE4B76332CC CRC64; MEENFFKLIL ITNKQNISVE EYLDFVCACV HSGVTSVQLR EKELSYRELL GFGEALKSML DPLEIPLIVS DSVSVCLDLD ATGVHLGQTD GDVIEARELL GSDKIIGWNV NTLDQLLNAN TLPIDYLGLS AMFATQNKPD ATNLWGFSGL EQAVSLCEHP IVAIGGIDES NAAEVIEAGA AGIAAIGVFH SAQNPGLVTK TLREIVDRGL RC // ID F6FWU6_ISOV2 Unreviewed; 232 AA. AC F6FWU6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Isova_0732; OS Isoptericola variabilis (strain 225). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Promicromonosporaceae; Isoptericola. OX NCBI_TaxID=743718; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=225; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Siebers A., RA Allgaier M., Thelen M., Hugenholtz P., Gladden J., Woyke T.; RT "Complete sequence of Isoptericola variabilis 225."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002810; AEG43518.1; -; Genomic_DNA. DR RefSeq; YP_004541412.1; NC_015588.1. DR EnsemblBacteria; AEG43518; AEG43518; Isova_0732. DR GeneID; 10732332; -. DR KEGG; iva:Isova_0732; -. DR KO; K00788; -. DR BioCyc; IVAR743718:GI39-744-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 57 61 HMP-PP binding (By similarity). FT REGION 155 157 THZ-P binding (By similarity). FT METAL 90 90 Magnesium (By similarity). FT METAL 109 109 Magnesium (By similarity). FT BINDING 89 89 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 158 158 HMP-PP (By similarity). FT BINDING 186 186 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 232 AA; 24292 MW; D61022153A2413C8 CRC64; MTTPSPLGTP APAAAPLDPR ARLADARLYL CTDAREERGD LEDFLHAVLA GGVDVVQLRD KTLDVARELE LQELVARVAS EHGALWAVND RADVARLTGA PVVHMGQRDL PVPAVRALLG PDPVLGRSTH SAEQAAAADA DPAVDYFCVG PLWATPTKPG RPAVGLDLLR TVAASAPATP WFAIGGIDAE RLGAVLDAGA RRVVVVRALT LAANPERAAR ELRERLTAAG PA // ID F6G649_RALS8 Unreviewed; 388 AA. AC F6G649; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=RSPO_c03257; OS Ralstonia solanacearum (strain Po82). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=1031711; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Po82; RX PubMed=21685279; DOI=10.1128/JB.05384-11; RA Xu J., Zheng H.J., Liu L., Pan Z.C., Prior P., Tang B., Xu J.S., RA Zhang H., Tian Q., Zhang L.Q., Feng J.; RT "Complete genome sequence of the plant pathogen Ralstonia solanacearum RT strain Po82."; RL J. Bacteriol. 193:4261-4262(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002819; AEG70548.1; -; Genomic_DNA. DR RefSeq; YP_006031084.1; NC_017574.1. DR EnsemblBacteria; AEG70548; AEG70548; RSPO_c03257. DR GeneID; 12627365; -. DR KEGG; rsn:RSPO_c03257; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR BioCyc; RSOL1031711:GLJ5-3303-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 388 AA; 40606 MW; F4E0AF2C8FA97B26 CRC64; MSVNVLYIST AWPGAVALAA QIVDRHADAF GRAPHAWRVT DRADEATTAA TVLLTADAAQ ADRARAAGAA VVLTETRDGE RIDTVHDRLG TYRFAGAATG EALGERFVAM FGAALALAFE PRDALCVARA WIAEAPADAL AWPARFDTLP RVLEPALPCA ASPELAFAPC PTRLGIYAVV PDADWVERLV ALGVPTVQLR VKSDDMQAVA GQVRRAAAAA RGSTTRLFIN DHWRVALDVH AGRPGGAPDS GLYGIHLGQE DIDDADLPAI RASGLRLGIS THGYAEMLRV APLNPSYLAL GAVFATPTKT MPTVPQGLGR LFAHAAAMRT RVPAPPLVAI GGIDLAAMPR VLQSGVGCVA VVRALTQAED VPAAVQVLQA TFAAHVRA // ID F6GBM7_RALS8 Unreviewed; 198 AA. AC F6GBM7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE SubName: Full=Thiamine-phosphate pyrophosphorylase protein; GN Name=thiE2; OrderedLocusNames=RSPO_m01532; OS Ralstonia solanacearum (strain Po82). OG Plasmid megaplasmid. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=1031711; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Po82; PLASMID=megaplasmid; RX PubMed=21685279; DOI=10.1128/JB.05384-11; RA Xu J., Zheng H.J., Liu L., Pan Z.C., Prior P., Tang B., Xu J.S., RA Zhang H., Tian Q., Zhang L.Q., Feng J.; RT "Complete genome sequence of the plant pathogen Ralstonia solanacearum RT strain Po82."; RL J. Bacteriol. 193:4261-4262(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002820; AEG72167.1; -; Genomic_DNA. DR RefSeq; YP_006032703.1; NC_017575.1. DR EnsemblBacteria; AEG72167; AEG72167; RSPO_m01532. DR GeneID; 12628975; -. DR KEGG; rsn:RSPO_m01532; -. DR OMA; QLMLNGP; -. DR BioCyc; RSOL1031711:GLJ5-4923-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Plasmid. SQ SEQUENCE 198 AA; 21752 MW; 12F41858C8CD3295 CRC64; MKDISLPDFY QITPEPVGSP HFETFFAELT DTLRSGIRLL QLRAKQLGPR EHLDVARRTR DLCRQSGAML MLNGPIDMAR EVGCDGVHLG SDALMSLRSR PVPDTVLLSA ACHSAEQLEQ AARMAVDFVT LSPVLRTRTH PDADPLGWER FTELAQRARV PVFALGGMHP DMLAQAKRAG AWGVAAISAT WCHRSANA // ID F6GCD5_LACS5 Unreviewed; 195 AA. AC F6GCD5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 16. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase; GN OrderedLocusNames=Lacal_1633; OS Lacinutrix sp. (strain 5H-3-7-4). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Lacinutrix. OX NCBI_TaxID=983544; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5H-3-7-4; RX PubMed=21725025; DOI=10.1128/JB.05518-11; RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C., RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M., RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T., RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., RA Antranikian G.; RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of RT the family Flavobacteriaceae."; RL J. Bacteriol. 193:4545-4546(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002825; AEH01481.1; -; Genomic_DNA. DR RefSeq; YP_004579909.1; NC_015638.1. DR EnsemblBacteria; AEH01481; AEH01481; Lacal_1633. DR GeneID; 10779285; -. DR KEGG; lan:Lacal_1633; -. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR BioCyc; LSP983544:GHSZ-1656-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 195 AA; 22890 MW; DCC4B75D66DBFF09 CRC64; MIVLIAPEND IKNEIEILNQ LFQEGLQYYH LRKPNKDFKQ HCDYLNQIDE KYHNRIVVHY FHELINTFNL KGIHFQEQKR KDHIDNPGQY FKNLNMFGKT ISSSFHEPDE LENCYFEFDY HLLSPVFSSI SKQGYKGRGF NVNHIDKTII GMGGVTASNL NEFDKLGYKG VGILGGIWNS NQPMEVFKAI KRHFD // ID F6GCD8_LACS5 Unreviewed; 216 AA. AC F6GCD8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Lacal_1636; OS Lacinutrix sp. (strain 5H-3-7-4). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Lacinutrix. OX NCBI_TaxID=983544; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5H-3-7-4; RX PubMed=21725025; DOI=10.1128/JB.05518-11; RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C., RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M., RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T., RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., RA Antranikian G.; RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of RT the family Flavobacteriaceae."; RL J. Bacteriol. 193:4545-4546(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002825; AEH01484.1; -; Genomic_DNA. DR RefSeq; YP_004579912.1; NC_015638.1. DR EnsemblBacteria; AEH01484; AEH01484; Lacal_1636. DR GeneID; 10779288; -. DR KEGG; lan:Lacal_1636; -. DR KO; K00788; -. DR OMA; HIANIQK; -. DR BioCyc; LSP983544:GHSZ-1659-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23918 MW; D3CBC5B33058C8FD CRC64; MIIPKLHYIS QGDSPKEHIA NIQKACTSGA ELVQLRLKNI SEKKILKQAE EAREITSHFQ TRLIINDHYK IAKAIKAGGV HLGKTDTCPT IARKHLYTWQ IIGGTANTLE ECETLINKNV DYIGLGPFRF TITKDNLSPV LGLDGYKVIL DKLETKTPII GIGGITLEDV PAILETGISG IAVSGEITKD FNKIRTFNQL LNASSTLEQR HTFNKK // ID F6IFZ2_9SPHN Unreviewed; 223 AA. AC F6IFZ2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PP1Y_AT28704; OS Novosphingobium sp. PP1Y. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=702113; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PP1Y; RA D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., RA Notomista E., Paolella G., Di Donato A., Salvatore F.; RT "De Novo Sequencing and Assembly of the Whole Genome of RT Novosphingobium sp. Strain PP1Y."; RL J. Bacteriol. 193:4296-4296(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR856862; CCA93650.1; -; Genomic_DNA. DR RefSeq; YP_004535468.1; NC_015580.1. DR ProteinModelPortal; F6IFZ2; -. DR EnsemblBacteria; CCA93650; CCA93650; PP1Y_AT28704. DR GeneID; 10716214; -. DR KEGG; npp:PP1Y_AT28704; -. DR KO; K00788; -. DR BioCyc; NSP702113:GJD2-2726-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 51 55 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23932 MW; 94B616264E08AC74 CRC64; MTDQIDTDQA EQDEIEREPT LLYLISPLKV DGDFPQRLAR ALDAGPVAAF QFRVKDIDQH EAARLAEPLQ AICAEREVAF IVNDSISLAK RLGADGVHLG QEDGTVEEAR KALGRDAQIG VTCHDSRHLA MEAGDAGADY VAFGAYFPTT TKDVKHKAGL DLLEWWQRIF EIPCVAIGGI TPENCGALVE AGADFLAVSG AVWNGDEAAA VKAFNEAIAA AMP // ID F6ITR4_LACPE Unreviewed; 218 AA. AC F6ITR4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LPE_00964; OS Lactobacillus pentosus MP-10. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1028490; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MP-10; RX PubMed=21705590; DOI=10.1128/JB.05171-11; RA Abriouel H., Benomar N., Perez Pulido R., Canamero M.M., Galvez A.; RT "Annotated genome sequence of Lactobacillus pentosus MP-10, which has RT probiotic potential, from naturally fermented Alorena green table RT olives."; RL J. Bacteriol. 193:4559-4560(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR871780; CCB81952.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 22733 MW; E0EB7F4EF47F853E CRC64; MTLEFEPAQL RAYFVCGTQD VVGRDLETVV QTALDAGITA FQYRDKGASQ LTAAQRLTLG ERLRQRCADA HVPFIVDDDV ELALGLQADG IHVGQSDDRV TQVIERVAGQ LFVGLSCSTL AEIKVANQID GIAYIGSGPI FPTNSKDDAD PVVGLAGLRE LVAASQRPIV AIGGITVDQL PAIAATGAAG AAVISMLAQS PDMAATVKAM LTASEAQL // ID F7JMP5_9FIRM Unreviewed; 211 AA. AC F7JMP5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0988_01512; OS Lachnospiraceae bacterium 1_4_56FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658655; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_4_56FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 1_4_56FAA."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTN01000010; EGN38273.1; -; Genomic_DNA. DR EnsemblBacteria; EGN38273; EGN38273; HMPREF0988_01512. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22933 MW; B83E93B7221D3889 CRC64; MKKFDPSLYF ITDSTNYTEE EFLCRVEQAL KGGVTLLQLR EKNRSTREYI ELAEKVHAIA KRYNVPLIID DRVDVALAMD AEGVHVGAED MPVATARRLM GDDKIVGATA KTVPWAKEAY EQGADYLGVG AIYPTTTKVK TVLTSTDTLR DICNAVPIPA NAIGGLNKGN IDVLTGIPIA GICVVSAIMK ADDPKMATEE LKARAHELAL I // ID F7JWX8_9FIRM Unreviewed; 211 AA. AC F7JWX8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0991_01650; OS Lachnospiraceae bacterium 2_1_58FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658082; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_58FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 2_1_58FAA."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTO01000024; EGN47735.1; -; Genomic_DNA. DR ProteinModelPortal; F7JWX8; -. DR EnsemblBacteria; EGN47735; EGN47735; HMPREF0991_01650. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22887 MW; E3DC0B31E1BE3103 CRC64; MRCDKESLLL YAVTDRSWTK NDTLYHQVEE ALKGGVTFLQ LREKDLNTEN FLQEAEEMKK LCAAYRVPFV INDNVEIART VGADGVHVGQ DDMPAWKVRE ILGEDKIIGV SAQTVEQAIK AEKDGADYLG VGAVFPTSSK ADAVEVEHAT LRDICVAVQI PVVAIGGISA ENVSQLAGTG IDGIAVISAI FAQDFPKLAA EELKKKVEAI Q // ID F7KRI6_9FIRM Unreviewed; 213 AA. AC F7KRI6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0993_01582; OS Lachnospiraceae bacterium 5_1_57FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658085; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_57FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 5_1_57FAA."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTR01000011; EGN39335.1; -; Genomic_DNA. DR ProteinModelPortal; F7KRI6; -. DR EnsemblBacteria; EGN39335; EGN39335; HMPREF0993_01582. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23026 MW; D2C65B4F08DF61DD CRC64; MKCDKKDLLL YAVTDRHWLN GRTLYSQVEE ALKGGATFIQ LREKELDEEH FLEEAKEIKE LCRRYQVPFV INDNVEIALA VDADGVHVGQ SDMEAGDVRA KLGPDKIIGV SAQTVEQAVM AEQNGADYLG VGAVFPTGSK ADALEVSHDT LKAICKAVKI PVIAIGGISK ENILELSGSG ICGIAVISAI FAKDDIEEAA RELRGLTEKM VTA // ID F7KVK5_9FIRM Unreviewed; 196 AA. AC F7KVK5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-MAR-2014, entry version 13. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF0993_02997; OS Lachnospiraceae bacterium 5_1_57FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658085; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_57FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 5_1_57FAA."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTR01000037; EGN34362.1; -; Genomic_DNA. DR EnsemblBacteria; EGN34362; EGN34362; HMPREF0993_02997. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 21561 MW; CB546A629AD743F6 CRC64; MGILGNSEDF YSRVIAVTNR HLCAGPYLEQ IERICRRQPG AVIVREKDMG PEDYELLYRQ VREICQTYGV PCIAHTYAKA ALHVGSRAIH VPLHLLKETP KIRGQFDIIG VSIHGKEEAL LAERLGASYL TAGHIFATDC KKGVAPRGVE FLENVCEAVC LPVYAIGGMK GEIGCVEEMM AHGARGICVM SECMGW // ID F7L143_FUSNU Unreviewed; 206 AA. AC F7L143; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Regulatory protein TENI; GN ORFNames=HMPREF0401_01564; OS Fusobacterium nucleatum subsp. animalis 11_3_2. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=457403; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=11_3_2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., White A.P., RA Crowley S., Surette M., Strauss J.C., Ambrose C.E., Allen-Vercoe E., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Fusobacterium sp. 11_3_2."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACUO01000020; EGN66885.1; -; Genomic_DNA. DR EnsemblBacteria; EGN66885; EGN66885; HMPREF0401_01564. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 24004 MW; D8F9A5B49E95F1E2 CRC64; MIENKIKLNI ISNRKLCENE NLEKQIEKTF SAYQRKIILE NFEIVALTLR EKDLYKNEYL KLVEKIYPIC QKYRIDLILH QNYDLGLDNK YNIKGLHLSY DSFKSLNKNI REELIRKYKK IGVSIHSVDE AKEVENLGAN YVVAGHIFKT DCKKDLEPRG LKFIQELSLI LTIPIFAIGG INQENSHLVI NSGVFGVCMM SSLMRY // ID F7L149_FUSNU Unreviewed; 206 AA. AC F7L149; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0401_01570; OS Fusobacterium nucleatum subsp. animalis 11_3_2. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=457403; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=11_3_2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., White A.P., RA Crowley S., Surette M., Strauss J.C., Ambrose C.E., Allen-Vercoe E., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Fusobacterium sp. 11_3_2."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACUO01000020; EGN66891.1; -; Genomic_DNA. DR EnsemblBacteria; EGN66891; EGN66891; HMPREF0401_01570. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22663 MW; EAB27FEDCA28EE21 CRC64; MKLKDCKIYL VTDEKSCNGK DFYKCIEEAI KGGVKIVQLR EKTLSTKDFF IKALKIKEIC KSYGVVFIIN DRLDIAQAVE ADGVHLGQSD IPIEKAREIL KDKFLIGATA RNIEEAKKAE LLGADYIGSG AIFGTSTKDN AKKLEMEDLK KIVNSVKIPV FAIGGINTNN VSMLKNIGLQ GICSVSGILS EKDCKKAVEN ILKNFN // ID F7L7R2_BACOV Unreviewed; 205 AA. AC F7L7R2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1017_01092; OS Bacteroides ovatus 3_8_47FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=665954; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_8_47FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides ovatus 3_8_47FAA."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWH01000005; EGM96635.1; -; Genomic_DNA. DR EnsemblBacteria; EGM96635; EGM96635; HMPREF1017_01092. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22533 MW; 68FB7104E01764FB CRC64; MVSLQFITHQ TERYSYLESA RMALEGGCKW IQLRMKEAPL EEVEAVALQL KPLCKEHEAI LVLDDHVELA RKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYSSILSQ MKEANIEVPV VAIGGITYED IPAILHTGVN GIALSGTILG ADNPVEETRR ILNHA // ID F7L7R7_BACOV Unreviewed; 202 AA. AC F7L7R7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF1017_01097; OS Bacteroides ovatus 3_8_47FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=665954; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_8_47FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides ovatus 3_8_47FAA."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWH01000005; EGM96640.1; -; Genomic_DNA. DR ProteinModelPortal; F7L7R7; -. DR SMR; F7L7R7; 1-202. DR EnsemblBacteria; EGM96640; EGM96640; HMPREF1017_01097. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23599 MW; 772F8DFC6BF5D5DD CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNKFD ACQDQNYLAV IEHFKKLKKL SD // ID F7LR90_9BACE Unreviewed; 204 AA. AC F7LR90; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1018_02633; OS Bacteroides sp. 2_1_56FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=665938; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_56FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. 2_1_56FAA."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWI01000017; EGN07407.1; -; Genomic_DNA. DR EnsemblBacteria; EGN07407; EGN07407; HMPREF1018_02633. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22105 MW; 23496B89150674DF CRC64; MLSLQFITHQ TENYSYLESA RMALEGGCKW IQLRMKEASP EEVEAVALQL KPLCKAKEAI LILDDHVELA KKLEVDGVHL GKKDMPIGEA RQMLGEAFII GGTANTFEDV KLHHAAGADY LGIGPFRFTT TKKNLSPVLG LEGYTSILAQ MNEADIRIPV VAIGGIVAED IPAIMETGVN GIALSGAILQ APDPVEETKR ILNI // ID F7LR96_9BACE Unreviewed; 202 AA. AC F7LR96; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF1018_02639; OS Bacteroides sp. 2_1_56FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=665938; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_56FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. 2_1_56FAA."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWI01000017; EGN07413.1; -; Genomic_DNA. DR ProteinModelPortal; F7LR96; -. DR SMR; F7LR96; 1-202. DR EnsemblBacteria; EGN07413; EGN07413; HMPREF1018_02639. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23245 MW; A6533F52928C16DB CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHKRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYSGH ISCSCHSVEE VKNKKHFYDY VFMSPVYDSI SKEGYNSPYT AEELRLAAKD KIIDNKVMAL GGITPDNILE VKDFGFGGAV VLGDLWGKFD ACSDQDYLAV IEHFKKLKRM AD // ID F7M717_9BACE Unreviewed; 206 AA. AC F7M717; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0127_03251; OS Bacteroides sp. 1_1_30. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457387; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_30; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. 1_1_30."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADCL01000065; EGN00555.1; -; Genomic_DNA. DR ProteinModelPortal; F7M717; -. DR EnsemblBacteria; EGN00555; EGN00555; HMPREF0127_03251. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22655 MW; C71D2CE7B5A79C06 CRC64; MISLQFITHQ TERYSYLESA RMALEGGCKW IQLRMKDALL EEVEAVALQL KPLCKEHEAI LILDDHVELA KKLEVDGVHL GKKDMPIDQA RQILGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYSSILSQ MKEANIEIPV VAIGGITFED IPAILHTGVN GIALSGTILG ADNPVEETRR IIESDL // ID F7M722_9BACE Unreviewed; 202 AA. AC F7M722; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF0127_03256; OS Bacteroides sp. 1_1_30. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457387; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_30; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides sp. 1_1_30."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADCL01000065; EGN00560.1; -; Genomic_DNA. DR ProteinModelPortal; F7M722; -. DR EnsemblBacteria; EGN00560; EGN00560; HMPREF0127_03256. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23627 MW; 6FBE04FC6BF5D5DD CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDVL HLRKPETPAM YSERLLTLIP DKYHRRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYYGH ISCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQRA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNRFD ACQDQNYLAV IEHFKKLKKL SD // ID F7MCW7_FUSNU Unreviewed; 206 AA. AC F7MCW7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0404_01980; OS Fusobacterium nucleatum subsp. animalis 21_1A. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469601; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21_1A; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 21_1A."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADEE02000002; EGN66416.1; -; Genomic_DNA. DR EnsemblBacteria; EGN66416; EGN66416; HMPREF0404_01980. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22713 MW; F7CA23C35A390138 CRC64; MKLKDCKIYL VTDENSCNGK DFYKCIEESI KGGVKIVQLR EKNISTKDFY EKALKVKEIC KSYGVLFIIN DRLDIAQAVE ADGVHLGQSD MPIEKAREIL KDKFLIGATA RNIEEAKKAE LLGADYIGSG AIFGTSTKDN AKKLEMEDLK KIVNSVKIPV FAIGGINTNN VSMLKNIGLQ GVCSVSGILS EKDCKKAVEN ILKNFN // ID F7MCX3_FUSNU Unreviewed; 206 AA. AC F7MCX3; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF0404_01986; OS Fusobacterium nucleatum subsp. animalis 21_1A. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469601; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21_1A; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 21_1A."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADEE02000002; EGN66422.1; -; Genomic_DNA. DR EnsemblBacteria; EGN66422; EGN66422; HMPREF0404_01986. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 23887 MW; 9F7DA07FE41E87E4 CRC64; MIENKIKLNI ISNRKLCENE NLEKQIEKIF SAYQRKIILE NFEIVALTLR EKDLNKNKYL KLVEKIYSIC QKYRIDLILH QNYDLGLDNK YNIKGLHLSY NTFKSLNKNI REELIRKYKK IGVSIHSVDE AKEVENLGAN YVVAGHIFKT DCKKDLEPRG LKFIQELSLI LTIPIFAIGG INQENSHLVI NSGAFGVCMM SSLMKH // ID F7N3Y7_ECOLX Unreviewed; 211 AA. AC F7N3Y7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PPECC33_39820; OS Escherichia coli PCN033. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1001989; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCN033; RX PubMed=21742868; DOI=10.1128/JB.05551-11; RA Tan C., Xu Z., Zheng H., Liu W., Tang X., Shou J., Wu B., Wang S., RA Zhao G.P., Chen H.; RT "Genome Sequence of a Porcine Extraintestinal Pathogenic Escherichia RT coli Strain."; RL J. Bacteriol. 193:5038-5038(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFAT01000082; EGP22625.1; -; Genomic_DNA. DR EnsemblBacteria; EGP22625; EGP22625; PPECC33_39820. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22987 MW; FFFA0D1B29E1EA43 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVLTLQLRI KDRRDEEAEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLP RAPAVMATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F7NAZ3_XYLFS Unreviewed; 204 AA. AC F7NAZ3; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=XFEB_01571; OS Xylella fastidiosa EB92.1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=945689; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EB92.1; RX PubMed=21914886; DOI=10.1128/JB.05430-11; RA Zhang S., Flores-Cruz Z., Kumar D., Chakrabarty P., Hopkins D.L., RA Gabriel D.W.; RT "The Xylella fastidiosa Biocontrol Strain EB92-1 Genome Is Very RT Similar and Syntenic to Pierce's Disease Strains."; RL J. Bacteriol. 193:5576-5577(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDJ01000090; EGO81632.1; -; Genomic_DNA. DR ProteinModelPortal; F7NAZ3; -. DR EnsemblBacteria; EGO81632; EGO81632; XFEB_01571. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21869 MW; 1DE42CE42C6D56EA CRC64; MPQPRGIYLI TPDETDTARL IAHTAPLLNG IVWLQYRNKL ANTALRTEQA QALLALCRPT GIPLLINDDL ELAQTIGADG VHLGMHDSNA SIARAQLGPH AIIGVSCYNQ IERAKQAIKA GASYVGFGAF YPSHTKTTPY RATPELLRQT THLGVPRVAI GGLTPKNIAP IIEAGAELLA VISGIYSAKN PITALKAYQS QFNI // ID F7NB59_XYLFS Unreviewed; 320 AA. AC F7NB59; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Thiamine monophosphate synthase ThiE; GN Name=thiE; ORFNames=XFEB_01638; OS Xylella fastidiosa EB92.1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=945689; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EB92.1; RX PubMed=21914886; DOI=10.1128/JB.05430-11; RA Zhang S., Flores-Cruz Z., Kumar D., Chakrabarty P., Hopkins D.L., RA Gabriel D.W.; RT "The Xylella fastidiosa Biocontrol Strain EB92-1 Genome Is Very RT Similar and Syntenic to Pierce's Disease Strains."; RL J. Bacteriol. 193:5576-5577(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDJ01000091; EGO81447.1; -; Genomic_DNA. DR ProteinModelPortal; F7NB59; -. DR EnsemblBacteria; EGO81447; EGO81447; XFEB_01638. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 320 AA; 35468 MW; E7754B57E973CFA1 CRC64; MTDSLRSIHV VAAVIADVRG RLLLSRRTEN SDMPGLWEFP GGKRESGETS EQALARELYE ELGISADVGE WLMEVPQLYP GKRLRLEVRR VRAWKGGLRG REGQALTWVE PDKLLRYSMP PADQPVVGML RQPDRYLVTP EPGEQDAEWL DAVEHAYRLG IERIQLRMRQ HDPVRWSGLV RQAVQRRGRA HVEVLLNRDI ALAEALGIGV HLGAEQLAVL DARPLPVGLP VGASCHCLAD LCHAQRIGCD FAVLGPVLPT ESHPGAVTLG WERFEQLREQ VALPIYAIGG MCADQVKEAR RHGAQGIAAM RGLWPGGAKQ // ID F7NKT4_9FIRM Unreviewed; 215 AA. AC F7NKT4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ALO_13514; OS Acetonema longum DSM 6540. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Acetonema. OX NCBI_TaxID=1009370; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 6540; RX PubMed=21673657; DOI=10.1038/emboj.2011.186; RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R., RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J., RA Jensen G.J.; RT "Structural diversity of bacterial flagellar motors."; RL EMBO J. 30:2972-2981(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGF01000119; EGO63388.1; -; Genomic_DNA. DR EnsemblBacteria; EGO63388; EGO63388; ALO_13514. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23576 MW; 6D054EDB963D717C CRC64; MNHASTRRGK WPAADIYGIT AEEYSNGRSN IEVVRAMIDA GVKVIQYREK EKKKLYKYQE CIRIREMTQK AGVTFIINDD IDLALLVKPD GVHIGQEDLP IEEVRQLVGE EMIIGLSTHS PQQAQEAVKR GADYIGVGPV FATRTKKDVS AATGLDYVKY VAEHIPLPSV AIGGIKTDNI ASVRQAGADC FALITDIVGA ADIGARIKEL RARLV // ID F7P1J9_9GAMM Unreviewed; 517 AA. AC F7P1J9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=Rhein_3950; OS Rheinheimera sp. A13L. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Rheinheimera. OX NCBI_TaxID=506534; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A13L; RX PubMed=21742876; DOI=10.1128/JB.05636-11; RA Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.; RT "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from RT Pangong Lake, India."; RL J. Bacteriol. 193:5873-5874(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHI01000072; EGM75958.1; -; Genomic_DNA. DR EnsemblBacteria; EGM75958; EGM75958; Rhein_3950. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 517 AA; 55989 MW; 28242CF90F2BA369 CRC64; MTDSANRANK TTVVWSIAGS DNSAGAGIQA DLKTIQSFST PEQPLHLCTL VTAITAQHSS GVDSCMAVSV AMLHQQAMAL LKDAPPAVIK IGLLVNKLQV LWLAEFLQEL RQQQPELLVI YDPVAISSSG SRMADADLYQ AVMQHLLPQL DLLTPNLPEL EALIKAAPIQ QAVQQLFEFG VKAVLVKGGH DFDTQSCTDE LFVSPQFRYR GYPAYSHQIS LCSPRQQHQF NHGTGCCFSS ALAAALALGY ALEDAFVLAK TYINQGLSQP VAITECSGTL GHWGFPAKPE YLPELLTENL LPPAKAFAPL KAPLGLYVIV PSVAELQRAL AAGVKTLQLR IKSTDQALLR QEIQQAIQLC QQHDIQLFIN DHWQLALELG AYGVHLGQED INSANLATLQ QAGLRLGLSS HGFYKLLRAQ QLKPSYLAIG AVFATQTKEM SGKLQGLQKL ARYPGLFPTT PLVAIGGINQ NNAKAVLVCG IQHLAVVQAF ATAAEPKLWV QQMQQLIAGA QLEQKLC // ID F7P6K5_MYCPC Unreviewed; 223 AA. AC F7P6K5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MAPs_41600; OS Mycobacterium avium subsp. paratuberculosis S397. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=1010838; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S397; RX PubMed=22409516; DOI=10.1186/1471-2164-13-89; RA Bannantine J.P., Wu C.W., Hsu C., Zhou S., Schwartz D.C., Bayles D.O., RA Paustian M.L., Alt D.P., Sreevatsan S., Kapur V., Talaat A.M.; RT "Genome Sequencing of Ovine Isolates of Mycobacterium avium subspecies RT paratuberculosis Offers Insights Into Host Association."; RL BMC Genomics 13:89-89(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFIF01000059; EGO39262.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23306 MW; 11D46F803C2D8C6F CRC64; MHQRLATLAA ARLYLCTDAR RERGDLAEFA DAALAGGVDV IQLRDKGSPG EQRFRPLEAR DELAACEILA DAARRHGALF AVNDRADIAR AAGADVLHLG QGDLPLEVAR AFVGPDVLLG LSSHDRDQMA AAAAGPADYF CVGPCWPTPT KPGRAAPGLA LVRAAAELHT GKPWFAIGGI DAQRLPEVLD AGARRVVVVR AITAADDPAA AARRLSSALA AAR // ID F7PNR1_9EURY Unreviewed; 211 AA. AC F7PNR1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-MAR-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HLRTI_001196, HTIA_1576; OS Halorhabdus tiamatea SARL4B. OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halorhabdus. OX NCBI_TaxID=1033806; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SARL4B; RX PubMed=21705593; DOI=10.1128/JB.05462-11; RA Antunes A., Alam I., Bajic V.B., Stingl U.; RT "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated RT from a deep-sea anoxic brine lake."; RL J. Bacteriol. 193:4553-4554(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SARL4B; RX PubMed=24324765; RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U., RA Bajic V.B.; RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples RT from the Red Sea Extremophiles."; RL PLoS ONE 8:E82210-E82210(2013). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Type strain: SARL4B; RA Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S., RA Ciordia S., Albar J.P., Alcaide M., Yakimov M.M., Antunes A., RA Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V., RA Golyshin P.N., Teeling H.; RT "Halorhabdus tiamatea: Complete genome sequencing and proteomics RT identify the first cultivated euryarchaeon from a deep-sea anoxic RT brine lake as polysaccharide degrader."; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HF571520; CCQ33703.1; -; Genomic_DNA. DR EMBL; AFNT02000010; ERJ06780.1; -; Genomic_DNA. DR RefSeq; YP_008377014.1; NC_021921.1. DR EnsemblBacteria; EGM29240; EGM29240; HLRTI_15530. DR GeneID; 16487376; -. DR KEGG; hti:HTIA_1576; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22084 MW; 0CE233A10676359A CRC64; MTDWDVYLVT QSSLSGERST PEVVQRAIDG GVDVVQLREK DVAARERYEI GQEVRELTRE AGVPLIVNDR LDLALALDAD GVHLGETDLP VAVARDLLGE AAIVGRSVSF VEDARAAERA GVDYLGVGAI YATGSKDDID DDEYAIGTDR LADIVAAVDI PVVGIGGVTS ENAARVIEAG ADGVAVITEI TGADDPAAAT RTLARVVAEA R // ID F7QFK8_9BRAD Unreviewed; 226 AA. AC F7QFK8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 22-JAN-2014, entry version 15. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=CSIRO_0511; OS Bradyrhizobiaceae bacterium SG-6C. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae. OX NCBI_TaxID=709797; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SG-6C; RX PubMed=21742875; DOI=10.1128/JB.05647-11; RA Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G., RA Pandey G.; RT "Genome Sequence of the Newly Isolated Chemolithoautotrophic RT Bradyrhizobiaceae Strain SG-6C."; RL J. Bacteriol. 193:5057-5057(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOF01000007; EGP10077.1; -; Genomic_DNA. DR EnsemblBacteria; EGP10077; EGP10077; CSIRO_0511. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 226 AA; 23315 MW; 992F0A2880F7BDD7 CRC64; MATKPPPQRP APRLYLATPV VADPAQLVAE LPALLAAADV AAVLLRLAHG DERSIIQRAK ALAPPVQAAG AALLIDGHFA QTARAGADGA NVYGIAAMQE AMPSLKPDRI LGVGGLVTRH DAMVAGEAGA DYVLFGEPDA NGERPSADAI CERLDWWAEL FEPPCVAFAT AVEEAGLFAA AGADFVLLGN FIWQDSRGAK TALIEAGKAV ARGFEKSVAQ AAVTGE // ID F7QR81_9BRAD Unreviewed; 202 AA. AC F7QR81; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 22-JAN-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=CSIRO_4102; OS Bradyrhizobiaceae bacterium SG-6C. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae. OX NCBI_TaxID=709797; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SG-6C; RX PubMed=21742875; DOI=10.1128/JB.05647-11; RA Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G., RA Pandey G.; RT "Genome Sequence of the Newly Isolated Chemolithoautotrophic RT Bradyrhizobiaceae Strain SG-6C."; RL J. Bacteriol. 193:5057-5057(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOF01000036; EGP06291.1; -; Genomic_DNA. DR EnsemblBacteria; EGP06291; EGP06291; CSIRO_4102. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 202 AA; 21904 MW; DD9E0B032A07B0C1 CRC64; MPYPDRFYPV VDSVAWVARL TRLGVGTVQL RAKSLDDAAA LAIVKEALAV TKGTQTKLVV NDYWRAAIDA GAQHLHLGQE DLDTADVHAI RRAGLTLGLS THDEDELDNA LAYKPDYIAL GPIYETTLKK MRFAPQGIER ITAWKLLIGD IPLVAIGGIK LEQADKIFAA GANSIAVVSD VTQNADPDAR VRAWLDHASQ PV // ID F7REC4_SHIFL Unreviewed; 211 AA. AC F7REC4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SFJ1713_3797; OS Shigella flexneri J1713. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=754092; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J1713; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOW01000040; EGM60053.1; -; Genomic_DNA. DR ProteinModelPortal; F7REC4; -. DR SMR; F7REC4; 10-208. DR EnsemblBacteria; EGM60053; EGM60053; SFJ1713_3797. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F7RNB9_9GAMM Unreviewed; 613 AA. AC F7RNB9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=SOHN41_01863; OS Shewanella sp. HN-41. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=327275; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HN-41; RX PubMed=21868804; DOI=10.1128/JB.05578-11; RA Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S., RA Hur H.G.; RT "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces RT Arsenic-Sulfide Nanotubes."; RL J. Bacteriol. 193:5039-5040(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HN-41; RA Kim D.-H., Cho Y.-J., Jiang S., Lee J.-H., Chun J., Hur H.-G.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOZ01000022; EGM70269.1; -; Genomic_DNA. DR EnsemblBacteria; EGM70269; EGM70269; SOHN41_01863. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 613 AA; 64751 MW; E21417DE7821B8F6 CRC64; MQDIHGDKLP MNTERPALVW TIAGSDCGGG AGIQADLATI QDLGCHGCSV ITTVTAQSSV AVTLVEPVSA AMLLAQLTTL LSDLPPKAIK IGLLADQTQV GLLADWIASF KIHYPTVPVI VDPVMVASCG DALAADNRLD IKNTAKSALD FKPFRGLIDL ITPNVLELGR LTHSDVSTKA QFAAAALALS QSLDCSVLAK GGDVSFQANA HNIAHDIAHK SNSWDSELAE DYLVCHQVRA SSELHQNGRF WLASQRVNTR HNHGSGCTLS SAIAAVLAQD FVLQDAVVVA KAYVSQGLSA AIGLGQGPGP LARTGWPNDL SRYAKINQCD GNFINNHLNQ HLDIVSDLSA TDQATAQVRI TSTPPQDISS LGFKVLETDL GVYPVVSDLV MLESLLAAGV KTVQLRIKTD SSESTAAELA ESDLGKSALV GSDLDAKIQT AIALGKHFNA QLFINDHWQL AIKHHAFGVH LGQEDLAATD LAAIQAAGLA LGISSHSYFE LLLAHQYSPS YIALGHIFPT TTKQMPSTPQ GLVKLKHYVA LLQDHYPLVA IGGIDLDNLA GVKATGVGNI AVVRAITKAK DPFAAFAELS QAWAQRCVSE VLGAKHELGA KHG // ID F7S1G9_9PROT Unreviewed; 206 AA. AC F7S1G9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=APM_0050; OS Acidiphilium sp. PM. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=1043206; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PM; RX PubMed=21914891; DOI=10.1128/JB.05386-11; RA San Martin-Uriz P., Gomez M.J., Arcas A., Bargiela R., Amils R.; RT "Draft Genome Sequence of the Electricigen Acidiphilium sp. Strain PM RT (DSM 24941)."; RL J. Bacteriol. 193:5585-5586(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFPR01000008; EGO97003.1; -; Genomic_DNA. DR ProteinModelPortal; F7S1G9; -. DR EnsemblBacteria; EGO97003; EGO97003; APM_0050. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21645 MW; 3C40584C425FBD47 CRC64; MTELYLITPP RLGPDFADAL AAALDAGPVA CVQLRLKEAG ADEMRRAIDA LRPVAQSRGV AFLLNDDPRL AVETGCDGAH LGQDDLAAHG GLARVRRVLD GLSLGITCHD SRHLAMEAAE QGADYVAFGA FYPTGTKEPK ARADVEILRW WSELMEVPCV AIGGITPGNA APLVEAGADF LAVVGAVWQH PDGPAAGVRA FRAELA // ID F7SJU8_9GAMM Unreviewed; 315 AA. AC F7SJU8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-MAR-2014, entry version 16. DE SubName: Full=Uncharacterized protein; GN ORFNames=GME_03792; OS Halomonas sp. TD01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=999141; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TD01; RX PubMed=22040376; DOI=10.1186/1475-2859-10-88; RA Cai L., Tan D., Aibaidula G., Dong X.R., Chen J.C., Tian W.D., RA Chen G.Q.; RT "Comparative genomics study of polyhydroxyalkanoates (PHA) and ectoine RT relevant genes from Halomonas sp. TD01 revealed extensive horizontal RT gene transfer events and co-evolutionary relationships."; RL Microb. Cell Fact. 10:88-88(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQW01000013; EGP21085.1; -; Genomic_DNA. DR ProteinModelPortal; F7SJU8; -. DR EnsemblBacteria; EGP21085; EGP21085; GME_03792. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; SQ SEQUENCE 315 AA; 35284 MW; 829597D6D05249DC CRC64; MVKRRVHVAA AAMISADQKR VLIARRPSNV DQGGLWEFPG GKLAPYETGL EGLKRELHEE LGVEIVRARP LIRVHHEYPD KHILLDVWQV QEFAGEPFGR EGQAVRWVPM EELVNYPFPA ANLPILRAVM LPTDYLITGE EADEERFDSL LERALSEDGV RLVQLRAKNL DEAAYIARAE RALRLCRQYD AKLLLNGEPA LLDAVDADGI HLTSARLMDL ERRPIAENKW LSASTHDQKQ LSQAAVLGCD FVTLSPLRTT PSHPEVAPLG WHDFQQLVER AGMPVFALGG MTRFDASHAR AVGAQGIASI RDFWK // ID F7SQ59_9GAMM Unreviewed; 204 AA. AC F7SQ59; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GME_13185; OS Halomonas sp. TD01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=999141; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TD01; RX PubMed=22040376; DOI=10.1186/1475-2859-10-88; RA Cai L., Tan D., Aibaidula G., Dong X.R., Chen J.C., Tian W.D., RA Chen G.Q.; RT "Comparative genomics study of polyhydroxyalkanoates (PHA) and ectoine RT relevant genes from Halomonas sp. TD01 revealed extensive horizontal RT gene transfer events and co-evolutionary relationships."; RL Microb. Cell Fact. 10:88-88(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQW01000062; EGP19122.1; -; Genomic_DNA. DR EnsemblBacteria; EGP19122; EGP19122; GME_13185. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21092 MW; 165283397C8CB348 CRC64; MPFDLSLYLV TDAGLCADIG LEKTVEAAVQ GGVTMVQLRD KYASDEQMIV QAKRLKAMLA GSGVPLMIND RLNVAVASQA DGLHVGQSDM AVQEARNTLG QHAIIGLSIN TLAQLQGAPI ELLDYVGLGP VFATVSKQDH AQPIGFDGLA QLANACQLPS VAIGGLKAEH IAKVKAAGAN GIAVISAICG QPDPRLAAQA FLAQ // ID F7T162_ALCXX Unreviewed; 320 AA. AC F7T162; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-MAR-2014, entry version 15. DE SubName: Full=Uncharacterized protein; GN ORFNames=AXXA_13354; OS Achromobacter xylosoxidans AXX-A. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=1003200; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AXX-A; RA Bador J., Amoureux L., Newirth C.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFRQ01000048; EGP45963.1; -; Genomic_DNA. DR ProteinModelPortal; F7T162; -. DR EnsemblBacteria; EGP45963; EGP45963; AXXA_13354. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 320 AA; 34135 MW; 31144E20C62020CE CRC64; MSDKIIDVAA GLILRPDGML LLGQRPEGKP WSGWWELPGG KLEPGETVLQ ALARELQEEI GIRVTQSRPW VTYVHAYPHT TVRLAFCHVT GWEGEPRSLE NQRLEWVDPA NAASVGDLLP ATLPPLRWLQ LPTAYGISAI GSRAGLSAFL ARLDAALARG VRLVQLREPQ WPDGPASASL HEALQQIVKR CHAAGARVLV NSAHPAAWWR EADGVHLRGA DAARLTARPE LPAGALVGVS AHDNAQVVHA RELGADFAVL GPVLDTPSHP GAPTLGWDGF VEGNRDAGIP VFALGGQSTQ TVSQALRHGA HGIAGIRGLI // ID F7T194_ALCXX Unreviewed; 221 AA. AC F7T194; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AXXA_13514; OS Achromobacter xylosoxidans AXX-A. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=1003200; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AXX-A; RA Bador J., Amoureux L., Newirth C.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFRQ01000050; EGP45918.1; -; Genomic_DNA. DR EnsemblBacteria; EGP45918; EGP45918; AXXA_13514. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23362 MW; DF5002F4C8514157 CRC64; MKALRFPAGL YGVTPEWDDT ERLVRAVRQA ADGGMRALQL RRKDVPDAVR AEQARALAPL CRELGVVFLI NDDWRLALEV GADGAHVGRD DDSLARIRAE AGPDLILGGS SYDDLARARE LLDAGADYIA FGAMFPSRVK PDTVRAPLSV LTEARALVEE RDAPRPAVVA IGGITPENAA LVAAAGADSI AVITGLFEAP AIRAAAAACA APYSINRNLK P // ID F7TD34_PASMD Unreviewed; 221 AA. AC F7TD34; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GEW_07723; OS Pasteurella multocida subsp. gallicida str. Anand1_poultry. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=1032866; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Anand1_poultry; RX PubMed=21914901; DOI=10.1128/JB.05706-11; RA Ahir V.B., Roy A., Jhala M.K., Bhanderi B.B., Mathakiya R.A., RA Bhatt V.D., Padiya K.B., Jakhesara S.J., Koringa P.G., Joshi C.G.; RT "Genome Sequence of Pasteurella multocida subsp. gallicida RT Anand1_poultry."; RL J. Bacteriol. 193:5604-5604(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFRR01000142; EGP05360.1; -; Genomic_DNA. DR EnsemblBacteria; EGP05360; EGP05360; GEW_07723. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23706 MW; 8216E7ECF5E63C82 CRC64; MKPVHAFMRL YFIAGTQDCL HLDGDPAQNL LNILQQALQS GITCYQFREK GKKALQDPDK IKALAIQCRD LCRQYQVPFV VNDDVQLAID IGADGIHVGQ TDMAVADVAA LCHSHCFIGT SVNTLEQGIA AQANPLIDYF GTGPIFPTQS KEDPKPVVGV DFVSTIRAHG IDKPIVAIGG VTAQTAEELR RRGANGVAVI SAITQSADIA KTVKELLGNA Q // ID F7TJT2_PASMD Unreviewed; 221 AA. AC F7TJT2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AAUPMG_07523; OS Pasteurella multocida subsp. multocida str. Anand1_goat. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=1032869; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Anand1_goat; RA Ahir V.B., Roy A., Bhanderi B.B., Jhala M.K., Koringa P.G., RA Jakhesara S.J., Bhatt V.D., Mathakiya R.A., Padiya K.B., Joshi C.G.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFRS01000084; EGP04325.1; -; Genomic_DNA. DR EnsemblBacteria; EGP04325; EGP04325; AAUPMG_07523. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23765 MW; D81445672B5A20B7 CRC64; MKPVHAFMRL YFIAGTQDCL HLDGDPAQNL LNILQQALQS GITCYQFREK GKKALQDRDK IKALAIQCRD LCRQYQVPFV VNDDVQLAID IGADGIHVGQ TDMAVADVAA LCHSHCFIGT SVNTLEQGIA AQANPLIDYF GTGPIFPTQS KEDPKPVVGV DFVSTIRAHG IDKPIVAIGG VTAQTAEELR RRGANGVAVI SAITQSADIA KTVKELLGNA Q // ID F7TWQ0_BRELA Unreviewed; 260 AA. AC F7TWQ0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; ORFNames=BRLA_c23740; OS Brevibacillus laterosporus LMG 15441. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=1042163; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 15441; RX PubMed=21914864; DOI=10.1128/JB.05696-11; RA Djukic M., Poehlein A., Thurmer A., Daniel R.; RT "Genome Sequence of Brevibacillus laterosporus LMG 15441, a Pathogen RT of Invertebrates."; RL J. Bacteriol. 193:5535-5536(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFRV01000003; EGP33900.1; -; Genomic_DNA. DR EnsemblBacteria; EGP33900; EGP33900; BRLA_c23740. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 260 AA; 28896 MW; EA54D6B8171BD548 CRC64; MVPTRSVSYR GSFQTTRNKA YANVFAKGVE FLRARSLHLI TTGRQALREV LPIIEKADQA GVDYLHIREK QRTARELAEW IRLLSDVFPR DRIIVNDRVD VAMTYHCGGV QLGQQSLHAS LAGRMLASHQ LLGCSVHNDQ ECLSVQSLQP SDQYDSLTEH NFVPSRPPTF VIAGHVFVTE CKPGVEPRGL PFVTRMRKLL APSISLLAIG GITPHRVKDV IAAGADGIAV MSGIMQSAQP QERMKEYRDQ LDKTAENAIQ // ID F7TWQ3_BRELA Unreviewed; 227 AA. AC F7TWQ3; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BRLA_c23770; OS Brevibacillus laterosporus LMG 15441. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=1042163; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 15441; RX PubMed=21914864; DOI=10.1128/JB.05696-11; RA Djukic M., Poehlein A., Thurmer A., Daniel R.; RT "Genome Sequence of Brevibacillus laterosporus LMG 15441, a Pathogen RT of Invertebrates."; RL J. Bacteriol. 193:5535-5536(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFRV01000003; EGP33903.1; -; Genomic_DNA. DR EnsemblBacteria; EGP33903; EGP33903; BRLA_c23770. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 24564 MW; CC7703F937DAD8AF CRC64; MKLARLALLS QKWSIYLVIG SQDCGNSVEN MFRILTEALQ AGVGCVQWRE KGAGSISDAI QREQIAIRMK KLCHTYDAIF LINDDVSLAC KVQADGVHVG HEDMPFAQVK QLVPPEMIIG ISAGNIEEAR IALTYGADYL GVGPMYTSKS KTDAGKPIGP NGLSAIRKFV GGYPIVAIGG IKPEHVSCLR KNGADAIAVI SAITQAPDTK KAVQDFIYHV HKNHNYT // ID F7UCT8_RHIRD Unreviewed; 217 AA. AC F7UCT8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Agau_L100351; OS Agrobacterium tumefaciens F2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=1050720; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F2; RX PubMed=21914861; DOI=10.1128/JB.05690-11; RA Li A., Geng J., Cui D., Shu C., Zhang S., Yang J., Xing J., Wang J., RA Ma F., Hu S.; RT "Genome Sequence of Agrobacterium tumefaciens Strain F2, a RT Bioflocculant-Producing Bacterium."; RL J. Bacteriol. 193:5531-5531(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFSD01000003; EGP55266.1; -; Genomic_DNA. DR EnsemblBacteria; EGP55266; EGP55266; Agau_L100351. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 217 AA; 22735 MW; 01A00FBE3D1DC94C CRC64; MTIVEDRCRL VLIVPQSDDA QKQATDVEEA LRGGDVASVI IPQYGLDDAS FQKRAELIVP LVQKAGAAAL IAGDSRVAGR VKADGLHVAG NAEALAEAVE NFTPKMIVGG GNADDRHKAL EQGESNPDYV FFGKLEGDIK PEAHPKNLAL GEWWASMIEI PAIVMGGTDP SSVVAVAETA VEFVAMRSGV FDNAAGAAQA VSEINALLDE KAPRFGG // ID F7UGC8_RHIRD Unreviewed; 220 AA. AC F7UGC8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Agau_L300518; OS Agrobacterium tumefaciens F2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=1050720; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F2; RX PubMed=21914861; DOI=10.1128/JB.05690-11; RA Li A., Geng J., Cui D., Shu C., Zhang S., Yang J., Xing J., Wang J., RA Ma F., Hu S.; RT "Genome Sequence of Agrobacterium tumefaciens Strain F2, a RT Bioflocculant-Producing Bacterium."; RL J. Bacteriol. 193:5531-5531(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFSD01000005; EGP54783.1; -; Genomic_DNA. DR EnsemblBacteria; EGP54783; EGP54783; Agau_L300518. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22916 MW; A2F67076FF938EF0 CRC64; MNKVDYRLNA LVDASLGDVA PLAELALAAA LNGATILQYR DKHGSTREMI ENARAIHEAI AGTGVPLVIN DRVDVALASG ADGVHLGADD MDAETARRIL GEKAIIGLTV KNRADAERAA SMPADYACIG GVFETVSKVN PDKPVGIDGF TLLRGLLREW RPEMPVGAIA GIDLARVPPV VTAGADGVAV ISAIFRAGDI ASATKDFRAA VDTALKARQP // ID F7UL63_SYNYG Unreviewed; 343 AA. AC F7UL63; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 24. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SYNGTS_0407; OS Synechocystis sp. (strain PCC 6803 / GT-S). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechocystis. OX NCBI_TaxID=1111707; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / GT-S; RX PubMed=21803841; DOI=10.1093/dnares/dsr026; RA Tajima N., Sato S., Maruyama F., Kaneko T., Sasaki N.V., Kurokawa K., RA Ohta H., Kanesaki Y., Yoshikawa H., Tabata S., Ikeuchi M., Sato N.; RT "Genomic structure of the cyanobacterium Synechocystis sp. PCC 6803 RT strain GT-S."; RL DNA Res. 18:393-399(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012205; BAK49155.1; -; Genomic_DNA. DR RefSeq; NP_440303.1; NC_000911.1. DR RefSeq; YP_005650360.1; NC_017277.1. DR RefSeq; YP_007450186.1; NC_020286.1. DR ProteinModelPortal; F7UL63; -. DR EnsemblBacteria; BAK49155; BAK49155; SYNGTS_0407. DR GeneID; 12256049; -. DR GeneID; 14615833; -. DR GeneID; 953602; -. DR KEGG; syn:sll0635; -. DR KEGG; syy:SYNGTS_0407; -. DR KEGG; syz:MYO_14110; -. DR KO; K00788; -. DR BioCyc; SSP1148:GJOT-412-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 123 Unknown (By similarity). FT REGION 124 343 Thiamine-phosphate synthase (By FT similarity). FT REGION 171 175 HMP-PP binding (By similarity). FT REGION 268 270 THZ-P binding (By similarity). FT METAL 204 204 Magnesium (By similarity). FT METAL 223 223 Magnesium (By similarity). FT BINDING 203 203 HMP-PP (By similarity). FT BINDING 242 242 HMP-PP (By similarity). FT BINDING 271 271 HMP-PP (By similarity). FT BINDING 298 298 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 343 AA; 37883 MW; 84BE7074EC082056 CRC64; MQQASPTAIA RILDANLNRA REGLRTVEEW CRFALENREL AEECKQLRQA LAPWHQDDLR AARDTPNDVG TQLTHAQEAL RTDVRALLQA NLCRVEEALR VLEEYGKLRD PAMGACCKQL RYRVYALESG LLGSKLVQRL QQCSLYLVTS PQENLLATVE AALQGGLKLV QYRDKDAEDQ LRWQRAKDLR ELCRQYEALF LVNDRVDLAL AVDADGVHLG QQDLPIAVAR QLLGPDKIIG RSTTNPEEMA KAIAEGADYI GVGPVYATPT KAGKKPAGLE YVQYAVTNSP VPWFAIGGID GENLGEVMEA GATQVAIVRA IMETTNPTQA TAQLLTQLSR INP // ID F7V068_EEGSY Unreviewed; 219 AA. AC F7V068; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EGYY_09740; OS Eggerthella sp. (strain YY7918). OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Eggerthella. OX NCBI_TaxID=502558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YY7918; RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.; RT "Complete genome sequence of the equol-producing bacterium Eggerthella RT sp. strain YY7918 isolated from adult human intestine."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012211; BAK44161.1; -; Genomic_DNA. DR RefSeq; YP_004710562.1; NC_015738.1. DR EnsemblBacteria; BAK44161; BAK44161; EGYY_09740. DR GeneID; 10927274; -. DR KEGG; eyy:EGYY_09740; -. DR KO; K00788; -. DR BioCyc; ESP502558:GI1S-887-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 21927 MW; DADC211CBE6C6D45 CRC64; MYPREQLRHA LALYAVTDRS WLGERTLAEC VEEALSGGAT CVQLREKDAP QAEVVLRARA LAPLCRQAGV PLIVNDDVQA ALAAGADGVH VGQSDTACAD ARAALGPDAI VGVSAQTVEQ ALAAQAAGAD YLGVGAVFGT ATKPDAADVG LEKLAAICDA VDIPVVAIGG LNAATIPALA GSGVDGVAVV SAIFAADDIR AATSSLRAIT AKTLGLFAD // ID F7V4L8_CLOSS Unreviewed; 201 AA. AC F7V4L8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN Name=ThiE; OrderedLocusNames=CXIVA_17310; OS Clostridium sp. (strain SY8519). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1042156; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SY8519; RX PubMed=21914882; DOI=10.1128/JB.05637-11; RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.; RT "Complete genomic sequence of the O-desmethylangolensin-producing RT bacterium Clostridium rRNA cluster XIVa strain SY8519, isolated from RT adult human intestine."; RL J. Bacteriol. 193:5568-5569(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012212; BAK47697.1; -; Genomic_DNA. DR RefSeq; YP_004708799.1; NC_015737.1. DR EnsemblBacteria; BAK47697; BAK47697; CXIVA_17310. DR GeneID; 10925283; -. DR KEGG; cls:CXIVA_17310; -. DR KO; K00788; -. DR BioCyc; CSP1042156:GHDR-1775-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 21897 MW; EDB3D03386476BB7 CRC64; MKIIGVTSRK LSREPFLERI RKIVRGHPDA LILREKDLSP EQYRRLAAEV LELCRREQVT GILHSYPAAA RSLQAAALHV PLPALVQMSA EERKSFRVLG ASCHSVEEAR QAEALGCTYL TAGHIFATDC KKGLPGRGAE FLTEVCGAVH IPVYAIGGIT PERLKELRDT GCAGVCVMSS LMGCADPGAL IDALRESDFM E // ID F7V8I1_CLOSS Unreviewed; 220 AA. AC F7V8I1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CXIVA_04740; OS Clostridium sp. (strain SY8519). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1042156; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SY8519; RX PubMed=21914882; DOI=10.1128/JB.05637-11; RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.; RT "Complete genomic sequence of the O-desmethylangolensin-producing RT bacterium Clostridium rRNA cluster XIVa strain SY8519, isolated from RT adult human intestine."; RL J. Bacteriol. 193:5568-5569(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012212; BAK46441.1; -; Genomic_DNA. DR RefSeq; YP_004707543.1; NC_015737.1. DR EnsemblBacteria; BAK46441; BAK46441; CXIVA_04740. DR GeneID; 10924376; -. DR KEGG; cls:CXIVA_04740; -. DR KO; K00788; -. DR BioCyc; CSP1042156:GHDR-496-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24140 MW; 31D039B01FEF72E6 CRC64; MKFDKKSLLL YAVTDRHWLQ GRTLYEAVEQ ALKGGVSFLQ VREKDDMRLS HDEYLKEALQ LRDLCRRYQV PFVIDDDVDL ALETDADGVH VGQNDMEAGN VREKLGPDKI LGVSAHTVKE ALLAQERGAD YLGVGAVFPT DSKDDAEQVD HAVLSEICRA VDIPVIAIGG ITRDNILSLS GTGIAGIAVI SAIFAKKDIQ AAARDLRSQT LKAVNREVNL // ID F7V9U0_9PROT Unreviewed; 201 AA. AC F7V9U0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=ATPR_0139; OS Acetobacter tropicalis NBRC 101654. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=749388; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 101654; RX PubMed=21554859; DOI=10.1016/j.bbrc.2011.04.126; RA Matsutani M., Hirakawa H., Nishikura M., Soemphol W., Ali I.A.I., RA Yakushi T., Matsushita K.; RT "Increased number of Arginine-based salt bridges contributes to the RT thermotolerance of thermotolerant acetic acid bacteria, Acetobacter RT tropicalis SKU1100."; RL Biochem. Biophys. Res. Commun. 409:120-124(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BABS01000002; GAA07135.1; -; Genomic_DNA. DR EnsemblBacteria; GAA07135; GAA07135; ATPR_0139. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 21312 MW; B1530A8DDC719A69 CRC64; MTASDLYLAT PILQDGEAFL PDLVRGLAAQ PPAALLLRLA DAPESRLITQ IQKIQPLVQA QDIALMLEDR PALALKTGCD GVHLSTGFTA SSVRDVRKSI GDALQLGVAV GASRDAAMRA GEDGADYVCF SAEGAEGAVQ DEDEPEDLTA LVRWWCLMME LPAVVLAPEP TDVAGFVQAG ADFIMPAATF WAHPQDWPSL A // ID F7VGC0_9PROT Unreviewed; 207 AA. AC F7VGC0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=ATPR_2419; OS Acetobacter tropicalis NBRC 101654. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=749388; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 101654; RX PubMed=21554859; DOI=10.1016/j.bbrc.2011.04.126; RA Matsutani M., Hirakawa H., Nishikura M., Soemphol W., Ali I.A.I., RA Yakushi T., Matsushita K.; RT "Increased number of Arginine-based salt bridges contributes to the RT thermotolerance of thermotolerant acetic acid bacteria, Acetobacter RT tropicalis SKU1100."; RL Biochem. Biophys. Res. Commun. 409:120-124(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BABS01000089; GAA09415.1; -; Genomic_DNA. DR EnsemblBacteria; GAA09415; GAA09415; ATPR_2419. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 207 AA; 22756 MW; 99FBC15119B6294E CRC64; MSALPQKIYP VVDTAEWVNR LGGAGARFIQ LRIKNYSPEK LVAEIRQAHT YAKQHGVCLV LNDYWQIALD EGIDYLHLGQ EDLDTADLAA IRKAGVRLGI STHCHEELDR ALACAPDYVA LGPIWPTRLK KMAFGPQGVE KLTEWKKLIG DLPLVAIGGI TFERLRACLD AGADSVAAVS DFTLHADPEG QVKRWLTEAD AETRAAV // ID F7W341_SORMK Unreviewed; 523 AA. AC F7W341; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 16. DE SubName: Full=WGS project CABT00000000 data, contig 2.23; GN ORFNames=SMAC_02265; OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / OS K-hell). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; OC Sordaria. OX NCBI_TaxID=771870; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell; TISSUE=Mycelium; RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891; RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K., RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., RA Poeggeler S., Read N., Seiler S., Smith K., Zickler D., Kueck U., RA Freitag M.; RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence RT reads: Sordaria macrospora, a model organism for fungal RT morphogenesis."; RL PLoS Genet. 6:E1000891-E1000891(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CABT02000023; CCC12043.1; -; Genomic_DNA. DR RefSeq; XP_003350552.1; XM_003350504.1. DR ProteinModelPortal; F7W341; -. DR GeneID; 10808100; -. DR KEGG; smp:SMAC_02265; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 523 AA; 55671 MW; 8C78E99A484194D9 CRC64; MDRNSVNYAV YLVTDSTPAI LGDRDLYEVV EASVRGGTTI VQLRDKTSDT GDMIAMGKKL HAITKKYNVP LLINDRIDVA LAVGCEGVHI GQDDMELSTA RRLLGPDAII GVTVSTIEEA MVACKGGADY LGIGTVYATP TKTNTKNIIG AAGVRDILQA MADAGYDHVK TVCIGGINAE NLQRIVYQSE APSKKLDGVA VVSALVAAPD PEAAAKNLVV LFNSLPPFIR EPTGLRGETA DAILKLVPDV VREVANKKPL SHNMTNLVVQ NFAANVALAI GASPIMANYG EEAFDLCKLG GALVVNMGTV DPDGLQNYLK ALRAYNSVGQ PVVYDPVGAG ATTLRRAAVK TILSNGYLDI IKGNEGEIRT VYGIDGHGTI QQRGVDSSSE LDVSQKAELV RKLAAREKDV VVMTGETDYL SDGQHTFRID NGHVYLEMVT GTGCVLGTTI SAFVAAFPQD KLAATVAALL HFEIAAERAA ERKDVQGPGT FVPAFLDELF KIRKETGESK LGWLKSAKLT RLS // ID F7WLA2_MYCTC Unreviewed; 222 AA. AC F7WLA2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 25. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CCDC5079_0388; ORFNames=CFBS_0430; OS Mycobacterium tuberculosis (strain CCDC5079). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=443149; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCDC5079; RX PubMed=21914894; DOI=10.1128/JB.05452-11; RA Zhang Y., Chen C., Liu J., Deng H., Pan A., Zhang L., Zhao X., RA Huang M., Lu B., Dong H., Du P., Chen W., Wan K.; RT "Complete Genome Sequences of Mycobacterium tuberculosis Strains RT CCDC5079 and CCDC5080, Which Belong to the Beijing Family."; RL J. Bacteriol. 193:5591-5592(2011). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCDC5079; RX PubMed=23627759; DOI=10.1186/1471-2164-14-289; RA Tang B., Wang Q., Yang M., Xie F., Zhu Y., Zhuo Y., Wang S., Gao H., RA Ding X., Zhang L., Zhao G., Zheng H.; RT "ContigScape: a Cytoscape plugin facilitating microbial genome gap RT closing."; RL BMC Genomics 14:289-289(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001641; AEJ45578.1; -; Genomic_DNA. DR EMBL; CP002884; AGL98862.1; -; Genomic_DNA. DR RefSeq; YP_005911811.1; NC_017523.1. DR RefSeq; YP_008005266.1; NC_021251.1. DR SMR; F7WLA2; 1-221. DR EnsemblBacteria; AEJ45578; AEJ45578; CCDC5079_0388. DR EnsemblBacteria; AGL98862; AGL98862; CFBS_0430. DR GeneID; 12501864; -. DR GeneID; 15614644; -. DR KEGG; mte:CCDC5079_0388; -. DR KEGG; mtur:CFBS_0430; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; MTUB443149:GLGT-392-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID F7WQ35_MYCTD Unreviewed; 222 AA. AC F7WQ35; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CCDC5180_0383; ORFNames=CFBR_0429; OS Mycobacterium tuberculosis (strain CCDC5180). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=443150; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCDC5180; RX PubMed=21914894; DOI=10.1128/JB.05452-11; RA Zhang Y., Chen C., Liu J., Deng H., Pan A., Zhang L., Zhao X., RA Huang M., Lu B., Dong H., Du P., Chen W., Wan K.; RT "Complete Genome Sequences of Mycobacterium tuberculosis Strains RT CCDC5079 and CCDC5080, Which Belong to the Beijing Family."; RL J. Bacteriol. 193:5591-5592(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCDC5180; RA Wan K., Liu H., Tang B., Jiang Y., Zheng H., Zhang Y., Lv B., Liu Z., RA Zhao X., Dong H., Zhao G.; RT "Beijing/W Lineage of Mycobacterium tuberculosis Develop Totally Drug RT Resistant Phenotype by Reductive Evolution."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001642; AEJ49220.1; -; Genomic_DNA. DR EMBL; CP002885; AHJ53514.1; -; Genomic_DNA. DR RefSeq; YP_005908215.1; NC_017522.1. DR ProteinModelPortal; F7WQ35; -. DR SMR; F7WQ35; 1-221. DR EnsemblBacteria; AEJ49220; AEJ49220; CCDC5180_0383. DR GeneID; 12498220; -. DR KEGG; mtl:CCDC5180_0383; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; MTUB443150:GLGS-387-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID F7X8C6_SINMM Unreviewed; 217 AA. AC F7X8C6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; OrderedLocusNames=SM11_chr2945; OS Sinorhizobium meliloti (strain SM11). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=707241; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM11; RX PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018; RA Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., RA Neuweger H., Stiens M., Vorholter F.J., Weidner S., Goesmann A., RA Puhler A., Schluter A.; RT "The complete genome sequence of the dominant Sinorhizobium meliloti RT field isolate SM11 extends the S. meliloti pan-genome."; RL J. Biotechnol. 155:20-33(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001830; AEH80190.1; -; Genomic_DNA. DR RefSeq; YP_005721451.1; NC_017325.1. DR ProteinModelPortal; F7X8C6; -. DR EnsemblBacteria; AEH80190; AEH80190; SM11_chr2945. DR GeneID; 12309573; -. DR KEGG; smx:SM11_chr2945; -. DR KO; K00788; -. DR BioCyc; SMEL707241:GLKB-2944-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 217 AA; 22682 MW; 219C4A7B75DEEA83 CRC64; MSNIEDRCRL VLVVPDIADS AERARLVGEA LKGGDVASVI VPQYALSDAD FQKHAEALVP VIQQAGAAAL IEGDTRVAGR AKADGLHIAG GPDALADAIE RHAPKLIVGG GNATDRHHAL EIGELRPDYV FFGRTDGDIK PEAHPKNLAL AEWWASMIEI PCIVMGGTDP QSALAVAETG AEFVALRLAV FGEAGQAPSV VAAVNALLDE KAPRFEG // ID F7XIA5_SINMM Unreviewed; 201 AA. AC F7XIA5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 13-NOV-2013, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SM11_pD0091; OS Sinorhizobium meliloti (strain SM11). OG Plasmid pSmeSM11d. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=707241; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM11; PLASMID=pSmeSM11d; RX PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018; RA Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., RA Neuweger H., Stiens M., Vorholter F.J., Weidner S., Goesmann A., RA Puhler A., Schluter A.; RT "The complete genome sequence of the dominant Sinorhizobium meliloti RT field isolate SM11 extends the S. meliloti pan-genome."; RL J. Biotechnol. 155:20-33(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001832; AEH82924.1; -; Genomic_DNA. DR RefSeq; YP_005722425.1; NC_017326.1. DR EnsemblBacteria; AEH82924; AEH82924; SM11_pD0091. DR GeneID; 12313280; -. DR KEGG; smx:SM11_pD0091; -. DR KO; K00788; -. DR BioCyc; SMEL707241:GLKB-5698-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Plasmid; Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22603 MW; F3ADC30F1CFCA429 CRC64; MKLDPFYLIV DSAQWIERLV PLGVKLVQLR IKDRNEEDIR HQLRVARAVC SAHACQLIVN DYWQLAIEEA CDFIHLGQED LAEADLAAIR AAGLKLGVST HDEAELAKAL AAEPDYVALG PIYPTILKKM KWAPQGLERL SWWRERVHPL PLVAIGGLNT ERIEGVFAHG ADSAAVVTDI TLNADPEGRT REWIRKTEAW R // ID F7XY75_MOREP Unreviewed; 218 AA. AC F7XY75; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MEPCIT_429; OS Moranella endobia (strain PCIT). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Candidatus Moranella. OX NCBI_TaxID=903503; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCIT; RA McCutcheon J.P., von Dohlen C.D.; RT "An interdependent metabolic patchwork in the nested three-way RT symbiosis of mealybugs."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCIT; RX PubMed=21835622; DOI=10.1016/j.cub.2011.06.051; RA McCutcheon J.P., von Dohlen C.D.; RT "An interdependent metabolic patchwork in the nested symbiosis of RT mealybugs."; RL Curr. Biol. 21:1366-1372(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002243; AEI75051.1; -; Genomic_DNA. DR RefSeq; YP_004706919.1; NC_015735.1. DR EnsemblBacteria; AEI75051; AEI75051; MEPCIT_429. DR GeneID; 10929926; -. DR KEGG; men:MEPCIT_429; -. DR KO; K00788; -. DR OMA; HIANIQK; -. DR BioCyc; MEND903503:GHNJ-445-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23822 MW; 7B9BA3CAAC81F988 CRC64; MNANHTCAPV PQRIGLYPVV DSLVWLVRIL DAGIKTVQLR IKKLREPQVA AEIEAAVMLG RRYEARVFIN DYWQLAMHYG AYGVHLGQDD MYSADATAIR NAGLRLGLSA HDKTEIVRAL VWQPSYIAIG HIFPTTTKVM TSDYQGLEQL QQLVTELPPI PTVAIGGISC EQVEAVLMCG VGSVAVVSAI TSAPDWRQAI YALQSIIAQQ HGSATIGR // ID F7YGQ2_MESOW Unreviewed; 215 AA. AC F7YGQ2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN OrderedLocusNames=Mesop_1303; OS Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=536019; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 24607 / HAMBI 3007 / WSM2075; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Mavrommatis K.M., RA Tiwari R.P., Howieson J.G., O'Hara G.W., Nandasena K.G., Woyke T.; RT "Complete sequence of Mesorhizobium opportunistum WSM2075."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002279; AEH85786.1; -; Genomic_DNA. DR RefSeq; YP_004609880.1; NC_015675.1. DR ProteinModelPortal; F7YGQ2; -. DR EnsemblBacteria; AEH85786; AEH85786; Mesop_1303. DR GeneID; 10825117; -. DR KEGG; mop:Mesop_1303; -. DR KO; K00788; -. DR BioCyc; MOPP536019:GH56-1313-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Signal. FT SIGNAL 1 22 Potential. FT CHAIN 23 215 Potential. FT /FTId=PRO_5000761370. SQ SEQUENCE 215 AA; 22565 MW; D8C7B5D768FFEAAF CRC64; MNDATPPNRC RIVLIAPPGV PADRIAAAFD GGDVASLILP ENGMDEASFQ AFAEQIVPAA QAAGVAVIIA GDTRIAGRVQ ADGIHVEVSK TELAETIGHF QAKMMVGTGG AKTRDDALEL GETRPDYIFF GRFGYDNKPE PHPRNLSLGR WWADMIQIPC IVMAGSDLAS VETVAATGAE FVALSSAVFA DGVDPQAAIA QANASLDETA PRFED // ID F7YHW6_VIBA7 Unreviewed; 431 AA. AC F7YHW6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 16. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; GN OrderedLocusNames=VAA_00205; OS Vibrio anguillarum (strain ATCC 68554 / 775) (Listonella anguillarum). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=882102; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 68554 / 775; RX PubMed=21576332; DOI=10.1128/IAI.05138-11; RA Naka H., Dias G.M., Thompson C.C., Dubay C., Thompson F.L., RA Crosa J.H.; RT "Complete genome sequence of the marine fish pathogen Vibrio RT anguillarum harboring the pJM1 virulence plasmid and genomic RT comparison with other virulent strains of V. anguillarum and V. RT ordalii."; RL Infect. Immun. 79:2889-2900(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002284; AEH31836.1; -; Genomic_DNA. DR RefSeq; YP_004564878.1; NC_015633.1. DR EnsemblBacteria; AEH31836; AEH31836; VAA_00205. DR GeneID; 10774040; -. DR KEGG; van:VAA_00205; -. DR KO; K00788; -. DR OMA; RIKDSTH; -. DR BioCyc; LANG882102:GIWG-261-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 431 AA; 47804 MW; 480B1032030F2916 CRC64; MIQLLIPRDD IALTAQVQQV LLLAKHHGFD IDDIFLGASP TLYCQLVTPS YSSLIGSDCL ASCEDALSVL TDKPNLFLQY QVNFCAQMPF EHSQKRETCL VKIGLTAADS DDYVDEWYHG EELRSIRYST NAHAADAKSE HFAWVLSLLC LDFPLEDALV VARAAMSVSR ETWPTDSRYF PQLQHSVAGI FADDKQNHIC FPKIDKNIGL YPVVDSAEWV ERLLKFDVKT IQLRIKDSTH PDLESQIIAA IELGQAYQAQ VFINDHWQLA IKHGAFGIHL GQEDLTNVDL AQIAQAGICL GISTHGYYEI LNIASLNPSY IALGHIFPTT TKIMPSKPQG LVRLKLYQQL IESLSCAANS DEVVSAKIPT VAIGGINLEN ALQVWQCDVS GLAVVRAVTE AKSPQLVIDS FNRIIQNRLP SSAEEVCDYA F // ID F7Z4Q9_BACC6 Unreviewed; 214 AA. AC F7Z4Q9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BCO26_1384; OS Bacillus coagulans (strain 2-6). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=941639; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2-6; RX PubMed=21705584; DOI=10.1128/JB.05378-11; RA Su F., Yu B., Sun J., Ou H.Y., Zhao B., Wang L., Qin J., Tang H., RA Tao F., Jarek M., Scharfe M., Ma C., Ma Y., Xu P.; RT "Genome sequence of the thermophilic strain Bacillus coagulans 2-6, an RT efficient producer of high-optical-purity L-lactic acid."; RL J. Bacteriol. 193:4563-4564(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002472; AEH53443.1; -; Genomic_DNA. DR RefSeq; YP_004568829.1; NC_015634.1. DR EnsemblBacteria; AEH53443; AEH53443; BCO26_1384. DR GeneID; 10765075; -. DR KEGG; bck:BCO26_1384; -. DR KO; K00788; -. DR BioCyc; BCOA941639:GHC1-1405-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22521 MW; B813F4CAC56AC96C CRC64; MTAEYLRGAL KLYFIMGSPN CTLPPEQVLE KAIRGGVTLF QFREKGNGAR KGEEKKALGE KLKWICQKNG IPFLVNDDIA LALELDADGV HVGQEDEPLA SVREKLGDKI IGVSAYTLEE ARQAANGGAD YLGVGPIFPT KSKEDAKAAK GTTVIREIRQ NGIRIPIVGI GGIGPGNAKS VIEAGADGVS VISAIAGAED AEAAAVLLKR ELAL // ID F7Z9S1_ROSLO Unreviewed; 214 AA. AC F7Z9S1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; Synonyms=thiE; OrderedLocusNames=RLO149_c008550; OS Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC OS 15278 / OCh 149). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149; RX PubMed=21693016; DOI=10.1186/1471-2164-12-324; RA Kalhoefer D., Thole S., Voget S., Lehmann R., Liesegang H., RA Wollher A., Daniel R., Simon M., Brinkhoff T.; RT "Comparative genome analysis and genome-guided physiological analysis RT of Roseobacter litoralis."; RL BMC Genomics 12:324-324(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002623; AEI92880.1; -; Genomic_DNA. DR RefSeq; YP_004689843.1; NC_015730.1. DR ProteinModelPortal; F7Z9S1; -. DR EnsemblBacteria; AEI92880; AEI92880; RLO149_c008550. DR GeneID; 10949249; -. DR KEGG; rli:RLO149_c008550; -. DR KO; K00788; -. DR BioCyc; RLIT391595:GJEH-854-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22065 MW; 52714878785E96F8 CRC64; MTGQLKDHLR LYLVTDPQLC AQTGIVETVR RAVAGGVTMV QLRAKHATTA QRIDLAMALK AALQGTGVPL VINDDVTAAV AADADGAHIG QGDIAPDKAR AMLGPDRILG LSCETPQTVR DADPAYVDYL GLGPVFGTDT KTDHAQPTGF DGLADLIALS SLPNVAIGGL KPDHIDGVLA SGADGMAVVS AICGQADPKA AARAFHSFKP EHKT // ID F7ZDT2_ROSLO Unreviewed; 198 AA. AC F7ZDT2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; OrderedLocusNames=RLO149_c039660; OS Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC OS 15278 / OCh 149). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149; RX PubMed=21693016; DOI=10.1186/1471-2164-12-324; RA Kalhoefer D., Thole S., Voget S., Lehmann R., Liesegang H., RA Wollher A., Daniel R., Simon M., Brinkhoff T.; RT "Comparative genome analysis and genome-guided physiological analysis RT of Roseobacter litoralis."; RL BMC Genomics 12:324-324(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002623; AEI95867.1; -; Genomic_DNA. DR RefSeq; YP_004692830.1; NC_015730.1. DR ProteinModelPortal; F7ZDT2; -. DR EnsemblBacteria; AEI95867; AEI95867; RLO149_c039660. DR GeneID; 10952334; -. DR KEGG; rli:RLO149_c039660; -. DR KO; K00788; -. DR BioCyc; RLIT391595:GJEH-3939-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 198 AA; 22065 MW; 2555DDE220F5595B CRC64; MTLPRFYPIF DDVAWLRRML PLGVKLVQLR IKDQPQDALR AQLTESRELC RAHSALLVVN DHWQLAIDLD CDWVHLGQED LDAADVAAIR SAGLKLGIST HDKAELARAL ELKPDYVALG PIYPTILKKM KWHQQGVEKL SEWKDRVGDI PLVAIGGMST DRAPGAFDAG ADVVSAVTDI TLHDDPEGRV REWLEVCG // ID F7ZIU2_ROSLO Unreviewed; 206 AA. AC F7ZIU2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine monophosphate synthase-like protein; GN OrderedLocusNames=RLO149_c018210; OS Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC OS 15278 / OCh 149). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149; RX PubMed=21693016; DOI=10.1186/1471-2164-12-324; RA Kalhoefer D., Thole S., Voget S., Lehmann R., Liesegang H., RA Wollher A., Daniel R., Simon M., Brinkhoff T.; RT "Comparative genome analysis and genome-guided physiological analysis RT of Roseobacter litoralis."; RL BMC Genomics 12:324-324(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002623; AEI93811.1; -; Genomic_DNA. DR RefSeq; YP_004690774.1; NC_015730.1. DR ProteinModelPortal; F7ZIU2; -. DR EnsemblBacteria; AEI93811; AEI93811; RLO149_c018210. DR GeneID; 10950204; -. DR KEGG; rli:RLO149_c018210; -. DR KO; K00788; -. DR BioCyc; RLIT391595:GJEH-1809-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22289 MW; D9E332F1C6304979 CRC64; MDLPEKPQLY LITPPEFELS SFPDVLAQVL DTHKVACVRL DLATRDEDTL SRAADALREI THARDIALVL SDHSVLADRL GLDGVHLSDA ARSVRETRKL LGDEAIIGSF CGTSRHDGMS AGEAGADYVC FGPVAASALG DGSYVEQEVF EWWSEVIEVP VVAEGGLDAA RIAQLTPFTD FFAFGEEVWT AENPAQRLGE LLEAMG // ID F7ZR84_CLOAT Unreviewed; 211 AA. AC F7ZR84; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SMB_G0505; OS Clostridium acetobutylicum DSM 1731. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=991791; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1731; RX PubMed=21742891; DOI=10.1128/JB.05596-11; RA Bao G., Wang R., Zhu Y., Dong H., Mao S., Zhang Y., Chen Z., Li Y., RA Ma Y.; RT "Complete Genome Sequence of Clostridium acetobutylicum DSM 1731, a RT Solvent-Producing Strain with Multireplicon Genome Architecture."; RL J. Bacteriol. 193:5007-5008(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002660; AEI34332.1; -; Genomic_DNA. DR RefSeq; YP_004635156.1; NC_015687.1. DR ProteinModelPortal; F7ZR84; -. DR EnsemblBacteria; AEI34332; AEI34332; SMB_G0505. DR GeneID; 10849152; -. DR KEGG; cae:SMB_G0505; -. DR KO; K00788; -. DR BioCyc; CACE991791:GIVN-545-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23159 MW; 8857F93D17AAFCA6 CRC64; MKNVDYKLYL VTDRKVLKER DLYKSIEEAI KGGVTLVQLR EKEMSTLDFY ESALKLKKIT ETYKIPLIIN DRIDIALAIN ADGVHIGQSD MPLIKARELL GKDKIIGVSA HSIEEALEAE RNGATYLGVG AIYNTSTKGD AQAVSLEELK NIKNSVKIPV VGIGGINEEN ANKVIETGVD GISVISGILS AQKIKDKARV MFDIVKKNST K // ID F7ZWU8_CLOAT Unreviewed; 195 AA. AC F7ZWU8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 22-JAN-2014, entry version 18. DE SubName: Full=Thiamine monophosphate synthase; GN Name=thiE; ORFNames=SMB_G2956; OS Clostridium acetobutylicum DSM 1731. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=991791; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1731; RX PubMed=21742891; DOI=10.1128/JB.05596-11; RA Bao G., Wang R., Zhu Y., Dong H., Mao S., Zhang Y., Chen Z., Li Y., RA Ma Y.; RT "Complete Genome Sequence of Clostridium acetobutylicum DSM 1731, a RT Solvent-Producing Strain with Multireplicon Genome Architecture."; RL J. Bacteriol. 193:5007-5008(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002660; AEI33328.1; -; Genomic_DNA. DR RefSeq; YP_004637575.1; NC_015687.1. DR ProteinModelPortal; F7ZWU8; -. DR EnsemblBacteria; AEI33328; AEI33328; SMB_G2956. DR GeneID; 10850504; -. DR KEGG; cae:SMB_G2956; -. DR KO; K00788; -. DR BioCyc; CACE991791:GIVN-3026-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 195 AA; 21204 MW; A665BB197818F6B9 CRC64; MIYVVTNRKL AKNKDLLGCV EKVLKYGACS VILREKDLGY DELYEIAKKI KFITDKHSAK LIVNGSLRVA EEVKAYAYHS SFVNFINNGG SKIIKNGVSI HSLEEAKRAE ENGADYVLAG NIYETACKPG LKGRGLEFVN SISKNITIPE IAIGGISEEN VQELINSGAN GAAVMSSAMK NPAVIKKIIG KLNKK // ID F8AD02_THEID Unreviewed; 207 AA. AC F8AD02; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Thein_2017; OS Thermodesulfatator indicus (strain DSM 15286 / JCM 11887 / CIR29812). OC Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales; OC Thermodesulfobacteriaceae; Thermodesulfatator. OX NCBI_TaxID=667014; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15286 / JCM 11887 / CIR29812; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., RA Saunders L., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Thermodesulfatator indicus DSM 15286."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002683; AEH45868.1; -; Genomic_DNA. DR RefSeq; YP_004626832.1; NC_015681.1. DR EnsemblBacteria; AEH45868; AEH45868; Thein_2017. DR GeneID; 10842297; -. DR KEGG; tid:Thein_2017; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; TIND667014:GI6G-2073-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22085 MW; C34E9209A2A1AF09 CRC64; MSFKEKLRLY VLTDRKLAPE IESVKAALEG GATAIQLRLK NVSTREILEV AKKLRELTRD YGALFFVNDH LDVALAVNAD GVQLGPDDLP VSLAKKIAPH LIVGASVYSL EEALKAEQEG ADYLGAGAVF PTETKSEAQV LGLDGLKKIV ASVKIPVVAI GGINHENVLE VLKTGVCGIA LVSAIMGATD ITMATKKMKD LLNEHSI // ID F8AUF7_BIFLN Unreviewed; 917 AA. AC F8AUF7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE SubName: Full=Thiamine biosynthesis protein; GN ORFNames=BLNIAS_00890; OS Bifidobacterium longum subsp. longum KACC 91563. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=1035817; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KACC 91563; RX PubMed=21742881; DOI=10.1128/JB.05620-11; RA Ham J.S., Lee T., Byun M.J., Lee K.T., Kim M.K., Han G.S., Jeong S.G., RA Oh M.H., Kim D.H., Kim H.; RT "Complete Genome Sequence of Bifidobacterium longum subsp. longum KACC RT 91563."; RL J. Bacteriol. 193:5044-5044(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KACC 91563; RA Ham J.-S., Kim M.-K., Han G.-S., Jeong S.-G., Oh M.-H., Ki D.-H., RA Lee K.-T., Lee T., Byun M.-J., Kim H.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002794; AEI97168.1; -; Genomic_DNA. DR RefSeq; YP_005586919.1; NC_017221.1. DR EnsemblBacteria; AEI97168; AEI97168; BLNIAS_00890. DR GeneID; 12163994; -. DR KEGG; blk:BLNIAS_00890; -. DR KO; K03147; -. DR BioCyc; BLON1035817:GL98-617-MONOMER; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100241 MW; F6B9841BEFABEB8E CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICAASEFP VVVGGGVTAA DMAMLAGTKA AGWFAVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID F8AYE5_FRADG Unreviewed; 251 AA. AC F8AYE5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=FsymDg_3139; OS Frankia symbiont subsp. Datisca glomerata. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=656024; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4085684; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Chertkov O., Teshima H., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Berry A., RA Pawlowski K., Persson T., Vanden Heuvel B., Benson D., Woyke T.; RT "Complete sequence of chromosome of Frankia symbiont of Datisca RT glomerata."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002801; AEH10448.1; -; Genomic_DNA. DR RefSeq; YP_004584369.1; NC_015656.1. DR ProteinModelPortal; F8AYE5; -. DR EnsemblBacteria; AEH10448; AEH10448; FsymDg_3139. DR GeneID; 10783820; -. DR KEGG; fsy:FsymDg_3139; -. DR KO; K00788; -. DR OMA; CTLLQYR; -. DR BioCyc; FSYM656024:GHLT-3163-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 158 160 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 161 161 HMP-PP (By similarity). FT BINDING 194 194 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 251 AA; 26523 MW; 9F2EF2A37B3869FF CRC64; MTQDVDAPRS SYASSYTRSA EAEARLVRLA DARLYLCLGL RPELAAFLDE VVAAGVDVVQ LREKGLEWQL EADGLAVVRQ VARRRGALVA ANDRADLAAF TGVDVLHVGQ HDIPPRLARQ LLGPDVLIGL STHDPDQLAA AIEDPDVDYF CVGPVWATPT KQGRPPVGLE LPRLAARLAP PFTPGAKPWF VTGGVDATTL DDVLDTGARR VVVVRGITQA AEPGPAVTAL ATRLRAALSH HPDGAGGCAE A // ID F8BAW7_LISMM Unreviewed; 214 AA. AC F8BAW7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LMM7_0348; OS Listeria monocytogenes serotype 4a (strain M7). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1030009; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M7; RX PubMed=21742872; DOI=10.1128/JB.05501-11; RA Chen J., Xia Y., Cheng C., Fang C., Shan Y., Jin G., Fang W.; RT "Genome Sequence of the Nonpathogenic Listeria monocytogenes Serovar RT 4a Strain M7."; RL J. Bacteriol. 193:5019-5020(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002816; AEH91354.1; -; Genomic_DNA. DR RefSeq; YP_005946412.1; NC_017537.1. DR ProteinModelPortal; F8BAW7; -. DR EnsemblBacteria; AEH91354; AEH91354; LMM7_0348. DR GeneID; 12537131; -. DR KEGG; lmq:LMM7_0348; -. DR KO; K00788; -. DR BioCyc; LMON1030009:GLFW-364-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22444 MW; 1CA16767F5492E91 CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGVGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEGIRQVI ASCAGKMKIG LSVHSVSEAA EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GIKLPIVGIG GINEKNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GSPS // ID F8BM20_OLICM Unreviewed; 229 AA. AC F8BM20; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 11-DEC-2013, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase ThiE; DE EC=2.5.1.3; GN Name=thiE1; OrderedLocusNames=OCA4_c08020; OS Oligotropha carboxidovorans (strain OM4). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Oligotropha. OX NCBI_TaxID=1031710; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OM4; RX PubMed=21742883; DOI=10.1128/JB.05619-11; RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., RA Meyer O.; RT "Complete genome sequences of the chemolithoautotrophic Oligotropha RT carboxidovorans strains OM4 and OM5."; RL J. Bacteriol. 193:5043-5043(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002821; AEI01949.1; -; Genomic_DNA. DR RefSeq; YP_005949830.1; NC_017538.1. DR ProteinModelPortal; F8BM20; -. DR EnsemblBacteria; AEI01949; AEI01949; OCA4_c08020. DR GeneID; 12540632; -. DR KEGG; oco:OCA4_c08020; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR BioCyc; OCAR1031710:GLI1-802-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 229 AA; 24231 MW; ED734198A12E5A38 CRC64; MAPSRSSAPA QPMPRLYLAT PALDDTAAFA ASLPPLLTAC DVAAVLLRLN EADERTLTSR IKTLAGPVQA AGTALLVEGR QSLAVRGGAD GVHVEGLEQM EDAASLKAQR IVGVGQLHTR HDAMLAGERG ADYLLFGEPS RNGERPSPEA IFERLQWWAE LFEPPCVGYA ATLEEATLFA GSGADFIMAA DFIWNDARGP KAALEEAQAA IRARFEATFS AAAGQVTRS // ID F8BPE3_OLICM Unreviewed; 202 AA. AC F8BPE3; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE SubName: Full=Thiamine-phosphate pyrophosphorylase ThiE; DE EC=2.5.1.3; GN Name=thiE2; OrderedLocusNames=OCA4_c10620; OS Oligotropha carboxidovorans (strain OM4). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Oligotropha. OX NCBI_TaxID=1031710; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OM4; RX PubMed=21742883; DOI=10.1128/JB.05619-11; RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., RA Meyer O.; RT "Complete genome sequences of the chemolithoautotrophic Oligotropha RT carboxidovorans strains OM4 and OM5."; RL J. Bacteriol. 193:5043-5043(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002821; AEI02205.1; -; Genomic_DNA. DR RefSeq; YP_005950086.1; NC_017538.1. DR ProteinModelPortal; F8BPE3; -. DR EnsemblBacteria; AEI02205; AEI02205; OCA4_c10620. DR GeneID; 12540892; -. DR KEGG; oco:OCA4_c10620; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR BioCyc; OCAR1031710:GLI1-1062-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 202 AA; 21831 MW; CBB85739686CB2EA CRC64; MPYPDRFYPV VDSVAWLARL AKLGVGTVQL RTKELDDPQA STLVRDALAA VAGTQTKLVV NDYWRAAIDH GAQHLHLGQE DLVDADLAAI RKAGLTLGIS THDEEELAIA LKARPDYIAL GPIFFTTLKA MRFKPQGIPR ITEWKRAIGT IPLVAIGGIK LEHAADVFAA GADSIAVVSD VTQNADPDAR VRAWLDATME TA // ID F8C3B2_THEGP Unreviewed; 211 AA. AC F8C3B2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TOPB45_0313; OS Thermodesulfobacterium geofontis (strain OPB45). OC Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales; OC Thermodesulfobacteriaceae; Thermodesulfobacterium. OX NCBI_TaxID=795359; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OPB45; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Hamilton-Brehm S., Elkins J., Woyke T.; RT "Complete sequence of Thermodesulfobacterium sp. OPB45."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002829; AEH22426.1; -; Genomic_DNA. DR RefSeq; YP_004627354.1; NC_015682.1. DR EnsemblBacteria; AEH22426; AEH22426; TOPB45_0313. DR GeneID; 10838864; -. DR KEGG; top:TOPB45_0313; -. DR KO; K00788; -. DR BioCyc; TSP795359:GI1V-328-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23633 MW; A245B005C60E32FB CRC64; MKLSGLYVIT DEKLTPYEND EILEKVEKAL KGGAKIVQLR DKSHSDEFLL PYAKALKKLC EKYGAIFIVN DRVSLTLSAN ADGVHLGKED PFIGEVRKIL KDKIIGVSCY GDIRRAKEME FLGASYVAFG SFFPSPTKPE SEIIDKEILL SAKKVLKIPI CAIGGITLDK AEELIKLSAD MVAIVSDIWK AEDIEKRAKK YREIFKKYGK D // ID F8CDR6_MYXFH Unreviewed; 191 AA. AC F8CDR6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 22. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LILAB_33375; OS Myxococcus fulvus (strain ATCC BAA-855 / HW-1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Myxococcus. OX NCBI_TaxID=483219; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-855 / HW-1; RX PubMed=21868801; DOI=10.1128/JB.05516-11; RA Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., RA Li Y.Z.; RT "Genome Sequence of the Halotolerant Marine Bacterium Myxococcus RT fulvus HW-1."; RL J. Bacteriol. 193:5015-5016(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002830; AEI68556.1; -; Genomic_DNA. DR RefSeq; YP_004669634.1; NC_015711.1. DR EnsemblBacteria; AEI68556; AEI68556; LILAB_33375. DR GeneID; 10881153; -. DR KEGG; mfu:LILAB_33375; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; MFUL483219:GJEO-6690-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 16 20 HMP-PP binding (By similarity). FT REGION 113 115 THZ-P binding (By similarity). FT REGION 164 165 THZ-P binding (By similarity). FT METAL 49 49 Magnesium (By similarity). FT METAL 68 68 Magnesium (By similarity). FT BINDING 48 48 HMP-PP (By similarity). FT BINDING 87 87 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 144 144 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 191 AA; 19266 MW; 92C3D177F08AD511 CRC64; MDKAARLVAG GARVVQLRMK RTPVREALAA ARQVVALCRQ EGALCLVNDR VDLALLADAH GVHVGDEDLP AEDARALLGP GRLLGVTVRD GAGARAARAA GADYVGLGPV FPTATKQVPA PVLGLEAFAA VVRESPLPVV GIGGVGLGNI ASVAAAGARC AAVVSDALLA ADITERVRQL ATAFEQGRSG A // ID F8CQI6_MYXFH Unreviewed; 211 AA. AC F8CQI6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-APR-2014, entry version 19. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=LILAB_24115; OS Myxococcus fulvus (strain ATCC BAA-855 / HW-1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Myxococcus. OX NCBI_TaxID=483219; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-855 / HW-1; RX PubMed=21868801; DOI=10.1128/JB.05516-11; RA Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., RA Li Y.Z.; RT "Genome Sequence of the Halotolerant Marine Bacterium Myxococcus RT fulvus HW-1."; RL J. Bacteriol. 193:5015-5016(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002830; AEI66718.1; -; Genomic_DNA. DR RefSeq; YP_004667796.1; NC_015711.1. DR EnsemblBacteria; AEI66718; AEI66718; LILAB_24115. DR GeneID; 10879287; -. DR KEGG; mfu:LILAB_24115; -. DR KO; K00788; -. DR OMA; VITDWRL; -. DR BioCyc; MFUL483219:GJEO-4824-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 211 AA; 21988 MW; B44AA995198BC68D CRC64; MTPPLPRLIV ITDWRLPPQR LRWALSQALD AGPQVALQHR HPEATGRRFF EEARELAALC QQRGNPLFVN GRFDVALRVG AHVHLPAHGP TPEEVRPHLP SGTWISAAVH DVSEAHAARG ADLALVSPVF SPGSKPGDTR PPLGPTGFST LAAALGCPAL ALGGITPARA AELPGAAGSA VISSVLEADD PRAAALSLLA ACAGRAMLRT P // ID F8CYR1_GEOTC Unreviewed; 219 AA. AC F8CYR1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Geoth_1691; OS Geobacillus thermoglucosidasius (strain C56-YS93). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=634956; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C56-YS93; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Brumm P., Kourtz L., Mead D., Woyke T.; RT "Complete sequence of chromosome of Geobacillus thermoglucosidasius RT C56-YS93."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002835; AEH47661.1; -; Genomic_DNA. DR RefSeq; YP_004587742.1; NC_015660.1. DR EnsemblBacteria; AEH47661; AEH47661; Geoth_1691. DR GeneID; 10787854; -. DR KEGG; gth:Geoth_1691; -. DR KO; K00788; -. DR BioCyc; GTHE634956:GHH3-1737-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23147 MW; 70A04CC1DE3FE91B CRC64; MARIAREEMK QRLKVYFIMG SVNCKKSPFE VLTEAIDGGI TLFQFREKGS GALVGEQKYE FAKQLQAICQ KRGIPFIVND DVELALAIDA DGVHIGQDDE DARIVREKIG DKILGVSAHN LAEAQAAAAA GADYIGVGPI YPTKSKADAK QAQGPGMIRL LRDNGIDIPI VGIGGITAEN ASEVMNAGAD GVSVISAIAS APSPLLATKQ LAQTVLNNE // ID F8D125_GEOTC Unreviewed; 202 AA. AC F8D125; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Geoth_3207; OS Geobacillus thermoglucosidasius (strain C56-YS93). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=634956; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C56-YS93; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Brumm P., Kourtz L., Mead D., Woyke T.; RT "Complete sequence of chromosome of Geobacillus thermoglucosidasius RT C56-YS93."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002835; AEH49081.1; -; Genomic_DNA. DR RefSeq; YP_004589162.1; NC_015660.1. DR ProteinModelPortal; F8D125; -. DR EnsemblBacteria; AEH49081; AEH49081; Geoth_3207. DR GeneID; 10789373; -. DR KEGG; gth:Geoth_3207; -. DR KO; K10810; -. DR BioCyc; GTHE634956:GHH3-3256-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 202 AA; 22080 MW; 2814052C216810D2 CRC64; MERQLHIIST GKQPLEQFVA ICARVHPYVD AIHVREKRKT AREISEFLTE LIERGIPPKK IIVNDRIDVA VVFGVKGVQL AHHSLSVHQT KRHFPSLSVG CSVHSLEEAM EAEKSGADYC IYGHIFPTAS KLGAPPRGIE SLRNIVHHVN IPVIAIGGIH SDNAEQVLQA GAHGIAVMSA VFCAKDPVSE AKKLAKIVKK MA // ID F8DC10_HALXS Unreviewed; 222 AA. AC F8DC10; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Halxa_1354; OS Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halopiger. OX NCBI_TaxID=797210; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18323 / JCM 14033 / SH-6; RX PubMed=22675596; DOI=10.4056/sigs.2505605; RA Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A., RA Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N., RA Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., RA Klenk H.P., Kyrpides N., Ivanova N.; RT "Complete genome sequence of Halopiger xanaduensis type strain (SH- RT 6(T))."; RL Stand. Genomic Sci. 6:31-42(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002839; AEH35987.1; -; Genomic_DNA. DR RefSeq; YP_004595866.1; NC_015666.1. DR ProteinModelPortal; F8DC10; -. DR EnsemblBacteria; AEH35987; AEH35987; Halxa_1354. DR GeneID; 10796324; -. DR KEGG; hxa:Halxa_1354; -. DR KO; K00788; -. DR OMA; GLGPICH; -. DR BioCyc; HXAN797210:GIXL-684-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 22548 MW; 04942D45A5F6700B CRC64; MNPPNWQTYL VTQASLSEGR STLEIVEAAI AGGVDAVQLR EKDTDARRRY ELGLEVRELT AEAGVDLIVN DRVDIARAID ADGVHVGQSD LPVAVARGLL GSDAIVGCSA STVAEAREAE AEGADYLGVG TIYGTTSKDV DPEQDGVGPE RVAAIADAVS IPIVGIGGIT ADNAGSVVEA GATGVAVISE ITAADDPRAA TEALAQAVET ATPIENGGIA NE // ID F8DSZ7_ZYMMA Unreviewed; 238 AA. AC F8DSZ7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Zmob_0879; OS Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG OS 404 / NCIMB 8938 / NRRL B-806 / ZM1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=555217; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1; RX PubMed=21725006; DOI=10.1128/JB.05395-11; RA Pappas K.M., Kouvelis V.N., Saunders E., Brettin T.S., Bruce D., RA Detter C., Balakireva M., Han C.S., Savvakis G., Kyrpides N.C., RA Typas M.A.; RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. RT mobilis lectotype strain ATCC 10988."; RL J. Bacteriol. 193:5051-5052(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002850; AEH62716.1; -; Genomic_DNA. DR RefSeq; YP_005621167.1; NC_017262.1. DR ProteinModelPortal; F8DSZ7; -. DR EnsemblBacteria; AEH62716; AEH62716; Zmob_0879. DR GeneID; 12280813; -. DR KEGG; zmm:Zmob_0879; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; ZMOB555217:GLMZ-907-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 158 160 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 161 161 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 238 AA; 25614 MW; B79C390DBF103D9D CRC64; MAENEILTDN DEALDAFTNN YQRPSENPCG LYLISPPEID EHFVERLKKA FDGGDVSAFQ LRLKGLNEHA IARLAEPLQK VCADRDVAFI VNDSVSLAKR LGADGVHLGQ GDGDAAEARV ILGPSAQIGV TCHNSRHLAM IAGEKGADYV AFGAFYPTTS KDVRYYARPE ILSWWATLFE LPSVAIGGIT TENVAPIVKA GADFVAVCAG IWKAKEGEDK AVAHFNTVLD QAVKGEIA // ID F8DWC2_ZYMMA Unreviewed; 196 AA. AC F8DWC2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 11-DEC-2013, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Zmob_1683; OS Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG OS 404 / NCIMB 8938 / NRRL B-806 / ZM1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=555217; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1; RX PubMed=21725006; DOI=10.1128/JB.05395-11; RA Pappas K.M., Kouvelis V.N., Saunders E., Brettin T.S., Bruce D., RA Detter C., Balakireva M., Han C.S., Savvakis G., Kyrpides N.C., RA Typas M.A.; RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. RT mobilis lectotype strain ATCC 10988."; RL J. Bacteriol. 193:5051-5052(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002850; AEH63497.1; -; Genomic_DNA. DR RefSeq; YP_005621948.1; NC_017262.1. DR ProteinModelPortal; F8DWC2; -. DR EnsemblBacteria; AEH63497; AEH63497; Zmob_1683. DR GeneID; 12281004; -. DR KEGG; zmm:Zmob_1683; -. DR KO; K00788; -. DR OMA; NRRDSIM; -. DR BioCyc; ZMOB555217:GLMZ-1739-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 196 AA; 22853 MW; 6CED699F5EB6DD5A CRC64; MNDKLKNTWP RLWLMTDERF GDGLLEAVKK LPQGSGIVFR HYRLPFKIRK NLFEKIQRIA KKRKLVLFLA GSARLAAAWK ADGVHGRFSS QRTARPLLRS QAVHNRRDSI MCRKVDFVFL SPLFSTRSHP GKPFLGRVKF LQLKRSIRQK VFALGGINAK TIRALPACDG FSGIDIWQDD QFRHHRLWSF WANQQR // ID F8E1P0_CORRG Unreviewed; 204 AA. AC F8E1P0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CRES_0951; OS Corynebacterium resistens (strain DSM 45100 / JCM 12819 / GTC 2026). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=662755; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45100 / JCM 12819 / GTC 2026; RX PubMed=22524407; DOI=10.1186/1471-2164-13-141; RA Schroder J., Maus I., Meyer K., Wordemann S., Blom J., Jaenicke S., RA Schneider J., Trost E., Tauch A.; RT "Complete genome sequence, lifestyle, and multi-drug resistance of the RT human pathogen Corynebacterium resistens DSM 45100 isolated from blood RT samples of a leukemia patient."; RL BMC Genomics 13:141-141(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002857; AEI09307.1; -; Genomic_DNA. DR RefSeq; YP_004605471.1; NC_015673.1. DR EnsemblBacteria; AEI09307; AEI09307; CRES_0951. DR GeneID; 10817664; -. DR KEGG; crd:CRES_0951; -. DR KO; K00788; -. DR OMA; RPTPTKN; -. DR BioCyc; CRES662755:GIVW-972-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 16 20 HMP-PP binding (By similarity). FT REGION 121 123 THZ-P binding (By similarity). FT METAL 51 51 Magnesium (By similarity). FT METAL 74 74 Magnesium (By similarity). FT BINDING 50 50 HMP-PP (By similarity). FT BINDING 93 93 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). SQ SEQUENCE 204 AA; 20903 MW; 5CD49519A01B63FC CRC64; MGVATKAAIG GAGIIQIRSK PITVRALTEL AIKVAAAVRE VNPETKVVID DRVDVAAALM AKHNIHGVHI GQDDLDPRLA REVLGPDAII GLTTGTLKLV ENANSYADVI DYVGAGPFRP TPTKNSGREP LGVAGYSPLV EASQVPVVAI GDVHAEDAAD LAATGVAGVA IVRGFMQAAD PAAAARQVKQ AFNSDATPAP HNAE // ID F8E6U7_FLESM Unreviewed; 214 AA. AC F8E6U7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Flexsi_0035; OS Flexistipes sinusarabici (strain DSM 4947 / MAS 10). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Flexistipes. OX NCBI_TaxID=717231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4947 / MAS 10; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Flexistipes sinusarabici DSM 4947."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002858; AEI13733.1; -; Genomic_DNA. DR RefSeq; YP_004602301.1; NC_015672.1. DR EnsemblBacteria; AEI13733; AEI13733; Flexsi_0035. DR GeneID; 10814321; -. DR KEGG; fsi:Flexsi_0035; -. DR KO; K00788; -. DR BioCyc; FSIN717231:GI70-35-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23619 MW; C837A8A303693FD2 CRC64; MCSKNRSEVA DFLKLYLIFE SSMLKLPLDE FMEQVIKGGI TAFQLRDKNV PARKRVENGK KAAEFCKVNN IPFIVNDRLD IARILTADGV HLGDKDIPLD IAGNKFGEFF YGYSCNNSDD VKHAASCNAA YIGIGPIFDT STKRDLREIL DKGKIRELAF AADIPSVGIG GINKTNVDSL KNTGLNGIAV VSAICASENP YRETRILREL VEDL // ID F8E6X5_FLESM Unreviewed; 185 AA. AC F8E6X5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Flexsi_0065; OS Flexistipes sinusarabici (strain DSM 4947 / MAS 10). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Flexistipes. OX NCBI_TaxID=717231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4947 / MAS 10; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Flexistipes sinusarabici DSM 4947."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002858; AEI13761.1; -; Genomic_DNA. DR RefSeq; YP_004602329.1; NC_015672.1. DR EnsemblBacteria; AEI13761; AEI13761; Flexsi_0065. DR GeneID; 10814351; -. DR KEGG; fsi:Flexsi_0065; -. DR KO; K00788; -. DR BioCyc; FSIN717231:GI70-65-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 185 AA; 21060 MW; 13469066077D9233 CRC64; MKKIIFVLDF DTFKDTLFET ALYAAKFDVC IWLRIKGRSG RFVFNTAYKI RKLVPQAHLI LSERADIAHL CSFESVHLNA GSPPPQEIRM FFPDLTVGYS AHSKDEIRET EADYYTLSPL FYTKKNYPVA PLENTDLTGI NKKIYALGGI NSSNISKVKD MGFYGAAGIS FVQELPRIKK FFNQP // ID F8EPI0_RUNSL Unreviewed; 213 AA. AC F8EPI0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Runsl_3247; OS Runella slithyformis (strain ATCC 29530 / DSM 19594 / LMG 11500 / OS NCIMB 11436 / LSU 4). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Runella. OX NCBI_TaxID=761193; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29530 / DSM 19594 / LMG 11500 / NCIMB 11436 / LSU 4; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Zhang X., Misra M., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Faehrich R., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Runella slithyformis DSM RT 19594."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002859; AEI49623.1; -; Genomic_DNA. DR RefSeq; YP_004656755.1; NC_015703.1. DR EnsemblBacteria; AEI49623; AEI49623; Runsl_3247. DR GeneID; 10871780; -. DR KEGG; rsi:Runsl_3247; -. DR KO; K00788; -. DR BioCyc; RSLI761193:GHKZ-3271-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 213 AA; 23337 MW; 9A95FF36D938B4CB CRC64; MNITKKIMGG VYLVIDPGWE STFTFPRLTQ ALKAGISALQ IWDNWPAGMD KLAFIQEVTS LAHARDVPVL INNNPELLGE TPLDGIHFDS PCIAIDQMES TLGRSFLKGI TCGNDLTTVH WANDRHFDYI SFCSLFPSAS ADSCEIVSKE TLQKARKLTK MPIFVAGGIS LENITTLQNC GINGAALISA IMQSADPFEA TQLFNDYFNT VNS // ID F8ESI4_ZYMMT Unreviewed; 238 AA. AC F8ESI4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Zymop_0859; OS Zymomonas mobilis subsp. pomaceae (strain ATCC 29192 / JCM 10191 / OS NBRC 13757 / NCIMB 11200 / NRRL B-4491). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=579138; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29192 / JCM 10191 / NBRC 13757 / NCIMB 11200 / NRRL RC B-4491; RX PubMed=21742897; DOI=10.1128/JB.05273-11; RA Kouvelis V.N., Davenport K.W., Brettin T.S., Bruce D., Detter C., RA Han C.S., Nolan M., Tapia R., Damoulaki A., Kyrpides N.C., Typas M.A., RA Pappas K.M.; RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. RT pomaceae lectotype strain ATCC 29192."; RL J. Bacteriol. 193:5049-5050(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002865; AEI37759.1; -; Genomic_DNA. DR RefSeq; YP_004662049.1; NC_015709.1. DR EnsemblBacteria; AEI37759; AEI37759; Zymop_0859. DR GeneID; 10882794; -. DR KEGG; zmp:Zymop_0859; -. DR KO; K00788; -. DR BioCyc; ZMOB579138:GJDN-889-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 61 65 HMP-PP binding (By similarity). FT REGION 159 161 THZ-P binding (By similarity). FT METAL 94 94 Magnesium (By similarity). FT METAL 113 113 Magnesium (By similarity). FT BINDING 93 93 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 162 162 HMP-PP (By similarity). FT BINDING 189 189 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 238 AA; 25567 MW; FC21447B75774FB6 CRC64; MPENNILNED QDEGLEAFKE NYQRPKDNPC GLYLISPPEI DASFTDRLAK AFDGGPVSAF QLRLKGINEH AIARLAEPLQ KLCEERDVAF IINDSVSLAK RLGADGVHLG QGDGDAAEAR VILGPSAQIG VTCHNSRHLA MEAGEKGADY VAFGAFYPTT SKEVRHYAKP EILSWWATLF ELPSVAIGGI TTANAGVLVK AGADFIATCA GVWKAEEGET KAVENFNALF TATMRGDA // ID F8EWC0_ZYMMT Unreviewed; 202 AA. AC F8EWC0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 11-DEC-2013, entry version 19. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Zymop_1641; OS Zymomonas mobilis subsp. pomaceae (strain ATCC 29192 / JCM 10191 / OS NBRC 13757 / NCIMB 11200 / NRRL B-4491). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=579138; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29192 / JCM 10191 / NBRC 13757 / NCIMB 11200 / NRRL RC B-4491; RX PubMed=21742897; DOI=10.1128/JB.05273-11; RA Kouvelis V.N., Davenport K.W., Brettin T.S., Bruce D., Detter C., RA Han C.S., Nolan M., Tapia R., Damoulaki A., Kyrpides N.C., Typas M.A., RA Pappas K.M.; RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. RT pomaceae lectotype strain ATCC 29192."; RL J. Bacteriol. 193:5049-5050(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002865; AEI38530.1; -; Genomic_DNA. DR RefSeq; YP_004662820.1; NC_015709.1. DR EnsemblBacteria; AEI38530; AEI38530; Zymop_1641. DR GeneID; 10883608; -. DR KEGG; zmp:Zymop_1641; -. DR KO; K00788; -. DR BioCyc; ZMOB579138:GJDN-1704-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 23175 MW; A9DDB9EE25718F61 CRC64; MNRKTKKFLP SLWLMTDERL GESLIPAIKR LPRHSGIIFR HYYLPLKDRK KLFFKIKKIA KKRNIILFLA DSPQRAAAWR ADGVHGSNSL KRTARPLLRS KAIHNQYDIA TAQKCDLVLL SPIFATRSHP GKAPLGRVKF LQLSRFIKPA IIALGGIKAK TLRALPAVSG FAGIDIWQNN ELQSCVIGRR WLYKNNRINR RF // ID F8EWV4_TRECH Unreviewed; 211 AA. AC F8EWV4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-MAR-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Spica_0172; OS Treponema caldaria (strain ATCC 51460 / DSM 7334 / H1) (Spirochaeta OS caldaria). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=744872; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51460 / DSM 7334 / H1; RX PubMed=23961314; DOI=10.4056/sigs.3096473; RA Abt B., Goker M., Scheuner C., Han C., Lu M., Misra M., Lapidus A., RA Nolan M., Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., RA Goodwin L.A., Pitluck S., Liolios K., Pagani I., Ivanova N., RA Mavromatis K., Mikhailova N., Huntemann M., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Rohde M., RA Spring S., Gronow S., Detter J.C., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Woyke T., Klenk H.P.; RT "Genome sequence of the thermophilic fresh-water bacterium Spirochaeta RT caldaria type strain (H1(T)), reclassification of Spirochaeta RT caldaria, Spirochaeta stenostrepta, and Spirochaeta zuelzerae in the RT genus Treponema as Treponema caldaria comb. nov., Treponema RT stenostrepta comb. nov., and Treponema zuelzerae comb. nov., and RT emendation of the genus Treponema."; RL Stand. Genomic Sci. 8:88-105(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002868; AEJ18340.1; -; Genomic_DNA. DR RefSeq; YP_004696848.1; NC_015732.1. DR EnsemblBacteria; AEJ18340; AEJ18340; Spica_0172. DR GeneID; 10945545; -. DR KEGG; scd:Spica_0172; -. DR KO; K00788; -. DR BioCyc; SCAL744872:GHIK-173-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23399 MW; 27AB0185B59C8019 CRC64; MLPFDARLCL ITDRSFCSSD DFFRILEISI DAGVTWVQFR EKSGPNDRDI FELGKKVRAL TARKGVPMIV NDRLDLAMAL EADGIHLGQG DLPLEVAKKL WRPNKIYGLS VQTLEHAERA RHDGADYLGL GSLFPTSSKN DAIMVHHQQI ELIKMIGIPL IGIGGITPER IKEIRNLNLS GVAVISAIWG APDPSAVVKQ FIQQWNSLIT C // ID F8F912_PAEMK Unreviewed; 214 AA. AC F8F912; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=KNP414_03922; OS Paenibacillus mucilaginosus (strain KNP414). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1036673; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KNP414; RA Wang J., Hu S., Hu X., Zhang B., Dong D., Zhang S., Zhao K., Wu D.; RT "Complete genome sequence of Paenibacillus mucilaginosus KNP414."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002869; AEI42460.1; -; Genomic_DNA. DR RefSeq; YP_004642330.1; NC_015690.1. DR ProteinModelPortal; F8F912; -. DR EnsemblBacteria; AEI42460; AEI42460; KNP414_03922. DR GeneID; 10856801; -. DR KEGG; pms:KNP414_03922; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; PMUC1036673:GJD1-3922-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22495 MW; 5CD2F1779A30FAC0 CRC64; MYRSSLHDTL SVYLVTDTAG YEHRSAAEIV RAAVAGGVTL VQLRDKQAQL RDVLPAGREI RELCRSAGIP FVVNDRADLA LLLEADGVHV GQDDLPAQEA RRLLGPDAII GVSAGTMEEA EWAVAQGADY LGVGPVYATA SKKDAGEAIG TDLIARIRSR WPQLPLVGIG GIHQGNAAPV LASGAQGVAV ISAITRQSDP QSAARGLADV CRRR // ID F8FMJ7_PAEMK Unreviewed; 229 AA. AC F8FMJ7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Regulatory protein TenI; GN OrderedLocusNames=KNP414_01516; OS Paenibacillus mucilaginosus (strain KNP414). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1036673; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KNP414; RA Wang J., Hu S., Hu X., Zhang B., Dong D., Zhang S., Zhao K., Wu D.; RT "Complete genome sequence of Paenibacillus mucilaginosus KNP414."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002869; AEI40080.1; -; Genomic_DNA. DR RefSeq; YP_004639950.1; NC_015690.1. DR EnsemblBacteria; AEI40080; AEI40080; KNP414_01516. DR GeneID; 10854395; -. DR KEGG; pms:KNP414_01516; -. DR OMA; ELVNVAM; -. DR BioCyc; PMUC1036673:GJD1-1516-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 229 AA; 23938 MW; 25BF20A09900B413 CRC64; MTHEHPGAAA PPPAGRTHAL HVLTTGRLEL DAAASILSII PAGMIDMLHI REKHRSAHEL AAWYRRLKPL LPPGAALAVN DRLDAALAVR ADAVQLTGAS LSPAEARELA PPGRMRIGCS VHSPEEAAEA AAAGADYVLY GHVYETGSKP GLAPRGLQAL ADTVEACPVP VIAIGGIEPA LVDEVLSTGA AGIAVLSSVF GHPDPAGQLR AFRFGLDRTR HKPRKGWTF // ID F8G569_PSEPU Unreviewed; 314 AA. AC F8G569; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-APR-2014, entry version 21. DE SubName: Full=Uncharacterized protein; GN ORFNames=PPS_4345; OS Pseudomonas putida S16. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1042876; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S16; RX PubMed=21914868; DOI=10.1128/JB.05663-11; RA Yu H., Tang H., Wang L., Yao Y., Wu G., Xu P.; RT "Complete Genome Sequence of the Nicotine-Degrading Pseudomonas putida RT Strain S16."; RL J. Bacteriol. 193:5541-5542(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002870; AEJ14878.1; -; Genomic_DNA. DR RefSeq; YP_004703758.1; NC_015733.1. DR ProteinModelPortal; F8G569; -. DR EnsemblBacteria; AEJ14878; AEJ14878; PPS_4345. DR GeneID; 10939961; -. DR KEGG; ppt:PPS_4345; -. DR KO; K03574; -. DR BioCyc; PPUT1042876:GH0R-4289-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 34333 MW; 99EB0B6DA33AADFE CRC64; MKRIHVVAAV IRGTDGRILI ARRADTQHQG GLWEFPGGKV EEGEGVEAAL ARELREELGI EVSRSRALIK VSHDYPDKQV LLDVREVEAF AGEPHGAEGQ PLEWVAPRDL PQYEFPEANK PIVAAARLPD QYLITPDGLE VPQMLKGIQK AVASGIRLIQ LRAPDMYDPK YRDVAVDAVG LCAGKAQLML KGPLEWLGDF PAAGWHLTAA QLRKYAANGR PFPKERWLAA SCHSAEELAL AEQMGVDFVT LSPVQATRTH PEAVPLGWDE AQRLIAGFNK PVYLLGGVGP GEREQAWEAG AQGVAGIRAF WPEI // ID F8G6N7_PSEPU Unreviewed; 207 AA. AC F8G6N7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-APR-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PPS_4626; OS Pseudomonas putida S16. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1042876; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S16; RX PubMed=21914868; DOI=10.1128/JB.05663-11; RA Yu H., Tang H., Wang L., Yao Y., Wu G., Xu P.; RT "Complete Genome Sequence of the Nicotine-Degrading Pseudomonas putida RT Strain S16."; RL J. Bacteriol. 193:5541-5542(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002870; AEJ15157.1; -; Genomic_DNA. DR RefSeq; YP_004704037.1; NC_015733.1. DR EnsemblBacteria; AEJ15157; AEJ15157; PPS_4626. DR GeneID; 10940240; -. DR KEGG; ppt:PPS_4626; -. DR KO; K00788; -. DR BioCyc; PPUT1042876:GH0R-4568-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21773 MW; 5923FF30FC435F46 CRC64; MKLRGLYAIT DSQLLAGRFL SHVEAALEGG VCLLQYRDKS DDAARRLREA EGLMQLCERY GTQLIINDDA ELAARLGVGV HLGQTDGPLT PARALLGRQA IIGSTCHASL ELAAQAASEG ASYVAFGRFF NSVTKPGAPA ANIELLEQAR AQVKLPIAVI GGITLDNAAP LVAHGADLLA VIHGLFGADS AQKVTRRARA FNALFAS // ID F8G6U2_FRAST Unreviewed; 485 AA. AC F8G6U2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 17. DE SubName: Full=Phosphomethylpyrimidine kinase / Thiamin-phosphate pyrophosphorylase; DE EC=2.7.4.7; GN OrderedLocusNames=F7308_1159; OS Francisella sp. (strain TX077308). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=573569; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TX077308; RA Kuske C.R., Challacombe J.F., Siddaramappa S., Petersen J.M.; RT "The complete genome of Francisella sp. TX077308."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002872; AEI36085.1; -; Genomic_DNA. DR RefSeq; YP_004647685.1; NC_015696.1. DR EnsemblBacteria; AEI36085; AEI36085; F7308_1159. DR GeneID; 10862177; -. DR KEGG; frt:F7308_1159; -. DR KO; K14153; -. DR BioCyc; FSP573569:GHZ6-1193-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 485 AA; 53872 MW; A7C496CB89B119C7 CRC64; MRDIFLTIGG SDSSSGAGIQ ADIKTANNIG VHACTIISCV TAQNSTNILN IEKVSKGIFK EQIQAISKEF KIKVIKTSVL SSTEQIDIVV DLLNDLKDVF YICDPVMVST TGYSLVDYRA VEYSKQKLYP LANILVPNLD EAKMLLDEHV SPNVEIAEIA KAIQEKYNCK SVLLKGGHDS DKNISLDCYY TPEVNYTLTS KRYKLDEKVR GTGCTFASAI ASFLTLGFDV NNSIILAKSY ISNAIKSSQK IASHGFFIVD SKYINKQGLF PKVSVHGKDL SIKFRSINKT GFYPIVDSAD KIPSLANLGV KTIQLRIKSN DSEYIQKHIV EAVEYQNKYG LQLFINDYYE LAIKHKAFGV HLGHEDLLSI DRQTLLKIKN TDIALGLSTH DYYELAIALG VNPSYIALGP IYTTNTKKMK FAPQGINKIH EWLNITNTRL VTIGGIKKRH IQSIANIGVD GIAVVTLIDE ISNYEIQNII KLLEK // ID F8GHS6_NITSI Unreviewed; 322 AA. AC F8GHS6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Nit79A3_0409; OS Nitrosomonas sp. (strain Is79A3). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=261292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Is79A3; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., RA Norton J., Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., RA Woyke T.; RT "Complete sequence of Nitrosomonas sp. Is79A3."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002876; AEJ00293.1; -; Genomic_DNA. DR RefSeq; YP_004693692.1; NC_015731.1. DR ProteinModelPortal; F8GHS6; -. DR EnsemblBacteria; AEJ00293; AEJ00293; Nit79A3_0409. DR GeneID; 10932485; -. DR KEGG; nii:Nit79A3_0409; -. DR KO; K03574; -. DR BioCyc; NSP261292:GH7H-413-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 322 AA; 35682 MW; DA4C611BBA67476F CRC64; MHRLSAPLAE SVPIVEVVAA VILRPDGQFL LARRPGGKVY SGYWEFPGGK VEKNESLLHA LERELWEELG IHIRQAHPWL TRIFTYSHAT VRLHFFRVVE WEGKPSPREK QGLSWQQPHQ VEVSPILPAN GPILQALLLP PVYAITQATE IGIEATLKQI EQALQNGLHL LQIREKQMAK DVLREFSLQV LALAQSYQAK VLINGDAELA REMGADGVHF TSSQLMALPC RPDSEYGLCG ASCHNAEELF AAEQLGLDFV VLGPVQSTQS HPGLTPLGWR RFAALIRDYS LPVYALGGLH PEDLPIAQEM GAHGIAMMRG IV // ID F8GIL5_NITSI Unreviewed; 210 AA. AC F8GIL5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Nit79A3_1703; OS Nitrosomonas sp. (strain Is79A3). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=261292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Is79A3; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., RA Norton J., Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., RA Woyke T.; RT "Complete sequence of Nitrosomonas sp. Is79A3."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002876; AEJ01517.1; -; Genomic_DNA. DR RefSeq; YP_004694916.1; NC_015731.1. DR EnsemblBacteria; AEJ01517; AEJ01517; Nit79A3_1703. DR GeneID; 10933796; -. DR KEGG; nii:Nit79A3_1703; -. DR KO; K00788; -. DR BioCyc; NSP261292:GH7H-1725-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22670 MW; 906E4F5E4D7B1887 CRC64; MRNPKINGLY AITPELENTG GLLDKTRQVL EGGAQLIQYR NKSANRILLK EQAGLLLQLC REYTVPLIIN DYLDLTIEIG ADGLHVGQHD AAIAKARNQL GDDKIIGASC YNNLNLALQA EKEGVDYVAF GAFFPSLTKP NTVSVTMNLI AEAKNKITVP IVGIGGIRLT NAKKVIQSGC AAIAVCNDLF QSVNIKAKAA QYAQLFAETN // ID F8H2D5_PSEUT Unreviewed; 213 AA. AC F8H2D5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PSTAB_3710; OS Pseudomonas stutzeri (strain ATCC 17588 / DSM 5190 / CCUG 11256 / JCM OS 5965 / LMG 11199 / NCIMB 11358 / Stanier 221). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=96563; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17588; RA Yan Y., Chen M., Lu W., Zhang W., Ping S., Lin M.; RT "Complete Genome Sequence of Pseudomonas stutzeri Strain CGMCC RT 1.1803."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17588 / DSM 5190 / CCUG 11256 / JCM 5965 / LMG 11199 / RC NCIMB 11358 / Stanier 221; RA Yan Y., Chen M., Lu W., Zhang W., Ping S., Lin M.; RT "Complete genome sequence of Pseudomonas stutzeri strain CGMCC RT 1.1803."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002881; AEJ06991.1; -; Genomic_DNA. DR RefSeq; YP_004716080.1; NC_015740.1. DR ProteinModelPortal; F8H2D5; -. DR EnsemblBacteria; AEJ06991; AEJ06991; PSTAB_3710. DR GeneID; 10944753; -. DR KEGG; psz:PSTAB_3710; -. DR KO; K00788; -. DR BioCyc; PSTU96563:GHIN-3801-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22683 MW; 99A5EB7B84E94725 CRC64; MKESSRLRGL YAITDSKLLA DGRLLPYVEA ALKGGARLLQ YRDKTSDEAR RLREADALQE LCARHGAQLI INDDAELAAR LGVGLHLGQE DGSLAAARAL LGRQAIIGAT CHAQLPLAEQ AARDGASYVA FGRFFQSHTK PGAPAANHEL LREARARIGL PIVAIGGITL DTAPSLIAEG VQMIAVIHAL FAADSAAEVE RRAQAFSQLF NTP // ID F8HA91_PSEUT Unreviewed; 312 AA. AC F8HA91; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 18. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=PSTAB_3211; OS Pseudomonas stutzeri (strain ATCC 17588 / DSM 5190 / CCUG 11256 / JCM OS 5965 / LMG 11199 / NCIMB 11358 / Stanier 221). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=96563; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17588; RA Yan Y., Chen M., Lu W., Zhang W., Ping S., Lin M.; RT "Complete Genome Sequence of Pseudomonas stutzeri Strain CGMCC RT 1.1803."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17588 / DSM 5190 / CCUG 11256 / JCM 5965 / LMG 11199 / RC NCIMB 11358 / Stanier 221; RA Yan Y., Chen M., Lu W., Zhang W., Ping S., Lin M.; RT "Complete genome sequence of Pseudomonas stutzeri strain CGMCC RT 1.1803."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002881; AEJ06492.1; -; Genomic_DNA. DR RefSeq; YP_004715581.1; NC_015740.1. DR ProteinModelPortal; F8HA91; -. DR EnsemblBacteria; AEJ06492; AEJ06492; PSTAB_3211. DR GeneID; 10944254; -. DR KEGG; psz:PSTAB_3211; -. DR KO; K03574; -. DR BioCyc; PSTU96563:GHIN-3286-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 312 AA; 33598 MW; 09B74A2E0217C5DF CRC64; MKRIHVAAAV IRGPESSVLI AKRPLDKHQG GLWEFPGGKV EDGEGVESAL ARELQEELGI EVTQAQPLIQ VRHDYPDKQV LLDVWEVLAF AGEPHGAEGQ PLAWVAPEEL VDYSFPAANQ PIVTAARLPQ HYLITPDGLA VPRLLEGIAR ALDAGIRLIQ LRAPSLPPAD YRTLAERVLA LCAGRAQLML KGPLEWVEDF PGAGWHLTAE QLRRAGSGRP VQAQRWLAAS CHGAEELALA AALEVDFVTL SPVQSTATHP GAPTLGWQRA ADLLSGFDRP VFLLGGLQAG DMGRARQIGA QGIAAIRAFW PD // ID F8HT92_LEUS2 Unreviewed; 211 AA. AC F8HT92; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LGMK_08365; OS Leuconostoc sp. (strain C2). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=979982; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C2; RX PubMed=21914872; DOI=10.1128/JB.05707-11; RA Lee S.H., Jung J.Y., Lee S.H., Jeon C.O.; RT "Complete genome sequence of Leuconostoc kimchii strain C2, isolated RT from Kimchi."; RL J. Bacteriol. 193:5548-5548(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002898; AEJ31722.1; -; Genomic_DNA. DR RefSeq; YP_004706345.1; NC_015734.1. DR EnsemblBacteria; AEJ31722; AEJ31722; LGMK_08365. DR GeneID; 10931868; -. DR KEGG; lec:LGMK_08365; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR BioCyc; LSP979982:GHM6-1734-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23405 MW; 62DA552825807F1B CRC64; MVDKNIDYSL YLITNRYDSS DEQFLNIVFE ACNSGVTLVQ LREKDVTTKR YFDLAVAVKK ITDKFKVPLI IDDRVDICLA VNAAGVHIGD NELPVKRVRQ LIGKDKILGV SVKDVERAKE SEAQGADYFG VGAIYPTKTK VITKHTTMAT LKDIVYNVAI PVNAIGGIKE DNILSFKNTG ISGVCMVSEI MQAENVRTKV TNCLKNVEQL M // ID F8HTS2_LEUS2 Unreviewed; 212 AA. AC F8HTS2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LGMK_07320; OS Leuconostoc sp. (strain C2). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=979982; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C2; RX PubMed=21914872; DOI=10.1128/JB.05707-11; RA Lee S.H., Jung J.Y., Lee S.H., Jeon C.O.; RT "Complete genome sequence of Leuconostoc kimchii strain C2, isolated RT from Kimchi."; RL J. Bacteriol. 193:5548-5548(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002898; AEJ31514.1; -; Genomic_DNA. DR RefSeq; YP_004706137.1; NC_015734.1. DR ProteinModelPortal; F8HTS2; -. DR EnsemblBacteria; AEJ31514; AEJ31514; LGMK_07320. DR GeneID; 10931645; -. DR KEGG; lec:LGMK_07320; -. DR KO; K00788; -. DR OMA; MLARYFI; -. DR BioCyc; LSP979982:GHM6-1511-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22600 MW; 0A22959297DBE904 CRC64; MIFKQAMLAR YFILGTQNVA SEAVFFDVLT QALAHGITLF QYREKGPGAL TGSEKRRVAQ RVRELTTQYQ VPLVIDDDID LAHAIKADGV HFGQGDGDIK KNIQASQPLF VGVSVSTQEE YDRIAGLSGI DNVGIGPVFA TMSKADAKPA IGISGLQGLV RQSQWPAIAI GGISQANLPD VLKTGVAGAS VISMISASEN IAKTLAFWKQ LS // ID F8HY43_WEIKK Unreviewed; 215 AA. AC F8HY43; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=WKK_02275; OS Weissella koreensis (strain KACC 15510). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Weissella. OX NCBI_TaxID=1045854; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC 15510; RX PubMed=21914863; DOI=10.1128/JB.05704-11; RA Lee S.H., Jung J.Y., Lee S.H., Jeon C.O.; RT "Complete genome sequence of Weissella koreensis KACC 15510, isolated RT from Kimchi."; RL J. Bacteriol. 193:5534-5534(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002899; AEJ23329.1; -; Genomic_DNA. DR RefSeq; YP_004726008.1; NC_015759.1. DR EnsemblBacteria; AEJ23329; AEJ23329; WKK_02275. DR GeneID; 10953743; -. DR KEGG; wko:WKK_02275; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; WKOR1045854:GH3T-468-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23254 MW; 1BCA2C04484A503D CRC64; MKIEQLQCYL VAGPQDYPEL SLTEFIVQIE VLMQSGITAY QFRDKGTHYQ NCEERLDLVL KLQFLAKKWQ VLFIINDDVD LAQQIHADGL HVGQGDQIQA ALKVPQALPM VIGLSVSNAS ELAAAQDSGA DYLGIGPIFA TQSKTDAAPA LGLAKLAEIL PQNHLPIVGI GGITESVLSD LAELGLNGVA VISMLTRSDN PIETVQKIKE AWHGI // ID F8IC73_SULAT Unreviewed; 213 AA. AC F8IC73; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=TPY_3618; OS Sulfobacillus acidophilus (strain TPY). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus. OX NCBI_TaxID=1051632; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TPY; RX PubMed=21914875; DOI=10.1128/JB.05684-11; RA Li B., Chen Y., Liu Q., Hu S., Chen X.; RT "Complete Genome Analysis of Sulfobacillus acidophilus Strain TPY, RT Isolated from a Hydrothermal Vent in the Pacific Ocean."; RL J. Bacteriol. 193:5555-5556(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002901; AEJ41770.1; -; Genomic_DNA. DR RefSeq; YP_004721513.1; NC_015757.1. DR EnsemblBacteria; AEJ41770; AEJ41770; TPY_3618. DR GeneID; 10962293; -. DR KEGG; say:TPY_3618; -. DR OMA; PCPVIAI; -. DR BioCyc; SACI1051632:GH78-3623-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 213 AA; 23752 MW; E815ED720321A86F CRC64; MIWGLIDAAR FEEPQWAWLP KVAPYLDGVW LRAPTFTLEE WLDWGRRIRG SAPQIPLWVG HLAAATALDA EGVQVSSTGP AAAWLKKRWT RSVAASVHHV AEARYHDAAD VWIWGHAFET RSKPGLAPRP RTHLMELLAE PARPPVLVVG GITVETVGEV AGWGVQGLVV GDGIWRTLAP AEASRKIRQI WDERREKPSY PVSKEGMRFD GFD // ID F8IC76_SULAT Unreviewed; 208 AA. AC F8IC76; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TPY_3621; OS Sulfobacillus acidophilus (strain TPY). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus. OX NCBI_TaxID=1051632; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TPY; RX PubMed=21914875; DOI=10.1128/JB.05684-11; RA Li B., Chen Y., Liu Q., Hu S., Chen X.; RT "Complete Genome Analysis of Sulfobacillus acidophilus Strain TPY, RT Isolated from a Hydrothermal Vent in the Pacific Ocean."; RL J. Bacteriol. 193:5555-5556(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002901; AEJ41773.1; -; Genomic_DNA. DR RefSeq; YP_004721516.1; NC_015757.1. DR EnsemblBacteria; AEJ41773; AEJ41773; TPY_3621. DR GeneID; 10962296; -. DR KEGG; say:TPY_3621; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; SACI1051632:GH78-3626-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22249 MW; 6932165FC40C3BEA CRC64; MDLRLMVIID PRQVPVDQLG GFCREVRQGG ATVIQLRGKI RSTRELVTYG RALRVETRRH GLSLIVNDRT DVALAIQADG VHVGQEDMPV RDVRRMAPGL TVGLSVSASE EIPAQPADWP DYFGVGPVYA TSSKDDAGDP LGVEGLRSLW QECRRIAPVV AIGGITPANV GPLWQLPVAG VAVISAVVNA PDKALACRQL ITGKEISG // ID F8IEQ0_ALIAT Unreviewed; 211 AA. AC F8IEQ0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-APR-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TC41_2034; OS Alicyclobacillus acidocaldarius (strain Tc-4-1) (Bacillus OS acidocaldarius). OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=1048834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tc-4-1; RA Chen Y., He Y., Dong Z., Hu S.; RT "The complete genome sequence of Alicyclobacillus acidocaldarius sp. RT Tc-4-1."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002902; AEJ43946.1; -; Genomic_DNA. DR RefSeq; YP_005518465.1; NC_017167.1. DR EnsemblBacteria; AEJ43946; AEJ43946; TC41_2034. DR GeneID; 12108945; -. DR KEGG; aad:TC41_2034; -. DR KO; K00788; -. DR BioCyc; AACI1048834:GL7E-2033-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21858 MW; E75794277680ECE6 CRC64; MTRRDWTDKL RVYLVTDDRP DHGEVATIVE QALAGGVTCV QLRRKQEDGG PMLKLALRLR ELASAHGALF IVNDRLDIAL LSGADGVHVG QTDLPASLVK SRFPELVVGV SARSVGEAVQ AEQDGADYLG VGSVYPTATK GDAVLTGLDV LAACKGAVRI PIVGIGGITV ERAPEVMAAG ADGVAVVSAI MSAPDPKAAA AAFVGRTFMN S // ID F8IJF6_ALIAT Unreviewed; 257 AA. AC F8IJF6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TC41_2776; OS Alicyclobacillus acidocaldarius (strain Tc-4-1) (Bacillus OS acidocaldarius). OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=1048834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tc-4-1; RA Chen Y., He Y., Dong Z., Hu S.; RT "The complete genome sequence of Alicyclobacillus acidocaldarius sp. RT Tc-4-1."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002902; AEJ44669.1; -; Genomic_DNA. DR RefSeq; YP_005519188.1; NC_017167.1. DR EnsemblBacteria; AEJ44669; AEJ44669; TC41_2776. DR GeneID; 12108365; -. DR KEGG; aad:TC41_2776; -. DR KO; K00788; -. DR BioCyc; AACI1048834:GL7E-2765-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 62 66 HMP-PP binding (By similarity). FT REGION 164 166 THZ-P binding (By similarity). FT BINDING 96 96 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 HMP-PP (By similarity). FT BINDING 194 194 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 257 AA; 26357 MW; 9BCA68D28654E99B CRC64; MRRRVCEVQT GNLPCPMGCG FSFGDDSMTH VLHVLSDRAR GAKVPLEDAL WLAALGGADV IQVREKKAPA LAVFEFACAL LARIREAGAS ARVLVNDRLD VAMAAGADGV HLAAKSLPVA VAREVVKRAG GGLVVGCSVH SIEEAKAAEA AGADYVTFGH IFPTASHPGL PPKGVRELAR VVEVLSIPVV AIGGIDAGNV GEVLATGASG VAVIGAVVEA ADPRAAAARL KEAMARSPVT PKVPFPTLEG GMRRARV // ID F8JD90_HYPSM Unreviewed; 200 AA. AC F8JD90; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HYPMC_0734; OS Hyphomicrobium sp. (strain MC1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Hyphomicrobium. OX NCBI_TaxID=717785; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC1; RA Genoscope.; RT "The complete genome of Hyphomicrobium sp. MC1."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ859181; CCB63967.1; -; Genomic_DNA. DR RefSeq; YP_004674543.1; NC_015717.1. DR EnsemblBacteria; CCB63967; CCB63967; HYPMC_0734. DR GeneID; 10894201; -. DR KEGG; hmc:HYPMC_0734; -. DR KO; K00788; -. DR BioCyc; HSP717785:GJ7O-731-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 200 AA; 21916 MW; DC7EA8A3193E42A2 CRC64; MILDRFYPIV PDVGWLERIV PLGVTFVQLR IKDASAADIA AQAKRANAFC KERSCTLVLN DYWEAALDAG VGFIHLGQDD LRDADLEAIK LAGIKLGIST HDIVELDNAL AAEPDYVALG PIYETKLKAM AWAPQGLDKI KEWRRRIGAL PLVAIGGLTP ERAAGVLEAG ADSLAVITDF FTAPDPEARI KLWLRQLQTR // ID F8JFQ9_HYPSM Unreviewed; 215 AA. AC F8JFQ9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=HYPMC_0992; OS Hyphomicrobium sp. (strain MC1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Hyphomicrobium. OX NCBI_TaxID=717785; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC1; RA Genoscope.; RT "The complete genome of Hyphomicrobium sp. MC1."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ859181; CCB64225.1; -; Genomic_DNA. DR RefSeq; YP_004674799.1; NC_015717.1. DR EnsemblBacteria; CCB64225; CCB64225; HYPMC_0992. DR GeneID; 10890081; -. DR KEGG; hmc:HYPMC_0992; -. DR KO; K00788; -. DR BioCyc; HSP717785:GJ7O-994-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 215 AA; 22752 MW; 9E718EE18B598FA6 CRC64; MSTPASLYLD FQIDDTPAAQ AKSVLSAAIE AAPIASVLLR PGQGAKIASE TTRPLIALAQ AQGIAVLIAS ETGETKMLGA DGVHLLWSQD IIRSFKTARQ SAPDAIVGAD AGRSRHDAME LGESGADYVA FGIPPHVEDR EKAAQRQRDL IAWWSELFEV PCVAFDVPDS DAAHALAILG ADFVSVRVTS SETEKDAAAR VRAFSEALRI PETAT // ID F8K0T2_STREN Unreviewed; 224 AA. AC F8K0T2; G8WRL9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SCAT_1226, SCATT_12250; OS Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC OS 14057 / NRRL 8057). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1003195; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057, and RC NRRL 8057; RX PubMed=21868806; DOI=10.1128/JB.05583-11; RA Barbe V., Bouzon M., Mangenot S., Badet B., Poulain J., Segurens B., RA Vallenet D., Marliere P., Weissenbach J.; RT "Complete genome sequence of Streptomyces cattleya NRRL 8057, a RT producer of antibiotics and fluorometabolites."; RL J. Bacteriol. 193:5055-5056(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL 8057; RA Genoscope - CEA; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057; RA Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.; RT "Complete genome sequence of Streptomyces cattleya strain DSM 46488."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 46488; RA Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003219; AEW93596.1; -; Genomic_DNA. DR EMBL; FQ859185; CCB73946.1; -; Genomic_DNA. DR RefSeq; YP_004910753.1; NC_016111.1. DR RefSeq; YP_006053118.1; NC_017586.1. DR EnsemblBacteria; AEW93596; AEW93596; SCATT_12250. DR EnsemblBacteria; CCB73946; CCB73946; SCAT_1226. DR GeneID; 11357555; -. DR GeneID; 12647995; -. DR KEGG; sct:SCAT_1226; -. DR KEGG; scy:SCATT_12250; -. DR KO; K00788; -. DR BioCyc; SCAT1003195:GJCM-1220-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23318 MW; 5939B0A3D1C656EA CRC64; MSTATAADRR ARLADARLYL CTDARKRQGD LAEFLDAVLA SGVDVVQLRD KGMEAREELE HLAVFADACR RHGKLLAVND RADVAHAAGA DVLHLGQGDL PVPAARALLG DEVLIGRSTH AESEAAAAAA EPGADYFCTG PVWPTPTKPG RHAPGLPLVE YAAGLGTARP WFAIGGIGLD NVEQVLAAGA RRIVVVRAIT EADDPADAAA RLAKIVRGAD GNPA // ID F8KBC8_LACRE Unreviewed; 214 AA. AC F8KBC8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LRATCC53608_0005; OS Lactobacillus reuteri ATCC 53608. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=927703; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 53608; RX PubMed=21622738; DOI=10.1128/JB.05282-11; RA Heavens D., Tailford L.E., Crossman L., Jeffers F., Mackenzie D.A., RA Caccamo M., Juge N.; RT "Genome sequence of the vertebrate gut symbiont Lactobacillus reuteri RT ATCC 53608."; RL J. Bacteriol. 193:4015-4016(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 53608; RA Davey R.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR854361; CCC02754.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23691 MW; 7F2541100BF503AB CRC64; MFDPKMLQVY LVGGTQDVHN DVVKFLEKVE LAMKSGITAF QYREKGNSKL RPNERVDLGL ELRTLCTRYG IPLIVDDNYE LAQQINADGV HVGQNDTKIE QVSVAVGHQM FIGYSCNTPE QVERANTMNF IDYIGCGPVF PTKSKPDADT AIGLNRLERL NMISERPVVA IGGIGEENMK VVHDTGVAGL AVISLVFDSK DLAATVKKMK KLYK // ID F8KKG7_STALN Unreviewed; 196 AA. AC F8KKG7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-APR-2014, entry version 20. DE SubName: Full=Thiamine monophosphate synthase/TENI family protein; GN ORFNames=SLUG_04960; OS Staphylococcus lugdunensis (strain N920143). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1034809; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=N920143; RA Heilbronner S., Holden M.T., van Tonder A., Geoghegan J.A., RA Foster T.J., Parkhill J., Bentley S.D.; RT "Genome sequence of Staphylococcus lugdunensis N920143 allows RT identification of putative colonization and virulence factors."; RL FEMS Microbiol. Lett. 322:60-67(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR870271; CCB52938.1; -; Genomic_DNA. DR RefSeq; YP_005759620.1; NC_017353.1. DR ProteinModelPortal; F8KKG7; -. DR EnsemblBacteria; CCB52938; CCB52938; SLUG_04960. DR GeneID; 12426001; -. DR KEGG; sln:SLUG_04960; -. DR KO; K10810; -. DR BioCyc; SLUG1034809:GLKV-500-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 196 AA; 22570 MW; 8D0598C59E1D47A5 CRC64; MFIFIAITEY KFLDNNDLQH FLTIEQDIDF LLFRTSMSQK ELQHFIQQLI YQGFPKSKMM IHSDVKLLNT LGLQNIHFRE NDAQAFHLKS KYPDIHVSMS THHLSSVIRA YEAGLDAVFF GHIFPTPSKP NLPPRSQVEI DSVLEVPIPV YAIGGITTDT IRKLSPKFAG ICAISFFMKS SASVIHQFRK EWHHHA // ID F8KNM5_STALN Unreviewed; 212 AA. AC F8KNM5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-APR-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SLUG_09740; OS Staphylococcus lugdunensis (strain N920143). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1034809; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=N920143; RA Heilbronner S., Holden M.T., van Tonder A., Geoghegan J.A., RA Foster T.J., Parkhill J., Bentley S.D.; RT "Genome sequence of Staphylococcus lugdunensis N920143 allows RT identification of putative colonization and virulence factors."; RL FEMS Microbiol. Lett. 322:60-67(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR870271; CCB53441.1; -; Genomic_DNA. DR RefSeq; YP_005760093.1; NC_017353.1. DR ProteinModelPortal; F8KNM5; -. DR EnsemblBacteria; CCB53441; CCB53441; SLUG_09740. DR GeneID; 12426478; -. DR KEGG; sln:SLUG_09740; -. DR KO; K00788; -. DR BioCyc; SLUG1034809:GLKV-986-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23242 MW; 9479E06EB38F9005 CRC64; MFKSTDLKVY FICGTQDIPE GKSLEQVVTQ ALESGVTMFQ FREKGSKVSQ DKKIEQLALK LKELCHNYQV PFIVNDNVAL ALKVQADGIH VGQDDAKVED FFEQFHDKII GLSVSNLDEL KRSDLTHVDY IGVGPIYQTP SKSDASTPVG PEMILTLRKE IGDFPIVAIG GVTENNAQAV VDAGADGISV ISAIARSQNI DSTVNKFLSY YN // ID F8KR95_HELBC Unreviewed; 197 AA. AC F8KR95; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Putative uncharacterized protein; GN OrderedLocusNames=HBZC1_02830; OS Helicobacter bizzozeronii (strain CIII-1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1002804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIII-1; RX PubMed=21705603; DOI=10.1128/JB.05439-11; RA Schott T., Rossi M., Hanninen M.L.; RT "Genome sequence of Helicobacter bizzozeronii strain CIII-1, an RT isolate from human gastric mucosa."; RL J. Bacteriol. 193:4565-4566(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR871757; CCB79269.1; -; Genomic_DNA. DR RefSeq; YP_004606981.1; NC_015674.1. DR EnsemblBacteria; CCB79269; CCB79269; HBZC1_02830. DR GeneID; 10819419; -. DR KEGG; hbi:HBZC1_02830; -. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 197 AA; 21618 MW; D2186473D5C50EE0 CRC64; MSLETYWITP QLSSDLQIFQ ATLQATLQTH TIHKAALRGA NFSAQLLDLF AKTCHAHHTT SFLNLPTLEL SIQKALEHGF QGVHVKGAQI LEIPHIPANL QIFYSAHNAR EVLQALDLGA HFCTISPICA TPNKPPSLGL EYLDQFSLEV RACLFALGGM GYDLASLLEE KGLRGFAGMR CFAPNVAILQ THTPTRT // ID F8KSA6_HELBC Unreviewed; 209 AA. AC F8KSA6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HBZC1_06850; OS Helicobacter bizzozeronii (strain CIII-1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1002804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIII-1; RX PubMed=21705603; DOI=10.1128/JB.05439-11; RA Schott T., Rossi M., Hanninen M.L.; RT "Genome sequence of Helicobacter bizzozeronii strain CIII-1, an RT isolate from human gastric mucosa."; RL J. Bacteriol. 193:4565-4566(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR871757; CCB79671.1; -; Genomic_DNA. DR RefSeq; YP_004607383.1; NC_015674.1. DR EnsemblBacteria; CCB79671; CCB79671; HBZC1_06850. DR GeneID; 10819821; -. DR KEGG; hbi:HBZC1_06850; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22747 MW; C50E0C99A85F794C CRC64; MGIELKGLYA LSDELLTPYD QLPHMLSLAI QGGVKIFQFR DKSHSDSELL SLAKDLAKIC QKHSVGFVIN DRLDLALKCH AWGLHVGSDD VPLAQARRLF KGHLGVSCYG NLDQALQAQQ ARASYAAFGA CFPSSTKPNA PCIPLDTLQH AKAHLNIPIC AIGGINPQNA PQLKNADMIA VISSLWSGDI VQNARKLLNC WQDKTSNLH // ID F8M1L9_MYCA0 Unreviewed; 222 AA. AC F8M1L9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MAF_04160; OS Mycobacterium africanum (strain GM041182). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=572418; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GM041182; RX PubMed=22389744; DOI=10.1371/journal.pntd.0001552; RA Bentley S.D., Comas I., Bryant J.M., Walker D., Smith N.H., RA Harris S.R., Thurston S., Gagneux S., Wood J., Antonio M., Quail M.A., RA Gehre F., Adegbola R.A., Parkhill J., de Jong B.C.; RT "The genome of Mycobacterium africanum West African 2 reveals a RT lineage-specific locus and genome erosion common to the M. RT tuberculosis complex."; RL PLoS Negl. Trop. Dis. 6:E1552-E1552(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR878060; CCC25488.1; -; Genomic_DNA. DR RefSeq; YP_004722125.1; NC_015758.1. DR ProteinModelPortal; F8M1L9; -. DR SMR; F8M1L9; 1-221. DR EnsemblBacteria; CCC25488; CCC25488; MAF_04160. DR GeneID; 10957901; -. DR KEGG; maf:MAF_04160; -. DR KO; K00788; -. DR BioCyc; MAFR572418:GJCK-417-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID F8MMJ0_NEUT8 Unreviewed; 523 AA. AC F8MMJ0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-APR-2014, entry version 14. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=NEUTE1DRAFT_81844; OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; OC Neurospora. OX NCBI_TaxID=510951; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC 2508 / P0657; RX PubMed=21750257; DOI=10.1534/genetics.111.130690; RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A., RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., RA Taylor J.W.; RT "Massive changes in genome architecture accompany the transition to RT self-fertility in the filamentous fungus Neurospora tetrasperma."; RL Genetics 189:55-69(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL891304; EGO57864.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 523 AA; 56001 MW; 0C68ED5B4AA9A45E CRC64; MDRNNVNYAV YLVTDSTPAI LGDRDLCEVV EASVRGGTTI VQLREKTSDT GDMIAMGKKL HAITKKYNVP LLINDRVDVA LAVGCEGVHI GQDDMELSTA RRLLGPDAII GVTVSTIQEA MVACKGGADY LGIGTVYATP TKTNTKNIIG AAGVRDILQA MADAGYDHVR TVCIGGINAE NLQRIVYQSE APSKKLDGVA VVSALVAAPD PEAAAKNLLG LFNSQPPFVR ESTSPRAETA DSILELVPEV VLEVARKKPL SHNMTNLVVQ NFAANVALAI GASPIMANNG EEAFDLCKLG GALVVNMGTV DPDGLQNYLK ALRAYNSVGQ PVVYDPVGAG ATTLRRSAVK TILSHGYLDI IKGNEGEIRT VYGIYERETF QQRGVDSSAE LEVSQKAELV RKLALREKNV VVMTGEIDYL SDGQHTFRID NGHAYLEMVT GTGCVLGTTI SAFVAAFPND KLAATVAALL HFEIAAERAA ERRDVQGPGT FVPAFLDELF KIRRETGQGR MGWLKSAKLT RLS // ID F8NU39_SERL9 Unreviewed; 531 AA. AC F8NU39; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-APR-2014, entry version 11. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=SERLADRAFT_348122; OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Agaricomycetidae; Boletales; Coniophorineae; OC Serpulaceae; Serpula. OX NCBI_TaxID=578457; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S7.9; RX PubMed=21764756; DOI=10.1126/science.1205411; RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P., RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., RA Blumentritt M., Coutinho P.M., Cullen D., de Vries R.P., Gathman A., RA Goodell B., Henrissat B., Ihrmark K., Kauserud H., Kohler A., RA LaButti K., Lapidus A., Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., RA Lucas S., Morin E., Murat C., Oguiza J.A., Park J., Pisabarro A.G., RA Riley R., Rosling A., Salamov A., Schmidt O., Schmutz J., Skrede I., RA Stenlid J., Wiebenga A., Xie X., Kuees U., Hibbett D.S., RA Hoffmeister D., Hoegberg N., Martin F., Grigoriev I.V., RA Watkinson S.C.; RT "The plant cell wall-decomposing machinery underlies the functional RT diversity of forest fungi."; RL Science 333:762-765(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL945433; EGO25805.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 531 AA; 55865 MW; 7628FD278D732500 CRC64; MVDYSLYLVT GRELLPQGKD YLVSLEESLQ GGVTIVQVRE KHIDTLEFLE IAQKTKLLCN KYNVPLIIND RIDIALAVQA DGVHLGQTDM PIHIARSLLP PGTILGVSCN TKEHVQKAIS DGADYVGIGA VWGTSTKQLT SPVIGVRGVG QILKTLDGTN VKGSFIGGIK SANALRTLHG SVSTTGHVLD GIAVVSDIVA STTPFHAAQN LSSILGAFNR NITLRVDQRY DATSSHIIDK IKNGVCNLMQ TIKKTSPLIH QITNVVVTNQ SANATLALGA SPIMATAPEE MYDLSLAIGA LLINFGTVKD KEGMILAGQF ANASQKPVVF DPVGVGATQF RKRTAAELLN TWQASVIKGN AAELGALADS KEVQAKGVDS VGGGFLDPAG FVKELAKKER CVIVLTGKTD WISDGTTVVK LDNGHEILGD ITGSGCLVGT CVAVFCGGAW AEAVSHEGNG ALNQDPSGQL VKGDMLLGAI SGVLALTIAA ELAVERSDVH GSGTFLPALI DELYHLTPQE IIEKAKIEVV S // ID F8PW74_SERL3 Unreviewed; 531 AA. AC F8PW74; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 16-APR-2014, entry version 11. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=SERLA73DRAFT_180734; OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Agaricomycetidae; Boletales; Coniophorineae; OC Serpulaceae; Serpula. OX NCBI_TaxID=936435; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=strain S7.3; RX PubMed=21764756; DOI=10.1126/science.1205411; RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P., RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., RA Blumentritt M., Coutinho P.M., Cullen D., de Vries R.P., Gathman A., RA Goodell B., Henrissat B., Ihrmark K., Kauserud H., Kohler A., RA LaButti K., Lapidus A., Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., RA Lucas S., Morin E., Murat C., Oguiza J.A., Park J., Pisabarro A.G., RA Riley R., Rosling A., Salamov A., Schmidt O., Schmutz J., Skrede I., RA Stenlid J., Wiebenga A., Xie X., Kuees U., Hibbett D.S., RA Hoffmeister D., Hoegberg N., Martin F., Grigoriev I.V., RA Watkinson S.C.; RT "The plant cell wall-decomposing machinery underlies the functional RT diversity of forest fungi."; RL Science 333:762-765(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL945479; EGO00250.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 531 AA; 55815 MW; 4BEADA63716BFCFF CRC64; MVDYSLYLVT GRELLPQGKD YLVSLEESLQ GGVTIVQVRE KHIDTLEFLE IAQKTKLLCN KYNVPLIIND RIDIALAVQA DGVHLGQTDM PIHIARSLLP PGTILGVSCN TKEHVQKAIS DGADYVGIGA VWGTSTKQLT SPVIGVRGVG QILKTLDGTN VKAVAIGGIK SANALRTLHG SVSTTGHVLD GIAVVSDIVA STTPFHAAQN LSSILGAFNR NITLRVDQRY DATSSHIIDK IKNGVCNLMQ TIKKTSPLIH QITNVVVTNQ SANATLALGA SPIMATAPEE MYDLSLAIGA LLINFGTVKD KEGMILAGQF ANASQKPVVF DPVGVGATQF RKRTAAELLN TWQASVIKGN AAELGALADS KEVQAKGVDS VGGGFLDPAG FVKELAKKER CVIVLTGKTD WISDGTTVVK LDNGHEILGD ITGSGCLVGT CVAVFCGGAW AEAVSHEGNG ALNQDPSGQL VKGDMLLGAI SGVLALTIAA ELAVERSDVH GSGTFLPALI DELYHLTPQE IIEKAKIEVV S // ID F8VM47_SALBC Unreviewed; 211 AA. AC F8VM47; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SBG_3637; OS Salmonella bongori (strain ATCC 43975 / DSM 13772 / NCTC 12419). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=218493; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43975 / DSM 13772 / NCTC 12419; RX PubMed=21876672; DOI=10.1371/journal.ppat.1002191; RA Fookes M., Schroeder G.N., Langridge G.C., Blondel C.J., Mammina C., RA Connor T.R., Seth-Smith H., Vernikos G.S., Robinson K.S., Sanders M., RA Petty N.K., Kingsley R.A., Baumler A.J., Nuccio S.P., Contreras I., RA Santiviago C.A., Maskell D., Barrow P., Humphrey T., Nastasi A., RA Roberts M., Frankel G., Parkhill J., Dougan G., Thomson N.R.; RT "Salmonella bongori provides insights into the evolution of the RT Salmonellae."; RL PLoS Pathog. 7:E1002191-E1002191(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR877557; CCC32682.1; -; Genomic_DNA. DR RefSeq; YP_004732433.1; NC_015761.1. DR GeneID; 10970228; -. DR KEGG; sbg:SBG_3637; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; SBON218493:GJAH-3681-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23167 MW; 7644AEEDC7473C6D CRC64; MYQPDFPPVP FHLGLYPVVD SLVWIERLLA AGVRTLQLRI KDKRDEEVEA DVVAAIALGR HYSARLFIND YWRLAIKHNA YGVHLGQEDL ETTDLQAIRA AGLRLGVSTH DDMEIDVALA TRPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIERLADYP TVAIGGISLQ RAPAVLETGV GSIAVVSAIT GAEDWRTATQ RLLKIVGVGD E // ID F8X1J3_9PORP Unreviewed; 211 AA. AC F8X1J3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9456_02241; OS Dysgonomonas mossii DSM 22836. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Dysgonomonas. OX NCBI_TaxID=742767; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 22836; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Dysgonomonas mossii DSM 22836."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLW01000010; EGK05977.1; -; Genomic_DNA. DR EnsemblBacteria; EGK05977; EGK05977; HMPREF9456_02241. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22878 MW; F83D93230D7EFB86 CRC64; MKDFDLTLYL VTERSLSLGR PLDDVVEEAV KGGVTMVQLR EKTCSSKEFY DQALRLKKCL KPYNVPLIIN DRLDIALACD AEGLHIGQND IPYHIARKIL GKNKIIGLSV ENIQDAIEAN KLDIDYIGIS PVFGTLTKTD TAQALGLSGV SDITQISKHP SVGIGGINKS NTQDIIRAGA DGISVVSAIM SADNPRLAAS ELFEIIIKSK K // ID F8XH86_ECOLX Unreviewed; 211 AA. AC F8XH86; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9349_04194; OS Escherichia coli MS 79-10. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=796392; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 79-10; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWR01000052; EGU95902.1; -; Genomic_DNA. DR ProteinModelPortal; F8XH86; -. DR SMR; F8XH86; 10-208. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F8XS85_9GAMM Unreviewed; 217 AA. AC F8XS85; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GGI1_13739; OS Acidithiobacillus sp. GGI-221. OC Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=872330; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GGI-221; RA Bagatharia S.B., Saxena A.K., Dave S.R., Vyas J.M., Dahiya M.S., RA Joshi C.G., Joshi M.N., Pandit A.S., Saiyed Z.M., Patel M.J., RA Sajnani M.R., Ahir V.B., Koringa P.G., Jakhesara S.J., Tipre D.R., RA Saxena R.S.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEFB01000814; EGQ62578.1; -; Genomic_DNA. DR ProteinModelPortal; F8XS85; -. DR EnsemblBacteria; EGQ62578; EGQ62578; GGI1_13739. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22628 MW; 01F0013C44881B3F CRC64; MAGDDHLISG LYAITDAHLM PEPVFLARAE AALRGGARIL QYRDKGDVVT DARRRRMQAG ALRELCAQYG ALFVVNDDPR LARVVGAPAL HVGAEDAPPA ALRAQFGRAI LIGVSCYGSV PQAQEAATQG ADYVAFGSFF ASPSKPQAPV VSVDVLTAAR AMIDLPIVAI GGITEANGRA LIAAGADALA VISGVFAAED VEGAARRFTA LFNNRKE // ID F8XZY8_STRAG Unreviewed; 223 AA. AC F8XZY8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FSLSAGS3026_04825; OS Streptococcus agalactiae FSL S3-026. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=876138; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL S3-026; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Lang P., RA Stanhope M.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL S3-026; RX PubMed=21536150; DOI=10.1016/j.meegid.2011.04.019; RA Richards V.P., Lang P., Pavinski Bitar P.D., Lefebure T., RA Schukken Y.H., Zadoks R.N., Stanhope M.J.; RT "Comparative genomics and the role of lateral gene transfer in the RT evolution of bovine adapted Streptococcus agalactiae."; RL Infect. Genet. Evol. 11:1263-1275(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXT01000007; EGS27337.1; -; Genomic_DNA. DR EnsemblBacteria; EGS27337; EGS27337; FSLSAGS3026_04825. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24579 MW; BE93BD7D2C0AFCA5 CRC64; MKDTLKLYFV CGTVDCSRKN ILTVVEEALQ AGITLFQFRE KGFTALQGKE KIAMAKQLQI LCKQYQVPFI IDDDIDLVEL IDADGLHIGQ NDLPVDEARR RLPDKIIGLS VSTMAEYQKS QLSVVDYIGI GPFNPTQSKA DAKPAVGNRT TKAVREINQD IPIVAIGGIT SDFVHDIIES GADGIAVISA ISKANHIVDA TRQLRYEVEK ALVNRQKHSD VTK // ID F8YNC6_ECOLX Unreviewed; 211 AA. AC F8YNC6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HUSEC_22622; OS Escherichia coli O104:H4 str. LB226692. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1040638; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LB226692; RX PubMed=21799941; DOI=10.1371/journal.pone.0022751; RA Mellmann A., Harmsen D., Cummings C.A., Zentz E.B., Leopold S.R., RA Rico A., Prior K., Szczepanowski R., Ji Y., Zhang W., McLaughlin S.F., RA Henkhaus J.K., Leopold B., Bielaszewska M., Prager R., Brzoska P.M., RA Moore R.L., Guenther S., Rothberg J.M., Karch H.; RT "Prospective Genomic Characterization of the German Enterohemorrhagic RT Escherichia coli O104:H4 Outbreak by Rapid Next Generation Sequencing RT Technology."; RL PLoS ONE 6:E22751-E22751(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOB02000115; EGR71835.1; -; Genomic_DNA. DR ProteinModelPortal; F8YNC6; -. DR SMR; F8YNC6; 20-202. DR EnsemblBacteria; EGR71835; EGR71835; HUSEC_22622. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F8YUI1_VIBCL Unreviewed; 440 AA. AC F8YUI1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC40A1_0068; OS Vibrio cholerae HC-40A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991961; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-40A1; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio cholerae HC-40A1."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOK01000102; EGS53889.1; -; Genomic_DNA. DR ProteinModelPortal; F8YUI1; -. DR EnsemblBacteria; EGS53889; EGS53889; VCHC40A1_0068. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID F8Z581_VIBCL Unreviewed; 440 AA. AC F8Z581; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC48A1_0068; OS Vibrio cholerae HC-48A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991965; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-48A1; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio cholerae HC-48A1."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOL01000112; EGS53584.1; -; Genomic_DNA. DR ProteinModelPortal; F8Z581; -. DR EnsemblBacteria; EGS53584; EGS53584; VCHC48A1_0068. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID F8ZD97_VIBCL Unreviewed; 440 AA. AC F8ZD97; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC49A2_0092; OS Vibrio cholerae HC-49A2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991935; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-49A2; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio cholerae HC-49A2."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOM01000004; EGR07006.1; -; Genomic_DNA. DR ProteinModelPortal; F8ZD97; -. DR EnsemblBacteria; EGR07006; EGR07006; VCHC49A2_0092. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID F8ZRB0_VIBCL Unreviewed; 440 AA. AC F8ZRB0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC70A1_0068; OS Vibrio cholerae HC-70A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991984; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-70A1; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio cholerae HC-70A1."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFON01000087; EGS52147.1; -; Genomic_DNA. DR ProteinModelPortal; F8ZRB0; -. DR EnsemblBacteria; EGS52147; EGS52147; VCHC70A1_0068. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID F8ZZJ7_VIBCL Unreviewed; 440 AA. AC F8ZZJ7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHCUF01_0092; OS Vibrio cholerae HCUF01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991930; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HCUF01; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio cholerae HCUF01."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOO01000005; EGR06685.1; -; Genomic_DNA. DR ProteinModelPortal; F8ZZJ7; -. DR EnsemblBacteria; EGR06685; EGR06685; VCHCUF01_0092. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID F9ABI7_VIBCL Unreviewed; 442 AA. AC F9ABI7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHE09_0064; OS Vibrio cholerae HE-09. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991998; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HE-09; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio cholerae HE-09."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOP01000102; EGS64012.1; -; Genomic_DNA. DR EnsemblBacteria; EGS64012; EGS64012; VCHE09_0064. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 442 AA; 49204 MW; E29AD776BDAF3696 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGFA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQEEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLII YPSENHRLNS KKNQHLAWVL ATLALGFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST STKVFPTTRA FPRIDKAKFN LYPVVDDVNW IEHLLKLGVR TVQLRIKDLM QGDLEAQIIR AITLGREFNA QVFINDYWQL AIKHQAYGVH LGQEDLTSAN LTELLDAGIR LGLSTHGYYE LLIAAGIQPS YIALGHIFPT TTKQMPSKPQ GLARLAAYQR LVNQMPYQGK NGIPTVAIGG IDLSNIRDVL DCGVTAVAVV RAITESPDPS LAVQALSSAF ADFVDAEYKL MPASESFEPI GFLAREVADA HR // ID F9AKC8_VIBCL Unreviewed; 419 AA. AC F9AKC8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHE39_0094; OS Vibrio cholerae HE39. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991945; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HE39; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio cholerae HE39."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOQ01000002; EGR04970.1; -; Genomic_DNA. DR EnsemblBacteria; EGR04970; EGR04970; VCHE39_0094. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 419 AA; 46745 MW; 133FC0418F90F742 CRC64; MQAKEQGFAI QHIRLDVGSE AQFILEKSEE SLRIGSSLCS QEEDFEPCDY YLDYVSENRV LPEAMMCNAR CSVTVGLHDE YGFTLDKWQY GHAAEQLIIY PSENHRLNSK VNQHLAWVLA TLTLDFSIGD GLCIARATIT QGDSVSRETW PTQFERFPAV QSNIRALSTQ VFTTTRAFPT IDKAKFNLYP VVDDVNWIEH LLKLGVRTVQ LRIKDPKQCD LEAQIIRAIA LGREFNAQVF INDYWQLAIK HQAYGVHLGQ EDLTSANLTE LLDAGIRLGL STHGYYELLI AAGIQPSYIA LGHIFPTTTK QMPSKPQGLV RLAAYQRLVN QMPYQGQHGI PTVAIGGIDR SNIRDVLDCG VTAVAVVRAI TESPDPSLAV QALSSVFADF VDAEYKLMPA RESCEPLSCL AREVADAHR // ID F9AVH1_VIBCL Unreviewed; 440 AA. AC F9AVH1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHE48_0097; OS Vibrio cholerae HE48. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991947; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HE48; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio cholerae HE48."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOR01000002; EGR10578.1; -; Genomic_DNA. DR EnsemblBacteria; EGR10578; EGR10578; VCHE48_0097. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48949 MW; 230CB8B98F30A390 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGFA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQEETSEPCD YYLDYVSENR VLPEAMMCNA RCSVTVGLHD EYGFTLDKWQ YGNAAEQLII YSSETHRLNS KLNQHLAWIL ATLTLDFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPA MQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CSNIRDVLDC GVTAVAVVRA ITESSDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAREVADANR // ID F9B6H7_VIBCL Unreviewed; 440 AA. AC F9B6H7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHFU02_0087; OS Vibrio cholerae HFU-02. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991989; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HFU-02; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio cholerae HFU-02."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOS01000010; EGS66444.1; -; Genomic_DNA. DR ProteinModelPortal; F9B6H7; -. DR EnsemblBacteria; EGS66444; EGS66444; VCHFU02_0087. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID F9BHC8_VIBCL Unreviewed; 440 AA. AC F9BHC8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC02A1_0083; OS Vibrio cholerae HC-02A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991948; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-02A1; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio cholerae HC-02A1."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOT01000080; EGS66432.1; -; Genomic_DNA. DR EnsemblBacteria; EGS66432; EGS66432; VCHC02A1_0083. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 49005 MW; A0B92CC841E5F854 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGFA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQEETSEPCD YYLDYVSENR VLPEAMMCNA RCSVTVGLHD EYGFTLDKWQ YGNAAEQLII YSSETHRLNS KLNQHLAWVL ATLTLDFPIE DGLCIARAAI TQGDSVSRET WPTQFERFPA MQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDYWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQVQHG IPTVAIGGID CSNIRDVLDC GVTAVAVVRA ITESSDPSLA VQALSSAFVD FVDAEYKLMP ASESCEPLSY LAREVADANR // ID F9BUY1_VIBCL Unreviewed; 440 AA. AC F9BUY1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCBJG01_0066; OS Vibrio cholerae BJG-01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991997; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BJG-01; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio Cholerae BJG-01."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOU01000109; EGS73278.1; -; Genomic_DNA. DR EnsemblBacteria; EGS73278; EGS73278; VCBJG01_0066. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 49043 MW; 553261A1EF23286E CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGFA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQEEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLII YPSENHRLNS KLNQHLAWVL ATLILDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRALST QVFPTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQC DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID RSNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSVFAD FVDAEYKLMP ASESCEPLSY LAREVADAHR // ID F9C2W4_VIBCL Unreviewed; 440 AA. AC F9C2W4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC38A1_0086; OS Vibrio cholerae HC-38A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991959; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-38A1; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio Cholerae Vibrio cholerae HC-38A1."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOV01000019; EGS73196.1; -; Genomic_DNA. DR ProteinModelPortal; F9C2W4; -. DR EnsemblBacteria; EGS73196; EGS73196; VCHC38A1_0086. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID F9CQS3_ECOLX Unreviewed; 211 AA. AC F9CQS3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HUSEC41_22185; OS Escherichia coli O104:H4 str. 01-09591. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1042803; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=01-09591; RX PubMed=21799941; DOI=10.1371/journal.pone.0022751; RA Mellmann A., Harmsen D., Cummings C.A., Zentz E.B., Leopold S.R., RA Rico A., Prior K., Szczepanowski R., Ji Y., Zhang W., McLaughlin S.F., RA Henkhaus J.K., Leopold B., Bielaszewska M., Prager R., Brzoska P.M., RA Moore R.L., Guenther S., Rothberg J.M., Karch H.; RT "Prospective Genomic Characterization of the German Enterohemorrhagic RT Escherichia coli O104:H4 Outbreak by Rapid Next Generation Sequencing RT Technology."; RL PLoS ONE 6:E22751-E22751(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFPS01000092; EGR61148.1; -; Genomic_DNA. DR ProteinModelPortal; F9CQS3; -. DR SMR; F9CQS3; 20-202. DR EnsemblBacteria; EGR61148; EGR61148; HUSEC41_22185. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F9D8V0_9BACT Unreviewed; 203 AA. AC F9D8V0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 13-NOV-2013, entry version 12. DE SubName: Full=Thiamine phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF9419_0425; OS Prevotella nigrescens ATCC 33563. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=997352; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33563; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFPX01000011; EGQ17072.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ17072; EGQ17072; HMPREF9419_0425. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 203 AA; 23505 MW; 4FDAAB83B0CCAE89 CRC64; MKLVVMTKST YFVEEDKILT ALFEEGLDNL HISKNEKSAL YLERLLSLIP KIYHKYITIH QHYYLKAEKQ LAGIHLDTEN AVPPIGYKGQ IGRTCRNSMW LKEMKKNSDY VFLGNMYGDD CNVTVEEHTF SDLELNELKD QGLLGKRVYA MGGITLERVP DIKQYGFGGV VVGREFWNQF DLHADIDFKG IIKYFQKLQQ AIE // ID F9DBG4_9BACT Unreviewed; 204 AA. AC F9DBG4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; ORFNames=HMPREF9419_1426; OS Prevotella nigrescens ATCC 33563. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=997352; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33563; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFPX01000032; EGQ14324.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ14324; EGQ14324; HMPREF9419_1426. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22090 MW; F9F249EFBA070EE2 CRC64; MNNIQFITHE NQRFDYVEGA EMALRGGCKW VQLRMKDTTD NKFLSIGRKV AALCRSYNAT FLLDDRVHLV AELGADGVHL GKNDMPISEA RRILGNEKII GGTANTFADV QHLAAQGADY IGCGPFRYTP TKRNLAPILG LEGFQNILKQ MQQAGINLPL IAIGGIVSTD IAALRDIGVN GIAVSGAVLG AADPIKEMKK LIEI // ID F9DBG8_9BACT Unreviewed; 222 AA. AC F9DBG8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 13-NOV-2013, entry version 12. DE SubName: Full=Thiamine phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE3; ORFNames=HMPREF9419_1430; OS Prevotella nigrescens ATCC 33563. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=997352; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33563; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFPX01000033; EGQ13987.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ13987; EGQ13987; HMPREF9419_1430. DR OrthoDB; EOG679THR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 222 AA; 25029 MW; 27233F2DFF93390B CRC64; MYVINQLIYI ICIVYERKCL INNKTMYLII ITEPQFTDNE AAIIAQLLHW GVDLMHLRKP ESSADELAKL IEAIPTAYHN RLVLHDHFDL ATHFTLHGLH LNRRNSVLPP NHKGTVSQSC HTLDEVKVCK TKCNYVFLSP VFNSISKLGY TSAFTPKALS EAKKQGVIDQ KVVALGGITA ANIDKTKYYG FGGGALLGDI WSRTADKNFE EYVRKIVEIC HV // ID F9DEU3_9BACT Unreviewed; 194 AA. AC F9DEU3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 13-NOV-2013, entry version 12. DE SubName: Full=Thiamine phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF9144_0183; OS Prevotella pallens ATCC 700821. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=997353; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700821; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFPY01000005; EGQ22639.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ22639; EGQ22639; HMPREF9144_0183. DR OrthoDB; EOG679THR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 194 AA; 22023 MW; 0AEC9625A24A1468 CRC64; MYLIVITEPQ FVSNEATIIA QLLHWGVDLV HLRKPESNAD ELAKLIEAIP TVYHNRLVLH DHFNLATHFT LHGLHLNRRN YVLPPNYKGA VSKSCHTFSE VETYKQHCNY VFLSPIFNSI SKQGYASAFS PKALFEAKQK GIINEKVVAL GGITAANINR IKRYGFGGVA LLGDVWRRTA DPFFEQYIKR CVKL // ID F9DEU6_9BACT Unreviewed; 204 AA. AC F9DEU6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; ORFNames=HMPREF9144_0186; OS Prevotella pallens ATCC 700821. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=997353; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700821; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFPY01000005; EGQ22642.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ22642; EGQ22642; HMPREF9144_0186. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22247 MW; E0FAD46FA1B699BA CRC64; MNNIQFITHE NQRFGYVEGA EMALRGGCKW VQLRMKDATD NEFLSVGRKV STLCRNYNAT FLLDDRVHLV AELGADGVHL GKNDMPISEA RCMLGSEKII GGTANTFTDV QRLATEGANY IGCGPFRYTK TKRNLAPILG LEGYRNILEQ MKKTNICLPL IAIGGIVSTD IAALITIGIS GIAVSGAILE AINPINEMTK LIEI // ID F9DHA9_9BACT Unreviewed; 203 AA. AC F9DHA9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 13-NOV-2013, entry version 12. DE SubName: Full=Thiamine phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE3; ORFNames=HMPREF9144_1049; OS Prevotella pallens ATCC 700821. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=997353; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700821; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFPY01000041; EGQ19153.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ19153; EGQ19153; HMPREF9144_1049. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 203 AA; 23497 MW; 174C85E4330BB1C3 CRC64; MKLVVMTKST YFVEEDKILT ALFEEGLENL HISKTDGTAL YLERLLSLIP KTYHKHITIH QHYYLKAEKQ LAGIHLDTET AVPPIGYKGQ IGRTCRNSMR LKEMRKSSDY VFLDNIYDDK HNVATDEHKF SSLELTELKS QGLLGKRVYA MGGISLEHIP DIKQYGFGGI VVGKEFWKHF DVYNDINYKG IIKYFYNLQK AIE // ID F9DS36_9BACL Unreviewed; 219 AA. AC F9DS36; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=HMPREF9372_1616; OS Sporosarcina newyorkensis 2681. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Sporosarcina. OX NCBI_TaxID=1027292; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2681; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFPZ01000046; EGQ26336.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ26336; EGQ26336; HMPREF9372_1616. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 219 AA; 24153 MW; EF3E576AFEF63C6B CRC64; MHADTSNHFP IREVVFSFGG EQEMKLVGVT DDCHSVDELL LKLLETEPYV DEFILREKSK TDEQLIELIS RLSTRGFPLD KIIVHARPSL ANSLSVPCQL TGYGMSVKEA RTTFPSLRLG SSIHSLEEAR EAQAAGADWL LYGHIYLTSS KKGLAPRGTD ELFEIALSCT IPVYAIGGIR PVHLPFFKRH GVRGAAILSP ISSQDAVSAV RDYARARDS // ID F9DUE0_9BACL Unreviewed; 222 AA. AC F9DUE0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; ORFNames=HMPREF9372_2421; OS Sporosarcina newyorkensis 2681. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Sporosarcina. OX NCBI_TaxID=1027292; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2681; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFPZ01000071; EGQ24738.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ24738; EGQ24738; HMPREF9372_2421. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23356 MW; D6418E6FAB97B9B7 CRC64; MRNAEVRKAL GLYFVMGTPN TASNGEQETL DILEAALRGG ITCFQLREKG ENALQGEALV SFAKKCQSLC RQFHIPFIIN DDVDLALAIN ADGVHVGQDD EQAGIVRTRI GPSKWLGVST HNAEEVQLAQ AIGADYVGIG PIYPTTTKLD ASAVVGSALI KEIHTAFPDM PIVGIGGISL ENFGPALHAG ADGIAVISSI ASAEDPLAAT QTFSESIRAI TK // ID F9EHC3_9ACTO Unreviewed; 220 AA. AC F9EHC3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9062_1845; OS Actinomyces sp. oral taxon 448 str. F0400. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Actinomycineae; Actinomycetaceae; Actinomyces. OX NCBI_TaxID=888056; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0400; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQC01000051; EGQ73294.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ73294; EGQ73294; HMPREF9062_1845. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22206 MW; 9B41EC336782D54C CRC64; MRPAPDLSVY LVTDADQCRS RGRSVLRTAE EAVAGGVTCV QLRAKRADGG AFLDEVLAVA GAIGGRVPVI VNDRIDVFLA ARRLSAAVAG VHVGQADLPA VLVRRLIGDD AFLGLSAATP DELRLADEQG ACDHVGIGTI RDTPTKPDAP AGLGLDGAAR LAALTDLPAV AIGGVTVADA PALRAGGLNG IAVVSAICAA EDPRAAAAAL HSAWNEGESR // ID F9EJH3_FUSNU Unreviewed; 206 AA. AC F9EJH3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9094_0077; OS Fusobacterium nucleatum subsp. animalis ATCC 51191. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=997347; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51191; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQD01000011; EGQ80898.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ80898; EGQ80898; HMPREF9094_0077. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22838 MW; 7903F05723E55837 CRC64; MDLKECKIYL VTDENSCNGK DFYKCIEESI KGGVKIVQLR EKNISTKDFY EKALKVKEIC KNYGVLFIIN DRLDIAQAIE ADGVHLGQSD MPIEKARDIL KDKFLIGATA RNIEEAKKAE LLGADYIGSG AIFGTSTKDN AKKLEMTELK KIVNSVKIPV FAIGGININN VWMLKNIGLQ GVCSVSGILS EKDCKKAVEL ILKNFN // ID F9ET71_9NEIS Unreviewed; 205 AA. AC F9ET71; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9418_0348; OS Neisseria macacae ATCC 33926. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=997348; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33926; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQE01000022; EGQ78123.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ78123; EGQ78123; HMPREF9418_0348. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22005 MW; 8FC84F3BED9230B2 CRC64; MTFPPLKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKTL HGDELKHEIA RCTAACQGNR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQARGTPVVA IGGIDLNNAE DVLATGVSSL AVVRAVTEAE NPEAVVKAFQ ALWDE // ID F9FB88_FUSOF Unreviewed; 508 AA. AC F9FB88; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 15. DE SubName: Full=Uncharacterized protein; GN ORFNames=FOXB_03640; OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae; OC Fusarium; Fusarium oxysporum species complex. OX NCBI_TaxID=660025; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fo5176; RX PubMed=21942452; DOI=10.1094/MPMI-08-11-0212; RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.; RT "A highly conserved effector in Fusarium oxysporum is required for RT full virulence on Arabidopsis."; RL Mol. Plant Microbe Interact. 25:180-190(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQF01001219; EGU85792.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 508 AA; 53008 MW; 6747D277D58EB341 CRC64; MAKPTVNYGL YLVTDSTPEI LGDRSLEEVV EASLRGGVTI LQYRDKHSER PVAVDTAKKL HAIARRYNVP LLINDRVDIA AEIDCEGVHI GQDDMAYEEA RKLLGPNKII GVTASSKEEA LKACEAGADY LGIGTVYSTQ TKKDTKSIIG PSGVRDILSA LYDAGYGSVP TVCIGGINAS NTAPVLAAAG SPSKSLDGVA VVSALIAAPE PATAARDLLG KVIVAKIPEV IRAVADKTPL SHNMTNLVVQ NFAANVALCV GASPIMANYA QEAADLAKLG GALVVNMGTV TPDGLKNYLQ AIKAYNESDR PIVLDPVGAG ATTVRRNAVK TLLDAGHFTI IKGNEGEIQT VAGATITQRG VDSTSSLTFP QKASLVRSIA LHRHTVVILT GATDLVSDGT RTLAISNGHP YLGEVTGTGC TLGTTVSAMV AAYGADPLLA AVAATVMFGL AAELAAERNE VRGPGSFVPT FLDELYNIRK STAKGDLRWL NMAKVKAVEV DIDVIPGE // ID F9GQ22_HAEHA Unreviewed; 226 AA. AC F9GQ22; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GG9_1167; OS Haemophilus haemolyticus M19501. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=1028803; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M19501; RX PubMed=21952546; DOI=10.1128/JB.05863-11; RA Jordan I.K., Conley A.B., Antonov I.V., Arthur R.A., Cook E.D., RA Cooper G.P., Jones B.L., Knipe K.M., Lee K.J., Liu X., Mitchell G.J., RA Pande P.R., Petit R.A., Qin S., Rajan V.N., Sarda S., Sebastian A., RA Tang S., Thapliyal R., Varghese N.J., Ye T., Katz L.S., Wang X., RA Rowe L., Frace M., Mayer L.W.; RT "Genome Sequences for Five Strains of the Emerging Pathogen RT Haemophilus haemolyticus."; RL J. Bacteriol. 193:5879-5880(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQO01000010; EGT75204.1; -; Genomic_DNA. DR EnsemblBacteria; EGT75204; EGT75204; GG9_1167. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24736 MW; 5E31329F75694010 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRKA GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAISHAENV QAATKALREA SDEYAK // ID F9GV25_HAEHA Unreviewed; 226 AA. AC F9GV25; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GGA_1173; OS Haemophilus haemolyticus M21127. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=1028804; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M21127; RX PubMed=21952546; DOI=10.1128/JB.05863-11; RA Jordan I.K., Conley A.B., Antonov I.V., Arthur R.A., Cook E.D., RA Cooper G.P., Jones B.L., Knipe K.M., Lee K.J., Liu X., Mitchell G.J., RA Pande P.R., Petit R.A., Qin S., Rajan V.N., Sarda S., Sebastian A., RA Tang S., Thapliyal R., Varghese N.J., Ye T., Katz L.S., Wang X., RA Rowe L., Frace M., Mayer L.W.; RT "Genome Sequences for Five Strains of the Emerging Pathogen RT Haemophilus haemolyticus."; RL J. Bacteriol. 193:5879-5880(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQP01000015; EGT75725.1; -; Genomic_DNA. DR EnsemblBacteria; EGT75725; EGT75725; GGA_1173. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24829 MW; 4D054C561BF3898A CRC64; MKNIQEILPL YFVAGTQDCR HLGDNPADNL LSVLKQALEG GITCFQFRDK GKFSLENSPD EQRSLAISCR DLCHQYDVPF IVDDNVDLAL EIEVDGIHVG QSDTPVKTIR AKTNKPLIIG WSINRLDEAK IGEEIAEIDY FGVGPIFTTQ SKENPSPTLG IEFIQTLRNE GITKPLVAIG GIKLEHVRTL RKYGADGVAV ITAITQANDI KAATQALKEE SNALNL // ID F9GX11_HAEHA Unreviewed; 226 AA. AC F9GX11; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GGC_0231; OS Haemophilus haemolyticus M21621. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=1028805; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M21621; RX PubMed=21952546; DOI=10.1128/JB.05863-11; RA Jordan I.K., Conley A.B., Antonov I.V., Arthur R.A., Cook E.D., RA Cooper G.P., Jones B.L., Knipe K.M., Lee K.J., Liu X., Mitchell G.J., RA Pande P.R., Petit R.A., Qin S., Rajan V.N., Sarda S., Sebastian A., RA Tang S., Thapliyal R., Varghese N.J., Ye T., Katz L.S., Wang X., RA Rowe L., Frace M., Mayer L.W.; RT "Genome Sequences for Five Strains of the Emerging Pathogen RT Haemophilus haemolyticus."; RL J. Bacteriol. 193:5879-5880(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQQ01000001; EGT82078.1; -; Genomic_DNA. DR EnsemblBacteria; EGT82078; EGT82078; GGC_0231. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24776 MW; 38AA5A1BD1907AAB CRC64; MKNIQEILPL YFVAGTQDCR HLGDNPADNL LSVLKQALEG GITCFQFRDK GKFSLENSPD EQRALAISCR DLCHQYDVPF IVDDNVDLAL EIEADGIHVG QNDTPVKTIR AKTNKPLIIG WSINRLDEAK IGEEISEIDY FGVGPIFTTQ SKENPSPTLG MEFIQTLRNG GITKPLVAIG GIKLEHVKTL RKYGADGVAV ITAITQANDI KAVTQALKEE SNIVNS // ID F9H2U7_HAEHA Unreviewed; 226 AA. AC F9H2U7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GGE_0193; OS Haemophilus haemolyticus M21639. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=1028806; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M21639; RX PubMed=21952546; DOI=10.1128/JB.05863-11; RA Jordan I.K., Conley A.B., Antonov I.V., Arthur R.A., Cook E.D., RA Cooper G.P., Jones B.L., Knipe K.M., Lee K.J., Liu X., Mitchell G.J., RA Pande P.R., Petit R.A., Qin S., Rajan V.N., Sarda S., Sebastian A., RA Tang S., Thapliyal R., Varghese N.J., Ye T., Katz L.S., Wang X., RA Rowe L., Frace M., Mayer L.W.; RT "Genome Sequences for Five Strains of the Emerging Pathogen RT Haemophilus haemolyticus."; RL J. Bacteriol. 193:5879-5880(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQR01000005; EGT83148.1; -; Genomic_DNA. DR EnsemblBacteria; EGT83148; EGT83148; GGE_0193. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24683 MW; 9E95FCE4FC572FEA CRC64; MKNIQEILPL YFVAGTQDCR HLGDNPTDNL LSVLKQALEG GITCFQFRDK GKFSLENSPD EQLALAINCL DLCRQYNVPF IVDDNVDLAL EIEADGIHVG QSDTPVKTIR AKTNKPLIIG WSVNRLDEAK IGEEISDIDY FGVGPIFSTQ SKENPSPTLG MEFIQTLRNG GITKPLVAIG GIKLEHVKTL RKYGADGVAV ITAITQSNDI KSATQALKEE NNAANL // ID F9HD45_STRMT Unreviewed; 210 AA. AC F9HD45; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9958_1031; OS Streptococcus mitis SK1073. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1008452; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK1073; RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., RA Methe B., Sutton G., Nelson K.E.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQT01000042; EGP67693.1; -; Genomic_DNA. DR EnsemblBacteria; EGP67693; EGP67693; HMPREF9958_1031. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22940 MW; E329DA2DF2296B96 CRC64; MNREAFRLYL VTNRYQDSLE SFLEKVETAC RSGVTIIQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE EGGADYLGTG AIFPTTTKEN APITLISTLK TICQRVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIETKTQA FLTKLDDIIF // ID F9I5H2_ECOLX Unreviewed; 211 AA. AC F9I5H2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=C22711_5346, EUAG_02908; OS Escherichia coli O104:H4 str. C227-11. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1048254; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C227-11; RX PubMed=21793740; DOI=10.1056/NEJMoa1106920; RA Rasko D.A., Webster D.R., Sahl J.W., Bashir A., Boisen N., Scheutz F., RA Paxinos E.E., Sebra R., Chin C.-S., Iliopoulos D., Klammer A., RA Peluso P., Lee L., Kislyuk A., Bullard J., Kasarskis A., Wang S., RA Eid J., Rank D., Redman J.C., Steyert S.R., Frimodt-Moller J., RA Struve C., Petersen A.M., Krogfelt K.A., Nataro J.P., Schadt E.E., RA Waldor M.K.; RT "Origins of the E. coli strain causing an outbreak of hemolytic-uremic RT syndrome in Germany."; RL N. Engl. J. Med. 365:709-717(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C227-11; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFST01000022; EGT71310.1; -; Genomic_DNA. DR EMBL; AFRH01000012; EHF21763.1; -; Genomic_DNA. DR EnsemblBacteria; EGT71310; EGT71310; C22711_5346. DR EnsemblBacteria; EHF21763; EHF21763; EUAG_02908. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F9I7D0_ACIBA Unreviewed; 299 AA. AC F9I7D0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Bifunctional protein dGTP-pyrophosphohydrolase/thiamine phosphate synthase; GN ORFNames=ABNIH1_02976; OS Acinetobacter baumannii ABNIH1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=992402; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ABNIH1; RX PubMed=21825119; DOI=10.1073/pnas.1104404108; RG NISC Comparative Sequence Program; RA Snitkin E.S., Zelazny A.M., Montero C.I., Stock F., Mijares L., RA Murray P.R., Segre J.A.; RT "Genome-wide recombination drives diversification of epidemic strains RT of Acinetobacter baumannii."; RL Proc. Natl. Acad. Sci. U.S.A. 108:13758-13763(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFSZ01000016; EGT96331.1; -; Genomic_DNA. DR ProteinModelPortal; F9I7D0; -. DR EnsemblBacteria; EGT96331; EGT96331; ABNIH1_02976. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 299 AA; 34203 MW; 49BD9DC168F2FC57 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLNPELK KQIKTVHLKQ SQLMSLHKGD LEVGVRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID F9IAP2_ACIBA Unreviewed; 203 AA. AC F9IAP2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ABNIH1_09136; OS Acinetobacter baumannii ABNIH1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=992402; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ABNIH1; RX PubMed=21825119; DOI=10.1073/pnas.1104404108; RG NISC Comparative Sequence Program; RA Snitkin E.S., Zelazny A.M., Montero C.I., Stock F., Mijares L., RA Murray P.R., Segre J.A.; RT "Genome-wide recombination drives diversification of epidemic strains RT of Acinetobacter baumannii."; RL Proc. Natl. Acad. Sci. U.S.A. 108:13758-13763(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFSZ01000044; EGT93162.1; -; Genomic_DNA. DR ProteinModelPortal; F9IAP2; -. DR EnsemblBacteria; EGT93162; EGT93162; ABNIH1_09136. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21778 MW; F47FCEF0DAC9A9AE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKID KAEQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID F9IL58_ACIBA Unreviewed; 299 AA. AC F9IL58; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Bifunctional protein dGTP-pyrophosphohydrolase/thiamine phosphate synthase; GN ORFNames=ABNIH2_08622; OS Acinetobacter baumannii ABNIH2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=992403; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ABNIH2; RX PubMed=21825119; DOI=10.1073/pnas.1104404108; RG NISC Comparative Sequence Program; RA Snitkin E.S., Zelazny A.M., Montero C.I., Stock F., Mijares L., RA Murray P.R., Segre J.A.; RT "Genome-wide recombination drives diversification of epidemic strains RT of Acinetobacter baumannii."; RL Proc. Natl. Acad. Sci. U.S.A. 108:13758-13763(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTA01000047; EGT94683.1; -; Genomic_DNA. DR ProteinModelPortal; F9IL58; -. DR EnsemblBacteria; EGT94683; EGT94683; ABNIH2_08622. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 299 AA; 34203 MW; 49BD9DC168F2FC57 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLNPELK KQIKTVHLKQ SQLMSLHKGD LEVGVRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID F9ILW6_ACIBA Unreviewed; 203 AA. AC F9ILW6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ABNIH2_09954; OS Acinetobacter baumannii ABNIH2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=992403; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ABNIH2; RX PubMed=21825119; DOI=10.1073/pnas.1104404108; RG NISC Comparative Sequence Program; RA Snitkin E.S., Zelazny A.M., Montero C.I., Stock F., Mijares L., RA Murray P.R., Segre J.A.; RT "Genome-wide recombination drives diversification of epidemic strains RT of Acinetobacter baumannii."; RL Proc. Natl. Acad. Sci. U.S.A. 108:13758-13763(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTA01000053; EGT93935.1; -; Genomic_DNA. DR ProteinModelPortal; F9ILW6; -. DR EnsemblBacteria; EGT93935; EGT93935; ABNIH2_09954. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21778 MW; F47FCEF0DAC9A9AE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKID KAEQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID F9IVW2_ACIBA Unreviewed; 203 AA. AC F9IVW2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ABNIH3_06646; OS Acinetobacter baumannii ABNIH3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=992404; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ABNIH3; RX PubMed=21825119; DOI=10.1073/pnas.1104404108; RG NISC Comparative Sequence Program; RA Snitkin E.S., Zelazny A.M., Montero C.I., Stock F., Mijares L., RA Murray P.R., Segre J.A.; RT "Genome-wide recombination drives diversification of epidemic strains RT of Acinetobacter baumannii."; RL Proc. Natl. Acad. Sci. U.S.A. 108:13758-13763(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTB01000092; EGT99831.1; -; Genomic_DNA. DR ProteinModelPortal; F9IVW2; -. DR EnsemblBacteria; EGT99831; EGT99831; ABNIH3_06646. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21778 MW; F47FCEF0DAC9A9AE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKID KAEQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID F9J0H6_ACIBA Unreviewed; 299 AA. AC F9J0H6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Bifunctional protein dGTP-pyrophosphohydrolase/thiamine phosphate synthase; GN ORFNames=ABNIH3_14987; OS Acinetobacter baumannii ABNIH3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=992404; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ABNIH3; RX PubMed=21825119; DOI=10.1073/pnas.1104404108; RG NISC Comparative Sequence Program; RA Snitkin E.S., Zelazny A.M., Montero C.I., Stock F., Mijares L., RA Murray P.R., Segre J.A.; RT "Genome-wide recombination drives diversification of epidemic strains RT of Acinetobacter baumannii."; RL Proc. Natl. Acad. Sci. U.S.A. 108:13758-13763(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTB01000207; EGT93719.1; -; Genomic_DNA. DR ProteinModelPortal; F9J0H6; -. DR EnsemblBacteria; EGT93719; EGT93719; ABNIH3_14987. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 299 AA; 34203 MW; 49BD9DC168F2FC57 CRC64; MPKPIVDVAI AILIHRGKIL VGWRGEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWTWYTREQL LHLNFPKANK DIIKRLYWPH FIKISHTLTS VENSDALLYW RIEDEFGPRE VEQLTALDEG QRSNLIINVD IWQQLNPELK KQIKTVHLKQ SQLMSLHKGD LEVGVRFIAA CHDAVSLQHA QQIGCDAVFV SPVKVTATHP DVSALGWDRF ADLIEKCQIP VFALGGMSPD DLATAQQHGA YGLAGIRNF // ID F9J6X7_ACIBA Unreviewed; 203 AA. AC F9J6X7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ABNIH4_05404; OS Acinetobacter baumannii ABNIH4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=992405; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ABNIH4; RX PubMed=21825119; DOI=10.1073/pnas.1104404108; RG NISC Comparative Sequence Program; RA Snitkin E.S., Zelazny A.M., Montero C.I., Stock F., Mijares L., RA Murray P.R., Segre J.A.; RT "Genome-wide recombination drives diversification of epidemic strains RT of Acinetobacter baumannii."; RL Proc. Natl. Acad. Sci. U.S.A. 108:13758-13763(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTC01000038; EGU03013.1; -; Genomic_DNA. DR ProteinModelPortal; F9J6X7; -. DR EnsemblBacteria; EGU03013; EGU03013; ABNIH4_05404. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21778 MW; F47FCEF0DAC9A9AE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKID KAEQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID F9JEY0_9LACO Unreviewed; 217 AA. AC F9JEY0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9102_0588; OS Lactobacillus oris F0423. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=944562; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0423; RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., RA Methe B., Sutton G., Nelson K.E.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTL01000002; EGS39444.1; -; Genomic_DNA. DR EnsemblBacteria; EGS39444; EGS39444; HMPREF9102_0588. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23332 MW; 421F7945500D57B9 CRC64; MKFEPTMLRA YLVGGSQDTH HAPAELLTKT EEALQAGITA FQYREKGSSN LSADQRLKLA QQLRELTRHY RVPFFIDDDE ELALAVGADG VHVGQKDQRI EQVIQRAQGK LMIGYSCNRP AQIEKANQLA AVDYIGSGPV FPTQSKADAD PALGLSRLAL LNRLSEQPVV AIGGITADNI AATLATGVAG AAVISMVFQS DDISQTVHQM LTASSQS // ID F9JN40_STAAU Unreviewed; 213 AA. AC F9JN40; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21195_1572; OS Staphylococcus aureus subsp. aureus 21195. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904728; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21195; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTM01000022; EGS97986.1; -; Genomic_DNA. DR ProteinModelPortal; F9JN40; -. DR EnsemblBacteria; EGS97986; EGS97986; SA21195_1572. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F9JYN8_STAAU Unreviewed; 213 AA. AC F9JYN8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21200_0047; OS Staphylococcus aureus subsp. aureus 21200. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904730; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21200; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTN01000024; EGS92890.1; -; Genomic_DNA. DR ProteinModelPortal; F9JYN8; -. DR EnsemblBacteria; EGS92890; EGS92890; SA21200_0047. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23374 MW; 87C8D3399EE9DFCF CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDEVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F9K4J0_STAAU Unreviewed; 213 AA. AC F9K4J0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21201_0003; OS Staphylococcus aureus subsp. aureus 21201. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904731; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21201; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTO01000031; EGS94909.1; -; Genomic_DNA. DR ProteinModelPortal; F9K4J0; -. DR SMR; F9K4J0; 4-209. DR PRIDE; F9K4J0; -. DR EnsemblBacteria; EGS94909; EGS94909; SA21201_0003. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F9KFD6_STAAU Unreviewed; 213 AA. AC F9KFD6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21235_1837; OS Staphylococcus aureus subsp. aureus 21235. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904738; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21235; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTQ01000078; EGS81206.1; -; Genomic_DNA. DR EnsemblBacteria; EGS81206; EGS81206; SA21235_1837. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23386 MW; DE32F92F588D8D4C CRC64; MFNQLYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F9KHS1_STAAU Unreviewed; 213 AA. AC F9KHS1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21259_0032; OS Staphylococcus aureus subsp. aureus 21259. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904744; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21259; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTS01000008; EGS89862.1; -; Genomic_DNA. DR ProteinModelPortal; F9KHS1; -. DR SMR; F9KHS1; 4-209. DR PRIDE; F9KHS1; -. DR EnsemblBacteria; EGS89862; EGS89862; SA21259_0032. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F9KN82_STAAU Unreviewed; 213 AA. AC F9KN82; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21266_0816; OS Staphylococcus aureus subsp. aureus 21266. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904747; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21266; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTT01000003; EGS90088.1; -; Genomic_DNA. DR ProteinModelPortal; F9KN82; -. DR SMR; F9KN82; 4-209. DR PRIDE; F9KN82; -. DR EnsemblBacteria; EGS90088; EGS90088; SA21266_0816. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F9L351_STAAU Unreviewed; 213 AA. AC F9L351; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21269_0896; OS Staphylococcus aureus subsp. aureus 21269. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904749; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21269; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTU01000056; EGS84251.1; -; Genomic_DNA. DR ProteinModelPortal; F9L351; -. DR EnsemblBacteria; EGS84251; EGS84251; SA21269_0896. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23301 MW; A8845F534C160E89 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLGEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID F9L623_STACP Unreviewed; 212 AA. AC F9L623; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU116_1843; OS Staphylococcus capitis VCU116. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904334; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU116; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTX01000024; EGS40151.1; -; Genomic_DNA. DR ProteinModelPortal; F9L623; -. DR EnsemblBacteria; EGS40151; EGS40151; SEVCU116_1843. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23706 MW; FFE3130988D42CA8 CRC64; MFSSEQLQVY FICGTQDIPE NRTIEQVLDE ALKAGITMYQ FREKGPSSLI GEEKKQLAIN LKRKCERYHV PFIVNDDIEL AKDIDADGVH VGQDDKEVKD FAMQFRNKII GLSVGNLDEY QQSDLSQVDY IGVGPMYTTS SKDDANAPVG PHMITKLRDY VGELPIVAIG GINETNIEPI AEACADGVSV ISAITRSKNI DKTVKHFRKY FN // ID F9L7Q6_STACP Unreviewed; 196 AA. AC F9L7Q6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU116_1272; OS Staphylococcus capitis VCU116. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904334; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU116; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTX01000030; EGS39147.1; -; Genomic_DNA. DR ProteinModelPortal; F9L7Q6; -. DR EnsemblBacteria; EGS39147; EGS39147; SEVCU116_1272. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 22520 MW; A2ECCFDB921F4F37 CRC64; MHIFIAITYD KTLTTQDLEH FLNIEEGIDA LLFRTSMPKN ELKKILIQLI NQGFPKDKMI IHSDTALLEE LNLSRIHFKE NVKTAFAYKK SHPEIQVGMS THSIDTIYTC IDEGLDYVFY GHIFPTPSHP HDAPRSHDEI VEALNLPIPI YAIGGISEHT ILKLEYGFDG ICAISFFMNA SLKEIKELRR KWLQHA // ID F9LCR3_STAEP Unreviewed; 213 AA. AC F9LCR3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU037_0429; OS Staphylococcus epidermidis VCU037. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904319; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU037; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTY01000016; EGS78395.1; -; Genomic_DNA. DR ProteinModelPortal; F9LCR3; -. DR EnsemblBacteria; EGS78395; EGS78395; SEVCU037_0429. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID F9LDP8_STAEP Unreviewed; 160 AA. AC F9LDP8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU037_1741; OS Staphylococcus epidermidis VCU037. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904319; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU037; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTY01000028; EGS77149.1; -; Genomic_DNA. DR ProteinModelPortal; F9LDP8; -. DR EnsemblBacteria; EGS77149; EGS77149; SEVCU037_1741. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID F9LH80_STAEP Unreviewed; 160 AA. AC F9LH80; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU105_1969; OS Staphylococcus epidermidis VCU105. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904328; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU105; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTZ01000002; EGS79305.1; -; Genomic_DNA. DR ProteinModelPortal; F9LH80; -. DR EnsemblBacteria; EGS79305; EGS79305; SEVCU105_1969. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID F9LMG5_STAEP Unreviewed; 213 AA. AC F9LMG5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU105_0624; OS Staphylococcus epidermidis VCU105. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904328; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU105; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFTZ01000029; EGS74524.1; -; Genomic_DNA. DR ProteinModelPortal; F9LMG5; -. DR EnsemblBacteria; EGS74524; EGS74524; SEVCU105_0624. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID F9LRE8_STAEP Unreviewed; 213 AA. AC F9LRE8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU107_1012; OS Staphylococcus epidermidis VCU109. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904330; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU109; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUA01000029; EGS78106.1; -; Genomic_DNA. DR ProteinModelPortal; F9LRE8; -. DR EnsemblBacteria; EGS78106; EGS78106; SEVCU107_1012. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID F9LTD1_STAEP Unreviewed; 199 AA. AC F9LTD1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU107_2318; OS Staphylococcus epidermidis VCU109. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904330; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU109; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUA01000045; EGS75826.1; -; Genomic_DNA. DR ProteinModelPortal; F9LTD1; -. DR EnsemblBacteria; EGS75826; EGS75826; SEVCU107_2318. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 22752 MW; A468A47409C7D4D7 CRC64; MGGIFIFIAI TYHKQLTRDD LQHYKHIEEA IDGLLFRTSM NNEENKDMIQ SLLQLGFSKD KIIIHSDVTL LEDLHLKRIH FKENDTTAFT YKEAHPDICV SMSTHDVETV KRCYENGLDS VFFGHIFPTS SHPNVPPRSK EAIQQALNVP IPIYAIGGIN EHSLQKMPPG FKGICAISYF NNASLEEIKQ LRKEWSTHA // ID F9MK83_STRMT Unreviewed; 210 AA. AC F9MK83; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_1; Synonyms=thiE; ORFNames=HMPREF9959_0991; OS Streptococcus mitis SK569. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1035187; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK569; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUF01000032; EGU70422.1; -; Genomic_DNA. DR EnsemblBacteria; EGU70422; EGU70422; HMPREF9959_0991. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22849 MW; AC775D7C9EF932C5 CRC64; MNREALRLYL VTNRYQDSLE SFLEKLETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVTRALEAE EGGADYLGTG AIFPTTTKEN APITLISTLK TICQRVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDDIIF // ID F9MK90_STRMT Unreviewed; 209 AA. AC F9MK90; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_2; Synonyms=thiE; ORFNames=HMPREF9959_0999; OS Streptococcus mitis SK569. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1035187; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK569; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUF01000032; EGU70427.1; -; Genomic_DNA. DR EnsemblBacteria; EGU70427; EGU70427; HMPREF9959_0999. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23290 MW; D307C0C824F31072 CRC64; MFHKELLKLY FICGTTTCRG KDLYTVVEEA LKGGITLFQF REKGEGALEG KEKVELAMKL QDLCKKYNVP FIVNDDIELA LEIDADGVHV GQDDLGVDEI RKLMPAKIIG LSIKNEKEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLKLMRKLL PQMPLVAIGG IQTQHIKDIM KINMDGVSII SAISYAKNIE KTVREMSEQ // ID F9MMU3_9FIRM Unreviewed; 220 AA. AC F9MMU3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1040_0002; OS Megasphaera sp. UPII 135-E. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=1000569; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UPII 135-E; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUG01000008; EGS35743.1; -; Genomic_DNA. DR EnsemblBacteria; EGS35743; EGS35743; HMPREF1040_0002. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24648 MW; 7A0D9CE4248734CE CRC64; MMKHDDHVHQ IRTEPIYAIL GETFSRGRTN RQVAKALLGA GVRIIQYREK EKSWQEKYEE ARDICQWCNE YGATFIMNDS IDLAIACEAP AIHVGQDDAP VAWVRRLAQR DIVVGVSTHT IAEMKKAVRD GADYVGLGPM YQTTSKMDVH DIVADVDKAY ALTLPIPVVT IGGIDLIHIR QLYTEGFRSF AMISALVGAT DIVEQIGAFR QVLQEKIDEC // ID F9MR06_9FIRM Unreviewed; 198 AA. AC F9MR06; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 13-NOV-2013, entry version 12. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF1040_1584; OS Megasphaera sp. UPII 135-E. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=1000569; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UPII 135-E; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUG01000044; EGS32099.1; -; Genomic_DNA. DR EnsemblBacteria; EGS32099; EGS32099; HMPREF1040_1584. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 198 AA; 22040 MW; 1E499E8B2341F39B CRC64; MLKILAITNH ALVSTNYWDR LEKIVASPID SIILREKTLS EDDYAEYAQR LLKICNIHDK TCILHNFGKV AVRLHIPRFQ CSLSYLESHS SLLYYMTNLG VSVHTVAEAK RAEELGATYI MASHVFPTSC KKDMPPIGVD TVREICQAVS IPVYALGGIN LETITQLRDV PITGVALMSS LLTCKNPSTY VEALKSNL // ID F9MZJ3_FINMA Unreviewed; 214 AA. AC F9MZJ3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_1; Synonyms=thiE; ORFNames=HMPREF9489_1263; OS Finegoldia magna SY403409CC001050417. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Finegoldia. OX NCBI_TaxID=866779; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SY403409CC001050417; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUI01000010; EGS34464.1; -; Genomic_DNA. DR EnsemblBacteria; EGS34464; EGS34464; HMPREF9489_1263. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23814 MW; 872D2518B5DC98A6 CRC64; MRKKLNLSLY LVTDRTNVED EEKFLTKIEE SLKGGVTLVQ LREKNISTKE YIDLAKKVKI ICDKFEVPLL IDDRIDVCLA SECAGVHLGD EDMEIKDARK ILGDNYIIGA TAKSVERAVQ CEKEGADYLG VGAIYPTKTH VKTKITSVDT LRDINNSINI KTVAIGGLNE DNMDVLKNSG ASGIAVVRAL MNDDNPQEKA HRLLEKSKQI LELR // ID F9N020_FINMA Unreviewed; 212 AA. AC F9N020; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_2; Synonyms=thiE; ORFNames=HMPREF9489_1443; OS Finegoldia magna SY403409CC001050417. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Finegoldia. OX NCBI_TaxID=866779; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SY403409CC001050417; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUI01000010; EGS34303.1; -; Genomic_DNA. DR ProteinModelPortal; F9N020; -. DR EnsemblBacteria; EGS34303; EGS34303; HMPREF9489_1443. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23461 MW; 67152E1CA9AE7BC1 CRC64; MNKQFNLGLN LVTNKQTLKG RDLTETIEIA LKNGADSVRL REKNMDTRSI MQEAFKIKEI TQRMGKLLIV NDRVDIAKAC DVDGVHLGQK DMPIKYAREM LGDDKIIGIS CHTLEQALEA QEAGADYIGV GAIFPTFTGD DFVRVTIDTL KEISEKIHVP ITAIGGINKN NIRMIFDSNV DSVSLTSAVF STGDVAASTQ ELKQKFDMIL KK // ID F9N3T2_9FIRM Unreviewed; 278 AA. AC F9N3T2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI domain protein; GN ORFNames=HMPREF9200_1541; OS Veillonella sp. oral taxon 780 str. F0422. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=944564; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0422; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUJ01000005; EGS39860.1; -; Genomic_DNA. DR EnsemblBacteria; EGS39860; EGS39860; HMPREF9200_1541. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 278 AA; 31906 MW; 4ABA67F5DAC89E3C CRC64; MCSMKKNNQS IDTLVLITNR QLLKDDISLA TYGVALSRGI ERIQKYGKHC INHTEESSLP YNIRRAYRST VKANLHSTRL PKQRADSAEP DNWMRNHSSL YTLCRDTDLP FEEYLQLCDA IGDTVVHHGK VITNREQLGV VLATAKRIHL PTNLIRYWQS EQEELWITLQ QCFQDITMWS TVHNQDDIKL LASLGIPNLE YVLISPIFPT PCKTGHPGIG VSRGEILLQQ MQNHYRYVKG IALGGIHEYN YQQCLQYSFT GVAIMSDFMK RVHSNIDT // ID F9N738_9FIRM Unreviewed; 223 AA. AC F9N738; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9200_0300; OS Veillonella sp. oral taxon 780 str. F0422. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=944564; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0422; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUJ01000059; EGS33020.1; -; Genomic_DNA. DR EnsemblBacteria; EGS33020; EGS33020; HMPREF9200_0300. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24918 MW; DC15F0E7465633CC CRC64; MKHHDIDTVR SMIGVYFICG TPNTKDIHTT LTEACKGGIT CFQFREKGEG ALVGEEKEQL ARELQHICKE YGVPFIINDD VELAEKIGAD GVHVGQDDMD LDEVRKRLPH ALVGTSINSV EELENTKLDY VDYIGVGPMY ETSTKKDAKT VRGPELILAL RAHSPTIPMV AIGGINRDNF DDVLAEPVDG IAVISAITEM EDIEYETAMW IENMEWCKMF LEK // ID F9N9X5_9ACTO Unreviewed; 216 AA. AC F9N9X5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9949_1673; OS Propionibacterium sp. CC003-HC2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1005703; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CC003-HC2; RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., RA Methe B., Sutton G., Nelson K.E.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUK01000001; EGR90374.1; -; Genomic_DNA. DR ProteinModelPortal; F9N9X5; -. DR EnsemblBacteria; EGR90374; EGR90374; HMPREF9949_1673. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F9NAW4_9ACTO Unreviewed; 217 AA. AC F9NAW4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9949_0613; OS Propionibacterium sp. CC003-HC2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1005703; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CC003-HC2; RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., RA Methe B., Sutton G., Nelson K.E.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUK01000001; EGR89407.1; -; Genomic_DNA. DR EnsemblBacteria; EGR89407; EGR89407; HMPREF9949_0613. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22390 MW; E5AE81023BCB1FFC CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F9NMU5_PROAA Unreviewed; 216 AA. AC F9NMU5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9205_0326; OS Propionibacterium acnes SK182. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=679193; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK182; RA Durkin A.S., Madupu R., Hostetler J., Radune D., Torralba M., RA Methe B., Sutton G., Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Propionibacterium acnes SK182."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUM01000003; EGR95728.1; -; Genomic_DNA. DR ProteinModelPortal; F9NMU5; -. DR EnsemblBacteria; EGR95728; EGR95728; HMPREF9205_0326. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID F9NQ44_PROAA Unreviewed; 217 AA. AC F9NQ44; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9205_1149; OS Propionibacterium acnes SK182. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=679193; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK182; RA Durkin A.S., Madupu R., Hostetler J., Radune D., Torralba M., RA Methe B., Sutton G., Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Propionibacterium acnes SK182."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUM01000011; EGR94592.1; -; Genomic_DNA. DR ProteinModelPortal; F9NQ44; -. DR EnsemblBacteria; EGR94592; EGR94592; HMPREF9205_1149. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F9NTX8_PROAA Unreviewed; 216 AA. AC F9NTX8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1162_0503; OS Propionibacterium acnes SK182B-JCVI. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1051006; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK182B-JCVI; RA Durkin A.S., Madupu R., Hostetler J., Radune D., Torralba M., RA Methe B., Sutton G., Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Propionibacterium acnes SK182B-JCVI."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUN01000007; EGR97806.1; -; Genomic_DNA. DR EnsemblBacteria; EGR97806; EGR97806; HMPREF1162_0503. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22667 MW; 4F587C36635C87DB CRC64; MSRPKFDLSV YLVTDTAQCG GPDEVVETVR RAIAGGVTLV QFRDHDLPDD EFVTLGRRVR EICVSGGVPL IIDDRVHLVT EIGADGAHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSHGRDIV DYLGVGALHG SGTKPEAGEL GLVGIRDVVD ASPWPVCVIG GVSASDAQDI ARVGCDGLSV VSAICRSTDP QSRARELAEA WRAAKK // ID F9NY22_PROAA Unreviewed; 220 AA. AC F9NY22; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1162_1523; OS Propionibacterium acnes SK182B-JCVI. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1051006; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK182B-JCVI; RA Durkin A.S., Madupu R., Hostetler J., Radune D., Torralba M., RA Methe B., Sutton G., Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Propionibacterium acnes SK182B-JCVI."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUN01000047; EGR94534.1; -; Genomic_DNA. DR EnsemblBacteria; EGR94534; EGR94534; HMPREF1162_1523. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 220 AA; 22642 MW; 89ACD33E2D69686E CRC64; MTLDLRCYLV TSGSDRHTVE TAALAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAMRA QGNVHGVHVG SQDLPVRDTR AMLGPDAIVG YTTGTLDLVR SAELFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVA ASSLPIVAIG DVQVADVPAL AATGVAGIAM VRAIMASADP AAVVRQVVQA FDEVRVSSGS // ID F9P3F1_STRMT Unreviewed; 210 AA. AC F9P3F1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9178_1753; OS Streptococcus mitis bv. 2 str. F0392. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=768726; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0392; RA Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M., RA Methe B., Sutton G., Nelson K.E.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUO01000001; EGR92895.1; -; Genomic_DNA. DR EnsemblBacteria; EGR92895; EGR92895; HMPREF9178_1753. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; 88D1AD3B7E2C1AC6 CRC64; MNREALRLYL VTNRYQDSLK SFLEKVETTC HSGVTIIQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE EGGADYLGTG AIFPTTTKEN APITLISTLK TICQKVAIPV VAIGGLTSEN IDQLAATGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDDIIS // ID F9PJV5_9ACTO Unreviewed; 220 AA. AC F9PJV5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9058_2225; OS Actinomyces sp. oral taxon 175 str. F0384. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Actinomycineae; Actinomycetaceae; Actinomyces. OX NCBI_TaxID=944560; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0384; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUR01000001; EGV14507.1; -; Genomic_DNA. DR EnsemblBacteria; EGV14507; EGV14507; HMPREF9058_2225. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22559 MW; F791EE275EB67408 CRC64; MRAAPDLSVY LVTDEGQCRS RGRDVLATVE AAVDGGVTCV QLRAKGTDGG LFLTQVLEVA EVIGDQVPVI VNDRVDIFLA ARDQGAPVAG VHLGQSDLPA RIARRLVGEE AYLGLSAATP DELRTAQEQG ACDHVGIGVV HPTATKADAP KSLGVNGVTR MAALIDLPAV AIGGITAGDL PALRAGGLAG AAVVSAICTA EDPRSVAADL HRAWDEGCRR // ID F9Q2D1_STROR Unreviewed; 144 AA. AC F9Q2D1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9950_1212; OS Streptococcus oralis SK313. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1035190; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK313; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUU01000003; EGV01529.1; -; Genomic_DNA. DR EnsemblBacteria; EGV01529; EGV01529; HMPREF9950_1212. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 144 AA; 14999 MW; 5A2A5303F4E0F845 CRC64; MIIDDRLDVC LAVDAAGLHI GDDELPVSVA RKVLGPEKIL GVTAKTVKRA LEAETSGADY LGTGAIFPTT TKENAPITLI STLKTICQTV AIPVVAIGGL TSENIDQLIG TGIAGVAVVR DLMQAEDIEA KTQAFLTKLD DIVS // ID F9Q2D2_STROR Unreviewed; 66 AA. AC F9Q2D2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI domain protein; GN ORFNames=HMPREF9950_1213; OS Streptococcus oralis SK313. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1035190; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK313; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUU01000003; EGV02062.1; -; Genomic_DNA. DR EnsemblBacteria; EGV02062; EGV02062; HMPREF9950_1213. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 66 AA; 7775 MW; 50DE7DD3A8409A97 CRC64; MNRKVLKLYL VTNRYQDSLE SFLEKVETAC RSGVTIIQLR EKISPPINTI NWQNKSRKLQ MPIRSP // ID F9R585_ECOLX Unreviewed; 211 AA. AC F9R585; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IAE_18862; OS Escherichia coli XH140A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1068608; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XH140A; RX PubMed=21994923; DOI=10.1128/JB.06011-11; RA Yang H., Liao Y., Wang B., Lin Y., Pan L.; RT "Genome Sequence of Escherichia coli XH140A, Which Produces L- RT Threonine."; RL J. Bacteriol. 193:6090-6091(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XH140A; RA Yang H.L., Liao Y.L., Lin Y., Pan L.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFVX01000048; EGU25312.1; -; Genomic_DNA. DR ProteinModelPortal; F9R585; -. DR SMR; F9R585; 20-202. DR EnsemblBacteria; EGU25312; EGU25312; IAE_18862. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID F9REN4_9VIBR Unreviewed; 419 AA. AC F9REN4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VIBRN418_03881; OS Vibrio sp. N418. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=701176; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=N418; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWD01000063; EGU32376.1; -; Genomic_DNA. DR EnsemblBacteria; EGU32376; EGU32376; VIBRN418_03881. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 419 AA; 46264 MW; E2E2AD548DDFBC6F CRC64; MVEILVPSSS IELTAEIQQA LLVAEQNGFA IDQVMLGVSS TSLFAINLAD KQFVIGADFI GSDDSVSDYH LCYSNQKSLV AAPSQRNTIS LGLADSGHAL DIWHHPLGDE VRALSYPLQT LDDKQQPRHL SWVLVLLSLE FPIEDCLTLA RAMINVSRET WAADFTLFPR PVLEDKRLGI QVGWSVQRCA ASFARLDKQK IGLYPVVDSV EWVERLLKLG VNTVQLRIKD ASQSDLEAQV KHAIALGKQH NSQVFINDYW QLALKYGAFG VHLGQEDIEH ADLSSINQAG VCLGLSTHGY FELLRISQLK PSYIALGHIF PTTTKEMPSK PQGLVRLTLY QRLIDTIPYH DELGYPTVAI GGIDLATAPE VWCCGVSSLA VVRAITLAPD PQKVLSEFGR VMQPKTRMCL SERGAEHVI // ID F9RHV4_9VIBR Unreviewed; 210 AA. AC F9RHV4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VIBRN418_16798; OS Vibrio sp. N418. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=701176; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=N418; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWD01000099; EGU29261.1; -; Genomic_DNA. DR EnsemblBacteria; EGU29261; EGU29261; VIBRN418_16798. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22365 MW; 88A7A4A550809954 CRC64; MNPYRLYLVT DDQQDLATLK HVVQQAVAGG VTMVQVREKH GDIRAFIERA RAVKVLLEGT SVALIINDRI DVALAVDADG VHLGQSDMPV ELARQLIGKN KILGLSIEDE NQLIIANSLP IDYIGLSAIF PTASKTNTKK HWGLEGLTMA LRCTSLPIVA IGGINESNIP ALCKTGVQGL AIVSAICHAQ DPKAASANLL NLIQTASKSG // ID F9RVE9_9VIBR Unreviewed; 419 AA. AC F9RVE9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VIS19158_13717; OS Vibrio scophthalmi LMG 19158. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=870967; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 19158; RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0; RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., RA Naum M., McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.; RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge RT Scleritoderma cyanea."; RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWE01000224; EGU29596.1; -; Genomic_DNA. DR EnsemblBacteria; EGU29596; EGU29596; VIS19158_13717. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 419 AA; 46350 MW; DAB56645236B16E1 CRC64; MVEILVPSSA IELTAEIQQA LLVAEQNGFA IDQVMLGVSS TSLFAINLAD KKLVIGADFI GSDDSVSDYH LCYSNQKSVV TAPSQRNTIS LGLADSGHAL DIWHHPLGDE VRALSYPLQT LDDKQQPRHL SWVLVLLSLE FPIEDCLTLA RAMINVSRET WAADFTQFPR PVLEDKRLGI QVGWSTQRCA ASFTRLDKQK IGLYPVVDSV EWVEKLLKLG VNTVQLRIKD ANQSDLEAQV KHAIDLGKQH NSQVFINDYW QLALKYGAFG VHLGQEDIEH ADLSSINQAG VCLGLSTHGY FELLRISQLK PSYIALGHIF PTTTKEMPSK PQGLVRLALY QRLIDTIPYH DELGYPTVAI GGIDLATAPE VWCCGVSSLA VVRAITLAPD PQKVLSEFGR VMQPKTRMYL SERGAEHVI // ID F9S403_9VIBR Unreviewed; 419 AA. AC F9S403; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=VII00023_18544; OS Vibrio ichthyoenteri ATCC 700023. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=870968; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700023; RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0; RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., RA Naum M., McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.; RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge RT Scleritoderma cyanea."; RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWF01000193; EGU37334.1; -; Genomic_DNA. DR EnsemblBacteria; EGU37334; EGU37334; VII00023_18544. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 419 AA; 46270 MW; 52AB242BBD14D83C CRC64; MVEILVPSSS IELTAHIQQA LLVAKQNGFA VEEVTLGVSS ASQFEIKLAD IELVIGADLI GSASGVSDFY LSYTPQSSEV AAPSQRSLIA VGLVDSHNCL DVWYHPLADE VRALSYSPQF LDANQQQRHL SWVVTLLSLG FPIEDSLTVA RAMMNVSRET WASEYRHYPR PVLDDPRLGI QVDWSTQCKM QPFAYLDKTQ MGLYPVVDSV EWIERLLKLG VRTLQLRIKD ASQVDLEAQV SRAIALGKQY NGHVYINDYW QLAIKHGAYG VHLGQEDIEQ ANLSLINQAG IRLGLSTHGY FELLRISQLQ PSYIALGHIF PTTTKQMPSK PQGLVRLALY QRLIDTIPFH HELGYPTVAI GGIDLETAPA VWCCGVSSLA VVRAITLAAE PKRTMLGFAQ IMQPRESSSV AKRGAGYAI // ID F9SIQ4_VIBSP Unreviewed; 430 AA. AC F9SIQ4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VISP3789_14828; OS Vibrio splendidus ATCC 33789. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1051645; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33789; RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0; RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., RA Naum M., McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.; RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge RT Scleritoderma cyanea."; RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWG01000041; EGU40741.1; -; Genomic_DNA. DR EnsemblBacteria; EGU40741; EGU40741; VISP3789_14828. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 430 AA; 47557 MW; CA047FBAC8B4AA47 CRC64; MTVKILIPSQ YIELTGEVQH CLLVAKRQGL ATVAVELGVS PTQYFSIVDS QHSLAIGFAS DVVSVKSEQL SSLDHIVSYD ESLSLTDVRD ALAQYPNTIH VGVADEAAVL DIWSHLNANR AIKSITTDHQ AIDSRHHFAW FLTLLALDFP LEDALVLARA ASNVSRGTWP SHYQEFPIPV LEDKRLGISV GWTHQGTSLS FPDLTKKSLG LYPVVDDVDW IERLLKLGIN TVQLRIKNPQ QADLEHQVAR SIVLGRQYQA QVFINDYWQL ALKHGAFGVH LGQEDIEESN LSQLSKAGIK IGLSTHGYYE LLRIVQINPS YIALGHIFPT TTKQMPSKPQ GLVRLALYQQ LIDTIPYSEE LIGYPTVAIG GIDQSTAEQV WDCGVSSLAV VRAITLAEDP KAVIEFFEAL MNGNSSTFTE EVTQELSYAE // ID F9T6U9_9VIBR Unreviewed; 458 AA. AC F9T6U9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=VITU9109_19612; OS Vibrio tubiashii ATCC 19109. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1051646; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19109; RA Hoffman M., Strain E.A., Brown E., Allard M.W.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19109; RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0; RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., RA Naum M., McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.; RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge RT Scleritoderma cyanea."; RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWI01000155; EGU54372.1; -; Genomic_DNA. DR EnsemblBacteria; EGU54372; EGU54372; VITU9109_19612. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 458 AA; 51094 MW; 4F3C186A0233534E CRC64; MSKILIPSSL IELTGLVQQC LLLAKERGFC VEEVELGVSP TQSVQLVRDQ QITHVATDLI DGYDYDSDYP FTLYYRSGLS VEACAEQPSN AIYIGIADGL ACDKKDEVLQ IDIWRHPIND EVRALSVKSK LNSVFESEYH FAWIVVLTVL DFPIEDALTL ARGMTTQQAN VSRETVLNEK SLTHWAEHFN EFPTPVLEDS RLGIQVGWSA QGESVRFANL TKQSLGLYPV VDDVAWIERL LPLGINTIQL RIKNPQQADL EQQIIRAIEL GRQYKAQVFI NDYWQLAIKH GAYGVHLGQE DIEESNLAQL TKAGIHLGLS THGYYELLRI VQIHPSYIAL GHIFPTTTKQ MPSKPQGLVR LALYQKLIDS IPYGCAHEGA SGLALGYPTV AIGGIDQSNA DQVWQTGVSS LAVVRAITLA QSPKPVIEFF NQLMKERQST FTDSISIATN EEREQHAH // ID F9TSY5_9VIBR Unreviewed; 397 AA. AC F9TSY5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VINI7043_25762; OS Vibrio nigripulchritudo ATCC 27043. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1051649; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27043; RA Hoffman M., Strain E.A., Brown E., Allard M.W.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27043; RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0; RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., RA Naum M., McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.; RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge RT Scleritoderma cyanea."; RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWJ01000297; EGU54577.1; -; Genomic_DNA. DR EnsemblBacteria; EGU54577; EGU54577; VINI7043_25762. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 397 AA; 44071 MW; 207A6252B1C609C4 CRC64; MPQLLLPQDK VHLTGLVQSR LLLAKEQGFD ISDIELGISP TPLVQCHVDD RTTTLFLGEG ESDADFVCRF ASGQASPLAI SDLSKQANLL LLDVYHDFQL VDLWAHEGTN RAIAFEGSPL NEQEQESYVA WLLTALVIDF PIEDALVIAR AAVRDDVSRE TWPLNLDAFP VPVLSDSLLN IDVGWNIESD IQFPSTDSER LKLYPVVDTV EWVARLLELG VKTVQLRIKD SQDPGLESKV KQAIELGQQY DAQVYINDYW QLAIKHGAYG VHLGQEDLEV AELDDIADAG LRIGLSTHGY YEILRIKQVN PSYIALGHIF PTTTKVMPSR PQGLVRLELY QKLVGTFPTV AIGGIDLERA PSVWKCGVSS LAVVRAITLS DDPKEVIEKF NTLMSSR // ID F9TTZ2_9VIBR Unreviewed; 209 AA. AC F9TTZ2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VINI7043_13296; OS Vibrio nigripulchritudo ATCC 27043. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1051649; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27043; RA Hoffman M., Strain E.A., Brown E., Allard M.W.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27043; RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0; RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., RA Naum M., McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.; RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge RT Scleritoderma cyanea."; RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWJ01000310; EGU52886.1; -; Genomic_DNA. DR EnsemblBacteria; EGU52886; EGU52886; VINI7043_13296. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22450 MW; CB42993C8ED0037D CRC64; MNPYPLYLVT DDRQNLDTFC HVVEQAAKGG VTMIQVREKH GDVRAFIERA ARAKSILEGT NIPLIINDRV DVALAVDADG VHLGQSDMPA EIARKLIGDN KILGLSVENE AQLEEAKSLP VDYLGVSAIF STPTKTDIKR EWGIDGLAYA VRTSPFPTVA IGGINHTNLS DVLGTGVNGI ALVSAICQAE DPKSASESLL KSIKLCQNQ // ID F9U6K0_9GAMM Unreviewed; 211 AA. AC F9U6K0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ThimaDRAFT_0551; OS Thiocapsa marina 5811. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiocapsa. OX NCBI_TaxID=768671; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5811; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L., RA Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., RA Frigaard N.-U., Bryant D., Woyke T.J.; RT "The draft genome of Thiocapsa marina 5811."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWV01000002; EGV19876.1; -; Genomic_DNA. DR EnsemblBacteria; EGV19876; EGV19876; ThimaDRAFT_0551. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21824 MW; 7AD961D5636F4F0A CRC64; MTHLDGLYLI TPDTADAPDV LAEQVAQAIS GGAGLVQYRH KGPDRQLRRD QATALLGVCR IARVPFIVND DVALAAEIGA DGVHLGRDDG DPMAARRRLG ANAVIGVSCY DDLTLARAAE RAGASYVAFG SFFPSATKPH AVRASPELLS AARDSLRIPA VAIGGITPQN GGLLIAAGAR MLAVVTGVFA QPDLAAAARA YASLFVDGDP R // ID F9U8H6_9GAMM Unreviewed; 308 AA. AC F9U8H6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=ThimaDRAFT_1034; OS Thiocapsa marina 5811. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiocapsa. OX NCBI_TaxID=768671; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5811; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L., RA Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., RA Frigaard N.-U., Bryant D., Woyke T.J.; RT "The draft genome of Thiocapsa marina 5811."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWV01000003; EGV19588.1; -; Genomic_DNA. DR EnsemblBacteria; EGV19588; EGV19588; ThimaDRAFT_1034. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 308 AA; 32843 MW; 88C3F8438F6B846A CRC64; MVGAISDSAG RVLVTKRPDH VHQGGLWEFP GGKLEPGESP EQGLARELAE ELGIEVRDSR PLIRIRHHYG DRHVLLDVRR VESYAGIPAG LEGQPLAWQS PETLDPGCFP AADRPIITAL RLPACILITG SDPLEPEVFL ARIAQAVAGG IKLVQLRAHG LNQGAYGDLA RRAFVLCAQG GARLLLNRDP DETLGIPRHG LHLGGQALAR LTERPGRPDD LVGASCHAAD DLLRAARLGL DYALLSPVQP TASHPEAEPL GWQRFAELTD AATLPVYALG GVTGADLDVA REHGAQGVAG IRGFWSID // ID F9UWM2_MYCBI Unreviewed; 222 AA. AC F9UWM2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BCGM_0421c; OS Mycobacterium bovis BCG str. Moreau RDJ. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=413996; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Moreau RDJ; RA Gomes L.H., Otto T.D., Vasconcellos E.A., Ferrao P.M., Maia R.M., RA Moreira A.S., Ferreira M.A., Castello-Branco L.R., Degrave W.M., RA Mendonca-Lima L.; RT "Genome Sequence of Mycobacterium bovis BCG Moreau, the Brazilian RT Vaccine Strain against Tuberculosis."; RL J. Bacteriol. 193:5600-5601(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM412059; CCC63014.1; -; Genomic_DNA. DR ProteinModelPortal; F9UWM2; -. DR SMR; F9UWM2; 1-221. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID F9VQT3_9ACTO Unreviewed; 265 AA. AC F9VQT3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GOALK_016_00950; OS Gordonia alkanivorans NBRC 16433. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1027371; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 16433; RA Hosoyama A., Nakamura S., Takarada H., Tsuchikane K., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Gordonia alkanivorans NBRC 16433."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BACI01000016; GAA10972.1; -; Genomic_DNA. DR EnsemblBacteria; GAA10972; GAA10972; GOALK_016_00950. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 87 91 HMP-PP binding (By similarity). FT REGION 194 196 THZ-P binding (By similarity). FT METAL 129 129 Magnesium (By similarity). FT METAL 148 148 Magnesium (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 167 167 HMP-PP (By similarity). FT BINDING 197 197 HMP-PP (By similarity). FT BINDING 225 225 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 265 AA; 27713 MW; F93076089D07F02F CRC64; MTRIRFDGLR RGPHSQPACP GSRVFSRSTL RPAGRRRASL VAVTTASESR RRLDSARLYL CTDARRERGD LLDFVGSALA GGVDIVQLRD KGSAGEKKFG TLEAREELEI LAALRGVVDA HGALLAVNDR ADIAALSGAD VLHVGQGDLP PEVARRIVGP DTIIGASTHD REQAAAATAD PDVDYFCVGP CWTTPTKPGR SAAGLDLVTT TAGAAPGKPW FAIGGIDAPR VPEVTAAGAR RIVVVRAITA ATDPAAAAAD LLGRW // ID F9X559_MYCGM Unreviewed; 515 AA. AC F9X559; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 17. DE SubName: Full=Uncharacterized protein; GN ORFNames=MYCGRDRAFT_69865; OS Mycosphaerella graminicola (strain CBS 115943 / IPO323) (Speckled leaf OS blotch fungus) (Septoria tritici). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae; OC Zymoseptoria. OX NCBI_TaxID=336722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 115943 / IPO323; RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070; RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H., Crane C.F., RA Hane J.K., Foster A.J., Van der Lee T.A., Grimwood J., Aerts A., RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., RA van der Burgt A., Canto-Canche B., Churchill A.C., Conde-Ferraez L., RA Cools H.J., Coutinho P.M., Csukai M., Dehal P., De Wit P., RA Donzelli B., van de Geest H.C., van Ham R.C., Hammond-Kosack K.E., RA Henrissat B., Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., RA Kuzniar A., Lindquist E., Lombard V., Maliepaard C., Martins N., RA Mehrabi R., Nap J.P., Ponomarenko A., Rudd J.J., Salamov A., RA Schmutz J., Schouten H.J., Shapiro H., Stergiopoulos I., RA Torriani S.F., Tu H., de Vries R.P., Waalwijk C., Ware S.B., RA Wiebenga A., Zwiers L.H., Oliver R.P., Grigoriev I.V., Kema G.H.; RT "Finished genome of the fungal wheat pathogen Mycosphaerella RT graminicola reveals dispensome structure, chromosome plasticity, and RT stealth pathogenesis."; RL PLoS Genet. 7:E1002070-E1002070(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001198; EGP89383.1; -; Genomic_DNA. DR RefSeq; XP_003854407.1; XM_003854359.1. DR EnsemblFungi; Mycgr3T69865; Mycgr3P69865; Mycgr3G69865. DR GeneID; 13404181; -. DR KEGG; ztr:MYCGRDRAFT_69865; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 515 AA; 53887 MW; E5C69780F9BA462B CRC64; MAVDYSVYLV TDSTPAILGD KDLLTVVQAA VDGGVTIVQY RDKTSDTADL VRIAKELHKI TKAAGVPLLI NDRVDVALAA GVEGVHVGQD DIDLQTARKL LGPDAIIGVT ANREEEALIA ATAGADYLGI GTVYATPTKE NTKSIIGTAG VQQVLTSLAA KKLDVKTVCI GGINASNLQR VLYQSASPQK KLDGVAVVSA IIASDNAKEA ASKIRELVHQ PPPFAISSTK PKLSQQDIIS KVPGIIRRMA EKKPLCHNMT NLVVQNFAAN VALAIGSSPI MSNNGLEAGD LAALGGSLVI NMGTTTPEIR ANHLKSLAAY NAIGGPVLFD PVGAGATQQR RDGVKALMAG GYFDVIKGNE GEIRTVAGSA GVKQHGVDSG ASQLSLDERV TLVKATALRE HNIILMTGST DVISDGERTV TISNGHEYLG EITGSGCTLG TTIASVLAAE REDKLLAAVC AILMYEIAAE RAAVREDVKG PGTFVPAFID ELFRIRQESV RGSTDWAQAA KIEVL // ID F9XUH0_CAMFE Unreviewed; 140 AA. AC F9XUH0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 22-JAN-2014, entry version 12. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=CFV354_0845; OS Campylobacter fetus subsp. venerealis NCTC 10354. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=983328; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 10354; RA Stynen A.P.R., Ruiz J.C., Rezende A.M., Moore R., Lage A.P.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001228; EGU23892.1; -; Genomic_DNA. DR EnsemblBacteria; EGU23892; EGU23892; CFV354_0845. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 140 AA; 15927 MW; 3A62965E0E372D0D CRC64; MLSYAITDPK LYSNLKDSFF KFERLQTADF ILFRDKICSD YVKKAEIFMS LKPNFKAKFI IHNDLNLALN LKADGIHFSS NLIANLKNTP QSLIKFASTH NEKEIEDAIK LGADFITFSP IFSTPNKGEP VGIETLKKSF // ID F9XVU2_CAMFE Unreviewed; 202 AA. AC F9XVU2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CFV354_1339; OS Campylobacter fetus subsp. venerealis NCTC 10354. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=983328; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 10354; RA Stynen A.P.R., Ruiz J.C., Rezende A.M., Moore R., Lage A.P.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001228; EGU24322.1; -; Genomic_DNA. DR EnsemblBacteria; EGU24322; EGU24322; CFV354_1339. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 202 AA; 22069 MW; E5A9597EE18F7F10 CRC64; MCQLYVLTDK ELTPQNSISQ QILELLNSGI KLIQYRNKTQ DHDIKLLKSI ANLCDDFNAK FIINDDPFLA KACGAHGVHI GKDDEDIKKA KELLGKNSII GVSCYNDISL ALKAQKDGAS YVAFGAMYPS QTKPNAPLCD HNTIKKAKEN LNVPICVIGG INALNLKEVS ALMPDLIAIV SAAYSPKSIS ENITNLNNII RN // ID F9Y225_BIFBU Unreviewed; 917 AA. AC F9Y225; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 22. DE SubName: Full=Thiamine biosynthesis protein thiC; GN Name=thiC; Synonyms=thiE; OrderedLocusNames=Bbr_1312; OS Bifidobacterium breve (strain NCIMB 8807 / UCC2003). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=326426; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIMB 8807 / UCC2003; RX PubMed=21690406; DOI=10.1073/pnas.1105380108; RA O'Connell Motherway M., Zomer A., Leahy S.C., Reunanen J., RA Bottacini F., Claesson M.J., O'Brien F., Flynn K., Casey P.G., RA Moreno Munoz J.A., Kearney B., Houston A.M., O'Mahony C., RA Higgins D.G., Shanahan F., Palva A., de Vos W.M., Fitzgerald G.F., RA Ventura M., O'Toole P.W., van Sinderen D.; RT "Functional genome analysis of Bifidobacterium breve UCC2003 reveals RT type IVb tight adherence (Tad) pili as an essential and conserved RT host-colonization factor."; RL Proc. Natl. Acad. Sci. U.S.A. 108:11217-11222(2011). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000303; ABE95987.1; -; Genomic_DNA. DR RefSeq; YP_007555112.1; NC_020517.1. DR EnsemblBacteria; ABE95987; ABE95987; Bbr_1312. DR GeneID; 14790704; -. DR KEGG; bbru:Bbr_1312; -. DR KO; K03147; -. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100181 MW; D803622E603CC38F CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVQLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLAGTKA AGWFAVSAIA GAENPEGATR AMVEGWKAVR GDKKHGYAPR IVAHAPAADT QAAQEGTAAA GSEDTEKKFT NAKQAKDAQK LAKQQRVDIA ARGSEQRDKA HIRKTKTVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYSTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHQPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AQDRDDAISK ARFEFRWLDQ FNLSYDPDTA IAFHDETLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LAKAKANVDN DVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID F9Y6Y9_KETVW Unreviewed; 212 AA. AC F9Y6Y9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 19. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=KVU_1168; OS Ketogulonicigenium vulgare (strain WSH-001). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ketogulonicigenium. OX NCBI_TaxID=759362; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSH-001; RX PubMed=21994934; DOI=10.1128/JB.06007-11; RA Liu L., Li Y., Zhang J., Zhou Z., Liu J., Li X., Zhou J., Du G., RA Wang L., Chen J.; RT "Complete Genome Sequence of the Industrial Strain Ketogulonicigenium RT vulgare WSH-001."; RL J. Bacteriol. 193:6108-6109(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002018; AEM41006.1; -; Genomic_DNA. DR RefSeq; YP_005795002.1; NC_017384.1. DR EnsemblBacteria; AEM41006; AEM41006; KVU_1168. DR GeneID; 12374040; -. DR KEGG; kvl:KVU_1168; -. DR KO; K00788; -. DR BioCyc; KVUL759362:GLEX-1212-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 212 AA; 23295 MW; 8732AD9CD1801335 CRC64; MTDTTTAADD LPQIYLISPP TFDLDVFPDL MARCLDAVET SCVRLSLATR DEDVIQRAAD SLRQITHDRD IALVIENHAL LVERLGLDGV HLTDGSRSVH KMRRDLGEDA IVGTYCGTSR HDGMTAGDMG ADYVSFGPVG QSLLGTGERA TLDLFQWWSE MIEVPAVTEG GLDEELIRQL APYSDFFGFG EEIWATEDPV ATYQRLVAAT RG // ID F9YJI7_BRUPB Unreviewed; 221 AA. AC F9YJI7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 17. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=BPI_I1768; OS Brucella pinnipedialis (strain NCTC 12890 / BCCN 94-73 / B2/94). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520461; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 12890 / BCCN 94-73 / B2/94; RX PubMed=21745361; DOI=10.1186/1471-2148-11-200; RA Audic S., Lescot M., Claverie J.M., Cloeckaert A., Zygmunt M.S.; RT "The genome sequence of Brucella pinnipedialis B2/94 sheds light on RT the evolutionary history of the genus Brucella."; RL BMC Evol. Biol. 11:200-200(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002078; AEK55004.1; -; Genomic_DNA. DR RefSeq; YP_004756772.1; NC_015857.1. DR ProteinModelPortal; F9YJI7; -. DR EnsemblBacteria; AEK55004; AEK55004; BPI_I1768. DR GeneID; 10998245; -. DR KEGG; bpp:BPI_I1768; -. DR KO; K00788; -. DR BioCyc; BPIN520461:GJF0-1766-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID F9YWL8_PROAA Unreviewed; 217 AA. AC F9YWL8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; ORFNames=PAZ_c01210; OS Propionibacterium acnes 266. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=909952; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=266; RA Brzuszkiewicz E.B., Thuermer A., Wollherr A., Liesegang H., RA Lehmann R., Gottschalk G., Brueggemann H., Daniel R.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=266; RX PubMed=21738717; DOI=10.1371/journal.pone.0021581; RA Brzuszkiewicz E., Weiner J., Wollherr A., Thurmer A., Hupeden J., RA Lomholt H.B., Kilian M., Gottschalk G., Daniel R., Mollenkopf H.J., RA Meyer T.F., Bruggemann H.; RT "Comparative Genomics and Transcriptomics of Propionibacterium RT acnes."; RL PLoS ONE 6:E21581-E21581(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002409; AEE71328.1; -; Genomic_DNA. DR RefSeq; YP_005941359.1; NC_017534.1. DR ProteinModelPortal; F9YWL8; -. DR EnsemblBacteria; AEE71328; AEE71328; PAZ_c01210. DR GeneID; 12531915; -. DR KEGG; paw:PAZ_c01210; -. DR KO; K00788; -. DR BioCyc; PACN909952:GLIJ-121-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID F9Z118_PROAA Unreviewed; 188 AA. AC F9Z118; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; ORFNames=PAZ_c09230; OS Propionibacterium acnes 266. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=909952; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=266; RA Brzuszkiewicz E.B., Thuermer A., Wollherr A., Liesegang H., RA Lehmann R., Gottschalk G., Brueggemann H., Daniel R.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=266; RX PubMed=21738717; DOI=10.1371/journal.pone.0021581; RA Brzuszkiewicz E., Weiner J., Wollherr A., Thurmer A., Hupeden J., RA Lomholt H.B., Kilian M., Gottschalk G., Daniel R., Mollenkopf H.J., RA Meyer T.F., Bruggemann H.; RT "Comparative Genomics and Transcriptomics of Propionibacterium RT acnes."; RL PLoS ONE 6:E21581-E21581(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002409; AEE72102.1; -; Genomic_DNA. DR RefSeq; YP_005942133.1; NC_017534.1. DR EnsemblBacteria; AEE72102; AEE72102; PAZ_c09230. DR GeneID; 12532713; -. DR KEGG; paw:PAZ_c09230; -. DR KO; K00788; -. DR BioCyc; PACN909952:GLIJ-919-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 113 115 THZ-P binding (By similarity). FT REGION 163 164 THZ-P binding (By similarity). FT METAL 46 46 Magnesium (By similarity). FT METAL 65 65 Magnesium (By similarity). FT BINDING 45 45 HMP-PP (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 143 143 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 188 AA; 19593 MW; 0C374D5A47C6461C CRC64; MRHAIAGGVT LVQFRDHDLS DDEFVALGRR VREICVSGGV PLIIDDRVHL VAEIGADGVH VGQSDMPVDQ ARAILGDDLL IGLSAQTPAH VEAALSQGRD IVDYLGVGAL HGTGTKPEAG ELGLAEIRDV VNASPWPVCV IGGVSASDAQ DVARVGCDGL SVVSAICRST DPKSSARELA EAWRTAKE // ID F9Z6S8_ODOSD Unreviewed; 655 AA. AC F9Z6S8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Odosp_0632; OS Odoribacter splanchnicus (strain ATCC 29572 / DSM 20712 / JCM 15291 / OS NCTC 10825 / 1651/6) (Bacteroides splanchnicus). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Odoribacter. OX NCBI_TaxID=709991; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6; RX PubMed=21677857; DOI=10.4056/sigs.1714269; RG US DOE Joint Genome Institute (JGI-PGF); RA Goker M., Gronow S., Zeytun A., Nolan M., Lucas S., Lapidus A., RA Hammon N., Deshpande S., Cheng J.F., Pitluck S., Liolios K., RA Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., RA Tapia R., Han C., Goodwin L., Chen A., Palaniappan K., Land M., RA Hauser L., Jeffries C.D., Brambilla E.M., Rohde M., Detter J.C., RA Woyke T., Bristow J., Markowitz V., Hugenholtz P., Eisen J.A., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Odoribacter splanchnicus type strain RT (1651/6)."; RL Stand. Genomic Sci. 4:200-209(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002544; ADY31715.1; -; Genomic_DNA. DR RefSeq; YP_004251895.1; NC_015160.1. DR EnsemblBacteria; ADY31715; ADY31715; Odosp_0632. DR GeneID; 10252339; -. DR KEGG; osp:Odosp_0632; -. DR OMA; WINAIRS; -. DR BioCyc; OSPL709991:GI68-636-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 655 AA; 74070 MW; 0ACE6AB39BDD839C CRC64; MKIIVITSPT PVKDEAAICN HLFTHGLKYL HLRKPGASAE VYERFIRQIF PVYRNRIVLH EHYELVKKYR LHGIHLKYPQ ANEYIYYIQQ YAVSISCHRV DEIRQLPFRP AYCFLSPIFD SISKTGYRSR FGQLPDLSDI DCPVIALGGL EPDKTGLCRR AGFEGIAVLG YLWNNPDEAI ERYIRLKTPF VLSIAGFDPS SGAGIGADLK TFEATGSYGL GVCSALTFQN EDTFTGVHWT AWEDIKKQCD LLLQKYNVEF LKIGLIESFE ILDRLLDYLL DQDKRLKIIW DPILKASAGF SFHRYTPEDQ ERLKRILDRV YLITPNTDEL YRLFGEGITP DRLQIVCRDH HLNILWKGGH NAGVDATDVL FQPDRTTNFS VPRSRYTKHG TGCTLSSALL SALAQGDALA TSCNKAQLYV SRFIESNNSL LGYHCIGKYT PDSKPWLGEL SLQYITAPKE GMTLCEQVEA VCQGGMRWIQ LRMKGASLAE MLCEGRKVKE ICRRHRALFI INDRVDVARL LEADGVHLGK EDMDPWEARR ILGPGKIVGA TCNTWDDILL RQKQQVDYIG LGPYAFTTTK EKLSPVLGLE GYRFLLGRMQ ENKISIPVFA IGGITETDIP PLMQTGIQGI ALSGLIKNSP DLKRQTIKIL NLLNS // ID F9ZDK7_9PROT Unreviewed; 210 AA. AC F9ZDK7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NAL212_0554; OS Nitrosomonas sp. AL212. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=153948; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AL212; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Suwa Y., Klotz M.G., Bollmann A., Stein L.Y., Laanbroek H.J., RA Arp D.J., Norton J.M., Woyke T.; RT "Complete sequence of chromosome of Nitrosomonas sp. AL212."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002552; ADZ25498.1; -; Genomic_DNA. DR RefSeq; YP_004293660.1; NC_015222.1. DR ProteinModelPortal; F9ZDK7; -. DR EnsemblBacteria; ADZ25498; ADZ25498; NAL212_0554. DR GeneID; 10297057; -. DR KEGG; nit:NAL212_0554; -. DR KO; K00788; -. DR BioCyc; NSP153948:GHZ8-392-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22690 MW; 29D74A54D7340CE7 CRC64; MRNHKIRGLY AITPDSNNTG ELLDKTQQAL VGGAQYIQYR NKSVDNLLRK KQAGLLLQLC KKHAIPLIIN DDIDLAIEID ADGVHVGRND SSISDARKFL RQDKIVGASC YNNLDLAIEA EKQGADYVAF GSFFPSVTKP QATPVSISLI NQARQILTIP VVGIGGIQLT NAAMVIHNGC DAIAVCSNLF QAGDVRGRAA QYAQLFAGNL // ID F9ZIE8_9PROT Unreviewed; 322 AA. AC F9ZIE8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 22-JAN-2014, entry version 18. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=NAL212_2705; OS Nitrosomonas sp. AL212. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=153948; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AL212; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Suwa Y., Klotz M.G., Bollmann A., Stein L.Y., Laanbroek H.J., RA Arp D.J., Norton J.M., Woyke T.; RT "Complete sequence of chromosome of Nitrosomonas sp. AL212."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002552; ADZ27495.1; -; Genomic_DNA. DR RefSeq; YP_004295657.1; NC_015222.1. DR ProteinModelPortal; F9ZIE8; -. DR EnsemblBacteria; ADZ27495; ADZ27495; NAL212_2705. DR GeneID; 10299245; -. DR KEGG; nit:NAL212_2705; -. DR KO; K03574; -. DR BioCyc; NSP153948:GHZ8-2581-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 322 AA; 35520 MW; 70C953805A01292E CRC64; MSHITLPSPE FIPIVEVVAA IILQPDGRFL LAQRPEGKIY SGYWEFPGGK VEPGESLLHA LERELWEELG IRVHYAQPWI SRIFAYAHAT VRLHFFRVVE WGGKLIPREM QAVSWQMPQE IAVAPILPAN GPILQALLLP PLYAITRASE IGLESALQQI NRALQNGLRL LQIREKQMEK DKLREFAEKV LALARAHQAK VLINSDSKLA RETGADGIHL TSAQLMALSC RPGPEYGLCG ASCHNAEELY AAELLGLDFV VLGPVQSTLS HPGLAPLGWR KFASIIRDYS LPVYALGGLS SEDLIIAQEM GAQGIAMMRG IT // ID F9ZQV1_ACICS Unreviewed; 315 AA. AC F9ZQV1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 16. DE SubName: Full=Mutator mutT protein (7,8-dihydro-8-oxoguanine-triphosphatase) / Thiamin-phosphate pyrophosphorylase-like protein; GN OrderedLocusNames=Atc_2643; OS Acidithiobacillus caldus (strain SM-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=990288; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM-1; RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006; RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B., RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.; RT "Unraveling the Acidithiobacillus caldus complete genome and its RT central metabolisms for carbon assimilation."; RL J. Genet. Genomics 38:243-252(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002573; AEK59290.1; -; Genomic_DNA. DR RefSeq; YP_004749992.1; NC_015850.1. DR ProteinModelPortal; F9ZQV1; -. DR EnsemblBacteria; AEK59290; AEK59290; Atc_2643. DR GeneID; 10990427; -. DR KEGG; acu:Atc_2643; -. DR KO; K03574; -. DR BioCyc; ACAL990288:GJBS-2688-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 33501 MW; 1EA075213DEF9DB0 CRC64; MLLDLRPADK PWPGYWEFPG GKMEAGESPE AALHRELAEE LGITVRAATP WQVREYAYPE RRVRLHLYKV TAWEGRVHGR EGQELRWLSP AAAAALHLLP ANRGILADLS AEALPCPPLF LIADPQRAAA GAFLKILEQS TAAGLRALIL RIKGPLPAGL DAETLADWLA RAKGRGVQVY LNHPDPLPSW PVVGRHFTEA QLADCDASPS SPFGVSCHSA AGLARAEALG ASYALLSPLF PTATHPHTPA LGLARFAELA AAVAVPVIAL GGIDARRIPE ARRAGARGAA VLSEILSASD PHAATQTLIH AWNAA // ID F9ZTV0_ACICS Unreviewed; 219 AA. AC F9ZTV0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Atc_2880; OS Acidithiobacillus caldus (strain SM-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=990288; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM-1; RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006; RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B., RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.; RT "Unraveling the Acidithiobacillus caldus complete genome and its RT central metabolisms for carbon assimilation."; RL J. Genet. Genomics 38:243-252(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002573; AEK59526.1; -; Genomic_DNA. DR RefSeq; YP_004750228.1; NC_015850.1. DR ProteinModelPortal; F9ZTV0; -. DR EnsemblBacteria; AEK59526; AEK59526; Atc_2880. DR GeneID; 10990663; -. DR KEGG; acu:Atc_2880; -. DR KO; K00788; -. DR BioCyc; ACAL990288:GJBS-2931-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22950 MW; D4A6049206BDC078 CRC64; MTTTAIAGVY GITDSTLMPG DALLCKSEAA LRAGLRILQY RDKSDDAARR LREAAALHAL CRDYGALFVV NDDAALAAKI AAPALHVGRE DAPLAELRRH FGGSLCIGVS CYDDLARAER AQAEGADYVA FGAFFPSPSK PDTSRAPLHL LREARRRLQV PVVAIGGIRA DNGADLLAAG ADALAVISAL FGSADVAAAM RRLQALFVLA GGSQTMEES // ID G0A297_METMM Unreviewed; 311 AA. AC G0A297; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 13-NOV-2013, entry version 17. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=Metme_0465; OS Methylomonas methanica (strain MC09). OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomonas. OX NCBI_TaxID=857087; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC09; RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M., RA Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., RA Teshima H., Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., RA Goodwin L., Han C., Hauser L., Land M., Lapidus A., Lucas S., RA Pitluck S., Woyke T., Stein L.Y., Murrell C.; RT "Complete genome sequence of the aerobic marine methanotroph RT Methylomonas methanica MC09."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC09; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.; RT "Complete sequence of Methylomonas methanica MC09."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002738; AEF98909.1; -; Genomic_DNA. DR RefSeq; YP_004511409.1; NC_015572.1. DR ProteinModelPortal; G0A297; -. DR EnsemblBacteria; AEF98909; AEF98909; Metme_0465. DR GeneID; 10670450; -. DR KEGG; mmt:Metme_0465; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; MMET857087:GH4A-473-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 311 AA; 33657 MW; C6B5D2577CA0B854 CRC64; MSGSAAVHVA VGVIRDGNGN ILLTQRAKHT HQGGLWEFPG GKLEAHETVT QALRRELQEE VGITVQTAKP LIKINHCYPD LRVLLDVWQV TDFSGVAEAC EGQAMQWVEP RQLSDYAFPV ANVPIITASR LPDRYAILEG SSAKQVLANL ERIINKRITM LQLRIKSLPA AETAAVCHAV LANCRQHGIQ VLLNSDLLLT GLPADGLHLS SRALLACQTK PSPYRWVAAS CHNLQELRHA ENIGADFAVL APILPTATHP DAQPLGWETM AKLIDQVNLP VFALGGLELD DMDRVLHAGA QGIAGISAFL S // ID G0A7C9_METMM Unreviewed; 205 AA. AC G0A7C9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Metme_2195; OS Methylomonas methanica (strain MC09). OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomonas. OX NCBI_TaxID=857087; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC09; RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M., RA Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., RA Teshima H., Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., RA Goodwin L., Han C., Hauser L., Land M., Lapidus A., Lucas S., RA Pitluck S., Woyke T., Stein L.Y., Murrell C.; RT "Complete genome sequence of the aerobic marine methanotroph RT Methylomonas methanica MC09."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC09; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.; RT "Complete sequence of Methylomonas methanica MC09."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002738; AEG00599.1; -; Genomic_DNA. DR RefSeq; YP_004513098.1; NC_015572.1. DR EnsemblBacteria; AEG00599; AEG00599; Metme_2195. DR GeneID; 10672195; -. DR KEGG; mmt:Metme_2195; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; MMET857087:GH4A-2218-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21759 MW; 285A0DC2D21F4687 CRC64; MKFPRRGLYA ITQPEHKTLE QILNEVEAAL KGGAVVIQYR DKQPLDAEGL ARQLLTLCHA YQVPLLINDS VELAVKVGAD GVHLGRDDGD IANARSRLGE NAIIGISCYN DVQKARIAAE HGADYVAFGR FFPSGSKPLA ASADLTTLTQ AKQLLNLPIV AIGGILPENG GQLIAAGADL LAVIGGIFDH EPQAAAQAYQ ALFHS // ID G0AF25_COLFT Unreviewed; 204 AA. AC G0AF25; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CFU_0718; OS Collimonas fungivorans (strain Ter331). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Collimonas. OX NCBI_TaxID=1005048; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ter331; RA Leveau J.H.; RT "Complete sequence of Collimonas fungivorans Ter331."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002745; AEK60552.1; -; Genomic_DNA. DR RefSeq; YP_004751375.1; NC_015856.1. DR EnsemblBacteria; AEK60552; AEK60552; CFU_0718. DR GeneID; 10991435; -. DR KEGG; cfu:CFU_0718; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; CFUN1005048:GJNH-724-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21882 MW; B7E3015D8BB5F291 CRC64; MKGLYIVTPD WDDTDKLLQV TEQALQGGAA LLQYRHKTAD AVQRRQQAEA LLKLCRRYQR PFIVNDYVEL CMELGADGIH VGGTDASVAE VRAMVGADKI VGASCYGDLE LAHAAYRDGA SYVAFGGFYP SRVKKYPVTT PPDIVTRAKA QIAAPNVVIG GMTQENAAPL IAAGADMVAA ISSVYLADDP AAAARSFVTL FENR // ID G0AYR9_9GAMM Unreviewed; 646 AA. AC G0AYR9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN ORFNames=Sbal175_2086; OS Shewanella baltica BA175. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=693974; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BA175; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Pagani I., Konstantinidis K., Deng J., RA Brettar I., Hofle M., Tiedje J., Auchtung J., Woyke T.; RT "Complete sequence of chromosome of Shewanella baltica BA175."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BA175; RX PubMed=22328742; DOI=10.1128/JB.06468-11; RA Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M., RA Tiedje J.M., Konstantinidis K.T.; RT "Genome Sequencing of Five Shewanella baltica Strains Recovered from RT the Oxic-Anoxic Interface of the Baltic Sea."; RL J. Bacteriol. 194:1236-1236(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002767; AEG11350.1; -; Genomic_DNA. DR RefSeq; YP_006020656.1; NC_017571.1. DR ProteinModelPortal; G0AYR9; -. DR EnsemblBacteria; AEG11350; AEG11350; Sbal175_2086. DR GeneID; 12616573; -. DR KEGG; sbb:Sbal175_2086; -. DR KO; K14153; -. DR BioCyc; SBAL693974:GLK2-2172-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 646 AA; 68280 MW; 69576481957ED8AE CRC64; MLGIHGDNVP MNTERPAFVW TIAGSDSGGG AGIQADLATI QDLGCHGCSV VTTVTAQSSV AVTLVEPVSA AMLMAQLTTL LSDLPPKAIK IGLLADQTQV ALLADWIASF KINYPSVPVI VDPVMVASCG DALAVDNCQD IKSAAKSALD FKPFKGLIEL ITPNVLELGR LTHSDVSTKA QFAAAALALS QSLDCSVLAK GGDVSFGCTD ILDDTHAKTH DNTHAQTHDN TYAETQANAY KSNGWDLELA EDYLVCRQVR ASSKLHQNGR FWLASQRVNT HHNHGSGCTL SSAIAAVLAQ GFVLQDAVVV AKAYVSQGLS AAIGLGQGPG PLARTGWPND VSHYAKIRLC CDNGINQHLD VGNDLVATVL SATDQATAQV RIASTPPQNI LSHCFKVLDA DLGVYPVVSD LTMLESLLAA GVKTVQLRIK TDISELTTTT APAEFDLGKS ALGRCESGEP ELIGSELEAQ IQTAIALGKH FNAQLFINDH WQLAIKYHAF GVHLGQEDLA VTDLAAIQAA GLALGISSHS YFELLLAHQY SPSYIALGHI FPTTTKQMPS APQGLAKLKH YVALLQGHYP LVAIGGIDLT NLAKVKATGV GNIAVVRAIT KAKEPLAAFA ELSQAWEQCS LSEELAVKHE LVAKHE // ID G0B1U1_SERSA Unreviewed; 212 AA. AC G0B1U1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SerAS9_0245; OS Serratia plymuthica (strain AS9). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=768492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Lu M., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Neupane S., Alstrom S., RA Finlay R., Hogberg N., Woyke T.; RT "Complete sequence of Serratia sp. AS9."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AS9; RX PubMed=22675598; DOI=10.4056/sigs.2595762; RA Neupane S., Hogberg N., Alstrom S., Lucas S., Han J., Lapidus A., RA Cheng J.F., Bruce D., Goodwin L., Pitluck S., Peters L., RA Ovchinnikova G., Lu M., Han C., Detter J.C., Tapia R., Fiebig A., RA Land M., Hauser L., Kyrpides N.C., Ivanova N., Pagani I., Klenk H.P., RA Woyke T., Finlay R.D.; RT "Complete genome sequence of the rapeseed plant-growth promoting RT Serratia plymuthica strain AS9."; RL Stand. Genomic Sci. 6:54-62(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002773; AEF43407.1; -; Genomic_DNA. DR RefSeq; YP_004503668.1; NC_015567.1. DR EnsemblBacteria; AEF43407; AEF43407; SerAS9_0245. DR GeneID; 10619321; -. DR KEGG; srr:SerAS9_0245; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; SPLY768492:GLK1-259-MONOMER; -. DR BioCyc; SSP768492:GH0N-259-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22936 MW; 8EF9BE796998D51D CRC64; MNDIITPFPA TPHRLGLYPV VDSVEWIARL LEAGVTTIQL RIKDLPDEQV EDDIAAAIAL GKQYHARLFI NDYWQLAIKH GAYGVHLGQE DLDTTDLAAI HRAGLRLGVS THDDAELARA IAVKPSYIAL GHIFPTQTKE MPSAPQGLAE LKRHVAELDD YPTVAIGGIG IDRVAAVLDC GVGSVAVVSA ITKAPDWRVA TVQLLQLIEG KE // ID G0BIN7_9ENTR Unreviewed; 212 AA. AC G0BIN7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SerAS12_0245; OS Serratia sp. AS12. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=768490; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AS12; RX PubMed=22768360; DOI=10.4056/sigs.2705996; RA Neupane S., Finlay R.D., Alstrom S., Goodwin L., Kyrpides N.C., RA Lucas S., Lapidus A., Bruce D., Pitluck S., Peters L., RA Ovchinnikova G., Chertkov O., Han J., Han C., Tapia R., Detter J.C., RA Land M., Hauser L., Cheng J.F., Ivanova N., Pagani I., Klenk H.P., RA Woyke T., Hogberg N.; RT "Complete genome sequence of Serratia plymuthica strain AS12."; RL Stand. Genomic Sci. 6:165-173(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002774; AEF48359.1; -; Genomic_DNA. DR RefSeq; YP_004498716.1; NC_015566.1. DR EnsemblBacteria; AEF48359; AEF48359; SerAS12_0245. DR GeneID; 10624444; -. DR KEGG; srs:SerAS12_0245; -. DR KO; K00788; -. DR BioCyc; SSP768490:GH4I-259-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22936 MW; 8EF9BE796998D51D CRC64; MNDIITPFPA TPHRLGLYPV VDSVEWIARL LEAGVTTIQL RIKDLPDEQV EDDIAAAIAL GKQYHARLFI NDYWQLAIKH GAYGVHLGQE DLDTTDLAAI HRAGLRLGVS THDDAELARA IAVKPSYIAL GHIFPTQTKE MPSAPQGLAE LKRHVAELDD YPTVAIGGIG IDRVAAVLDC GVGSVAVVSA ITKAPDWRVA TVQLLQLIEG KE // ID G0BYD0_9ENTR Unreviewed; 212 AA. AC G0BYD0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SerAS13_0244; OS Serratia sp. AS13. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=768493; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AS13; RX PubMed=23450001; DOI=10.4056/sigs.2966299; RA Neupane S., Finlay R.D., Kyrpides N.C., Goodwin L., Alstrom S., RA Lucas S., Land M., Han J., Lapidus A., Cheng J.F., Bruce D., RA Pitluck S., Peters L., Ovchinnikova G., Held B., Han C., Detter J.C., RA Tapia R., Hauser L., Ivanova N., Pagani I., Woyke T., Klenk H.P., RA Hogberg N.; RT "Complete genome sequence of the plant-associated Serratia plymuthica RT strain AS13."; RL Stand. Genomic Sci. 7:22-30(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002775; AEG26067.1; -; Genomic_DNA. DR RefSeq; YP_006023131.1; NC_017573.1. DR EnsemblBacteria; AEG26067; AEG26067; SerAS13_0244. DR GeneID; 12619171; -. DR KEGG; sra:SerAS13_0244; -. DR KO; K00788; -. DR BioCyc; SSP768493:GLK0-259-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22936 MW; 8EF9BE796998D51D CRC64; MNDIITPFPA TPHRLGLYPV VDSVEWIARL LEAGVTTIQL RIKDLPDEQV EDDIAAAIAL GKQYHARLFI NDYWQLAIKH GAYGVHLGQE DLDTTDLAAI HRAGLRLGVS THDDAELARA IAVKPSYIAL GHIFPTQTKE MPSAPQGLAE LKRHVAELDD YPTVAIGGIG IDRVAAVLDC GVGSVAVVSA ITKAPDWRVA TVQLLQLIEG KE // ID G0CDC0_XANCA Unreviewed; 315 AA. AC G0CDC0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 22-JAN-2014, entry version 17. DE SubName: Full=Dgtp-pyrophosphohydrolase; GN ORFNames=XCR_0906; OS Xanthomonas campestris pv. raphani 756C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=990315; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=756C; RX PubMed=21784931; DOI=10.1128/JB.05262-11; RA Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., RA Patil P.B., Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., RA Aparna G., Rajaram M., Delcher A.L., Phillippy A.M., Puiu D., RA Schatz M.C., Shumway M., Sommer D.D., Trapnell C., Benahmed F., RA Dimitrov G., Madupu R., Radune D., Sullivan S., Jha G., Ishihara H., RA Lee S.W., Pandey A., Sharma V., Sriariyanun M., Szurek B., RA Vera-Cruz C.M., Dorman K.S., Ronald P.C., Verdier V., Dow J.M., RA Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D., Leach J.E., RA White F.F., Salzberg S.L.; RT "Two New Complete Genome Sequences Offer Insight into Host and Tissue RT Specificity of Plant Pathogenic Xanthomonas spp."; RL J. Bacteriol. 193:5450-5464(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002789; AEL05823.1; -; Genomic_DNA. DR RefSeq; YP_005635941.1; NC_017271.1. DR ProteinModelPortal; G0CDC0; -. DR EnsemblBacteria; AEL05823; AEL05823; XCR_0906. DR GeneID; 12262965; -. DR KEGG; xcp:XCR_0906; -. DR KO; K03574; -. DR BioCyc; XCAM990315:GLMR-905-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34430 MW; 63764B908851E660 CRC64; MPDSLRSIHV VAGVITDARG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIDAHVGA WVMDVPQLYP DKRLRLEVRE ITGWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGVL RQPDRYLITP EPQDDAAWLD GVEQALQQGI ARIQLRAPAV DPARWHALVH QVMGLRGRQR AQWLLNRDIG LASELGIGVH LGSEQLATLT ERPLPADQPV AASCHGLEDL RHAQRLGCDF AVLGPVQATA SHPGATPLGW EGFEALREQV SLPIYALGGM QPGDVREARA HGAQGIAAIR GLWPA // ID G0CEK0_XANCA Unreviewed; 207 AA. AC G0CEK0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=XCR_3610; OS Xanthomonas campestris pv. raphani 756C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=990315; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=756C; RX PubMed=21784931; DOI=10.1128/JB.05262-11; RA Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., RA Patil P.B., Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., RA Aparna G., Rajaram M., Delcher A.L., Phillippy A.M., Puiu D., RA Schatz M.C., Shumway M., Sommer D.D., Trapnell C., Benahmed F., RA Dimitrov G., Madupu R., Radune D., Sullivan S., Jha G., Ishihara H., RA Lee S.W., Pandey A., Sharma V., Sriariyanun M., Szurek B., RA Vera-Cruz C.M., Dorman K.S., Ronald P.C., Verdier V., Dow J.M., RA Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D., Leach J.E., RA White F.F., Salzberg S.L.; RT "Two New Complete Genome Sequences Offer Insight into Host and Tissue RT Specificity of Plant Pathogenic Xanthomonas spp."; RL J. Bacteriol. 193:5450-5464(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002789; AEL08471.1; -; Genomic_DNA. DR RefSeq; YP_005638589.1; NC_017271.1. DR EnsemblBacteria; AEL08471; AEL08471; XCR_3610. DR GeneID; 12262387; -. DR KEGG; xcp:XCR_3610; -. DR KO; K00788; -. DR BioCyc; XCAM990315:GLMR-3605-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21297 MW; 1AA951EA449841E6 CRC64; MPTLQNARGV YLITPDTRDT AQLLACTLPL LPHITWLQYR NKQADAALRL AQATALRAAC TAQGVPLIIN DDAALAQQVG ADGVHLGEDD GEVAAARALL GASAIIGVSC YDEIERARAA AAAGANYVAF GAFFPTTTKV TTRRATPALL HETAALGLPR VAIGGITPPQ VPELVTAGAD LIAVVSGVYA AADPVAAVQA YRAGFTQ // ID G0CSL1_CORUL Unreviewed; 232 AA. AC G0CSL1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CULC809_01414; OS Corynebacterium ulcerans 809. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=945711; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=809; RX PubMed=21801446; DOI=10.1186/1471-2164-12-383; RA Trost E., Al-Dilaimi A., Papavasiliou P., Schneider J., Viehoever P., RA Burkovski A., Soares S.C., Almeida S.S., Dorella F.A., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Santos C.S., Santos L.S., RA Sabbadini P., Dias A.A., Hirata R.Jr., Mattos-Guaraldi A.L., Tauch A.; RT "Comparative analysis of two complete Corynebacterium ulcerans genomes RT and detection of candidate virulence factors."; RL BMC Genomics 12:383-383(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002790; AEG81946.1; -; Genomic_DNA. DR RefSeq; YP_005711040.1; NC_017317.1. DR EnsemblBacteria; AEG81946; AEG81946; CULC809_01414. DR GeneID; 12285991; -. DR KEGG; cuc:CULC809_01414; -. DR KO; K00788; -. DR BioCyc; CULC945711:GLC2-1446-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 232 AA; 24451 MW; 2BD4D22ED369296D CRC64; MRKTTPPVDL RCYFVTGYSP DPRHIVHIAV AAAAGGAGII QIRSKPISAR DLYKLSSEVA CAVATINPFT RVLIDDRLDV AIALRSQNIP IAGVHVGQDD LSPHICRKLL GPEAIIGLTT GSLELVEKAN TQAEHIDYIG CGPFHETPTK DSGRAPLGLD SYAELVARSA VPLVAIGGIT LNDAAPLAAQ GVSGLAVVRG FMEAADPTDF ASKVLREFDR GASQWAKDSS CA // ID G0CV03_CORUB Unreviewed; 232 AA. AC G0CV03; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CULC22_01428; OS Corynebacterium ulcerans (strain BR-AD22). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=945712; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BR-AD22; RX PubMed=21801446; DOI=10.1186/1471-2164-12-383; RA Trost E., Al-Dilaimi A., Papavasiliou P., Schneider J., Viehoever P., RA Burkovski A., Soares S.C., Almeida S.S., Dorella F.A., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Santos C.S., Santos L.S., RA Sabbadini P., Dias A.A., Hirata R.Jr., Mattos-Guaraldi A.L., Tauch A.; RT "Comparative analysis of two complete Corynebacterium ulcerans genomes RT and detection of candidate virulence factors."; RL BMC Genomics 12:383-383(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002791; AEG84138.1; -; Genomic_DNA. DR RefSeq; YP_004630057.1; NC_015683.1. DR EnsemblBacteria; AEG84138; AEG84138; CULC22_01428. DR GeneID; 10844006; -. DR KEGG; cul:CULC22_01428; -. DR KO; K00788; -. DR BioCyc; CULC945712:GHG6-1461-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 232 AA; 24541 MW; A0B88DD4717C5F9A CRC64; MRKTTPPVDL RCYFVTGHSP DPRHIVHIAV AAVAGGAGII QIRSKPISAR DLYKLSSEVA CAVATINPFT RVLIDDRLDV AIALRSQNIP IAGVHVGQDD LSPHICRKLL GPEAIIGLTT GSLELVEKAN TQAEYIDYIG CGPFRETPTK DSGRAPLGLD SYAELVTRSA VPLVAIGGIT LNDAAPLAAQ GVSGLAVVRG FMEAADPTDF ASKILREFNR GASQWAKDSS CA // ID G0D3D3_ECOLX Unreviewed; 211 AA. AC G0D3D3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECNA114_3430; OS Escherichia coli NA114. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1033813; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NA114; RX PubMed=21685291; DOI=10.1128/JB.05413-11; RA Avasthi T.S., Kumar N., Baddam R., Hussain A., Nandanwar N., RA Jadhav S., Ahmed N.; RT "Genome of multidrug-resistant uropathogenic Escherichia coli strain RT NA114 from India."; RL J. Bacteriol. 193:4272-4273(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002797; AEG38269.1; -; Genomic_DNA. DR RefSeq; YP_006140543.1; NC_017644.1. DR ProteinModelPortal; G0D3D3; -. DR EnsemblBacteria; AEG38269; AEG38269; ECNA114_3430. DR GeneID; 12681683; -. DR KEGG; ena:ECNA114_3430; -. DR KO; K00788; -. DR BioCyc; ECOL1033813:GI9U-3506-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23027 MW; 9C5E679AD0EA42DC CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G0DIE9_9GAMM Unreviewed; 650 AA. AC G0DIE9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 21. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN ORFNames=Sbal117_2231; OS Shewanella baltica OS117. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=693970; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OS117; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Lu M., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Hofle M., Brettar I., RA Konstantinidis K., Deng J., Tiedje J., Auchtung J., Woyke T.; RT "Complete sequence of chromosome of Shewanella baltica OS117."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OS117; RX PubMed=22328742; DOI=10.1128/JB.06468-11; RA Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M., RA Tiedje J.M., Konstantinidis K.T.; RT "Genome Sequencing of Five Shewanella baltica Strains Recovered from RT the Oxic-Anoxic Interface of the Baltic Sea."; RL J. Bacteriol. 194:1236-1236(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002811; AEH13956.1; -; Genomic_DNA. DR RefSeq; YP_006037450.1; NC_017579.1. DR ProteinModelPortal; G0DIE9; -. DR EnsemblBacteria; AEH13956; AEH13956; Sbal117_2231. DR GeneID; 12633988; -. DR KEGG; sbs:Sbal117_2231; -. DR KO; K14153; -. DR BioCyc; SBAL693970:GLK3-2270-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 650 AA; 68610 MW; 1F1747E4725471E7 CRC64; MLGIHGDNAP MNTEHPAFVW TIAGSDSGGG AGIQADLATI QDLGCHGCSV VTTVTAQSSV AVTLVEPVSA AMLMAQLTTL LSDLPPKAIK IGLLADQTQV ALLADWIASF KIHYPSVPVI VDPVMVASCG DALAVDNCQD IKSAAKSALD FKPFKGLIEL ITPNVLELGR LTHSDVSTKA QFAAAALALS QSLDCSVLAK GGDVSFGSTD ILDDTHAQTH DNTYAQTQAN VHVIALDSNG WDLELAEDYL VCRQVRASSK LHQNGRFWLA SQRVNTPHNH GSGCTLSSAI AAVLAQGFVL QDAVVVAKAY VSQGLSAAIG LGQGPGPLAR TGWPNDVSRY AKINLCDSNF ISHQLNQHLD VGNDLVATVL SATDQATAQV RIASTQPQNI LSHGFKVLDA DLGVYPVVND LTMLESLLAA GVKTLQLRIK TDISELTTAG LAESDLGKSA LSRCESGKSK SGEPELIGSE LEAQIQTAIA LGKHFNAQLF INDHWQLAIK YHAFGVHLGQ EDLAVTDLAA IQAAGLALGI SSHSYFELLL AHQYSPSYIA LGHIFPTTTK QMPSAPQGLA KLKHYVALLQ DHYPLVAIGG IDLTNLAKVK ATGVGNIAVV RAITKAKDPL AAFAELSQAW EQCSLSEELA VKHELDAKHE // ID G0DS64_PROAA Unreviewed; 217 AA. AC G0DS64; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TIB1ST10_00575; OS Propionibacterium acnes 6609. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1031709; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6609; RX PubMed=21705602; DOI=10.1128/JB.05372-11; RA Hunyadkurti J., Feltoti Z., Horvath B., Nagymihaly M., Voros A., RA McDowell A., Patrick S., Urban E., Nagy I.; RT "Complete genome sequence of Propionibacterium acnes type IB strain RT 6609."; RL J. Bacteriol. 193:4561-4562(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002815; AEH28429.1; -; Genomic_DNA. DR RefSeq; YP_005943708.1; NC_017535.1. DR ProteinModelPortal; G0DS64; -. DR EnsemblBacteria; AEH28429; AEH28429; TIB1ST10_00575. DR GeneID; 12534353; -. DR KEGG; pcn:TIB1ST10_00575; -. DR KO; K00788; -. DR BioCyc; PACN1031709:GLIK-116-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID G0DWS1_PROAA Unreviewed; 216 AA. AC G0DWS1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TIB1ST10_04580; OS Propionibacterium acnes 6609. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1031709; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6609; RX PubMed=21705602; DOI=10.1128/JB.05372-11; RA Hunyadkurti J., Feltoti Z., Horvath B., Nagymihaly M., Voros A., RA McDowell A., Patrick S., Urban E., Nagy I.; RT "Complete genome sequence of Propionibacterium acnes type IB strain RT 6609."; RL J. Bacteriol. 193:4561-4562(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002815; AEH29213.1; -; Genomic_DNA. DR RefSeq; YP_005944492.1; NC_017535.1. DR EnsemblBacteria; AEH29213; AEH29213; TIB1ST10_04580. DR GeneID; 12535150; -. DR KEGG; pcn:TIB1ST10_04580; -. DR KO; K00788; -. DR BioCyc; PACN1031709:GLIK-913-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22504 MW; D68C19AB366F1623 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAGMRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTAP KSSARELAEA WRTAKE // ID G0DYD6_ENTAK Unreviewed; 211 AA. AC G0DYD6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=EAE_08175; OS Enterobacter aerogenes (strain ATCC 13048 / DSM 30053 / JCM 1235 / OS KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006) (Aerobacter OS aerogenes). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=1028307; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / RC NCIMB 10102 / NCTC 10006; RA Shin S.H., Kim S., Kim J.Y., Yang K.-S., Seo J.-S.; RT "Complete sequence of Enterobacter aerogenes KCTC 2190."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002824; AEG96559.1; -; Genomic_DNA. DR RefSeq; YP_004591838.1; NC_015663.1. DR EnsemblBacteria; AEG96559; AEG96559; EAE_08175. DR GeneID; 10791831; -. DR KEGG; eae:EAE_08175; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; EAER1028307:GHNA-1673-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22921 MW; B071D7CB4AD23689 CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDQRDSEVED DVIAAIALGR RYRARLFIND YWQLAIKHRA YGVHLGQEDL ETTDLSAIRK AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA GHIQRLADYP TVAIGGISLE KAPGVLATGV GSIAVVSAIT QAADWRAATA QLLTLAGAGD E // ID G0EIF1_BRAIP Unreviewed; 233 AA. AC G0EIF1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Bint_0325; OS Brachyspira intermedia (strain ATCC 51140 / PWS/A) (Serpulina OS intermedia). OC Bacteria; Spirochaetes; Spirochaetales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=1045858; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51140 / PWS/A; RX PubMed=21816042; DOI=10.1186/1471-2164-12-395; RA Hafstrom T., Jansson D.S., Segerman B.; RT "Complete genome sequence of Brachyspira intermedia reveals unique RT genomic features in Brachyspira species and phage-mediated horizontal RT gene transfer."; RL BMC Genomics 12:395-395(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002874; AEM20959.1; -; Genomic_DNA. DR RefSeq; YP_005593539.1; NC_017243.1. DR EnsemblBacteria; AEM20959; AEM20959; Bint_0325. DR GeneID; 12157742; -. DR KEGG; bip:Bint_0325; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR BioCyc; BINT1045858:GL9O-325-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 59 63 HMP-PP binding (By similarity). FT REGION 159 161 THZ-P binding (By similarity). FT REGION 210 211 THZ-P binding (By similarity). FT METAL 95 95 Magnesium (By similarity). FT METAL 114 114 Magnesium (By similarity). FT BINDING 94 94 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 162 162 HMP-PP (By similarity). FT BINDING 190 190 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 26532 MW; 34C500B33DEBCB34 CRC64; MKGIQDIINT KYINKRREIL KEKYFKDSIY CVTAEDFSNG RNNIEVVKSM LEAGIKIIQY REKDNPNKYM REKYEECLKI RELTKEHDAL FIIDDYADLA IAVEADGVHI GQKDMPIEVV RKIVGFDKIV GLSTTNEKQA EEAIHTSADY IGIGPIFSTN TKPDANEATG IDYLDYVVKN LDVPFVCIGG IKLSNIDLLI EHKAMSLCML TEIVSSEDIK SKCELLIKKM KRL // ID G0ETC4_CUPNN Unreviewed; 378 AA. AC G0ETC4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 18. DE SubName: Full=Thiamine-phosphate pyrophosphorylase ThiE; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=CNE_1c02260; OS Cupriavidus necator (strain ATCC 43291 / DSM 13513 / N-1) (Ralstonia OS eutropha). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=1042878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43291 / DSM 13513 / N-1; RX PubMed=21742890; DOI=10.1128/JB.05660-11; RA Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.; RT "Complete Genome Sequence of the Type Strain Cupriavidus necator N- RT 1."; RL J. Bacteriol. 193:5017-5017(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002877; AEI75595.1; -; Genomic_DNA. DR RefSeq; YP_004684076.1; NC_015726.1. DR EnsemblBacteria; AEI75595; AEI75595; CNE_1c02260. DR GeneID; 10916617; -. DR KEGG; cnc:CNE_1c02260; -. DR KO; K00788; -. DR BioCyc; CNEC1042878:GH0Z-226-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 378 AA; 40131 MW; A10D73C152484E92 CRC64; MTRRAVHAAS DGPLRQAVLE HYGETFGVDD KPWQAWRLAD APAQPGAHDV LLFDGEADAG TIARLAAAGA TLIETDREGG QWIDTVRSPM GTWVFSVAAD TDQPHSPAFV AVLLASLSLH FPAHDALCLS RAWEPGSADW PSDFARFPHV RHAALAAPEQ AAAPFAPCPA LGLYVVVPSA EWIERLAPLN VPTVQLRFKS DDPAEVRAEI ARAAKAMQGS SSRLFVNDHW QAAIDYRAAN GGEHSGIYGI HLGQEDLDDA DLDAIRASGL RLGVSTHGYA EMLRVAAIRP SYLALGAIFP TTTKVMPTQP QGMGRFRAYV KLMQPVIPSL VGIGGVNVAN MREVLAVGVG SAAVVRAVTE ADDVPAAVAH LVSLFPAA // ID G0F9V0_ECOLX Unreviewed; 211 AA. AC G0F9V0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=UMNF18_4940; OS Escherichia coli UMNF18. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1050617; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UMNF18; RX PubMed=22081385; DOI=10.1128/JB.06225-11; RA Shepard S.M., Danzeisen J.L., Isaacson R.E., Seemann T., Achtman M., RA Johnson T.J.; RT "Genome Sequences and Phylogenetic Analysis of K88- and F18-Positive RT Porcine Enterotoxigenic Escherichia coli."; RL J. Bacteriol. 194:395-405(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTD01000001; AEJ59387.1; -; Genomic_DNA. DR ProteinModelPortal; G0F9V0; -. DR SMR; G0F9V0; 20-202. DR EnsemblBacteria; AEJ59387; AEJ59387; UMNF18_4940. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G0G4B4_AMYMS Unreviewed; 219 AA. AC G0G4B4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AMES_8448, RAM_44035; OS Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Amycolatopsis. OX NCBI_TaxID=713604; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S699; RX PubMed=21914879; DOI=10.1128/JB.05819-11; RA Verma M., Kaur J., Kumar M., Kumari K., Saxena A., Anand S., Nigam A., RA Ravi V., Raghuvanshi S., Khurana P., Tyagi A.K., Khurana J.P., Lal R.; RT "Whole genome sequence of the rifamycin B-producing strain RT Amycolatopsis mediterranei S699."; RL J. Bacteriol. 193:5562-5563(2011). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S699; RX PubMed=23012281; DOI=10.1128/JB.01295-12; RA Tang B., Zhao W., Zheng H., Zhuo Y., Zhang L., Zhao G.P.; RT "Complete genome sequence of Amycolatopsis mediterranei S699 based on RT de novo assembly via a combinatorial sequencing strategy."; RL J. Bacteriol. 194:5699-5700(2012). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S699; RA Biao T.; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002896; AEK47274.1; -; Genomic_DNA. DR EMBL; CP003729; AFO81980.1; -; Genomic_DNA. DR RefSeq; YP_005536731.1; NC_017186.1. DR RefSeq; YP_006554925.1; NC_018266.1. DR EnsemblBacteria; AEK47274; AEK47274; RAM_44035. DR EnsemblBacteria; AFO81980; AFO81980; AMES_8448. DR GeneID; 12125510; -. DR GeneID; 13409272; -. DR KEGG; amm:AMES_8448; -. DR KEGG; amn:RAM_44035; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22846 MW; 82C1A8E84F9D5BC3 CRC64; MPALSGDKIR ARLDSARLYL CTDARTNRGD LAAFADAALA GGVDIVQLRD KTGALEAAGE IAALEVLAEA CARHGALLSV NDRADVALAV GADVLHLGQD DIPVPLARRI LGDEVVIGRS THSLDQALAA AAEPGVDYFC TGPCWPTPTK PGRPAPGLDL VRATAAWTPD RPWFAIGGID GPRLPEVLDA GASRIVVVRA ITEAEDPEAA ARELRARLP // ID G0GC55_SPITZ Unreviewed; 383 AA. AC G0GC55; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Spith_0132; OS Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta. OX NCBI_TaxID=869211; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700085 / DSM 6578 / Z-1203; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L., RA Kyrpides N., Mavromatis K., Ivanova N., Mikailova N., Pagani I., RA Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Merkhoffer B., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Spirochaeta thermophila DSM 6578."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002903; AEJ60419.1; -; Genomic_DNA. DR RefSeq; YP_006044136.1; NC_017583.1. DR EnsemblBacteria; AEJ60419; AEJ60419; Spith_0132. DR GeneID; 12638856; -. DR KEGG; stq:Spith_0132; -. DR KO; K00788; -. DR BioCyc; STHE869211:GLKE-132-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 383 AA; 42826 MW; A576A6E83F6F7EFA CRC64; MRGLYRMLDA NWNRAAEGLR VLEDVARFVW NDGPLAERLK GMRHRVRGVL REREGLMAGA RDVEGDVGKG MGVRGDGREG LEGLVRGNCA RVEEALRSME EALRSMGLER KAGVCEEVRY GVYEVEGRLA GWLRRVRVAR AFDGGVYAIT AEEYSRGRGN LRVMREALEG GARIVQYREK EKSYRAMYEE ARAIRELCRE YGALFVVNDH VELALMVEAD GVHVGQDDWP VEEVRRVVGP GMVVGLSTHG PAQAQEAVER GVVDYIGVGP VFPTSTKKDV CAPVGLEYVA YASREVRIPW VAIGGIKEHN LDAVCELGAR CVAMVTEIVG AEDVRGKVRR VRERVEGWRE RGPEPRWVKE WEAVLARQEA PTDQTRPTGE EEP // ID G0GSW5_KLEPN Unreviewed; 211 AA. AC G0GSW5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=KPN2242_24825; OS Klebsiella pneumoniae KCTC 2242. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=1049565; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KCTC 2242; RX PubMed=22535926; DOI=10.1128/JB.00027-12; RA Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J., RA Yang K.S.; RT "Complete Genome Sequence of the 2,3-Butanediol-Producing Klebsiella RT pneumoniae Strain KCTC 2242."; RL J. Bacteriol. 194:2736-2737(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002910; AEK00837.1; -; Genomic_DNA. DR RefSeq; YP_005957401.1; NC_017540.1. DR ProteinModelPortal; G0GSW5; -. DR EnsemblBacteria; AEK00837; AEK00837; KPN2242_24825. DR GeneID; 12548372; -. DR KEGG; kpo:KPN2242_24825; -. DR KO; K00788; -. DR BioCyc; KPNE1049565:GLF0-5018-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 21B54D01518D3CB0 CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIERLLE AGVRTLQLRI KDRRDSEVED DVIAAIALGR RYHARLFIND YWQLAIKHQA YGVHLGQEDL ETTDLSAIRQ AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIQRLADYP TVAIGGISLE KAPGVLATGV GSIAVVSAIT QAADWRAATD QLLALAGAGD E // ID G0H115_METMI Unreviewed; 207 AA. AC G0H115; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GYY_06545; OS Methanococcus maripaludis X1. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=1053692; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X1; RX PubMed=21914896; DOI=10.1128/JB.05835-11; RA Wang X., Greenfield P., Li D., Hendry P., Volk H., Sutherland T.D.; RT "Complete Genome Sequence of a Nonculturable Methanococcus maripaludis RT Strain Extracted in a Metagenomic Survey of Petroleum Reservoir RT Fluids."; RL J. Bacteriol. 193:5595-5595(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002913; AEK20172.1; -; Genomic_DNA. DR RefSeq; YP_004742915.1; NC_015847.1. DR GeneID; 10982720; -. DR KEGG; mmd:GYY_06545; -. DR KO; K00788; -. DR OMA; GLGPICH; -. DR BioCyc; MMAR1053692:GH1C-1305-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22354 MW; 756E072B0140BA48 CRC64; MKFKDKLKFY VITDSNYSDE AISVEEALKG GATSIQLRMK SSSTRKMIEV GNKLRKLTSE YDALFFVNDR LDVAQAVNAD GIHVGIDDMP VSKIKEIAPN LIIGASAYHL DEMKTAESEG ADYLGVGAVY STNTKLDARD LGINGLKDIS KISKLPIVAI GGINHSNVEN VLKCGVSGVA VVSAIVGAEN ILKSAENMNE LIKKYIK // ID G0H6R4_BIFAN Unreviewed; 564 AA. AC G0H6R4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE SubName: Full=Hydroxymethylpyrimidine kinase; DE EC=2.7.1.49; DE EC=2.7.4.7; GN ORFNames=BALAC2494_01478; OS Bifidobacterium animalis subsp. lactis CNCM I-2494. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=1042403; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNCM I-2494; RX PubMed=21914878; DOI=10.1128/JB.05716-11; RA Chervaux C., Grimaldi C., Bolotin A., Quinquis B., Legrain-Raspaud S., RA van Hylckama Vlieg J.E., Denariaz G., Smokvina T.; RT "Genome Sequence of the Probiotic Strain Bifidobacterium animalis RT subsp. lactis CNCM I-2494."; RL J. Bacteriol. 193:5560-5561(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNCM I-2494; RA McNulty N.P.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002915; AEK30702.1; -; Genomic_DNA. DR RefSeq; YP_005578421.1; NC_017215.1. DR ProteinModelPortal; G0H6R4; -. DR EnsemblBacteria; AEK30702; AEK30702; BALAC2494_01478. DR GeneID; 12175523; -. DR KEGG; bnm:BALAC2494_01478; -. DR KO; K14153; -. DR BioCyc; BANI1042403:GL94-1305-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 564 AA; 59777 MW; C0D07895B7146A86 CRC64; MGRDRSKPRS STLCGTLRRR KSPPHRSIWP RICHGTACRH TTNESGDTMN SFPYPSMRDR FDLRFYFVVG PDDCGNRPIL DVVAKALDGG ASFIQLRAKT QDVAEIVSLA NDIAEEIAGH HVEHSVAFVV DDRVDAALEA RAKGIKVDGV HIGQDDLDPV VARKLLGPDA IIGLSAKTVD EVREANHLPE GTIDYIGAGP LHMTATKPES MIVDENGDIT TLNVSSIDEM RTMSKYPLIV GGGVKADDIP MLAKTKADGW FVVSAIAGAT DPEQATRRLV DDWTAIRGDE KPRYTGRKPA ATKLPAVLTI ATTDSSGGAG IPADLKTMLA NDVFGECVVA GITAQNTTGV QAIAAVDPSI VGAQIDSVFD DIRPTAVKIG VIVGVESVKT VARKLRDHQA TNIVVDPVMV ATSGSSLAAD DTIAEEISSL FPIATVITPN IPEAQVLAQM PIGNQADMET AAVQLAKDYG TCVLVKGGHG VKDADDVLAF PTGAVTWFEG ERIANDNTHG TGCTLSSAIA SYLAQGEDLE DAVRDAKAYL SGALRANLNL GKGHGPMDHA WAMH // ID G0HBE8_CORVD Unreviewed; 202 AA. AC G0HBE8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE1; OrderedLocusNames=CVAR_1310; OS Corynebacterium variabile (strain DSM 44702 / JCM 12073 / NCIMB 30131) OS (Corynebacterium mooreparkense). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=858619; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131; RX PubMed=22053731; DOI=10.1186/1471-2164-12-545; RA Schroeder J., Maus I., Trost E., Tauch A.; RT "Complete genome sequence of Corynebacterium variabile DSM 44702 RT isolated from the surface of smear-ripened cheeses and insights into RT cheese ripening and flavor generation."; RL BMC Genomics 12:545-545(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002917; AEK36666.1; -; Genomic_DNA. DR RefSeq; YP_004759739.1; NC_015859.1. DR EnsemblBacteria; AEK36666; AEK36666; CVAR_1310. DR GeneID; 11000086; -. DR KEGG; cva:CVAR_1310; -. DR KO; K00788; -. DR BioCyc; CVAR858619:GHOU-1368-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 17 21 HMP-PP binding (By similarity). FT REGION 118 120 THZ-P binding (By similarity). FT REGION 172 173 THZ-P binding (By similarity). FT METAL 49 49 Magnesium (By similarity). FT METAL 67 67 Magnesium (By similarity). FT BINDING 48 48 HMP-PP (By similarity). FT BINDING 86 86 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). SQ SEQUENCE 202 AA; 21056 MW; 6B28DAD33128A90F CRC64; MPGIVDAAVR GGVSVVQLRD KDATDEVVTQ RAAQLKDTLA DRVPLFVNDR VETAVELGLH LHIGQDDMPY CTARDLLPSG CMIGLSVETP AHLDAVARDI AHGIRPPDVL GIGPVEQTST KPDAAAPLGV EGVRTLAARA RVLGIPTVAI GHVSTRNGAA LLRAGVDGLC TVSAVMAAAD PLAAAQDLRT LIDDTLTRQE IK // ID G0HE73_CORVD Unreviewed; 243 AA. AC G0HE73; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; OrderedLocusNames=CVAR_3070; OS Corynebacterium variabile (strain DSM 44702 / JCM 12073 / NCIMB 30131) OS (Corynebacterium mooreparkense). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=858619; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131; RX PubMed=22053731; DOI=10.1186/1471-2164-12-545; RA Schroeder J., Maus I., Trost E., Tauch A.; RT "Complete genome sequence of Corynebacterium variabile DSM 44702 RT isolated from the surface of smear-ripened cheeses and insights into RT cheese ripening and flavor generation."; RL BMC Genomics 12:545-545(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002917; AEK36465.1; -; Genomic_DNA. DR RefSeq; YP_004759538.1; NC_015859.1. DR EnsemblBacteria; AEK36465; AEK36465; CVAR_3070. DR GeneID; 10999880; -. DR KEGG; cva:CVAR_3070; -. DR KO; K00788; -. DR BioCyc; CVAR858619:GHOU-1162-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 56 60 HMP-PP binding (By similarity). FT REGION 154 156 THZ-P binding (By similarity). FT METAL 89 89 Magnesium (By similarity). FT METAL 108 108 Magnesium (By similarity). FT BINDING 88 88 HMP-PP (By similarity). FT BINDING 127 127 HMP-PP (By similarity). FT BINDING 157 157 HMP-PP (By similarity). FT BINDING 193 193 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 243 AA; 25937 MW; 395313EDA7640F5F CRC64; MSLSRFRATP DRDLRDSRLR QLADSPLYLC TPARTEQGDL RDFLHAAYEG GVDIVQLRDK SIDTCDEIAA LEVLASVAKE HGKMFAVNDR ADIAALVGAD VFHVGQDDLT IAQVRSLLGP DVVVGLSTHS LLQARAAMED ADLDYFCTGP LWETPTKPGR SATGLSLVTE TAAMLASAPE QWQREKVWFT IGGVNASTLP EVQAAAGAGA EGCPVRAVVV RPLTEAGDPR AAAAELKAVL DKN // ID G0HQR0_HALHT Unreviewed; 211 AA. AC G0HQR0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HAH_2625; OS Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC OS 102182 / NCIMB 2187 / VKM B-1755). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Haloarcula. OX NCBI_TaxID=634497; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / RC VKM B-1755; RX PubMed=21994921; DOI=10.1128/JB.05953-11; RA Liu H., Wu Z., Li M., Zhang F., Zheng H., Han J., Liu J., Zhou J., RA Wang S., Xiang H.; RT "Complete genome sequence of Haloarcula hispanica, a model RT haloarchaeon for studying genetics, metabolism, and virus-host RT interaction."; RL J. Bacteriol. 193:6086-6087(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002921; AEM58211.1; -; Genomic_DNA. DR RefSeq; YP_004797199.1; NC_015948.1. DR EnsemblBacteria; AEM58211; AEM58211; HAH_2625. DR GeneID; 11051501; -. DR KEGG; hhi:HAH_2625; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; HHIS634497:GIY3-2621-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21761 MW; CC2770DEA09D2B8B CRC64; MVDWDVYLVT QASLSAGRTT ADIVADAIDG GVGVVQLREK DRTARERYEL GRELRALTRE AGVTFVVNDR VDIAQALDAD GVHLGDDDLP VPVARELLGE DALIGRSVST VADAEAAAAA GADYLGVGAV FATGSKDDID DDEYAIGTDR VAAIADAVDI PFVGIGGITT ENATEVVEAG ADGVAVITEI TQADDPAAAA EALKHAVERG Q // ID G0I7N0_STRES Unreviewed; 209 AA. AC G0I7N0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPPN_03665; OS Streptococcus pseudopneumoniae (strain IS7493). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1054460; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IS7493; RX PubMed=21994930; DOI=10.1128/JB.06075-11; RA Shahinas D., Tamber G.S., Arya G., Wong A., Lau R., Jamieson F., RA Ma J.H., Alexander D.C., Low D.E., Pillai D.R.; RT "Whole-Genome Sequence of Streptococcus pseudopneumoniae Isolate RT IS7493."; RL J. Bacteriol. 193:6102-6103(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002925; AEL10173.1; -; Genomic_DNA. DR RefSeq; YP_004768033.1; NC_015875.1. DR EnsemblBacteria; AEL10173; AEL10173; SPPN_03665. DR GeneID; 11028242; -. DR KEGG; std:SPPN_03665; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; SPSE1054460:GHLA-724-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23310 MW; D126C068BE7FB0B5 CRC64; MFHKELLKLY FICGTTTCQG KNLYRVVEEA LKGGITLFQF REKGEGALEG KEKVELAIKL QDLCKKYNVP FIVNDDIELA LEIDADGVHV GQDDLGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G0I7N7_STRES Unreviewed; 210 AA. AC G0I7N7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPPN_03700; OS Streptococcus pseudopneumoniae (strain IS7493). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1054460; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IS7493; RX PubMed=21994930; DOI=10.1128/JB.06075-11; RA Shahinas D., Tamber G.S., Arya G., Wong A., Lau R., Jamieson F., RA Ma J.H., Alexander D.C., Low D.E., Pillai D.R.; RT "Whole-Genome Sequence of Streptococcus pseudopneumoniae Isolate RT IS7493."; RL J. Bacteriol. 193:6102-6103(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002925; AEL10180.1; -; Genomic_DNA. DR RefSeq; YP_004768040.1; NC_015875.1. DR EnsemblBacteria; AEL10180; AEL10180; SPPN_03700. DR GeneID; 11028249; -. DR KEGG; std:SPPN_03700; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; SPSE1054460:GHLA-731-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22788 MW; F554FECD23B385CB CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPDKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDIIS // ID G0IJG2_BACAM Unreviewed; 205 AA. AC G0IJG2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 22-JAN-2014, entry version 19. DE SubName: Full=Transcriptional regulator TenI; GN Name=tenI; ORFNames=BAXH7_02403; OS Bacillus amyloliquefaciens XH7. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1034836; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XH7; RX PubMed=21914895; DOI=10.1128/JB.05880-11; RA Yang H., Liao Y., Wang B., Lin Y., Pan L.; RT "Complete Genome Sequence of Bacillus amyloliquefaciens XH7, Which RT Exhibits Production of Purine Nucleosides."; RL J. Bacteriol. 193:5593-5594(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XH7; RA Yang H.L., Liao Y.L., Lin Y., Pan L.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002927; AEK89533.1; -; Genomic_DNA. DR RefSeq; YP_005550381.1; NC_017191.1. DR EnsemblBacteria; AEK89533; AEK89533; BAXH7_02403. DR GeneID; 12197352; -. DR KEGG; bxh:BAXH7_02403; -. DR KO; K10810; -. DR BioCyc; BAMY1034836:GL8J-2442-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 22628 MW; 4FAA6755F0DD266E CRC64; MELHAVTDNR KPVAELAEDI LSIQHEVSFI HIRERDKTAG EIMQLLALLK KGGADKDKLV INDRADVALF ANIHRVQLPA RSFSVKQVRN RFPHLHIGRS VHSLKEAVQA EKEDADYVVF GHVFETECKQ GLEARGISLL SDIKSTLSIP VIAIGGVTLQ TIGKAKQAKP DGIAVMSGIF SAENPEEAAK RYARAIREAD YEEAL // ID G0IPT8_BACAM Unreviewed; 222 AA. AC G0IPT8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BAXH7_03973; OS Bacillus amyloliquefaciens XH7. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1034836; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XH7; RX PubMed=21914895; DOI=10.1128/JB.05880-11; RA Yang H., Liao Y., Wang B., Lin Y., Pan L.; RT "Complete Genome Sequence of Bacillus amyloliquefaciens XH7, Which RT Exhibits Production of Purine Nucleosides."; RL J. Bacteriol. 193:5593-5594(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XH7; RA Yang H.L., Liao Y.L., Lin Y., Pan L.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002927; AEK91081.1; -; Genomic_DNA. DR RefSeq; YP_005551929.1; NC_017191.1. DR EnsemblBacteria; AEK91081; AEK91081; BAXH7_03973. DR GeneID; 12197620; -. DR KEGG; bxh:BAXH7_03973; -. DR KO; K00788; -. DR BioCyc; BAMY1034836:GL8J-4019-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23553 MW; 3A14191D1C159089 CRC64; MTRISREMMK DILSVYFIMG SNNTSADPVS VVKKAIEGGA TLFQFREKGS GSLTGEDLVL FAKQVQDVCR RAGIPFIIND DVELALRLEA DGVHIGQDDA DAEETRAAIG DMILGVSAHN VSEVKLAEAA GADYVGMGPV YPTETKKDAE AVQGVTLIEE VRRQGITIPI VGIGGITADN AAPVIEAGAD GVSMISAISQ AEDPKAAARR FFEEVRRSKA KS // ID G0J045_CYCMS Unreviewed; 215 AA. AC G0J045; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 16. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Cycma_3586; OS Cyclobacterium marinum (strain ATCC 25205 / DSM 745) (Flectobacillus OS marinus). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae; OC Cyclobacterium. OX NCBI_TaxID=880070; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25205 / DSM 745; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Schuetze A., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Cyclobacterium marinum DSM 745."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002955; AEL27306.1; -; Genomic_DNA. DR RefSeq; YP_004775537.1; NC_015914.1. DR EnsemblBacteria; AEL27306; AEL27306; Cycma_3586. DR GeneID; 11034750; -. DR KEGG; cmr:Cycma_3586; -. DR KO; K00788; -. DR OMA; YLVIDPS; -. DR BioCyc; CMAR880070:GHDK-3629-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 215 AA; 23987 MW; BF00433B9F823FFF CRC64; MKKLNLQSEK GIYLVIDPSD KPEEELFSLL EKLFTFPLIA VQIWDNFGET QDAVAFTNKV VNLASAYNFP ILVNNRWDLL KLSQADGIHL DSIPVNLSGI PEFSQKNHLV GLTVNNDLNL IHQADLLGFD YVSFCSVYPT STTQHCDLVS FESIRKAAEI TNLPVFLAGG IKTRHLPELH ALPYSGIAII SGVMQNDNPE MALQNYLNSI QKNQS // ID G0JDU1_YERPE Unreviewed; 224 AA. AC G0JDU1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=A1122_07160; OS Yersinia pestis A1122. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=1035377; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A1122; RA Doggett N., Munk A.C., Bruce D.C., Detter J.C., Johnson S.L., Han C.; RT "Finished sequence of Yersinia pestis A1122."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002956; AEL72087.1; -; Genomic_DNA. DR RefSeq; YP_005521107.1; NC_017168.1. DR ProteinModelPortal; G0JDU1; -. DR EnsemblBacteria; AEL72087; AEL72087; A1122_07160. DR GeneID; 12110332; -. DR KEGG; ypt:A1122_07160; -. DR KO; K00788; -. DR BioCyc; YPES1035377:GLMV-1429-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24186 MW; E12654E4BD4B0703 CRC64; MSQLDALSPV ATPGFPSTEQ RLGLYPVVDS LLWIERLLAA GVTTLQLRIK NADDAQVEQD IVAAIELGKR YQARLFINDY WQLAVKHGAY GVHLGQEDLE AADLAAIQQA GLRLGISTHD EHELAVAKTL RPSYIALGHI FPTQTKQMPS SPQGLASLSR QVKNTPDYPT VAIGGISIER VPHVLATGVG SVAVVSAITL ASDWQRATAQ LLHLIEGKEL ADEK // ID G0JMF8_9GAMM Unreviewed; 217 AA. AC G0JMF8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Acife_3262; OS Acidithiobacillus ferrivorans SS3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=743299; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS3; RX PubMed=21705598; DOI=10.1128/JB.05373-11; RA Liljeqvist M., Valdes J., Holmes D.S., Dopson M.; RT "Draft Genome of the Psychrotolerant Acidophile Acidithiobacillus RT ferrivorans SS3."; RL J. Bacteriol. 193:4304-4305(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS3; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Liljeqvist M., RA Valdes J., Holmes D., Dopson M., Woyke T.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002985; AEM49320.1; -; Genomic_DNA. DR RefSeq; YP_004785646.1; NC_015942.1. DR ProteinModelPortal; G0JMF8; -. DR EnsemblBacteria; AEM49320; AEM49320; Acife_3262. DR GeneID; 11044698; -. DR KEGG; afi:Acife_3262; -. DR KO; K00788; -. DR BioCyc; AFER743299:GH39-3318-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22481 MW; 05E21D440ACCE16C CRC64; MARQNPIISG LYAITEAHLM PEPVFLAQAE AALRGGARIL QYRDKGDVVA EAPRRRRQAG ALRELCAQYN ALFVVNDDPL LAQAIGAPAL HVGAEDAPLA ALRVQLGRAI LIGVSCYGSV RQAQEAAAQG ADYVAFGSFF ASPSKPQAPV ISMDVLTAAR AVMDLPIVAI GGITEASGGA LLAAGADALA VISGIFGAND VEGAARRFTA LFGDRKE // ID G0JSG8_9GAMM Unreviewed; 329 AA. AC G0JSG8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 22-JAN-2014, entry version 19. DE SubName: Full=Mutator MutT protein; GN ORFNames=Acife_2801; OS Acidithiobacillus ferrivorans SS3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=743299; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS3; RX PubMed=21705598; DOI=10.1128/JB.05373-11; RA Liljeqvist M., Valdes J., Holmes D.S., Dopson M.; RT "Draft Genome of the Psychrotolerant Acidophile Acidithiobacillus RT ferrivorans SS3."; RL J. Bacteriol. 193:4304-4305(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS3; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Liljeqvist M., RA Valdes J., Holmes D., Dopson M., Woyke T.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002985; AEM48876.1; -; Genomic_DNA. DR RefSeq; YP_004785202.1; NC_015942.1. DR ProteinModelPortal; G0JSG8; -. DR EnsemblBacteria; AEM48876; AEM48876; Acife_2801. DR GeneID; 11044586; -. DR KEGG; afi:Acife_2801; -. DR KO; K03574; -. DR BioCyc; AFER743299:GH39-2851-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 329 AA; 35345 MW; F6C903E786B2A5CF CRC64; MRTVPVATGI IEDAAGRLLI SLRPEGKPWP GFWEFPGGKV EPGETPEQAL VRELWEELGI TVTVPEPFRV LDYTYPERTV RLHFYRVRHW TGTAHGREGQ EVRWLYPWEI PALECLPANF CITAAVLAEA LPQPPLCLIA DPDRLPLLDF RKSLEAALGA GLRWLVLRCK TVPDAPTAAV LSALCAEALA QGAQVYLNHP DPLPGWPRSG RHLTQTQLDA GVRPDAAFGV SCHDAAGLLQ AARRGARYAF LSPLFPTPSH PGATALEPLA FAAMATESSL PLIALGGVTA ARVPVALAAG ARGVAVLSGI LEAPDPAAAT RAYLQHWNG // ID G0JXU1_STEMA Unreviewed; 317 AA. AC G0JXU1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 22-JAN-2014, entry version 20. DE SubName: Full=Mutator MutT protein; GN ORFNames=BurJV3_0630; OS Stenotrophomonas maltophilia JV3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=868597; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JV3; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Medau R., RA Furlan B., Mui Tsai S., Rodriques J., Tiedje J., Woyke T.; RT "Complete sequence of Stenotrophomonas maltophilia JV3."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002986; AEM49964.1; -; Genomic_DNA. DR RefSeq; YP_004791190.1; NC_015947.1. DR ProteinModelPortal; G0JXU1; -. DR EnsemblBacteria; AEM49964; AEM49964; BurJV3_0630. DR GeneID; 11045345; -. DR KEGG; buj:BurJV3_0630; -. DR KO; K03574; -. DR BioCyc; SMAL868597:GHCG-643-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 317 AA; 34705 MW; 2EA451E8D248FB28 CRC64; MPSPTRSIHV VAAVITDARG RVLLNRRTEN RDMAGLWEFP GGKRESGETS EQALVRELRE ELGIEADVGP WLMDVPQRYP DKHLTLEVSH VRSWKGTPRG REGQAITWVA QDKLGRYSMP PADLPVVAAL RQPDRYLITP APAEDAGGVQ HWHDRLQQAV AAGQQRIQLR LPPEHPQRQA MIEQTVRAHR RGVQWLLNRD IALARALGVG VHLGSEQLLA LQERPLPEGQ LVAASCHDLE QLQAAQRLGC DFAVLGPVQA TASHPEAAPL GWEAFAALRA QVSLPIYALG GMAAGHIAEA RRHGGQGIAA IRGLWPA // ID G0K1G2_STEMA Unreviewed; 208 AA. AC G0K1G2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BurJV3_3318; OS Stenotrophomonas maltophilia JV3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=868597; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JV3; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Medau R., RA Furlan B., Mui Tsai S., Rodriques J., Tiedje J., Woyke T.; RT "Complete sequence of Stenotrophomonas maltophilia JV3."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002986; AEM52634.1; -; Genomic_DNA. DR RefSeq; YP_004793860.1; NC_015947.1. DR EnsemblBacteria; AEM52634; AEM52634; BurJV3_3318. DR GeneID; 11048095; -. DR KEGG; buj:BurJV3_3318; -. DR KO; K00788; -. DR BioCyc; SMAL868597:GHCG-3394-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21159 MW; 5A1A0DA152E12C8B CRC64; MTSASPAPRG VYLITPDEPD TARLLARTAP LLAAGATWLQ YRNKTASDAL RRLQATALQA LCVEHGVPLI VNDDPALAKA VGAAGVHLGG TDGDVPSARA LLGTDAIIGA SCYDQLANAE KAVAAGASYV AFGAFFPTTT KITSSRAHTD LLRQSAALGV PRVAIGGLTP DNVGPIIDAG ADLVAVVSSV FAAEDPVAVQ RAYLAQFA // ID G0L8R9_ZOBGA Unreviewed; 217 AA. AC G0L8R9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=zobellia_3656; OS Zobellia galactanivorans (strain DSM 12802 / CIP 106680 / NCIMB 13871 OS / Dsij). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Zobellia. OX NCBI_TaxID=63186; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12802 / CIP 106680 / NCIMB 13871 / Dsij; RG Genoscope - CEA; RT "Complete genome sequence of Zobellia galactanivorans Dsij."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP476056; CAZ97794.1; -; Genomic_DNA. DR RefSeq; YP_004738073.1; NC_015844.1. DR GeneID; 10976212; -. DR KEGG; zga:zobellia_3656; -. DR KO; K00788; -. DR BioCyc; ZGAL63186:GJN9-3656-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23894 MW; 583811E0870652DF CRC64; MNIPKLHYIS QGKTPEEHLE NIQKACTSGA ELVQLRLKNV KKSVVLKTAE KARELTAHFQ TRLIINDHYQ IAKEVQADGV HLGKTDADPV VARKLLGDYY IIGGTANTLD DCLALVKKGV NYIGLGPFRF TTTKENLSPI IPLIGYQGIV GELNSDMPII AIGGITIDDV PEILKTGVYG IAASGEITKD FNKINAFHKL LKAPSTNEQI WNRETKF // ID G0LLH5_HALWC Unreviewed; 223 AA. AC G0LLH5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 21. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Hqrw_2983; OS Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Haloquadratum. OX NCBI_TaxID=768065; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16854 / JCM 12705 / C23; RX PubMed=21701686; DOI=10.1371/journal.pone.0020968; RA Dyall-Smith M., Pfeiffer F., Klee K., Palm P., Gross K., RA Schuster S.C., Rampp M., Oesterhelt D.; RT "Haloquadratum walsbyi: limited diversity in a global pond."; RL PLoS ONE 6:E20968-E20968(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR746099; CCC40781.1; -; Genomic_DNA. DR RefSeq; YP_005840426.1; NC_017459.1. DR EnsemblBacteria; CCC40781; CCC40781; Hqrw_2983. DR GeneID; 12447758; -. DR KEGG; hwc:Hqrw_2983; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; HWAL768065:GLDV-2157-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 22979 MW; F1982B16F1C6323C CRC64; MNTSMQTYLV TQEDRSAGRS TTEIVEAAID GGIDIVQLRE KETTARRRYE IGQTVRTQTA QAGVTFLVND RVDLAAAVNA DGVHLGDDDL PVTAAREVLG QDAIIGRSVS TPAAAQRAED IGADYLGVGA VYPTGTKDVT AESAEIGPKT VTAITDAVSI PVIGIGGITP SNTTEVIRAG ADGVAVVSAI TTADDPAAAT RKLQESVDTA SVESQLPSEE PSA // ID G0LVP0_STAAU Unreviewed; 213 AA. AC G0LVP0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SARLGA251_18930; OS Staphylococcus aureus subsp. aureus LGA251. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=985006; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LGA251; RA Garcia-Alvarez L., Holden M.T., Lindsay H., Webb C.R., Brown D.F., RA Curran M.D., Walpole E., Brooks K., Pickard D.J., Teale C., RA Parkhill J., Bentley S.D., Edwards G.F., Girvan E.K., Kearns A.M., RA Pichon B., Hill R.L., Larsen A.R., Skov R.L., Peacock S.J., RA Maskell D.J., Holmes M.A.; RT "Meticillin-resistant Staphylococcus aureus with a novel mecA RT homologue in human and bovine populations in the UK and Denmark: a RT descriptive study."; RL Lancet Infect. Dis. 11:595-603(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR821779; CCC88658.1; -; Genomic_DNA. DR RefSeq; YP_005755868.1; NC_017349.1. DR EnsemblBacteria; CCC88658; CCC88658; SARLGA251_18930. DR GeneID; 12909011; -. DR KEGG; suf:SARLGA251_18930; -. DR KO; K00788; -. DR BioCyc; SAUR985006:GLKO-1991-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23315 MW; A892338D83DEAD89 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIINDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLGEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID G0M469_LACPE Unreviewed; 218 AA. AC G0M469; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LPENT_01671; OS Lactobacillus pentosus IG1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1042160; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IG1; RA Maldonado-Barragan A., Caballero-Guerrero B., Lucena-Padros H., RA Ruiz-Barba J.L.; RT "Genome Sequence of Lactobacillus pentosus IG1, a Strain Isolated from RT Spanish-Style Green Olive Fermentations."; RL J. Bacteriol. 193:5605-5605(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR874854; CCC16975.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 22790 MW; F54FFCB9BB145025 CRC64; MTLEFEPVQL RAYFVCGTQD VVGRDLETVV QTALDAGITA FQYRDKGASQ LTAAQRLTLG QRLRQRCSDA HVPFIVDDDV ELALALQADG IHVGQSDDRV TQVIERVAGQ LFVGLSCSTL AEIKVANQID GIAYIGSGPI FPTNSKADAD PVVGLAGLRE LVAASQRPIV AIGGITVDQL PAIAATGAAG AAVISMLAQS PDMAATVKSM LTASEARL // ID G0PZG0_STRGR Unreviewed; 216 AA. AC G0PZG0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACT1_5713; OS Streptomyces griseus XylebKG-1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=649189; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XylebKG-1; RX PubMed=21460079; DOI=10.1128/JB.00330-11; RA Grubbs K.J., Biedermann P.H., Suen G., Adams S.M., Moeller J.A., RA Klassen J.L., Goodwin L.A., Woyke T., Munk A.C., Bruce D., Detter C., RA Tapia R., Han C.S., Currie C.R.; RT "Genome Sequence of Streptomyces griseus Strain XylebKG-1, an Ambrosia RT Beetle-Associated Actinomycete."; RL J. Bacteriol. 193:2890-2891(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XylebKG-1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M.L., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Adams S., Grubbs K., Currie C., Woyke T.J.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL877172; EGE45022.1; -; Genomic_DNA. DR ProteinModelPortal; G0PZG0; -. DR EnsemblBacteria; EGE45022; EGE45022; SACT1_5713. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22860 MW; 0436C9E301943904 CRC64; MSTPREQLSD ARLYLCTDAR TRQGDLPAFL DAVLAAGVDI VQLRDKGMEA AEELEHLAVF ADACRRHGKL LAVNDRADVA HAVGADVLHL GQGDLPVPAA RAIIGSDRLI GRSTHAEAEV DAALAQDGVD YFCTGPCWPT PTKPGRHAPG LDLVRYTASL GGSRPWFAIG GIDTGNLDQV LDAGARRVVV VRAVTEADDP AAATAELARR VRARAL // ID G0RD18_HYPJQ Unreviewed; 510 AA. AC G0RD18; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 13. DE SubName: Full=Predicted protein; GN ORFNames=TRIREDRAFT_75992; OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae; OC Trichoderma. OX NCBI_TaxID=431241; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QM6a; RX PubMed=18454138; DOI=10.1038/nbt1403; RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., RA Baker S.E., Chapman J., Chertkov O., Coutinho P.M., Cullen D., RA Danchin E.G., Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., RA Han C.S., Ho I., Larrondo L.F., de Leon A.L., Magnuson J.K., RA Merino S., Misra M., Nelson B., Putnam N., Robbertse B., Salamov A.A., RA Schmoll M., Terry A., Thayer N., Westerholm-Parvinen A., Schoch C.L., RA Yao J., Barabote R., Nelson M.A., Detter C., Bruce D., Kuske C.R., RA Xie G., Richardson P., Rokhsar D.S., Lucas S.M., Rubin E.M., RA Dunn-Coleman N., Ward M., Brettin T.S.; RT "Genome sequencing and analysis of the biomass-degrading fungus RT Trichoderma reesei (syn. Hypocrea jecorina)."; RL Nat. Biotechnol. 26:553-560(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL985059; EGR50682.1; -; Genomic_DNA. DR RefSeq; XP_006963252.1; XM_006963190.1. DR EnsemblFungi; EGR50682; EGR50682; TRIREDRAFT_75992. DR GeneID; 18488555; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 510 AA; 52703 MW; 981962A9AEC8F2C0 CRC64; MDKSKVDYSV YLVTDSTPAI LGTKDLVRVV EAAVRGGVSI VQYRDKHSDR QTAVQTARKL LEVTRRFGVP LLVNDRVDVA VEVGCEGVHI GQDDMAYEEA RKLLGPDKII GVTASSVDEA LAACKAGADY LGLGTVYATP TKKDTKSIIG PSGIRSILQA LSSAGHASIP TVCIGGINAR NATAVLLESS AAPQKSLDGI AVVSALVAAD DPAAAARDLL AKVVTGRVPD VLRAVAEATP LSHNMTNLVV QNFAANVALA VGASPIMANY AEEAADLAKL GGALVINMGT VTPDGLKNHI QAIQAYNAAG GPVVLDPVGA GATSIRRSAV QTLLSSGKFT IIKGNEREIH TISNTSSAIV QRGVDSSSTL SIPQRAALAK SVSRSTGGGA VVVLTGKTDI VSDGVRTLRI DNGHEYLGRV TGTGCTLGTT LSAMVAAFRG KKSPLVAAVA GLVMFEIAAE RAGVRDDVRG PGTFVPAFLD ELSALREETV RGDVKWLAGA KVEAVEVEEE // ID G0S545_CHATD Unreviewed; 546 AA. AC G0S545; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 12. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme-like protein; GN ORFNames=CTHT_0024040; OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae; OC Chaetomium. OX NCBI_TaxID=759272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719; RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039; RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., RA Devos D.P., Arumugam M., Bork P., Hurt E.; RT "Insight into structure and assembly of the nuclear pore complex by RT utilizing the genome of a eukaryotic thermophile."; RL Cell 146:277-289(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL988041; EGS20570.1; -; Genomic_DNA. DR RefSeq; XP_006692866.1; XM_006692803.1. DR GeneID; 18256442; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 546 AA; 58792 MW; A0007E39099C997A CRC64; MGTEFGVLST GFGLSGEWRK SHTDADLNYT LYLVTDSSPQ ILGDRDLCDV VEQAIKGGVT IVQLREKNCD TREFIEKARR LHAITKKYDV PLLINDRIDV ALAVNCEGVH IGQDDMDIHE ARRLLGPWAI IGVTVSTVEE AIKAAKDGAN YLGIGTIYAT STKKDTKHII GTAGVARILS ALHKAGHPVD CVGIGGINES NVHRIVYQSA VDRDRIFLKG VAVVSAIMAA PDPQAAAKRL KEKMTSVPPY GVDVPSYIAD TTEKVLAEVP SVITAVDANT PLSHNMTNLV VQNFAANVAL AIGASPIMSN CGDEAADLSK LGGSLVINMG TVDDDALANY IKAVRAYNAV DRPVIFDPVG AGATTIRRQA VKTLLHECYF DVIKGNEGEI RTVFGDSDVQ QRGVDSTSTL DETAKATLVR ALAKREKNVV VMTGKTDYVS DGINTYAVEN GHPYLGLVTG TGCTLGTAIS AAVAKRTTYG RIVHVIAALL HFEIAAELAA ERADVKGPGT FLPAFLDELY RIRKDTVEEN LEWLQRAKVR KIELRD // ID G0ST34_VIBMI Unreviewed; 420 AA. AC G0ST34; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=SX4_1279; OS Vibrio mimicus SX-4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=756012; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SX-4; RX PubMed=21731695; DOI=10.1371/journal.pone.0021299; RA Wang D., Wang H., Zhou Y., Zhang Q., Zhang F., Du P., Wang S., RA Chen C., Kan B.; RT "Genome Sequencing Reveals Unique Mutations in Characteristic RT Metabolic Pathways and the Transfer of Virulence Genes between V. RT mimicus and V. cholerae."; RL PLoS ONE 6:E21299-E21299(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL989620; EGU17870.1; -; Genomic_DNA. DR EnsemblBacteria; EGU17870; EGU17870; SX4_1279. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 420 AA; 46841 MW; 4041B19C6BEF0DC1 CRC64; MTRLVFPCSS VELIGRVQYV LLQAKEQGFD IQNISLDVAT SDCFVLEAES TLRIACDLCL CEDTSELLDY YLQYLPEHRD IEARCKVKIG LRSHSDLGVD EWQVEENSSQ RITYPYPSLI SNCQLDQHVA WVLAMLALGF PIADALCVAR AAMSQKQDVS RETWPINLES FPSVHSGSEL QATKGFPAID KSQFTLYPVV DDVSWIELLL KLGVKTVQLR IKDPMQVDLE EQIVRAIDLG REYNAQVFIN DYWQIAIKHK AYGVHLGQED LTTANLTELA QAGLRLGLST HGYYELLNVA CLQPSYIALG HIFPTTTKQM PSKPQGLVRL AAYQGLANQL SYHGQKGMPT VAIGGIDHSN IEEVLRCGVT SAAVVRAITQ SANPALAVHQ LMFAFSGQKE SELRKQAKSY NMEWETSNVE // ID G0T164_RHOG2 Unreviewed; 521 AA. AC G0T164; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 13. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme Thi4; GN ORFNames=RTG_02860; OS Rhodotorula glutinis (strain ATCC 204091 / IIP 30 / MTCC 1151) OS (Yeast). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; OC Microbotryomycetes; Sporidiobolales; mitosporic Sporidiobolales; OC Rhodotorula. OX NCBI_TaxID=1001064; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204091 / IIP 30 / MTCC 1151; RX PubMed=24526636; DOI=10.1128/genomeA.00046-14; RA Paul D., Magbanua Z., Arick M.II., French T., Bridges S.M., RA Burgess S.C., Lawrence M.L.; RT "Genome Sequence of the Oleaginous Yeast Rhodotorula glutinis ATCC RT 204091."; RL Genome Announc. 2:e00046-14(2014). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVR02000018; EGU11363.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 521 AA; 55317 MW; AA96514C32F8CF14 CRC64; MPNFSLYYVT GRSLLPPPPS SYTGPKEDYY LAHLEQALKG GVTVVQVREK DVDGAEFLEV ARRTKEVCDK YDVPLFINDR VDVALALKCH CHVGQTDLPA RLVRQLLGPD ALIGVSVNTP EEMQVVMDEG VADYVGVGPC FGTQTKKNLN PILGPRGVRA VLETLGESEI KAVIIGGITP STIPNVLAQT PAPLPSGGYR ALDGLAVVSA IAASTEPETA ARELREMFDR KPAYPSRLLD PGELSADHVV EQAVELLRIL KDGEKTPLVH HITNFVVMND TANLTLAFGA SPIMSASPDE APHLSQLISC LLLNLGTITE AQLNAQKIAG AAANKNRKPV VFDPVGVGAT EYRKKSASDL LNTCHVSIIK GNAGEIGALS GLSEVKARGV DSVGKGFKDP ATVVKTLAAR EKLVVAMSGE TDYISDGQVS FTIKNGTFWQ EKITGSGCMA SAAVALFAGL QHESGPFIAA IAGLLAINVA AEIAAARPEV NGPNTFRAAL IDACYNLRPE DVRSRAKVQR V // ID G0TNZ6_MYCCP Unreviewed; 222 AA. AC G0TNZ6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MCAN_04121; OS Mycobacterium canettii (strain CIPT 140010059). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1048245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIPT 140010059; RX PubMed=23291586; DOI=10.1038/ng.2517; RA Supply P., Marceau M., Mangenot S., Roche D., Rouanet C., Khanna V., RA Majlessi L., Criscuolo A., Tap J., Pawlik A., Fiette L., Orgeur M., RA Fabre M., Parmentier C., Frigui W., Simeone R., Boritsch E.C., RA Debrie A.S., Willery E., Walker D., Quail M.A., Ma L., Bouchier C., RA Salvignol G., Sayes F., Cascioferro A., Seemann T., Barbe V., RA Locht C., Gutierrez M.C., Leclerc C., Bentley S.D., Stinear T.P., RA Brisse S., Medigue C., Parkhill J., Cruveiller S., Brosch R.; RT "Genomic analysis of smooth tubercle bacilli provides insights into RT ancestry and pathoadaptation of Mycobacterium tuberculosis."; RL Nat. Genet. 45:172-179(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE572590; CCC42752.1; -; Genomic_DNA. DR RefSeq; YP_004743891.1; NC_015848.1. DR EnsemblBacteria; CCC42752; CCC42752; MCAN_04121. DR GeneID; 10986538; -. DR KEGG; mce:MCAN_04121; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; MCAN1048245:GJCJ-416-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23270 MW; A0BAB0878F8862C1 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THNPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID G0UFZ6_9LACT Unreviewed; 205 AA. AC G0UFZ6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=WT2_00674; OS Weissella thailandensis fsh4-2. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Weissella. OX NCBI_TaxID=1056112; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Fsh4-2; RA Benomar N., Abriouel H., Lee H., Cho G.S., Huch M., Pulido R.P., RA Holzapfel W.H., Galvez A., Franz C.M.; RT "Genome Sequence of Weissella thailandensis fsh4-2."; RL J. Bacteriol. 193:5868-5868(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Fsh4-2; RA Franz C.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE575150; CCC56674.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22193 MW; 5714752E36229BF5 CRC64; MAKQLYLVTA RYGETESEFL NKVETACANG VTLVQLREKN LSTRDYYELA LKVKQITDRY GLKLIIDDRI DICQAVDAGG VHIGDDELPV SVARQLLGKE KLLGVSAKTV ARATEAAAEG ADYLGTGAIF PTQTKVVTKQ TSVDTLREIT AAVNIPVVAI GGITEDRIMT FKGTGIAGIS VVSEIMKADD IAQKVQHLKK KLEQL // ID G0V5C5_NAUCC Unreviewed; 542 AA. AC G0V5C5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 16. DE SubName: Full=Uncharacterized protein; GN Name=NCAS0A01010; OrderedLocusNames=NCAS_0A01010; OS Naumovozyma castellii (strain ATCC 76901 / CBS 4309 / NBRC 1992 / NRRL OS Y-12630) (Yeast) (Saccharomyces castellii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Naumovozyma. OX NCBI_TaxID=1064592; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 76901 / CBS 4309 / NBRC 1992 / NRRL Y-12630; RX PubMed=22123960; DOI=10.1073/pnas.1112808108; RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., RA Byrne K.P., Wolfe K.H.; RT "Evolutionary erosion of yeast sex chromosomes by mating-type RT switching accidents."; RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Type strain:CBS 4309; RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., RA Byrne K.P., Wolfe K.H.; RT "Genome sequence of Naumovozyma castellii."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE576752; CCC66661.1; -; Genomic_DNA. DR RefSeq; XP_003673052.1; XM_003673004.1. DR GeneID; 11529704; -. DR KEGG; ncs:NCAS_0A01010; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 542 AA; 57976 MW; 9F50562AB4348531 CRC64; MVFDKSKVDY SLYLVTDSTM LPEGTTLYSQ VEAGLKNGVT LVQLREKDSD TKIFIEEALE VKKLCVKYNV PLIINDRVDV ALAIDADGVH VGQGDMPIPM VRALVGPDRI VGWSVGKTSE VETLAQWGPD MVDYIGIGMV FPTMTKKNPK KSPMGPQGVI EILDALEINN ADWCRTVAIG GLHPNNIERV LYQCGSSNGK RSLDGISVVS DIMAASDAGA ATRTLRKLLS QSSYQYVALD LKYSDSVSNR GLIKSIIEQV TNNSPLVQHI TNKVHQNFGA NVALALGSSP IMSEVESEVD ELAHIPNASL LVNTGTVAPV EMLKTAIAAY NNAKRPIVFD PVGYSATQTR LILNDTLLTY GQFTCIKGNS GEILSLANLN QGKMKGVDAG EETVSKELLA RATRVVAYKY KTIAVCTGEY DFIADGTFGG SYSLSNATAG VSADKIPCWM VEDGPIPIMG EITASGCSLG STISCLVGGL SATGNVFHAV VAAVILYKSA GKLASTKCKG NGSFNVELID ALYQLFHDNK PETWTANLTQ IA // ID G0VLH1_MEGEL Unreviewed; 196 AA. AC G0VLH1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 22-JAN-2014, entry version 15. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=MELS_0328; OS Megasphaera elsdenii DSM 20460. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=1064535; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20460; RA Marx H., Graf A.B., Tatto N., Thallinger G.G., Mattanovich D., RA Sauer M.; RT "Genome sequence of the ruminal bacterium Megasphaera elsdenii."; RL J. Bacteriol. 193:5578-5579(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20460; RA Graf A.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE576794; CCC72551.1; -; Genomic_DNA. DR RefSeq; YP_004765378.1; NC_015873.1. DR EnsemblBacteria; CCC72551; CCC72551; MELS_0328. DR GeneID; 11185229; -. DR KEGG; med:MELS_0328; -. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 196 AA; 21721 MW; F2FE40C9550B5A33 CRC64; MLKVAAITNH ELASTNYWDQ LEQIAASDVD FIVLREKNLT EEEYTDYAKR ALRLCSIHQK TCVLQHFGKA AIRLHIPRFQ CSLPYLETHS SLLYYMTTLG VSVHTVEEAI KAEQLGATYL MASHVFPTAC KPSDPPIGVD TVEAICKAVK IPVYALGGVT PKTISQLQDV PIKGVALMSG LMTCPDVPEY LKELRA // ID G0VLW5_MEGEL Unreviewed; 215 AA. AC G0VLW5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MELS_2096; OS Megasphaera elsdenii DSM 20460. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=1064535; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20460; RA Marx H., Graf A.B., Tatto N., Thallinger G.G., Mattanovich D., RA Sauer M.; RT "Genome sequence of the ruminal bacterium Megasphaera elsdenii."; RL J. Bacteriol. 193:5578-5579(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20460; RA Graf A.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE576794; CCC74313.1; -; Genomic_DNA. DR RefSeq; YP_004767140.1; NC_015873.1. DR EnsemblBacteria; CCC74313; CCC74313; MELS_2096. DR GeneID; 11184030; -. DR KEGG; med:MELS_2096; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23568 MW; C0300B68CB72AB77 CRC64; MTKEEHVKHL LEDPVYAIMG NEELCLGRSN MDVAKELIAA GVTIIQYREK HKKWRAKYEE TKAIAQLCHD HNVTFIMNDS TDLAIACGAD GIHVGQDDAP AQIVRQLAGP DVFIGVSTNT IDEMKQALAD GADYVGFGPM FPTQSKKDAD EVVTPEAKAY ALHYELPVVT IGGVSLENIR SLYDEGFRSF AMISAIVGQK DIKGAVEKIR QTLGC // ID G0VXN7_PAEPO Unreviewed; 197 AA. AC G0VXN7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 22-JAN-2014, entry version 17. DE SubName: Full=Regulatory protein TenI; DE EC=2.5.1.3; GN Name=tenI; ORFNames=PPM_2608; OS Paenibacillus polymyxa M1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1052684; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M1; RA Niu B., Rueckert C., Blom J., Wang Q., Borriss R.; RT "The Genome of the Plant Growth-Promoting Rhizobacterium Paenibacillus RT polymyxa M-1 Contains Nine Sites Dedicated to Nonribosomal Synthesis RT of Lipopeptides and Polyketides."; RL J. Bacteriol. 193:5862-5863(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE577054; CCC85545.1; -; Genomic_DNA. DR RefSeq; YP_005960252.1; NC_017542.1. DR EnsemblBacteria; CCC85545; CCC85545; PPM_2608. DR GeneID; 12551323; -. DR KEGG; ppo:PPM_2608; -. DR KO; K10810; -. DR BioCyc; PPOL1052684:GLI7-2701-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 197 AA; 21038 MW; E1F9E4768363CEE5 CRC64; MESVSCVNVP QVAAAICPYI HYVHARSKQK GASALLSLTR SMIKQEVPLR QIVVNDRVDV ALLTSAGAVQ LPANGLSVVD AKSLLSEGTR CGVSVHSLEE VQTAEQAGAD YVLFGHVYET HCKAGLVPRG IAQLERICRL SDIPVIALGG IQPHHVPELY HAGASGIAVM SGIWEAKSPV AAAMEYRRMV DLVVHDL // ID G0WCG2_NAUDC Unreviewed; 541 AA. AC G0WCG2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 16-APR-2014, entry version 15. DE SubName: Full=Uncharacterized protein; GN Name=NDAI0F01540; OrderedLocusNames=NDAI_0F01540; OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / OS NBRC 0211 / NRRL Y-12639) (Saccharomyces dairenensis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Naumovozyma. OX NCBI_TaxID=1071378; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639; RX PubMed=22123960; DOI=10.1073/pnas.1112808108; RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., RA Byrne K.P., Wolfe K.H.; RT "Evolutionary erosion of yeast sex chromosomes by mating-type RT switching accidents."; RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE580272; CCD25473.1; -; Genomic_DNA. DR RefSeq; XP_003670716.1; XM_003670668.1. DR GeneID; 11499212; -. DR KEGG; ndi:NDAI_0F01540; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 541 AA; 58222 MW; F56356EA2A21C8ED CRC64; MVFPKDKVDY SLYLVTDSTM LPEGTTLYSQ VEAGLKNGVT LVQLREKDTD TKIFIEEAIA VQKLCKAYDV PLIINDRIDV ALAIDADGVH VGQSDMPIPM VRQLLGPDKI VGWSVGKTSE VETLAQWGTD MVDYIGIGMV FPTETKKNPR KSPMGPTGVI DILNALETTQ ATWCRTVAIG GLHPNNIPRV LYQCVSHNGK RALDGISVVS DIMASDDAGA STKILRGLLD YSKFEYIPLD FSHQENITSK DIKDTLSQVQ KNHPLVQHMT NKVHQNFGAN VTLALGSSPI MSEVPSEVDE LASVPNAALL LNTGSVAPVE ALKEAVRAYN ERKRPIIFDP VGYSATQTRL TLNNTLLQYG QYTCIKGNSG EILSLAKLNQ GKMRGVDAGD DKVDKALLAR ATRLVAFTYK TIAVCTGEYD FIADGTMSSS YRLGHGVGEL SANDIPCVMI EDGPIPLMEK ITASGCSLGT AIAALVGGLS PNGIAFNAVV SAVLLYKSAG KLASLNCRGS GSFHVHLIDA LDQLFTTNDP SSWTAKVEIV T // ID G1USP4_9DELT Unreviewed; 215 AA. AC G1USP4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1022_01617; OS Desulfovibrio sp. 6_1_46AFAA. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=665942; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_46AFAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C.E., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Desulfovibrio sp. 6_1_46AFAA."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWM01000051; EGW51408.1; -; Genomic_DNA. DR EnsemblBacteria; EGW51408; EGW51408; HMPREF1022_01617. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23174 MW; CBB982CFBBAA41AF CRC64; MPAILPGRTD LYALTDSRLS LGRPLAVVAG ALLESGVRIL QYREKKLKAG KMLEECRLLR RLTERAGACF IVNDHIDIAM LVGADGVHIG QEDLPVPEVR RLVGPDMLIG LSTHTPEQAV AAVNAGADYI GVGPIFATQT KEDVVDPVGF EYLEWVARNI ELPFVAIGGI KEHNIADVAR HGARCCALVS ELVGAQDIHA KVEAVRRAMR EGLGV // ID G1V8N8_9DELT Unreviewed; 214 AA. AC G1V8N8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0178_03885; OS Bilophila sp. 4_1_30. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Bilophila. OX NCBI_TaxID=693988; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_1_30; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C.E., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bilophila sp. 4_1_30."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADCO01000343; EGW43177.1; -; Genomic_DNA. DR EnsemblBacteria; EGW43177; EGW43177; HMPREF0178_03885. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22984 MW; 47FA4DC1F832E731 CRC64; MPRLLPGTSP ETDLYALTDD GLSLGRPAVE VAKALLDSGI KILQYREKEK KAGQMLKECM ELRRLTREAG ACFIVNDHVD IAILCEADGV HVGQEDLPVE AVRRLVGPDM IIGLSTHTPD QARAAVASGA DYIGVGPIYP TQTKKDVCAA VTLDYLDWVV ANITLPFVAI GGIKRHNIAD VIAHGARCCA IVSEFVSAPD IPARVAEVRS AMKK // ID G1VQ02_9FIRM Unreviewed; 209 AA. AC G1VQ02; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9022_02083; OS Erysipelotrichaceae bacterium 2_2_44A. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=457422; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_2_44A; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C.E., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Erysipelotrichaceae bacterium 2_2_44A."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADCZ01000020; EGX75584.1; -; Genomic_DNA. DR EnsemblBacteria; EGX75584; EGX75584; HMPREF9022_02083. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22577 MW; E81E8BD772415F8E CRC64; MRFDLTLYLV SDSTGLSEEE FLRRLEQALR GGVTLLQLRE KNRTTLEYYE LARKVKKLTD AYGVPLMIDD RVDIALAVDA AGVHVGAEDM PVKEARRLMG PDKIVGATAK RVDTAMQAEA DGADYLGVGA IYPTTTKVKT VLTSVETLQD ICAHVSIPVG AIGGLNAENC EILKGTGIKG ICVVSAIMKQ ENSYDAAKAL KAKIMTICK // ID G1WSY3_9FIRM Unreviewed; 214 AA. AC G1WSY3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9457_02234; OS Dorea formicigenerans 4_6_53AFAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea. OX NCBI_TaxID=742765; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_6_53AFAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C.E., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Dorea formicigenerans 4_6_53AFAA."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLU01000048; EGX72897.1; -; Genomic_DNA. DR EnsemblBacteria; EGX72897; EGX72897; HMPREF9457_02234. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23023 MW; 26022F1CD30F829A CRC64; MKCDKKDLLL YAVTDRSWLN AETLYSQVEK ALEGGATFVQ LREKHLDHDA FLQEAKEIKE LCAKYQVPFV LDDDVELALE VGADGVHVGQ SDMEAGDVRA KLGEDKIVGV SAQTVEQALL AQERGADYLG VGAVFPTSSK DDAVEVDHEM VKAICEAVDI PVIAIGGITK DNVQELSGCG LCGIAVISAI FAKPDIKKAT EELKAATEKM LKAC // ID G1WUZ4_9FIRM Unreviewed; 224 AA. AC G1WUZ4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-MAR-2014, entry version 13. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF9457_02945; OS Dorea formicigenerans 4_6_53AFAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea. OX NCBI_TaxID=742765; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_6_53AFAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C.E., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Dorea formicigenerans 4_6_53AFAA."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLU01000064; EGX70860.1; -; Genomic_DNA. DR EnsemblBacteria; EGX70860; EGX70860; HMPREF9457_02945. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 224 AA; 25060 MW; 991E6BB149BB416A CRC64; MNCNDSMINN SILKKRNDPG KNFQILAISN RHLCNQPFED QIKRVCEWHP DALVLREKDL PEDEYKALAK SILDICKAYD VPCILHTYWK AALELGHDAI HLPLPLLREL SAESQKHLQS QNSTISQSFH VTDFHKIGTS VHSVEDAMEA ERLGATYVTA GHIFTTDCKK GLPPRGLDFL KNVCDAVTIP VYGIGGIKFD PQQWNSLKKQ GACGGCIMSG MMQL // ID G1XIZ7_ARTOA Unreviewed; 553 AA. AC G1XIZ7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-APR-2014, entry version 13. DE SubName: Full=Uncharacterized protein; GN ORFNames=AOL_s00097g324; OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491) OS (Nematode-trapping fungus) (Didymozoophaga oligospora). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes; OC Orbiliales; Orbiliaceae; Orbilia. OX NCBI_TaxID=756982; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491; RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179; RA Yang J., Wang L., Ji X., Feng Y., Li X., Xou C., Xu J., Ren Y., Mi Q., RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., RA Luo Y., Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., RA Zhang K.-Q., Ji K., Wang L., Zhang K.; RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora RT provide insights into nematode-trap formation."; RL PLoS Pathog. 7:E1002179-E1002179(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADOT01000174; EGX46898.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 553 AA; 58125 MW; 588B29CA38AAC7E6 CRC64; MSEQAAMMSD AAKGPAVEMS TSTSMVPTSP TKPKFDLTLY LVTSSSLLPQ NCTLESHIEA AIKGGVTIVQ LREKNLDTAP FIALGKRIHS ITKKYGVPLL INDRVDVALA VGCEGAHIGW DDMDYNTARN LLGPTAIIGL SVSNVTQASL AASTTADYIG IGPIFPTRTK PDASAPLYPS GLRQILGLIS SKRPELPSVA IGSINAANLQ AVLYKSRPTE GLPLAGVAVV SAIISSTDPE SAASGLLSLY KSPPLWASPP PSQSTAFNHF YLPLILDKVV TILRTIKEHK PLVHHITNAV VKNFSANVTL AVGGSPIMSD NLEEVADLAA IAPHSACLVN MGTSGPGERR LYLQAIRENN KTGKPVVFDP VGAGATGMRK ETVRWVLDEC GYVDVIKGNE GEIRTIAGEG IRMKGVDSDS AGGIDDLIKV VKGVAGRERN VVVTTGVTDV LSDGVRTVLV NNGHPFQALV TGMGCALGSV LCAALAVNKD DKLMSCLAAV LLYNVAAERA VKKDGSRGPG SFSAAFLDEL YEIGEICARG ESGWLDGVKV EFM // ID G1XWX4_9PROT Unreviewed; 172 AA. AC G1XWX4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=AZA_87500; OS Azospirillum amazonense Y2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=1003237; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y2; RX PubMed=21838888; DOI=10.1186/1471-2164-12-409; RA Sant'anna F.H., Almeida L.G., Cecagno R., Reolon L.A., Siqueira F.M., RA Machado M.R., Vasconcelos A.T., Schrank I.S.; RT "Genomic insights into the versatility of the plant growth-promoting RT bacterium Azospirillum amazonense."; RL BMC Genomics 12:409-409(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y2; RA Sant' Anna F.H., Almeida L.G.P., Cecagno R., Reolon R., Maboni F., RA Machado M.R.S., Vasconcelos A.T.R., Schrank I.S.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBX01000123; EGY02223.1; -; Genomic_DNA. DR EnsemblBacteria; EGY02223; EGY02223; AZA_87500. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 172 AA; 18621 MW; 06900830261B3EF7 CRC64; MRLKDVDDDT VRRAIDALRP IAQSREVAFI LNDHPRLARE TGCDGVHVGQ ADTPYREARK IMGAEAIVGV TCHDSRHLAM VAGEDGADYV AFGAFFPTGT KETEHRATPD LLTWWQEMME IPCVAIGGIT PDNCGDLVRA GADFLAVVSS VWHHPEGPGA AVRAFNKAIA EA // ID G1YH40_ECOLX Unreviewed; 211 AA. AC G1YH40; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECSTECB2F1_4387; OS Escherichia coli STEC_B2F1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754084; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STEC_B2F1; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDQ01000032; EGW65215.1; -; Genomic_DNA. DR EnsemblBacteria; EGW65215; EGW65215; ECSTECB2F1_4387. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23069 MW; 886F5E43FE4A8ADE CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEV DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G1YXT2_ECOLX Unreviewed; 211 AA. AC G1YXT2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECSTECC16502_4890; OS Escherichia coli STEC_C165-02. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754085; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STEC_C165-02; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDR01000030; EGW63034.1; -; Genomic_DNA. DR ProteinModelPortal; G1YXT2; -. DR EnsemblBacteria; EGW63034; EGW63034; ECSTECC16502_4890. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 4A5B4907CA38B2E8 CRC64; MYQPDFPPVP FHLGLYPVVD SAQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAITLGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVMATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G1ZCP2_ECOLX Unreviewed; 211 AA. AC G1ZCP2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EC253486_5123; OS Escherichia coli 2534-86. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754079; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2534-86; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDS01000072; EGW64035.1; -; Genomic_DNA. DR ProteinModelPortal; G1ZCP2; -. DR SMR; G1ZCP2; 10-208. DR EnsemblBacteria; EGW64035; EGW64035; EC253486_5123. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G1ZRQ0_ECOLX Unreviewed; 193 AA. AC G1ZRQ0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EC30301_4620; OS Escherichia coli 3030-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754080; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3030-1; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDT01000061; EGW79807.1; -; Genomic_DNA. DR EnsemblBacteria; EGW79807; EGW79807; EC30301_4620. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 19 23 HMP-PP binding (By similarity). FT REGION 116 118 THZ-P binding (By similarity). FT REGION 168 169 THZ-P binding (By similarity). FT METAL 52 52 Magnesium (By similarity). FT METAL 71 71 Magnesium (By similarity). FT BINDING 51 51 HMP-PP (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 193 AA; 20955 MW; 221F8D93D776B08B CRC64; MDSVQWIERL LDAGVRTLQL RIKDRRDEEV EADVVAAIAL GRRYNARLFI NDYWRLAIKH QAYGVHLGQE DLQATDLNAI RAAGLRLGVS THDDMEIDVA LAARPSYIAL GHVFPTQTKQ MPSAPQGLEQ LARHVERLAD YPTVAIGGIS LARAPAVIAT GVGSIAVVSA ITQAADWRLA TAQLLEIAGV GDE // ID G2A758_ECOLX Unreviewed; 211 AA. AC G2A758; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECSTEC94C_4772; OS Escherichia coli STEC_94C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754083; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STEC_94C; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDU01000030; EGW78934.1; -; Genomic_DNA. DR ProteinModelPortal; G2A758; -. DR SMR; G2A758; 11-208. DR EnsemblBacteria; EGW78934; EGW78934; ECSTEC94C_4772. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23027 MW; 0AE827392C8C3853 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGVSLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G2ANN7_ECOLX Unreviewed; 211 AA. AC G2ANN7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECSTECDG1313_5206; OS Escherichia coli STEC_DG131-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754086; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STEC_DG131-3; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDV01000065; EGW84882.1; -; Genomic_DNA. DR ProteinModelPortal; G2ANN7; -. DR SMR; G2ANN7; 11-208. DR EnsemblBacteria; EGW84882; EGW84882; ECSTECDG1313_5206. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23027 MW; 0AE827392C8C3853 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGVSLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G2B2I8_ECOLX Unreviewed; 211 AA. AC G2B2I8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECSTECEH250_4764; OS Escherichia coli STEC_EH250. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754087; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STEC_EH250; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDW01000037; EGW89565.1; -; Genomic_DNA. DR ProteinModelPortal; G2B2I8; -. DR SMR; G2B2I8; 20-202. DR EnsemblBacteria; EGW89565; EGW89565; ECSTECEH250_4764. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G2BGR9_ECOLX Unreviewed; 211 AA. AC G2BGR9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECG581_4531; OS Escherichia coli G58-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754078; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=G58-1; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDX01000045; EGX00348.1; -; Genomic_DNA. DR ProteinModelPortal; G2BGR9; -. DR SMR; G2BGR9; 20-202. DR EnsemblBacteria; EGX00348; EGX00348; ECG581_4531. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G2BX54_ECOLX Unreviewed; 211 AA. AC G2BX54; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECSTECH18_4997; OS Escherichia coli STEC_H.1.8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754088; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STEC_H.1.8; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDY01000047; EGX02762.1; -; Genomic_DNA. DR ProteinModelPortal; G2BX54; -. DR SMR; G2BX54; 10-208. DR EnsemblBacteria; EGX02762; EGX02762; ECSTECH18_4997. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G2CC48_ECOLX Unreviewed; 211 AA. AC G2CC48; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECSTECMHI813_4456; OS Escherichia coli STEC_MHI813. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754089; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STEC_MHI813; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDZ01000027; EGX00877.1; -; Genomic_DNA. DR EnsemblBacteria; EGX00877; EGX00877; ECSTECMHI813_4456. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23013 MW; 2C3103AAC598690F CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLQLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G2CSP2_ECOLX Unreviewed; 211 AA. AC G2CSP2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECSTECS1191_4943; OS Escherichia coli STEC_S1191. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754090; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STEC_S1191; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFEA01000023; EGX14307.1; -; Genomic_DNA. DR ProteinModelPortal; G2CSP2; -. DR SMR; G2CSP2; 20-202. DR EnsemblBacteria; EGX14307; EGX14307; ECSTECS1191_4943. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G2D6X4_ECOLX Unreviewed; 211 AA. AC G2D6X4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECTX1999_4758; OS Escherichia coli TX1999. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670903; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TX1999; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFEB01000062; EGX19336.1; -; Genomic_DNA. DR ProteinModelPortal; G2D6X4; -. DR SMR; G2D6X4; 10-208. DR EnsemblBacteria; EGX19336; EGX19336; ECTX1999_4758. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G2DCJ0_9GAMM Unreviewed; 311 AA. AC G2DCJ0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Rifp1Sym_bc00060; OS endosymbiont of Riftia pachyptila (vent Ph05). OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=1048808; RN [1] RP NUCLEOTIDE SEQUENCE. RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D., RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., RA Hecker M., Sievert S.M., Schweder T.; RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and RT Tevnia jerichonana share an identical physiology as revealed by RT proteogenomic analyses."; RL ISME J. 0:0-0(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOC01000030; EGV51645.1; -; Genomic_DNA. DR ProteinModelPortal; G2DCJ0; -. DR EnsemblBacteria; EGV51645; EGV51645; Rifp1Sym_bc00060. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 311 AA; 34453 MW; CD1B32AACE40DBF8 CRC64; MTLIHVAAAA IIDSAGRVLI SKRHEHLHQG GLWEFPGGKL EPGESVEAAL RRELYEELGI RISRFEPLIR VTHHYAECSV LLDVYRVFSY QGEPRGMEGQ PLNWVLPEAM EPALFPAADR PIISALQLPS RYLITGEDPT NPEAFCARLE RALKRDCRLL QLRAHGLSDV AYRSLLGEAL ALSQAHGARL LINRPQRSLD WFGVADGVHL NRHQLFELTA RPQAAGLLGA SCHDLQELKQ AERLGLDYAL LSSVLPTATH PEARPLGWAQ FRTLLEQVNI PVYALGGMGM EQLSTAREHG AQGIAAIRGL W // ID G2DDH7_9GAMM Unreviewed; 215 AA. AC G2DDH7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Rifp1Sym_bn00130; OS endosymbiont of Riftia pachyptila (vent Ph05). OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=1048808; RN [1] RP NUCLEOTIDE SEQUENCE. RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D., RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., RA Hecker M., Sievert S.M., Schweder T.; RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and RT Tevnia jerichonana share an identical physiology as revealed by RT proteogenomic analyses."; RL ISME J. 0:0-0(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOC01000041; EGV51321.1; -; Genomic_DNA. DR EnsemblBacteria; EGV51321; EGV51321; Rifp1Sym_bn00130. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22943 MW; CD04854AF1EFE461 CRC64; MTRDDRLRGL YAITDPKLGG ELPLPQQVEQ ALQGGARVIQ YRDKGDDPVR RLAEAQTLAG CCHRHNALLL INDDVALALA SGADGVHLGR NDADIEQARA QLGECAIIGV SCYNQLQLAQ QASAAGADYV AFGRFFPSQT KPGAVQAEPL LLRQARHEID LPLVAIGGIT PENGRPLIDA GADMLAVIHA IFGQPDIKTA CQAFQSLFQA EDSPT // ID G2DLG2_9NEIS Unreviewed; 204 AA. AC G2DLG2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=l11_12350; OS Neisseria weaveri LMG 5135. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=1051985; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 5135; RX PubMed=22188430; DOI=10.1111/j.1574-6968.2011.02485.x; RA Yi H., Cho Y.J., Yoon S.H., Park S.C., Chun J.; RT "Comparative genomics of Neisseria weaveri clarifies the taxonomy of RT this species and identifies genetic determinants that may be RT associated with virulence."; RL FEMS Microbiol. Lett. 328:100-105(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWQ01000023; EGV37482.1; -; Genomic_DNA. DR EnsemblBacteria; EGV37482; EGV37482; l11_12350. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22032 MW; 79919F4C03D5BBE0 CRC64; MFFQPLAARL RFYAVVPTAE WVGRMVKAGA DTVQLRNKDL TGEDLYREIE RSVALCQGTA TQLFINDYWQ EAIRAGAYGV HLGQEDMDSA DLQAIADAGL RLGISTHSVA ELDRALSVRP SYVASGAVFP TTTKKMPTEP QGLENLRRYV EQAGETPVVA IGGIDLTNAE AVLATGVSSL AVVRAVTEAE NPEAVVKAFQ SLFD // ID G2DUI9_9NEIS Unreviewed; 180 AA. AC G2DUI9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=l13_18050; OS Neisseria weaveri ATCC 51223. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=1051972; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51223; RX PubMed=22188430; DOI=10.1111/j.1574-6968.2011.02485.x; RA Yi H., Cho Y.J., Yoon S.H., Park S.C., Chun J.; RT "Comparative genomics of Neisseria weaveri clarifies the taxonomy of RT this species and identifies genetic determinants that may be RT associated with virulence."; RL FEMS Microbiol. Lett. 328:100-105(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWR01000039; EGV34946.1; -; Genomic_DNA. DR EnsemblBacteria; EGV34946; EGV34946; l13_18050. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 180 AA; 19224 MW; 5EB33391008678C1 CRC64; MVKAGADTVQ LRNKDLTGED LYREIERSVA LCQGTATQLF INDYWQEAIR AGAYGVHLGQ EDMDSADLQA IADAGLRLGI STHSVAELDR ALSVRPSYVA SGAVFPTTTK KMPTEPQGLE NLRRYVEQAG ETPVVAIGGI DLTNAEAVLA TGVSSLAVVR AVTEAENPEA VVKAFQSLFD // ID G2E011_9GAMM Unreviewed; 310 AA. AC G2E011; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=ThidrDRAFT_1624; OS Thiorhodococcus drewsii AZ1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiorhodococcus. OX NCBI_TaxID=765913; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AZ1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., RA Frigaard N.-U., Bryant D.A., Woyke T.J.; RT "The draft genome of Thiorhodococcus drewsii AZ1."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWT01000009; EGV32050.1; -; Genomic_DNA. DR ProteinModelPortal; G2E011; -. DR EnsemblBacteria; EGV32050; EGV32050; ThidrDRAFT_1624. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 310 AA; 33928 MW; 79FAC7CA4056AE50 CRC64; MAGAIADTDG RILVTRRPDH VHQGGLWEFP GGKLEPGESP EDGLARELDE ELGIRVLDSR PLIRVHHDYG DRYILLEVRR VDDYEGVPRG REGQPLRWLA PEAMDPDLFP AADRPIINAL RLPPLFLITG EDPLDSDAFL ERLEESLARG IRLVQLRAPN LDCERYASLA RRAHALCESQ GARLLLNRDP DAVEDLPRHG LHLTSGRLMR STRRPGRPGE LVGASCHDAG QLAHAARLGL DYALLSPVLH TLTHPEAAPL GWRAFADLVD PVPLPVYALG GLGPGHLGEA IAHGAQGVAA IRGLWSMRGR // ID G2E816_9GAMM Unreviewed; 211 AA. AC G2E816; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ThidrDRAFT_4430; OS Thiorhodococcus drewsii AZ1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiorhodococcus. OX NCBI_TaxID=765913; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AZ1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., RA Frigaard N.-U., Bryant D.A., Woyke T.J.; RT "The draft genome of Thiorhodococcus drewsii AZ1."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWT01000061; EGV27759.1; -; Genomic_DNA. DR EnsemblBacteria; EGV27759; EGV27759; ThidrDRAFT_4430. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21939 MW; BAAB90C172E3F626 CRC64; MNQILDGLYA ITPDASPSAE ALTKQVAQAI EGGARVIQYR DKHSDHTGRE ARASALLALC RASGVALIVN DDLELARKLG ADGVHLGRDD PDPRQARALL GRQAIIGVSC YDDFSRAEAA AEAGASYVAF GSFFPSTTKP NAVAADPGLL TLAREHLPIP PVAIGGITPQ NGGLLISAGA RMLAVVSGVF AQPDIASAAR AYTTLFPKET H // ID G2E9I2_9FLAO Unreviewed; 214 AA. AC G2E9I2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BZARG_193; OS Bizionia argentinensis JUB59. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Bizionia. OX NCBI_TaxID=1046627; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JUB59; RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0; RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M., RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., RA Criscuolo M., Memoli M., Arguelles M., Mac Cormack W.P.; RT "Bizionia argentinensis sp. nov., isolated from surface marine water RT in Antarctica."; RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JUB59; RA Bercovich A.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFXZ01000002; EGV44774.1; -; Genomic_DNA. DR EnsemblBacteria; EGV44774; EGV44774; BZARG_193. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23737 MW; 3F56C08BE77C9AB9 CRC64; MIIPKLHYIS QGNSPKEHLE NIQKACSSGA ELVQLRLKNI SEKKHIKIAL EAREITMHFQ TRLIINDNYK IAKEVKADGV HLGQTDVCPT VARKHLHSWQ MIGGTANTLE DCERLLDKAI DYISLGPFRE TTTKENLPPL LGLKGFMAIT DVLKTPIPII GVGGINTDDV KDILETGISG IAVSGEITRD FNSIKLFNEL LNASSTAEQR HTFE // ID G2EB27_9FLAO Unreviewed; 195 AA. AC G2EB27; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Hydroxymethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase; GN ORFNames=BZARG_710; OS Bizionia argentinensis JUB59. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Bizionia. OX NCBI_TaxID=1046627; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JUB59; RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0; RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M., RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., RA Criscuolo M., Memoli M., Arguelles M., Mac Cormack W.P.; RT "Bizionia argentinensis sp. nov., isolated from surface marine water RT in Antarctica."; RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JUB59; RA Bercovich A.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFXZ01000009; EGV44257.1; -; Genomic_DNA. DR EnsemblBacteria; EGV44257; EGV44257; BZARG_710. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Kinase; Transferase. SQ SEQUENCE 195 AA; 22693 MW; 97B667B49C30097B CRC64; MIVLIAPEKD VPNEIDILNQ LFHEGLQYYH IRKPDKNYQQ HADYLNQIDT KYHNRVVTHN FHELINEYNL KGIHFQEQKR IDHIDNPGRY FKGLNMYGKT ISSSFHEVET IEDCYFEFDY HLLSPVFTSI SKEGYAGRGF DVNHVDKLII GMGGVTTNNL DTIIKLGFKG VGVLGGIWNS ENPVEDFKTM RNHFN // ID G2EB29_9FLAO Unreviewed; 210 AA. AC G2EB29; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BZARG_712; OS Bizionia argentinensis JUB59. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Bizionia. OX NCBI_TaxID=1046627; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JUB59; RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0; RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M., RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., RA Criscuolo M., Memoli M., Arguelles M., Mac Cormack W.P.; RT "Bizionia argentinensis sp. nov., isolated from surface marine water RT in Antarctica."; RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JUB59; RA Bercovich A.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFXZ01000009; EGV44266.1; -; Genomic_DNA. DR EnsemblBacteria; EGV44266; EGV44266; BZARG_712. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22849 MW; CEDEA9AE9311221F CRC64; MIPKLHYISQ GTTIKEHLEN AQAACESGAN LIQLRIKNAS PKDVLKAAEE AREITNHYQT RLIINDYYKI AKQVKADGVH LGKEDAEIAT AKATLFSWQI IGGTANTIED CSILINEKVD YIGLGPYQFT NTKTNLSPVL GYSGYLTIIG ELNTKTPIIA IGGITLNEVP KLLKTGVYGI AVSGEVTRNF KAISTFNNLL EVEGALGKEI // ID G2ELS7_CORGT Unreviewed; 763 AA. AC G2ELS7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE SubName: Full=Multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; DE EC=2.7.4.7; GN ORFNames=CgS9114_07150; OS Corynebacterium glutamicum S9114. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1075088; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S9114; RX PubMed=21994927; DOI=10.1128/JB.06074-11; RA Lv Y., Wu Z., Han S., Lin Y., Zheng S.; RT "Genome Sequence of Corynebacterium glutamicum S9114, a Strain for RT Industrial Production of Glutamate."; RL J. Bacteriol. 193:6096-6097(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFYA01000009; EGV40756.1; -; Genomic_DNA. DR EnsemblBacteria; EGV40756; EGV40756; CgS9114_07150. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.910.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF03070; TENA_THI-4; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; SSF48613; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Transferase. SQ SEQUENCE 763 AA; 80443 MW; D9B1CCACD616001C CRC64; MTDFSLYLVT DPVLGGGPEK VAGIVDSAIS GGVSVVQLRD KNSGVEDVRA AAKELKELCD ARGVALVVND YLDIAVELGL HLHIGQGDTP YTQARELLPA HLELGLSIEN LDQLHAVIAQ CAETGVALPD VIGIGPVAST ATKPDAAPAL GVEGIAEIAA VAQDHGIASV AIGGVGLRNA AELAATPIDG LCVVSEIMTA ANPAAAATRL RTAFQPTFSP ETQTELSQTE LQGAFVNSPS APRVLSIAGT DPTGGAGIQA DLKSIAAGGG YGMCVVTSLV AQNTHGVNTI HTPPLTFLEE QLEAVFSDVT VDAIKLGMLG SADTVDLVAS WLGSHEHGPV VLDPVMIATS GDRLLDASAE ESLRRLAVHV DVVTPNIPEL AVLCDSAPAI TMDEAIAQAQ GFARTHDTIV IVKGGHLTGT LADNAVVRPD GSVFQVENLR VNTTNSHGTG CSLSASLATR IAAGESVEKA LEWSTRWLNE ALRHADHLAV GTGNGPVDHG HLARRMTHAA ETTPWAHLRA PRLDGATAAS FTTPSTVKSP APRIEPAGPF TRALWEASGD IIAGINSSDF ITMLGDGTLR RPEFDFYIDQ DAQYLAQYSR ALARLSSIAP DSHAQIEWAQ SAAECLVVEA ELHRSYMTGK EVSAPSHITM AYTDFLIART YTEDYVCGVA AVLPCYWLYA EIGLMLAEQN HDEHPYKDWL NTYSGEEFIA GTRAAIARLE KALENAGAEQ RVDAARAFLS ASVHEREFFD QATRHGWTMV GSS // ID G2EP11_CORGT Unreviewed; 221 AA. AC G2EP11; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CgS9114_11722; OS Corynebacterium glutamicum S9114. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1075088; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S9114; RX PubMed=21994927; DOI=10.1128/JB.06074-11; RA Lv Y., Wu Z., Han S., Lin Y., Zheng S.; RT "Genome Sequence of Corynebacterium glutamicum S9114, a Strain for RT Industrial Production of Glutamate."; RL J. Bacteriol. 193:6096-6097(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFYA01000016; EGV39852.1; -; Genomic_DNA. DR ProteinModelPortal; G2EP11; -. DR EnsemblBacteria; EGV39852; EGV39852; CgS9114_11722. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). SQ SEQUENCE 221 AA; 23098 MW; 4CEE5D0936EE0FFC CRC64; MFENRFDLRC YVVTGAGSVD EVVHTASAAA RGGAGVVQVR SKPISPEAMR ELASKVALEV ARCSPTTRVL IDDHLHVASS LMREGLPIHG VHLGQDDVSV LEARELLGPE AIIGLTTGTL ELVAAANELS DVLDYIGAGP FRKTPTKDSG RPPIGLAGYP PLVELSKVPI VAIGDVTPAD VRALSATGVA GVAMVRAFSE SDDPQQVAEN VVANFELGRL S // ID G2F8T4_ECOLX Unreviewed; 211 AA. AC G2F8T4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IAM_20039; OS Escherichia coli XH001. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1069495; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XH001; RA Yang H.L., Liao Y.L., Lin Y., Pan L.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFYG01000042; EGV45799.1; -; Genomic_DNA. DR ProteinModelPortal; G2F8T4; -. DR SMR; G2F8T4; 20-202. DR EnsemblBacteria; EGV45799; EGV45799; IAM_20039. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G2FES2_9GAMM Unreviewed; 311 AA. AC G2FES2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=Thiamine monosphosphate synthase TENI/TMP; GN ORFNames=TevJSym_aj00190; OS endosymbiont of Tevnia jerichonana (vent Tica). OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=1049564; RN [1] RP NUCLEOTIDE SEQUENCE. RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D., RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., RA Hecker M., Sievert S.M., Schweder T.; RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and RT Tevnia jerichonana share an identical physiology as revealed by RT proteogenomic analyses."; RL ISME J. 0:0-0(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFZB01000010; EGW54654.1; -; Genomic_DNA. DR ProteinModelPortal; G2FES2; -. DR EnsemblBacteria; EGW54654; EGW54654; TevJSym_aj00190. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 311 AA; 34453 MW; CD1B32AACE40DBF8 CRC64; MTLIHVAAAA IIDSAGRVLI SKRHEHLHQG GLWEFPGGKL EPGESVEAAL RRELYEELGI RISRFEPLIR VTHHYAECSV LLDVYRVFSY QGEPRGMEGQ PLNWVLPEAM EPALFPAADR PIISALQLPS RYLITGEDPT NPEAFCARLE RALKRDCRLL QLRAHGLSDV AYRSLLGEAL ALSQAHGARL LINRPQRSLD WFGVADGVHL NRHQLFELTA RPQAAGLLGA SCHDLQELKQ AERLGLDYAL LSSVLPTATH PEARPLGWAQ FRTLLEQVNI PVYALGGMGM EQLSTAREHG AQGIAAIRGL W // ID G2FGV1_9GAMM Unreviewed; 215 AA. AC G2FGV1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TevJSym_as00130; OS endosymbiont of Tevnia jerichonana (vent Tica). OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=1049564; RN [1] RP NUCLEOTIDE SEQUENCE. RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D., RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., RA Hecker M., Sievert S.M., Schweder T.; RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and RT Tevnia jerichonana share an identical physiology as revealed by RT proteogenomic analyses."; RL ISME J. 0:0-0(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFZB01000019; EGW53920.1; -; Genomic_DNA. DR EnsemblBacteria; EGW53920; EGW53920; TevJSym_as00130. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23001 MW; 620485493EEEFB63 CRC64; MTRDDRLRGL YAITDPKLGG ELPLPQQVEQ ALQGGARVIQ YRDKGDDPVR RLAEAQTLAG CCHRHNALLL INDDVALALA SDADGVHLGR NDADIEQARA QLGECAIIGV SCYNQLQLAQ QASAAGADYV AFGRFFPSQT KPGAVQAEPL LLRQARHEID LPLVAIGGIT PENGRPLIDA GADMLAVIHA IFGQPDIKTA CQAFQSLFQA EDSPT // ID G2FK88_9FIRM Unreviewed; 214 AA. AC G2FK88; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DOT_0098; OS Desulfosporosinus sp. OT. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=913865; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OT; RX PubMed=21994931; DOI=10.1128/JB.06018-11; RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.; RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate- RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern RT Siberia."; RL J. Bacteriol. 193:6104-6105(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAF01000007; EGW41970.1; -; Genomic_DNA. DR EnsemblBacteria; EGW41970; EGW41970; DOT_0098. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22872 MW; AF1C9A408C2695B2 CRC64; MNKAVTKRTL PAGIYALTSE PHSLGRSNLE VAGEILAAGV PILQYREKNK KVRVMYEECL VLRAMTHQAG ALFIINDHLD LALAVSADGV HIGQDDLPLS KVRELVGPNL LIGVSTHSPA QAQAAVKDGA DYIGVGPIFA TQTKVDVCDP VGLDYLDYVV KNLEIPFVAI GGIKEHNLAA IVKAGARTIA LVSEIVGNPD IPDKIKSLQR ILRA // ID G2FS57_9FIRM Unreviewed; 192 AA. AC G2FS57; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DOT_2533; OS Desulfosporosinus sp. OT. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=913865; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OT; RX PubMed=21994931; DOI=10.1128/JB.06018-11; RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.; RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate- RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern RT Siberia."; RL J. Bacteriol. 193:6104-6105(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAF01000120; EGW39480.1; -; Genomic_DNA. DR EnsemblBacteria; EGW39480; EGW39480; DOT_2533. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 23 27 HMP-PP binding (By similarity). FT REGION 120 122 THZ-P binding (By similarity). FT REGION 170 171 THZ-P binding (By similarity). FT METAL 56 56 Magnesium (By similarity). FT METAL 75 75 Magnesium (By similarity). FT BINDING 55 55 HMP-PP (By similarity). FT BINDING 94 94 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 150 150 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 192 AA; 20540 MW; 4C49AB887FE59E57 CRC64; MLHERDLGQS IELAIQGGVT LVQLREKSVS TREFLQLAIR VKEITSHHRI PLIINDRLDI ALAVDADGLH VGQDDLPLPK ARELLGPRKI IGVSASTLAE ALLAQQQGAD YLGVGAIFST STKTDASEVS LEQLEIIKKS VTIPVVAIGG INEMNIKQVL ATGIDGVSVV SAILAKTDIL TAAKKLQELI RS // ID G2FSD3_9FIRM Unreviewed; 216 AA. AC G2FSD3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DOT_2609; OS Desulfosporosinus sp. OT. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=913865; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OT; RX PubMed=21994931; DOI=10.1128/JB.06018-11; RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.; RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate- RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern RT Siberia."; RL J. Bacteriol. 193:6104-6105(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAF01000121; EGW39452.1; -; Genomic_DNA. DR EnsemblBacteria; EGW39452; EGW39452; DOT_2609. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23259 MW; EE7E3A226F9471BC CRC64; MHKPAKKRTL PAGLYALTSE PHSLGRSNIE VAGEILTSGV PILQYREKSK KVRVMYEECL MLRAMTQQAG ALFIINDYLD LALAVGADGV HIGQDDLPLS KVRELVGPDL LIGVSTHSPA QAHQAVKDGA DYIGVGPLFA TQTKIDVCDP VGLDYLNYVV KNLKIPFVAI GGIKEHNLAE VVKSGAQTIA LVTEIVGNPD IPGKIKSLQR IMQTLT // ID G2G7Z5_9ACTO Unreviewed; 225 AA. AC G2G7Z5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-MAR-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SZN_08044; OS Streptomyces zinciresistens K42. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=700597; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K42; RA Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGBF01000015; EGX60428.1; -; Genomic_DNA. DR EnsemblBacteria; EGX60428; EGX60428; SZN_08044. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 53 57 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 23452 MW; CE25E376F0AC0B80 CRC64; MTDTSVADTS VADTARSRLD GARLYLCTGA RRERGDLAEF LDAVLAAGVD IVQLRDKGME AAEELDHLRT FAEACARHGR LLAVNDRADV AHAAGAGVLH LGQGDLPVPA ARAILGDDVL IGRSTHSAAE ASAAAVQDGV DYFCTGPCWP TPTKPGRHAP GLDLVRHTAA LGTDRPWFAI GGIDLGNLDQ VLDAGARRVV VVRAITDAPD PGAAAAELAK RLRQA // ID G2H568_9DELT Unreviewed; 217 AA. AC G2H568; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DA2_0887; OS Desulfovibrio sp. A2. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=298701; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A2; RX PubMed=22072648; DOI=10.1128/JB.06019-11; RA Mancini S., Abicht H.K., Karnachuk O.V., Solioz M.; RT "Genome Sequence of Desulfovibrio sp. A2, a Highly Copper Resistant, RT Sulfate-Reducing Bacterium Isolated from Effluents of a Zinc Smelter RT at the Urals."; RL J. Bacteriol. 193:6793-6794(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGFG01000019; EGY26988.1; -; Genomic_DNA. DR EnsemblBacteria; EGY26988; EGY26988; DA2_0887. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23161 MW; A9D1CDBE72FA7057 CRC64; MPRILPGSTP EADIYCLTDD GLSRGRSAVD VVDAMLRGGA RIVQYREKDK HAGEMLRECM ELRRMTHEAG ACFIVNDHVD IAMLCDADGV HVGQEDLPVQ AVRQLVGPGR IIGLSTHSPE QARAAVESGA DYIGVGPIFA TRTKKDVCAP VGFEYLDWVV ANIDLPFVAI GGIKLHNIGQ VAAHGARCCA LVSEIVGADD VAARFAVARA AMRTARG // ID G2HCP6_9DELT Unreviewed; 216 AA. AC G2HCP6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DA2_3540; OS Desulfovibrio sp. A2. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=298701; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A2; RX PubMed=22072648; DOI=10.1128/JB.06019-11; RA Mancini S., Abicht H.K., Karnachuk O.V., Solioz M.; RT "Genome Sequence of Desulfovibrio sp. A2, a Highly Copper Resistant, RT Sulfate-Reducing Bacterium Isolated from Effluents of a Zinc Smelter RT at the Urals."; RL J. Bacteriol. 193:6793-6794(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGFG01000064; EGY24239.1; -; Genomic_DNA. DR EnsemblBacteria; EGY24239; EGY24239; DA2_3540. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22554 MW; E3A5914B4B47DB31 CRC64; MITAHRYMDY GVYLVTDRTL CRGRALADVV AAAVAGGVTV VQLREKHADT REFVELARAL KALLAPRGVP LLINDRVDVA LACRADGVHV GQGDMHPAEV RALLGHAALV GLSVETMDQV REAETLDVDY LGVSPVFATP TKTDTASPWG LDGLARLRAA TGRTLVAIGG IGAANAASVL AAGADGLAVV SALCAADDPE RAAAELRRVV RTVRGW // ID G2HLB6_9PROT Unreviewed; 203 AA. AC G2HLB6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=ABED_0422; OS Arcobacter butzleri ED-1. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=944546; RN [1] RP NUCLEOTIDE SEQUENCE. RA Toh H., Sharma V.K., Oshima K., Kondo S., Hattori M., Ward F.B., RA Free A., Taylor T.D.; RT "Complete Genome Sequences of Arcobacter butzleri ED-1 and Arcobacter RT sp. Strain L, Both Isolated from a Microbial Fuel Cell."; RL J. Bacteriol. 193:6411-6412(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012047; BAK70139.1; -; Genomic_DNA. DR RefSeq; YP_005537949.1; NC_017187.1. DR EnsemblBacteria; BAK70139; BAK70139; ABED_0422. DR GeneID; 12128967; -. DR KEGG; abt:ABED_0422; -. DR KO; K00788; -. DR BioCyc; ABUT944546:GL87-430-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 203 AA; 23110 MW; E2BC327A7ABCA0EE CRC64; MISNLEKALG FKLEAFNYLY VLCDYETLLK KNISLETFVD LCRKKDVKII QYRDKISSLE EQKINLLYLK LQLNIPIIVN DKIELIDFAD GLHLGQEDLE KIHKDKNLAI KLVRTKIKDK LLGLSTHNEI EILEANELNL DMIGLGAYKQ TNTKDVSSIL GEKISYLAKI SKHPVCAIGG VKIEDKILNI KFNVVGSGFF DEN // ID G2HQD2_9PROT Unreviewed; 184 AA. AC G2HQD2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=ABED_1838; OS Arcobacter butzleri ED-1. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=944546; RN [1] RP NUCLEOTIDE SEQUENCE. RA Toh H., Sharma V.K., Oshima K., Kondo S., Hattori M., Ward F.B., RA Free A., Taylor T.D.; RT "Complete Genome Sequences of Arcobacter butzleri ED-1 and Arcobacter RT sp. Strain L, Both Isolated from a Microbial Fuel Cell."; RL J. Bacteriol. 193:6411-6412(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012047; BAK71555.1; -; Genomic_DNA. DR RefSeq; YP_005539365.1; NC_017187.1. DR EnsemblBacteria; BAK71555; BAK71555; ABED_1838. DR GeneID; 12127563; -. DR KEGG; abt:ABED_1838; -. DR KO; K00788; -. DR BioCyc; ABUT944546:GL87-1898-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 184 AA; 21255 MW; 0D2A0B55EAB47564 CRC64; MKKYLITDPK YYTNDKLTFK QTLSKAFEKH KVDFACFRDK ESNNFEALAK TFIETCHEKN IENTFLNSDF FLAQKLGFYG VHLTSTQFED IKKAKELNLK IIISSHNTKD IETARKYGAD YITYSPIFDT PNKGKAKGIK DLELVLNSFK DMKIIALGGI IDENQISKIE NTKVFGFASI RYFI // ID G2HTL5_9PROT Unreviewed; 202 AA. AC G2HTL5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=ABLL_0593; OS Arcobacter sp. L. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=944547; RN [1] RP NUCLEOTIDE SEQUENCE. RA Toh H., Sharma V.K., Oshima K., Kondo S., Hattori M., Ward F.B., RA Free A., Taylor T.D.; RT "Complete Genome Sequences of Arcobacter butzleri ED-1 and Arcobacter RT sp. Strain L, Both Isolated from a Microbial Fuel Cell."; RL J. Bacteriol. 193:6411-6412(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012048; BAK72468.1; -; Genomic_DNA. DR RefSeq; YP_005552785.1; NC_017192.1. DR EnsemblBacteria; BAK72468; BAK72468; ABLL_0593. DR GeneID; 12195854; -. DR KEGG; arc:ABLL_0593; -. DR KO; K00788; -. DR BioCyc; ASP944547:GL86-601-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 23004 MW; 8B45C3A039801022 CRC64; MISNLEKALG FELKAFNYLY VLCDYETLLK KNITLDKFID LCKKKDVKLV QYRDKISSLE EQKTNLLYLK SKLNIPIIIN DKIELIKYAD GLHLGQEDFL AIHRDKKIAI KLVRAKIKDK LLGLSTHNEI EILEANELPL DMIGLGAYKN TTTKDVSTIL GDKISYLAKI SKHPVCAIGG VQINDKIPNI RFNVIGSGFY YE // ID G2HZE8_9PROT Unreviewed; 184 AA. AC G2HZE8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=ABLL_2522; OS Arcobacter sp. L. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=944547; RN [1] RP NUCLEOTIDE SEQUENCE. RA Toh H., Sharma V.K., Oshima K., Kondo S., Hattori M., Ward F.B., RA Free A., Taylor T.D.; RT "Complete Genome Sequences of Arcobacter butzleri ED-1 and Arcobacter RT sp. Strain L, Both Isolated from a Microbial Fuel Cell."; RL J. Bacteriol. 193:6411-6412(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012048; BAK74397.1; -; Genomic_DNA. DR RefSeq; YP_005554714.1; NC_017192.1. DR EnsemblBacteria; BAK74397; BAK74397; ABLL_2522. DR GeneID; 12196175; -. DR KEGG; arc:ABLL_2522; -. DR KO; K00788; -. DR BioCyc; ASP944547:GL86-2585-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 184 AA; 21150 MW; AD9E3F6C978992D5 CRC64; MKKYLITDPQ YYSNDIKIFR KTLIKALTKH KIDIACFRDK ESKNFEELAK IFIEICKKFN VKEILLNSNY LLAKKLGASG VHLNSKQFDK IKEAKEKNLF TIISCHTFLE IEEAMKLKAD AITFSPIFNT PNKGEPKGIE KLEEATNLYK DIKIIALGGI VSKEQISKIE NTKAYGFASI RYFV // ID G2I0P7_GLUMN Unreviewed; 211 AA. AC G2I0P7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GLX_20930; OS Gluconacetobacter medellinensis (strain NBRC 3288 / BCRC 11682 / LMG OS 1693 / Kondo 51). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Komagataeibacter. OX NCBI_TaxID=634177; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 3288 / BCRC 11682 / LMG 1693; RX PubMed=22123756; DOI=10.1128/JB.06158-11; RA Ogino H., Azuma Y., Hosoyama A., Nakazawa H., Matsutani M., RA Hasegawa A., Otsuyama K., Matsushita K., Fujita N., Shirai M.; RT "Complete genome sequence of NBRC 3288, a unique cellulose- RT nonproducing strain of Gluconacetobacter xylinus isolated from RT vinegar."; RL J. Bacteriol. 193:6997-6998(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012159; BAK84505.1; -; Genomic_DNA. DR RefSeq; YP_004868875.1; NC_016027.1. DR EnsemblBacteria; BAK84505; BAK84505; GLX_20930. DR GeneID; 11163687; -. DR KEGG; gxy:GLX_20930; -. DR KO; K00788; -. DR BioCyc; GXYL634177:GHBT-2147-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21824 MW; 217417A1242F8C5D CRC64; MNDCQLYLIT PESLDPAAFA PCLAEALDAG PVAAVQLRLK NVPDDTIHRA VDVLQPVAHA RNVAFILNDR PDLAVACGCD GAHVGMDDGD VATARRILGA DLQLGVSCYD SRDMALRAGE AGADYVAFGA FFPSPSKETE VRADPALLTW WSSMIELPVV AIGGITPANC GALVRAGADF LSVISAVWSH PDGPGAGVQA MNAAIAAAED A // ID G2I1K1_GLUMN Unreviewed; 206 AA. AC G2I1K1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 18. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN OrderedLocusNames=GLX_00110; OS Gluconacetobacter medellinensis (strain NBRC 3288 / BCRC 11682 / LMG OS 1693 / Kondo 51). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Komagataeibacter. OX NCBI_TaxID=634177; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 3288 / BCRC 11682 / LMG 1693; RX PubMed=22123756; DOI=10.1128/JB.06158-11; RA Ogino H., Azuma Y., Hosoyama A., Nakazawa H., Matsutani M., RA Hasegawa A., Otsuyama K., Matsushita K., Fujita N., Shirai M.; RT "Complete genome sequence of NBRC 3288, a unique cellulose- RT nonproducing strain of Gluconacetobacter xylinus isolated from RT vinegar."; RL J. Bacteriol. 193:6997-6998(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012159; BAK82423.1; -; Genomic_DNA. DR RefSeq; YP_004866793.1; NC_016027.1. DR EnsemblBacteria; BAK82423; BAK82423; GLX_00110. DR GeneID; 11164475; -. DR KEGG; gxy:GLX_00110; -. DR KO; K00788; -. DR BioCyc; GXYL634177:GHBT-11-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22232 MW; CEAA7072264BD7CF CRC64; MSAPLPSRIY PVVDSAQWVA RLGQAGARLI QLRLKDRTAD ALRHEIREGI RHARAHGVTL VLNDYWQAAI EEGMDYIHLG QEDLDTADLS AIRAAGIRLG VSTHDEHELE RALSVAPDYV ALGPVWPTTL KKMPWAPQGT ARLTVWKQRI GAIPLVAIGG VTLARAPLCL AAGADCVSAV SDFIRMPDPA AQVRAWLEAT AGPATV // ID G2II81_9SPHN Unreviewed; 208 AA. AC G2II81; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SLG_23290; OS Sphingobium sp. SYK-6. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=627192; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SYK-6; RA Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S., RA Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., RA Katano Y., Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., RA Fukuda M., Yamazaki S., Fujita N.; RT "Complete Genome Sequence of Sphingobium sp. Strain SYK-6, a Degrader RT of Lignin-Derived Biaryls and Monoaryls."; RL J. Bacteriol. 194:534-535(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012222; BAK67004.1; -; Genomic_DNA. DR RefSeq; YP_004835461.1; NC_015976.1. DR EnsemblBacteria; BAK67004; BAK67004; SLG_23290. DR GeneID; 11142404; -. DR KEGG; ssy:SLG_23290; -. DR KO; K00788; -. DR BioCyc; SSP627192:GI2Q-2366-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21745 MW; 296B3A462ACCC959 CRC64; MTHMPSCQLY LISPPAIGPD FPAQLKAALD GGPVAAFQLR LKGIDEHEIA RLAAPLQALC AEREVAFIVN DSVALAKRLG ADGVHLGQGD GDPAEARRIL GPGPQIGVTC HDSRHLAMEA GEAGADYVAF GAFYPTETKE TSHRPEPDIL RWWSSLFELP CVAIGGITPE NARPLVEAGA DFLAVSGAVW NHPDGPGAGV AAFAPVLG // ID G2IR78_9SPHN Unreviewed; 195 AA. AC G2IR78; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=SLG_37690; OS Sphingobium sp. SYK-6. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=627192; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SYK-6; RA Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S., RA Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., RA Katano Y., Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., RA Fukuda M., Yamazaki S., Fujita N.; RT "Complete Genome Sequence of Sphingobium sp. Strain SYK-6, a Degrader RT of Lignin-Derived Biaryls and Monoaryls."; RL J. Bacteriol. 194:534-535(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012222; BAK68444.1; -; Genomic_DNA. DR RefSeq; YP_004836901.1; NC_015976.1. DR EnsemblBacteria; BAK68444; BAK68444; SLG_37690. DR GeneID; 11145472; -. DR KEGG; ssy:SLG_37690; -. DR KO; K00788; -. DR BioCyc; SSP627192:GI2Q-3825-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 195 AA; 21190 MW; 72B62A1274ACF58D CRC64; MRQGHGKSRG DVPAIWLMTD ERLSEAQLLR AVARLPRGSA VVLRHHATAQ TARLALFDRL RTLTLRRGCR LLVAGNPAVA RALGADGHHG RVKPSRFSTG RERPWLHSAP VHDQRELRAA VRAGADAVLI SPLFATRSHP DARPLGAVRF AALARYSPVP VIALGGVRPH HAALVRRLGA HGFAAIDGLS GYRRR // ID G2IY64_PSEUL Unreviewed; 313 AA. AC G2IY64; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 13-NOV-2013, entry version 17. DE SubName: Full=Thiamine-monophosphate synthase; GN OrderedLocusNames=NH8B_0789; OS Pseudogulbenkiania sp. (strain NH8B). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Pseudogulbenkiania. OX NCBI_TaxID=748280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NH8B; RX PubMed=22038961; DOI=10.1128/JB.06127-11; RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.; RT "Complete genome sequence of the denitrifying and N(2)O-reducing RT bacterium Pseudogulbenkiania sp. strain NH8B."; RL J. Bacteriol. 193:6395-6396(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012224; BAK75621.1; -; Genomic_DNA. DR RefSeq; YP_004846035.1; NC_016002.1. DR ProteinModelPortal; G2IY64; -. DR EnsemblBacteria; BAK75621; BAK75621; NH8B_0789. DR GeneID; 11158084; -. DR KEGG; pse:NH8B_0789; -. DR KO; K03574; -. DR BioCyc; PSP748280:GHJ9-789-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 313 AA; 33653 MW; FD0B87D8B99E5A9D CRC64; MQSDHKIIPV VAGALMRPDG SFMLGSRPEG KPYAGYWEFP GGKVEPGEAP FAALVREFQE EMGITVTHAT PWLTKVHHYE HASVHLTFYR IWAWDGTPQP HEEQAFAWQQ PGHYTVGPML PANGPILKSL ELPDVYAISC AHEIGVEAFL EALEARPELT LIQLREPQLG RDELAALAER VVAIVHPRGG KVVVNADPAW LAGWPVDGVH LNGKRLAEAT ARPAFAWVGA SVHSTAELNQ AAELGLDYAL LGHVKATASH PGAAPLGWDG FECRLAGGTP LPVYALGGLS AADLSDARAH GAHGVALMRG AWR // ID G2J282_PSEUL Unreviewed; 205 AA. AC G2J282; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NH8B_4028; OS Pseudogulbenkiania sp. (strain NH8B). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Pseudogulbenkiania. OX NCBI_TaxID=748280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NH8B; RX PubMed=22038961; DOI=10.1128/JB.06127-11; RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.; RT "Complete genome sequence of the denitrifying and N(2)O-reducing RT bacterium Pseudogulbenkiania sp. strain NH8B."; RL J. Bacteriol. 193:6395-6396(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012224; BAK78765.1; -; Genomic_DNA. DR RefSeq; YP_004849179.1; NC_016002.1. DR EnsemblBacteria; BAK78765; BAK78765; NH8B_4028. DR GeneID; 11156139; -. DR KEGG; pse:NH8B_4028; -. DR KO; K00788; -. DR BioCyc; PSP748280:GHJ9-4025-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21126 MW; D07772295B44D639 CRC64; MATLEGLYAI TPDTDDSERL IELVSDVLPH GVRLLQYRNK SQDPVRRLWQ ANLLASLCHS HGVTFIVNDD VELALAVGAD GVHLGRDDAA IAAARARLGA DAIIGASCYD DIKLAEAAVA AGASYVAFGA VFPSGTKPHA VRAPLQLFAQ AKRLGVPSAA IGGITADNAG EVVSAGADML AVIGALFDAA DPAATAEQLA AAFRR // ID G2J2Z2_PSEUL Unreviewed; 213 AA. AC G2J2Z2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NH8B_1620; OS Pseudogulbenkiania sp. (strain NH8B). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Pseudogulbenkiania. OX NCBI_TaxID=748280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NH8B; RX PubMed=22038961; DOI=10.1128/JB.06127-11; RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.; RT "Complete genome sequence of the denitrifying and N(2)O-reducing RT bacterium Pseudogulbenkiania sp. strain NH8B."; RL J. Bacteriol. 193:6395-6396(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012224; BAK76437.1; -; Genomic_DNA. DR RefSeq; YP_004846851.1; NC_016002.1. DR EnsemblBacteria; BAK76437; BAK76437; NH8B_1620. DR GeneID; 11154809; -. DR KEGG; pse:NH8B_1620; -. DR KO; K00788; -. DR BioCyc; PSP748280:GHJ9-1619-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22091 MW; 8677953652CD3151 CRC64; MNNATQRPTR PVWLDGLYAV TPDTSDSAWL LPRVAAVLAG GASLVQYRNK SRDTALRREQ AAAIRALCRQ HGAWFLVNDD VGLAEEVGAD GVHLGRGDTS LCAARQRLGP HAIIGATCHD QPALAVQAVG NGASYVAFGA LFPSRSKPEA VSAPLALFAA LPPLEVPCVA IGGITPTNAA LAWQTGVDML AIIGGLFDAP APDEAARAIL AAR // ID G2JK76_ACIBA Unreviewed; 203 AA. AC G2JK76; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ABZJ_02920; OS Acinetobacter baumannii MDR-ZJ06. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=497978; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MDR-ZJ06; RX PubMed=21788470; DOI=10.1128/AAC.01134-10; RA Zhou H., Zhang T., Yu D., Pi B., Yang Q., Zhou J., Hu S., Yu Y.; RT "Genomic Analysis of the Multidrug-Resistant Acinetobacter baumannii RT Strain MDR-ZJ06 Widely Spread in China."; RL Antimicrob. Agents Chemother. 55:4506-4512(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001937; AEP07380.1; -; Genomic_DNA. DR RefSeq; YP_005526876.1; NC_017171.1. DR ProteinModelPortal; G2JK76; -. DR EnsemblBacteria; AEP07380; AEP07380; ABZJ_02920. DR GeneID; 12117393; -. DR KEGG; abz:ABZJ_02920; -. DR KO; K00788; -. DR BioCyc; ABAU497978:GL7S-2968-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21778 MW; F47FCEF0DAC9A9AE CRC64; MRGLYLITND DPIQLLLEKL DAALATRQIA ILQYRRKKID KAEQPAEVEQ IKQLCEKYQV PFVINDDLKL AAQFGLGVHL GQSDGEITDA KSQLPEGVII GRTCLNSLEL AQKAIADGAT YVAFGAVYAT ATKPEAGNVG IEVIKQAAAQ YDLPICAIGG LTVENSKPVI EAGADLCAVI SDILGRSTAE IPARVQAWAQ LFS // ID G2JLY2_ACIBA Unreviewed; 303 AA. AC G2JLY2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Putative bifunctional protein; GN ORFNames=ABZJ_02676; OS Acinetobacter baumannii MDR-ZJ06. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=497978; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MDR-ZJ06; RX PubMed=21788470; DOI=10.1128/AAC.01134-10; RA Zhou H., Zhang T., Yu D., Pi B., Yang Q., Zhou J., Hu S., Yu Y.; RT "Genomic Analysis of the Multidrug-Resistant Acinetobacter baumannii RT Strain MDR-ZJ06 Widely Spread in China."; RL Antimicrob. Agents Chemother. 55:4506-4512(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001937; AEP07136.1; -; Genomic_DNA. DR RefSeq; YP_005526632.1; NC_017171.1. DR EnsemblBacteria; AEP07136; AEP07136; ABZJ_02676. DR GeneID; 12117146; -. DR KEGG; abz:ABZJ_02676; -. DR KO; K03574; -. DR BioCyc; ABAU497978:GL7S-2721-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 303 AA; 34706 MW; ED79473D22D8710D CRC64; MSRKMPKPIV DVAIAILIHR GKILVGWRGE QQHQGGKHEF PGGKVEQGET PEEACRREIY EEVGIGLKDW HQFDYIHHEY DDIIVNLHLF HSYVPDELLN LIHQPWTWYT REQLLHLNFP KANKDIIKRL YWPHFIKISH TLTSVENSDA LLYWRIEDEF GPREVEQLTA LDEGQRSNLI INVDIWQQLN PELKKQIKTV HLKQSQLMSL HKGDLEVGVR FIAACHDAVS LQHAQQIGCD AVFVSPVKVT ATHPDVSALG WDRFADLIEK CQIPVFALGG MSPDDLATAQ QHGAYGLAGI RNF // ID G2JRS7_LISMN Unreviewed; 214 AA. AC G2JRS7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMOG_02513; OS Listeria monocytogenes J0161. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393130; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J0161; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease.; RA Borowsky M., Borodovsky M., Young S.K., Zeng Q., Koehrsen M., RA Fitzgerald M., Wiedmann M., Swaminathan B., Lauer P., Portnoy D., RA Cossart P., Buchrieser C., Higgins D., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Borenstein D., Brown A., Chapman S.B., RA Chen Z., Dunbar C.D., Engels R., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., RA Jen D., Larson L., Lui A., MacDonald J., Mehta T., Montmayeur A., RA Neiman D., Park D., Pearson M., Priest M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Listeria monocytogenes strain J0161."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002001; AEO02389.1; -; Genomic_DNA. DR RefSeq; YP_005964289.1; NC_017545.1. DR ProteinModelPortal; G2JRS7; -. DR EnsemblBacteria; AEO02389; AEO02389; LMOG_02513. DR GeneID; 12555458; -. DR KEGG; lmj:LMOG_02513; -. DR KO; K00788; -. DR BioCyc; LMON393130:GLFV-330-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22392 MW; 67844F688FC140A4 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALKCQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAA EAELLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GITIPIVGIG GINETNLAEV LTAGADGVSV ISAITQSDDC HSVIKQLKNP GSPS // ID G2K354_LISM4 Unreviewed; 214 AA. AC G2K354; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LMRG_00011; OS Listeria monocytogenes serotype 1/2a (strain 10403S). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393133; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=10403S; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease.; RA Borowsky M., Borodovsky M., Young S.K., Zeng Q., Koehrsen M., RA Fitzgerald M., Wiedmann M., Swaminathan B., Lauer P., Portnoy D., RA Cossart P., Buchrieser C., Higgins D., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Borenstein D., Brown A., Chapman S.B., RA Chen Z., Dunbar C.D., Engels R., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., RA Jen D., Larson L., Lui A., MacDonald J., Mehta T., Montmayeur A., RA Neiman D., Park D., Pearson M., Priest M., Richards J., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Listeria monocytogenes strain 10403S."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002002; AEO05332.1; -; Genomic_DNA. DR RefSeq; YP_005961463.1; NC_017544.1. DR ProteinModelPortal; G2K354; -. DR EnsemblBacteria; AEO05332; AEO05332; LMRG_00011. DR GeneID; 12552548; -. DR KEGG; lmt:LMRG_00011; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22406 MW; 0651E7AEFECF8C06 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALEFQ KLCAKYQVPF IINDDVALAL EIGADGIHVG QTDEAIRQVI ASCSGKMKIG LSVHSVSEAK EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEICRA GITIPIVGIG GINETNSAEV LAAGADGVSV ISAITRSEDC QSVIKQLKNP GSPS // ID G2KBX0_LISMN Unreviewed; 214 AA. AC G2KBX0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMKG_01599; OS Listeria monocytogenes FSL R2-561. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393126; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL R2-561; RA Borowsky M., Young S.K., Zeng Q., Koehrsen M., Fitzgerald M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Borodovsky M., Wiedmann M., RA Swaminathan B., Lauer P., Portnoy D., Cossart P., Buchrieser C., RA Higgins D., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Listeria monocytogenes strain FSL R2-561."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002003; AEO24618.1; -; Genomic_DNA. DR RefSeq; YP_005967238.1; NC_017546.1. DR ProteinModelPortal; G2KBX0; -. DR EnsemblBacteria; AEO24618; AEO24618; LMKG_01599. DR GeneID; 12558507; -. DR KEGG; lmg:LMKG_01599; -. DR KO; K00788; -. DR BioCyc; LMON393126:GLFU-333-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22398 MW; CD29EC73FEF09751 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK GGITCFQYRE KGAGSLQTAS ERKEMALECQ KLCAKYQVPF IINDDVALAL EIGADGIHVG QTDEAIRQVI ASCSGKMKIG LSVHSVSEAK EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GITIPIVGIG GINETNSAEV LTAGADGVSV ISAITQSDDC HSVIKQLKNP GSPS // ID G2KGF5_LISMN Unreviewed; 214 AA. AC G2KGF5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMLG_0732; OS Listeria monocytogenes Finland 1998. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393127; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Finland 1988; RA Borowsky M., Young S.K., Zeng Q., Koehrsen M., Fitzgerald M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Borodovsky M., Wiedmann M., RA Swaminathan B., Lauer P., Portnoy D., Cossart P., Buchrieser C., RA Higgins D., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Listeria monocytogenes strain Finland 1998."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002004; AEO37872.1; -; Genomic_DNA. DR RefSeq; YP_005970154.1; NC_017547.1. DR ProteinModelPortal; G2KGF5; -. DR EnsemblBacteria; AEO37872; AEO37872; LMLG_0732. DR GeneID; 12563716; -. DR KEGG; lms:LMLG_0732; -. DR KO; K00788; -. DR BioCyc; LMON393127:GLFT-339-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22469 MW; 347B29E27644DDA9 CRC64; MRAELAVYFI AGTQDIVRGT LLGVLEEALK AGITCFQYRE KGAGSLQTTS ERKEMALKCR QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAA EAEQLGEVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GITIPIVGIG GINETNSAEV LAAGSDGVSV ISAITQSDDC HSVIKQLKNP GSPS // ID G2L8K0_PSEAI Unreviewed; 315 AA. AC G2L8K0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-APR-2014, entry version 19. DE SubName: Full=Uncharacterized protein; GN ORFNames=PAM18_4491; OS Pseudomonas aeruginosa M18. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=941193; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M18; RX PubMed=21884571; DOI=10.1186/1471-2164-12-438; RA Wu D.Q., Ye J., Ou H.Y., Wei X., Huang X., He Y.W., Xu Y.; RT "Genomic analysis and temperature-dependent transcriptome profiles of RT the rhizosphere originating strain Pseudomonas aeruginosa M18."; RL BMC Genomics 12:438-438(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002496; AEO76972.1; -; Genomic_DNA. DR RefSeq; YP_005977074.1; NC_017548.1. DR ProteinModelPortal; G2L8K0; -. DR EnsemblBacteria; AEO76972; AEO76972; PAM18_4491. DR GeneID; 12568558; -. DR KEGG; paf:PAM18_4491; -. DR KO; K03574; -. DR BioCyc; PAER941193:GLIQ-4540-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34085 MW; F3F27D67D096A02B CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EDGEPVRAAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEAHGAEGQ PLAWVEPREL ADYEFPAANA PIVQAARLPA HYLITPDGLE PGELISGVRK AVEAGIRLIQ LRTPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDAEELAL AASMGVEFVT LSPVQPTESH PGEPALGWDK AAELIAGFNQ PVYLLGGLGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID G2LBJ5_PSEAI Unreviewed; 209 AA. AC G2LBJ5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PAM18_0963; OS Pseudomonas aeruginosa M18. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=941193; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M18; RX PubMed=21884571; DOI=10.1186/1471-2164-12-438; RA Wu D.Q., Ye J., Ou H.Y., Wei X., Huang X., He Y.W., Xu Y.; RT "Genomic analysis and temperature-dependent transcriptome profiles of RT the rhizosphere originating strain Pseudomonas aeruginosa M18."; RL BMC Genomics 12:438-438(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002496; AEO73450.1; -; Genomic_DNA. DR RefSeq; YP_005973552.1; NC_017548.1. DR ProteinModelPortal; G2LBJ5; -. DR SMR; G2LBJ5; 24-200. DR EnsemblBacteria; AEO73450; AEO73450; PAM18_0963. DR GeneID; 12564991; -. DR KEGG; paf:PAM18_0963; -. DR KO; K00788; -. DR BioCyc; PAER941193:GLIQ-973-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22146 MW; 898DA261D0AFA265 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER HGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAQ LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID G2LHM9_CHLTF Unreviewed; 202 AA. AC G2LHM9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 16. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN OrderedLocusNames=Cabther_A1948; OS Chloracidobacterium thermophilum (strain B). OC Bacteria; Acidobacteria; Candidatus Chloracidobacterium. OX NCBI_TaxID=981222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B; RX PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x; RA Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M., RA Bryant D.A.; RT "Complete genome of Candidatus Chloracidobacterium thermophilum, a RT chlorophyll-based photoheterotroph belonging to the phylum RT Acidobacteria."; RL Environ. Microbiol. 14:177-190(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002514; AEP12693.1; -; Genomic_DNA. DR RefSeq; YP_004863209.1; NC_016024.1. DR EnsemblBacteria; AEP12693; AEP12693; Cabther_A1948. DR GeneID; 11169560; -. DR KEGG; ctm:Cabther_A1948; -. DR KO; K00788; -. DR OMA; FGPPQGL; -. DR BioCyc; CTHE981222:GHDQ-1948-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 202 AA; 21802 MW; 5AF9B66B4D1D06B0 CRC64; MQRYLITDRR RLFREGEPYT EAIAVRRLVA LARFAAREGI DYLQLREKDW PVRQLTEVAA AMAAALAETR TRLLVNDRFD VALAARAHGV HLTTQSLPAR VVRQCVPSGF LIAVSTHSRC EIAEAEGFAD FAVCGPVFPS GDKPVLGLEA FAELARTTSL PLFALGGIGP DQAAHVRQAG AAGIAAIRAF ANDFLASSSP DT // ID G2LI65_CHLTF Unreviewed; 212 AA. AC G2LI65; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cabther_A0766; OS Chloracidobacterium thermophilum (strain B). OC Bacteria; Acidobacteria; Candidatus Chloracidobacterium. OX NCBI_TaxID=981222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B; RX PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x; RA Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M., RA Bryant D.A.; RT "Complete genome of Candidatus Chloracidobacterium thermophilum, a RT chlorophyll-based photoheterotroph belonging to the phylum RT Acidobacteria."; RL Environ. Microbiol. 14:177-190(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002514; AEP11523.1; -; Genomic_DNA. DR RefSeq; YP_004862039.1; NC_016024.1. DR EnsemblBacteria; AEP11523; AEP11523; Cabther_A0766. DR GeneID; 11170172; -. DR KEGG; ctm:Cabther_A0766; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; CTHE981222:GHDQ-766-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22058 MW; 3FAA17A963145C51 CRC64; MKMNAVLSWT LPPVYPITSP QVGLSLRTVV EALIAGGATM VQIRDKQAAA RTLYEAVCAV MELARPRGVR VIVNDRVDVA RAAAADGVHL GQDDLDPVAA RAILGPTAII GYSTHNVAQA RAADRLPVDY LAIGPVFETQ TKEQPDPVVG LEGVRAVRAV TTKPLVAIGG ITADRIAPVR AAGADAVALI SALYTGPDDI AGRMAALLAL AR // ID G2LS87_9XANT Unreviewed; 212 AA. AC G2LS87; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=XACM_3303; OS Xanthomonas axonopodis pv. citrumelo F1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=981368; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F1; RX PubMed=21908674; DOI=10.1128/JB.05777-11; RA Jalan N., Aritua V., Kumar D., Yu F., Jones J.B., Graham J.H., RA Setubal J.C., Wang N.; RT "Comparative Genomic Analysis of Xanthomonas axonopodis pv. citrumelo RT F1, Which Causes Citrus Bacterial Spot Disease, and Related Strains RT Provides Insights into Virulence and Host Specificity."; RL J. Bacteriol. 193:6342-6357(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002914; AEO43550.1; -; Genomic_DNA. DR RefSeq; YP_004852848.1; NC_016010.1. DR EnsemblBacteria; AEO43550; AEO43550; XACM_3303. DR GeneID; 11134847; -. DR KEGG; xax:XACM_3303; -. DR KO; K00788; -. DR BioCyc; XALF981368:GH9H-3303-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22173 MW; D30448E52C986EA3 CRC64; MPNRLDVRGV YLITPDEPNT QRLLLRTAPL LGSITWLQYR NKQADAALRL RQAGALREAC AAHGVPLIIN DDAQLAAQVG AQGVHLGEDD GDVAAARALL GEQAIIGVSC YDDIERARAA AEAGANYVAF GAFFPTTTKQ TTRRATPALL QQAAELNLPR VAIGGIAPAQ VPALVTAGAD LIAVVSGVYA APDPVAAVQE YRAGFAAQRG KL // ID G2LSG7_9XANT Unreviewed; 315 AA. AC G2LSG7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 22-JAN-2014, entry version 18. DE SubName: Full=Thiamine monophosphate synthase ThiE; GN ORFNames=XACM_0785; OS Xanthomonas axonopodis pv. citrumelo F1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=981368; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F1; RX PubMed=21908674; DOI=10.1128/JB.05777-11; RA Jalan N., Aritua V., Kumar D., Yu F., Jones J.B., Graham J.H., RA Setubal J.C., Wang N.; RT "Comparative Genomic Analysis of Xanthomonas axonopodis pv. citrumelo RT F1, Which Causes Citrus Bacterial Spot Disease, and Related Strains RT Provides Insights into Virulence and Host Specificity."; RL J. Bacteriol. 193:6342-6357(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002914; AEO41089.1; -; Genomic_DNA. DR RefSeq; YP_004850387.1; NC_016010.1. DR ProteinModelPortal; G2LSG7; -. DR EnsemblBacteria; AEO41089; AEO41089; XACM_0785. DR GeneID; 11133275; -. DR KEGG; xax:XACM_0785; -. DR KO; K03574; -. DR BioCyc; XALF981368:GH9H-785-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34949 MW; 1F053438483BAD82 CRC64; MPDSLRSIHV VAGVITDPRG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIEAQVGD WVMEVPQLYP DKRLRLEVRH ITSWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGAL RQPDRYLITP EPEDEARWLE GLELALHNGI TRIQLRARQL APARWQALLQ QVMRLRGRAR AQLLLNRDIA LAADLGIGVH LGSEQLAGLQ ERPLPADRLV AASCHGLDDL RHAQRIGCDF AVLGPVQATA SHPGATPIGW DGFETLREQV WLPIYALGGM QGEDVRQARS HGAQGIAAIR ALWPQ // ID G2M4U1_HELPX Unreviewed; 219 AA. AC G2M4U1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HPPN120_04195; OS Helicobacter pylori Puno120. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1055528; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Puno120; RA Kersulyte D., Cabrera L., Hooper C.C., Jahuira Arias H., Gilman R.H., RA Berg D.E.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002980; AEN15454.1; -; Genomic_DNA. DR RefSeq; YP_005788505.1; NC_017378.1. DR EnsemblBacteria; AEN15454; AEN15454; HPPN120_04195. DR GeneID; 12368801; -. DR KEGG; hep:HPPN120_04195; -. DR KO; K00788; -. DR BioCyc; HPYL1055528:GLEL-813-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23890 MW; F75B4676ADE341DA CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLALQDP VEIKQLALKC QKLCQKYGAP FIINDEVQLA LELKANGVHV GQEDMAIEEV MTLCKKRLFI GLSVNTLEQA LKARHLDGVA YFGVGPIFPT QSKKDKQVVG VELLKKIKDS GVKKPLVAIG GITTHNASKL REYGGIAVIS AITQAKDKAL AVGKLLKNA // ID G2M9Z1_HELPX Unreviewed; 219 AA. AC G2M9Z1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HPPN135_04185; OS Helicobacter pylori Puno135. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1055529; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Puno135; RA Kersulyte D., Cabrera L., Hooper C.C., Jahuira Arias H., Gilman R.H., RA Berg D.E.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002982; AEN18529.1; -; Genomic_DNA. DR RefSeq; YP_005790046.1; NC_017379.1. DR EnsemblBacteria; AEN18529; AEN18529; HPPN135_04185. DR GeneID; 12370385; -. DR KEGG; heu:HPPN135_04185; -. DR KO; K00788; -. DR BioCyc; HPYL1055529:GLEM-829-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23866 MW; 6586392FE64C90AC CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLALQDP IEIKQLALKC QKLCQKYGAP FMVNDEAKLA LELKADGVHV GQEDMAIEEV MALCKKRLFI GLSVNTLEQA LKARHLDGVA YFGVGPIFPT QSKKDKQVVG VELLKKIKDS GIKKPLIAIG GITTHNASKL REYGGIAVIS AITQAKDKAL AVGKLLNDA // ID G2MEI2_HELPX Unreviewed; 220 AA. AC G2MEI2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HPSNT_04370; OS Helicobacter pylori SNT49. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1055530; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Santal49; RA Kersulyte D., Choudhury A., Mukhopadhyay A.K., Nair G.B., Berg D.E.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002983; AEN17024.1; -; Genomic_DNA. DR RefSeq; YP_005787005.1; NC_017376.1. DR EnsemblBacteria; AEN17024; AEN17024; HPSNT_04370. DR GeneID; 12367273; -. DR KEGG; hen:HPSNT_04370; -. DR KO; K00788; -. DR BioCyc; HPYL1055530:GLER-843-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23898 MW; 395703C3B95D01A4 CRC64; MFDANCLKLM FVAGSQDFYH ISGGKNDRIN ALLDTLESAL QSKITAFQFR QKGDLALQDP VKIKQLALEC QKLCQKYGAP FIVNDEVQLA LELKADGVHV GQEDMAIEEV VTLCQKRLFI GLSVNTLEQA LKARHLDAVA YLGVGPIFPT PSKKDAKQVV GVELLKKIKD SGVKKPLIAI GGINTDNASK LREYGGIAVI SAIAQAKDKA LAIEKLLNHA // ID G2MSV9_9THEO Unreviewed; 213 AA. AC G2MSV9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Thewi_0725; OS Thermoanaerobacter wiegelii Rt8.B1. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=697303; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rt8.B1; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Zeytun A., Daligault H., Detter J.C., RA Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., RA Pagani I., Hemme C., Woyke T.; RT "Complete sequence of Thermoanaerobacter wiegelii Rt8.B1."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002991; AEM78174.1; -; Genomic_DNA. DR RefSeq; YP_004819458.1; NC_015958.1. DR EnsemblBacteria; AEM78174; AEM78174; Thewi_0725. DR GeneID; 11081823; -. DR KEGG; twi:Thewi_0725; -. DR KO; K00788; -. DR BioCyc; TWIE697303:GH3A-750-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23065 MW; D0456F2E6C6A3D22 CRC64; MDLTLYAITD RSYIKDMDIA DAVELAIKGG ATIIQLREKD ISSREFYEIA LKVKEVTKRN KIPLIINDRV DIALAVDADG VHVGQEDLPA DVVRKIIGRD KIVGVSASTV EEALKAQKDG ADYLGVGAVF KTPTKPEAEA IGIEGLKKIK EAVTIPVVAI GGITKDNAYE VMLKSGVDGI SSVSAVFYGD IENNTRKLLE VIAKAINDRR NLK // ID G2N736_MYCTX Unreviewed; 222 AA. AC G2N736; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MTCTRI2_0417; OS Mycobacterium tuberculosis CTRI-2. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=707235; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CTRI-2; RA Shitikov E., Ilina E., Ikryannikova L., Malakhova M., Parfenova T., RA Afanas'ev M., Kamashev D., Bazaleev N., Ischenko D., Aliper A., RA Alekseev D., Smirnova T., Chernousova L., Larionova E., Beletsky A., RA Mardanov A., Ravin N., Skryabin K., Govorun V.; RT "The Complete Genome Sequence of Mycobacterium tuberculosis CTRI2."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CTRI-2; RX PubMed=23437175; DOI=10.1371/journal.pone.0056577; RA Ilina E.N., Shitikov E.A., Ikryannikova L.N., Alekseev D.G., RA Kamashev D.E., Malakhova M.V., Parfenova T.V., Afanas'ev M.V., RA Ischenko D.S., Bazaleev N.A., Smirnova T.G., Larionova E.E., RA Chernousova L.N., Beletsky A.V., Mardanov A.V., Ravin N.V., RA Skryabin K.G., Govorun V.M.; RT "Comparative Genomic Analysis of Mycobacterium tuberculosis Drug RT Resistant Strains from Russia."; RL PLoS ONE 8:E56577-E56577(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002992; AEM98860.1; -; Genomic_DNA. DR RefSeq; YP_005915482.1; NC_017524.1. DR ProteinModelPortal; G2N736; -. DR SMR; G2N736; 1-221. DR EnsemblBacteria; AEM98860; AEM98860; MTCTRI2_0417. DR GeneID; 12505585; -. DR KEGG; mto:MTCTRI2_0417; -. DR KO; K00788; -. DR OMA; YEVINRS; -. DR BioCyc; MTUB707235:GLGU-417-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID G2NDP3_9ACTO Unreviewed; 216 AA. AC G2NDP3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACTE_1536; OS Streptomyces sp. SirexAA-E. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=862751; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SirexAA-E; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., RA Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Adams A., Raffa K., Adams S., Book A., Currie C., Woyke T.; RT "Complete sequence of Streptomyces sp. SirexAA-E."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002993; AEN09452.1; -; Genomic_DNA. DR RefSeq; YP_004801992.1; NC_015953.1. DR ProteinModelPortal; G2NDP3; -. DR EnsemblBacteria; AEN09452; AEN09452; SACTE_1536. DR GeneID; 11098480; -. DR KEGG; ssx:SACTE_1536; -. DR KO; K00788; -. DR BioCyc; SSP862751:GHMW-1552-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22532 MW; 826DE1591CD54135 CRC64; MSTPRSRLAD ARLYLCTDAR KRQGDLPAFL DAVLSSGVDV VQLRDKGMEA AEELEHLAVF ADACARHGAL LAVNDRADVA HAAGSAVLHL GQGDLPVPAA RAILGDDVLI GRSTHAEAEV DAAVAEAGTD YFCTGPCWPT PTKPGRHAPG LGLVRYAASL PTTRPWFAIG GIDAGNLDEV LDAGARRVVV VRAVTEADDP AAAAAELAKR VRARSL // ID G2P6N3_STRVO Unreviewed; 217 AA. AC G2P6N3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Strvi_7187; OS Streptomyces violaceusniger Tu 4113. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=653045; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tu 4113; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ivanova N., Daligault H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Hagen A., RA Katz L., Fiedler H.-P., Keasling J., Fortman J., Woyke T.; RT "Complete sequence of chromosome of Streptomyces violaceusniger Tu RT 4113."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002994; AEM86553.1; -; Genomic_DNA. DR RefSeq; YP_004816833.1; NC_015957.1. DR ProteinModelPortal; G2P6N3; -. DR EnsemblBacteria; AEM86553; AEM86553; Strvi_7187. DR GeneID; 11085741; -. DR KEGG; svl:Strvi_7187; -. DR KO; K00788; -. DR BioCyc; SVIO653045:GHK6-6989-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22793 MW; 57F49D7A2AFFA367 CRC64; MSTTATAHEP LADARLYLCT DARKRQGDLP EFLDAVLAAG VDIVQLREKE MEAAEELEHL QVLADACRRH GKLLAVNDRA DVAHAIGSDV LHLGQGDLPV PAARAILGAD VLIGRSTHAE AEVDAAAVQP GVDYFCTGPC WPTPTKPGRP APGLSLVRHA AALGTERPWF AIGGIDASNL DQVLEAGARR IVVVRAITAA DDPAAATAEL AKRVRAA // ID G2PQC5_MURRD Unreviewed; 212 AA. AC G2PQC5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Murru_2595; OS Muricauda ruestringensis (strain DSM 13258 / LMG 19739 / B1). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Muricauda. OX NCBI_TaxID=886377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13258 / LMG 19739 / B1; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Muricauda ruestringensis DSM 13258."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002999; AEM71631.1; -; Genomic_DNA. DR RefSeq; YP_004789053.1; NC_015945.1. DR EnsemblBacteria; AEM71631; AEM71631; Murru_2595. DR GeneID; 11055444; -. DR KEGG; mrs:Murru_2595; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; MRUE886377:GI6V-2637-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). SQ SEQUENCE 212 AA; 23590 MW; 5070A84FC367E469 CRC64; MKLHSQFPYP LYLVISEEAC RGKDMLKVTE QAIQGGVDIL QLREKKLLEH LFLERAQRLR EITEKYSVPL IINDNPKVAY QVNAAGIHVG NKDSRPATLR QQPYFKEKLI GYSIEYLAQL DNAQTTVSDY LAISPVFRTD TKRDTVTEWG LEGLATIREL TQKPLVAIGN IHAINAGAVI QAGANCIAVV SAICGADNPK KAAYELKNEI VK // ID G2PVJ9_9FIRM Unreviewed; 219 AA. AC G2PVJ9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Calla_2032; OS Caldicellulosiruptor lactoaceticus 6A. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=632516; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6A; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Blumer-Schuette S.E., Kelly R.M., Woyke T.; RT "Complete sequence of Caldicellulosiruptor lactoaceticus 6A."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003001; AEM74599.1; -; Genomic_DNA. DR RefSeq; YP_004799576.1; NC_015949.1. DR EnsemblBacteria; AEM74599; AEM74599; Calla_2032. DR GeneID; 11106086; -. DR KEGG; clc:Calla_2032; -. DR KO; K00788; -. DR BioCyc; CLAC632516:GHP3-2078-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24303 MW; 1108A41720BC2815 CRC64; MTKEEKLKLF STYTIYGMTA EKFSNGRSNI EVVKAMLDGG IKIIQYREKY KSLKEKYKEC LEIRKLTEDY GALLIVNDHA DLCQMVGADG VHLGQSDLPA VEVRKLLGDK FIIGVTTHTK EQVLKAKEDG ADYVGLGPIY ASFTKDNPHP PIGLEMVRWA AENSPLPFVA IGGIKDHNLK EVLANGARCI CAVTEIVGAD NIQLKIEGLF KILKSFERS // ID G2QEB1_THIHA Unreviewed; 521 AA. AC G2QEB1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-APR-2014, entry version 15. DE SubName: Full=Uncharacterized protein; GN ORFNames=MYCTH_2304176; OS Thielavia heterothallica (strain ATCC 42464 / BCRC 31852 / DSM 1799) OS (Myceliophthora thermophila). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae; OC Myceliophthora. OX NCBI_TaxID=573729; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799; RX PubMed=21964414; DOI=10.1038/nbt.1976; RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., RA Reid I., Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., RA Coutinho P.M., Lombard V., Natvig D.O., Lindquist E., Schmutz J., RA Lucas S., Harris P., Powlowski J., Bellemare A., Taylor D., Butler G., RA de Vries R.P., Allijn I.E., van den Brink J., Ushinsky S., Storms R., RA Powell A.J., Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., RA LaBoissiere S., Clutterbuck A.J., Martinez D., Wogulis M., RA de Leon A.L., Rey M.W., Tsang A.; RT "Comparative genomic analysis of the thermophilic biomass-degrading RT fungi Myceliophthora thermophila and Thielavia terrestris."; RL Nat. Biotechnol. 29:922-927(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003004; AEO57694.1; -; Genomic_DNA. DR RefSeq; XP_003662939.1; XM_003662891.1. DR GeneID; 11507565; -. DR KEGG; mtm:MYCTH_2304176; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 521 AA; 54974 MW; F377F184CC8405B9 CRC64; MGKPQVDYRL YLVTDSTPAI LGDRDLNEVV EASLKGGVTI VQLREKKGDT AEIIAKAQKM QQVTRKYNVP LLINDRVDVA LAVDCEGVHI GQDDMELSTA RNLLGPDKII GVTVSTVEEA LKACEGGADY LGIGTVYATA TKTNTKDIIG TAGVREILRR IAEAGYNTPA VCIGGINASN LQRVLYQCAA PNKVLNGVAI VSAIMAAADP EAATKNLAAL SRGPPAFTLD TSRDLSADAD GKAVIALAAP VIRRIHDTTP LSHNMTNLVV QNFAANVALA VGASPIMAGY GEEAADLCKL GGALVINMGS VDPSGLANYV KALKAYNLEG RPVVFDPVGA GATSLRREAV KMIMANGYLD VIKGNEGEIK TVFGNSKEQQ RGVDSTSTLD ASQKAKLVRE LASREKNVVL MTGKTDFVSD GVRTYAIDNG HEYLGMVTGT GCTLGTAISA AIASRQTDRL AAVVAAILHF EIAAELAAER PEVRGPGTFV PAFLDELYLI RQATARNDLA WLARAKVRGV E // ID G2RBY1_THITE Unreviewed; 521 AA. AC G2RBY1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-APR-2014, entry version 14. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=THITE_2119543; OS Thielavia terrestris (strain ATCC 38088 / NRRL 8126) (Acremonium OS alabamense). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae; OC Thielavia. OX NCBI_TaxID=578455; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38088 / NRRL 8126; RX PubMed=21964414; DOI=10.1038/nbt.1976; RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., RA Reid I., Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., RA Coutinho P.M., Lombard V., Natvig D.O., Lindquist E., Schmutz J., RA Lucas S., Harris P., Powlowski J., Bellemare A., Taylor D., Butler G., RA de Vries R.P., Allijn I.E., van den Brink J., Ushinsky S., Storms R., RA Powell A.J., Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., RA LaBoissiere S., Clutterbuck A.J., Martinez D., Wogulis M., RA de Leon A.L., Rey M.W., Tsang A.; RT "Comparative genomic analysis of the thermophilic biomass-degrading RT fungi Myceliophthora thermophila and Thielavia terrestris."; RL Nat. Biotechnol. 29:922-927(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003012; AEO69302.1; -; Genomic_DNA. DR RefSeq; XP_003655638.1; XM_003655590.1. DR GeneID; 11524448; -. DR KEGG; ttt:THITE_2119543; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 521 AA; 54652 MW; 761B1470039B4162 CRC64; MGKPAVDYSL YLVTDSTRPI LGDRSLESVV EQALRGGVTL VQLREKTADT AELISVARGL HAITRRYNVP LLINDRVDVA LAVGCEGVHI GQDDMDLSTA RKLLGPDAII GVTASTVDEA LRACEGGADY LGIGTVYATP TKTNTKNIIG TAGVRDILGK IAEAGYDTRT VCIGGINESN VQRILFQSAD PRKGLDGVAV VSAIMAASDP EAAARKLLEL VKSPPAFQAD LRSAGSDIAD APSLVALAPS VVRRVHETTP LSHNMTNLVV QNFAANVALA VGASPIMAGY GEEAPDLCKL GGALVINMGS VDPAGLANYL KALRAYNLAG RPVVYDPVGA GATSLRRETV KTILASGYLD VIKGNEGEIR TVLGDSQEQQ RGVDSSSTLN AAQKARVVRA LAAREKNVVV MTGRTDFVSD GARTFAVENG HEYLGLVTGT GCTLGTAISA AVAPRQTDRL AAVIAAILHF EIAAEVAAER PDVRGPGTFV PAFLDELYRI RQATAAGDHS WLQRAKVARV E // ID G2RR33_BACME Unreviewed; 214 AA. AC G2RR33; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BMWSH_3087; OS Bacillus megaterium WSH-002. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1006007; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WSH-002; RA Liu L., Li Y., Zhang J., Zou W., Zhou Z., Liu J., Li X., Wang L., RA Chen J.; RT "Complete Genome Sequence of the Industrial Strain Bacillus megaterium RT WSH-002."; RL J. Bacteriol. 193:6389-6390(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003017; AEN89969.1; -; Genomic_DNA. DR RefSeq; YP_005495278.1; NC_017138.1. DR EnsemblBacteria; AEN89969; AEN89969; BMWSH_3087. DR GeneID; 12085057; -. DR KEGG; bmh:BMWSH_3087; -. DR KO; K00788; -. DR BioCyc; BMEG1006007:GL8N-3166-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23099 MW; F5AE6E6050DC9536 CRC64; MTNEEIKKLL QVYFIMGSNN CKKDPKEVLK EAIEGGVTVF QFREKGEGAL KGEAKYQLAK ELQQICQQHS VPFVVNDDLD LAIRLQADGV HIGQEDEKAH IVREKIGKGI VGVSVHNVQE LQQAIKDGAD YVGMGPVFPT STKKDAKAVQ GTKLIEEVRN QNIDFPIVGI GGITPENAKQ VVEAGADGVS IITAISLAAS PKEKAAQLKE AVGK // ID G2RRT2_BACME Unreviewed; 233 AA. AC G2RRT2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 22-JAN-2014, entry version 18. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN Name=tenI; ORFNames=BMWSH_4685; OS Bacillus megaterium WSH-002. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1006007; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WSH-002; RA Liu L., Li Y., Zhang J., Zou W., Zhou Z., Liu J., Li X., Wang L., RA Chen J.; RT "Complete Genome Sequence of the Industrial Strain Bacillus megaterium RT WSH-002."; RL J. Bacteriol. 193:6389-6390(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003017; AEN91563.1; -; Genomic_DNA. DR RefSeq; YP_005496872.1; NC_017138.1. DR EnsemblBacteria; AEN91563; AEN91563; BMWSH_4685. DR GeneID; 12081960; -. DR KEGG; bmh:BMWSH_4685; -. DR KO; K10810; -. DR BioCyc; BMEG1006007:GL8N-4801-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 233 AA; 25560 MW; 427AD21757111BC0 CRC64; MYVIKPSTQD KVIEISLYSE WKGFDHMDIP KFHVITTDKQ PIEEVRDILT AIVPFAGAIH IREKKKTAKQ IQCLLESLPF CRSKMIVNDR VDVAHALKAK GVQLAYHSLD VSCVRDAFPS LIVGKSVHSV EEALEAEKDG AHYILYGHIY STHSKKELKS RGIAALKEVV DAVKIPVIAI GGITPVNAKE VLQTGAHGIA VMSGVMLAQD PLKAIKQYSH IWTSGGGENE AAL // ID G2SA15_ENTAL Unreviewed; 211 AA. AC G2SA15; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Entas_0228; OS Enterobacter asburiae (strain LF7a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=640513; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LF7a; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., RA Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA van der Lelie D., Woyke T.; RT "Complete sequence of chromosome of Enterobacter asburiae LF7a."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003026; AEN62983.1; -; Genomic_DNA. DR RefSeq; YP_004826768.1; NC_015968.1. DR EnsemblBacteria; AEN62983; AEN62983; Entas_0228. DR GeneID; 11111785; -. DR KEGG; eas:Entas_0228; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; EASB640513:GKDM-234-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22934 MW; EBB7D2498FD0D61D CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIARLLE AGVRTIQLRI KDKRDEEVEA DVVAAIELGR RYDARLFIND YWRLAIKHQA YGVHLGQEDL ETTDLDAIRN AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLGQLA GHIQRLTDYP TVAIGGISLE RAPAVLETGV GSIAVVSAIT QAPDWQAATA QLLTLAGAGD E // ID G2SHJ2_RHOMR Unreviewed; 220 AA. AC G2SHJ2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Rhom172_1072; OS Rhodothermus marinus SG0.5JP17-172. OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Rhodothermus. OX NCBI_TaxID=762570; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SG0.5JP17-172; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Chertkov O., Detter J.C., Han C., RA Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Gladden J., Woyke T.; RT "Complete sequence of chromosome of Rhodothermus marinus SG0.5JP17- RT 172."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003029; AEN73002.1; -; Genomic_DNA. DR RefSeq; YP_004824839.1; NC_015966.1. DR EnsemblBacteria; AEN73002; AEN73002; Rhom172_1072. DR GeneID; 11114235; -. DR KEGG; rmg:Rhom172_1072; -. DR KO; K00788; -. DR BioCyc; RMAR762570:GJAN-1103-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23604 MW; 56384A243F9DFE80 CRC64; MGKKPIGRLH VLTDFYFQQR YGHAELARLV IAGGADTVQF RQKFGGIRHR LYEARRTAAV CKEAGVPLII DDHIDIALAV EADGVHLGQE DFPVAEARRI LGPDFIIGAT ATTVEQAVEA WQAGADYIGF GPVFPTASKA NPASVKGIEG LRQVCEAVPI PVIAIAGITV QRVRPVLEAG AYGVAVMTAI TTAPDPRAAT AQFRLEIESV LRTLPETPRT // ID G2SIT3_RHOMR Unreviewed; 208 AA. AC G2SIT3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Rhom172_0776; OS Rhodothermus marinus SG0.5JP17-172. OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Rhodothermus. OX NCBI_TaxID=762570; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SG0.5JP17-172; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Chertkov O., Detter J.C., Han C., RA Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Gladden J., Woyke T.; RT "Complete sequence of chromosome of Rhodothermus marinus SG0.5JP17- RT 172."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003029; AEN72711.1; -; Genomic_DNA. DR RefSeq; YP_004824548.1; NC_015966.1. DR EnsemblBacteria; AEN72711; AEN72711; Rhom172_0776. DR GeneID; 11112956; -. DR KEGG; rmg:Rhom172_0776; -. DR KO; K00788; -. DR BioCyc; RMAR762570:GJAN-795-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 131 133 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22126 MW; 0FF5BECDC197B869 CRC64; MLPRLLLIAD RFTEPHRVDA VRRAVAAGVP WVQLRDHRVD FDTFARAAEA LVPMLKAENP NLLLSVNTNL DVARRLGLGL HVGRRGPSVA EARRQLGSGA LLGYSAHDLD AARQAADEGA DYLLFSPVFP TASKPGVPAV GLEALATVCR AVAVPVLALG GITPERVSVC LQQGAHGVAV VSAILEAPDP AAAVRQFLER IENALHHR // ID G2SSJ4_BIFAN Unreviewed; 516 AA. AC G2SSJ4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 22. DE SubName: Full=Phosphomethylpyrimidine kinase; GN ORFNames=BLC1_1199; OS Bifidobacterium animalis subsp. lactis BLC1. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=1075106; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BLC1; RA Bottacini F., Dal Bello F., Turroni F., Milani C., Duranti S., RA Foroni E., Viappiani A., Strati F., Mora D., van Sinderen D., RA Ventura M.; RT "Complete Genome Sequence of Bifidobacterium animalis subsp. lactis RT BLC1."; RL J. Bacteriol. 193:6387-6388(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BLC1; RA Bottacini F., Foroni E., Milani C., Duranti S., Turroni F., RA Viappiani A., Mora D., Dal Bello F., van Douwe S., Ventura M.; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003039; AEN76971.1; -; Genomic_DNA. DR RefSeq; YP_005580004.1; NC_017216.2. DR ProteinModelPortal; G2SSJ4; -. DR EnsemblBacteria; AEN76971; AEN76971; BLC1_1199. DR GeneID; 12172354; -. DR KEGG; bbc:BLC1_1199; -. DR KO; K14153; -. DR BioCyc; BANI1075106:GL93-1236-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 516 AA; 54334 MW; BA2BECA74309264A CRC64; MNSFPYPSMR DRFDLRFYFV VGPDDCGNRP ILDVVAKALD GGASFIQLRA KTQDVAEIVS LANDIAEEIA GHHVEHSVAF VVDDRVDAAL EARAKGIKVD GVHIGQDDLD PVVARKLLGP DAIIGLSAKT VDEVREANHL PEGTIDYIGA GPLHMTATKP ESMIVDENGD ITTLNVSSID EMRTMSKYPL IVGGGVKADD IPMLAKTKAD GWFVVSAIAG ATDPEQATRR LVDDWTAIRG DEKPRYTGRK PAATKLPAVL TIATTDSSGG AGIPADLKTM LANDVFGECV VAGITAQNTT GVQAIAAVDP SIVGAQIDSV FDDIRPTAVK IGVIVGVESV KTVARKLRDH QATNIVVDPV MVATSGSSLA ADDTIAEEIS SLFPIATVIT PNIPEAQVLA QMPIGNQADM ETAAVQLAKD YGTCVLVKGG HGVKDADDVL AFPTGAVTWF EGERIANDNT HGTGCTLSSA IASYLAQGED LEDAVRDAKA YLSGALRANL NLGKGHGPMD HAWAMH // ID G2T5Q7_ROSHA Unreviewed; 215 AA. AC G2T5Q7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=RHOM_14735; OS Roseburia hominis (strain DSM 16839 / NCIMB 14029 / A2-183). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=585394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16839 / NCIMB 14029 / A2-183; RA Mulder I.E., Aminov R.I., Travis A.J., Lan A., Gaboriau-Routhiau V., RA Garden K., Logan E., Delday M., Coutts A.G.P., Grant G., RA Patterson A.M., Cerf-Bensussan N., Kelly D.; RT "Bi-directional cross-talk between a Clostridium symbiont, Roseburia RT hominis, the gut immune system and appetite regulation."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003040; AEN98053.1; -; Genomic_DNA. DR RefSeq; YP_004839985.1; NC_015977.1. DR EnsemblBacteria; AEN98053; AEN98053; RHOM_14735. DR GeneID; 11148465; -. DR KEGG; rho:RHOM_14735; -. DR KO; K00788; -. DR BioCyc; RHOM585394:GHYQ-2990-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22966 MW; 6168DA93456B0AD6 CRC64; MKCDKRDLLL YAVTDRSWSE GTTLGAQVEE ALRGGATFVQ LREKKLTGEA LRAEALEIQA VCRRYGVPFV INDDVALAKE IDADGVHVGQ DDMEAGDVRA ILGADKIIGV SAHNVEEALR AERHGADYLG VGAAFTTSSK PEAGHIDAAT IRAICETVKI PVIAIGGIKE ENLLQLRGNG LCGVAVISAI FAQKDIEAAT RRLRALVEEM AGDQE // ID G2TEC6_RHORU Unreviewed; 216 AA. AC G2TEC6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=F11_05565; OS Rhodospirillum rubrum F11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=1036743; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F11; RX PubMed=22194448; DOI=10.1128/JB.06319-11; RA Lonjers Z.T., Dickson E.L., Chu T.P., Kreutz J.E., Neacsu F.A., RA Anders K.R., Shepherd J.N.; RT "Identification of a New Gene Required for the Biosynthesis of RT Rhodoquinone in Rhodospirillum rubrum."; RL J. Bacteriol. 194:965-971(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003046; AEO47583.1; -; Genomic_DNA. DR RefSeq; YP_006047380.1; NC_017584.1. DR ProteinModelPortal; G2TEC6; -. DR EnsemblBacteria; AEO47583; AEO47583; F11_05565. DR GeneID; 12642210; -. DR KEGG; rrf:F11_05565; -. DR KO; K00788; -. DR BioCyc; RRUB1036743:GLJ7-1136-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22991 MW; 6778BD683175801C CRC64; MSDPACRLYL ITPPRLDDWA AFAETLKRTL AAGDVACLQL RMKDESDDAI RRAVAAIRPV CHGADVALLL NDRPDLAKET GCDGVHVGQT DASYAQARAI VGADAIVGVT CHDSRHLAMI AGEAGADYVA FGAFFPSTTK EPPTQADPEI LRWWSEMMIV PSVAIGGITV ENCAPLVETG TDFLAVCNGV WGHAEGPEAA VRAFVRVIAE VYAQPD // ID G2TFE1_RHORU Unreviewed; 259 AA. AC G2TFE1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 22-JAN-2014, entry version 18. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=F11_18590; OS Rhodospirillum rubrum F11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=1036743; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F11; RX PubMed=22194448; DOI=10.1128/JB.06319-11; RA Lonjers Z.T., Dickson E.L., Chu T.P., Kreutz J.E., Neacsu F.A., RA Anders K.R., Shepherd J.N.; RT "Identification of a New Gene Required for the Biosynthesis of RT Rhodoquinone in Rhodospirillum rubrum."; RL J. Bacteriol. 194:965-971(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003046; AEO50178.1; -; Genomic_DNA. DR RefSeq; YP_006049975.1; NC_017584.1. DR EnsemblBacteria; AEO50178; AEO50178; F11_18590. DR GeneID; 12644858; -. DR KEGG; rrf:F11_18590; -. DR BioCyc; RRUB1036743:GLJ7-3774-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 259 AA; 27132 MW; 0BFCE7C01030417C CRC64; MPRTLVHFIA KGSPLSRLGS RRSAAAPPRL LLMTDDQRLA DPLGAADRLP PKAGVIVRHY ACAGAVRHGL ARALIARLRA RRIAVILAAP SPAHALPAGL AGLHLPDKLA AHGLLARLLL WRRAARGRWL CAAAHDAPAM IRARRLGCAL IVLSPLFPTA SHPGARGLGA RRAALLIHRL AARRAPAGSR AGKAPAVIAL GGISTLSFRR LAGCGFGGIA GISALPGMKW RRSGREKPKP RTGDGKSRRP PVCLSPLSA // ID G2TPW2_BACCO Unreviewed; 214 AA. AC G2TPW2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Bcoa_3136; OS Bacillus coagulans 36D1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=345219; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=36D1; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Bruce D., Goodwin L., Chertkov O., Brettin T., RA Han C., Detter C., Pitluck S., Shanmugam K.T.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=36D1; RX PubMed=22675583; DOI=10.4056/sigs.2365342; RA Rhee M.S., Moritz B.E., Xie G., Glavina Del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Chertkov O., Brettin T., Han C., Detter C., RA Pitluck S., Land M.L., Patel M., Ou M., Harbrucker R., Ingram L.O., RA Shanmugam K.T.; RT "Complete Genome Sequence of a thermotolerant sporogenic lactic acid RT bacterium, Bacillus coagulans strain 36D1."; RL Stand. Genomic Sci. 5:331-340(2011). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=36D1; RA Shanmugan K.T.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003056; AEP02308.1; -; Genomic_DNA. DR RefSeq; YP_004861088.1; NC_016023.1. DR ProteinModelPortal; G2TPW2; -. DR EnsemblBacteria; AEP02308; AEP02308; Bcoa_3136. DR GeneID; 11174062; -. DR KEGG; bag:Bcoa_3136; -. DR KO; K00788; -. DR BioCyc; BCOA345219:GH5A-3098-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22569 MW; AD1159581BE9C8AA CRC64; MTGEHLRDAL KLYFIMGSPN CTLPPEQVLE NAIRGGVTLF QFREKGKGAR KGEEKKVLGE KLKWICQKNG IPFLVNDDIA LALELDADGV HVGQEDEPLA SVREKLGDKI IGVSAYTLEE ARQAANGGAD YLGVGPIFPT KSKEDAKAAK GTTVIREIRQ NGIRIPIVGI GGIGPGNAKS VIEAGADGVS VISAIAGAED AEAAAALLKR ELTL // ID G2U6D7_PSEAI Unreviewed; 209 AA. AC G2U6D7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NCGM1179_0285; OS Pseudomonas aeruginosa NCMG1179. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1078464; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCGM1179; RA Tada T., Kitao T., Miyoshi-Akiyama T., Kirikae T.; RT "Genome Sequence of Multidrug-Resistant Pseudomonas aeruginosa RT NCGM1179."; RL J. Bacteriol. 193:6397-6397(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF126593; GAA15473.1; -; Genomic_DNA. DR ProteinModelPortal; G2U6D7; -. DR SMR; G2U6D7; 24-200. DR EnsemblBacteria; GAA15473; GAA15473; NCGM1179_0285. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22146 MW; 898DA261D0AFA265 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER HGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAQ LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID G2UDS0_PSEAI Unreviewed; 315 AA. AC G2UDS0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE SubName: Full=Probable pyrophosphohydrolase; GN ORFNames=NCGM1179_6041; OS Pseudomonas aeruginosa NCMG1179. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1078464; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCGM1179; RA Tada T., Kitao T., Miyoshi-Akiyama T., Kirikae T.; RT "Genome Sequence of Multidrug-Resistant Pseudomonas aeruginosa RT NCGM1179."; RL J. Bacteriol. 193:6397-6397(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF126593; GAA21165.1; -; Genomic_DNA. DR ProteinModelPortal; G2UDS0; -. DR SMR; G2UDS0; 6-123, 127-313. DR EnsemblBacteria; GAA21165; GAA21165; NCGM1179_6041. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34055 MW; 9165F7469596B47A CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EDGEPVRAAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEAHGAEGQ PLAWVEPREL ADYEFPAANA PIVQAARLPA HYLITPDGLE PGELISGVRK AVEAGIRLIQ LRAPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDAEELAL AASMGVEFVT LSPVQPTESH PGEPALGWDK AAELIAGFNQ PVYLLGGLGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID G2UQT6_MYCTX Unreviewed; 222 AA. AC G2UQT6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NCGM2209_0801; OS Mycobacterium tuberculosis NCGM2209. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1078763; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCGM2209; RA Miyoshi-Akiyama T., Matsumura K., Kobayashi N., Maeda S., Kirikae T.; RT "Genome Sequence of Clinical Isolate Mycobacterium tuberculosis RT NCGM2209."; RL J. Bacteriol. 193:6792-6792(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCGM2209; RA Akiyama T., Matsumura K., Kirikae T.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF126614; GAA44199.1; -; Genomic_DNA. DR ProteinModelPortal; G2UQT6; -. DR SMR; G2UQT6; 1-221. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID G2WNX1_YEASK Unreviewed; 540 AA. AC G2WNX1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-APR-2014, entry version 13. DE SubName: Full=K7_Thi6p; GN Name=K7_THI6; ORFNames=SYK7_068821; OS Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's OS yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=721032; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kyokai no. 7 / NBRC 101557; RX PubMed=21900213; DOI=10.1093/dnares/dsr029; RA Akao T., Yashiro I., Hosoyama A., Kitagaki H., Horikawa H., RA Watanabe D., Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., RA Kajiwara S., Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., RA Masubuchi T., Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., RA Ogata T., Ohta A., Sato M., Shibasaki S., Takatsume Y., Tanimoto S., RA Tsuboi H., Nishimura A., Yoda K., Ishikawa T., Iwashita K., Fujita N., RA Shimoi H.; RT "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai RT no. 7."; RL DNA Res. 18:423-434(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DG000052; GAA26764.1; -; Genomic_DNA. DR ProteinModelPortal; G2WNX1; -. DR SMR; G2WNX1; 3-536. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 58059 MW; F34FA1E0B76E3930 CRC64; MVFTKEEVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDIE TKNFVAEALE VQKICKKYNV PLIINDRIDV AMAIDADGVH VGQDDMPIPM VRKLLGPSKI LGWSVGKPSE VETLAKWGPD MVDYIGVGTL FPTSTKKNPK KSPMGPQGAI AILDALEEFK ATWCRTVGIG GLHPDNIQRV LCQCVASNGK RSLDGISLVS DIMAAPDACA ATKRLRGLLD ATRYQFVECE LNNTFPTTTS IQNVISQVSN NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL ARIPNASLLL NTGSVAPIEM LKAAINAYNE VNRPITFDPV GYSATETRLC LNNTLLTYGQ FACIKGNCSE ILSLAKLNNH KMKGVDSSSG KTNIDTLVRA TQIVAFQYRT VAVCTGEFDC VADGTFGGEY KLSSGTEGIT AEDLPCVIIE DGPIPIMGDI TASGCSLGST IASFIGGLDS TGKLFDAVVG AVLLYKSAGK LASTRCQGSG SFHVELIDAL YQLFHENKPE KWSASLKKFK // ID G2YJT3_BOTF4 Unreviewed; 522 AA. AC G2YJT3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-APR-2014, entry version 13. DE SubName: Full=Similar to thiamine biosynthetic bifunctional enzyme; GN ORFNames=BofuT4_P082840.1; OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis OS cinerea). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Botryotinia. OX NCBI_TaxID=999810; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T4; RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230; RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., RA Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., RA Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., RA Pradier J.-M., Quevillon E., Sharon A., Simon A., ten Have A., RA Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., RA Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., RA Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., RA Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., RA Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., RA Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., RA Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., RA Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., RA Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.; RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia RT sclerotiorum and Botrytis cinerea."; RL PLoS Genet. 7:E1002230-E1002230(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ790339; CCD34962.1; -; Genomic_DNA. DR ProteinModelPortal; G2YJT3; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 522 AA; 54995 MW; 03596C5735F8EE45 CRC64; MAPQNVDYSL YLVTDSTPAI LGDRNLVDVV DAAVRGGVTI VQYRDKHSDT AALVDTARKL HAVTRKYNVP LLINDRIDVA LAVACEGVHI GQDDMDLKTA RALLGKDAII GVTVANVQEA LTASKDGADY LGIGTMFATP TKTNTKEIIG TAGTKEVLHS LQQSGSQVRT VAIGGINSSN LQRVLYQSAS EGKQLDGVAI VSAIISAQDA EKAASELAEL VRTPAPFALA NLPHDQKIED PRELLLQVPS IVGDVAKKTP LSHNMTNLVV QNFAANVALA IGASPIMANY GEEAADLAKL GGGLVINMGT VTPEGIQNYS KALRAYNNEG GPIVLDPVGC GATAVRRSAV KSLLANGYFD VIKGNEGEIK TVSGSLIQQR GVDSGSSTLS LVEKATIVRD LALRERNVVL MTGAVDILSD GVRTLAISNG HEILGRITGS GCVLGTIISA MLAVSRGDKL LAVLSALLHY EIAAEMAALR DDVRGPGTFV PALIDELYVI QKANSQGDLR WLEKARVETI AW // ID G2ZNZ0_9RALS Unreviewed; 384 AA. AC G2ZNZ0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=BDB_110199; OS blood disease bacterium R229. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=741978; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R229; RA Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S., RA Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., RA Prior P.; RT "Phylotype IV strains of Ralstonia solanacearum, R. syzygii and the RT blood disease bacterium form a single genomic species despite their RT divergent life-styles."; RL PLoS ONE 0:0-0(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R229; RA Genoscope - CEA; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR854067; CCA80767.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 384 AA; 40374 MW; DA2CD916EC0AA25E CRC64; MSASALRFAA AWPDAAALAG RIIDRHADAF GRAPHAWSVT DRADEATTAT TVLLTADRAQ AERARAAGAR VVLTETRNGE RIDTVHDRLG TYRFASTATG EALGERFVAM FGAALALAFE PRDALCVARA WIAEAPADAL AWPARFDTLP RVLEPALPCA ASPDLAFAPC PTQLGVYAVV PDAAWVERLV ALKVPTVQLR VKSDNAQAVA EQVRRAAAAA HGSQTRLFIN DHWRVALDVH AQTPDSGLYG IHLGQEDIDD ADLAAIRAAG LRLGISTHGY AEMLRVAPLN PSYLALGAVF ATPTKTMPTV PQGLGRLFAY AAAMRTRVPA PPLVAIGGID LAAMPRVLES GVGCVAVVRA ITQAGDVPAA VQALQATFAA HVRA // ID G2ZSU6_9RALS Unreviewed; 198 AA. AC G2ZSU6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase (ThiE); DE EC=2.5.1.3; GN ORFNames=BDB_180152; OS blood disease bacterium R229. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=741978; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R229; RA Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S., RA Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., RA Prior P.; RT "Phylotype IV strains of Ralstonia solanacearum, R. syzygii and the RT blood disease bacterium form a single genomic species despite their RT divergent life-styles."; RL PLoS ONE 0:0-0(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R229; RA Genoscope - CEA; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR854074; CCA82109.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 198 AA; 21695 MW; DB21452C89A9C686 CRC64; MRRVSLPDFY QITPEPVGSP YFEKFFAELT DTLRSGIRLL QLRAKQLEPR EHLDVARRTR DLCRQFGAIL MLNGPIDMAR EVGCDGVHLS SDALMSLRSR PAPDTVLISA ACHSVAQLEQ AARVEVDFVT LSPVLRTRTH PDADPLGWES FSELVQCSRV PVFALGGMSP ETLDQAKSAG AWGVAAISAT WCQQSAGA // ID G3A3F5_9RALS Unreviewed; 384 AA. AC G3A3F5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; DE EC=2.5.1.3; GN Name=thiE; ORFNames=RALSY_30136; OS Ralstonia syzygii R24. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=907261; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R24; RA Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S., RA Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., RA Prior P.; RT "Phylotype IV strains of Ralstonia solanacearum, R. syzygii and the RT blood disease bacterium form a single genomic species despite their RT divergent life-styles."; RL PLoS ONE 0:0-0(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R24; RA Genoscope - CEA; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR854088; CCA88399.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 384 AA; 40333 MW; 649C01B7B90AEA31 CRC64; MSASALRFAA AWPDAAALAG RIIDRHADAF GRAPHAWSVT DRADEATTAT TVLLTADRAQ AERARAAGAG VVLTETRNGE RIDTVHDRLG TYRFASTATG EALGERFVAM FGAALALAFE PRDALCVARA WIAEAPADAL AWPARFDTLP RVLEPALPCA ASPDLAFAPC PTQLGVYAVV PDAAWVERLV ALKVPTVQLR VKSDNAQAVA EQVRRAEAAA HGSQTRLFIN DHWRVALDVH AQTPDSGLYG IHLGQEDIDD ADLAAIRAAG LRLGISTHGY AEMLRVAPLN PSYLALGAVF ATPTKTMPTV PQGLGRLFAY AAAMRTRVPA PPLVAIGGID LAAMPRVLES GVGCVAVVRA ITQAGDVPAA VQALQATFAA HVRA // ID G3A9Y8_9RALS Unreviewed; 198 AA. AC G3A9Y8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase (ThiE); DE EC=2.5.1.3; GN ORFNames=RALSY_mp10662; OS Ralstonia syzygii R24. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=907261; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R24; RA Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S., RA Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., RA Prior P.; RT "Phylotype IV strains of Ralstonia solanacearum, R. syzygii and the RT blood disease bacterium form a single genomic species despite their RT divergent life-styles."; RL PLoS ONE 0:0-0(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R24; RA Genoscope - CEA; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR854090; CCA88122.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 198 AA; 21659 MW; 3A2DEE4D9B955EEB CRC64; MRRVSLPDFY QITPEPVGSP HFEKFFAELT DTLRSGIRLL QLRAKQLEPR EHLDVARRTR DLCRQFGAIL MLNGPIDMAR EVGCDGVHLS SDALMSLRSR PAPDTVLISA ACHSVAQLEQ AARVEVDFVT LSPVLRTRTH PDADPLGWES FSELVQCSRV PVFALGGMSS ETLDQAKSAG AWGVAAISAT WCQQSAGA // ID G3AQG7_SPAPN Unreviewed; 500 AA. AC G3AQG7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-APR-2014, entry version 11. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=SPAPADRAFT_140906; OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Spathaspora. OX NCBI_TaxID=619300; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL Y-27907 / 11-Y1; RX PubMed=21788494; DOI=10.1073/pnas.1103039108; RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., RA Labutti K.M., Sun H., Clum A., Pangilinan J.L., Lindquist E.A., RA Lucas S., Lapidus A., Jin M., Gunawan C., Balan V., Dale B.E., RA Jeffries T.W., Zinkel R., Barry K.W., Grigoriev I.V., Gasch A.P.; RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel RT production."; RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL996503; EGW31514.1; -; Genomic_DNA. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 500 AA; 53480 MW; F388C37812D123A5 CRC64; MTVDYSLYLV TDSTMIPESS TFLRQVELAI ANGATIVQLR EKKLSTLDFI TRAQQVHALT KAKGIPLIIN DRVDVALAID AEGVHVGQDD MPAELVRRLI GENKILGVTC SVPEEVEAVT ASGIADYVGL GTVYATNTKK DVTDPEGTGP IGIRKMLQVL GRYNQSHEKK INSVAIGGIN HTNADKVMYE CAVDGERIDG VAVVSCIMAS ENAGKATSDL LKIIETTPNW ASRSCIQEAD IGKFVAQTHP LVHHITNNVV KNFSANVTLA LGASPIMSEL AAEFHEFASD IPMIALVLNL GTPTPELMSV FKTAIQVYNK YAKHIVFDPV ACGATQARLQ ASKKLLNSGH VSVIKGNLGE IQGIWKLTST YSESSNSGSL MRGVDSIAKL TEEKIIQIGK EVSKDFKTVV VITGKVNYII DGDKYTKSEG GSELMGLVTG SGCSLGSTIA AFLATGADVY LSAVDAVNLY NEAGRRAAGY SSTPGSFMIS FVDELYKLTH // ID G3AY78_CANTC Unreviewed; 520 AA. AC G3AY78; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 13. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=CANTEDRAFT_101804; OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / OS NBRC 10315 / NRRL Y-1498 / VKM Y-70) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; OC Candida. OX NCBI_TaxID=590646; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 / RC NRRL Y-1498 / VKM Y-70; RX PubMed=21788494; DOI=10.1073/pnas.1103039108; RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., RA Labutti K.M., Sun H., Clum A., Pangilinan J.L., Lindquist E.A., RA Lucas S., Lapidus A., Jin M., Gunawan C., Balan V., Dale B.E., RA Jeffries T.W., Zinkel R., Barry K.W., Grigoriev I.V., Gasch A.P.; RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel RT production."; RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL996512; EGV65784.1; -; Genomic_DNA. DR RefSeq; XP_006684358.1; XM_006684295.1. DR GeneID; 18245501; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 520 AA; 55892 MW; F2AF3A6289EE1527 CRC64; MNVDYTLYLV TDSTMVPESS TFLKQVEDSI NAGATIVQLR EKSISTLDFI ERAQKVHELT KKKNIPLIIN DRIDVALVVD AEGVHVGQDD MPAKLARQLL GPNKIIGVTC SNPSEVQQVC DEDVADYVGI GTVYKTLTKT DTKTPMGTGP IGIRKMLQTL KTRNTNRQPI KCVAIGGINE TNVTKVLYQC SIPGQKLDGV AVVSCIMAKE DAYKATVELQ EQINGIVPWK KDGMSKFDTF TYNNSHLEIQ TQKIQKAGAL VHHITNNVVK NFSANVTLAI GASPIMSELA EEYEEFAQKI PNISLVLNLG TPTVEMMQTF IHAITTYNKY GKHVIFDPVA AGATNARLEC SRVLLNAGQM SVIKGNVGEI SAIFKLTSTY EVAKNEEVLM RGVDSIANLS EESIRNIGYA VSQDFKCVVV ITGPTNHVID AESGSFAQVP GGNKLMGLIT GSGCSLGSAI GSFVAAKADS SATENLNLFE AVVGAVTLYN AAGKLVGTKC SAPGAFVPAF VDSLYLKANK // ID G3IT36_9GAMM Unreviewed; 307 AA. AC G3IT36; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Mutator MutT protein; GN ORFNames=Mettu_0078; OS Methylobacter tundripaludum SV96. OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylobacter. OX NCBI_TaxID=697282; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SV96; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Klotz M.G., RA Dispirito A.A., Murrell J.C., Dunfield P., Kalyuzhnaya M.G., RA Svenning M., Trotsenko Y.A., Stein L.Y., Woyke T.; RT "Genomic sequence of Methylobacter tundripaludum SV96."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH109152; EGW21320.1; -; Genomic_DNA. DR ProteinModelPortal; G3IT36; -. DR EnsemblBacteria; EGW21320; EGW21320; Mettu_0078. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 307 AA; 33458 MW; F95C803CEA292E82 CRC64; MNPLQVAVGV VKNPEGKVLI SLRHADLHQG GLWEFPGGKI EASETAEQAL ARELKEELNI TVTAATPLIT VKHQYPDRFV QLNVFLVEQF SGEAKSLEGQ SFKWVTPAEL QHYAFPAANQ PIITAARLPH HYAILDDADE AMLLSNLQKI LNRGVKLIQA RLKTLPSVDV AKFFEQAYPL CKQQQAVLLM NSAVECSVEV DGIHLTSSHL MALTKRPENS KWLAASCHNL EQLQQAQKIG VDFVVLAPVL ATQTHPGAAS LGWEQFADLV AKVNLPVYAL GGMTESSLTT SQQSGGQGIA AIRAFLD // ID G3IYC4_9GAMM Unreviewed; 206 AA. AC G3IYC4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Mettu_4305; OS Methylobacter tundripaludum SV96. OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylobacter. OX NCBI_TaxID=697282; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SV96; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Klotz M.G., RA Dispirito A.A., Murrell J.C., Dunfield P., Kalyuzhnaya M.G., RA Svenning M., Trotsenko Y.A., Stein L.Y., Woyke T.; RT "Genomic sequence of Methylobacter tundripaludum SV96."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH109153; EGW21146.1; -; Genomic_DNA. DR EnsemblBacteria; EGW21146; EGW21146; Mettu_4305. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21555 MW; 8CC6F0D5A6568FCB CRC64; MIKFPASGLY AITQTENKSG DTIINEVAAA IKGGAVIVQY RDKNPADAPF LARELVKICH QHGVPLLIND DIELAALVGA DGVHLGREDG AVTQARKQLG SDAIIGVSCY NFVEQAIAAQ AQGATYAAFG RFFPSSSKPL AAPAQIETLR QAKHALTIPI VAIGGILPDN GAQLLAAGAD LLAVIGGVFD HQPEQSARAY QALFSR // ID G3J5D8_CORMM Unreviewed; 467 AA. AC G3J5D8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-MAY-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=CCM_01506; OS Cordyceps militaris (strain CM01) (Caterpillar fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae; OC Cordyceps. OX NCBI_TaxID=983644; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CM01; RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116; RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., RA Huang Y., Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.; RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, RT a valued traditional chinese medicine."; RL Genome Biol. 12:R116-R116(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH126399; EGX96848.1; -; Genomic_DNA. DR RefSeq; XP_006666725.1; XM_006666662.1. DR GeneID; 18163537; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 467 AA; 47606 MW; 1BB690EA2EACEE67 CRC64; MLPLLTPKRA TTSPPPPPPN YGVYLVTDST PAILGSRDLV AVVEAALRGG VTCVQYRDKH GAPAAVVATA RRLHALTQRY GVPLLINDRV DVAVQVGCEG VHIGQDDMDV HQARTLLGSG KIVGVTASNV DEAIKACQDG ADYLGIGTVY STATKKDTKS IIGPSGVRAI LKAMAAGGYG AVPTVCIGGV HTDNAAAVLA QSSAAPAKSL SGVAVVSAII AAEDPAEAAR QLAGHVAVAA IPLVVGAVGR ATPLSHNMTN LVVQNFAANV ALAVGASPIM SNYAAEAGDL AKLGGALVVN MGTVTPEGLA NYKQAIQAYN DADRPIILDP VGAGATAIRR AASAEMLAVG RFAVIKGNVA ELQTLLGQAV TQRGVDSTAE VDVASRARAM VAAWPADALL AAVAAAAVFG IAAQYAVDRD DVRGPGTFVP AFLDELHAIT RATAEGDLRW LVRARVQGVL VEQDDEA // ID G3XVI8_ASPNA Unreviewed; 519 AA. AC G3XVI8; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-APR-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=ASPNIDRAFT_49671; OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB OS Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=380704; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / RC NRRL 328 / USDA 3528.7; RX PubMed=21543515; DOI=10.1101/gr.112169.110; RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I., RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., RA Albermann K., Berka R.M., Braus G.H., Braus-Stromeyer S.A., RA Corrochano L.M., Dai Z., van Dijck P.W.M., Hofmann G., Lasure L.L., RA Magnuson J.K., Menke H., Meijer M., Meijer S.L., Nielsen J.B., RA Nielsen M.L., van Ooyen A.J.J., Pel H.J., Poulsen L., Samson R.A., RA Stam H., Tsang A., van den Brink J.M., Atkins A., Aerts A., RA Shapiro H., Pangilinan J., Salamov A., Lou Y., Lindquist E., Lucas S., RA Grimwood J., Grigoriev I.V., Kubicek C.P., Martinez D., RA van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.; RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC RT 1015 versus enzyme-producing CBS 513.88."; RL Genome Res. 21:885-897(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJE01000006; EHA25241.1; -; Genomic_DNA. DR ProteinModelPortal; G3XVI8; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 519 AA; 54530 MW; 9894F9DCA20AD49E CRC64; MTLDLSVYLV TDSTPAILKG RDLCAVVEEA VKGGVTIVQY RDKKSDTGVQ VETAKKLHQI TKKYNVPLLI NDRVDVALAA GVEGVHLGQD DMAIEVARKL LPENSIIGIS ASSIEEAQKA VAAGADYLGI GTMFATPTKT NTKSIIGTAG TQAILEAISE SGRTVGTVSI GGINASNVQR VLYQSRAPNK ALDGVAIVSA IMAADDPKAA AAEFVKLVSS PPPFVRSDAT TPARDTSALL EQVPQVVQEV VKGHPLVHNM INYVVANFVA NVALSMGASP IMSPYGDEAV DLCQFDGALV INMGTLTSES IPNYLKAQKA YNMRGNPVVY DPVGAAATSI RRGAVTQLMS GGYFDLIKGN EGEIRQVFGS SGVTQRGVDS GPSNLDSHGK ARLARDLARR EHNIVLLTGA TDYLSDGERV VAVSNGHELL GQVTGTGCAV GTVSGAFLTT HPKDKFLAVL AGILMYEIAA ENAASADNVR GPGSFVPAFL DELYAIRQAA LKGDHSWFAG RAKVEEIQL // ID G3Z0U8_9NEIS Unreviewed; 205 AA. AC G3Z0U8; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1028_00213; OS Neisseria sp. GT4A_CT1. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=665946; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GT4A_CT1; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Daigneault M., RA Ambrose C.E., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Neisseria sp. GT4A_CT1."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWS01000009; EGY59423.1; -; Genomic_DNA. DR EnsemblBacteria; EGY59423; EGY59423; HMPREF1028_00213. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21993 MW; FDC38D3B8F702701 CRC64; MTFPPLKSPL KFYAVVPTAD WVERMVKAGA DTVQLRCKTL HGDELKREIA RCVAACRGGR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYVASGAIFP TTTKQMPTAP QGLDKLREYV KQARGTPVVA IGGIDLNNAE DVLATGVSSL AVVRAVTEAE NPEAVVKAFQ ALWDE // ID G4AB82_AGGAC Unreviewed; 59 AA. AC G4AB82; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-OCT-2013, entry version 8. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=SC1083_2117; OS Aggregatibacter actinomycetemcomitans serotype e str. SC1083. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=907488; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SC1083; RA Chen C., Kittichotirat W., Asikainen S., Bumgarner R.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEJM01000048; EGY32423.1; -; Genomic_DNA. DR EnsemblBacteria; EGY32423; EGY32423; SC1083_2117. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 59 AA; 6662 MW; 9A891A918EAF0D5C CRC64; MDLIAIQHAE LHFSVSNHNA EEIVRVLSLR PSSIAYGHIF PTQAGDMPFR PQDIENFPC // ID G4BFX3_AGGAP Unreviewed; 225 AA. AC G4BFX3; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ATCC33389_1642; OS Aggregatibacter aphrophilus ATCC 33389. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=985008; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33389; RA Kittichotirat W., Bumgarner R.E., Checn C.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEWB01000017; EGY30700.1; -; Genomic_DNA. DR EnsemblBacteria; EGY30700; EGY30700; ATCC33389_1642. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 53 57 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 202 203 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 24611 MW; 3C66D8B8ED83F337 CRC64; MELAMPTSVS NLAEIVPPNA PFAPTEFKLG LYVIVDSYEW IERLIHASVK TLQIRIKDRS PEQAEEEIAR CIALAKQHQV RLFVDDFWQL AIKYQAYGVH LGQEDLLTAD LNAIQQAGLR LGVSTHNREE IELVLPLRPS YIALGHIFPT QSKIMPSAPQ GIANLAAQVK DLGDIPTVAI GGITASHFAD VLATGVSSIA VISAVTQAED WQSAVKNLLN YFDAS // ID G4C9D5_SALIN Unreviewed; 211 AA. AC G4C9D5; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEENIN0B_04429; OS Salmonella enterica subsp. enterica serovar Infantis str. SARB27. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=596155; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SARB27; RA McClelland M., Clifton S., Porwollik S., Cheng P., Wollam A., Wang C., RA Pepin K., Bhonagiri V., Fulton R., Fulton L.F., Delehaunty K., RA Fronick C., O'Laughlin M., Godfrey J., Waligorski J., Appelbaum E., RA Farmer C., Strong C., Tomlinson C., Hou S., Minx P., Warren W., RA Wilson R.K.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFYI01000006; EHB39677.1; -; Genomic_DNA. DR EnsemblBacteria; EHB39677; EHB39677; SEENIN0B_04429. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22965 MW; 459E10B03EFF94F3 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHLA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLANYP TVAIGGISLE RAPSVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID G4CEN6_9NEIS Unreviewed; 220 AA. AC G4CEN6; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9371_0075; OS Neisseria shayeganii 871. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=1032488; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=871; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAY01000002; EGY53764.1; -; Genomic_DNA. DR EnsemblBacteria; EGY53764; EGY53764; HMPREF9371_0075. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 49 53 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22989 MW; 33D193C65565A039 CRC64; MTPAPLPDAD SRPVTPGFPP PVRPLKFYAV VPDADWVARM VAAGADTVQL RNKTLSGDAL RQEVRRAVAA AAGSGSQLFI NDYWRLALEE GAYGVHLGQE DLDAADLHAL CEAGIRLGIS THSDAELARA LAVQPSYVAC GAIFPTTTKT MPTAPQGLDN LRRYVAQAGN TPTVAIGGID LHNAADVLAT GVSSLAVVRA VTEAADPAAV VKAFQALWPE // ID G4CMG8_9NEIS Unreviewed; 208 AA. AC G4CMG8; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9370_0277; OS Neisseria wadsworthii 9715. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=1030841; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=9715; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAZ01000009; EGZ51114.1; -; Genomic_DNA. DR EnsemblBacteria; EGZ51114; EGZ51114; HMPREF9370_0277. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22388 MW; 0DD634E9E19AE7DB CRC64; MSKMLRFVGV DSPLKFYAVV PDAQWVERMV RAGADTVQLR TKTISGDALL QEIMRCVKAC EGSRTKLFIN DYWQEAIAAG AHGVHLGQED MDDADLQEIA DAGLRLGLST HSVAELDRAL SVNPSYVASG AVFPTTTKVM KSEPQGLEKL REYVRQAGNT PVVAIGGIDL NNAREVLSTG VASLAVVRAV TEAADPEAAV KAFQALWD // ID G4CX91_9ACTO Unreviewed; 217 AA. AC G4CX91; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9153_1148; OS Propionibacterium avidum ATCC 25577. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=997355; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25577; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGBA01000013; EGY77605.1; -; Genomic_DNA. DR EnsemblBacteria; EGY77605; EGY77605; HMPREF9153_1148. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22384 MW; C773D93A3258D0BF CRC64; MTLDLRCYLV TSGTDRHTVE TAALAAGAGA GIVQVRAKTL ATRDLLSLVL QVGEAVRRAN PETRVVVDDR ADVAWAAMRA RGNVHGVHLG VEDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPLADALD YLGAGPFRPT PTKDSGRPPL GVEGYPALVQ ASSRPVVAIG DVQVDDVAAL ATTGIAGVAM VRAVMAADDP AAVVAQAIAA FDRGREG // ID G4D051_9ACTO Unreviewed; 215 AA. AC G4D051; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=thiE2; ORFNames=HMPREF9153_2073; OS Propionibacterium avidum ATCC 25577. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=997355; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25577; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGBA01000015; EGY77120.1; -; Genomic_DNA. DR EnsemblBacteria; EGY77120; EGY77120; HMPREF9153_2073. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 139 141 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22587 MW; 071DDE01BB61C0CB CRC64; MSRPDFDLSV YLVTDTAQCG GPEEIVETVR RAISGGVTLV QFRDHDLPDD EFVALGRRVR DVCDEIPLII DDRVHLVAEI GADGAHVGQS DMPVAQARKV LGDNLLIGLS AQTPAHVEAA LSHGPDVVDY LGVGALHATG TKPEAGELGL AAIRDVVDVS PWPVCVIGGV TASDAQDVAR VGCDGLSVVS AICRNADPES NARELAQAWC HAKGR // ID G4D2W3_9FIRM Unreviewed; 215 AA. AC G4D2W3; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9129_0743; OS Peptoniphilus indolicus ATCC 29427. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XI. Incertae Sedis; Peptoniphilus. OX NCBI_TaxID=997350; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29427; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGBB01000063; EGY80129.1; -; Genomic_DNA. DR EnsemblBacteria; EGY80129; EGY80129; HMPREF9129_0743. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23666 MW; F7F56787B48F0841 CRC64; MKSVDYSIYL VTDRDLITGD NLLNEIEESL IGGTKLVQLR EKNATTREFL KLATELKELC HRYNAKLLIN DRIDIALAIN ADGVHLGQTD MPADIARKIL GEDKIIGVST QTIEMAKEAE SLGADYIGVG AVFPTQTKDV IYDMNPEILS SIAVSVSIPV VAIGGINRNT IDDLKDIDVA GYAVVTGILM AEDKKSETEY LLNKYRENTR SFNAK // ID G4E2I0_9GAMM Unreviewed; 212 AA. AC G4E2I0; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ThisiDRAFT_0509; OS Thiorhodospira sibirica ATCC 700588. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thiorhodospira. OX NCBI_TaxID=765914; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700588; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., RA Frigaard N.-U., Bryant D., Woyke T.; RT "The draft genome of Thiorhodospira sibirica ATCC 700588."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGFD01000006; EGZ49629.1; -; Genomic_DNA. DR EnsemblBacteria; EGZ49629; EGZ49629; ThisiDRAFT_0509. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 21982 MW; 9797A50EBB67FF55 CRC64; MINKTRLCGL YVLTDQTLMP APHLLSEVEA ALQGGARLVQ YRDKHSAASV RLTQAQQLRA LCQRFGALFL VNDDVALAQA VDADGVHLGQ SDMPLPQARA LLGPDKLIGI TCHASLALAY QAVAQGADYL AFGAFYPSVT KPQAASAPLA LLHQAKQQLS LPLCAIGGIT ADNAAPLVAA GADLLAVTAG VFASADTQQA AAQLARLYAI SA // ID G4E2L1_9GAMM Unreviewed; 326 AA. AC G4E2L1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=ThisiDRAFT_0540; OS Thiorhodospira sibirica ATCC 700588. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thiorhodospira. OX NCBI_TaxID=765914; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700588; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., RA Frigaard N.-U., Bryant D., Woyke T.; RT "The draft genome of Thiorhodospira sibirica ATCC 700588."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGFD01000006; EGZ49660.1; -; Genomic_DNA. DR ProteinModelPortal; G4E2L1; -. DR EnsemblBacteria; EGZ49660; EGZ49660; ThisiDRAFT_0540. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 326 AA; 35902 MW; 8292F6D4F3FF6846 CRC64; MAKDLPQRVA VALISNALDQ YLIASRIPPG HTEALWEFPG GKIEPGETTA QALQRELCEE LGVYPLVQDP LLSVVQDAVC LEVHCVRAID RPPQPCEGQQ LRWVDRQQLP RYRFWPANQI ILQTLLARPR PLPLYYLITP EPGADWAGFL QHLQQRLSHG DIGMVRLRST AQTPLSLTQV AEFVRCCQHQ QVQALLSDDV PLAQRSGADG VHFSQQHLLQ GLPVRQMAQQ SLCYGASVHD AHSLSVAASL PLDFLTLSPL APTASHPDTP TLGWDAFCKL AQHSPIPIYA LGGLDMADLP TALNHRACGI AAIRALWQMP LHAASR // ID G4EPT6_BACIU Unreviewed; 215 AA. AC G4EPT6; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSSC8_03660; OS Bacillus subtilis subsp. subtilis str. SC-8. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1089443; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SC-8; RX PubMed=22207744; DOI=10.1128/JB.06442-11; RA Yeo I.C., Lee N.K., Hahm Y.T.; RT "Genome sequencing of Bacillus subtilis SC-8, antagonistic to the RT Bacillus cereus group, isolated from traditional Korean fermented- RT soybean food."; RL J. Bacteriol. 194:536-537(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGFW01000001; EHA32109.1; -; Genomic_DNA. DR EnsemblBacteria; EHA32109; EHA32109; BSSC8_03660. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22807 MW; F6B102C89D8B6865 CRC64; MMKELLSVYF IMGSNNTKAD PVTVVQKALK GGATLYQFRE KGGDALTGEA RIKFAEKAQA ACREAGVPFI VNDDVELALN LKADGIHIGQ EDANAKEVRA AIGDMILGVS AHTMSEVKQA EEDGADYVGL GPIYPTETKK DTRAVQGVSL IEAVRRQGIS IPIVGIGGIT IDNAAPVIQA GADGVSMISA ISQAEDPESA ARKFREEIQT YKTGR // ID G4EXS1_BACIU Unreviewed; 205 AA. AC G4EXS1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Transcriptional regulator TenI; DE EC=2.5.1.3; GN ORFNames=BSSC8_31510; OS Bacillus subtilis subsp. subtilis str. SC-8. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1089443; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SC-8; RX PubMed=22207744; DOI=10.1128/JB.06442-11; RA Yeo I.C., Lee N.K., Hahm Y.T.; RT "Genome sequencing of Bacillus subtilis SC-8, antagonistic to the RT Bacillus cereus group, isolated from traditional Korean fermented- RT soybean food."; RL J. Bacteriol. 194:536-537(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGFW01000009; EHA30054.1; -; Genomic_DNA. DR ProteinModelPortal; G4EXS1; -. DR SMR; G4EXS1; 1-200. DR EnsemblBacteria; EHA30054; EHA30054; BSSC8_31510. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 205 AA; 22929 MW; B04749ED70F0A088 CRC64; MELHAITDDS KPVEELARII ITIQNEVDFI HIRERSKSAA DILKLLDLIF EGGIDKRKLV MNGRVDIALF STIHRVQLPS GSFSPKQIRA RFPHLHIGRS VHSLEEAVQA EKEDADYVLF GHVFETDCKK GLEGRGVSLL SDIKQRISIP VIAIGGMTPD RLRDVKQAGA DGIAVMSGIF SSAEPLEAAR RYSRKLKEMR YEKAL // ID G4F3E8_9GAMM Unreviewed; 318 AA. AC G4F3E8; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=HAL1_04472; OS Halomonas sp. HAL1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=550984; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HAL1; RX PubMed=22156396; DOI=10.1128/JB.06359-11; RA Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A., RA Wang G., Rensing C.; RT "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately RT Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine RT Soil."; RL J. Bacteriol. 194:199-200(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGIB01000017; EHA17001.1; -; Genomic_DNA. DR EnsemblBacteria; EHA17001; EHA17001; HAL1_04472. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; SQ SEQUENCE 318 AA; 35796 MW; 1C58DA6216CC6C17 CRC64; MSIKVKRRVH VAAAAIISAD QQQVLIARRP SNVDHGGLWE FPGGKLAPYE TGLEGLKREL HEELGVEIVC AQPLIRVHHE YPDKHILLDV WQVHEFAGEP FGREGQAVRW VPMSELSNYP FPAANLPILR AVRLPTEYLI TNEEADEARF DAFLERALRE DKIRLVQLRA KQLDEAAYLA RAQRALTLCR EYGARLLLNG EPTLLDHIDA DGIHLTSERL MQLERRPIAE NKWLSASTHN QKQLTQAAVL GCDFVSLSPL RTTPSHPEVA PLGWHDFQQL VERAGMPVFA LGGMTRFDAN HARAVGAQGI ASIRDFWK // ID G4F7X1_9GAMM Unreviewed; 207 AA. AC G4F7X1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HAL1_12444; OS Halomonas sp. HAL1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=550984; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HAL1; RX PubMed=22156396; DOI=10.1128/JB.06359-11; RA Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A., RA Wang G., Rensing C.; RT "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately RT Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine RT Soil."; RL J. Bacteriol. 194:199-200(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGIB01000054; EHA15205.1; -; Genomic_DNA. DR EnsemblBacteria; EHA15205; EHA15205; HAL1_12444. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21267 MW; 4CA07422CA915DF2 CRC64; MALDLSLYLV TDAALCSDYG LEQTVEAAVN GGVTVVQLRD KHASDAQMTA QAKRLKELLT GTGVPLIIND RLQVALESQA DGLHVGQSDA AVQEARRALG DQAIIGLSIN TLAQLQAAPI ELLDYVGLGP VFATVSKQDH AQPIGLDGLA TLVKACPLPC VAIGGLKASH TGSVQQAGAN GLAVISAICG QPDPCQAARA FQVIPVT // ID G4FQH1_9SYNE Unreviewed; 353 AA. AC G4FQH1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Syn8016DRAFT_2925; OS Synechococcus sp. WH 8016. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=166318; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 8016; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Palenik B., Woyke T.J.; RT "The draft genome of Synechococcus sp. WH 8016."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGIK01000008; EHA58609.1; -; Genomic_DNA. DR EnsemblBacteria; EHA58609; EHA58609; Syn8016DRAFT_2925. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 128 Unknown (By similarity). FT REGION 129 353 Thiamine-phosphate synthase (By FT similarity). FT REGION 185 189 HMP-PP binding (By similarity). FT REGION 282 284 THZ-P binding (By similarity). FT METAL 218 218 Magnesium (By similarity). FT METAL 237 237 Magnesium (By similarity). FT BINDING 217 217 HMP-PP (By similarity). FT BINDING 256 256 HMP-PP (By similarity). FT BINDING 285 285 HMP-PP (By similarity). FT BINDING 312 312 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 353 AA; 39034 MW; 7E1940808B008299 CRC64; MEPMVVEADA NLRVARLIDA NLDRAREGLR VIEDWCRFGL DRDDLVVPLK DWRQRLGQQH RDRYRRARSS ATDVAAGLGH PAQASRCSAP AIVKANASRV QEALRVLEEF ARNLDPDLAS TAAEIRYGLY DLEVSILEAC GRQHRQERLE AAKLCLITDP DRDNDLERLL QGVEAALLAG VSLVQYRRKQ GHDQQRLREA QALKALCRRF DALFIINDRI DLALLVDADG VHLGQDDLPL SEARQLVGPE RLLGRSTHRL EHLLEAQQEG ADYLGVGPVF ATQTKRDRSP AGLSWVTEAS RHASVPWFAI GGIDAETIGS VRAAGAERVA VVSAIMGSND PEAASRTLLQ TLT // ID G4HJ99_9BACL Unreviewed; 224 AA. AC G4HJ99; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PaelaDRAFT_4060; OS Paenibacillus lactis 154. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=743719; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=154; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P., RA Allgaier M., Woyke T.J.; RT "The draft genome of Paenibacillus lactis 154."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGIP01000009; EHB62817.1; -; Genomic_DNA. DR EnsemblBacteria; EHB62817; EHB62817; PaelaDRAFT_4060. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23864 MW; 45E9CFECDE8D99A7 CRC64; MTGRVAPEMM RRHLRMYLVL GSVNCIVEPS LVVQEALAGG ATMVQFREKG HGALNGEPML RLARRIQEQC RQARVPFIVN DDVELALKLD ADGVHIGQDD ESAASVRERI GNRMLGVSAH TVEEARRAIL HGADYLGIGP IYPTRSKDDA KAAQGPAILR ELREAGIRLP IVGIGGITVE RVEEVIGAGA DGVAVISAVT GAASAQEAVE AFMGKIRRGA EGIS // ID G4HZU2_MYCRH Unreviewed; 235 AA. AC G4HZU2; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MycrhDRAFT_3022; OS Mycobacterium rhodesiae JS60. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=931627; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JS60; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Mattes T., Holmes A., Rutledge P., RA Paulsen I., Coleman N., Woyke T.J.; RT "The draft genome of Mycobacterium rhodesiae JS60."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGIQ01000002; EHB55828.1; -; Genomic_DNA. DR EnsemblBacteria; EHB55828; EHB55828; MycrhDRAFT_3022. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 160 162 THZ-P binding (By similarity). FT METAL 96 96 Magnesium (By similarity). FT METAL 115 115 Magnesium (By similarity). FT BINDING 95 95 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 HMP-PP (By similarity). FT BINDING 191 191 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 235 AA; 24809 MW; 73ADC3BC52A459CD CRC64; MPTVHASRYR RGVHEPHTRL ATARLYLCTD ARRERGDLAE FADAALAGGV DLIQLRDKGS PGEQQFGPLE ARGELQALEI LADAAGRHGA LLAVNDRADI ARAAGADVLH LGQDDLPLEV ARDIVGDATV IGRSTHAIGE AAQALTEDVD YFCVGPCWPT PTKPGRPAPG LDLVREVAAL QPDKPWFAIG GIDEERLADV LAAGATRIVV VRAITAADDP RAAAARLRTA LISAS // ID G4KJ67_YEREN Unreviewed; 223 AA. AC G4KJ67; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IOK_19612; OS Yersinia enterocolitica subsp. palearctica PhRBD_Ye1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=1071969; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PhRBD_Ye1; RX PubMed=22207747; DOI=10.1128/JB.06451-11; RA Klinzing D.C., Matias R.R., Skowronski E., Alvarez M., Liles V., RA Dimamay M.P., Natividad F.F.; RT "Shotgun genome sequence of a Yersinia enterocolitica isolate from the RT Philippines."; RL J. Bacteriol. 194:542-543(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQO01000074; EHB19200.1; -; Genomic_DNA. DR EnsemblBacteria; EHB19200; EHB19200; IOK_19612. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24371 MW; 73F1F69E77A483AC CRC64; MKPSDTPIFS AQKGFPTTEQ RLGLYPVVDS VLWIERLLAL GVTTIQLRIK ELDEAQVEQD IVAAIELGKR YQARLFINDY WRLAIKHGAY GVHLGQEDLE STDLAAIQQA GLRLGVSTHD EYELAIAKAV RPSYIAMGHI FPTQTKQMPS SPQGLAVLKQ MVENTPDYPT VAIGGISIER VPAVLATGVG SVAVVSAITQ AEDWQQATAQ LLHLIEGKEL ADE // ID G4KTN5_OSCVS Unreviewed; 212 AA. AC G4KTN5; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=OBV_30910; OS Oscillibacter valericigenes (strain DSM 18026 / NBRC 101213 / OS Sjm18-20). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Oscillospiraceae; OC Oscillibacter. OX NCBI_TaxID=693746; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18026 / NBRC 101213 / Sjm18-20; RA Katano Y., Fujinami S., Kawakoshi A., Ohji S., Nakazawa H., Ankai A., RA Oguchi A., Fukui S., Terui Y., Harada T., Takahashi M., Suzuki K., RA Fujita N.; RT "Whole genome sequence of Oscillibacter valericigenes Sjm18-20."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012044; BAL00290.1; -; Genomic_DNA. DR RefSeq; YP_004882795.1; NC_016048.1. DR EnsemblBacteria; BAL00290; BAL00290; OBV_30910. DR GeneID; 11234925; -. DR KEGG; ova:OBV_30910; -. DR KO; K00788; -. DR BioCyc; OVAL693746:GJWX-3136-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22979 MW; 68F4A1A8E9BAE97E CRC64; MDKMFDYTLY LVTDRGLMST EILETAVEKA IEGGVTMVQL REKEASSREF YDQSVRIKKI TDRYGVPLIV NDRIDIALAI GADGVHIGQS DLPAAVARTI IGREMLLGVS ASSLSEALQA QLDGADYLGV GAMFHTGTKQ EAQIVSMEKL LRIRQTVRIP VVAIGGIDRG NAASFRKAKI DGLAVVSAII SQPDIKDAAE ELKRLFLEGV TV // ID G4KYX7_OSCVS Unreviewed; 212 AA. AC G4KYX7; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=OBV_15730; OS Oscillibacter valericigenes (strain DSM 18026 / NBRC 101213 / OS Sjm18-20). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Oscillospiraceae; OC Oscillibacter. OX NCBI_TaxID=693746; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18026 / NBRC 101213 / Sjm18-20; RA Katano Y., Fujinami S., Kawakoshi A., Ohji S., Nakazawa H., Ankai A., RA Oguchi A., Fukui S., Terui Y., Harada T., Takahashi M., Suzuki K., RA Fujita N.; RT "Whole genome sequence of Oscillibacter valericigenes Sjm18-20."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012044; BAK98771.1; -; Genomic_DNA. DR RefSeq; YP_004881277.1; NC_016048.1. DR EnsemblBacteria; BAK98771; BAK98771; OBV_15730. DR GeneID; 11237738; -. DR KEGG; ova:OBV_15730; -. DR KO; K00788; -. DR BioCyc; OVAL693746:GJWX-1599-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 21985 MW; 252E5EAA48C6377D CRC64; MELKRNSFRL YAVTDRAWLH GEALADQVAK AITGGAGFVQ LREKALDNEE FLAEAKWFVP LCRKLGAVSI INDSVEIALA SGADGVHVGQ EDMAAAKARS SLGPDKIVGV SVHNVAEALA AQAAGADYLG VGAAFASHTK AEAKPLSIET IRSVTAAVRI PVIAIGGIKA DNISQLSGCG LDGVAVVSAL FAQPDVESAA RQMLALSEKI TH // ID G4L3R5_TETHN Unreviewed; 209 AA. AC G4L3R5; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 14-MAY-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TEH_00540; OS Tetragenococcus halophilus (strain DSM 20338 / JCM 20259 / NCIMB 9735 OS / NBRC 12172) (Pediococcus halophilus). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Tetragenococcus. OX NCBI_TaxID=945021; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20338 / JCM 20259 / NCIMB 9735 / NBRC 12172; RA Nakazawa H., Omata S., Koga C., Watanabe Y., Katano Y., Ito N., RA Tsukatani N., Ankai A., Oguchi A., Fukui S., Yashiro I., Kamata S., RA Hashimoto Y., Yamazaki J., Taguchi H., Tanaka A., Koyama T., RA Ichige A., Hanya Y., Tanikawa S., Yamazaki S., Fujita N.; RT "Whole genome sequence of Tetragenococcus halophilus NBRC 12172."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012046; BAK93381.1; -; Genomic_DNA. DR RefSeq; YP_004885545.1; NC_016052.1. DR EnsemblBacteria; BAK93381; BAK93381; TEH_00540. DR GeneID; 11261502; -. DR KEGG; thl:TEH_00540; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR BioCyc; THAL945021:GJV6-55-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22915 MW; 223E6E316976761C CRC64; MKIDTSLYLV TSRYGESESV FLQKIEEACK NGVTLVQLRE KELTTSAYYS LAQKVKNVTD YYQIPLIIDD RVDICLAVDA SGVHIGDDEL PTEVTRQLIG DKILGVSAKN VSQAQEAQMS GADYLGIGAM FSTTTKKDAQ TTSFETLQQI TQEISIPVVA IGGITEERIT NFNHINIQGI AVVSEIMKAS NIGEKVGQMR AKFTQLEGK // ID G4LBW5_PSEAI Unreviewed; 209 AA. AC G4LBW5; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NCGM2_5175; OS Pseudomonas aeruginosa NCGM2.S1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1089456; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCGM2.S1; RA Miyoshi-Akiyama T., Kuwahara T., Tada T., Kitao T., Kirikae T.; RT "Complete Genome Sequence of Highly Multidrug-Resistant Pseudomonas RT aeruginosa NCGM2.S1, a Representative Strain of a Cluster Endemic to RT Japan."; RL J. Bacteriol. 193:7010-7010(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCGM2.S1; RA Akiyama T., Kuwahara T., Ando T., Tada T., Kirikae T.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012280; BAK91996.1; -; Genomic_DNA. DR RefSeq; YP_005983381.1; NC_017549.1. DR ProteinModelPortal; G4LBW5; -. DR SMR; G4LBW5; 24-200. DR EnsemblBacteria; BAK91996; BAK91996; NCGM2_5175. DR GeneID; 12574965; -. DR KEGG; pnc:NCGM2_5175; -. DR KO; K00788; -. DR BioCyc; PAER1089456:GLIR-5176-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22146 MW; 898DA261D0AFA265 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER HGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAQ LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID G4LLP1_PSEAI Unreviewed; 315 AA. AC G4LLP1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 22-JAN-2014, entry version 19. DE SubName: Full=Uncharacterized protein; GN Name=mutT; ORFNames=NCGM2_1203; OS Pseudomonas aeruginosa NCGM2.S1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1089456; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCGM2.S1; RA Miyoshi-Akiyama T., Kuwahara T., Tada T., Kitao T., Kirikae T.; RT "Complete Genome Sequence of Highly Multidrug-Resistant Pseudomonas RT aeruginosa NCGM2.S1, a Representative Strain of a Cluster Endemic to RT Japan."; RL J. Bacteriol. 193:7010-7010(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCGM2.S1; RA Akiyama T., Kuwahara T., Ando T., Tada T., Kirikae T.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012280; BAK88074.1; -; Genomic_DNA. DR RefSeq; YP_005979459.1; NC_017549.1. DR ProteinModelPortal; G4LLP1; -. DR EnsemblBacteria; BAK88074; BAK88074; NCGM2_1203. DR GeneID; 12570993; -. DR KEGG; pnc:NCGM2_1203; -. DR KO; K03574; -. DR BioCyc; PAER1089456:GLIR-1203-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34041 MW; FBCE869C3EE6B47B CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EDGEPVRAAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEAHGAEGQ PLAWVEPREL ADYEFPAANA PIVQAARLPA HYLITPDGLE PGELISGVRK AVEAGIRLIQ LRAPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDADELAL AASMGVEFVT LSPVQPTESH PGEPALGWDK AAELIAGFNQ PVYLLGGLGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID G4MBP9_9BURK Unreviewed; 361 AA. AC G4MBP9; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-OCT-2013, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BKIR_c31_1430; OS Candidatus Burkholderia kirkii UZHbot1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1055526; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UZHbot1; RA Carlier A.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UZHbot1; RA Carlier A.L., Eberl L.; RT "Draft genome sequence of Candidatus Burkholderia kirkii."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFE01000182; CCD38578.1; -; Genomic_DNA. DR EnsemblBacteria; CCD38578; CCD38578; BKIR_c31_1430. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 361 AA; 39461 MW; 2450EBB28A895D2A CRC64; MSLLNREVFW PPADELIEVA KRIRARLGEW PAAETRWRVC LTAPEAPNTG DLIVFTEGQN VDMERLAKSG AAVLEAHGSR VTLRRGDERF ALEGECSDNW LAALAAFLDC HFESHDALVL ALAWRAGDEN KDDAWPVDFA TFPRVAELPP APESRCPPCP DRLGLYPVLP SAEWVERVLD LGVRTAQLRR KTSDAADLQR EIARSVEAGR RHDAHLFIND HWREAIATGA YGVHLGQEDL QTADLNAIAK AGLRLGLSTH GYYEMLRALH FRPSYLALGA VFPTRTKVMP TKPQGLARLA RYVQLLSGHV PLVAIGGIDA KAMPGVLATG IGSGAVVRAV TEAPDTAAAV SSLQQMFASQ W // ID G4N790_MAGO7 Unreviewed; 534 AA. AC G4N790; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Hydroxyethylthiazole kinase; GN ORFNames=MGG_06448; OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice OS blast fungus) (Pyricularia oryzae). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Magnaporthales; Magnaporthaceae; OC Magnaporthe. OX NCBI_TaxID=242507; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958; RX PubMed=15846337; DOI=10.1038/nature03449; RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K., RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D., RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., RA Harding M., Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., RA Calvo S.E., Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., RA Birren B.W.; RT "The genome sequence of the rice blast fungus Magnaporthe grisea."; RL Nature 434:980-986(2005). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=70-15; RG The Broad Institute Genome Sequencing Platform; RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Magnaporthe oryzae 70-15."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001234; EHA50800.1; -; Genomic_DNA. DR RefSeq; XP_003717119.1; XM_003717071.1. DR ProteinModelPortal; G4N790; -. DR EnsemblFungi; MGG_06448T0; MGG_06448T0; MGG_06448. DR GeneID; 2684603; -. DR KEGG; mgr:MGG_06448; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 534 AA; 55462 MW; 71A290A296AD6361 CRC64; MTKKDLANYS LYLVTDSTPE ILGGRDICQV VEDAIEGGVT IVQYRDKKSD TAVLIEVAQK LHRITSKHNV PLLINDRVDV ALAIGCEGVH LGQDDMSLVT ARRLLGPDAI IGISASTREE ALTACADGAD YLGIGAVFST NTKTNTKHIL GPVGIQHLLE IMHKEGFGHV QTVAIGGINA TNVQRVFFQS ATPGKKVLDG VAIVSAIMAA PSPRDASKNL LRLIKEPSAA LDNTIQASES GDILALVPAI IKAVHESTPL SHNMTNLVVQ NFAANVALAV GASPIMANYG EEAADLAKLG GALVINMGTV TPEGVENYVK ALRAYNAAER PVVLDPVGAG ATTIRREAVK TILSAGHASV IKGNEGEIAA VLASTTPFSN GDPGPQQRGV DSVSTLPDDE ARARLAARLA AQQRGSIVVM TGPTDIVSDG ERTFAIVQHG DPILGRVTGT GCCLGTVISA MLCSGTSGST DKLVAVVAGI LLYEIAAEVA AGRCQGPGSF VPAFIDALDE LRRAAAGGDV KWMSHAKIVK MSAA // ID G4NWG8_BACPT Unreviewed; 205 AA. AC G4NWG8; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-APR-2014, entry version 17. DE SubName: Full=Regulatory protein TenI; DE EC=2.5.1.3; GN OrderedLocusNames=GYO_1471; OS Bacillus subtilis subsp. spizizenii (strain TU-B-10). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1052585; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TU-B-10; RX PubMed=22493193; DOI=10.1128/JB.05675-11; RA Earl A.M., Eppinger M., Fricke W.F., Rosovitz M.J., Rasko D.A., RA Daugherty S., Losick R., Kolter R., Ravel J.; RT "Whole-genome sequences of Bacillus subtilis and close relatives."; RL J. Bacteriol. 194:2378-2379(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002905; AEP86123.1; -; Genomic_DNA. DR RefSeq; YP_004876755.1; NC_016047.1. DR EnsemblBacteria; AEP86123; AEP86123; GYO_1471. DR GeneID; 11239043; -. DR KEGG; bst:GYO_1471; -. DR KO; K10810; -. DR BioCyc; BSUB1052585:GJWW-1460-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 205 AA; 22814 MW; A24AF272A2B61904 CRC64; MELHAITDDC KPVEELTRAI IAIRNEVDFI HIRERSKSAA DILKLLGLIS EGGVDKRKLV MNGRVDIALF STIHRVQLPS SSFSPKQVRA RFPHLHIGRS VHSLEEAVQA EKEDADYVLF GHVFETDCKK GLEGRGVSLL SDIKQRISVP VIAIGGMTPD RLRDVKRAGA DGIAVMSGIF SSADPLEAAR RYSRKLKEMR YEKAL // ID G4NY12_BACPT Unreviewed; 222 AA. AC G4NY12; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-APR-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GYO_4224; OS Bacillus subtilis subsp. spizizenii (strain TU-B-10). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1052585; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TU-B-10; RX PubMed=22493193; DOI=10.1128/JB.05675-11; RA Earl A.M., Eppinger M., Fricke W.F., Rosovitz M.J., Rasko D.A., RA Daugherty S., Losick R., Kolter R., Ravel J.; RT "Whole-genome sequences of Bacillus subtilis and close relatives."; RL J. Bacteriol. 194:2378-2379(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002905; AEP88786.1; -; Genomic_DNA. DR RefSeq; YP_004879418.1; NC_016047.1. DR EnsemblBacteria; AEP88786; AEP88786; GYO_4224. DR GeneID; 11242195; -. DR KEGG; bst:GYO_4224; -. DR KO; K00788; -. DR BioCyc; BSUB1052585:GJWW-4184-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23948 MW; 3DDE5A7C62D0C876 CRC64; MTRISREMMK ELLSVYFIMG SNNTKADPVT VVQKALKGGA TLYQFREKGG DALTGEARIE FAKKVQEACR EAGVPFIVND DVELALKLEA DGIHIGQEDA NAKEVRDAIG DMILGVSTHT MSEVKQAEED GADYVGLGPI YPTETKKDTR AVQGVSLIEA VRRQGIDIPI VGIGGITIEN AAPVIQAGAD GVSMISAISQ AEDPEGAARK FHEEIQTYKT RR // ID G4P8Q1_BACIU Unreviewed; 222 AA. AC G4P8Q1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=I33_3981; OS Bacillus subtilis subsp. subtilis str. RO-NN-1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1052588; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RO-NN-1; RX PubMed=22493193; DOI=10.1128/JB.05675-11; RA Earl A.M., Eppinger M., Fricke W.F., Rosovitz M.J., Rasko D.A., RA Daugherty S., Losick R., Kolter R., Ravel J.; RT "Whole-genome sequences of Bacillus subtilis and close relatives."; RL J. Bacteriol. 194:2378-2379(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002906; AEP92889.1; -; Genomic_DNA. DR RefSeq; YP_005558863.1; NC_017195.1. DR EnsemblBacteria; AEP92889; AEP92889; I33_3981. DR GeneID; 12191572; -. DR KEGG; bsr:I33_3981; -. DR KO; K00788; -. DR BioCyc; BSUB1052588:GL8O-3966-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23768 MW; 85D3696AB23F9497 CRC64; MTRISREMMK ELLSVYFIMG SNNTKADPVT VVQKALKGGA TLYQFREKGG DALTGEARIE FAEKAQAACR EAGVPFIVND DVELALKLKA DGIHIGQEDA NAKEVRAAIG DMILGVSAHT MSEVKQAEED GADYVGLGPI YPTETKKDTR AVQGVSLIEA VRRQGISIPI VGIGGITIDN AAPVIQAGAD GVSMISAISQ AEDPESAARK FREEIQTYKT ER // ID G4PAH2_BACIU Unreviewed; 205 AA. AC G4PAH2; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 22-JAN-2014, entry version 18. DE SubName: Full=Regulatory protein TenI; DE EC=2.5.1.3; GN ORFNames=I33_1300; OS Bacillus subtilis subsp. subtilis str. RO-NN-1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1052588; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RO-NN-1; RX PubMed=22493193; DOI=10.1128/JB.05675-11; RA Earl A.M., Eppinger M., Fricke W.F., Rosovitz M.J., Rasko D.A., RA Daugherty S., Losick R., Kolter R., Ravel J.; RT "Whole-genome sequences of Bacillus subtilis and close relatives."; RL J. Bacteriol. 194:2378-2379(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002906; AEP90270.1; -; Genomic_DNA. DR RefSeq; YP_005556244.1; NC_017195.1. DR EnsemblBacteria; AEP90270; AEP90270; I33_1300. DR GeneID; 12192001; -. DR KEGG; bsr:I33_1300; -. DR KO; K10810; -. DR BioCyc; BSUB1052588:GL8O-1295-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 205 AA; 22943 MW; 1A5D43466543A6E5 CRC64; MELHAITDDS KPVEELARII ITIQNEVDFI HIRERSKSAA DILKLLELIF EGGIDKRKLV MNGRVDIALF STIHRVQLPS GSFSPKQVRA RFPHLHIGRS VHSLEEAVQA EKEDADYVLF GHVFETDCKK GLEGRGVSLL TDIKQRISIP VIAIGGMTPD RLRDVKQAGA DGIAVMSGIF SSAEPLEAAR RYSRKLKEMR YEKAL // ID G4PFG3_BRUML Unreviewed; 203 AA. AC G4PFG3; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 22-JAN-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BMNI_I0210; OS Brucella melitensis NI. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1029825; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI; RX PubMed=23105063; DOI=10.1128/JB.01595-12; RA Liu W., Jing Z., Ou Q., Cui B., He Y., Wu Q.; RT "Complete Genome Sequence of Brucella melitensis Biovar 3 Strain NI, RT Isolated from an Aborted Bovine Fetus."; RL J. Bacteriol. 194:6321-6321(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002931; AEQ07838.1; -; Genomic_DNA. DR RefSeq; YP_005603018.1; NC_017248.1. DR ProteinModelPortal; G4PFG3; -. DR EnsemblBacteria; AEQ07838; AEQ07838; BMNI_I0210. DR GeneID; 12149583; -. DR KEGG; bmw:BMNI_I0210; -. DR KO; K00788; -. DR BioCyc; BMEL1029825:GL9Q-212-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID G4PGK9_BRUML Unreviewed; 221 AA. AC G4PGK9; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BMNI_I1641; OS Brucella melitensis NI. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1029825; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI; RX PubMed=23105063; DOI=10.1128/JB.01595-12; RA Liu W., Jing Z., Ou Q., Cui B., He Y., Wu Q.; RT "Complete Genome Sequence of Brucella melitensis Biovar 3 Strain NI, RT Isolated from an Aborted Bovine Fetus."; RL J. Bacteriol. 194:6321-6321(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002931; AEQ09260.1; -; Genomic_DNA. DR RefSeq; YP_005604447.1; NC_017248.1. DR ProteinModelPortal; G4PGK9; -. DR EnsemblBacteria; AEQ09260; AEQ09260; BMNI_I1641. DR GeneID; 12150395; -. DR KEGG; bmw:BMNI_I1641; -. DR KO; K00788; -. DR BioCyc; BMEL1029825:GL9Q-1673-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23242 MW; 9838EBF5FD9C7A47 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAIEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID G4Q234_ECOLX Unreviewed; 211 AA. AC G4Q234; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CE10_4673; OS Escherichia coli O7:K1 str. CE10. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1072459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CE10; RX PubMed=22123760; DOI=10.1128/JB.06284-11; RA Lu S., Zhang X., Zhu Y., Kim K.S., Yang J., Jin Q.; RT "Complete Genome Sequence of the Neonatal-Meningitis-Associated RT Escherichia coli Strain CE10."; RL J. Bacteriol. 193:7005-7005(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003034; AEQ15348.1; -; Genomic_DNA. DR RefSeq; YP_006146634.1; NC_017646.1. DR ProteinModelPortal; G4Q234; -. DR EnsemblBacteria; AEQ15348; AEQ15348; CE10_4673. DR GeneID; 12677469; -. DR KEGG; eoc:CE10_4673; -. DR KO; K00788; -. DR BioCyc; ECOL1072459:GLD5-4664-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23138 MW; C625E6545C9DF5D0 CRC64; MYQPDFPHVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLDAIRT AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLVDYP TVAIGGISLP RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGAGD E // ID G4Q5C7_ACIIR Unreviewed; 205 AA. AC G4Q5C7; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=Acin_2105; OS Acidaminococcus intestini (strain RyC-MR95). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=568816; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RyC-MR95; RX PubMed=22123762; DOI=10.1128/JB.06301-11; RA D'Auria G., Galan J.C., Rodriguez-Alcayna M., Moya A., Baquero F., RA Latorre A.; RT "Complete Genome Sequence of Acidaminococcus intestini RYC-MR95, a RT Gram-Negative Bacterium from the Phylum Firmicutes."; RL J. Bacteriol. 193:7008-7009(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003058; AEQ23305.1; -; Genomic_DNA. DR RefSeq; YP_004897445.1; NC_016077.1. DR ProteinModelPortal; G4Q5C7; -. DR EnsemblBacteria; AEQ23305; AEQ23305; Acin_2105. DR GeneID; 11265748; -. DR KEGG; ain:Acin_2105; -. DR KO; K00788; -. DR BioCyc; AINT568816:GHMB-2095-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 22587 MW; 6033630CB147FF90 CRC64; MNASFPYVLV TDRTIYPEPL IPYLKKRIPD LSPFPSALIL REKDLSKEAY EDLFKETAHL CKAWKLPLLA HNHPDLALDD AIAGVHMPLR SWTAWSKMHP QEAGCLLEKG KTKLPYPHGV GISIHFLSEV ETALQSGASY LIVSPLFPTS CKPNNLPLGL TPLPNFIHSS PLPIYVLGGL SWPDPRASLL EALGVRGAVI RSAIV // ID G4Q8K7_ACIIR Unreviewed; 215 AA. AC G4Q8K7; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Acin_0393; OS Acidaminococcus intestini (strain RyC-MR95). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=568816; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RyC-MR95; RX PubMed=22123762; DOI=10.1128/JB.06301-11; RA D'Auria G., Galan J.C., Rodriguez-Alcayna M., Moya A., Baquero F., RA Latorre A.; RT "Complete Genome Sequence of Acidaminococcus intestini RYC-MR95, a RT Gram-Negative Bacterium from the Phylum Firmicutes."; RL J. Bacteriol. 193:7008-7009(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003058; AEQ21636.1; -; Genomic_DNA. DR RefSeq; YP_004895776.1; NC_016077.1. DR ProteinModelPortal; G4Q8K7; -. DR EnsemblBacteria; AEQ21636; AEQ21636; Acin_0393. DR GeneID; 11265194; -. DR KEGG; ain:Acin_0393; -. DR KO; K00788; -. DR BioCyc; AINT568816:GHMB-393-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22985 MW; 6EE00CC7C93FDFBF CRC64; MKRTIDYSLY LVTDRKVTDK KGRDFYEAVE EALQAGITLV QLREKDVTTE ERIAIGRKVK ILCDHYDVPL LVDDDIACAK AIGADGVHLG QSDESLARGR QELGNDAIIG ISAHNLEEAQ AALRGGADYL GVGALYPTET KKDASCLGLG PFREIIAAIS LPIVGIGGIG KKEFPEVMKC GAAGCAMISS ILGAEDITAT VKAMKMAYEA LRKGE // ID G4QA63_TAYAM Unreviewed; 213 AA. AC G4QA63; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-APR-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=TASI_1396; OS Taylorella asinigenitalis (strain MCE3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Taylorella. OX NCBI_TaxID=1008459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MCE3; RA Hebert L., Moumen B., Pons N., Duquesne F., Breuil M.-F., Goux D., RA Batto J.-M., Renault P., Laugier C., Petry S.; RT "Genomic characterization of the Taylorella genus."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCE3; RX PubMed=22235352; DOI=10.1371/journal.pone.0029953; RA Hebert L., Moumen B., Pons N., Duquesne F., Breuil M.F., Goux D., RA Batto J.M., Laugier C., Renault P., Petry S.; RT "Genomic characterization of the Taylorella genus."; RL PLoS ONE 7:E29953-E29953(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003059; AEP37136.1; -; Genomic_DNA. DR RefSeq; YP_004875159.1; NC_016043.1. DR EnsemblBacteria; AEP37136; AEP37136; TASI_1396. DR GeneID; 11186407; -. DR KEGG; tas:TASI_1396; -. DR KO; K00788; -. DR BioCyc; TASI1008459:GH5G-1391-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23894 MW; A5910D1B5B64581F CRC64; MTIPKGLYGI TPDWDNFDKV IEAVRVACEA GLPILQFRRK KEEPYKLRLE QCKRIRDICL RENTLFIVND SIQLAMDSQA DGVHLGREDI VYRDIATTYA LERGNFVIGY SCYNSLDMAR DAVKNGASYI AFGAMYPSPT KPNAVKADTN LIKEAKKEFV DIPIVCIGGI TLQNALPLIE AGADNVAVIT GLFESEDIAK AVREFKNLFE HWK // ID G4QDH1_TAYAM Unreviewed; 336 AA. AC G4QDH1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-APR-2014, entry version 18. DE SubName: Full=Putative mutator mutt protein; GN OrderedLocusNames=TASI_0197; OS Taylorella asinigenitalis (strain MCE3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Taylorella. OX NCBI_TaxID=1008459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MCE3; RA Hebert L., Moumen B., Pons N., Duquesne F., Breuil M.-F., Goux D., RA Batto J.-M., Renault P., Laugier C., Petry S.; RT "Genomic characterization of the Taylorella genus."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCE3; RX PubMed=22235352; DOI=10.1371/journal.pone.0029953; RA Hebert L., Moumen B., Pons N., Duquesne F., Breuil M.F., Goux D., RA Batto J.M., Laugier C., Renault P., Petry S.; RT "Genomic characterization of the Taylorella genus."; RL PLoS ONE 7:E29953-E29953(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003059; AEP35988.1; -; Genomic_DNA. DR RefSeq; YP_004874011.1; NC_016043.1. DR ProteinModelPortal; G4QDH1; -. DR EnsemblBacteria; AEP35988; AEP35988; TASI_0197. DR GeneID; 11186662; -. DR KEGG; tas:TASI_0197; -. DR KO; K03574; -. DR BioCyc; TASI1008459:GH5G-197-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 336 AA; 37861 MW; 4850B9133C4C8E15 CRC64; MSEEKPFFNV SACVLIDSEG RFLMAQRPED KSWSGWWEFP GGKIEEGESP KEAVIRELRE ELGVELDPES TYPWVTMSYE YPKTDVLLHF YRCFKWSGEL RSLEKQAFEW FTQMPTDRDL LPASVEPIEW LSYGDVYLIS NFFDSNEGAG VGHGAGQAPR ETAFWAKLTA ALEAGVRLVQ FREPAAAKVL KTEELKRYLD EMREHCHRYG AKVLVNSCHP RAWAEEADGL HLRATDAIEM ELEDMPESGL LAVSCHNLAD LLYAHELGAN FVVLGHVLET ASHPDSEPIG WSQFEQWAAE SAIPVFAIGG QNADTFREAL RHGAHGIAVL RGEITE // ID G4R9V7_PELHB Unreviewed; 191 AA. AC G4R9V7; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-APR-2014, entry version 16. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=KKY_2476; OS Pelagibacterium halotolerans (strain JCM 15775 / CGMCC 1.7692 / B2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Pelagibacterium. OX NCBI_TaxID=1082931; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 15775 / CGMCC 1.7692 / B2; RX PubMed=22156395; DOI=10.1128/JB.06343-11; RA Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., RA Zhu X.F., Liu Y.F., Li P.F., Ni P.X., Wu M.; RT "Complete Genome Sequence of Pelagibacterium halotolerans B2T."; RL J. Bacteriol. 194:197-198(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003075; AEQ52484.1; -; Genomic_DNA. DR RefSeq; YP_004900234.1; NC_016078.1. DR EnsemblBacteria; AEQ52484; AEQ52484; KKY_2476. DR GeneID; 11344007; -. DR KEGG; phl:KKY_2476; -. DR KO; K00788; -. DR BioCyc; PHAL1082931:GJXT-2471-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 191 AA; 20874 MW; 41CB1DD54ADFF490 CRC64; MAAKGSETDW GTMAEIFLIA EPELSVGRLE ATLARLPAAA LLLKAGEEDD FAYTDRAKTL AKIAQKTNCA VLLDNRPHLV RKAYVDGVHM SGGIKALREA IEELKPDFIV GTGDIGSRHE AMTRGELEID YLMFGDRDDI EGREMADWWA ETFEVPSVYC ADGTQDLSGL KCEFVAFTQA NWDNAAPGDA S // ID G4ST11_META2 Unreviewed; 208 AA. AC G4ST11; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 19-FEB-2014, entry version 20. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MEALZ_1027; OS Methylomicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM OS B-2133 / 20Z). OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomicrobium. OX NCBI_TaxID=1091494; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z; RX PubMed=22207753; DOI=10.1128/JB.06392-11; RA Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., RA Lajus A., Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., RA Dispirito A.A., Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., RA Barbe V., Medigue C., Trotsenko Y.A., Kalyuzhnaya M.G.; RT "Genome sequence of the haloalkaliphilic methanotrophic bacterium RT Methylomicrobium alcaliphilum 20Z."; RL J. Bacteriol. 194:551-552(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO082060; CCE22721.1; -; Genomic_DNA. DR RefSeq; YP_004916315.1; NC_016112.1. DR GeneID; 11361332; -. DR KEGG; mah:MEALZ_1027; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22083 MW; AF9D5718511CB373 CRC64; MNMPKRGLYA ITQTDDKTVE TIIEEVAAAI RGGAVMVQYR DKNPSDTLKL AKALLETCHA ANVPLIVNDD IELAATIGAD GVHLGKDDED IVIARHRLGV NAIVGISCYD SIERALEAEK LGASYAAFGR FFASGTKPLA SPAKLETLQL AKHKLTIPIV AIGGILPENG NLLIDAGADL LAVVGGLYGR DTEQSAKMLN SLFERSNS // ID G4SYG0_META2 Unreviewed; 312 AA. AC G4SYG0; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 11-DEC-2013, entry version 20. DE SubName: Full=Mutator MutT protein; GN OrderedLocusNames=MEALZ_0462; OS Methylomicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM OS B-2133 / 20Z). OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomicrobium. OX NCBI_TaxID=1091494; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z; RX PubMed=22207753; DOI=10.1128/JB.06392-11; RA Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., RA Lajus A., Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., RA Dispirito A.A., Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., RA Barbe V., Medigue C., Trotsenko Y.A., Kalyuzhnaya M.G.; RT "Genome sequence of the haloalkaliphilic methanotrophic bacterium RT Methylomicrobium alcaliphilum 20Z."; RL J. Bacteriol. 194:551-552(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO082060; CCE22161.1; -; Genomic_DNA. DR RefSeq; YP_004915760.1; NC_016112.1. DR ProteinModelPortal; G4SYG0; -. DR GeneID; 11361705; -. DR KEGG; mah:MEALZ_0462; -. DR KO; K03574; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 312 AA; 33768 MW; D8C6D42350589B44 CRC64; MKSVLEVAVG AVVDRHGKIL IAKRPDDKHQ GGLWEFPGGK IEPGETQRQA LDRELHEELA IDVKTATPLI TIHHDYPDLS VRLKVWRIDR FEGDPHGREG QAVEWVAPTD LQNYSFPAAN RPIVTALRLP PFYAILDDST PSALFSNLKT ILANGIKLIQ LRLKKVTAGE AAEFIARILP LCRRHGASVL LNSAVSGIEA SAIDGIHLTG KDLMALRERP DSQGWLAASC HNEAELRHAE TVGVDFAVLA PVLPTATHPG ARILGWQGFT ALAETANIPV FGLGGLAKDD LARVREAGGQ GVAGIRAFIE TE // ID G4UQP9_NEUT9 Unreviewed; 523 AA. AC G4UQP9; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-APR-2014, entry version 13. DE SubName: Full=TMP-TENI-domain-containing protein; GN ORFNames=NEUTE2DRAFT_110869; OS Neurospora tetrasperma (strain FGSC 2509 / P0656). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; OC Neurospora. OX NCBI_TaxID=510952; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=strain FGSC 2509 / P0656; RX PubMed=21750257; DOI=10.1534/genetics.111.130690; RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A., RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., RA Taylor J.W.; RT "Massive changes in genome architecture accompany the transition to RT self-fertility in the filamentous fungus Neurospora tetrasperma."; RL Genetics 189:55-69(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL891236; EGZ71853.1; -; Genomic_DNA. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 523 AA; 56001 MW; 0C68ED5B4AA9A45E CRC64; MDRNNVNYAV YLVTDSTPAI LGDRDLCEVV EASVRGGTTI VQLREKTSDT GDMIAMGKKL HAITKKYNVP LLINDRVDVA LAVGCEGVHI GQDDMELSTA RRLLGPDAII GVTVSTIQEA MVACKGGADY LGIGTVYATP TKTNTKNIIG AAGVRDILQA MADAGYDHVR TVCIGGINAE NLQRIVYQSE APSKKLDGVA VVSALVAAPD PEAAAKNLLG LFNSQPPFVR ESTSPRAETA DSILELVPEV VLEVARKKPL SHNMTNLVVQ NFAANVALAI GASPIMANNG EEAFDLCKLG GALVVNMGTV DPDGLQNYLK ALRAYNSVGQ PVVYDPVGAG ATTLRRSAVK TILSHGYLDI IKGNEGEIRT VYGIYERETF QQRGVDSSAE LEVSQKAELV RKLALREKNV VVMTGEIDYL SDGQHTFRID NGHAYLEMVT GTGCVLGTTI SAFVAAFPND KLAATVAALL HFEIAAERAA ERRDVQGPGT FVPAFLDELF KIRRETGQGR MGWLKSAKLT RLS // ID G5ESQ2_9MICC Unreviewed; 206 AA. AC G5ESQ2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0737_01312; OS Rothia mucilaginosa M508. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Rothia. OX NCBI_TaxID=563033; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M508; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R., RA Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Rothia mucilaginosa M508."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACSB01000010; EHB87761.1; -; Genomic_DNA. DR EnsemblBacteria; EHB87761; EHB87761; HMPREF0737_01312. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). SQ SEQUENCE 206 AA; 22021 MW; 792C086CA84A0BB4 CRC64; MTRETHPYTT PARPLDLNLY LVTGDNPLET VRAAKNATCI QVRSKPISAR ELYQLTEAIA GIIQPHQTLL IDDRVDVALA LRARGVRVDG VHIGQDDLPV ADARALLGAD AIIGLTTGTR QLVEESNKIA HLIDYIGTGP FRPSPTKQSN RPPLGIDGLR ELAELSAVPT VAIGDITPED CPAIRTTGVA GIAMVRAFVD NPALKA // ID G5EVR1_9ACTO Unreviewed; 217 AA. AC G5EVR1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1003_00581; OS Propionibacterium sp. 5_U_42AFAA. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=450748; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_U_42AFAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C., RA Ambrose C.E., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Propionibacterium sp. 5_U_42AFAA."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACUE01000004; EHC27545.1; -; Genomic_DNA. DR ProteinModelPortal; G5EVR1; -. DR EnsemblBacteria; EHC27545; EHC27545; HMPREF1003_00581. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22340 MW; 2EAFC189E7C2BDCB CRC64; MTLDLRCYLV TSGTGRHTVE TAAAAAGAGA GMVQVRAKEL STRDLFSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPAL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID G5EZA5_9ACTO Unreviewed; 216 AA. AC G5EZA5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1003_01383; OS Propionibacterium sp. 5_U_42AFAA. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=450748; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_U_42AFAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C., RA Ambrose C.E., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Propionibacterium sp. 5_U_42AFAA."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACUE01000007; EHC26330.1; -; Genomic_DNA. DR ProteinModelPortal; G5EZA5; -. DR EnsemblBacteria; EHC26330; EHC26330; HMPREF1003_01383. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID G5F6C3_9CLOT Unreviewed; 227 AA. AC G5F6C3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1020_00019; OS Clostridium sp. 7_3_54FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=665940; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_3_54FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium sp. 7_3_54FAA."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWK01000001; EHF07920.1; -; Genomic_DNA. DR EnsemblBacteria; EHF07920; EHF07920; HMPREF1020_00019. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 24054 MW; 7E38C435A61D5E9E CRC64; MKFTKEEIHK SMLLYAVTDR MWLNEGETLI SVAEEVLKNG ATFLQIREKD LNEDDFEAEA EALHTLCAKY RIPFVVNDSV EIALRCNADG VHVGQSDIKG RDIRALIGPD AILGISAGTV QEAEAAEAAG ADYIGVGAVF TTGTKKDARS LTMEQLRAIR NAVSIPIVAI GGINSGNIMR LAGSGVDGVA VVSAIFAAPH PGEATAGMLK LAEEMLSAKT VRGEGNE // ID G5FL79_9PSED Unreviewed; 209 AA. AC G5FL79; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1030_00232; OS Pseudomonas sp. 2_1_26. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=665948; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_26; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Pseudomonas sp. 2_1_26."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWU01000003; EHF15981.1; -; Genomic_DNA. DR ProteinModelPortal; G5FL79; -. DR SMR; G5FL79; 24-200. DR EnsemblBacteria; EHF15981; EHF15981; HMPREF1030_00232. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22146 MW; 898DA261D0AFA265 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER HGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAQ LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID G5G074_9PSED Unreviewed; 150 AA. AC G5G074; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-MAR-2014, entry version 11. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF1030_05127; OS Pseudomonas sp. 2_1_26. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=665948; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_26; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Pseudomonas sp. 2_1_26."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWU01000205; EHF11025.1; -; Genomic_DNA. DR EnsemblBacteria; EHF11025; EHF11025; HMPREF1030_05127. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 150 AA; 15908 MW; AC3461117A0D07D5 CRC64; MFSPEYRDLA IDIQGLCAGK AQLMLKGPLE WLGDFPAAGW HLTSAQLRKY ASAGRPFPEG RLLAASCHDA EELALAASMG VEFVTLSPVQ PTESHPGEPA LGWDKAAELI AGFNQPVYLL GGVGPQQAEQ AWEHGAQGVA GIRAFWPGGL // ID G5G793_AGGAP Unreviewed; 220 AA. AC G5G793; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9335_01547; OS Aggregatibacter aphrophilus F0387. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=679198; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0387; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A., RA Blanton J.M., Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Aggregatibacter aphrophilus F0387."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZJ01000013; EHB89710.1; -; Genomic_DNA. DR ProteinModelPortal; G5G793; -. DR EnsemblBacteria; EHB89710; EHB89710; HMPREF9335_01547. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 49 53 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24139 MW; 6068529F0E0FE2F8 CRC64; MPTSVSHLAE IVPPNAPFAP TEFKLGLYVI VDSYEWIERL IHAGVKTLQI RIKDRSPEQA KEEIARCIAL AKQHQVRLFV DDFWQLAIKY QSYGVHLGQE DLLTADLNAI QQAGLRLGVS THNREEIELV LPLRPSYIAL GHIFPTQSKI MPSAPQGIAN LAAQVKDLGD IPTVAIGGIT VSHFADVLTT GVGSIAVISA VTQAEDWQSA VQNLLHYFDA // ID G5G9R9_9BACT Unreviewed; 198 AA. AC G5G9R9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 13-NOV-2013, entry version 11. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF9332_00320; OS Alloprevotella rava F0323. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Alloprevotella. OX NCBI_TaxID=679199; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0323; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M., RA Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella sp. oral taxon 302 str. F0323."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZK01000010; EHG24119.1; -; Genomic_DNA. DR EnsemblBacteria; EHG24119; EHG24119; HMPREF9332_00320. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 198 AA; 23096 MW; CD943D58B0EA5497 CRC64; MKIVLMTTPF FFVEESQILT ALFDEGLELL HLRKPDTEPV FSERLLSLIP ESYHRRIVTH DHFYLKNEYG LRGVHLNGRN LELPDGFKGT ISCSCYTVDE TEARRRKMDY VFLQSTDFNV PESREASWGL LEDAAHQMSE KELKKVYVSG GITLDDLPRL RSLGFGGAVV YGDIWNRFNI YSQQDYRELI LHFRKLLK // ID G5GF04_9FIRM Unreviewed; 219 AA. AC G5GF04; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9333_00142; OS Johnsonella ignava ATCC 51276. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Johnsonella. OX NCBI_TaxID=679200; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51276; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M., RA Baranova O.V., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Johnsonella ignava ATCC 51276."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZL01000003; EHI56695.1; -; Genomic_DNA. DR EnsemblBacteria; EHI56695; EHI56695; HMPREF9333_00142. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24223 MW; ED9FD65A03771DA5 CRC64; MIFKKGMIYA IADISGNEDE CCSEYKENFF YKVEEALKGG TEIIQLRYKS PYSQELLYEY AMKLCELTHR YSAMFIVNDY VELAKKTGAD GVHIGQEDIK KTGIVYTRNS LHDGAVIGVT AKTVSDAKKA RQLGADYIGS GAIFKTDTKA DAQSMDIDEL KDICTQLDIP VFAIGGIDIS NVNRLKGVPI TGIAVSRGIF AAKDIRLQVL KLKEAMLKL // ID G5GI57_9FIRM Unreviewed; 242 AA. AC G5GI57; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-MAR-2014, entry version 11. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF9333_01247; OS Johnsonella ignava ATCC 51276. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Johnsonella. OX NCBI_TaxID=679200; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51276; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M., RA Baranova O.V., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Johnsonella ignava ATCC 51276."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZL01000021; EHI55532.1; -; Genomic_DNA. DR EnsemblBacteria; EHI55532; EHI55532; HMPREF9333_01247. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 242 AA; 27891 MW; EDD066B44DEF8204 CRC64; MSEIVCITNR HLYKNKEGCI RLYGDIDSGD THSILKNTLY KSEEDILTYN LLSRVRLWIK CRVDKIILRE KDLEVSGYIE LAEKVLKLCK GTDTECILHN FADAAAVFDC KRIHFPLDML YRQPQSRLEG YEMMGVSLHS ADEIKDLEDY INKVHIKKEN VYINAGHIFE TKCKEGLSAR GVDFLRDICE KSPWKVYAIG GINKDNWKVA LDAGAYGVCL MSSAMQYEEN TFLKLCDDIH KY // ID G5GLH6_9FIRM Unreviewed; 228 AA. AC G5GLH6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9334_00106; OS Selenomonas infelix ATCC 43532. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=679201; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43532; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M., RA Baranova O.V., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Selenomonas infelix ATCC 43532."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZM01000002; EHG22479.1; -; Genomic_DNA. DR EnsemblBacteria; EHG22479; EHG22479; HMPREF9334_00106. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 206 207 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 186 186 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 23965 MW; 6CAA469A3A40271E CRC64; MRTKIDLSAY LVIGPENTSG RPVARVIAEA VRAGFTFVQI RAKGVDAREV IELTRAAADV IATQEKSDAV ALVMNDRLDC VLAAREQGIK VDGVHVGQTD IPVDVCRKYL GADAIVGLSA RTTELLDYVA HCDTACIDYL GAGPLHVTPT KPEAGRTASG EIVTRSLDEL AALHRISPVP VVVGGGVKAA DLPALRATGV EGFFVISAVA GAEHPYSAAE ELVRLWSA // ID G5GU97_FUSNP Unreviewed; 206 AA. AC G5GU97; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 2. DT 13-NOV-2013, entry version 12. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF9369_01017; OS Fusobacterium nucleatum subsp. polymorphum F0401. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=693991; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0401; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A., RA Blanton J.M., Baranova O.V., Ann Y.W., Finegold S., Dewhirst F.E., RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium nucleatum subsp. polymorphum RT F0401."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADDB02000001; EHG19440.2; -; Genomic_DNA. DR ProteinModelPortal; G5GU97; -. DR EnsemblBacteria; EHG19440; EHG19440; HMPREF9369_01017. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 23932 MW; D80B78263413E9F8 CRC64; MIENKIKLNI ISNRKLCENE NLEKQIEKIF SAYQRKIILE NFEIVSLTLR EKDLNKNKYL KLVEKIYPIC QKYRIDLILH QNYDLRLDNK YNIKGLHLSY NTFKSLNKNI REELIRKYKK IGVSIHSVDE AKEVENLGAN YVVAGHIFKT DCKKALEPRG LKFIQELSVI LTIPIFAIGG INQENSHLVI NSGAFGVCMM SSLMKD // ID G5GUA3_FUSNP Unreviewed; 206 AA. AC G5GUA3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 2. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9369_01023; OS Fusobacterium nucleatum subsp. polymorphum F0401. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=693991; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0401; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A., RA Blanton J.M., Baranova O.V., Ann Y.W., Finegold S., Dewhirst F.E., RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium nucleatum subsp. polymorphum RT F0401."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADDB02000001; EHG19446.2; -; Genomic_DNA. DR ProteinModelPortal; G5GUA3; -. DR EnsemblBacteria; EHG19446; EHG19446; HMPREF9369_01023. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. SQ SEQUENCE 206 AA; 22821 MW; DD796D41845C55F1 CRC64; MKLKDCKIYL VTDEKACSGK DFYKCIEESI KGGVKIVQLR EKNISTKDFY EKALKVKEIC KNYGVLFIIN DRLDITQAVE ADGVHLGQSD MPIEKAREIL KDKFLIGATA KNIEEAKKAE LLGADYIGSG AIFGTSTKDN AKKLEIEDLK KIVNSVKIPV FAIGGININN VWMLKNIGLQ GICSVSGILS EKDCKKAVEN ILKNFN // ID G5H2A1_9FIRM Unreviewed; 230 AA. AC G5H2A1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9432_01048; OS Selenomonas noxia F0398. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=702437; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0398; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A., RA Blanton J.M., Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Selenomonas noxia F0398."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGH01000008; EHG25018.1; -; Genomic_DNA. DR EnsemblBacteria; EHG25018; EHG25018; HMPREF9432_01048. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 208 209 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 24557 MW; 1348AB0F58871426 CRC64; MSMRHQFDLS SYLVIGPENT NGRPVAHIIA EALRAGFTFV QIRAKHAEAA EIIRLARAAA DAIAGQKKSD EVALVINDRL DVVLAARELR IKVDGVHVGQ EDIPPAVCRK YLGVNAVIGL SARTSDLINY VESCDTSCID YFGAGPLHAT ATKPDAGMDQ NGKIVTRSLD ELRALHRVSP LPVVVGGGVK ADDLPALRAT GVDGFFVVSA VAGAEHPYTA AKELVRCWHS // ID G5H5B1_9BACT Unreviewed; 504 AA. AC G5H5B1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF9450_00121; OS Alistipes indistinctus YIT 12060. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes. OX NCBI_TaxID=742725; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12060; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Alistipes indistinctus YIT 12060."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLD01000003; EHB93350.1; -; Genomic_DNA. DR EnsemblBacteria; EHB93350; EHB93350; HMPREF9450_00121. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 3. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 504 AA; 53750 MW; 3B30BD65FFA97CE9 CRC64; MDTPLHFPLG KPVAITLPRC YDGEAEALCA LLDAGAPVIH IRKPDAPAAQ VEALLRQLRD AGADMTRLTL HHDAALARRY GLGGIHLREG ALREWLRQHP DKRHATAQGA SAPDVQKTQT QQTQQGNDTY TPRLSAPAHS WEEAARLAPL CDYVTLSPLF DSVSKPGYLA GIDPADACRR LRRRTDETAK PIPAAIPAEL PVSGSGSRII ALGGITPDNI SVARAAAFDG AAVIGAVWTT EWLGTGPQPD PKNSDRTPSP GNRPPAGTPS HDISRIDLTA TLSNYQRLTR RWQAAGGTLQ FISDGDPAAA EAFLQGGGRW VQLRMKDTPA EGIIARGREI LALCRRYDAL LIVNDDPRLA KAIGADGVHL GQNDTPPDEA RIILGRQAII GCTANTFAHI ARIAQSSADY IGLGPFRYTT TKKNLSPILG EEGYRRILRQ MARAGIRLPV AAIGGITEED VPQVMACGVN GIALSGAISR AGEIAAATAR FTELVAAHRT IVTP // ID G5HHD7_9CLOT Unreviewed; 184 AA. AC G5HHD7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-MAR-2014, entry version 11. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF9469_01781; OS Clostridium citroniae WAL-17108. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=742733; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-17108; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., RA Summanen P.H., Molitoris D.R., Vaisanen M.L., Daigneault M., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Clostridium citroniae WAL-17108."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLJ01000014; EHE99212.1; -; Genomic_DNA. DR EnsemblBacteria; EHE99212; EHE99212; HMPREF9469_01781. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 184 AA; 19988 MW; 386710A5EE6B5D2A CRC64; MAVSNRSLCT RPFMDQVRRI CCFHPAALVL REKDMDEADY ESMAREVLKL CASYQVPCIL HTFTEAAHIL GADGIHLPLW KLREAAEKKQ LDGFTTIGVS VHAANEALEA QSLGATYLTA GHIYATDCKK GLPPRGTAFL REICQTVSIP VYAIGGIRLE AAQIREVMSC GAVGGCIMSG MMAL // ID G5HMI5_9CLOT Unreviewed; 225 AA. AC G5HMI5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9469_03916; OS Clostridium citroniae WAL-17108. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=742733; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-17108; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., RA Summanen P.H., Molitoris D.R., Vaisanen M.L., Daigneault M., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Clostridium citroniae WAL-17108."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLJ01000030; EHE97261.1; -; Genomic_DNA. DR EnsemblBacteria; EHE97261; EHE97261; HMPREF9469_03916. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 24179 MW; AB32E6766F8C314A CRC64; MRFHKDQLLI YAVTDRAWTG GRSLCGQVEE ALKGGATMVQ FREKSLEKKN FDQILGEAKA LRELTQRYHV PLIIDDNMDL AEACNADGLH VGQDDMDAQA ARRILGPDRI LGVTAKTVEQ ALRAQAQGAD YLGSGAVFGT TTKADARPMT METLREICDS VDIPVVAIGG INLGNIGQLS GSHVAGAAIV SGIFAAEDIC GTTQCLVEEM KKSLNLFPKT VDNSK // ID G5HY65_9CLOT Unreviewed; 226 AA. AC G5HY65; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9467_01448; OS Clostridium clostridioforme 2_1_49FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=742735; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_49FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Clostridium clostridioforme 2_1_49FAA."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLL01000025; EHG32809.1; -; Genomic_DNA. DR EnsemblBacteria; EHG32809; EHG32809; HMPREF9467_01448. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24077 MW; 110E965D37A75BDB CRC64; MRFDRKQLLI YAVTDKAWTG KLSLEEQVEE ALKGGATMVQ LREKELDKGN FEEVLRTACA IRKITEKYNV PLIIDDNLEL ALACHADGLH VGQDDMEASE ARRLLGPDRI LGVTAKTVDQ ARAAQAAGAD YLGSGAIFGT STKADARPMT METLNAICDS VDIPVVAIGG ICLDNIGRLA GSHAAGAAIV SGIFGAPNIR ETTEKLAEAM TEIAGLPRRD LRAGSV // ID G5IKM5_9CLOT Unreviewed; 209 AA. AC G5IKM5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9473_04053; OS Clostridium hathewayi WAL-18680. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=742737; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-18680; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., RA Summanen P.H., Molitoris D.R., Song M., Daigneault M., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Clostridium hathewayi WAL-18680."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLN01000112; EHI57957.1; -; Genomic_DNA. DR EnsemblBacteria; EHI57957; EHI57957; HMPREF9473_04053. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22245 MW; 29415501AAB9652A CRC64; MKPDYILYLV TDRRAMSTRT LAEAVEQAIA GGCTMVQLRE AETSALEFYQ LAVDIKAVTD RHHIPLIINN RIDIALAIRA AGVHLGQNDI PTAAARRIIG PNMLLGISVT TTAQALKAQA EGADYLGVGA MFPTRTKPDA SIVSMEELRS IRSAVSLPIV AIGGITPANA PQFHAAHVDG LAVVSAILSK PDIEAAAREL KQAFGQITR // ID G5J562_CROWT Unreviewed; 369 AA. AC G5J562; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CWATWH0003_2627; OS Crocosphaera watsonii WH 0003. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Crocosphaera. OX NCBI_TaxID=423471; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 0003; RX PubMed=22232617; RA Bench S.R., Ilikchyan I.N., Tripp H.J., Zehr J.P.; RT "Two Strains of Crocosphaera watsonii with Highly Conserved Genomes RT are Distinguished by Strain-Specific Features."; RL Front. Microbiol. 2:261-261(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESD01000384; EHJ12701.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ12701; EHJ12701; CWATWH0003_2627. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 152 Unknown (By similarity). FT REGION 153 369 Thiamine-phosphate synthase (By FT similarity). FT REGION 200 204 HMP-PP binding (By similarity). FT REGION 297 299 THZ-P binding (By similarity). FT METAL 233 233 Magnesium (By similarity). FT METAL 252 252 Magnesium (By similarity). FT BINDING 232 232 HMP-PP (By similarity). FT BINDING 271 271 HMP-PP (By similarity). FT BINDING 300 300 HMP-PP (By similarity). FT BINDING 327 327 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 369 AA; 41649 MW; B4E76E755C744E90 CRC64; MRYFNKFAPF SKHFYKQDAC ATFLAKKAQK NMDKNLAIAR ILDANLDRAR EGLRVVEEWC RLGLENSDCT DKCKQMRQEI AHWHTSDLRK ARDTINDPGT DLSHPQEAIR ENIEQLLQAN LCRVQEALRV LEEYGKLYDP NMGNAFKKIR YQVYILESEL LQSYRYKKLI NASLYLVTSS TKNLLKTVES ALQGGLTLVQ YRKKDVDDII RLEMAQKLSE LCHKYDALFI VNDRADIALE VNADGVHLGQ QDIPISLARR ILGPNKIIGR STTNPQEMAK AIAEKADYIG VGPVYATPTK PDKQAAGLDY VKYAAQHSPI PWFAIGGIDE HNVTEVIASG ATQVALVRAI MEADNPQKTT AKLLKKLKG // ID G5JKX5_9STAP Unreviewed; 214 AA. AC G5JKX5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SS7213T_10684; OS Staphylococcus simiae CCM 7213. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=911238; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCM 7213; RX PubMed=22272658; DOI=10.1186/1471-2164-13-38; RA Suzuki H., Lefebure T., Pavinski Bitar P., Stanhope M.J.; RT "Comparative genomic analysis of the genus Staphylococcus including RT Staphylococcus aureus and its newly described sister species RT Staphylococcus simiae."; RL BMC Genomics 13:38-38(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUN01000494; EHJ07180.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ07180; EHJ07180; SS7213T_10684. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23680 MW; C98E354D633A7A25 CRC64; MTFSPNMLQV YFICGTQDVR QDTTLTNVLT EALEAGITLF QFREKGDKAL KGDDKEHLAL ELKHLCHQFK VPFIVNDDVE LALRINADGI HVGQDDDTIS TFIERFDDKI IGLSISDEQE YQHSDLSEVD YIGVGPMYDT PSKKDAHPPV GPAMITKLKS YNSHMPIVAI GGITVANTQN IVKAGADGIS VISAISKSDN ITQTVKDFRS YFNN // ID G5KVG0_ECOLX Unreviewed; 211 AA. AC G5KVG0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=i01_05706; OS Escherichia coli cloneA_i1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=993513; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CloneA_i1; RX PubMed=22046404; DOI=10.1371/journal.pone.0026907; RA Reeves P.R., Liu B., Zhou Z., Li D., Guo D., Ren Y., Clabots C., RA Lan R., Johnson J.R., Wang L.; RT "Rates of Mutation and Host Transmission for an Escherichia coli Clone RT over 3 Years."; RL PLoS ONE 6:E26907-E26907(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYT01000047; EHF98540.1; -; Genomic_DNA. DR ProteinModelPortal; G5KVG0; -. DR SMR; G5KVG0; 9-208. DR EnsemblBacteria; EHF98540; EHF98540; i01_05706. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G5LHA9_SALET Unreviewed; 211 AA. AC G5LHA9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSEADE_5700; OS Salmonella enterica subsp. enterica serovar Adelaide str. A4-669. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913063; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-669; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCI01001889; EHC29173.1; -; Genomic_DNA. DR EnsemblBacteria; EHC29173; EHC29173; LTSEADE_5700. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22756 MW; F061173B20F12175 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHNA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE CAPAVLATGV GSVAVVSAIT QAADWRAATA QLLAIAGVGD E // ID G5LWP2_SALET Unreviewed; 193 AA. AC G5LWP2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSEALA_5796; OS Salmonella enterica subsp. enterica serovar Alachua str. R6-377. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913241; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R6-377; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCJ01002460; EHC29366.1; -; Genomic_DNA. DR EnsemblBacteria; EHC29366; EHC29366; LTSEALA_5796. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 19 23 HMP-PP binding (By similarity). FT REGION 116 118 THZ-P binding (By similarity). FT REGION 168 169 THZ-P binding (By similarity). FT METAL 52 52 Magnesium (By similarity). FT METAL 71 71 Magnesium (By similarity). FT BINDING 51 51 HMP-PP (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 193 AA; 20833 MW; 21824E54DE566E2A CRC64; MDSVAWIERL LEAGVRTIQL RIKDKRDEEV EADVIAAIAL GRRYDARLFI NDYWRLAIKH RAYGVHLGQE DLETTDLKAI QAAGLRLGVS THDDMEIDVA LAAKPSYIAL GHVFPTQTKQ MPSAPQGLAQ LASHIERLAD YPTVAIGGIS LERAPAVLAT GVGSVAVVSA ITQAADWREA TAQLLAIVGV GDE // ID G5MBI9_SALET Unreviewed; 211 AA. AC G5MBI9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SeGA_5624; OS Salmonella enterica subsp. enterica serovar Gaminara str. A4-567. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913071; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-567; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCL01001844; EHC29186.1; -; Genomic_DNA. DR EnsemblBacteria; EHC29186; EHC29186; SeGA_5624. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22951 MW; 47BE52D65F9F6603 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVISAIT QAADWRAATQ QLLAIAGVGD E // ID G5MR29_SALET Unreviewed; 211 AA. AC G5MR29; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSEGIV_5416; OS Salmonella enterica subsp. enterica serovar Give str. S5-487. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913072; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S5-487; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCM01001461; EHC43189.1; -; Genomic_DNA. DR EnsemblBacteria; EHC43189; EHC43189; LTSEGIV_5416. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22965 MW; 17263EAD6C7B9C2F CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLANYP TVAIGGISVE RAPSVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID G5N5K2_SALET Unreviewed; 211 AA. AC G5N5K2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSEHVI_5501; OS Salmonella enterica subsp. enterica serovar Hvittingfoss str. A4-620. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913073; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-620; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCN01001629; EHC43905.1; -; Genomic_DNA. DR ProteinModelPortal; G5N5K2; -. DR EnsemblBacteria; EHC43905; EHC43905; LTSEHVI_5501. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22936 MW; B72D3FAD6D6EC0DC CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIDRLADYP TVAIGGISVE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID G5NL31_SALET Unreviewed; 211 AA. AC G5NL31; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSEINV_5880; OS Salmonella enterica subsp. enterica serovar Inverness str. R8-3668. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913075; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R8-3668; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCO01001911; EHC48916.1; -; Genomic_DNA. DR EnsemblBacteria; EHC48916; EHC48916; LTSEINV_5880. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22924 MW; 376E78EF4511ECAD CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH NDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLSQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID G5P1U6_SALET Unreviewed; 211 AA. AC G5P1U6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSEJOH_5884; OS Salmonella enterica subsp. enterica serovar Johannesburg str. S5-703. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913077; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S5-703; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCP01001975; EHC56586.1; -; Genomic_DNA. DR EnsemblBacteria; EHC56586; EHC56586; LTSEJOH_5884. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22937 MW; 47A0A3395F9F6603 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G5PVQ4_SALET Unreviewed; 211 AA. AC G5PVQ4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSEMIS_5445; OS Salmonella enterica subsp. enterica serovar Mississippi str. A4-633. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913080; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-633; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCR01001570; EHC64999.1; -; Genomic_DNA. DR EnsemblBacteria; EHC64999; EHC64999; LTSEMIS_5445. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22980 MW; EF34B20E5845A654 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SSPQGLTQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLAIAGVGD E // ID G5QBA3_SALMO Unreviewed; 211 AA. AC G5QBA3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSEMON_5815; OS Salmonella enterica subsp. enterica serovar Montevideo str. S5-403. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913242; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S5-403; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCS01001281; EHC72491.1; -; Genomic_DNA. DR EnsemblBacteria; EHC72491; EHC72491; LTSEMON_5815. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G5QSM3_SALRU Unreviewed; 211 AA. AC G5QSM3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSERUB_6218; OS Salmonella enterica subsp. enterica serovar Rubislaw str. A4-653. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913081; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-653; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCT01002229; EHC78039.1; -; Genomic_DNA. DR ProteinModelPortal; G5QSM3; -. DR EnsemblBacteria; EHC78039; EHC78039; LTSERUB_6218. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22990 MW; 057A16E68A2D3E3E CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEINIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G5R6E3_SALSE Unreviewed; 211 AA. AC G5R6E3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSESEN_5253; OS Salmonella enterica subsp. enterica serovar Senftenberg str. A4-543. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913082; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-543; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCU01001689; EHC81643.1; -; Genomic_DNA. DR EnsemblBacteria; EHC81643; EHC81643; LTSESEN_5253. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22895 MW; F79C2391804D2ACE CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSVAVVSAIT QAADWREATA QLLAIAGVGD E // ID G5RNJ5_SALET Unreviewed; 211 AA. AC G5RNJ5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSEUGA_5602; OS Salmonella enterica subsp. enterica serovar Uganda str. R8-3404. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913083; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R8-3404; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCV01001404; EHC85356.1; -; Genomic_DNA. DR EnsemblBacteria; EHC85356; EHC85356; LTSEUGA_5602. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22955 MW; F50BE92C6575AFF2 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGINLE RAASVLATGV GSVAVVSAIT QAADWRAATA QLLDIAGVGD E // ID G5S3U7_SALET Unreviewed; 211 AA. AC G5S3U7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSEURB_6074; OS Salmonella enterica subsp. enterica serovar Urbana str. R8-2977. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913084; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R8-2977; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCW01002221; EHC97557.1; -; Genomic_DNA. DR EnsemblBacteria; EHC97557; EHC97557; LTSEURB_6074. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22937 MW; 47A0A3395F9F6603 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G5SB42_SALET Unreviewed; 211 AA. AC G5SB42; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSEWAN_2340; OS Salmonella enterica subsp. enterica serovar Wandsworth str. A4-580. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913086; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-580; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCX01000790; EHD03541.1; -; Genomic_DNA. DR EnsemblBacteria; EHD03541; EHD03541; LTSEWAN_2340. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22955 MW; F50BE92C6575AFF2 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGINLE RAASVLATGV GSVAVVSAIT QAADWRAATA QLLDIAGVGD E // ID G5STR5_9BACT Unreviewed; 210 AA. AC G5STR5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9441_02770; OS Paraprevotella clara YIT 11840. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Paraprevotella. OX NCBI_TaxID=762968; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11840; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFFY01000045; EHG99158.1; -; Genomic_DNA. DR EnsemblBacteria; EHG99158; EHG99158; HMPREF9441_02770. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23213 MW; 9ADBFAD6FE61DDC3 CRC64; MQNLQFITHY TEQYGYADAA RLALEGGCRW IQLRMKDASP EEWMRTGAEV EALCRRYGAT FILDDHVEWV DVLHADGVHL GKSDMPIDEA RRLLGQDRII GGTANTLEDV MLHAVRGADY IGCGPFRFTT TKEKLAPTLG LEGYRRILDG MKKKGISLPL IAIGGITKED IPALMETGVD GIALSGTILR AGSPTEETRN ILRILNVQQS // ID G5STR7_9BACT Unreviewed; 202 AA. AC G5STR7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 13-NOV-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF9441_02772; OS Paraprevotella clara YIT 11840. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Paraprevotella. OX NCBI_TaxID=762968; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11840; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFFY01000045; EHG99160.1; -; Genomic_DNA. DR EnsemblBacteria; EHG99160; EHG99160; HMPREF9441_02772. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23165 MW; 9C04F2F86DD51C2E CRC64; MKLILLTPPD FFVEEDKILT ALFEEGLDLL HLRKPDTEPV YSERLLTLLP ESHHNQIVVH DHFYLKEEFN LRGIHLNGRN PEPPVGYKGH ISKSFHHIDE LKAEKKNFNY VFLSPIFDSI SKSNYTSAFD MEVLKQASAH GIIDKRVMAL GGITTENMAV AKELGFGGVV VLGDLWNRFN IHSTLDYKEL INHFRKLRKA AD // ID G5TQR9_ECOLX Unreviewed; 211 AA. AC G5TQR9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUBG_04802; OS Escherichia coli O104:H4 str. C236-11. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1048256; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C236-11; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFRI01000012; EHF17463.1; -; Genomic_DNA. DR ProteinModelPortal; G5TQR9; -. DR SMR; G5TQR9; 20-202. DR EnsemblBacteria; EHF17463; EHF17463; EUBG_04802. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G5U5A4_ECOLX Unreviewed; 211 AA. AC G5U5A4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUEG_04579; OS Escherichia coli O104:H4 str. 09-7901. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1048266; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=09-7901; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFRK01000013; EHF30435.1; -; Genomic_DNA. DR ProteinModelPortal; G5U5A4; -. DR SMR; G5U5A4; 20-202. DR EnsemblBacteria; EHF30435; EHF30435; EUEG_04579. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G5UFQ4_ECOLX Unreviewed; 211 AA. AC G5UFQ4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUDG_03388; OS Escherichia coli O104:H4 str. 04-8351. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1048265; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=04-8351; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFRL01000017; EHF21240.1; -; Genomic_DNA. DR ProteinModelPortal; G5UFQ4; -. DR SMR; G5UFQ4; 20-202. DR EnsemblBacteria; EHF21240; EHF21240; EUDG_03388. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G5UZE8_ECOLX Unreviewed; 211 AA. AC G5UZE8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUFG_05097; OS Escherichia coli O104:H4 str. 11-3677. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1048334; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=11-3677; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFRM01000018; EHF36160.1; -; Genomic_DNA. DR ProteinModelPortal; G5UZE8; -. DR SMR; G5UZE8; 20-202. DR EnsemblBacteria; EHF36160; EHF36160; EUFG_05097. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G5VH78_ECOLX Unreviewed; 211 AA. AC G5VH78; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUHG_04795; OS Escherichia coli O104:H4 str. 11-4404. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1068614; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=11-4404; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUX01000029; EHF44830.1; -; Genomic_DNA. DR ProteinModelPortal; G5VH78; -. DR SMR; G5VH78; 20-202. DR EnsemblBacteria; EHF44830; EHF44830; EUHG_04795. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G5VWX3_ECOLX Unreviewed; 211 AA. AC G5VWX3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUIG_04735; OS Escherichia coli O104:H4 str. 11-4522. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1068615; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=11-4522; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUY01000027; EHF48556.1; -; Genomic_DNA. DR ProteinModelPortal; G5VWX3; -. DR SMR; G5VWX3; 20-202. DR EnsemblBacteria; EHF48556; EHF48556; EUIG_04735. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G5WDJ3_ECOLX Unreviewed; 211 AA. AC G5WDJ3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUJG_04431; OS Escherichia coli O104:H4 str. 11-4623. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1068616; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=11-4623; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUZ01000027; EHF52068.1; -; Genomic_DNA. DR ProteinModelPortal; G5WDJ3; -. DR SMR; G5WDJ3; 20-202. DR EnsemblBacteria; EHF52068; EHF52068; EUJG_04431. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G5WLQ8_ECOLX Unreviewed; 211 AA. AC G5WLQ8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUKG_04695; OS Escherichia coli O104:H4 str. 11-4632 C1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1068617; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=11-4632 C1; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFVA01000015; EHF63980.1; -; Genomic_DNA. DR ProteinModelPortal; G5WLQ8; -. DR SMR; G5WLQ8; 20-202. DR EnsemblBacteria; EHF63980; EHF63980; EUKG_04695. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G5X1C1_ECOLX Unreviewed; 211 AA. AC G5X1C1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EULG_04797; OS Escherichia coli O104:H4 str. 11-4632 C2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1068618; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=11-4632 C2; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFVB01000011; EHF67466.1; -; Genomic_DNA. DR ProteinModelPortal; G5X1C1; -. DR SMR; G5X1C1; 20-202. DR EnsemblBacteria; EHF67466; EHF67466; EULG_04797. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G5XKE6_ECOLX Unreviewed; 211 AA. AC G5XKE6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUMG_04774; OS Escherichia coli O104:H4 str. 11-4632 C3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1068619; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=11-4632 C3; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFVC01000027; EHF69212.1; -; Genomic_DNA. DR ProteinModelPortal; G5XKE6; -. DR SMR; G5XKE6; 20-202. DR EnsemblBacteria; EHF69212; EHF69212; EUMG_04774. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G5Y4I2_ECOLX Unreviewed; 211 AA. AC G5Y4I2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUNG_03147; OS Escherichia coli O104:H4 str. 11-4632 C4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1068620; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=11-4632 C4; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFVD01000035; EHF71911.1; -; Genomic_DNA. DR ProteinModelPortal; G5Y4I2; -. DR SMR; G5Y4I2; 20-202. DR EnsemblBacteria; EHF71911; EHF71911; EUNG_03147. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G5YA79_ECOLX Unreviewed; 211 AA. AC G5YA79; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EUOG_04817; OS Escherichia coli O104:H4 str. 11-4632 C5. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1068621; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=11-4632 C5; RX PubMed=22315421; DOI=10.1073/pnas.1121491109; RA Grad Y.H., Lipsitch M., Feldgarden M., Arachchi H.M., Cerqueira G.C., RA Fitzgerald M., Godfrey P., Haas B.J., Murphy C.I., Russ C., Sykes S., RA Walker B.J., Wortman J.R., Young S., Zeng Q., Abouelleil A., RA Bochicchio J., Chauvin S., Desmet T., Gujja S., McCowan C., RA Montmayeur A., Steelman S., Frimodt-Moller J., Petersen A.M., RA Struve C., Krogfelt K.A., Bingen E., Weill F.X., Lander E.S., RA Nusbaum C., Birren B.W., Hung D.T., Hanage W.P.; RT "Genomic epidemiology of the Escherichia coli O104:H4 outbreaks in RT Europe, 2011."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3065-3070(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFVE01000018; EHF79729.1; -; Genomic_DNA. DR ProteinModelPortal; G5YA79; -. DR SMR; G5YA79; 20-202. DR EnsemblBacteria; EHF79729; EHF79729; EUOG_04817. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID G6ALI5_LACRH Unreviewed; 209 AA. AC G6ALI5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0541_00487; OS Lactobacillus rhamnosus ATCC 21052. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1002365; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 21052; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFZY01000018; EHJ34842.1; -; Genomic_DNA. DR ProteinModelPortal; G6ALI5; -. DR EnsemblBacteria; EHJ34842; EHJ34842; HMPREF0541_00487. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21836 MW; FDF458E872FD9638 CRC64; MNAEALQLYL VTNRYADSPE VFLAKIAAAC ENGVTMVQLR EKSLTTRDYY ALAKQVKLIT DRYRIPLIID DRVDVCLAVD AAGVHIGDDE LPVAVTRQLL GPDKILGVST KTVATATAAV AAGADYLGVG AIFPTQTKAA APLTSLATLK AITAAVSVPV VAIGGIKADN LDTFKATGIA GVAIVSEIMQ APDTAQKVQT LSAKLKEVL // ID G6AYF9_9BACT Unreviewed; 202 AA. AC G6AYF9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 13-NOV-2013, entry version 11. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF0673_01669; OS Prevotella stercorea DSM 18206. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1002367; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18206; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFZZ01000147; EHJ39406.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ39406; EHJ39406; HMPREF0673_01669. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23207 MW; C18273F47D49F847 CRC64; MKLAIMTKST FFVEEDKILA ALFDVGLDNL HLYKPETSPI YSERLLSLLP DKAYEKIFVH GHYYLKDEYR LAGIHLDNAA EPVPEGYKGK VGRTCRDLTQ LKELKKQSAY IFLGNVFNSQ SEPLEPSTFT MNELEDAADK GLIDKRVYAL GGMNVDNIQI ARDLGFGGVV IRGDLWNKFN IHNQMDYKEL ITYFEKLRKL IY // ID G6AZ98_9BACT Unreviewed; 207 AA. AC G6AZ98; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0673_01962; OS Prevotella stercorea DSM 18206. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1002367; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18206; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFZZ01000169; EHJ38653.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ38653; EHJ38653; HMPREF0673_01962. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 30 34 HMP-PP binding (By similarity). FT REGION 127 129 THZ-P binding (By similarity). FT METAL 63 63 Magnesium (By similarity). FT METAL 82 82 Magnesium (By similarity). FT BINDING 62 62 HMP-PP (By similarity). FT BINDING 101 101 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22804 MW; DC31C32C08EAC80E CRC64; MIQFITHFNE RYGYVEGARL ALEGGCRWVQ LRMKDASEEK FVAAAEQIGK LCREHEAVFV LDDHAELVER CGADGVHLGK NDMPVDEARR LLGYDRIIGG TANTFEDIER LHRQGADYIG CGPFRFTTTK KNLSPVLGLE GYERIVSDMK AHGIDLPIVA IGGILKSDIA DIMQTGVTGI AVSGGILNAE SPAEEMKQFI SLIKPNR // ID G6AZA1_9BACT Unreviewed; 196 AA. AC G6AZA1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 13-NOV-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF0673_01965; OS Prevotella stercorea DSM 18206. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1002367; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18206; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFZZ01000169; EHJ38656.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ38656; EHJ38656; HMPREF0673_01965. DR OrthoDB; EOG679THR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 21841 MW; 7D32E7E23E2020B3 CRC64; MKWIVITSPD FVSGEALFID RLFGHGLDLL HLRKPGSTIE ACRKLLRQIP ERWHSRIVLH DHFQLTGEFL LHGVHLNRRC PHAPDGYTGS ISCSCHSLEE VAKKKPTSDY VFLSPIFNSI SKAGYEAAFS TAALHKAAAE SLIDNKVYAL GGVSKEHIAQ LKDLSFGGAA FLGDVWRRMD DPNADIYLDE LRSLLS // ID G6BB51_CLODI Unreviewed; 210 AA. AC G6BB51; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1122_03083; OS Peptoclostridium difficile 002-P50-2011. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=997827; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=002-P50-2011; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAA01000082; EHJ26322.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ26322; EHJ26322; HMPREF1122_03083. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23484 MW; 8FD604C8852679CF CRC64; MIDKEFLKKC LKLYLVTDSE MLKGRDFYKC LEDAISSGIT TVQLREKNAS GREFLRKAMK LREITKRYGV KFIINDRVDI ALICDADGVH VGQSDIEVRE VRKLIGNNKI LGVSARTLEE AICAKNDGAD YLGIGSIFTT STKLDAKSAS FETVKEIKEK VDIPFVLIGG INLDNIDKLK CLESDGYAII SAILKAEDIS KEVEKWTLKI // ID G6BBF6_CLODI Unreviewed; 229 AA. AC G6BBF6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 12. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF1122_03189; OS Peptoclostridium difficile 002-P50-2011. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=997827; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=002-P50-2011; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAA01000082; EHJ26427.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ26427; EHJ26427; HMPREF1122_03189. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 229 AA; 26958 MW; E456CC7251D910BB CRC64; MYLITNRKLC SEERYLEVIK ESILSGVENI IIREKDLEYQ ELKKLYMKIK TKINCIDFQE QISDESLKTN INQKECRNKF KVNFIINSNI EFFEKVDCQG IHLPFKLFLN LIENKYNFNE NKILGLSLHK VEEVDYLEKL IRNQNIKIDY ITLSHIYETK CKEGLNPKGI ELLKEAKKIT DIKIIALGGI LPSNVKETLK YCDDFAIMST IMKSKDIKKT ISNYNEKLN // ID G6BP23_CLODI Unreviewed; 210 AA. AC G6BP23; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1123_03929; OS Peptoclostridium difficile 050-P50-2011. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=997828; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=050-P50-2011; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAB01000084; EHJ24998.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ24998; EHJ24998; HMPREF1123_03929. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23484 MW; 8FD604C8852679CF CRC64; MIDKEFLKKC LKLYLVTDSE MLKGRDFYKC LEDAISSGIT TVQLREKNAS GREFLRKAMK LREITKRYGV KFIINDRVDI ALICDADGVH VGQSDIEVRE VRKLIGNNKI LGVSARTLEE AICAKNDGAD YLGIGSIFTT STKLDAKSAS FETVKEIKEK VDIPFVLIGG INLDNIDKLK CLESDGYAII SAILKAEDIS KEVEKWTLKI // ID G6BPJ5_CLODI Unreviewed; 229 AA. AC G6BPJ5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 12. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF1123_03823; OS Peptoclostridium difficile 050-P50-2011. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=997828; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=050-P50-2011; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAB01000084; EHJ24893.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ24893; EHJ24893; HMPREF1123_03823. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 229 AA; 26958 MW; E456CC7251D910BB CRC64; MYLITNRKLC SEERYLEVIK ESILSGVENI IIREKDLEYQ ELKKLYMKIK TKINCIDFQE QISDESLKTN INQKECRNKF KVNFIINSNI EFFEKVDCQG IHLPFKLFLN LIENKYNFNE NKILGLSLHK VEEVDYLEKL IRNQNIKIDY ITLSHIYETK CKEGLNPKGI ELLKEAKKIT DIKIIALGGI LPSNVKETLK YCDDFAIMST IMKSKDIKKT ISNYNEKLN // ID G6BTX3_CLODI Unreviewed; 210 AA. AC G6BTX3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9945_01496; OS Peptoclostridium difficile 70-100-2010. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=1002369; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=70-100-2010; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAC01000045; EHJ38823.1; -; Genomic_DNA. DR ProteinModelPortal; G6BTX3; -. DR EnsemblBacteria; EHJ38823; EHJ38823; HMPREF9945_01496. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23414 MW; F50956BE21E60D7E CRC64; MIDKESLKKC LKLYLVTDSE MLKGRDFYKC LEDAISSGIT TVQLREKNAS GREFLRKAMK LREITKRYGV KFIINDRVDI ALICDADGVH VGQSDIDVRE VRKLIGNNKI LGVSARTLEE AICAKNDGAD YLGVGSIFTT STKLDAKSAS FETVKEIKEK VDMPFVLIGG INLDNIDKLK CLESDGYAII SAILKAEDIS KEVEKWTLKI // ID G6BXX6_CLODI Unreviewed; 229 AA. AC G6BXX6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 12. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF9945_02901; OS Peptoclostridium difficile 70-100-2010. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=1002369; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=70-100-2010; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAC01000114; EHJ36767.1; -; Genomic_DNA. DR ProteinModelPortal; G6BXX6; -. DR EnsemblBacteria; EHJ36767; EHJ36767; HMPREF9945_02901. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 229 AA; 27058 MW; 8184257B7FAB2E97 CRC64; MYLITNRKLC SEERYLEVIK ESILSGVENI IIREKDLEYQ ELRKLYMKIK TKINCIDFQE QISDESLKTN INQKEFRNKF KVNFIINSNI EFFEKVDCQG IHLPFKLFLN LIENKYNFNE NKILGLSLHK VEEVDYLEKL IRNQNIKIDY ITLSHIYETK CKEGLNPKGI ELLKEAKKIT DIKIIALGGI LPSNVKETLK YCDDFAIMST IMRSKDIKKT ISNYNEKLN // ID G6C1A6_9FUSO Unreviewed; 206 AA. AC G6C1A6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9093_00334; OS Fusobacterium sp. oral taxon 370 str. F0437. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=861452; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0437; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAD01000042; EHI79390.1; -; Genomic_DNA. DR EnsemblBacteria; EHI79390; EHI79390; HMPREF9093_00334. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22731 MW; FDA0F061486BD600 CRC64; MDLKNCKIYL VTDEKACLGK DFYNCIEEAI KGGVRTVQLR EKNISTKDFY EKALKVKEIC KNYGVLFIIN DRLDIAQAVE ADGVHLGQSD MPIEKAREIL KDKFLIGATA RNVEEAKRAE LLGANYIGSG AIFGTNTKDN AKKLEMEELK KIVANIKIPV FAIGGININN VSSLKNIGLQ GICAVSGILS EKDCKKAVDI MLKNFN // ID G6C1B2_9FUSO Unreviewed; 205 AA. AC G6C1B2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 13-NOV-2013, entry version 11. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF9093_00340; OS Fusobacterium sp. oral taxon 370 str. F0437. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=861452; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0437; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAD01000042; EHI79396.1; -; Genomic_DNA. DR EnsemblBacteria; EHI79396; EHI79396; HMPREF9093_00340. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 205 AA; 23622 MW; F22986052D56FA2F CRC64; MINKIKLNII SNRKLCENEN LEKQIKKIFS AYEKKIILKN FEIVSLTLRE KDLDKNEYLN LVEKIYSICK KHKINLILHQ NYDLNLDDKY MIEGLHLSYE IFKSLNKNIR EGLIKKYKRI GVSIHSLEEA KEAEILGATY VVAGHIFETD CKKGLEPRGL KFVEELSSIL TIPIFAIGGI DEKNSQSVID SGAFSVCMMS SLMKY // ID G6C7D0_9STRE Unreviewed; 210 AA. AC G6C7D0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9184_00203; OS Streptococcus sp. oral taxon 058 str. F0407. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=861455; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0407; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAE01000017; EHI77806.1; -; Genomic_DNA. DR EnsemblBacteria; EHI77806; EHI77806; HMPREF9184_00203. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22753 MW; 9B567E5D3DFFBFE0 CRC64; MNREALKLYL VTNRYQDSLE SFLEKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKKIT DAYQIPLIID DRLDICLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE TSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLTGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDNMIS // ID G6CGP3_LACCU Unreviewed; 223 AA. AC G6CGP3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CRL705_1624; OS Lactobacillus curvatus CRL 705. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1074451; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CRL 705; RX PubMed=22207745; DOI=10.1128/JB.06416-11; RA Hebert E.M., Saavedra L., Taranto M.P., Mozzi F., Magni C., RA Nader M.E., Font de Valdez G., Sesma F., Vignolo G., Raya R.R.; RT "Genome sequence of the bacteriocin-producing Lactobacillus curvatus RT strain CRL705."; RL J. Bacteriol. 194:538-539(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGBU01000049; EHE85303.1; -; Genomic_DNA. DR EnsemblBacteria; EHE85303; EHE85303; CRL705_1624. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24394 MW; 3041D2FF95FA83F1 CRC64; MTNISREMFQ TYLVAGTQNT GMDDFLNILE QALQAGITCF QFREKGAGSL QDSDAILKYA TAAQALCRHY QVPFIIDDNL DLALQINADG IHVGQSDHPW HKIETAKAHG LITGLSCHTE QELHQSHNQP ILDYIGIGPI FPTNSKEDAK PALGTNRLRF LTQQSELPVV AIGGINQENV AQVAKTTVDG VAVISAITHA TDIAQTVQAL QKPWHRSTDE NQS // ID G6E3V8_9GAMM Unreviewed; 642 AA. AC G6E3V8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN ORFNames=Sbal625DRAFT_3453; OS Shewanella baltica OS625. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=693972; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OS625; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Hofle M., Brettar I., RA Konstantinidis K., Deng J., Tiedje J., Auchtung J., Woyke T.J.; RT "The High-Quality Draft genome of Shewanella baltica OS625."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEX01000009; EHC04893.1; -; Genomic_DNA. DR ProteinModelPortal; G6E3V8; -. DR EnsemblBacteria; EHC04893; EHC04893; Sbal625DRAFT_3453. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 2. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 642 AA; 67935 MW; ADC00DA2DF19E784 CRC64; MQGIHGGKLP MSTERPAFVW TIAGSDSGGG AGIQADLATI QDLGCHGCSV VTTVTAQSSV AVTLVEPVSA AMLMAQLTTL LSDLPPKAIK IGLLADQTQV ALLADWIASF KIHYPSVPVI VDPVMVASCG DALAVDNCQD IKSAAKSALD FRPFKGLIEL ITPNVLELGR LTHSDVSTKA QFAAAALALS QSLDCSVLAK GGDVSFGSTD ILENTHAKTH DNTYAQTQAN AHNSNGWDLE LAEDYLVCHQ VRASSKLHQN GRFWLASQRV NTRHNHGSGC TLSSAIAAVL AQGFVLQDAV VVAKAYVSQG LSAAIGLGQG PGPLARTGWP NNLSRYAKIN LCDGNFIRHH LNRHLDVRSD LVATVLSATD QATAQVRIAS TPPQNILSHG FKVLDAELGV YPVVSDLTML ESLLAAGVKT VQLRIKTDIS ELTTTTAPAE SDLGKSALGR CESGEPELIG SELEAQIQTA IALGKHFNAQ LFINDHWKLA IKYHAFGVHL GQEDLAVTDL AAIQAAGLAL GISSHSYFEL LLAHQYSPSY IALGHIFPTT TKQMPSAPQG LAKLKHYVAL LQGHYPLVAI GGIDLTNLAK VKATGVGNIA VVRAITKAKE PVAAFAELSQ AWEQCSLCEE LAVKQELDAK HE // ID G6ECB4_9SPHN Unreviewed; 184 AA. AC G6ECB4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 13-NOV-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=NSU_1985; OS Novosphingobium pentaromativorans US6-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1088721; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=US6-1; RX PubMed=22275104; DOI=10.1128/JB.06476-11; RA Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.; RT "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium RT pentaromativorans US6-1."; RL J. Bacteriol. 194:907-907(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGFM01000028; EHJ61049.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ61049; EHJ61049; NSU_1985. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 184 AA; 20181 MW; DB5A4FA1639FF82B CRC64; MNLPDIWLIS DERIDAQLPQ ALSRLPRGSG FVFRHYHLPP AHRRTRFEEL ARIARRYGHV VVLSGTPREA GRWQAHGAYG APRRLAGGPA TLRLATVHSL RELAQASRTR ADAVLLSPVF PTRSHPGASH LGQVRFHLMA ARSGVPVIAL GGMNAHRARS ARIGKWAAIQ GLAKSPTKSF PIHS // ID G6EI73_9SPHN Unreviewed; 223 AA. AC G6EI73; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=NSU_4043; OS Novosphingobium pentaromativorans US6-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1088721; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=US6-1; RX PubMed=22275104; DOI=10.1128/JB.06476-11; RA Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.; RT "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium RT pentaromativorans US6-1."; RL J. Bacteriol. 194:907-907(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGFM01000064; EHJ58814.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ58814; EHJ58814; NSU_4043. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 51 55 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23874 MW; 94B0BA4C8E08AC74 CRC64; MTDQIDTDQA EQDEIEREPT LLYLISPLKV DGDFPQRLAR ALDAGPVAAF QFRVKDIDQH EAARLAEPLQ AICAEREVAF IVNDSISLAK RLGADGVHLG QEDGTVEEAR KALGRDAQIG VTCHDSRHLA MEAGDAGADY VAFGAYFPTT TKDVKHKAGL DLLEWWQRIF EIPCVAIGGI TPENCGALVA AGADFLAVSG AVWNGDEAAA VKAFNEAIAA AMP // ID G6EYK3_9PROT Unreviewed; 210 AA. AC G6EYK3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CIN_05230; OS Commensalibacter intestini A911. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae. OX NCBI_TaxID=1088868; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A911; RA Lee W.-J., Kim E.-K.; RT "Genome Sequence of Commensalibacter intestini A911, isolated from RT Drosophila gut."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGFR01000003; EHD14591.1; -; Genomic_DNA. DR EnsemblBacteria; EHD14591; EHD14591; CIN_05230. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22924 MW; 36AC611CC5218026 CRC64; MNPCELYLLT PPSLDPFKFK PLLIKALDAG PVAAVQLRLK DVSDDEIRKA IDILRPVVQD HDIAFILNDR PDLAKECGCD GAHIDMADTP IELVRAQLGD DLQLGVSCYD SRDIAMKAGE KGADYITFGP FFPSKDTNIR APVDLLSWWF EMMEIPVVAT GGITAENCKP LVKAGTDFLS VSGAVWNHTG GPTQGVKSIL KAIQETENEK // ID G6FB31_LACLL Unreviewed; 215 AA. AC G6FB31; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-APR-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LLCRE1631_00724; OS Lactococcus lactis subsp. lactis CNCM I-1631. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=1042402; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNCM I-1631; RX PubMed=22030749; RA McNulty N.P., Yatsunenko T., Hsiao A., Faith J.J., Muegge B.D., RA Goodman A.L., Henrissat B., Oozeer R., Cools-Portier S., Gobert G., RA Chervaux C., Knights D., Lozupone C.A., Knight R., Duncan A.E., RA Bain J.R., Muehlbauer M.J., Newgard C.B., Heath A.C., Gordon J.I.; RT "The impact of a consortium of fermented milk strains on the gut RT microbiome of gnotobiotic mice and monozygotic twins."; RL Sci. Transl. Med. 3:106RA106-106RA106(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGHX01000018; EHE94140.1; -; Genomic_DNA. DR ProteinModelPortal; G6FB31; -. DR EnsemblBacteria; EHE94140; EHE94140; LLCRE1631_00724. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23657 MW; 824D01C7F484806A CRC64; MKNKILDLRA YFIAGPQDFP KLSIDDAIDK ISVIIKSGVT VYQFRDKGTI YKNKNQRLEV AKRLQEVAQK AAVSFIVNDD VELARELSAD GIHVGQDDDS VSKIRELIGQ EMWVGLSVSN DMELESAQKS GADYLGIGPI YPTNSKSDAA EPIGVDHLRK MLEHNQLPTV GIGGITENSL TELSKIGLGG VAVISLLTES ENYKNMVQKI KQNIR // ID G6FSJ4_9CYAN Unreviewed; 381 AA. AC G6FSJ4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FJSC11DRAFT_1741; OS Fischerella sp. JSC-11. OC Bacteria; Cyanobacteria; Stigonematales; Fischerella. OX NCBI_TaxID=741277; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JSC-11; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I., RA Woyke T.J.; RT "The draft genome of Fischerella sp. JSC-11."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGIZ01000005; EHC14830.1; -; Genomic_DNA. DR EnsemblBacteria; EHC14830; EHC14830; FJSC11DRAFT_1741. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 145 Unknown (By similarity). FT REGION 146 381 Thiamine-phosphate synthase (By FT similarity). FT REGION 193 197 HMP-PP binding (By similarity). FT REGION 290 292 THZ-P binding (By similarity). FT METAL 226 226 Magnesium (By similarity). FT METAL 245 245 Magnesium (By similarity). FT BINDING 225 225 HMP-PP (By similarity). FT BINDING 264 264 HMP-PP (By similarity). FT BINDING 293 293 HMP-PP (By similarity). FT BINDING 320 320 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 381 AA; 43321 MW; 08EDC17141F2AB64 CRC64; MKRTDCYDLN TNGIVVMVEP YSQREQRNLV IYRILDANLD RAREGLRIIE EWCRFGLNNA QFTGECKGMR QELASWHTAD LRSARDTLGD PGTELTHPQE EQRASIKSLL QANFCRVQEA MRVLEEYGKL YNPNMGKALK QMRYRVYTLE SNLMGYQRHQ LLLRSHLYLV TSPTDKLLEI VEAALKGGLT LVQYRDKNVD DAVRFQQAQK LRQLCHNYNA IFIINDRVDI ALAVDADGVH LGQQDMPIAV ARQLLGPHRI IGRSTTNADE MQRAIKEGAD YIGVGPVYET PTKEGKPAAG LEYVSYVAKN CSIPWFAIGG IDPNNINDVI DAGAKRVAVV RGIMQAEQPT LVTQYFLSQL NRIQPDPDHS YVESNYYPDQ W // ID G6IPB1_PEDAC Unreviewed; 226 AA. AC G6IPB1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-MAR-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=KIW_02693; OS Pediococcus acidilactici MA18/5M. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=1080365; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MA18/5M; RX PubMed=22275099; DOI=10.1128/JB.06563-11; RA Barreau G., Tompkins T.A., de Carvalho V.G.; RT "Draft genome sequence of probiotic strain Pediococcus acidilactici RT MA18/5M."; RL J. Bacteriol. 194:901-901(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGKB01000006; EHJ22467.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ22467; EHJ22467; KIW_02693. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23887 MW; 51349ACCF022FE95 CRC64; MKFNPTMLQA YFIAGTQDVA SKADFLPTVE RIVQAGATAF QFRNKGAVKT ASRDEVVELA RACHQITQKY QIPLFIDDDV DLALAVGAEG IHVGQKDERI TSVLERVGDR MIVGLSCNTA AQITAANQLN GVDYLGTGTV YETNSKADAG NALGVDKLRE LVQMSKFPVV AIGGITLKRV AETVATGAAG IAAISMFIQM TDPAQQIAEI KATIAQVGGA ACSPKK // ID G6IQK0_PEDAC Unreviewed; 209 AA. AC G6IQK0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-MAR-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=KIW_04990; OS Pediococcus acidilactici MA18/5M. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=1080365; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MA18/5M; RX PubMed=22275099; DOI=10.1128/JB.06563-11; RA Barreau G., Tompkins T.A., de Carvalho V.G.; RT "Draft genome sequence of probiotic strain Pediococcus acidilactici RT MA18/5M."; RL J. Bacteriol. 194:901-901(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGKB01000007; EHJ21984.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ21984; EHJ21984; KIW_04990. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22580 MW; 994AAE77F63841F2 CRC64; MLEKPLLYLV TDRLGLNQQQ FLERIELACQ GGVDLLQLRE KEISSAEYYK LAGHVKKITD RYQVPLIIDD QVAIAQAVDA AGVHLGQADL PVAVARRILG PHKIIGATTK TVVQARRAVE EGANYLGVGA IFPTTTHVKT VHTSVATLKR IKQEAKITVF AIGGLNAENL SVLRNTNVDG VAAVSAIMKA TQPQQVAQQL KSTVIDVLS // ID G6IXR5_LACRH Unreviewed; 209 AA. AC G6IXR5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-MAR-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=R0011_08238; OS Lactobacillus rhamnosus R0011. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=880592; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R0011; RX PubMed=22275100; DOI=10.1128/JB.06584-11; RA Tompkins T.A., Barreau G., de Carvalho V.G.; RT "Draft genome sequence of probiotic strain Lactobacillus rhamnosus RT R0011."; RL J. Bacteriol. 194:902-902(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGKC01000003; EHJ22064.1; -; Genomic_DNA. DR ProteinModelPortal; G6IXR5; -. DR EnsemblBacteria; EHJ22064; EHJ22064; R0011_08238. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21836 MW; FDF458E872FD9638 CRC64; MNAEALQLYL VTNRYADSPE VFLAKIAAAC ENGVTMVQLR EKSLTTRDYY ALAKQVKLIT DRYRIPLIID DRVDVCLAVD AAGVHIGDDE LPVAVTRQLL GPDKILGVST KTVATATAAV AAGADYLGVG AIFPTQTKAA APLTSLATLK AITAAVSVPV VAIGGIKADN LDTFKATGIA GVAIVSEIMQ APDTAQKVQT LSAKLKEVL // ID G6J2W7_STREE Unreviewed; 209 AA. AC G6J2W7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR19_0709; OS Streptococcus pneumoniae GA11184. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760760; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA11184; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA11184."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNU01000005; EHD31775.1; -; Genomic_DNA. DR ProteinModelPortal; G6J2W7; -. DR EnsemblBacteria; EHD31775; EHD31775; SPAR19_0709. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6J2X4_STREE Unreviewed; 210 AA. AC G6J2X4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR19_0716; OS Streptococcus pneumoniae GA11184. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760760; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA11184; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA11184."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNU01000005; EHD31782.1; -; Genomic_DNA. DR ProteinModelPortal; G6J2X4; -. DR EnsemblBacteria; EHD31782; EHD31782; SPAR19_0716. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6J9A6_STREE Unreviewed; 209 AA. AC G6J9A6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR98_0744; OS Streptococcus pneumoniae GA47502. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760839; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47502; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47502."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNV01000004; EHD31039.1; -; Genomic_DNA. DR EnsemblBacteria; EHD31039; EHD31039; SPAR98_0744. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23245 MW; E59983C784B2289D CRC64; MFHKELLKLY FICGTTTCQG KDLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6J9B3_STREE Unreviewed; 210 AA. AC G6J9B3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR98_0751; OS Streptococcus pneumoniae GA47502. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760839; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47502; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47502."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNV01000004; EHD31046.1; -; Genomic_DNA. DR EnsemblBacteria; EHD31046; EHD31046; SPAR98_0751. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E56B9DC3C1F8D491 CRC64; MNREALRLYL VTNRYQDSVE SFLAKIETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6JGI9_STREE Unreviewed; 209 AA. AC G6JGI9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR123_0650; OS Streptococcus pneumoniae 4027-06. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760864; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4027-06; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 4027-06."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNW01000002; EHD28057.1; -; Genomic_DNA. DR ProteinModelPortal; G6JGI9; -. DR EnsemblBacteria; EHD28057; EHD28057; SPAR123_0650. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6JGJ6_STREE Unreviewed; 210 AA. AC G6JGJ6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR123_0657; OS Streptococcus pneumoniae 4027-06. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760864; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4027-06; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 4027-06."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNW01000002; EHD28064.1; -; Genomic_DNA. DR ProteinModelPortal; G6JGJ6; -. DR EnsemblBacteria; EHD28064; EHD28064; SPAR123_0657. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6JP98_STREE Unreviewed; 209 AA. AC G6JP98; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR121_1392; OS Streptococcus pneumoniae 6735-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760862; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6735-05; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 6735-05."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNX01000007; EHD32466.1; -; Genomic_DNA. DR ProteinModelPortal; G6JP98; -. DR EnsemblBacteria; EHD32466; EHD32466; SPAR121_1392. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6JPA5_STREE Unreviewed; 210 AA. AC G6JPA5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR121_1399; OS Streptococcus pneumoniae 6735-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760862; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6735-05; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 6735-05."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNX01000007; EHD32473.1; -; Genomic_DNA. DR ProteinModelPortal; G6JPA5; -. DR EnsemblBacteria; EHD32473; EHD32473; SPAR121_1399. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6JTI9_STREE Unreviewed; 192 AA. AC G6JTI9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR81_0680; OS Streptococcus pneumoniae GA44288. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760822; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44288; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44288."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNY01000003; EHD38625.1; -; Genomic_DNA. DR EnsemblBacteria; EHD38625; EHD38625; SPAR81_0680. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 22 26 HMP-PP binding (By similarity). FT REGION 121 123 THZ-P binding (By similarity). FT REGION 173 174 THZ-P binding (By similarity). FT METAL 58 58 Magnesium (By similarity). FT METAL 77 77 Magnesium (By similarity). FT BINDING 57 57 HMP-PP (By similarity). FT BINDING 95 95 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 153 153 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 192 AA; 21341 MW; 9A67C106DCE139AA CRC64; MPRKNLYTVV EEALKGGITL FQFREKGEGA LEGLEKLELA IQIKELCKKY NVPFIVNDDI DLAMEIDADG VHVGQDDIGV DEIRKLMPDK IIGLSIRNEE EFQQSKVEYV DYVGVGPVFD TQSKDDAGGA IGYEGLELMR KLLPQMPLVA IGGIQTKHIK DIIKTNVDGV SIISAISYAK NIEKTVREMS EQ // ID G6JTJ6_STREE Unreviewed; 210 AA. AC G6JTJ6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR81_0687; OS Streptococcus pneumoniae GA44288. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760822; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44288; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44288."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNY01000003; EHD38632.1; -; Genomic_DNA. DR ProteinModelPortal; G6JTJ6; -. DR EnsemblBacteria; EHD38632; EHD38632; SPAR81_0687. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6JZN4_STREE Unreviewed; 209 AA. AC G6JZN4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR90_0694; OS Streptococcus pneumoniae GA47281. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760831; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47281; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47281."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNZ01000005; EHD40609.1; -; Genomic_DNA. DR ProteinModelPortal; G6JZN4; -. DR EnsemblBacteria; EHD40609; EHD40609; SPAR90_0694. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6JZP1_STREE Unreviewed; 210 AA. AC G6JZP1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR90_0701; OS Streptococcus pneumoniae GA47281. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760831; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47281; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47281."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNZ01000005; EHD40616.1; -; Genomic_DNA. DR ProteinModelPortal; G6JZP1; -. DR EnsemblBacteria; EHD40616; EHD40616; SPAR90_0701. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6K4H2_STREE Unreviewed; 209 AA. AC G6K4H2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR87_0236; OS Streptococcus pneumoniae GA47033. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760828; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47033; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47033."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOA01000003; EHD40305.1; -; Genomic_DNA. DR EnsemblBacteria; EHD40305; EHD40305; SPAR87_0236. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23352 MW; 24457EFDA912E780 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KYDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6K4H9_STREE Unreviewed; 210 AA. AC G6K4H9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR87_0243; OS Streptococcus pneumoniae GA47033. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760828; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47033; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47033."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOA01000003; EHD40312.1; -; Genomic_DNA. DR EnsemblBacteria; EHD40312; EHD40312; SPAR87_0243. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; 2BE4904FBC77D49C CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID G6KC11_STREE Unreviewed; 209 AA. AC G6KC11; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR77_0697; OS Streptococcus pneumoniae GA43265. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760818; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA43265; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA43265."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOB01000004; EHD43356.1; -; Genomic_DNA. DR ProteinModelPortal; G6KC11; -. DR EnsemblBacteria; EHD43356; EHD43356; SPAR77_0697. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6KC18_STREE Unreviewed; 210 AA. AC G6KC18; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR77_0704; OS Streptococcus pneumoniae GA43265. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760818; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA43265; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA43265."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOB01000004; EHD43363.1; -; Genomic_DNA. DR ProteinModelPortal; G6KC18; -. DR EnsemblBacteria; EHD43363; EHD43363; SPAR77_0704. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6KGV5_STREE Unreviewed; 209 AA. AC G6KGV5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR84_0704; OS Streptococcus pneumoniae GA44452. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760825; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44452; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44452."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOC01000002; EHD47248.1; -; Genomic_DNA. DR ProteinModelPortal; G6KGV5; -. DR EnsemblBacteria; EHD47248; EHD47248; SPAR84_0704. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6KGW2_STREE Unreviewed; 210 AA. AC G6KGW2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR84_0711; OS Streptococcus pneumoniae GA44452. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760825; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44452; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44452."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOC01000002; EHD47255.1; -; Genomic_DNA. DR EnsemblBacteria; EHD47255; EHD47255; SPAR84_0711. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22728 MW; E8F9319141D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGAGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6KPN0_STREE Unreviewed; 209 AA. AC G6KPN0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR110_0679; OS Streptococcus pneumoniae GA49138. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760851; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA49138; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA49138."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOD01000004; EHD45977.1; -; Genomic_DNA. DR ProteinModelPortal; G6KPN0; -. DR EnsemblBacteria; EHD45977; EHD45977; SPAR110_0679. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6KPN7_STREE Unreviewed; 210 AA. AC G6KPN7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR110_0686; OS Streptococcus pneumoniae GA49138. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760851; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA49138; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA49138."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOD01000004; EHD45984.1; -; Genomic_DNA. DR EnsemblBacteria; EHD45984; EHD45984; SPAR110_0686. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22734 MW; 55524965CF87E87D CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GSEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6KUE3_STREE Unreviewed; 209 AA. AC G6KUE3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR40_0741; OS Streptococcus pneumoniae GA16531. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760781; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA16531; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA16531."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOE01000004; EHD53099.1; -; Genomic_DNA. DR ProteinModelPortal; G6KUE3; -. DR EnsemblBacteria; EHD53099; EHD53099; SPAR40_0741. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6KUF0_STREE Unreviewed; 210 AA. AC G6KUF0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR40_0748; OS Streptococcus pneumoniae GA16531. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760781; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA16531; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA16531."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOE01000004; EHD53106.1; -; Genomic_DNA. DR ProteinModelPortal; G6KUF0; -. DR EnsemblBacteria; EHD53106; EHD53106; SPAR40_0748. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6L215_STREE Unreviewed; 209 AA. AC G6L215; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR122_0662; OS Streptococcus pneumoniae 6901-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760863; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6901-05; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 6901-05."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOF01000003; EHD50963.1; -; Genomic_DNA. DR ProteinModelPortal; G6L215; -. DR EnsemblBacteria; EHD50963; EHD50963; SPAR122_0662. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6L222_STREE Unreviewed; 210 AA. AC G6L222; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR122_0669; OS Streptococcus pneumoniae 6901-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760863; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6901-05; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 6901-05."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOF01000003; EHD50970.1; -; Genomic_DNA. DR ProteinModelPortal; G6L222; -. DR EnsemblBacteria; EHD50970; EHD50970; SPAR122_0669. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6L8R5_STREE Unreviewed; 210 AA. AC G6L8R5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR128_0929; OS Streptococcus pneumoniae 7286-06. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760869; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7286-06; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 7286-06."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOG01000004; EHD53721.1; -; Genomic_DNA. DR ProteinModelPortal; G6L8R5; -. DR EnsemblBacteria; EHD53721; EHD53721; SPAR128_0929. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6L8S2_STREE Unreviewed; 209 AA. AC G6L8S2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR128_0936; OS Streptococcus pneumoniae 7286-06. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760869; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7286-06; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 7286-06."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOG01000004; EHD53728.1; -; Genomic_DNA. DR ProteinModelPortal; G6L8S2; -. DR EnsemblBacteria; EHD53728; EHD53728; SPAR128_0936. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6LF01_STREE Unreviewed; 209 AA. AC G6LF01; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR143_0711; OS Streptococcus pneumoniae NP070. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760884; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NP070; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae NP070."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOH01000002; EHD57076.1; -; Genomic_DNA. DR ProteinModelPortal; G6LF01; -. DR EnsemblBacteria; EHD57076; EHD57076; SPAR143_0711. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23376 MW; 2FA03125014CC79F CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYL GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6LF08_STREE Unreviewed; 210 AA. AC G6LF08; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR143_0718; OS Streptococcus pneumoniae NP070. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760884; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NP070; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae NP070."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOH01000002; EHD57083.1; -; Genomic_DNA. DR EnsemblBacteria; EHD57083; EHD57083; SPAR143_0718. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22785 MW; 20B55C47CB70B024 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVRLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6LLG5_STREE Unreviewed; 209 AA. AC G6LLG5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR85_0687; OS Streptococcus pneumoniae GA44500. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760826; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44500; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44500."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOI01000007; EHD59663.1; -; Genomic_DNA. DR ProteinModelPortal; G6LLG5; -. DR EnsemblBacteria; EHD59663; EHD59663; SPAR85_0687. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6LLH2_STREE Unreviewed; 210 AA. AC G6LLH2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR85_0694; OS Streptococcus pneumoniae GA44500. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760826; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44500; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44500."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOI01000007; EHD59670.1; -; Genomic_DNA. DR ProteinModelPortal; G6LLH2; -. DR EnsemblBacteria; EHD59670; EHD59670; SPAR85_0694. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6LT29_STREE Unreviewed; 209 AA. AC G6LT29; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR70_0636; OS Streptococcus pneumoniae GA41410. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760811; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41410; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41410."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOJ01000009; EHD61031.1; -; Genomic_DNA. DR ProteinModelPortal; G6LT29; -. DR EnsemblBacteria; EHD61031; EHD61031; SPAR70_0636. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6LT37_STREE Unreviewed; 210 AA. AC G6LT37; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR70_0644; OS Streptococcus pneumoniae GA41410. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760811; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41410; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41410."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOJ01000009; EHD61039.1; -; Genomic_DNA. DR EnsemblBacteria; EHD61039; EHD61039; SPAR70_0644. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22728 MW; E8F9319141D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGAGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6M0F1_STREE Unreviewed; 209 AA. AC G6M0F1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR113_0753; OS Streptococcus pneumoniae GA49447. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760854; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA49447; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA49447."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOK01000003; EHD65393.1; -; Genomic_DNA. DR ProteinModelPortal; G6M0F1; -. DR EnsemblBacteria; EHD65393; EHD65393; SPAR113_0753. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6M0F9_STREE Unreviewed; 210 AA. AC G6M0F9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR113_0761; OS Streptococcus pneumoniae GA49447. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760854; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA49447; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA49447."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOK01000003; EHD65401.1; -; Genomic_DNA. DR EnsemblBacteria; EHD65401; EHD65401; SPAR113_0761. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22728 MW; E8F9319141D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGAGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6M758_STREE Unreviewed; 209 AA. AC G6M758; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR72_0761; OS Streptococcus pneumoniae GA41538. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760813; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41538; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41538."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOL01000007; EHD66130.1; -; Genomic_DNA. DR EnsemblBacteria; EHD66130; EHD66130; SPAR72_0761. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23302 MW; 094F9E0E007A2FA0 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGESALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6M765_STREE Unreviewed; 210 AA. AC G6M765; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR72_0768; OS Streptococcus pneumoniae GA41538. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760813; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41538; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41538."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOL01000007; EHD66137.1; -; Genomic_DNA. DR ProteinModelPortal; G6M765; -. DR EnsemblBacteria; EHD66137; EHD66137; SPAR72_0768. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6MDN6_STREE Unreviewed; 209 AA. AC G6MDN6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR125_0603; OS Streptococcus pneumoniae 5787-06. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760866; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5787-06; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 5787-06."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOM01000004; EHD67905.1; -; Genomic_DNA. DR ProteinModelPortal; G6MDN6; -. DR EnsemblBacteria; EHD67905; EHD67905; SPAR125_0603. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6MDP3_STREE Unreviewed; 210 AA. AC G6MDP3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR125_0610; OS Streptococcus pneumoniae 5787-06. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760866; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5787-06; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 5787-06."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOM01000004; EHD67912.1; -; Genomic_DNA. DR ProteinModelPortal; G6MDP3; -. DR EnsemblBacteria; EHD67912; EHD67912; SPAR125_0610. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6MJJ8_STREE Unreviewed; 209 AA. AC G6MJJ8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR124_0655; OS Streptococcus pneumoniae 6963-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760865; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6963-05; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 6963-05."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGON01000008; EHD70664.1; -; Genomic_DNA. DR ProteinModelPortal; G6MJJ8; -. DR EnsemblBacteria; EHD70664; EHD70664; SPAR124_0655. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6MJK5_STREE Unreviewed; 210 AA. AC G6MJK5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR124_0662; OS Streptococcus pneumoniae 6963-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760865; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6963-05; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 6963-05."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGON01000008; EHD70671.1; -; Genomic_DNA. DR ProteinModelPortal; G6MJK5; -. DR EnsemblBacteria; EHD70671; EHD70671; SPAR124_0662. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6MQV6_STREE Unreviewed; 209 AA. AC G6MQV6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR54_0691; OS Streptococcus pneumoniae GA18523. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760795; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA18523; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA18523."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOO01000007; EHD71735.1; -; Genomic_DNA. DR ProteinModelPortal; G6MQV6; -. DR EnsemblBacteria; EHD71735; EHD71735; SPAR54_0691. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6MQW3_STREE Unreviewed; 210 AA. AC G6MQW3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR54_0698; OS Streptococcus pneumoniae GA18523. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760795; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA18523; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA18523."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOO01000007; EHD71742.1; -; Genomic_DNA. DR ProteinModelPortal; G6MQW3; -. DR EnsemblBacteria; EHD71742; EHD71742; SPAR54_0698. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6MWY6_STREE Unreviewed; 209 AA. AC G6MWY6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR80_0664; OS Streptococcus pneumoniae GA44194. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760821; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44194; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44194."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOP01000004; EHD73984.1; -; Genomic_DNA. DR ProteinModelPortal; G6MWY6; -. DR EnsemblBacteria; EHD73984; EHD73984; SPAR80_0664. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6MWZ3_STREE Unreviewed; 210 AA. AC G6MWZ3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR80_0671; OS Streptococcus pneumoniae GA44194. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760821; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44194; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44194."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOP01000004; EHD73991.1; -; Genomic_DNA. DR ProteinModelPortal; G6MWZ3; -. DR EnsemblBacteria; EHD73991; EHD73991; SPAR80_0671. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22744 MW; A3239DF7871A7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6N360_STREE Unreviewed; 209 AA. AC G6N360; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR82_0648; OS Streptococcus pneumoniae GA44378. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760823; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44378; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44378."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOQ01000003; EHD78786.1; -; Genomic_DNA. DR ProteinModelPortal; G6N360; -. DR EnsemblBacteria; EHD78786; EHD78786; SPAR82_0648. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23275 MW; 54691E8B38ED4ED4 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LRGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6N367_STREE Unreviewed; 210 AA. AC G6N367; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR82_0655; OS Streptococcus pneumoniae GA44378. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760823; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44378; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44378."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOQ01000003; EHD78793.1; -; Genomic_DNA. DR ProteinModelPortal; G6N367; -. DR EnsemblBacteria; EHD78793; EHD78793; SPAR82_0655. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6N9T1_STREE Unreviewed; 209 AA. AC G6N9T1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR86_0691; OS Streptococcus pneumoniae GA44511. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760827; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44511; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44511."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOR01000010; EHD79686.1; -; Genomic_DNA. DR ProteinModelPortal; G6N9T1; -. DR EnsemblBacteria; EHD79686; EHD79686; SPAR86_0691. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23247 MW; 9D63833774B28637 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6N9T8_STREE Unreviewed; 210 AA. AC G6N9T8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR86_0698; OS Streptococcus pneumoniae GA44511. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760827; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44511; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44511."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOR01000010; EHD79693.1; -; Genomic_DNA. DR ProteinModelPortal; G6N9T8; -. DR EnsemblBacteria; EHD79693; EHD79693; SPAR86_0698. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6NG58_STREE Unreviewed; 209 AA. AC G6NG58; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR144_0645; OS Streptococcus pneumoniae NP170. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760885; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NP170; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae NP170."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOS01000005; EHD80345.1; -; Genomic_DNA. DR ProteinModelPortal; G6NG58; -. DR EnsemblBacteria; EHD80345; EHD80345; SPAR144_0645. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23275 MW; 54691E8B38ED4ED4 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LRGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6NG65_STREE Unreviewed; 210 AA. AC G6NG65; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR144_0652; OS Streptococcus pneumoniae NP170. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760885; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NP170; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae NP170."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOS01000005; EHD80352.1; -; Genomic_DNA. DR ProteinModelPortal; G6NG65; -. DR EnsemblBacteria; EHD80352; EHD80352; SPAR144_0652. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6NNR6_STREE Unreviewed; 209 AA. AC G6NNR6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR14_0674; OS Streptococcus pneumoniae GA07643. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760755; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA07643; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA07643."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOT01000001; EHD83471.1; -; Genomic_DNA. DR ProteinModelPortal; G6NNR6; -. DR EnsemblBacteria; EHD83471; EHD83471; SPAR14_0674. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6NNS3_STREE Unreviewed; 210 AA. AC G6NNS3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR14_0681; OS Streptococcus pneumoniae GA07643. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760755; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA07643; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA07643."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOT01000001; EHD83478.1; -; Genomic_DNA. DR ProteinModelPortal; G6NNS3; -. DR PRIDE; G6NNS3; -. DR EnsemblBacteria; EHD83478; EHD83478; SPAR14_0681. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; 60239DF9671A7380 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID G6NV38_STREE Unreviewed; 210 AA. AC G6NV38; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR22_0893; OS Streptococcus pneumoniae GA11304. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760763; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA11304; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA11304."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOU01000003; EHD88248.1; -; Genomic_DNA. DR ProteinModelPortal; G6NV38; -. DR EnsemblBacteria; EHD88248; EHD88248; SPAR22_0893. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6NV45_STREE Unreviewed; 209 AA. AC G6NV45; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR22_0900; OS Streptococcus pneumoniae GA11304. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760763; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA11304; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA11304."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOU01000003; EHD88255.1; -; Genomic_DNA. DR ProteinModelPortal; G6NV45; -. DR EnsemblBacteria; EHD88255; EHD88255; SPAR22_0900. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6P0Q1_STREE Unreviewed; 209 AA. AC G6P0Q1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR23_0722; OS Streptococcus pneumoniae GA11426. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760764; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA11426; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA11426."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOV01000003; EHE78567.1; -; Genomic_DNA. DR ProteinModelPortal; G6P0Q1; -. DR EnsemblBacteria; EHE78567; EHE78567; SPAR23_0722. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6P0Q8_STREE Unreviewed; 210 AA. AC G6P0Q8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR23_0729; OS Streptococcus pneumoniae GA11426. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760764; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA11426; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA11426."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOV01000003; EHE78574.1; -; Genomic_DNA. DR ProteinModelPortal; G6P0Q8; -. DR EnsemblBacteria; EHE78574; EHE78574; SPAR23_0729. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6P775_STREE Unreviewed; 209 AA. AC G6P775; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR24_0635; OS Streptococcus pneumoniae GA11663. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760765; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA11663; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA11663."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOW01000004; EHE78196.1; -; Genomic_DNA. DR ProteinModelPortal; G6P775; -. DR EnsemblBacteria; EHE78196; EHE78196; SPAR24_0635. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23275 MW; 54691E8B38ED4ED4 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LRGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6P782_STREE Unreviewed; 210 AA. AC G6P782; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR24_0642; OS Streptococcus pneumoniae GA11663. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760765; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA11663; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA11663."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOW01000004; EHE78203.1; -; Genomic_DNA. DR ProteinModelPortal; G6P782; -. DR EnsemblBacteria; EHE78203; EHE78203; SPAR24_0642. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6PDQ7_STREE Unreviewed; 209 AA. AC G6PDQ7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR28_0666; OS Streptococcus pneumoniae GA13338. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760769; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13338; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13338."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOX01000002; EHE81286.1; -; Genomic_DNA. DR EnsemblBacteria; EHE81286; EHE81286; SPAR28_0666. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23362 MW; A51A41EFBB2CC783 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6PDR4_STREE Unreviewed; 210 AA. AC G6PDR4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR28_0673; OS Streptococcus pneumoniae GA13338. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760769; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13338; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13338."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOX01000002; EHE81293.1; -; Genomic_DNA. DR ProteinModelPortal; G6PDR4; -. DR EnsemblBacteria; EHE81293; EHE81293; SPAR28_0673. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6PLM8_STREE Unreviewed; 209 AA. AC G6PLM8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR30_0696; OS Streptococcus pneumoniae GA13455. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760771; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13455; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13455."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOY01000004; EHD85843.1; -; Genomic_DNA. DR ProteinModelPortal; G6PLM8; -. DR EnsemblBacteria; EHD85843; EHD85843; SPAR30_0696. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6PLN5_STREE Unreviewed; 210 AA. AC G6PLN5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR30_0703; OS Streptococcus pneumoniae GA13455. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760771; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13455; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13455."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOY01000004; EHD85850.1; -; Genomic_DNA. DR ProteinModelPortal; G6PLN5; -. DR EnsemblBacteria; EHD85850; EHD85850; SPAR30_0703. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6PRH3_STREE Unreviewed; 209 AA. AC G6PRH3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR31_0713; OS Streptococcus pneumoniae GA13494. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760772; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13494; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13494."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOZ01000006; EHD89532.1; -; Genomic_DNA. DR ProteinModelPortal; G6PRH3; -. DR EnsemblBacteria; EHD89532; EHD89532; SPAR31_0713. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6PRI0_STREE Unreviewed; 210 AA. AC G6PRI0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR31_0720; OS Streptococcus pneumoniae GA13494. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760772; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13494; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13494."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGOZ01000006; EHD89539.1; -; Genomic_DNA. DR ProteinModelPortal; G6PRI0; -. DR EnsemblBacteria; EHD89539; EHD89539; SPAR31_0720. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22786 MW; 7BE4851AE6B66247 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GLEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID G6PYB3_STREE Unreviewed; 209 AA. AC G6PYB3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR32_0706; OS Streptococcus pneumoniae GA13637. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760773; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13637; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13637."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPA01000005; EHD96087.1; -; Genomic_DNA. DR ProteinModelPortal; G6PYB3; -. DR EnsemblBacteria; EHD96087; EHD96087; SPAR32_0706. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6PYC0_STREE Unreviewed; 210 AA. AC G6PYC0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR32_0713; OS Streptococcus pneumoniae GA13637. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760773; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13637; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13637."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPA01000005; EHD96094.1; -; Genomic_DNA. DR ProteinModelPortal; G6PYC0; -. DR EnsemblBacteria; EHD96094; EHD96094; SPAR32_0713. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6Q635_STREE Unreviewed; 209 AA. AC G6Q635; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR34_0640; OS Streptococcus pneumoniae GA13856. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760775; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13856; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13856."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPB01000003; EHD93060.1; -; Genomic_DNA. DR ProteinModelPortal; G6Q635; -. DR EnsemblBacteria; EHD93060; EHD93060; SPAR34_0640. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6Q642_STREE Unreviewed; 210 AA. AC G6Q642; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR34_0647; OS Streptococcus pneumoniae GA13856. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760775; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13856; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13856."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPB01000003; EHD93067.1; -; Genomic_DNA. DR EnsemblBacteria; EHD93067; EHD93067; SPAR34_0647. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22710 MW; A2119DE20A4F935E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT VAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6QCE8_STREE Unreviewed; 210 AA. AC G6QCE8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR37_1355; OS Streptococcus pneumoniae GA14798. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760778; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA14798; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA14798."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPC01000009; EHD95050.1; -; Genomic_DNA. DR ProteinModelPortal; G6QCE8; -. DR EnsemblBacteria; EHD95050; EHD95050; SPAR37_1355. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6QCF5_STREE Unreviewed; 209 AA. AC G6QCF5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR37_1362; OS Streptococcus pneumoniae GA14798. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760778; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA14798; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA14798."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPC01000009; EHD95057.1; -; Genomic_DNA. DR ProteinModelPortal; G6QCF5; -. DR EnsemblBacteria; EHD95057; EHD95057; SPAR37_1362. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6QHQ9_STREE Unreviewed; 209 AA. AC G6QHQ9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR38_0692; OS Streptococcus pneumoniae GA16121. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760779; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA16121; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA16121."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPD01000001; EHD99299.1; -; Genomic_DNA. DR ProteinModelPortal; G6QHQ9; -. DR EnsemblBacteria; EHD99299; EHD99299; SPAR38_0692. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6QHR6_STREE Unreviewed; 210 AA. AC G6QHR6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR38_0699; OS Streptococcus pneumoniae GA16121. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760779; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA16121; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA16121."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPD01000001; EHD99306.1; -; Genomic_DNA. DR ProteinModelPortal; G6QHR6; -. DR EnsemblBacteria; EHD99306; EHD99306; SPAR38_0699. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6QMN5_STREE Unreviewed; 209 AA. AC G6QMN5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR39_0706; OS Streptococcus pneumoniae GA16242. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760780; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA16242; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA16242."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPE01000002; EHE03216.1; -; Genomic_DNA. DR EnsemblBacteria; EHE03216; EHE03216; SPAR39_0706. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23302 MW; 094F9E0E007A2FA0 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGESALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6QMX4_STREE Unreviewed; 210 AA. AC G6QMX4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR39_0713; OS Streptococcus pneumoniae GA16242. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760780; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA16242; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA16242."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPE01000002; EHE03223.1; -; Genomic_DNA. DR ProteinModelPortal; G6QMX4; -. DR EnsemblBacteria; EHE03223; EHE03223; SPAR39_0713. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6QX37_STREE Unreviewed; 209 AA. AC G6QX37; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR41_0788; OS Streptococcus pneumoniae GA16833. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760782; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA16833; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA16833."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPF01000004; EHE03635.1; -; Genomic_DNA. DR ProteinModelPortal; G6QX37; -. DR EnsemblBacteria; EHE03635; EHE03635; SPAR41_0788. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6QX44_STREE Unreviewed; 210 AA. AC G6QX44; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR41_0795; OS Streptococcus pneumoniae GA16833. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760782; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA16833; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA16833."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPF01000004; EHE03642.1; -; Genomic_DNA. DR ProteinModelPortal; G6QX44; -. DR EnsemblBacteria; EHE03642; EHE03642; SPAR41_0795. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6R1F1_STREE Unreviewed; 209 AA. AC G6R1F1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR43_0689; OS Streptococcus pneumoniae GA17227. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760784; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17227; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA17227."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPG01000004; EHE05391.1; -; Genomic_DNA. DR EnsemblBacteria; EHE05391; EHE05391; SPAR43_0689. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23271 MW; B351214742E856CB CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVKYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6R1F8_STREE Unreviewed; 210 AA. AC G6R1F8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR43_0696; OS Streptococcus pneumoniae GA17227. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760784; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17227; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA17227."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPG01000004; EHE05398.1; -; Genomic_DNA. DR EnsemblBacteria; EHE05398; EHE05398; SPAR43_0696. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22740 MW; E8E4874C9DBCC48E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6R887_STREE Unreviewed; 209 AA. AC G6R887; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR49_0745; OS Streptococcus pneumoniae GA17328. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760790; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17328; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA17328."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPH01000004; EHE11473.1; -; Genomic_DNA. DR ProteinModelPortal; G6R887; -. DR EnsemblBacteria; EHE11473; EHE11473; SPAR49_0745. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6R894_STREE Unreviewed; 210 AA. AC G6R894; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR49_0752; OS Streptococcus pneumoniae GA17328. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760790; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17328; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA17328."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPH01000004; EHE11480.1; -; Genomic_DNA. DR ProteinModelPortal; G6R894; -. DR EnsemblBacteria; EHE11480; EHE11480; SPAR49_0752. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6REZ1_STREE Unreviewed; 209 AA. AC G6REZ1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR45_0690; OS Streptococcus pneumoniae GA17371. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760786; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17371; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA17371."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPI01000003; EHE12501.1; -; Genomic_DNA. DR ProteinModelPortal; G6REZ1; -. DR EnsemblBacteria; EHE12501; EHE12501; SPAR45_0690. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6REZ8_STREE Unreviewed; 210 AA. AC G6REZ8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR45_0697; OS Streptococcus pneumoniae GA17371. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760786; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17371; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA17371."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPI01000003; EHE12508.1; -; Genomic_DNA. DR ProteinModelPortal; G6REZ8; -. DR EnsemblBacteria; EHE12508; EHE12508; SPAR45_0697. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6RN14_STREE Unreviewed; 209 AA. AC G6RN14; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR52_0748; OS Streptococcus pneumoniae GA17971. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760793; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17971; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA17971."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPJ01000004; EHE10056.1; -; Genomic_DNA. DR ProteinModelPortal; G6RN14; -. DR EnsemblBacteria; EHE10056; EHE10056; SPAR52_0748. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6RN23_STREE Unreviewed; 210 AA. AC G6RN23; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR52_0757; OS Streptococcus pneumoniae GA17971. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760793; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17971; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA17971."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPJ01000004; EHE10065.1; -; Genomic_DNA. DR ProteinModelPortal; G6RN23; -. DR EnsemblBacteria; EHE10065; EHE10065; SPAR52_0757. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6RTA1_STREE Unreviewed; 209 AA. AC G6RTA1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR56_0904; OS Streptococcus pneumoniae GA19077. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760797; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA19077; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA19077."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPK01000003; EHE16820.1; -; Genomic_DNA. DR ProteinModelPortal; G6RTA1; -. DR EnsemblBacteria; EHE16820; EHE16820; SPAR56_0904. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6RTA8_STREE Unreviewed; 210 AA. AC G6RTA8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR56_0911; OS Streptococcus pneumoniae GA19077. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760797; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA19077; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA19077."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPK01000003; EHE16827.1; -; Genomic_DNA. DR EnsemblBacteria; EHE16827; EHE16827; SPAR56_0911. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22728 MW; E8F9319141D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGAGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6RYU1_STREE Unreviewed; 209 AA. AC G6RYU1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR58_0711; OS Streptococcus pneumoniae GA19451. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760799; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA19451; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA19451."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPL01000009; EHE17188.1; -; Genomic_DNA. DR ProteinModelPortal; G6RYU1; -. DR EnsemblBacteria; EHE17188; EHE17188; SPAR58_0711. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6RYU8_STREE Unreviewed; 210 AA. AC G6RYU8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR58_0718; OS Streptococcus pneumoniae GA19451. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760799; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA19451; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA19451."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPL01000009; EHE17195.1; -; Genomic_DNA. DR ProteinModelPortal; G6RYU8; -. DR EnsemblBacteria; EHE17195; EHE17195; SPAR58_0718. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6S4C9_STREE Unreviewed; 76 AA. AC G6S4C9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE1; ORFNames=SPAR67_0679; OS Streptococcus pneumoniae GA41277. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760808; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41277; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41277."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPM01000002; EHE19851.1; -; Genomic_DNA. DR EnsemblBacteria; EHE19851; EHE19851; SPAR67_0679. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 76 AA; 8656 MW; 80BAD410E8EF04AC CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKNTMFH LSLMTI // ID G6S4D0_STREE Unreviewed; 118 AA. AC G6S4D0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI family protein; GN ORFNames=SPAR67_0680; OS Streptococcus pneumoniae GA41277. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760808; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41277; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41277."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPM01000002; EHE19852.1; -; Genomic_DNA. DR EnsemblBacteria; EHE19852; EHE19852; SPAR67_0680. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 118 AA; 12905 MW; F829784985B7D337 CRC64; MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKI // ID G6S4D7_STREE Unreviewed; 210 AA. AC G6S4D7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR67_0687; OS Streptococcus pneumoniae GA41277. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760808; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41277; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41277."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPM01000002; EHE19859.1; -; Genomic_DNA. DR ProteinModelPortal; G6S4D7; -. DR EnsemblBacteria; EHE19859; EHE19859; SPAR67_0687. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6SCB2_STREE Unreviewed; 209 AA. AC G6SCB2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR71_0756; OS Streptococcus pneumoniae GA41437. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760812; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41437; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41437."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPN01000004; EHE24126.1; -; Genomic_DNA. DR ProteinModelPortal; G6SCB2; -. DR EnsemblBacteria; EHE24126; EHE24126; SPAR71_0756. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6SCB9_STREE Unreviewed; 210 AA. AC G6SCB9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR71_0763; OS Streptococcus pneumoniae GA41437. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760812; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41437; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41437."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPN01000004; EHE24133.1; -; Genomic_DNA. DR ProteinModelPortal; G6SCB9; -. DR EnsemblBacteria; EHE24133; EHE24133; SPAR71_0763. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6SK44_STREE Unreviewed; 209 AA. AC G6SK44; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR73_0666; OS Streptococcus pneumoniae GA41565. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760814; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41565; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41565."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPO01000002; EHE24557.1; -; Genomic_DNA. DR ProteinModelPortal; G6SK44; -. DR EnsemblBacteria; EHE24557; EHE24557; SPAR73_0666. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23275 MW; 54691E8B38ED4ED4 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LRGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6SK51_STREE Unreviewed; 210 AA. AC G6SK51; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR73_0673; OS Streptococcus pneumoniae GA41565. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760814; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41565; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41565."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPO01000002; EHE24564.1; -; Genomic_DNA. DR ProteinModelPortal; G6SK51; -. DR EnsemblBacteria; EHE24564; EHE24564; SPAR73_0673. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6SQ88_STREE Unreviewed; 209 AA. AC G6SQ88; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR74_0678; OS Streptococcus pneumoniae GA41688. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760815; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41688; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41688."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPP01000003; EHE26434.1; -; Genomic_DNA. DR EnsemblBacteria; EHE26434; EHE26434; SPAR74_0678. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23362 MW; A51A41EFBB2CC783 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6SQ95_STREE Unreviewed; 210 AA. AC G6SQ95; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR74_0685; OS Streptococcus pneumoniae GA41688. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760815; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA41688; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA41688."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPP01000003; EHE26441.1; -; Genomic_DNA. DR ProteinModelPortal; G6SQ95; -. DR EnsemblBacteria; EHE26441; EHE26441; SPAR74_0685. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6SVT7_STREE Unreviewed; 209 AA. AC G6SVT7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR78_0717; OS Streptococcus pneumoniae GA43380. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760819; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA43380; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA43380."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPQ01000003; EHE30556.1; -; Genomic_DNA. DR ProteinModelPortal; G6SVT7; -. DR EnsemblBacteria; EHE30556; EHE30556; SPAR78_0717. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6SVU4_STREE Unreviewed; 210 AA. AC G6SVU4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR78_0724; OS Streptococcus pneumoniae GA43380. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760819; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA43380; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA43380."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPQ01000003; EHE30563.1; -; Genomic_DNA. DR ProteinModelPortal; G6SVU4; -. DR EnsemblBacteria; EHE30563; EHE30563; SPAR78_0724. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6T2S7_STREE Unreviewed; 209 AA. AC G6T2S7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR91_0676; OS Streptococcus pneumoniae GA47283. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760832; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47283; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47283."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPR01000003; EHE32075.1; -; Genomic_DNA. DR ProteinModelPortal; G6T2S7; -. DR EnsemblBacteria; EHE32075; EHE32075; SPAR91_0676. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23244 MW; 69798D236EB6C679 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6T2T4_STREE Unreviewed; 210 AA. AC G6T2T4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR91_0683; OS Streptococcus pneumoniae GA47283. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760832; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47283; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47283."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPR01000003; EHE32082.1; -; Genomic_DNA. DR ProteinModelPortal; G6T2T4; -. DR EnsemblBacteria; EHE32082; EHE32082; SPAR91_0683. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6T988_STREE Unreviewed; 209 AA. AC G6T988; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR92_0694; OS Streptococcus pneumoniae GA47360. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760833; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47360; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47360."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPS01000004; EHE33296.1; -; Genomic_DNA. DR ProteinModelPortal; G6T988; -. DR EnsemblBacteria; EHE33296; EHE33296; SPAR92_0694. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6T995_STREE Unreviewed; 210 AA. AC G6T995; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR92_0701; OS Streptococcus pneumoniae GA47360. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760833; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47360; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47360."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPS01000004; EHE33303.1; -; Genomic_DNA. DR ProteinModelPortal; G6T995; -. DR PRIDE; G6T995; -. DR EnsemblBacteria; EHE33303; EHE33303; SPAR92_0701. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; 60239DF9671A7380 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID G6TGK7_STREE Unreviewed; 209 AA. AC G6TGK7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR94_0699; OS Streptococcus pneumoniae GA47373. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760835; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47373; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47373."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPT01000002; EHE36056.1; -; Genomic_DNA. DR EnsemblBacteria; EHE36056; EHE36056; SPAR94_0699. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23286 MW; AB8636BA21C660B9 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGAITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6TGL4_STREE Unreviewed; 210 AA. AC G6TGL4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR94_0706; OS Streptococcus pneumoniae GA47373. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760835; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47373; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47373."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPT01000002; EHE36063.1; -; Genomic_DNA. DR ProteinModelPortal; G6TGL4; -. DR EnsemblBacteria; EHE36063; EHE36063; SPAR94_0706. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6TLP6_STREE Unreviewed; 209 AA. AC G6TLP6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR96_0673; OS Streptococcus pneumoniae GA47388. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760837; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47388; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47388."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPU01000001; EHE38708.1; -; Genomic_DNA. DR ProteinModelPortal; G6TLP6; -. DR EnsemblBacteria; EHE38708; EHE38708; SPAR96_0673. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23247 MW; 9D63833774B28637 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6TLQ3_STREE Unreviewed; 210 AA. AC G6TLQ3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR96_0680; OS Streptococcus pneumoniae GA47388. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760837; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47388; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47388."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPU01000001; EHE38715.1; -; Genomic_DNA. DR ProteinModelPortal; G6TLQ3; -. DR EnsemblBacteria; EHE38715; EHE38715; SPAR96_0680. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6TSZ2_STREE Unreviewed; 209 AA. AC G6TSZ2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR119_0638; OS Streptococcus pneumoniae GA47439. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760860; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47439; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47439."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPV01000004; EHE40027.1; -; Genomic_DNA. DR ProteinModelPortal; G6TSZ2; -. DR EnsemblBacteria; EHE40027; EHE40027; SPAR119_0638. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6TSZ9_STREE Unreviewed; 210 AA. AC G6TSZ9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR119_0645; OS Streptococcus pneumoniae GA47439. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760860; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47439; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47439."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPV01000004; EHE40034.1; -; Genomic_DNA. DR ProteinModelPortal; G6TSZ9; -. DR EnsemblBacteria; EHE40034; EHE40034; SPAR119_0645. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6TZW0_STREE Unreviewed; 210 AA. AC G6TZW0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR103_0883; OS Streptococcus pneumoniae GA47688. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760844; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47688; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47688."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPW01000005; EHE42150.1; -; Genomic_DNA. DR ProteinModelPortal; G6TZW0; -. DR EnsemblBacteria; EHE42150; EHE42150; SPAR103_0883. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6TZW7_STREE Unreviewed; 209 AA. AC G6TZW7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR103_0890; OS Streptococcus pneumoniae GA47688. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760844; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47688; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47688."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPW01000005; EHE42157.1; -; Genomic_DNA. DR ProteinModelPortal; G6TZW7; -. DR EnsemblBacteria; EHE42157; EHE42157; SPAR103_0890. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6U6Z6_STREE Unreviewed; 210 AA. AC G6U6Z6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR106_1382; OS Streptococcus pneumoniae GA47778. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760847; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47778; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47778."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPX01000009; EHE42862.1; -; Genomic_DNA. DR ProteinModelPortal; G6U6Z6; -. DR EnsemblBacteria; EHE42862; EHE42862; SPAR106_1382. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6U703_STREE Unreviewed; 209 AA. AC G6U703; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR106_1389; OS Streptococcus pneumoniae GA47778. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760847; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47778; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47778."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPX01000009; EHE42869.1; -; Genomic_DNA. DR ProteinModelPortal; G6U703; -. DR EnsemblBacteria; EHE42869; EHE42869; SPAR106_1389. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6UB52_STREE Unreviewed; 209 AA. AC G6UB52; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR109_0661; OS Streptococcus pneumoniae GA47976. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760850; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47976; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47976."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPY01000003; EHE46159.1; -; Genomic_DNA. DR ProteinModelPortal; G6UB52; -. DR EnsemblBacteria; EHE46159; EHE46159; SPAR109_0661. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6UB59_STREE Unreviewed; 210 AA. AC G6UB59; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR109_0668; OS Streptococcus pneumoniae GA47976. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760850; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47976; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47976."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPY01000003; EHE46254.1; -; Genomic_DNA. DR EnsemblBacteria; EHE46254; EHE46254; SPAR109_0668. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; E8E496ABC1C7E57E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APIILISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6UHT2_STREE Unreviewed; 209 AA. AC G6UHT2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR115_0711; OS Streptococcus pneumoniae GA52306. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760856; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA52306; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA52306."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPZ01000008; EHE47690.1; -; Genomic_DNA. DR EnsemblBacteria; EHE47690; EHE47690; SPAR115_0711. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23352 MW; 24457EFDA912E780 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KYDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6UHT9_STREE Unreviewed; 210 AA. AC G6UHT9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR115_0718; OS Streptococcus pneumoniae GA52306. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760856; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA52306; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA52306."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGPZ01000008; EHE47697.1; -; Genomic_DNA. DR EnsemblBacteria; EHE47697; EHE47697; SPAR115_0718. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; 2BE4904FBC77D49C CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID G6UNW1_STREE Unreviewed; 209 AA. AC G6UNW1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR118_0679; OS Streptococcus pneumoniae GA54644. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760859; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA54644; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA54644."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQA01000001; EHE51041.1; -; Genomic_DNA. DR ProteinModelPortal; G6UNW1; -. DR EnsemblBacteria; EHE51041; EHE51041; SPAR118_0679. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23247 MW; 9D63833774B28637 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6UNW8_STREE Unreviewed; 210 AA. AC G6UNW8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR118_0686; OS Streptococcus pneumoniae GA54644. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760859; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA54644; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA54644."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQA01000001; EHE51048.1; -; Genomic_DNA. DR ProteinModelPortal; G6UNW8; -. DR EnsemblBacteria; EHE51048; EHE51048; SPAR118_0686. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6UVH2_STREE Unreviewed; 209 AA. AC G6UVH2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR147_0677; OS Streptococcus pneumoniae Netherlands15B-37. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760888; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Netherlands15B-37; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae Netherlands 15B-37."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQB01000004; EHE53080.1; -; Genomic_DNA. DR ProteinModelPortal; G6UVH2; -. DR EnsemblBacteria; EHE53080; EHE53080; SPAR147_0677. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6UVH9_STREE Unreviewed; 210 AA. AC G6UVH9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR147_0684; OS Streptococcus pneumoniae Netherlands15B-37. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760888; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Netherlands15B-37; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae Netherlands 15B-37."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQB01000004; EHE53087.1; -; Genomic_DNA. DR ProteinModelPortal; G6UVH9; -. DR EnsemblBacteria; EHE53087; EHE53087; SPAR147_0684. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6V0X2_STREE Unreviewed; 209 AA. AC G6V0X2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR145_0737; OS Streptococcus pneumoniae NP127. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760886; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NP127; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae NP127."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQC01000005; EHE56503.1; -; Genomic_DNA. DR ProteinModelPortal; G6V0X2; -. DR EnsemblBacteria; EHE56503; EHE56503; SPAR145_0737. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6V0X9_STREE Unreviewed; 210 AA. AC G6V0X9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR145_0744; OS Streptococcus pneumoniae NP127. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760886; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NP127; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae NP127."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQC01000005; EHE56510.1; -; Genomic_DNA. DR ProteinModelPortal; G6V0X9; -. DR EnsemblBacteria; EHE56510; EHE56510; SPAR145_0744. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6V7U0_STREE Unreviewed; 209 AA. AC G6V7U0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR104_0565; OS Streptococcus pneumoniae GA47751. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760845; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47751; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47751."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQD01000004; EHE57354.1; -; Genomic_DNA. DR ProteinModelPortal; G6V7U0; -. DR EnsemblBacteria; EHE57354; EHE57354; SPAR104_0565. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6V7U7_STREE Unreviewed; 210 AA. AC G6V7U7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR104_0572; OS Streptococcus pneumoniae GA47751. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760845; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47751; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47751."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQD01000004; EHE57361.1; -; Genomic_DNA. DR EnsemblBacteria; EHE57361; EHE57361; SPAR104_0572. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22728 MW; E8F9319141D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGAGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6VEH7_STREE Unreviewed; 209 AA. AC G6VEH7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR127_0685; OS Streptococcus pneumoniae 5185-06. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760868; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5185-06; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 5185-06."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQE01000003; EHE60078.1; -; Genomic_DNA. DR ProteinModelPortal; G6VEH7; -. DR EnsemblBacteria; EHE60078; EHE60078; SPAR127_0685. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6VEI4_STREE Unreviewed; 210 AA. AC G6VEI4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR127_0692; OS Streptococcus pneumoniae 5185-06. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760868; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5185-06; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 5185-06."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQE01000003; EHE60085.1; -; Genomic_DNA. DR ProteinModelPortal; G6VEI4; -. DR EnsemblBacteria; EHE60085; EHE60085; SPAR127_0692. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6VKL4_STREE Unreviewed; 209 AA. AC G6VKL4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR141_0669; OS Streptococcus pneumoniae NP112. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760882; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NP112; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae NP112."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQF01000003; EHE62262.1; -; Genomic_DNA. DR EnsemblBacteria; EHE62262; EHE62262; SPAR141_0669. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23302 MW; 094F9E0E007A2FA0 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGESALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6VKM1_STREE Unreviewed; 210 AA. AC G6VKM1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR141_0676; OS Streptococcus pneumoniae NP112. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760882; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NP112; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae NP112."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQF01000003; EHE62269.1; -; Genomic_DNA. DR ProteinModelPortal; G6VKM1; -. DR EnsemblBacteria; EHE62269; EHE62269; SPAR141_0676. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6VRS0_STREE Unreviewed; 209 AA. AC G6VRS0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR135_0685; OS Streptococcus pneumoniae 3063-00. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760876; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3063-00; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 3063-00."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQG01000003; EHE62719.1; -; Genomic_DNA. DR ProteinModelPortal; G6VRS0; -. DR EnsemblBacteria; EHE62719; EHE62719; SPAR135_0685. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6VRS7_STREE Unreviewed; 210 AA. AC G6VRS7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR135_0692; OS Streptococcus pneumoniae 3063-00. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760876; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3063-00; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 3063-00."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQG01000003; EHE62726.1; -; Genomic_DNA. DR ProteinModelPortal; G6VRS7; -. DR EnsemblBacteria; EHE62726; EHE62726; SPAR135_0692. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6VXV8_STREE Unreviewed; 209 AA. AC G6VXV8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR136_0705; OS Streptococcus pneumoniae EU-NP01. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760877; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EU-NP01; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae EU-NP01."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQH01000004; EHE70087.1; -; Genomic_DNA. DR ProteinModelPortal; G6VXV8; -. DR EnsemblBacteria; EHE70087; EHE70087; SPAR136_0705. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6VXW5_STREE Unreviewed; 210 AA. AC G6VXW5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR136_0712; OS Streptococcus pneumoniae EU-NP01. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760877; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EU-NP01; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae EU-NP01."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQH01000004; EHE70094.1; -; Genomic_DNA. DR ProteinModelPortal; G6VXW5; -. DR PRIDE; G6VXW5; -. DR EnsemblBacteria; EHE70094; EHE70094; SPAR136_0712. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; 60239DF9671A7380 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID G6W4G9_STREE Unreviewed; 209 AA. AC G6W4G9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR13_0690; OS Streptococcus pneumoniae GA07228. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760754; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA07228; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA07228."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQI01000003; EHE67871.1; -; Genomic_DNA. DR ProteinModelPortal; G6W4G9; -. DR EnsemblBacteria; EHE67871; EHE67871; SPAR13_0690. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6W4H6_STREE Unreviewed; 210 AA. AC G6W4H6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR13_0697; OS Streptococcus pneumoniae GA07228. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760754; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA07228; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA07228."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQI01000003; EHE67878.1; -; Genomic_DNA. DR ProteinModelPortal; G6W4H6; -. DR EnsemblBacteria; EHE67878; EHE67878; SPAR13_0697. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6WAI3_STREE Unreviewed; 209 AA. AC G6WAI3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR17_0685; OS Streptococcus pneumoniae GA08780. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760758; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA08780; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA08780."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQJ01000002; EHE69121.1; -; Genomic_DNA. DR ProteinModelPortal; G6WAI3; -. DR EnsemblBacteria; EHE69121; EHE69121; SPAR17_0685. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23247 MW; 9D63833774B28637 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6WAJ0_STREE Unreviewed; 210 AA. AC G6WAJ0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR17_0692; OS Streptococcus pneumoniae GA08780. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760758; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA08780; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA08780."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQJ01000002; EHE69128.1; -; Genomic_DNA. DR ProteinModelPortal; G6WAJ0; -. DR EnsemblBacteria; EHE69128; EHE69128; SPAR17_0692. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6WFA6_STREE Unreviewed; 209 AA. AC G6WFA6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR59_0630; OS Streptococcus pneumoniae GA19690. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760800; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA19690; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA19690."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQK01000001; EHE73762.1; -; Genomic_DNA. DR ProteinModelPortal; G6WFA6; -. DR EnsemblBacteria; EHE73762; EHE73762; SPAR59_0630. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID G6WFB3_STREE Unreviewed; 210 AA. AC G6WFB3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR59_0637; OS Streptococcus pneumoniae GA19690. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760800; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA19690; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA19690."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQK01000001; EHE73769.1; -; Genomic_DNA. DR ProteinModelPortal; G6WFB3; -. DR EnsemblBacteria; EHE73769; EHE73769; SPAR59_0637. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6WMY9_STREE Unreviewed; 209 AA. AC G6WMY9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR146_0743; OS Streptococcus pneumoniae NorthCarolina6A-23. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760887; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NorthCarolina6A-23; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae NorthCarolina6A-23."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQL01000006; EHE74455.1; -; Genomic_DNA. DR ProteinModelPortal; G6WMY9; -. DR EnsemblBacteria; EHE74455; EHE74455; SPAR146_0743. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID G6WMZ6_STREE Unreviewed; 210 AA. AC G6WMZ6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR146_0750; OS Streptococcus pneumoniae NorthCarolina6A-23. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760887; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NorthCarolina6A-23; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Sadzewicz L., Tallon L.J., RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae NorthCarolina6A-23."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQL01000006; EHE74462.1; -; Genomic_DNA. DR ProteinModelPortal; G6WMZ6; -. DR EnsemblBacteria; EHE74462; EHE74462; SPAR146_0750. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID G6WX28_CORGT Unreviewed; 221 AA. AC G6WX28; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=KIQ_08646; OS Corynebacterium glutamicum ATCC 14067. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1079988; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14067; RX PubMed=22247536; DOI=10.1128/JB.06514-11; RA Lv Y., Liao J., Wu Z., Han S., Lin Y., Zheng S.; RT "Genome Sequence of Corynebacterium glutamicum ATCC 14067, Which RT Provides Insight into Amino Acid Biosynthesis in Coryneform RT Bacteria."; RL J. Bacteriol. 194:742-743(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQQ01000026; EHE83392.1; -; Genomic_DNA. DR EnsemblBacteria; EHE83392; EHE83392; KIQ_08646. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). SQ SEQUENCE 221 AA; 23158 MW; C06316E922514B02 CRC64; MFENRFDLRC YVVTGAGSVD EVVHTASAAA RGGAGVVQVR SKPISPEAMR ELASKVALEV ARYSPTTRVL IDDHLHVASS LMREGLPIHG VHLGQDDVSV LEARELLGPE AIIGLTTGTL ELVAAANELS DVLDYIGAGP FRKTPTKDSG RPPIGLAGYP PLVELSKVPI VAIGDVTPAD VRALSATGVA GVAMVRAFSE SDDPQQVAEN VVANFELGRL S // ID G6X0R9_CORGT Unreviewed; 763 AA. AC G6X0R9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE SubName: Full=Multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; DE EC=2.7.4.7; GN ORFNames=KIQ_15293; OS Corynebacterium glutamicum ATCC 14067. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1079988; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14067; RX PubMed=22247536; DOI=10.1128/JB.06514-11; RA Lv Y., Liao J., Wu Z., Han S., Lin Y., Zheng S.; RT "Genome Sequence of Corynebacterium glutamicum ATCC 14067, Which RT Provides Insight into Amino Acid Biosynthesis in Coryneform RT Bacteria."; RL J. Bacteriol. 194:742-743(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQQ01000042; EHE82000.1; -; Genomic_DNA. DR EnsemblBacteria; EHE82000; EHE82000; KIQ_15293. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.910.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF03070; TENA_THI-4; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; SSF48613; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Kinase; Transferase. SQ SEQUENCE 763 AA; 80542 MW; A436612D089EF015 CRC64; MTDFSLYLVT DPVLGGGPEK VAGIVDSAIS GGVSVVQLRD KNSGVEDVRA AARELKELCD ARGVALVVND YLDIAVELGL HLHIGQGDTP YTQARELLPA HLELGLSIEN LDQLHAVIAQ CAETGVALPD VIGIGPVAST ATKPDAAPAL GVEGIAEIAA VAQDHGIASV AIGGVGLRNA AELAATPIDG LCVVSEIMTA ANPAAAATRL RTAFQPTFLP ETQTELSQTE LQGAFVNSPS APRVLSIAGT DPTGGAGIQA DLKSIAAGGG YGMCVVTSLV AQNTHGVNTI HTPPLTFLEE QLEAVFSDVT VDAIKLGMLG SADTVDLVAS WLGSHEHGPV VLDPVMIATS GDRLLDASAE ESLRRLAVHV DVVTPNIPEL AVLCDSAPAI TMDEAIAQAQ GFARTHDTIV IVKGGHLTGT LADNAVVRPD GSVFQVENLR VNTTNSHGTG CSLSASLATR IAAGESVEKA LEWSTRWLNE ALRHADHLAV GTGNGPVDHG HLARRMTHAA ETTPWAHLRT PRLDGATAAS FTTPSTVKSP APRIEPAGPF TRALWEASGD IIADINSSDF ITMLGDGTLR RPEFDFYIDQ DAQYLAQYSR ALARLSSIAP DSHAQIEWAQ SAAECLVVEA ELHRSYMAGK EVSAPSHITM AYTDFLIART YTEDYVCGVA AVLPCYWLYA EIGLMLAEQN HDEHPYKDWL NTYSGEEFIA GTRAAIARLE NALENAGAEQ RVDAARAFLS ASVHEREFFD QATRHGWTMV GSS // ID G6XA38_MYCAB Unreviewed; 223 AA. AC G6XA38; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MAB47J26_16002; OS Mycobacterium abscessus 47J26. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium abscessus. OX NCBI_TaxID=1087483; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=47J26; RA Chan J.Z.-M., Halachev M.R., Yates E., Smith G., Pallen M.J.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=47J26; RX PubMed=22207751; DOI=10.1128/JB.06440-11; RA Chan J., Halachev M., Yates E., Smith G., Pallen M.; RT "Whole-genome sequence of the emerging pathogen Mycobacterium RT abscessus strain 47J26."; RL J. Bacteriol. 194:549-549(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQU01000003; EHB98711.1; -; Genomic_DNA. DR EnsemblBacteria; EHB98711; EHB98711; MAB47J26_16002. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23450 MW; FBB584AFB530EB58 CRC64; MHSRSARLQS AHLYLCTDAR RERGDLAEFV DAALAGGVDI VQLRDKGSAG ERQFGRLEPT EELEYLAILS EAAARHGALF AVNDRADIAR AAGADVLHLG QDDLPLAVAR EIVGPDVLIG RSTHDAEQAT AAARDDEIDY FCCGPCWPTP TKPGRTASGL GLVHAAAELG TSKPWFAIGG IDQARVPEVV EAGASRIVVV RAITAAADPR AAAASLRGST HRA // ID G6XI53_9PROT Unreviewed; 206 AA. AC G6XI53; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=GMO_12630; OS Gluconobacter morbifer G707. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=1088869; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=G707; RA Lee W.-J., Kim E.-K.; RT "Genome sequence of Gluconobacter morbifer G707, isolated from RT Drosophila gut."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQV01000002; EHH68493.1; -; Genomic_DNA. DR EnsemblBacteria; EHH68493; EHH68493; GMO_12630. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 206 AA; 22836 MW; 10311D7F59DC46B0 CRC64; MSRLPSKIYP VVDHPRWVET LGSAGARFIE LYLRDLDLPE EELRAQAITA QELAVRHNVT LVLNTYWQIA IELGYEWVHL GPEDLATADL TTLRNSGIRL GTATHTHTEF EKALAISPDY ISFGPVWETK SVKTTFAPQG LERLKEWRGL CGDVPLVAIG GVTLEHLPAC LEAGADSVAG MSGFMKQDDP EGQVRRWLEA ARSFPA // ID G6XKN8_9PROT Unreviewed; 194 AA. AC G6XKN8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-MAR-2014, entry version 11. DE SubName: Full=Uncharacterized protein; GN ORFNames=GMO_20540; OS Gluconobacter morbifer G707. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=1088869; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=G707; RA Lee W.-J., Kim E.-K.; RT "Genome sequence of Gluconobacter morbifer G707, isolated from RT Drosophila gut."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQV01000007; EHH67601.1; -; Genomic_DNA. DR EnsemblBacteria; EHH67601; EHH67601; GMO_20540. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 20879 MW; 865C2472E851E3B2 CRC64; MTSTSCDLYP VLPASFDNDD MLATLPIILA HPEVTALRIP GDHRLNETEL NTLLKFLHES EVALIVDVGT DLSTAVPELL GESDGLHAPD PLQLTALRKQ LEGDIQIGCR CQTRDDAMKA GETGADYVAF TPTELDILRW WVSVMELPAV AEEITTPEAA VSARKAGADF LAIPLLLDDS DEARFTAILG ALAA // ID G6XVM9_RHIRD Unreviewed; 217 AA. AC G6XVM9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=ATCR1_13568; OS Agrobacterium tumefaciens CCNWGS0286. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=1082932; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWGS0286; RX PubMed=22636006; DOI=10.1128/AEM.01200-12; RA Hao X., Xie P., Johnstone L., Miller S.J., Rensing C., Wei G.; RT "Genome Sequence and Mutational Analysis of Plant-Growth-Promoting RT Bacterium Agrobacterium tumefaciens CCNWGS0286 Isolated from a Zinc- RT Lead Mine Tailing."; RL Appl. Environ. Microbiol. 78:5384-5394(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSM01000007; EHH05744.1; -; Genomic_DNA. DR EnsemblBacteria; EHH05744; EHH05744; ATCR1_13568. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 217 AA; 22690 MW; 83BE8959181C01C6 CRC64; MTLVEDRCRL VLIVPESDDA QKQATEVEEA LRGGDVASVI IPQYGLDDAA FQKRAELIVP VVQKAGAAAL IAGDSRVAGR VKADGLHVAG NAEALAEAVE KFTPKLIVGG GNADDRHKAL EQGESNPDYV FFGKLEGDIK PEAHPKNLAL GEWWASMIEI PAIVMGGTDV SSVVAVAETG VEFVAMRSGV FDNAGGAAQA VSEINALLDE KAPRFGG // ID G6XW01_RHIRD Unreviewed; 220 AA. AC G6XW01; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ATCR1_14186; OS Agrobacterium tumefaciens CCNWGS0286. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=1082932; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWGS0286; RX PubMed=22636006; DOI=10.1128/AEM.01200-12; RA Hao X., Xie P., Johnstone L., Miller S.J., Rensing C., Wei G.; RT "Genome Sequence and Mutational Analysis of Plant-Growth-Promoting RT Bacterium Agrobacterium tumefaciens CCNWGS0286 Isolated from a Zinc- RT Lead Mine Tailing."; RL Appl. Environ. Microbiol. 78:5384-5394(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSM01000008; EHH05286.1; -; Genomic_DNA. DR EnsemblBacteria; EHH05286; EHH05286; ATCR1_14186. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23002 MW; 44356E5BB4060A14 CRC64; MNKVDYRLNA LVDASLSDVA PLPELALAAA LNGATILQYR DKHGSTREMI ENARAIHEAI AGTGVPLVIN DRVDVALASG ADGVHLGADD MDAKTARRIL GEKAIIGLTV KNRADAERAA SMPVDYACIG GVFETVSKVN PDKPVGIDGF ATLRALLREW RPDMPVGAIA GIDLARVPSV IKAGADGVAV ISAIFRAADI ASAAKDFRSA IDATLKARQP // ID G6Y2W7_9RHIZ Unreviewed; 201 AA. AC G6Y2W7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MEA186_01416; OS Mesorhizobium amorphae CCNWGS0123. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1082933; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWGS0123; RX PubMed=22247533; DOI=10.1128/JB.06475-11; RA Hao X., Lin Y., Johnstone L., Baltrus D.A., Miller S.J., Wei G., RA Rensing C.; RT "Draft Genome Sequence of Plant Growth-Promoting Rhizobium RT Mesorhizobium amorphae, Isolated from Zinc-Lead Mine Tailings."; RL J. Bacteriol. 194:736-737(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSN01000015; EHH13944.1; -; Genomic_DNA. DR EnsemblBacteria; EHH13944; EHH13944; MEA186_01416. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22508 MW; 26C621E76E558ACB CRC64; MTLDPFYLIV DSAVWIERLV PLGVKLVQLR IKDRDEATLR TEIRRANDVC AVHCCQLVVN DHWRLAIEEG CDFVHLGQED LAAADLMAIK YSGLKVGLST HDHAELQTAL AVEPDYVALG PIYPTSLKKM KWAPQGLERI CEWKRRAAPI PLVAIGGLNP DRLDGVFAAG ADCAAVVTDI TRNENPEART REWIEKTGRW R // ID G6Y435_9RHIZ Unreviewed; 215 AA. AC G6Y435; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=MEA186_03469; OS Mesorhizobium amorphae CCNWGS0123. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1082933; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWGS0123; RX PubMed=22247533; DOI=10.1128/JB.06475-11; RA Hao X., Lin Y., Johnstone L., Baltrus D.A., Miller S.J., Wei G., RA Rensing C.; RT "Draft Genome Sequence of Plant Growth-Promoting Rhizobium RT Mesorhizobium amorphae, Isolated from Zinc-Lead Mine Tailings."; RL J. Bacteriol. 194:736-737(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSN01000048; EHH13486.1; -; Genomic_DNA. DR EnsemblBacteria; EHH13486; EHH13486; MEA186_03469. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 215 AA; 22628 MW; 6F608053EC20BE1A CRC64; MNDATPPNRC RIVLIAPKDA PAERIAAAFE GGDVASLILP ENGMDEASFQ AFAEQIVPAA QAAGIAVVIA GDSRIAGRVQ ADGIHVEVSK GELAETIEHF QGKMMVGAGG AKTRDDALEL GEARPDYIFF GRFGYDNKPE PHPRNLSLGQ WWADMIQIPC IVMAGSEIAS VETVAATGAE FVALSSAVFA DGIDPKTAVA TANAMLDETA PRFED // ID G6YTN0_9ALTE Unreviewed; 219 AA. AC G6YTN0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=KYE_11109; OS Marinobacter manganoxydans MnI7-9. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=1094979; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MnI7-9; RX PubMed=22275098; DOI=10.1128/JB.06551-11; RA Wang H., Li H., Shao Z., Liao S., Johnstone L., Rensing C., Wang G.; RT "Genome Sequence of Deep-Sea Manganese-Oxidizing Bacterium RT Marinobacter manganoxydans MnI7-9."; RL J. Bacteriol. 194:899-900(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTR01000039; EHJ04445.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ04445; EHJ04445; KYE_11109. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22630 MW; C4D19F719CC2A220 CRC64; MSKGLRPGLY AITDSVLTPP ETLIESVEAA LRGGAVMVQY REKSAPMAER ISQAVSLQAV CRNAGVPLLI NDDPDLAKRV GAAGVHMGQT DGSVAAARRL LGDEAIIGIT CHADLALAQA ALGAGADYLA FGRFYTSSTK PGAPAAPPGV LTDAKRFGLP ITAIGGVTTD NGEPLIRAGA DMLAVVGGLF GGDTHDIEMR AKAFERLFAS HHPLFSLPE // ID G6YXX1_9ALTE Unreviewed; 323 AA. AC G6YXX1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Mutator MutT protein; GN ORFNames=KYE_18958; OS Marinobacter manganoxydans MnI7-9. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=1094979; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MnI7-9; RX PubMed=22275098; DOI=10.1128/JB.06551-11; RA Wang H., Li H., Shao Z., Liao S., Johnstone L., Rensing C., Wang G.; RT "Genome Sequence of Deep-Sea Manganese-Oxidizing Bacterium RT Marinobacter manganoxydans MnI7-9."; RL J. Bacteriol. 194:899-900(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTR01000084; EHJ03183.1; -; Genomic_DNA. DR ProteinModelPortal; G6YXX1; -. DR EnsemblBacteria; EHJ03183; EHJ03183; KYE_18958. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 323 AA; 34633 MW; 4213A700A957CFF5 CRC64; MSARETPVKE VHVAVAVIVR DGRVLIARRP DHVHQGGLLE FPGGKVEPGE TVQAALVREI AEETGLHVPA GSLEPVIGIR HDYGDKRVFL DVWETSAAEG EARGCEGQPV EWLTSEQLRD EDFPAANRPI IRALRLPRQL AITGSENGLE PALAHLQEGL SAARPPLVLL RAPALSPLAY RELAANALPV CEKTGATLIV HGGPEVFRAI PGAHGLHLPW REAAKLSARP VPEDVWLGVS CHDRQEIDHA TAIGADYVTL GPVQPTESHP GAPTLGWSVF ADLVSEAVLP VFALGGLSPG DLREARQRGG QGIAGIRFWW PQS // ID G6Z1N2_VIBCL Unreviewed; 440 AA. AC G6Z1N2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC06A1_0092; OS Vibrio cholerae HC-06A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991950; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-06A1; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio Cholerae HC-06A1."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUI01000073; EHH76340.1; -; Genomic_DNA. DR ProteinModelPortal; G6Z1N2; -. DR EnsemblBacteria; EHH76340; EHH76340; VCHC06A1_0092. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID G6ZA67_VIBCL Unreviewed; 440 AA. AC G6ZA67; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC19A1_0090; OS Vibrio cholerae HC-19A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991952; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-19A1; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio Cholerae HC-19A1."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUJ01000007; EHH80991.1; -; Genomic_DNA. DR ProteinModelPortal; G6ZA67; -. DR EnsemblBacteria; EHH80991; EHH80991; VCHC19A1_0090. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID G6ZNP1_VIBCL Unreviewed; 440 AA. AC G6ZNP1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC21A1_0092; OS Vibrio cholerae HC-21A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991953; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-21A1; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio Cholerae HC-21A1."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUK01000073; EHH77043.1; -; Genomic_DNA. DR ProteinModelPortal; G6ZNP1; -. DR EnsemblBacteria; EHH77043; EHH77043; VCHC21A1_0092. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID G6ZZ32_VIBCL Unreviewed; 440 AA. AC G6ZZ32; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC22A1_0092; OS Vibrio cholerae HC-22A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991954; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-22A1; RA Eppinger M., Hasan N.A., Sengamalay N., Hine E., Su Q., RA Daugherty S.C., Young S., Sadzewicz L., Tallon L., Cebula T.A., RA Ravel J., Colwell R.R.; RT "Genome sequence of Vibrio Cholerae HC-22A1."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUL01000072; EHH89074.1; -; Genomic_DNA. DR ProteinModelPortal; G6ZZ32; -. DR EnsemblBacteria; EHH89074; EHH89074; VCHC22A1_0092. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID G7A6L5_VIBCL Unreviewed; 440 AA. AC G7A6L5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC23A1_0010; OS Vibrio cholerae HC-23A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991933; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-23A1; RA Eppinger M., Hasan N.A., Sengamalay N., Hine E., Su Q., RA Daugherty S.C., Young S., Sadzewicz L., Tallon L., Cebula T.A., RA Ravel J., Colwell R.R.; RT "Genome sequence of Vibrio Cholerae HC-23A1."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUM01000001; EHH87739.1; -; Genomic_DNA. DR ProteinModelPortal; G7A6L5; -. DR EnsemblBacteria; EHH87739; EHH87739; VCHC23A1_0010. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID G7AJE6_VIBCL Unreviewed; 440 AA. AC G7AJE6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC28A1_0091; OS Vibrio cholerae HC-28A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991955; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-28A1; RA Eppinger M., Hasan N.A., Sengamalay N., Hine E., Su Q., RA Daugherty S.C., Young S., Sadzewicz L., Tallon L., Cebula T.A., RA Ravel J., Colwell R.R.; RT "Genome sequence of Vibrio Cholerae HC-28A1."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUN01000072; EHH91825.1; -; Genomic_DNA. DR ProteinModelPortal; G7AJE6; -. DR EnsemblBacteria; EHH91825; EHH91825; VCHC28A1_0091. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID G7ASX7_VIBCL Unreviewed; 440 AA. AC G7ASX7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC32A1_0091; OS Vibrio cholerae HC-32A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991956; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-32A1; RA Eppinger M., Hasan N.A., Sengamalay N., Hine E., Su Q., RA Daugherty S.C., Young S., Sadzewicz L., Tallon L., Cebula T.A., RA Ravel J., Colwell R.R.; RT "Genome sequence of Vibrio Cholerae HC-32A1."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUO01000007; EHH98320.1; -; Genomic_DNA. DR ProteinModelPortal; G7ASX7; -. DR EnsemblBacteria; EHH98320; EHH98320; VCHC32A1_0091. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID G7B3H8_VIBCL Unreviewed; 424 AA. AC G7B3H8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC33A2_0092; OS Vibrio cholerae HC-33A2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991957; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-33A2; RA Eppinger M., Hasan N.A., Sengamalay N., Hine E., Su Q., RA Daugherty S.C., Young S., Sadzewicz L., Tallon L., Cebula T.A., RA Ravel J., Colwell R.R.; RT "Genome sequence of Vibrio Cholerae HC-33A2."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUP01000013; EHI03923.1; -; Genomic_DNA. DR EnsemblBacteria; EHI03923; EHI03923; VCHC33A2_0092. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 424 AA; 47107 MW; B519CDB0A75FC412 CRC64; MQYALLQAKE QGVAIQHIRL DVGSEAQFIL EKSEESLRIG SSLCSQKEGF EPCDYYLDYV SENRVLPEAM MCNARCTVTV GLHDEYGFTL DKWQYGHAAE QLIVYPSENH RLNSKVNQHL AWVLATLTLD FSIGDGLCIA RAAITQGDSV SRETWPTQFE RFPAVQSNIR SLSTQVFLTT RAFPTIDKAK FNLYPVVDDV NWIEHLLKLG VRTVQLRIKD PKQGDLEAQI IRAIALGREF NAQVFINDHW QLAIKHQAYG VHLGQEDLTS ANLTELLDAG IRLGLSTHGY YELLIAAGIQ PSYIALGHIF PTTTKQMPSK PQGLVRLAAY QRLVNQMPYQ GQHGIPTVAI GGIDCRNIRD VLDCGVTAVA VVRAITESPD PSLAVQALSS AFADFVDAEY KLMPASESCE PLSYLAMEVA DAHR // ID G7BEA3_VIBCL Unreviewed; 440 AA. AC G7BEA3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC43A1_0091; OS Vibrio cholerae HC-43A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991938; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-43A1; RA Eppinger M., Hasan N.A., Sengamalay N., Hine E., Su Q., RA Daugherty S.C., Young S., Sadzewicz L., Tallon L., Cebula T.A., RA Ravel J., Colwell R.R.; RT "Genome sequence of Vibrio Cholerae HC-43A1."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUQ01000008; EHI01335.1; -; Genomic_DNA. DR ProteinModelPortal; G7BEA3; -. DR EnsemblBacteria; EHI01335; EHI01335; VCHC43A1_0091. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID G7BS03_VIBCL Unreviewed; 440 AA. AC G7BS03; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC48B2_0068; OS Vibrio cholerae HC-48B2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991966; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-48B2; RA Eppinger M., Hasan N.A., Sengamalay N., Hine E., Su Q., RA Daugherty S.C., Young S., Sadzewicz L., Tallon L., Cebula T.A., RA Ravel J., Colwell R.R.; RT "Genome sequence of Vibrio Cholerae HC-48B2."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUR01000080; EHI09383.1; -; Genomic_DNA. DR ProteinModelPortal; G7BS03; -. DR EnsemblBacteria; EHI09383; EHI09383; VCHC48B2_0068. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID G7BZX9_VIBCL Unreviewed; 424 AA. AC G7BZX9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VCHC61A1_0009; OS Vibrio cholerae HC-61A1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=991942; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HC-61A1; RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C., RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., RA Colwell R.R.; RT "Genome sequence of Vibrio Cholerae HC-61A1."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUS01000001; EHI08240.1; -; Genomic_DNA. DR EnsemblBacteria; EHI08240; EHI08240; VCHC61A1_0009. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 424 AA; 47107 MW; B519CDB0A75FC412 CRC64; MQYALLQAKE QGVAIQHIRL DVGSEAQFIL EKSEESLRIG SSLCSQKEGF EPCDYYLDYV SENRVLPEAM MCNARCTVTV GLHDEYGFTL DKWQYGHAAE QLIVYPSENH RLNSKVNQHL AWVLATLTLD FSIGDGLCIA RAAITQGDSV SRETWPTQFE RFPAVQSNIR SLSTQVFLTT RAFPTIDKAK FNLYPVVDDV NWIEHLLKLG VRTVQLRIKD PKQGDLEAQI IRAIALGREF NAQVFINDHW QLAIKHQAYG VHLGQEDLTS ANLTELLDAG IRLGLSTHGY YELLIAAGIQ PSYIALGHIF PTTTKQMPSK PQGLVRLAAY QRLVNQMPYQ GQHGIPTVAI GGIDCRNIRD VLDCGVTAVA VVRAITESPD PSLAVQALSS AFADFVDAEY KLMPASESCE PLSYLAMEVA DAHR // ID G7CHT0_MYCTH Unreviewed; 219 AA. AC G7CHT0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=KEK_15863; OS Mycobacterium thermoresistibile ATCC 19527. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1078020; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19527; RG Tuberculosis Structural Genomics Consortium; RA Ioerger T.R.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVE01000046; EHI12390.1; -; Genomic_DNA. DR EnsemblBacteria; EHI12390; EHI12390; KEK_15863. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23110 MW; 6382FFC56DE71002 CRC64; MSAASLYLCT DARRERGDLA EFADAALAGG VDLIQLRDKG SPGEQRFGPL EARDELEALS VLADAARRHD ALLAVNDRAD VALAAGADVL HLGQDDLPLP VARRIVGDEV LIGRSTHDIE QVRTAIADRD VDYFCVGPCW PTPTKPGRPA PGLDLVRAAA AEGTGKPWFA IGGIDEQRLP EVVAAGARRI VVVRAITAAD DPEAAARRLK AMLPGGRTG // ID G7CVV3_AERSA Unreviewed; 524 AA. AC G7CVV3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=IYQ_13148; OS Aeromonas salmonicida subsp. salmonicida 01-B526. OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=1076135; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=01-B526; RX PubMed=22247525; DOI=10.1128/JB.06276-11; RA Charette S.J., Brochu F., Boyle B., Filion G., Tanaka K.H., Derome N.; RT "Draft Genome Sequence of the Virulent Strain 01-B526 of the Fish RT Pathogen Aeromonas salmonicida."; RL J. Bacteriol. 194:722-723(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVO01000050; EHI51930.1; -; Genomic_DNA. DR ProteinModelPortal; G7CVV3; -. DR EnsemblBacteria; EHI51930; EHI51930; IYQ_13148. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 524 AA; 55357 MW; A9C8600758E271C7 CRC64; MNSRPIVWTI AGSDSGGGAG IQADLHTLHD LGVHGCSVIT AITAQNSVAV KMVDPVLMQT FTAQIDALGV DLPPAAIKIG LLPTRLHVEV LARRLDTLTA PFVVYDPVAI ASTGTPMAEA NMLAAVREHL LPRLSLITPN GPELEALTGI PASSPELVRA GAARLRELGA RAVLVKGGHL GWSDELCLDY YQDEQREFWL GAPRIDTRHG HGTGCCYASA IAAVVAQDHP VDDAITLARA YLQQGLAGAQ GVGAGPGPIA HLGWPADLAH FPRAVLAGSS LDRRFGLYPA CEARLPEGPF AATEHRLGLY PVVDSVKWLK RLLGAGVKTL QLRIKNLPAA QVAPAIAEAV ALGHRFGARL FINDYWQQAI AAGAYGVHLG QEDMETADLA AIQAADLRLG LSTHGYFELM RARELAPSYI ALGHIFPTNT KQMPSRPQGL VRLQRYRALM CDWPTVAIGG IGEERIAAVQ ASGVGSIALV SAITASDDWQ GATARLLAAV GAGDEPCSAL IHQAITQQEA DHAL // ID G7DDQ0_BRAJP Unreviewed; 202 AA. AC G7DDQ0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 22-JAN-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BJ6T_27680; OS Bradyrhizobium japonicum USDA 6. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=1037409; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=USDA 6; RA Kaneko T., Maita S., Hirakawa H., Uchiike N., Minamisawa K., RA Watanabe A., Sato S.; RT "Complete Genome Sequence of the Soybean Symbiont Bradyrhizobium RT japonicum Strain USDA6T."; RL Genes (Basel) 2:763-787(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012206; BAL08046.1; -; Genomic_DNA. DR RefSeq; YP_005607634.1; NC_017249.1. DR EnsemblBacteria; BAL08046; BAL08046; BJ6T_27680. DR GeneID; 12144731; -. DR KEGG; bju:BJ6T_27680; -. DR KO; K00788; -. DR BioCyc; BJAP1037409:GL9L-2765-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 202 AA; 21910 MW; FF739E5EAEF52AFB CRC64; MPYPDRFYPV VDSLKWVERL TRLGVGTIQL RAKDLNDADA LQIVTDALAI TKDTQAKLVV NDYWRAAVVA GAKYLHLGQE DLADADLQAI REAGLSLGIS THDDAELETA LAADPDYVAL GPIFFTTLKS MRFEPQGIPK ITEWKKRIGS IPLVAIGGIK FEHAAEIFAA GADSIAVVSD VTQNADPDAR VRQWLGLPAE AA // ID G7DIF6_BRAJP Unreviewed; 229 AA. AC G7DIF6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BJ6T_83250; OS Bradyrhizobium japonicum USDA 6. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=1037409; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=USDA 6; RA Kaneko T., Maita S., Hirakawa H., Uchiike N., Minamisawa K., RA Watanabe A., Sato S.; RT "Complete Genome Sequence of the Soybean Symbiont Bradyrhizobium RT japonicum Strain USDA6T."; RL Genes (Basel) 2:763-787(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012206; BAL13568.1; -; Genomic_DNA. DR RefSeq; YP_005613156.1; NC_017249.1. DR EnsemblBacteria; BAL13568; BAL13568; BJ6T_83250. DR GeneID; 12142440; -. DR KEGG; bju:BJ6T_83250; -. DR KO; K00788; -. DR BioCyc; BJAP1037409:GL9L-8322-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 229 AA; 23821 MW; 76407D8A8F013227 CRC64; MSNKSPPPRP APRLYLATPA VDDPAAFVAE LPGLLAAADI AAVLLRLKET DQRTMITRIK ALAPPVQKAG AALLVEGHAE LVARGGADGA HLPGIAALKE ALPSLKPDRI AGVGGLTTRH HSMDAGEMGA DYVLFGEPDA KGQRPSSQAI AERLDWWAEL FEPPCVGFAT SLEEAHDFAA SGADFVLVGD FVWSDPRGPK AALIEVDAAI KKAHAAALVG QDPAGQEHG // ID G7DU99_MIXOS Unreviewed; 530 AA. AC G7DU99; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-APR-2014, entry version 11. DE SubName: Full=Uncharacterized protein; GN Name=Mo00807; ORFNames=E5Q_00807; OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; OC Mixiomycetes; Mixiales; Mixiaceae; Mixia. OX NCBI_TaxID=764103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970; RX PubMed=21478649; DOI=10.2323/jgam.57.63; RA Nishida H., Nagatsuka Y., Sugiyama J.; RT "Draft genome sequencing of the enigmatic basidiomycete Mixia RT osmundae."; RL J. Gen. Appl. Microbiol. 57:63-67(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BABT02000028; GAA94159.1; -; Genomic_DNA. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 530 AA; 55449 MW; 9286A311B8471881 CRC64; MALPRSPLYL VTQREALPPG VSLEQCVQEA LQGGVEIVQL REKHADSREF LEIARGLQTI CDAAEVPLVI NDRVDIALAC GCRAVHLGQS DLSVKDVCAL MPTAKSIGVS AHDVSEATVA CATDDVSLIG IGPIYATTSK SDAKEALGPR KLARIIDALR AYERTLSSAN GRVSIVAIGG INASNAARVL HMTCNFDTGE TEAGLAVISA IVSSPRPREA AQSLSDILAD YRSEGRSHKP SREDLLANVV RLHDSSRESG GLLHHITNTV VQNQCANVAL ALRASPIMSM SPEEAGDLSA ILGCLVINLG TLTDDSLRVM KEAGRHANSN KKPIVFDPVG VGASAFRQSK TDQLLDHVQM SIIKGNAGEL AALSGDKSVR ARGVDSAGGF ADPVKAVRDL ARQERCVVVL TGQIDYISDG MTVIKLSNGV PHLGNITGSG CATGTCIAAY ASAAHSMSTT MRATVPQASI WGGGDMLSAA VGGILAMTVA AEIAMEKQPG GPSTFTGHLI DALYNLTAQN LVERARVEVV // ID G7EK31_9GAMM Unreviewed; 511 AA. AC G7EK31; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE SubName: Full=Hydroxymethylpyrimidine kinase / phosphomethylpyrimidine kinase / thiamine-phosphate diphosphorylase; GN ORFNames=P20652_3131; OS Pseudoalteromonas sp. BSi20652. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=388384; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20652; RA Xie B.B., Qin Q.L., Bian F., Shu Y.L., Zhang Y.Z.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20652; RA Biana F., Xie B.-B., Qin Q.-L., Shu Y.-L., Zhang X.-Y., Yu Y., RA Chen B., Chen X.-L., Zhou B.-C., Zhang Y.-Z.; RT "Genome Sequences of Six Pseudoalteromonas Strains Isolated from RT Arctic Sea Ice."; RL J. Bacteriol. 194:908-909(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BADT01000183; GAA61254.1; -; Genomic_DNA. DR EnsemblBacteria; GAA61254; GAA61254; P20652_3131. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 511 AA; 55112 MW; 9DAF2ECF6CEC2293 CRC64; MNNVVWTIAG SDSGGGAGIQ ADIKAMQSFG VHGCTAITAL TAQNSLGVEA INAVSTDIIE SQLLALEKDM KAKVIKIGML ANVQQIQLIS EHISHYKAKW PVPPVIVYDP VAIASSGDLL TEEDTVSAIK ECLLPLVDVI TPNTHETQLL TGVYLIGPAA IKEAANKLLS WGAKAVVIKG GHWDYPSGYC IDYCIDSNAQ NGEEYWLGNQ KIQTPHNHGT GCSMASVIAA CLAKDYPLKD AFILAKAYIN QGLKQSVRYG EGIGPVAQTS FPTNLDDYPQ VIEPGSWLGD ELDFDVPLDF NMAADFAPCE SKSLGLYAVV DTTDWLEKCL QQGIKTAQLR VKNKTQDELD ELIKQAVELG KQYNAQVFIN DYWQLAIKHG AYGVHLGQED LDIANLAAIK EAGLRLGLST HGFYEMLRAH NYRPSYMAFG AIYPTTTKDM TGQIQGLEKL IKFVPIMQSY PTVAIGGVDL SRAGQVAKTG VGSVAVVRAI TEADNYIEAI SALQVAISSA D // ID G7EY12_9GAMM Unreviewed; 508 AA. AC G7EY12; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE SubName: Full=Hydroxymethylpyrimidine kinase / phosphomethylpyrimidine kinase / thiamine-phosphate diphosphorylase; GN ORFNames=P20311_3614; OS Pseudoalteromonas sp. BSi20311. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=383911; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20311; RA Xie B.B., Qin Q.L., Bian F., Shu Y.L., Zhang Y.Z.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20311; RA Biana F., Xie B.-B., Qin Q.-L., Shu Y.-L., Zhang X.-Y., Yu Y., RA Chen B., Chen X.-L., Zhou B.-C., Zhang Y.-Z.; RT "Genome Sequences of Six Pseudoalteromonas Strains Isolated from RT Arctic Sea Ice."; RL J. Bacteriol. 194:908-909(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BADU01000188; GAA65785.1; -; Genomic_DNA. DR EnsemblBacteria; GAA65785; GAA65785; P20311_3614. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 508 AA; 54599 MW; 94EB5686846DB023 CRC64; MNNVVWTIAG SDSGGGAGIQ ADIKAMQSFG VHGCTAITAL TAQNSLGVEA INPVSTDVIE SQLLALEKDM KAKVIKIGML ANVQQIQLIS EHISHYKAKW PTPPVIVYDP VAIASSGDVL TEEDTVSAIK ECLLPLVDVI TPNTHETQLL TGVYLIGPAA IKEAASKLMA WGAKAVVIKG GHWDYPSGYC IDYCSQGGEE YWLGNEKIQV PHNHGTGCSM ASVIAACLAK DYPLKDAFIL AKAYINQGLK QSVRYGEGIG PVAQTSFPTD LAHYPQVIEA GSWLGDELDF DVPLDFNMAA DFAACESKAL GAYAVVDSVE WLEKCLQNGI KTAQLRVKDK SEDELEQLVA SAVALGQQYS AHVFINDYWQ LAIKHGAYGV HLGQEDLESA NLAAIKEAGL RLGLSTHGFY EMLRAHNYRP SYMAFGAIYP TTTKDMAGQI QGLEKLTRFV PLMQSYPTVA IGGIDLNRAQ EVAKTGVGSV AVVRAITEAD DYVEAINTLK SVINENAC // ID G7F6G3_9GAMM Unreviewed; 511 AA. AC G7F6G3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE SubName: Full=Hydroxymethylpyrimidine kinase / phosphomethylpyrimidine kinase / thiamine-phosphate diphosphorylase; GN ORFNames=P20429_2863; OS Pseudoalteromonas sp. BSi20429. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=1097676; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20429; RA Xie B.B., Qin Q.L., Bian F., Shu Y.L., Zhang Y.Z.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20429; RA Biana F., Xie B.-B., Qin Q.-L., Shu Y.-L., Zhang X.-Y., Yu Y., RA Chen B., Chen X.-L., Zhou B.-C., Zhang Y.-Z.; RT "Genome Sequences of Six Pseudoalteromonas Strains Isolated from RT Arctic Sea Ice."; RL J. Bacteriol. 194:908-909(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BADV01000073; GAA68736.1; -; Genomic_DNA. DR EnsemblBacteria; GAA68736; GAA68736; P20429_2863. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 511 AA; 55112 MW; ADD412440A2BEF4D CRC64; MNNVVWTIAG SDSGGGAGIQ ADIKAMQSFG VHGCTAITAL TAQNSLGVEA INAVSTDIIE SQLLALEKDM KAKVIKIGML ANVQQIQLIS EHISHYKAKW TVPPVIVYDP VAIASSGDLL TEEDTVSAIK ECLLPLVDVI TPNTHETQLL TGVYLIGPAA IKEAANKLLS WGAKAVVIKG GHWDYPSGYC IDYCIDSNTQ NGEEYWLGNQ KIQTPHNHGT GCSMASVIAA CLAKDYPLKD AFILAKAYIN QGLKQSVRYG EGIGPVAHTS FPTNLADYPQ VIEPGSWLGD ELDFDVPLDF NMAADFAPCE SKSLGLYAVV DSTDWLEKCL QQGIKTAQLR VKNKTQDELD GLIKQAVELG KKYNAQVFIN DYWQLAIKHS AYGVHLGQED LDIANLAAIK DAGLRLGLST HGFYEMLRAH NYRPSYMAFG AIYPTTTKDM TGQIQGLEKL IKFVPLMQSY PTVAIGGIDL SRAEQVAKTG VGSVAVVRAI TEADNYVEAI SALQVAISSA N // ID G7FCZ1_9GAMM Unreviewed; 508 AA. AC G7FCZ1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE SubName: Full=Hydroxymethylpyrimidine kinase / phosphomethylpyrimidine kinase / thiamine-phosphate diphosphorylase; GN ORFNames=P20439_1085; OS Pseudoalteromonas sp. BSi20439. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=420915; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20439; RA Xie B.B., Qin Q.L., Bian F., Shu Y.L., Zhang Y.Z.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20439; RA Biana F., Xie B.-B., Qin Q.-L., Shu Y.-L., Zhang X.-Y., Yu Y., RA Chen B., Chen X.-L., Zhou B.-C., Zhang Y.-Z.; RT "Genome Sequences of Six Pseudoalteromonas Strains Isolated from RT Arctic Sea Ice."; RL J. Bacteriol. 194:908-909(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BADW01000055; GAA71014.1; -; Genomic_DNA. DR EnsemblBacteria; GAA71014; GAA71014; P20439_1085. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 508 AA; 54628 MW; 330E298716B22D2B CRC64; MNNVVWTIAG SDSGGGAGIQ ADIKAMQSFG VHGCTAITAL TAQNSLGVEA INPVSTDVIE SQLLALEKDM KAKVIKIGML ANVQQIQLIS EHISHYKAKW PTPPVIVYDP VAIASSGDVL TEEDTVSAIK ECLLPLVDVI TPNTHETQLL TGVYLIGPAA IKEAASKLMA WGAKAVVIKG GHWDYPSGYC IDYCSQGGEE YWLGNEKIQV PHNHGTGCSM ASVIAACLAK DYPLKDAFIL AKAYINQGLK QSVRYGEGIG PVAQTSFPTD LAHYPQVIEA GSWLGDELDF DVPLDFNMAA DFAACESKAL GAYAVVDSVE WLEKCLQNGI KTAQLRVKNK SEDELEQLVA SAVALGQQYS AHVFINDYWQ LAIKHGAYGA HLGQEDIENA NLAAIKEAGL RLGLSTHGFY EMLRAHNYRP SYMAFGAIYP TTTKDMTGQI QGLEKLTRFV PLMQSYPTVA IGGIDLDRAQ EVAKTGVGSV AVVRAITEAD DYVEAINTLK SVINENAC // ID G7FRF1_9GAMM Unreviewed; 508 AA. AC G7FRF1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE SubName: Full=Hydroxymethylpyrimidine kinase / phosphomethylpyrimidine kinase / thiamine-phosphate diphosphorylase; GN ORFNames=P20480_2193; OS Pseudoalteromonas sp. BSi20480. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=386428; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20480; RA Xie B.B., Qin Q.L., Bian F., Shu Y.L., Zhang Y.Z.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20480; RA Biana F., Xie B.-B., Qin Q.-L., Shu Y.-L., Zhang X.-Y., Yu Y., RA Chen B., Chen X.-L., Zhou B.-C., Zhang Y.-Z.; RT "Genome Sequences of Six Pseudoalteromonas Strains Isolated from RT Arctic Sea Ice."; RL J. Bacteriol. 194:908-909(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BADX01000099; GAA75724.1; -; Genomic_DNA. DR EnsemblBacteria; GAA75724; GAA75724; P20480_2193. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 508 AA; 55041 MW; BE402C40A4A00BDF CRC64; MNNVVWTIAG SDSGGGAGIQ ADIKAMQSFG VHGCTAITAL TAQNSLGVET INAVSTDIIE SQLLALEKDM KAKVIKIGML ANVQQIQLIS EHISHYKAKW PVPPVIVYDP VAIASSGDVL TEEDTVSAIK ECLLPLVDVI TPNTHETQLL TGVYLIGPSA VKDAANKLLS WGAKSVVIKG GHWDFPSGYC IDYCIQNNEE YWLGNKKIQT PHNHGTGCSM ASVIAACLAK DYPLKDAFIL AKAYINQGLK QSVRYGEGIG PVAQTSFPTH LDDYPQVIEP GSWLGDELDF DVPLEFNMAA DFAPCESKQL GLYAIVDSND WLEKCLQQGI KTAQLRVKNK TETELDELIK QAVELGKKYR AHVFINDYWQ LAIKHGAYGV HLGQEDLEIA NLAAIKEAGL RLGLSTHGFY EMLRAHNYRP SYMAFGAIYP TTTKDMTGQI QGLDKLKKCV PLMQSYPTVA IGGIDLTRAN EVANTGVGSV AVVRAISEAD DYIAAISSLQ SAINQPNG // ID G7G1S2_9GAMM Unreviewed; 511 AA. AC G7G1S2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE SubName: Full=Hydroxymethylpyrimidine kinase / phosphomethylpyrimidine kinase / thiamine-phosphate diphosphorylase; GN ORFNames=P20495_1844; OS Pseudoalteromonas sp. BSi20495. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=386429; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20495; RA Xie B.B., Qin Q.L., Bian F., Shu Y.L., Zhang Y.Z.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20495; RA Biana F., Xie B.-B., Qin Q.-L., Shu Y.-L., Zhang X.-Y., Yu Y., RA Chen B., Chen X.-L., Zhou B.-C., Zhang Y.-Z.; RT "Genome Sequences of Six Pseudoalteromonas Strains Isolated from RT Arctic Sea Ice."; RL J. Bacteriol. 194:908-909(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BADY01000061; GAA79345.1; -; Genomic_DNA. DR EnsemblBacteria; GAA79345; GAA79345; P20495_1844. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 511 AA; 55264 MW; E6B9F52908328ABB CRC64; MNNVVWTIAG SDSGGGAGIQ ADIKAMQSFG VHGCTAITAL TAQNSLGVEA INAVSTDIIE SQLLALEKDM KAKVIKIGML ANVQQIQLIS EHISHYKAKW PAPPVIVYDP VAIASSGDLL TEEDTVSAIK ECLLPLVDVI TPNTHETQLL TGVYLIGPAA IKEAANKLLS WGAKAVVIKG GHWDYPSGYC IDYCVNNFTQ NAEEYWLGNQ KIQTPHNHGT GCSMASVIAA CLAKDYPLKD AFILAKAYIN QGLKQSVRYG EGIGPVAHTS FPTNLDDYPQ VIEPGSWLGD ELDFDVPLDF NMAADFAPCE SKSLGLYAVV DSTDWLEKCL QQGIKTTQLR VKNKTQDELD ELIKHAVELG KQYNAQVFIN DYWQLAIKHG AYGVHLGQED LDIANLAAIK DAGLRLGLST HGFYEMLRAH NYRPSYMAFG AIYPTTTKDM TGQIQGLEKL IKFVPLMQSY PTVAIGGIDL SRAEQVAKTG VGSVAVVRAI TEADNYVEAI SALQVAISSA N // ID G7GDQ1_9GAMM Unreviewed; 203 AA. AC G7GDQ1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ACT4_021_03420; OS Acinetobacter sp. NBRC 100985. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1071390; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100985; RA Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Acinetobacter sp. NBRC 100985."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAEB01000021; GAB01726.1; -; Genomic_DNA. DR EnsemblBacteria; GAB01726; GAB01726; ACT4_021_03420. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21654 MW; 4A1351DF4D86202B CRC64; MRGLYLITND DPIQLLLEKL DVALSTGQVA ILQYRRKKIA KLDQPLEVQQ IKALCEKHQV PFVINDDLDL AEQFGLGVHL GQSDGEISDA AARLPKGVII GRTCLNSLEL AEQAIADGAT YVAFGAVYAT STKPEAGNVG IEVIKQAKQK FAVPICAIGG LTVENSQVVI EAGASLCAVI SDILGRSTAE IPARVNAWAT LFD // ID G7GEU6_9GAMM Unreviewed; 304 AA. AC G7GEU6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Putative NTP pyrophosphohydrolase; GN ORFNames=ACT4_025_00820; OS Acinetobacter sp. NBRC 100985. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1071390; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100985; RA Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Acinetobacter sp. NBRC 100985."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAEB01000025; GAB02121.1; -; Genomic_DNA. DR ProteinModelPortal; G7GEU6; -. DR EnsemblBacteria; GAB02121; GAB02121; ACT4_025_00820. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 304 AA; 34494 MW; 66DDEC13FB901DA4 CRC64; MAKATVDVAI AILLHKSKVL VGWRQANQHQ GNKHEFPGGK VEKGETPEQA CRREIYEEVG IGLKDWHKFD EISHEYDDII VNLHLFHTYV PDELLNLIHQ PWTWFNRDQL AELNFPKANA AILDRLIWPH LIKINHELSA LPQQASLFYW RPELTDIKKI EQQLLELDDQ QLAKLVINFD IWQHLLNTEL KGKITTIHLK QSQLMSLCKG DLNIGKRFLA ACHDAVSIQH AHHLGCDAIL LSPVNATATH PDTKVLGWDN FSELAQKSDI PVFALGGIAP TDIEQAQKHH AYGLAGISQF NSIV // ID G7GWQ2_9ACTO Unreviewed; 233 AA. AC G7GWQ2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GOAMR_78_00040; OS Gordonia amarae NBRC 15530. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1075090; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 15530; RA Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Gordonia amarae NBRC 15530."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAED01000078; GAB08027.1; -; Genomic_DNA. DR EnsemblBacteria; GAB08027; GAB08027; GOAMR_78_00040. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 51 55 HMP-PP binding (By similarity). FT REGION 158 160 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 161 161 HMP-PP (By similarity). FT BINDING 189 189 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 23959 MW; D0E59BFB72E04DFF CRC64; MTTGSTTRAA GSVHDRLARA RLYLCTDARR ERGDLDEFVA RAVTGGVDIV QLRDKGSAGE ERFGALEAAE ELAILARLRD ITHAGGALLS VNDRADLAKL SGADVLHVGQ GDLTPAQARG IVGEDVIIGQ STHDAAQAAA AAADRDVDYF CVGPCWPTPT KPGRTAPGLG LVREVAASAP AKAWFAIGGI DAQRLPEVVD AGARRIVVVR AITAAGDPAA AARTLTAGIT AAH // ID G7GY25_9ACTO Unreviewed; 226 AA. AC G7GY25; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GOARA_012_00500; OS Gordonia araii NBRC 100433. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1073574; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100433; RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Gordonia araii NBRC 100433."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAEE01000012; GAB08500.1; -; Genomic_DNA. DR EnsemblBacteria; GAB08500; GAB08500; GOARA_012_00500. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23607 MW; 0F72CDF8A3EC6CC6 CRC64; MEPVNRRERL ARSSLYLCTD ARRERGDLLD FVAAALDGGV DIVQLRDKGS PGEREFGALE AGLELNILAD LKTLTTRAGA LLAVNDRADI AIAADADVLH VGQDDLPVAT ARRLVGGDVI LGLSTHDPDQ ASAASANPDV DYFCVGPCWA TPTKPGRPGT GLDLVRHAAS LPTNRPWFAI GGIDVDRAPH VAEAGASRVV VVRALTDAAD PAAAAVALKT AVIPRV // ID G7H9D0_9BURK Unreviewed; 374 AA. AC G7H9D0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=I35_0291, I35_0427; OS Burkholderia cenocepacia H111. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=1055524; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H111; RA Carlier A., Bruggmann R., Agnoli K., Eberl L.; RT "Draft genome sequence of Burkholderia cenocepacia H111."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H111; RA Carlier A., Bruggmann R., Agnoli K., Eberl L.; RT "Draft genome sequence of Burkholderia cenocepacia H111."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFQ01000007; CCE46618.1; -; Genomic_DNA. DR EMBL; HG938370; CDN58814.1; -; Genomic_DNA. DR EnsemblBacteria; CCE46618; CCE46618; I35_0427. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 374 AA; 39239 MW; 655AEE12FD7F13C1 CRC64; MSARFADAFW PPADELAEAA ERIRARLGDW PDGAAPWRLC VAAPDVPADG DVLIVSAGDR AAQARASAVS RPASPDAVAI EFDERSAVLH AAGVRYALNA AHPLADDWIA ALAAFLDCGF APVDALVLAL AWRDGDETHA ADAWPVDAER FPCVAGLPPA PEPAFPPCPA QLGLYPVVPS AEWVERVLDG GARTVQLRVK DATPDALRQE IARAVAAGRR YPDARVFIND HWQIAAEEGA YGVHLGQEDL ETADLAAIAR AGLRLGLSSH GYYEMLRALH ERPSYLALGP VYATATKAVA APPQGLARIA RYARFAGARA PLVAIGGVGL DALPAVLATG VGSVAVVSAV TGAADYRTAL IALQQCFAGQ FDNR // ID G7HLI0_9BURK Unreviewed; 194 AA. AC G7HLI0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 11. DE SubName: Full=Thiamin-phosphate pyrophosphorylase-like protein; GN ORFNames=I35_4754, I35_4795; OS Burkholderia cenocepacia H111. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=1055524; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H111; RA Carlier A., Bruggmann R., Agnoli K., Eberl L.; RT "Draft genome sequence of Burkholderia cenocepacia H111."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H111; RA Carlier A., Bruggmann R., Agnoli K., Eberl L.; RT "Draft genome sequence of Burkholderia cenocepacia H111."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFQ01000046; CCE50868.1; -; Genomic_DNA. DR EMBL; HG938371; CDN62631.1; -; Genomic_DNA. DR EnsemblBacteria; CCE50868; CCE50868; I35_4754. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 20050 MW; ECF013842CC86E7F CRC64; MNAPLPRCCV ITPEPASASA ADRAAFLDRL SAVLARGETL VQLRVKSLDA AAFAALAAAA LARCDAAGAH LMLNGPIDAA GVMRLDGAGW HLDGAALRGV TQRPLPADRW VSVACHSQDD LLLAAQAGAD FVTLSPVLPT LSHPGAPTLG WARFDTLAAQ AAMPVFALGG MTRAHLDDAR RHGAYGIAGI RGFW // ID G7HWE6_9CORY Unreviewed; 227 AA. AC G7HWE6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CCAS_04620; OS Corynebacterium casei UCMA 3821. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1110505; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UCMA 3821; RX PubMed=22247534; DOI=10.1128/JB.06496-11; RA Monnet C., Loux V., Bento P., Gibrat J.F., Straub C., Bonnarme P., RA Landaud S., Irlinger F.; RT "Genome Sequence of Corynebacterium casei UCMA 3821, Isolated from a RT Smear-Ripened Cheese."; RL J. Bacteriol. 194:738-739(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFW01000028; CCE54511.1; -; Genomic_DNA. DR EnsemblBacteria; CCE54511; CCE54511; CCAS_04620. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). SQ SEQUENCE 227 AA; 23401 MW; FDEC14301F9FE15C CRC64; MKTRAQLDLR CYVVTGNGSQ DDIVATAAQA AAGGAGVIQV RSKPIGAGQL LKLAEKVSLA VAEANPSTKI LIDDRVDIAA ILIRRGLPVH GVHVGQSDIL VTDVRELLGP DAIIGLTTGT AELIQQANEY ADIIDYVGAG PFRPTPTKDS GRDPIGLDGY PRLVELSKLP IVAIGDVQPA DVAALASTGI AGVAMVRAFI EAPSATELAQ QIIADFSDGL QMSGATS // ID G7I225_9CORY Unreviewed; 217 AA. AC G7I225; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CCAS_15255; OS Corynebacterium casei UCMA 3821. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1110505; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UCMA 3821; RX PubMed=22247534; DOI=10.1128/JB.06496-11; RA Monnet C., Loux V., Bento P., Gibrat J.F., Straub C., Bonnarme P., RA Landaud S., Irlinger F.; RT "Genome Sequence of Corynebacterium casei UCMA 3821, Isolated from a RT Smear-Ripened Cheese."; RL J. Bacteriol. 194:738-739(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFW01000105; CCE56490.1; -; Genomic_DNA. DR EnsemblBacteria; CCE56490; CCE56490; CCAS_15255. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22437 MW; 9907031545DD4D59 CRC64; MSSSQDYGIY LVTDPVLCGA RGVVETVRLA VDGGVHTVQL RDKHASFDQQ LSQLEQLAEV IDGRAKLVIN DRLDVAVEAQ RRGIAIDGVH LGQADEAVLT AREELGTGAI IGLTANTEEH LAAVAALPAG TVDYVGVGVI RPTSTKPDHP PALGIAGFAH LTAISPVPTV AIGGVLAEDI ADLRAAGAAG VCFVSALCAA EDPEHVARSM ADAWNRP // ID G7INQ6_MEDTR Unreviewed; 576 AA. AC G7INQ6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 17. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=MTR_2g006350; OS Medicago truncatula (Barrel medic) (Medicago tribuloides). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Trifolieae; Medicago. OX NCBI_TaxID=3880; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A17; RX PubMed=22089132; DOI=10.1038/nature10625; RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., RA Udvardi M.K., Benedito V.A., Mayer K.F., Gouzy J., Schoof H., RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., RA Cheung F., De Mita S., Krishnakumar V., Gundlach H., Zhou S., RA Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B., RA Silverstein K.A., Tang H., Rombauts S., Zhao P.X., Zhou P., Barbe V., RA Bardou P., Bechner M., Bellec A., Berger A., Berges H., Bidwell S., RA Bisseling T., Choisne N., Couloux A., Denny R., Deshpande S., Dai X., RA Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S., Franken C., RA Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J., RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y., RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S., RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., RA Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F., RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O., RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., RA Shi R., Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., RA Wang B.B., Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., RA White D.D., White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., RA Yao Z., Ying F., Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., RA May G.D., Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.; RT "The Medicago genome provides insight into the evolution of rhizobial RT symbioses."; RL Nature 480:520-524(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001218; AES63234.1; -; Genomic_DNA. DR RefSeq; XP_003592983.1; XM_003592935.1. DR UniGene; Mtr.4805; -. DR GeneID; 11424195; -. DR KEGG; mtr:MTR_2g006350; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; SQ SEQUENCE 576 AA; 61893 MW; 7A19FA1633E9C7F7 CRC64; MSCVFNVVDF SSHYSPHLHL HLHAHSQITP PLLSKRAINR FWNCNSDSIN HQTPRFVKMQ SNITSNSIPT PIHTFDSELN KIPHVLTVAG SDSGAGAGIQ ADLKTCSARR VYCSTVITAV TAQNTLGVQG VNIVPHDFVQ HQLNSVLSDI NVDVVKTGML PSLSVLKVLC QSLRKFPVKA LVVDPVMIST SGDILAGPSV LDGFREELLP MADIVTPNVK EASALLGDLP IKTVSDMRTA AKLIHDLGPR SVLVKGGDLP NSSEAIDIFY DGQEFYELSS PRVNTRNTHG TGCTMASCIA AELAKGSSML SAVKIAKRFV EAALEYSRDL LIGNGVQGPF DHLLALKNIN QSSYRQDRFN PNDLFLYAVT DSGMNRKWGR SIAEAVKAAV EGGATIVQLR EKDAETKDFV DAAKVCLKIC RSYGVPLLIN DRIDVALACD ADGVHVGQSD MPARLARTIL GPEKIIGVSC KTPEHAHQAW LDGADYIGSG GVYPTNTKEN NRTIGLDGLK EVCKASKLPV VAIGGIGMSN ARAVMELGVP SLKGVAVVSA LFDRECILTE TRNLQAVISE AALLTQ // ID G7LS20_9ENTR Unreviewed; 221 AA. AC G7LS20; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BrE312_4190; OS Brenneria sp. EniD312. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Brenneria. OX NCBI_TaxID=598467; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EniD312; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Monk A.C., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Balakrishnan V., Glasner J., Perna N., Woyke T.; RT "Complete sequence of Brenneria sp. EniD312."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001230; EHD23511.1; -; Genomic_DNA. DR EnsemblBacteria; EHD23511; EHD23511; BrE312_4190. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23741 MW; DBF52E3ECEA497A2 CRC64; MTLSQTAASP IAAPFPPTAQ RLGLYPVVDS VEWIERLLSA GVKTIQLRIK DLPDEQVEAD IIRAIALGRQ YQARLFINDY WRLAVKHQAY GVHLGQEDLD GADLAAIRRA GLRLGVSTHD DAELARAAAI NPSYIALGHI FPTQTKDMPS APQGVAELAR HLQTLGDRFP TVAIGGISID RAPAVLATGV GGIAVVSAIT QAPDWRQATA TLLRMIEGRE A // ID G7LY27_9CLOT Unreviewed; 209 AA. AC G7LY27; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CDLVIII_1148; OS Clostridium sp. DL-VIII. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=641107; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DL-VIII; RX PubMed=23929491; RA Taghavi S., Izquierdo J.A., van der Lelie D.; RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge."; RL Genome Announc. 1:e00605-13(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001240; EHI97851.1; -; Genomic_DNA. DR EnsemblBacteria; EHI97851; EHI97851; CDLVIII_1148. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22499 MW; 8D6901AED0CD7E39 CRC64; MKPKIDYSIY LVTDRDLMST ETLEEAVEQA IIGGCTLIQL REKDCSSLDF YSTAVKVKEI TDKYNVPLII NDRLDIALAV DAAGVHVGQS DMPAAIVRKI IGEDKIIGVS TGSLEQALKA QKDGADYLGV GAMYATGTKK DANPTSMKEL KKIRENVSIP IVVIGGINKV TARDFKGIGI DGLAIVSAII AQKDIAEAAK EISEIFKQI // ID G7MA45_9CLOT Unreviewed; 216 AA. AC G7MA45; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 22-JAN-2014, entry version 11. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=CDLVIII_5329; OS Clostridium sp. DL-VIII. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=641107; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DL-VIII; RX PubMed=23929491; RA Taghavi S., Izquierdo J.A., van der Lelie D.; RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge."; RL Genome Announc. 1:e00605-13(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001240; EHJ01811.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ01811; EHJ01811; CDLVIII_5329. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 216 AA; 24293 MW; 9B09798B7D3D6D63 CRC64; MIIIGITNRK LCLDFYEQIR KIAKSKINYL MIREKDLESG ELLETALKVK KELENTDIKV IINSNEEVAE RVNADGIQLS FKDFLGINEK FYTENLKSME ATGDNFRFRG KEYKKYKMIG VSIHSFDEGI QAYNLGADYV IYGHVFKTDC KKGVPPRGIK EIEKLTKEID IPVIGLGGID KSNFKEVINS GAGGIAIMSS LMEAESPKAL IEEIIG // ID G7Q7C4_9DELT Unreviewed; 214 AA. AC G7Q7C4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DFW101_3639; OS Desulfovibrio sp. FW1012B. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=644968; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FW1012B; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Chertkov O., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Hazen T.C., Fields M.W., Hwang C., Ramsay B., Arkin A.P., Dehal P., RA Chivian D., Criddle C.S., Carroll S.L., Wu W., Woyke T.; RT "Complete sequence of chromosome Desulfovibrio sp. FW1012B."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001368; EHJ49635.1; -; Genomic_DNA. DR ProteinModelPortal; G7Q7C4; -. DR EnsemblBacteria; EHJ49635; EHJ49635; DFW101_3639. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 21528 MW; 5B9540DCAE79681B CRC64; MSRPRLDLGL YLVTDRPALL GRDLLDVVGQ AVAGGAGLVQ LREKTASTRE FVELARAVAG ILRPRGVPLL INDRVDVALA AGADGVHVGQ DDMRPADVRA ILGPDALIGL SVTGEAEARA ARGEPVDYLG AGPVFATATK PDAGAAQGLA GLAAMIALAE VPVVAIGAIT SANAASVLDQ GAAGLAVVSA ICSAPNPREA AARLRRIVDG VRPG // ID G7QJG6_LEPII Unreviewed; 214 AA. AC G7QJG6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 15. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LIF_A1608; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai OS (strain IPAV). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=573825; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IPAV; RX PubMed=21423275; DOI=10.1038/cr.2011.46; RA Zhong Y., Chang X., Cao X.J., Zhang Y., Zheng H., Zhu Y., Cai C., RA Cui Z., Zhang Y., Li Y.Y., Jiang X.G., Zhao G.P., Wang S., Li Y., RA Zeng R., Li X., Guo X.K.; RT "Comparative proteogenomic analysis of the Leptospira interrogans RT virulence-attenuated strain IPAV against the pathogenic strain RT 56601."; RL Cell Res. 21:1210-1229(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001221; AER02408.1; -; Genomic_DNA. DR RefSeq; YP_005988391.1; NC_017551.1. DR ProteinModelPortal; G7QJG6; -. DR EnsemblBacteria; AER02408; AER02408; LIF_A1608. DR GeneID; 12580063; -. DR KEGG; lie:LIF_A1608; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR BioCyc; LINT573825:GLFK-1604-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 214 AA; 24559 MW; 214912E2D1840FBC CRC64; MRANSFPWRV PGIYPILDLD FCKSRNLDYF SLPKFWIEYP DLIPFIQIRA KSASINELEF IVKSLQDLYP DLFWIVNDFW KQAIEWNCFG AHVGKEDYEA LNLEERNTLF KSKLYLGTSS HTLEEVSELD SSLWNYTGLG PIFPTENKED AKSAIGTKTL NKIKNGNYLP VTVIGGIKVE NLDLILKEGS FLISSISMAC LENEFRTAAT KLRK // ID G7QUD7_MYCBI Unreviewed; 222 AA. AC G7QUD7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BCGMEX_0424c; OS Mycobacterium bovis BCG str. Mexico. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=717522; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mexico; RX PubMed=21981907; DOI=10.1186/1471-2164-12-493; RA Orduna P., Cevallos M.A., de Leon S.P., Arvizu A., RA Hernandez-Gonzalez I.L., Mendoza-Hernandez G., Lopez-Vidal Y.; RT "Genomic and proteomic analyses of Mycobacterium bovis BCG Mexico 1931 RT reveal a diverse immunogenic repertoire against tuberculosis RT infection."; RL BMC Genomics 12:493-493(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002095; AET17712.1; -; Genomic_DNA. DR RefSeq; YP_005169895.1; NC_016804.1. DR ProteinModelPortal; G7QUD7; -. DR SMR; G7QUD7; 1-221. DR EnsemblBacteria; AET17712; AET17712; BCGMEX_0424c. DR GeneID; 11808689; -. DR KEGG; mbm:BCGMEX_0424c; -. DR KO; K00788; -. DR BioCyc; MBOV717522:GJXR-428-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID G7R8N4_ECOC2 Unreviewed; 212 AA. AC G7R8N4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=i02_4540; OS Escherichia coli (strain 'clone D i2'). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=885276; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN='clone D i2'; RX PubMed=22046404; DOI=10.1371/journal.pone.0026907; RA Reeves P.R., Liu B., Zhou Z., Li D., Guo D., Ren Y., Clabots C., RA Lan R., Johnson J.R., Wang L.; RT "Rates of Mutation and Host Transmission for an Escherichia coli Clone RT over 3 Years."; RL PLoS ONE 6:E26907-E26907(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002211; AER87057.1; -; Genomic_DNA. DR RefSeq; YP_006151681.1; NC_017651.1. DR ProteinModelPortal; G7R8N4; -. DR EnsemblBacteria; AER87057; AER87057; i02_4540. DR GeneID; 12672329; -. DR KEGG; eld:i02_4540; -. DR KO; K00788; -. DR BioCyc; ECOL885276:GJE7-4575-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23162 MW; 04F34CDA749CE849 CRC64; MMYQPEFPPV PFRLGLYPVV DSVQWIERLL DAGVRTLQLR IKDQRDEEVE ADVVAAIALG RRYNARLFIN DYWRLAIKHQ AYGVHLGQED LQATDLSTIR AAGLRLGVST HDDMEIDVAL AARPSYIALG HVFPTQTKQM PSAPQGLEQL ARHVERLADY PTVAIGGISL ARAPAVIATG VGSIAVVSAI TQAADWRLAT AQLLEIAGVG DE // ID G7RGH4_ECOC1 Unreviewed; 212 AA. AC G7RGH4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=i14_4540; OS Escherichia coli (strain 'clone D i14'). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=885275; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN='clone D i14'; RX PubMed=22046404; DOI=10.1371/journal.pone.0026907; RA Reeves P.R., Liu B., Zhou Z., Li D., Guo D., Ren Y., Clabots C., RA Lan R., Johnson J.R., Wang L.; RT "Rates of Mutation and Host Transmission for an Escherichia coli Clone RT over 3 Years."; RL PLoS ONE 6:E26907-E26907(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002212; AER91976.1; -; Genomic_DNA. DR RefSeq; YP_006156600.1; NC_017652.1. DR ProteinModelPortal; G7RGH4; -. DR EnsemblBacteria; AER91976; AER91976; i14_4540. DR GeneID; 12667280; -. DR KEGG; elc:i14_4540; -. DR KO; K00788; -. DR BioCyc; ECOL885275:GJE6-4575-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23162 MW; 04F34CDA749CE849 CRC64; MMYQPEFPPV PFRLGLYPVV DSVQWIERLL DAGVRTLQLR IKDQRDEEVE ADVVAAIALG RRYNARLFIN DYWRLAIKHQ AYGVHLGQED LQATDLSTIR AAGLRLGVST HDDMEIDVAL AARPSYIALG HVFPTQTKQM PSAPQGLEQL ARHVERLADY PTVAIGGISL ARAPAVIATG VGSIAVVSAI TQAADWRLAT AQLLEIAGVG DE // ID G7RZ82_STRSU Unreviewed; 229 AA. AC G7RZ82; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSUA7_0685; OS Streptococcus suis A7. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=993512; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A7; RX PubMed=22026465; DOI=10.1186/1471-2164-12-523; RA Zhang A., Yang M., Hu P., Wu J., Chen B., Hua Y., Yu J., Chen H., RA Xiao J., Jin M.; RT "Comparative Genomic Analysis of Streptococcus suis reveals RT significant genomic diversity among different serotypes."; RL BMC Genomics 12:523-523(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002570; AER44013.1; -; Genomic_DNA. DR RefSeq; YP_006084355.1; NC_017622.1. DR EnsemblBacteria; AER44013; AER44013; SSUA7_0685. DR GeneID; 12713300; -. DR KEGG; ssf:SSUA7_0685; -. DR KO; K00788; -. DR BioCyc; SSUI993512:GLLI-739-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 24867 MW; 13E429C3937D4B31 CRC64; MNRKMLQVYF ICGTSDCPKG KFLDVLEKAL QAGITCFQFR EKGEQGLTGA DKLLLAKQVQ HLCHRYQVPL IINDDVELAR AIDADGIHLG QEDLSVVEAR QLFPGEIIGL SVGTKEEYLN SPIDLVDYIG SGPVFPTLSK DDASPAIGMD GLKQLRKLNS DIPMVAIGGL SAKDCKEVLQ AGADGIAVIS AISHAEDPYK ATKILVDGMQ AMILKFNQVE SNKQILKNP // ID G7S5D7_STRSU Unreviewed; 229 AA. AC G7S5D7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSU12_0687; OS Streptococcus suis SS12. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1005041; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS12; RX PubMed=22026465; DOI=10.1186/1471-2164-12-523; RA Zhang A., Yang M., Hu P., Wu J., Chen B., Hua Y., Yu J., Chen H., RA Xiao J., Jin M.; RT "Comparative Genomic Analysis of Streptococcus suis reveals RT significant genomic diversity among different serotypes."; RL BMC Genomics 12:523-523(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002640; AER14874.1; -; Genomic_DNA. DR RefSeq; YP_006078122.1; NC_017619.1. DR ProteinModelPortal; G7S5D7; -. DR EnsemblBacteria; AER14874; AER14874; SSU12_0687. DR GeneID; 12719745; -. DR KEGG; suo:SSU12_0687; -. DR KO; K00788; -. DR BioCyc; SSUI1005041:GLLO-732-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 24866 MW; 13EC09C5B3734B31 CRC64; MNRKMLQVYF ICGTSDCPKG KFLDVLEKAL QAGITCFQFR EKGEQGLTGA DKLLLAKQVQ HLCHRYQVPL IINDDVELAR AIDADGIHLG QEDLSVVEAR QLFPGKIIGL SVGTKEEYLN SPIDLVDYIG SGPVFPTLSK DDASPAIGMD GLKQLRKLNS DIPMVAIGGL SAKDCKEVLQ AGADGIAVIS AISHAEDPYK ATKILVDGMQ AMILKFNQVE SNKQILKNP // ID G7SU75_PASMD Unreviewed; 221 AA. AC G7SU75; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Pmu_19200; OS Pasteurella multocida 36950. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=1075089; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=36950; RX PubMed=22001176; DOI=10.1093/jac/dkr411; RA Michael G.B., Kadlec K., Sweeney M.T., Brzuszkiewicz E., Liesegang H., RA Daniel R., Murray R.W., Watts J.L., Schwarz S.; RT "ICEPmu1, an integrative conjugative element (ICE) of Pasteurella RT multocida: structure and transfer."; RL J. Antimicrob. Chemother. 0:0-0(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003022; AET16778.1; -; Genomic_DNA. DR RefSeq; YP_005177747.1; NC_016808.1. DR EnsemblBacteria; AET16778; AET16778; Pmu_19200. DR GeneID; 11806070; -. DR BioCyc; PMUL1075089:GJSX-1898-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23678 MW; ADC6E7ECF5E63FB2 CRC64; MKPVHAFMRL YFIAGTQDCL HLDGDPAQNL LNILQQALQS GITCYQFREK GKKALQDPDK IKALAIQCRD LCRQYQVPFV VNDDVQLAID IGADGIHVGQ TDMAVADVAA LCHSHCFIGT SVNTLEQGIA AQANPLIDYF GTGPIFPTQS KEDPKPVVGV DFVSTIRAHG IDKPIVAIGG VTAQTAEELR QRGANGVAVI SAITQSADIA KTVKELLGNA Q // ID G7T5N9_SALPS Unreviewed; 211 AA. AC G7T5N9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPUL_3421; OS Salmonella pullorum (strain RKS5078 / SGSC2294). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1081093; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RKS5078 / SGSC2294; RX PubMed=22247537; DOI=10.1128/JB.06507-11; RA Feng Y., Xu H.F., Li Q.H., Zhang S.Y., Wang C.X., Zhu D.L., Cao F.L., RA Li Y.G., Johnston R.N., Zhou J., Liu G.R., Liu S.L.; RT "Complete Genome Sequence of Salmonella enterica Serovar Pullorum RT RKS5078."; RL J. Bacteriol. 194:744-744(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003047; AET55680.1; -; Genomic_DNA. DR RefSeq; YP_005214510.1; NC_016831.1. DR EnsemblBacteria; AET55680; AET55680; SPUL_3421. DR OMA; AVRPSYI; -. DR BioCyc; SENT1081093:GJVO-3479-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22884 MW; 3A859FEA5EC3483B CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQG AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RATAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID G7TDS2_9XANT Unreviewed; 315 AA. AC G7TDS2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 22-JAN-2014, entry version 15. DE SubName: Full=Dgtp-pyrophosphohydrolase, thiamine phosphate synthase; GN ORFNames=XOC_0855; OS Xanthomonas oryzae pv. oryzicola BLS256. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=383407; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BLS256; RX PubMed=21784931; DOI=10.1128/JB.05262-11; RA Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., RA Patil P.B., Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., RA Aparna G., Rajaram M., Delcher A.L., Phillippy A.M., Puiu D., RA Schatz M.C., Shumway M., Sommer D.D., Trapnell C., Benahmed F., RA Dimitrov G., Madupu R., Radune D., Sullivan S., Jha G., Ishihara H., RA Lee S.W., Pandey A., Sharma V., Sriariyanun M., Szurek B., RA Vera-Cruz C.M., Dorman K.S., Ronald P.C., Verdier V., Dow J.M., RA Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D., Leach J.E., RA White F.F., Salzberg S.L.; RT "Two New Complete Genome Sequences Offer Insight into Host and Tissue RT Specificity of Plant Pathogenic Xanthomonas spp."; RL J. Bacteriol. 193:5450-5464(2011). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003057; AEQ95061.1; -; Genomic_DNA. DR RefSeq; YP_005627228.1; NC_017267.1. DR ProteinModelPortal; G7TDS2; -. DR EnsemblBacteria; AEQ95061; AEQ95061; XOC_0855. DR GeneID; 12272844; -. DR KEGG; xor:XOC_0855; -. DR KO; K03574; -. DR BioCyc; XORY383407:GLMS-804-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34942 MW; EB2A24937F0B694E CRC64; MPDSLRSIHV VAGVITDPRG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIEAQVGD WLMDVPQLYP DKRLRLEVRH ITAWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGAL RQPDHYLITP EPEDDARWLE GLERALQNGI TRIQLRARQT APAQWQALLQ QVMRLRGRTR AQLLLNRDIA LAVELGVGVH LGSEQLAGLQ ERPLPTEQLV AASCHGLDDL RHAQRIGCDF AVLGPVQATA SHPGATPLGW DGFETLREQV SLPIYALGGM QIEDVREARS HGAQGIAAIR SLWPQ // ID G7TFL3_9XANT Unreviewed; 207 AA. AC G7TFL3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=XOC_3672; OS Xanthomonas oryzae pv. oryzicola BLS256. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=383407; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BLS256; RX PubMed=21784931; DOI=10.1128/JB.05262-11; RA Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., RA Patil P.B., Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., RA Aparna G., Rajaram M., Delcher A.L., Phillippy A.M., Puiu D., RA Schatz M.C., Shumway M., Sommer D.D., Trapnell C., Benahmed F., RA Dimitrov G., Madupu R., Radune D., Sullivan S., Jha G., Ishihara H., RA Lee S.W., Pandey A., Sharma V., Sriariyanun M., Szurek B., RA Vera-Cruz C.M., Dorman K.S., Ronald P.C., Verdier V., Dow J.M., RA Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D., Leach J.E., RA White F.F., Salzberg S.L.; RT "Two New Complete Genome Sequences Offer Insight into Host and Tissue RT Specificity of Plant Pathogenic Xanthomonas spp."; RL J. Bacteriol. 193:5450-5464(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003057; AEQ97762.1; -; Genomic_DNA. DR RefSeq; YP_005629930.1; NC_017267.1. DR EnsemblBacteria; AEQ97762; AEQ97762; XOC_3672. DR GeneID; 12274938; -. DR KEGG; xor:XOC_3672; -. DR KO; K00788; -. DR BioCyc; XORY383407:GLMS-3569-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21578 MW; 5B0E94B864810AB0 CRC64; MPNRLNVRGV YLITPDEPNT QRLLLRTTPL LASIAWLQYR NKQADAALRL RQASALREAC VAHGVPLIIN DDAQLAAQVG AQGVHLGEDD GEVTAARALL GEQAIIGVSC YDEIERARAA AAAGASYVAF GAFFPTITKQ TTRRATTALL QQSAELHLAR VAIGGIAPAQ VPALVSAGAD LIAVVSGVYA APDPVAAVQA YRAGFAG // ID G7TS12_VIBCL Unreviewed; 440 AA. AC G7TS12; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-MAR-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Vch1786_I2344; OS Vibrio cholerae O1 str. 2010EL-1786. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=914149; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2010EL-1786; RX PubMed=22099115; DOI=10.3201/eid1711.110794; RG V. cholerae Outbreak Genomics Task Force; RA Reimer A.R., Van Domselaar G., Stroika S., Walker M., Kent H., RA Tarr C., Talkington D., Rowe L., Olsen-Rasmussen M., Frace M., RA Sammons S., Dahourou G.A., Boncy J., Smith A.M., Mabon P., Petkau A., RA Graham M., Gilmour M.W., Gerner-Smidt P.; RT "Comparative genomics of Vibrio cholerae from Haiti, Asia, and RT Africa."; RL Emerg. Infect. Dis. 17:2113-2121(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003069; AET27923.1; -; Genomic_DNA. DR RefSeq; YP_004938477.1; NC_016445.1. DR ProteinModelPortal; G7TS12; -. DR EnsemblBacteria; AET27923; AET27923; Vch1786_I2344. DR GeneID; 11462163; -. DR KEGG; vce:Vch1786_I2344; -. DR KO; K00788; -. DR BioCyc; VCHO914149:GHG2-2344-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID G7U8V1_PROAA Unreviewed; 216 AA. AC G7U8V1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TIIST44_10220; OS Propionibacterium acnes ATCC 11828. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1091045; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11828; RX PubMed=22156398; DOI=10.1128/JB.06388-11; RA Horvath B., Hunyadkurti J., Voros A., Fekete C., Urban E., Kemeny L., RA Nagy I.; RT "Genome Sequence of Propionibacterium acnes Type II Strain ATCC RT 11828."; RL J. Bacteriol. 194:202-203(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003084; AER06499.1; -; Genomic_DNA. DR RefSeq; YP_005986510.1; NC_017550.1. DR ProteinModelPortal; G7U8V1; -. DR EnsemblBacteria; AER06499; AER06499; TIIST44_10220. DR GeneID; 12578169; -. DR KEGG; pad:TIIST44_10220; -. DR KO; K00788; -. DR BioCyc; PACN1091045:GLIL-2013-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22548 MW; D68AAF1B366F1623 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAGMRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID G7UA59_PROAA Unreviewed; 217 AA. AC G7UA59; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TIIST44_05205; OS Propionibacterium acnes ATCC 11828. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1091045; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11828; RX PubMed=22156398; DOI=10.1128/JB.06388-11; RA Horvath B., Hunyadkurti J., Voros A., Fekete C., Urban E., Kemeny L., RA Nagy I.; RT "Genome Sequence of Propionibacterium acnes Type II Strain ATCC RT 11828."; RL J. Bacteriol. 194:202-203(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003084; AER05536.1; -; Genomic_DNA. DR RefSeq; YP_005985547.1; NC_017550.1. DR ProteinModelPortal; G7UA59; -. DR EnsemblBacteria; AER05536; AER05536; TIIST44_05205. DR GeneID; 12577175; -. DR KEGG; pad:TIIST44_05205; -. DR KO; K00788; -. DR BioCyc; PACN1091045:GLIL-1027-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22508 MW; 6BD5C5023BD76D6C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRFPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRTIMASDDP AAVVRQVVQS FDEVRVS // ID G7UB30_PANAN Unreviewed; 210 AA. AC G7UB30; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PAGR_g4058; OS Pantoea ananatis PA13. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=1095774; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PA13; RX PubMed=22207741; DOI=10.1128/JB.06450-11; RA Choi O., Lim J.Y., Seo Y.S., Hwang I., Kim J.; RT "Complete Genome Sequence of the Rice Pathogen Pantoea ananatis Strain RT PA13."; RL J. Bacteriol. 194:531-531(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003085; AER34543.1; -; Genomic_DNA. DR RefSeq; YP_005994763.1; NC_017554.1. DR ProteinModelPortal; G7UB30; -. DR EnsemblBacteria; AER34543; AER34543; PAGR_g4058. DR GeneID; 12585597; -. DR KEGG; paq:PAGR_g4058; -. DR KO; K00788; -. DR BioCyc; PANA1095774:GLIA-4149-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23041 MW; 58C94673C26E3547 CRC64; MDAFPATASR LGLYPVVDSV EWIERLLEAG VRTLQLRIKD QPDEVVEPMI IRAIAAGKRY QARLFINDYW QLAIKHQAYG VHLGQEDLEV ANLQQILHAG LRLGLSTHDD AELDRALALR PSYVALGHIF PTQTKAMPSS PQGVAELKRH LARLHGISTV AIGGISIDRA PEVLATGVGS IAVVSAITQA EDWQEATRVL LRLAEPETAY // ID G7UN35_PSEUP Unreviewed; 208 AA. AC G7UN35; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=DSC_03465; OS Pseudoxanthomonas spadix (strain BD-a59). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Pseudoxanthomonas. OX NCBI_TaxID=1045855; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BD-a59; RX PubMed=22207748; DOI=10.1128/JB.06436-11; RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.; RT "Complete Genome Sequence of the BTEX-Degrading Bacterium RT Pseudoxanthomonas spadix BD-a59."; RL J. Bacteriol. 194:544-544(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003093; AER55346.1; -; Genomic_DNA. DR RefSeq; YP_004929387.1; NC_016147.2. DR EnsemblBacteria; AER55346; AER55346; DSC_03465. DR GeneID; 11375208; -. DR KEGG; psd:DSC_03465; -. DR KO; K00788; -. DR BioCyc; PSPA1045855:GH5V-497-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21384 MW; 29F98DCC536198D3 CRC64; MSTTTPPRGL YLITPDIADD AQLLARTRPL LDSGAVTWLQ YRNKSAGDAQ RRRQAEQLLA LCQAVGVPLI INDDLALALA IGAAGLHRED DISTLAQLRT ALGPHALLGA SCYDQPALAE AAVREGASYV SFGAFFASRS KPTTHRATPA VFQATASLGV PRVAIGGLTP DNAGPVVAAG ADLVAVIGGV VDAPDPIAAA RALQALFA // ID G7UNC2_PSEUP Unreviewed; 324 AA. AC G7UNC2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-APR-2014, entry version 17. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=DSC_03500; OS Pseudoxanthomonas spadix (strain BD-a59). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Pseudoxanthomonas. OX NCBI_TaxID=1045855; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BD-a59; RX PubMed=22207748; DOI=10.1128/JB.06436-11; RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.; RT "Complete Genome Sequence of the BTEX-Degrading Bacterium RT Pseudoxanthomonas spadix BD-a59."; RL J. Bacteriol. 194:544-544(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003093; AER55353.1; -; Genomic_DNA. DR RefSeq; YP_004929394.1; NC_016147.2. DR EnsemblBacteria; AER55353; AER55353; DSC_03500. DR GeneID; 11375215; -. DR KEGG; psd:DSC_03500; -. DR KO; K03574; -. DR BioCyc; PSPA1045855:GH5V-504-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 324 AA; 34943 MW; C86EB015AE858A4E CRC64; MDSASLRFIH VVAAVITDAR GRVLLARRGD GRDLAGLWEF PGGKREPGEA PEQTLVRELQ EELGITVQVG APIMRVPHLY PDKRLLLDIR RVTAWKGVPR GMEGQALAWV EQDKLGRYPM PDADKPVVAV LQQPDRYLVT PEPGADHAAW LVGVAAALAD GVRRVQLRAR NLDGDPAWPA LAAQAVALCH KAGVQVLVNS TAKLARELGA GLHVRGDQLE RLSTKPLLPG TAFAASCHSL EQLRRAEELG CDFVTLGDVR ATAAHPEQPP MGWETFARLR EQVSLPIYAT GGLGIADLAE ARQHGAQGIA AIRGLWPYAA ASSR // ID G7V377_LACRH Unreviewed; 209 AA. AC G7V377; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LRHK_370; OS Lactobacillus rhamnosus ATCC 8530. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1088720; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8530; RX PubMed=22247527; DOI=10.1128/JB.06430-11; RA Pittet V., Ewen E., Bushell B.R., Ziola B.; RT "Genome Sequence of Lactobacillus rhamnosus ATCC 8530."; RL J. Bacteriol. 194:726-726(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003094; AER63219.1; -; Genomic_DNA. DR RefSeq; YP_005872072.1; NC_017491.1. DR ProteinModelPortal; G7V377; -. DR EnsemblBacteria; AER63219; AER63219; LRHK_370. DR GeneID; 12480943; -. DR KEGG; lra:LRHK_370; -. DR KO; K00788; -. DR BioCyc; LRHA1088720:GLFB-365-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21826 MW; DB2D7C7B82C165F7 CRC64; MNAEALQLYL VTNRYADSPE VFLAKIAAAC ENGVTMVQLR EKSLTTRDYY ALAKQVKLIT DRYRIPLIID DRVDVCLAVD AAGVHIGDDE LPVAVTRQLL GSDKILGVST KTVATATAAV AAGADYLGVG AIFPTQTKAA APLTSLATLK AITAAVSVPV VAIGGIKADN LDTFKATGIA GVAIVSEIMQ APDTAQKVQT LSAKLKEVL // ID G7V689_THELD Unreviewed; 212 AA. AC G7V689; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tlie_0172; OS Thermovirga lienii (strain ATCC BAA-1197 / DSM 17291 / Cas60314). OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Thermovirga. OX NCBI_TaxID=580340; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1197 / DSM 17291 / Cas60314; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Saunders E., Kyrpides N., Mavromatis K., Ivanova N., Last F.I., RA Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E.-M., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Thermovirga lienii DSM 17291."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003096; AER65918.1; -; Genomic_DNA. DR RefSeq; YP_004932015.1; NC_016148.1. DR EnsemblBacteria; AER65918; AER65918; Tlie_0172. DR GeneID; 11377235; -. DR KEGG; tli:Tlie_0172; -. DR KO; K00788; -. DR BioCyc; TLIE580340:GH7T-172-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22669 MW; BF85B82970B80D77 CRC64; MTDLAKRLRL YVIPDLSSGR GLPLEEQAKA ALEGGATAIQ LRCKDATSKE LYRYALAFRH LADEYGALFI VNDRLDIALA AKADGVHLGK DDLPVRVARE LAPEGFIIGA TARTPQRAIE AQKEGASYLG VGAIYPTKTK KDTVVIGLDG LNNIVEKVSI PCVAIGGITI KDVKEVIKTG ACGVAVSSAI FGTQNPTETT RRFKAELEGF NN // ID G7VL40_LEUME Unreviewed; 212 AA. AC G7VL40; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MI1_02150; OS Leuconostoc mesenteroides subsp. mesenteroides J18. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=1107880; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J18; RX PubMed=22247530; DOI=10.1128/JB.06498-11; RA Jung J.Y., Lee S.H., Lee S.H., Jeon C.O.; RT "Complete Genome Sequence of Leuconostoc mesenteroides subsp. RT mesenteroides Strain J18, Isolated from Kimchi."; RL J. Bacteriol. 194:730-731(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003101; AET29890.1; -; Genomic_DNA. DR RefSeq; YP_005173856.1; NC_016805.1. DR EnsemblBacteria; AET29890; AET29890; MI1_02150. DR GeneID; 11806854; -. DR KEGG; lmm:MI1_02150; -. DR KO; K00788; -. DR BioCyc; LMES1107880:GLFP-480-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23180 MW; 83922CD682A9A309 CRC64; MFDPSILVNY FVLGTQDTNG ERHFFEVLEE ALQSKISVFQ YREKGQLALS GSEKLRVAKK VRQLTTDYHV PLIIDDDIQL AHEIDAEGVH FGQKDGDIIN NIQLAENLAV GVSVSNDSQY KRIENIKGID YIGIGPVFAT VSKADANPEI GVEGLKYLTS KSKWPSVAIG GISEINLSSV LSTGVNGAAV ISMISQSANI SATLKYWRSL HL // ID G7VN32_LEUME Unreviewed; 212 AA. AC G7VN32; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MI1_05115; OS Leuconostoc mesenteroides subsp. mesenteroides J18. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=1107880; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J18; RX PubMed=22247530; DOI=10.1128/JB.06498-11; RA Jung J.Y., Lee S.H., Lee S.H., Jeon C.O.; RT "Complete Genome Sequence of Leuconostoc mesenteroides subsp. RT mesenteroides Strain J18, Isolated from Kimchi."; RL J. Bacteriol. 194:730-731(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003101; AET30467.1; -; Genomic_DNA. DR RefSeq; YP_005174433.1; NC_016805.1. DR EnsemblBacteria; AET30467; AET30467; MI1_05115. DR GeneID; 11807436; -. DR KEGG; lmm:MI1_05115; -. DR KO; K00788; -. DR BioCyc; LMES1107880:GLFP-1062-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23469 MW; EE4969215AE567D8 CRC64; MDVNITKVLK LYLVTNRYDY SDEEFLGRIE KACQNGVTLV QLREKEVTTH KYFELATKVK EITDRFRIPL IIDDRIDICQ AVDAAGVHIG DNDLPISVAR RLIGPEKILG VSAKSVMRAT QAELEGADYL GVGAIYPTKT KVITKPTSIE TLKEITRTVS IPVIAIGGIK EHTIHNFKNT EVNGVAMVSE IMCAENIADK VSDTIKALDQ VL // ID G7VRX6_PAETH Unreviewed; 206 AA. AC G7VRX6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-OCT-2013, entry version 15. DE SubName: Full=Transcriptional regulator TenI; GN OrderedLocusNames=HPL003_20225; OS Paenibacillus terrae (strain HPL-003). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=985665; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HPL-003; RA Shin S.H., Kim S., Kim J.Y.; RT "Complete sequence of Paenibacillus terrae HPL-003."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HPL-003; RA Shin S.H., Kim S., Kim J.Y.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003107; AET60783.1; -; Genomic_DNA. DR RefSeq; YP_005077006.1; NC_016641.1. DR EnsemblBacteria; AET60783; AET60783; HPL003_20225. DR GeneID; 11583205; -. DR KEGG; pta:HPL003_20225; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR BioCyc; PTER985665:GHT3-4105-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22180 MW; D32CF7D7028F041A CRC64; MHVITMEGDS DAYAHTAQVA AAIHPYVHYI HVRLKQKGAL ELLALTRSMV NLGVPLQKIA VNDRVDVALL TSVGAIQLPA NGLPVAAVKS LLSEGTRCGV SVHSLEEAQA AEWAGAHYVL YGHVYETHCK PGVTPRGIAQ LKRISRLVSI PVIALGGIQP RHIPELYTAG ASGIAVRSGI WEAESPVAAV MAYRRMADRV AHRLHW // ID G7VTI1_PAETH Unreviewed; 220 AA. AC G7VTI1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HPL003_00390; OS Paenibacillus terrae (strain HPL-003). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=985665; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HPL-003; RA Shin S.H., Kim S., Kim J.Y.; RT "Complete sequence of Paenibacillus terrae HPL-003."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HPL-003; RA Shin S.H., Kim S., Kim J.Y.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003107; AET56864.1; -; Genomic_DNA. DR RefSeq; YP_005073087.1; NC_016641.1. DR EnsemblBacteria; AET56864; AET56864; HPL003_00390. DR GeneID; 11587751; -. DR KEGG; pta:HPL003_00390; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; PTER985665:GHT3-87-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23744 MW; 90ECCED001137E1A CRC64; MSSRILSEAV RRHLQMYLVL GSVNCLAEPS WVVQEALAGG ATMVQFREKG RGALTGAPMI ELARRLQDQC RRMGIPFIVN DDVELALELD ADGVHIGQDD ESADSVRERI GNRILGVSAH TIEEARRAIL QGADYLGVGP IYPTISKDDA NAVQGPAILH ELRKAGMDVP IVGIGGITVD RVEEVVRAGA DGVAVISAVT RAEQIRTAVE ELKKKVVLYI // ID G7WF00_DESOD Unreviewed; 209 AA. AC G7WF00; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Desor_2000; OS Desulfosporosinus orientis (strain ATCC 19365 / DSM 765 / NCIMB 8382 / OS VKM B-1628) (Desulfotomaculum orientis). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=768706; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Pester M., RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A., RA Woyke T.; RT "Complete sequence of Desulfosporosinus orientis DSM 765."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003108; AET67611.1; -; Genomic_DNA. DR RefSeq; YP_004970126.1; NC_016584.1. DR EnsemblBacteria; AET67611; AET67611; Desor_2000. DR GeneID; 11616060; -. DR KEGG; dor:Desor_2000; -. DR KO; K00788; -. DR BioCyc; DORI768706:GHQZ-1996-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22343 MW; A0DF3F7A29EF14F3 CRC64; MNKAAVDYTL YLVTDRKQLG NRDLAESIEQ AIQGGVTLVQ LREKSVSTKE FLQLAEKVKE ITSRYQIPLI INDRLDIALA IDADGLHVGQ DDLPMVKARE LLGPDKIIGV SASTLEEALL AEQQGADYLG VGAIFTTATK TDATDVSLKQ LEVIKHSVSI PVVAIGGIGT TNLPLVRAAG VDGVSVVSAI LGQENIYSAA MELKKILSF // ID G7XHS0_ASPKW Unreviewed; 519 AA. AC G7XHS0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-APR-2014, entry version 13. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme; GN ORFNames=AKAW_04593; OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus OS awamori var. kawachi). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=1033177; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 4308; RX PubMed=22045919; DOI=10.1128/EC.05224-11; RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., RA Takashita H., Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.; RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, RT used for brewing the Japanese distilled spirit shochu."; RL Eukaryot. Cell 10:1586-1587(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF126456; GAA86479.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 519 AA; 54604 MW; 72024B571BDAB582 CRC64; MTLDLSVYLV TDSTPAILKG RDLCAVVEEA VKGGVTIVQY RDKKSDTGVQ VETAKKLHQI TKKYNVPLLI NDRVDVALAA GVEGVHLGQD DMAIEVARKL LPENAIIGIS ASSIEEAQKA VAAGADYLGI GTMFATPTKT NTKSIIGTAG TQAILEAISE SGRNVGTVSI GGINASNVQR VLYQSRAPHK ALDGVAIVSA IMAADDPKAA AAEFVKLVSS PPPFVRSEAV TPARDTSALL EQVPQVVQEV VKGHPLVHNM INYVVANFVA NIALSMGASP IMSPYGDEAV DLCQFDGALV INMGTLTSES IPNYLKALKA YNVRGNPVVY DPVGAAATSI RRGAVTQLMA GGYFDLIKGN EGEIRQVYGS SGVTQRGVDS GPSNLDSHKK AQLARDLARR EHNIVLLTGA TDYLSDGERV VAVSNGHELL GQVTGTGCAV GTVSGAFLTT HPKDKFLAVL SGILMYEIAA ENAASKDTVK GPGSFVPAFL DELYAIRQAA LKGDHSWFAG RAKVEEIQL // ID G7Z458_AZOL4 Unreviewed; 224 AA. AC G7Z458; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; Synonyms=thiE; OrderedLocusNames=AZOLI_0809; OS Azospirillum lipoferum (strain 4B). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=862719; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4B; RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430; RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G., RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., RA Robertson J.S., Barbe V., Calteau A., Rouy Z., Mangenot S., RA Prigent-Combaret C., Normand P., Boyer M., Siguier P., Dessaux Y., RA Elmerich C., Condemine G., Krishnen G., Kennedy I., Paterson A.H., RA Gonzalez V., Mavingui P., Zhulin I.B.; RT "Azospirillum genomes reveal transition of bacteria from aquatic to RT terrestrial environments."; RL PLoS Genet. 7:E1002430-E1002430(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ311868; CBS86156.1; -; Genomic_DNA. DR RefSeq; YP_005038402.1; NC_016622.1. DR EnsemblBacteria; CBS86156; CBS86156; AZOLI_0809. DR GeneID; 11554543; -. DR KEGG; ali:AZOLI_0809; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR BioCyc; ALIP862719:GJAA-749-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23686 MW; 66B8364A90074325 CRC64; MAKGKPAQAE PPACRLYLVT PPALEPAAFA PLLREALDAG DVACVQLRLK DCSEDDIRRA CDLLRPIAQE RDVAFILNDH PRLARETGCD GVHVGQQDTP YREARKILGN DAIVGVTCHD SRHLAMIAGE EGADYVAFGA FFPTTTKTAE YKAEPELLSW WSELMEVPCV AIGGITADNC APLVTAGADF LAVVNAVWGH PQGPGAGVRA LNAAIEAALA GSTG // ID G7ZBB8_AZOL4 Unreviewed; 213 AA. AC G7ZBB8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 14-MAY-2014, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN Name=thiE2; OrderedLocusNames=AZOLI_p10289; OS Azospirillum lipoferum (strain 4B). OG Plasmid AZO_p1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=862719; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4B; RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430; RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G., RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., RA Robertson J.S., Barbe V., Calteau A., Rouy Z., Mangenot S., RA Prigent-Combaret C., Normand P., Boyer M., Siguier P., Dessaux Y., RA Elmerich C., Condemine G., Krishnen G., Kennedy I., Paterson A.H., RA Gonzalez V., Mavingui P., Zhulin I.B.; RT "Azospirillum genomes reveal transition of bacteria from aquatic to RT terrestrial environments."; RL PLoS Genet. 7:E1002430-E1002430(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ311869; CBS88575.1; -; Genomic_DNA. DR RefSeq; YP_004973754.1; NC_016585.1. DR EnsemblBacteria; CBS88575; CBS88575; AZOLI_p10289. DR GeneID; 11621686; -. DR KEGG; ali:AZOLI_p10289; -. DR KO; K00788; -. DR OMA; GRSCHTL; -. DR BioCyc; ALIP862719:GJAA-3210-MONOMER; -. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Transferase. SQ SEQUENCE 213 AA; 21605 MW; 0106693DDEAB7AC9 CRC64; MPVPVPPLLA ITDRHLSTLP LPELADRLFA SGLRWLSLRD KDLADADRLA LARVLLQRAR PRGARITLHG DAALAAEAGV DGVHLPTGSD PAAARALLGP AALIGLSGHD SDGADLVERA RGQVDYLTLS PVFPSASKPG YGPCLGISGL RRWAGRGVPV VALGGIDGVQ AVADCLAAGA AGVAVMGLAM RDPQALGPLL AVAAGRTAPS RPG // ID G7ZQA0_STAAU Unreviewed; 213 AA. AC G7ZQA0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAMSHR1132_19150; OS Staphylococcus aureus subsp. aureus MSHR1132. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=985002; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSHR1132; RA Holt D.C., Holden M.T., Tong S.Y., Castillo-Ramirez S., Clarke L., RA Quail M.A., Currie B.J., Parkhill J., Bentley S.D., Feil E.J., RA Giffard P.M.; RT "A very early-branching Staphylococcus aureus lineage lacking the RT carotenoid pigment staphyloxanthin."; RL Genome Biol. Evol. 3:881-895(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR821777; CCE59748.1; -; Genomic_DNA. DR RefSeq; YP_005326417.1; NC_016941.1. DR EnsemblBacteria; CCE59748; CCE59748; SAMSHR1132_19150. DR GeneID; 11933018; -. DR KEGG; suh:SAMSHR1132_19150; -. DR KO; K00788; -. DR BioCyc; SAUR985002:GLKP-1988-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23200 MW; B515EA795F2A74CB CRC64; MFNNSQLNVY FICGTPDVPS HRTIHDVLDE ALKAGITLFQ FREKGTNALK GTEKVELAKE LLNLCHQYQV PFIINDDVEL AKEINADGIH VGQDDAKVNE IAQFFTNKII GLSVSDLDEY SKSDLTDVDY IGVGPIYPTP SKNDAHTPVG PEMIATLKKV NPQLPIVAIG GINTDNVAPI VEAGADGISV ISAISKSENI EGTVKKFKDF FNN // ID G8ALC4_AZOBR Unreviewed; 207 AA. AC G8ALC4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 22-JAN-2014, entry version 12. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN Name=thiE1; ORFNames=AZOBR_110010; OS Azospirillum brasilense Sp245. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=1064539; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sp245; RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G., RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., RA Robertson J.S., Barbe V., Calteau A., Rouy Z., Mangenot S., RA Prigent-Combaret C., Normand P., Boyer M., Siguier P., Dessaux Y., RA Elmerich C., Condemine G., Krishnen G., Kennedy I., Paterson A.H., RA Gonzalez V., Mavingui P., Zhulin I.B.; RT "Azospirillum genomes reveal transition of bacteria from aquatic to RT terrestrial environments."; RL PLoS Genet. 7:e1002430-e1002430(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE577327; CCC98036.1; -; Genomic_DNA. DR RefSeq; YP_005031459.1; NC_016617.1. DR EnsemblBacteria; CCC98036; CCC98036; AZOBR_110010. DR GeneID; 13105556; -. DR KEGG; abs:AZOBR_110010; -. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 207 AA; 21240 MW; A48B4E3E30E7E7BF CRC64; MMAIPSPRLL AITDRRQAAQ PLPDLAARLF AGGLRWLSLR EKDLDESRQI ALAHALVERA RPWGAVVTLH GDPDLALAAG TDGVHLPEGA DVAAARRRLG PGALVGLSTH DAEGIRRAVA GGADYVTLSP VFPSPSKPGY GPPIGTEALR RLAAEAPLPI IALGGVESGT VGDCLAAGAA GVAVMGTAMR TPDRLPDLLK ALKGGQP // ID G8AMY7_AZOBR Unreviewed; 212 AA. AC G8AMY7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; ORFNames=AZOBR_150017; OS Azospirillum brasilense Sp245. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=1064539; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sp245; RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G., RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., RA Robertson J.S., Barbe V., Calteau A., Rouy Z., Mangenot S., RA Prigent-Combaret C., Normand P., Boyer M., Siguier P., Dessaux Y., RA Elmerich C., Condemine G., Krishnen G., Kennedy I., Paterson A.H., RA Gonzalez V., Mavingui P., Zhulin I.B.; RT "Azospirillum genomes reveal transition of bacteria from aquatic to RT terrestrial environments."; RL PLoS Genet. 7:e1002430-e1002430(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE577327; CCC98599.1; -; Genomic_DNA. DR RefSeq; YP_005031985.1; NC_016617.1. DR EnsemblBacteria; CCC98599; CCC98599; AZOBR_150017. DR GeneID; 13107275; -. DR KEGG; abs:AZOBR_150017; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22391 MW; 955CDE6E75F16F4C CRC64; MTETACRLYL VTPPVLEPAA FAPKLTEALD AGDVACVQLR LKDCSDDAVR RACDALRPIA QDRGVAFILN DHPELARETG CDGVHVGQKD TPYAQARRIV GNDAIVGVTC HDSRHLAMEA GEAGADYVAF GAFFPTTTKD AEFKAEPELL RWWSELMEVP CVAIGGITQE NCGPLVSAGA DFLAVVGAVW NHPDGPGTAV KAFNAAIAAA EG // ID G8B777_CANPC Unreviewed; 568 AA. AC G8B777; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-APR-2014, entry version 11. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=CPAR2_103480; OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia OS parapsilosis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; OC Candida. OX NCBI_TaxID=578454; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 317 / ATCC MYA-4646; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., RA Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., RA Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D., RA Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., RA Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., RA Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., RA Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., RA Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., RA Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., RA Kellis M., Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(2009). RN [2] RP GENOME REANNOTATION. RC STRAIN=CDC 317 / ATCC MYA-4646; RX PubMed=22192698; DOI=10.1186/1471-2164-12-628; RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., RA Corton N.J., Berriman M., Butler G.; RT "Using RNA-seq to determine the transcriptional landscape and the RT hypoxic response of the pathogenic yeast Candida parapsilosis."; RL BMC Genomics 12:628-628(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE605203; CCE40310.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 568 AA; 61552 MW; 5B3E73528A0076FC CRC64; MILIRISCYK HGCEWCSSKR IKFALLFEYE AIKFHGQDSR VKNDGLTSTT LKLFNQAMTV DYSLYLVTDS TMIPSSSTFL KQVEDAVNNG VTLVQLREKD ISTLDFIERA KEVHKVTKPK NIPLIINDRV DVALAVDAEG VHVGQDDMPA TLVRKLIGPD KIVGVTCSNP EEVRQVVKEG VADYVGLGTT FATNTKKDVK TPGGVGPVGI RKQMNELSKD IRCVAIGGIN HSNANRVIHQ CRVGDKKLDG IAVVSCIMAS EDAAKATRSL RDEINYTPDW AFTRSFGKNI PSHLMVKNMT DSHPLVHHIT NNVVKNFSAN VTLAIGASPI MSELPEEFEE FASGIPNIGL VINLGTPNAE LMNVFSKALV TYNKYDKPIV FDPVACGASK ARLESCRKLL NQGFVSVIKG NVGEIMSMWK LTPYYKEGSN HENHMRGVDS ISSVKEVEVL EKGFQVASTF GCTVVITGKQ NHILGSDKRS VSVPGGDVVM GSITGTGCSL GSTIAAFLAA EKASPIVGGD ILKATEIAVE LYNRAGACAA EVSQSPGTFM ITFLDKLSEM SQNPEGKT // ID G8BYX5_TETPH Unreviewed; 540 AA. AC G8BYX5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-APR-2014, entry version 13. DE SubName: Full=Uncharacterized protein; GN Name=TPHA0J02470; OrderedLocusNames=TPHA_0J02470; OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / OS NRRL Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; OC Tetrapisispora. OX NCBI_TaxID=1071381; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5; RX PubMed=22123960; DOI=10.1073/pnas.1112808108; RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., RA Byrne K.P., Wolfe K.H.; RT "Evolutionary erosion of yeast sex chromosomes by mating-type RT switching accidents."; RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE612865; CCE65067.1; -; Genomic_DNA. DR RefSeq; XP_003687501.1; XM_003687453.1. DR GeneID; 11532985; -. DR KEGG; tpf:TPHA_0J02470; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 58238 MW; 56DA5347530A0D14 CRC64; MGINKKEVDY SLYLVTDSTM LPEGTTVCSQ VEEGLKNGVT IVQLREKDCD TKSFVLEARK VQRLCIQYNV PLIINDRIDV ALAIQADGVH VGQSDMPIPL VRELVGPDMI VGWSVGNIEE VEQLARWGPN MIDNIGIGMV FPTKTKKNPK KQPFGPQGVI SILDALEENN ADWIKTVAIG GLHPDNIERV LYQCRSSNNR RALDGIAVVS DIMAAEDAGF AATRLRSLLD RTIYNFSNLD LSTPQISSEL IKVIIDQVSK QHPLVQHVTN KVHQNFGANV TLAIGGSPIM SENPDEVLDL ASVSNSALLL NTGTVAALND LKKIVHVYNE VRRPIVFDPV GYSASQTRLD LNNALLSYGQ YTCIKGNIGE ILALAGMGVS KMRGVDSGDD VIDEAILLKA TRRVAFKYKT IAVCTGITDI IVNGTMSGET QLGRNESNTN PELLSYITCT SGDIPIMGRI TASGCSLGST IATLLGSLSI GENAYRAVVA AVILYKTAGK IAANNCTGTG SFNVALLDEL YQLVQSNNPA SWDVTLNISS // ID G8F6V8_CAMJU Unreviewed; 201 AA. AC G8F6V8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=KW1_00595; OS Campylobacter jejuni subsp. jejuni NW. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=1093788; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NW; RA Jerome J.P., Klahn B.D., Bell J.A., Barrick J.E., Brown C.T., RA Mansfield L.S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH376988; EHI16529.1; -; Genomic_DNA. DR ProteinModelPortal; G8F6V8; -. DR EnsemblBacteria; EHI16529; EHI16529; KW1_00595. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID G8F6Z4_CAMJU Unreviewed; 210 AA. AC G8F6Z4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=KW1_00775; OS Campylobacter jejuni subsp. jejuni NW. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=1093788; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NW; RA Jerome J.P., Klahn B.D., Bell J.A., Barrick J.E., Brown C.T., RA Mansfield L.S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH376988; EHI16565.1; -; Genomic_DNA. DR EnsemblBacteria; EHI16565; EHI16565; KW1_00775. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23027 MW; B9C89047D8A65418 CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGNEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID G8FEX3_CAMJU Unreviewed; 210 AA. AC G8FEX3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=KY3_07831; OS Campylobacter jejuni subsp. jejuni D2600. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=1093789; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D2600; RA Jerome J.P., Klahn B.D., Bell J.A., Barrick J.E., Brown C.T., RA Mansfield L.S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH377088; EHI16999.1; -; Genomic_DNA. DR ProteinModelPortal; G8FEX3; -. DR EnsemblBacteria; EHI16999; EHI16999; KY3_07831. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID G8FF10_CAMJU Unreviewed; 201 AA. AC G8FF10; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Transferase; GN ORFNames=KY3_08016; OS Campylobacter jejuni subsp. jejuni D2600. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=1093789; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D2600; RA Jerome J.P., Klahn B.D., Bell J.A., Barrick J.E., Brown C.T., RA Mansfield L.S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH377088; EHI17036.1; -; Genomic_DNA. DR EnsemblBacteria; EHI17036; EHI17036; KY3_08016. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23428 MW; E75C9E503632E917 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID G8JP29_ERECY Unreviewed; 548 AA. AC G8JP29; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 16-APR-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=Ecym_2185; OS Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 OS / NRRL Y-17582) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=931890; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582; RX DOI=10.1534/g3.111.001032; RA Wendland J., Walther A.; RT "Genome evolution in the Eremothecium clade of the Saccharomyces RT complex revealed by comparative genomics."; RL G3 (Bethesda) 1:539-548(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002498; AET37934.1; -; Genomic_DNA. DR RefSeq; XP_003644751.1; XM_003644703.1. DR GeneID; 11470539; -. DR KEGG; erc:Ecym_2185; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 548 AA; 58840 MW; A710B0EB6DE2165E CRC64; MIEKCDVNYR LYLVTDSDML PDGKSFEHQV ESALKGGVTL VQLREKECES KEFLEKAYRL KDLCSRYNVP LIINDRVDIA LAVDADGVHV GQSDIPVPVV RKLLGPKKII GLSVGYSHEV EQLAEWGPGC VDYIGIGMIF STATKKNPKK HPMGTDGAIT ILDALEKCDA SWCRSVLIGG IHLNNVARVL LQSASTSGRR ATDGIAVVSE IMASTDALSA TVSLRKVLDS GRYPYISASA TGSIASSHEI NVQEVTDYLH LVSGRSPLVV HITNRVHENL AANISLALGG SPIITSNAAE CYDLARIKYG SLFINTGTIL PLDSCLNAAK AYNDAKLPIV FDPAGYSATK VRFDLNNQIL KGAQFTCIKG NAGEISSLDC LSVATTRGVD ASDVGKDISA LICSARNVAY RYRTVVVLTG EHDIIVDGSL GYNFNLTQGN YLKPQDLPTY VIHAGSFPII SSVTATGCSL GTVIASILGA ISDLHSVYHA VIAAAVIYKA AGRIASQRAK GNGSYQTELL DALYMLARCE REELISQLLG CDILIRRV // ID G8LGR6_ENTCL Unreviewed; 211 AA. AC G8LGR6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-APR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EcWSU1_00220; OS Enterobacter cloacae EcWSU1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=1045856; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EcWSU1; RX PubMed=22675579; DOI=10.4056/sigs.2174950; RA Humann J.L., Wildung M., Cheng C.H., Lee T., Stewart J.E., Drew J.C., RA Triplett E.W., Main D., Schroeder B.K.; RT "Complete genome of the onion pathogen Enterobacter cloacae EcWSU1."; RL Stand. Genomic Sci. 5:279-286(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002886; AEW71660.1; -; Genomic_DNA. DR RefSeq; YP_004950081.1; NC_016514.1. DR EnsemblBacteria; AEW71660; AEW71660; EcWSU1_00220. DR GeneID; 11486199; -. DR KEGG; eec:EcWSU1_00220; -. DR KO; K00788; -. DR BioCyc; ECLO1045856:GHCE-226-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23077 MW; A89AB49FC5FC6D12 CRC64; MYQPDFPPVP FRLGLYPVVD SVEWIARLLE AGVRTLQLRI KDKRDEEVEN DVAAAIALGR RYHARLFIND YWRLAIKHHA YGVHLGQEDL ETTDLKAIRE AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLAQLA AHVKRLAQYP TVAIGGISLE RAPAVLDTGV GSIAVVSAIT QAADWQAATR QLLQLAGAGD E // ID G8LYL6_CLOCD Unreviewed; 238 AA. AC G8LYL6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Clocl_3525; OS Clostridium clariflavum (strain DSM 19732 / NBRC 101661 / EBR45). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=720554; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19732 / NBRC 101661 / EBR45; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Kitzmiller T., Lynd L., RA Izquierdo J., Woyke T.; RT "Complete sequence of Clostridium clariflavum DSM 19732."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003065; AEV70004.1; -; Genomic_DNA. DR RefSeq; YP_005047928.1; NC_016627.1. DR EnsemblBacteria; AEV70004; AEV70004; Clocl_3525. DR GeneID; 11563938; -. DR KEGG; ccl:Clocl_3525; -. DR BioCyc; CCLA720554:GI2T-3518-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 208 209 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 238 AA; 25599 MW; C0BF12DE7C0D65C7 CRC64; MSMRKKLDIS AYLVVGPENT KGRPVVSIIK DAVEAGFTCV QIRSKVASAR ELIQLTQQAS EAIAQIGKSD EVTLLVNDRL DVVLAARKQG IKVDGIHVGQ SDIPVDVCRE YLGQDSVIGL SARTHEMFEY IKTADVSQID YFGVGPVHET MTKPDCGLDL DGKVVTRSFD EISELVRFSK IPVVVGGGVK LADIPPLAQT GAAGFFVVSA VSEADNPKQA AAELVNAWKQ YAGIIQKD // ID G8M0N2_CLOCD Unreviewed; 215 AA. AC G8M0N2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Clocl_2543; OS Clostridium clariflavum (strain DSM 19732 / NBRC 101661 / EBR45). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=720554; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19732 / NBRC 101661 / EBR45; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Kitzmiller T., Lynd L., RA Izquierdo J., Woyke T.; RT "Complete sequence of Clostridium clariflavum DSM 19732."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003065; AEV69113.1; -; Genomic_DNA. DR RefSeq; YP_005047037.1; NC_016627.1. DR EnsemblBacteria; AEV69113; AEV69113; Clocl_2543. DR GeneID; 11562959; -. DR KEGG; ccl:Clocl_2543; -. DR KO; K00788; -. DR BioCyc; CCLA720554:GI2T-2539-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 24280 MW; 53F766726F7630C2 CRC64; MKRRNDIIDT DLYCITSEEH SRGRNNIEVV REMIKAGVKV IQYRDKEKKL LQKYNECLKI REMTKEAGVT FIVNDHVDIA ILVKADGVHI GQDDLPIEKV RELVGEEMII GISTHSPKQA EEAVKRGADY IGVGPIYKTY TKKDVCEPVG LDYLRYVVRN IPIPHVAIGG IKQHNMHEVI ECGAKCIAMV TEIVGADDIG KKIRDIKESM RRGAL // ID G8M815_9BURK Unreviewed; 215 AA. AC G8M815; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BYI23_A010360; OS Burkholderia sp. YI23. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1097668; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YI23; RX PubMed=22275096; DOI=10.1128/JB.06479-11; RA Lim J.S., Choi B.S., Choi A.Y., Kim K.D., Kim D.I., Choi I.Y., RA Ka J.O.; RT "Complete Genome Sequence of the Fenitrothion-Degrading Burkholderia RT sp. Strain YI23."; RL J. Bacteriol. 194:896-896(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003087; AET88874.1; -; Genomic_DNA. DR RefSeq; YP_004976851.1; NC_016589.1. DR EnsemblBacteria; AET88874; AET88874; BYI23_A010360. DR GeneID; 11745268; -. DR KEGG; byi:BYI23_A010360; -. DR KO; K00788; -. DR BioCyc; BSP1097668:GKEO-1053-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22039 MW; 7705E471A71F5A8C CRC64; MRAAFDLSLY LVLDPVQCGG HDAALAVARA ALEGGATLVQ LRAPEWHKRA WFDLARELAP LARAHGVPFV VNDHVDVALA AGADGVHIGQ RDLPAEIARR LLGPDALIGL SVSNLDETAE ADARAGIVDY LGAGPVYATP TKTDASAPCG IDGLAAIRAA TRLPTVAIGG IQAHNAAEVM RAEPAGLAVV SAICKAPDPR EAAASLAATI AQSRN // ID G8M8Q6_9BURK Unreviewed; 361 AA. AC G8M8Q6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BYI23_A023840; OS Burkholderia sp. YI23. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1097668; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YI23; RX PubMed=22275096; DOI=10.1128/JB.06479-11; RA Lim J.S., Choi B.S., Choi A.Y., Kim K.D., Kim D.I., Choi I.Y., RA Ka J.O.; RT "Complete Genome Sequence of the Fenitrothion-Degrading Burkholderia RT sp. Strain YI23."; RL J. Bacteriol. 194:896-896(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003087; AET90222.1; -; Genomic_DNA. DR RefSeq; YP_004978199.1; NC_016589.1. DR EnsemblBacteria; AET90222; AET90222; BYI23_A023840. DR GeneID; 11747117; -. DR KEGG; byi:BYI23_A023840; -. DR KO; K00788; -. DR BioCyc; BSP1097668:GKEO-2441-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 361 AA; 38988 MW; E3B33447A3077F68 CRC64; MSMLNREVFW PPADELTEVA ERIRARLGAW PAADTRWRVC LTAPEAPSAA DLIVFTEAHD ADTARLAKSG AAVLDAHGGR VTLRRGGEVF ALEGEWSDDW LTALAAFLDC NFEPHDALTL ALAWRAGDEN KADAWPVDFA TFPRVAGLPA APEGGFPACP DRLGLYPVLP SAEWVERVLD LGVRTAQLRR KSADAADLQR EIARSVEAGR RHDAQLFIND HWREAIAAGA YGVHLGQEDV QTADLAAIAK AGLRLGLSTH GYYEMLRALH FRPSYLALGA VYPTTTKVMP TKPQGLERLA RYVQLLSGRV PLVAIGGIDA KVMPDVLATG VGSAAVVRAV TEAPDTASAV SSLRHMFACQ R // ID G8N430_GEOTH Unreviewed; 221 AA. AC G8N430; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GTCCBUS3UF5_17440; OS Geobacillus thermoleovorans CCB_US3_UF5. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1111068; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCB_US3_UF5; RA Muhd Sakaff M.K.L., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.; RT "Complete genome sequence of thermophilic Geobacillus thermoleovorans RT CCB_US3_UF5."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003125; AEV19056.1; -; Genomic_DNA. DR RefSeq; YP_004982156.1; NC_016593.1. DR ProteinModelPortal; G8N430; -. DR SMR; G8N430; 1-220. DR EnsemblBacteria; AEV19056; AEV19056; GTCCBUS3UF5_17440. DR GeneID; 11625964; -. DR KEGG; gte:GTCCBUS3UF5_17440; -. DR KO; K00788; -. DR BioCyc; GTHE1111068:GJY8-1798-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23044 MW; FCC8031FF0737252 CRC64; MVRIASGEMK ERLAVYFIMG SQNSERPAAD VLKEALDGGV TLFQFREKGP GALKGADKEA LARQLQRLCR AYGVPFIVND DVELALAIDA DGVHVGQDDE DARRVREKIG DKILGVSAHN VEEAMAAVEA GADYLGVGPI YPTSSKEDAK EAQGPDVLRR LREAGITIPI VAIGGITAAN AKTVVEAGAD GVSVISAIAS APSPKAAAAA LAEAVRAART R // ID G8N6A5_GEOTH Unreviewed; 201 AA. AC G8N6A5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=GTCCBUS3UF5_6900; OS Geobacillus thermoleovorans CCB_US3_UF5. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1111068; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCB_US3_UF5; RA Muhd Sakaff M.K.L., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.; RT "Complete genome sequence of thermophilic Geobacillus thermoleovorans RT CCB_US3_UF5."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003125; AEV18013.1; -; Genomic_DNA. DR RefSeq; YP_004981113.1; NC_016593.1. DR ProteinModelPortal; G8N6A5; -. DR EnsemblBacteria; AEV18013; AEV18013; GTCCBUS3UF5_6900. DR GeneID; 11628305; -. DR KEGG; gte:GTCCBUS3UF5_6900; -. DR KO; K10810; -. DR BioCyc; GTHE1111068:GJY8-753-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 21085 MW; 88EB5141BF610405 CRC64; MGVLHFVSTG RQTVDEFAAI CAHTHPYADL IHIREKGKTA REVAAFVAAL LRVGVPLQKI IVNDRVDVAA VYGVKGVQLA YHSLPVRAVR RSFPDLTVGC SVHGSEEAKQ AEQDGAHFCL YGHIFPTDSK PGLPPRGLDS LAEIAAAVSI PVIAIGGIHA GNARRVLEAG AAGVAVLSAV FFAADPVAEA KRLADIVKGR G // ID G8NDY8_9DEIN Unreviewed; 206 AA. AC G8NDY8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TCCBUS3UF1_13470; OS Thermus sp. CCB_US3_UF1. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=1111069; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCB_US3_UF1; RA Teh B.S., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.; RT "Complete genome sequence of thermophilic Thermus sp. CCB_US3_UF1."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003126; AEV16389.1; -; Genomic_DNA. DR RefSeq; YP_005654463.1; NC_017278.1. DR EnsemblBacteria; AEV16389; AEV16389; TCCBUS3UF1_13470. DR GeneID; 12252095; -. DR KEGG; thc:TCCBUS3UF1_13470; -. DR KO; K00788; -. DR BioCyc; TSP1111069:GLMD-1355-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22527 MW; 9F614EB407D192D2 CRC64; MQGRLYLVVT PRPGWTWEEV LDRTERALAG GVEVLQLRAK DWEARPILEL GERMGLLARR YGVPFFLNDR PDLAALLGAD GVHLGQGDLR PEEARRFFGG LVGRSTHAPE QALKALEEGA DYLSVGPVWE TPTKPGRPAA GLGYVRWAAA HLGEKPWFAI GGIDLGNLDQ VLATGARRVV VVRAILDAED PEGAARAFRE RLYGVA // ID G8NGC0_BRUSS Unreviewed; 203 AA. AC G8NGC0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BSVBI22_A0214; OS Brucella suis VBI22. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1112912; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VBI22; RX PubMed=22275106; DOI=10.1128/JB.06556-11; RA Tae H., Shallom S., Settlage R., Hawkins G.N., Adams L.G., RA Garner H.R.; RT "Complete Genome Sequence of Brucella suis VBI22, Isolated from Bovine RT Milk."; RL J. Bacteriol. 194:910-910(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003128; AEU05243.1; -; Genomic_DNA. DR RefSeq; YP_005153915.1; NC_016797.1. DR ProteinModelPortal; G8NGC0; -. DR EnsemblBacteria; AEU05243; AEU05243; BSVBI22_A0214. DR GeneID; 11727686; -. DR KEGG; bsv:BSVBI22_A0214; -. DR KO; K00788; -. DR BioCyc; BSUI1112912:GJTI-216-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID G8NHT1_BRUSS Unreviewed; 221 AA. AC G8NHT1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=BSVBI22_A1703; OS Brucella suis VBI22. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1112912; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VBI22; RX PubMed=22275106; DOI=10.1128/JB.06556-11; RA Tae H., Shallom S., Settlage R., Hawkins G.N., Adams L.G., RA Garner H.R.; RT "Complete Genome Sequence of Brucella suis VBI22, Isolated from Bovine RT Milk."; RL J. Bacteriol. 194:910-910(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003128; AEU06694.1; -; Genomic_DNA. DR RefSeq; YP_005155366.1; NC_016797.1. DR ProteinModelPortal; G8NHT1; -. DR EnsemblBacteria; AEU06694; AEU06694; BSVBI22_A1703. DR GeneID; 11729312; -. DR KEGG; bsv:BSVBI22_A1703; -. DR KO; K00788; -. DR BioCyc; BSUI1112912:GJTI-1740-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID G8NTB4_GRAMM Unreviewed; 202 AA. AC G8NTB4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=AciX8_4353; OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Granulicella. OX NCBI_TaxID=682795; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Rawat S., Mannisto M., Haggblom M., Woyke T.; RT "Complete sequence of Granulicella mallensis MP5ACTX8."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003130; AEU38626.1; -; Genomic_DNA. DR RefSeq; YP_005059656.1; NC_016631.1. DR EnsemblBacteria; AEU38626; AEU38626; AciX8_4353. DR GeneID; 11572252; -. DR KEGG; gma:AciX8_4353; -. DR KO; K00788; -. DR BioCyc; GMAL682795:GHBV-4405-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 21505 MW; 4747F6E82528746C CRC64; MNTLCEVLRY AITDGSRFED AVTRHDELIA DARRWASQEI DFVQLREKTI EAGELLALAE AMVAIFREEG GHTKLLINSR VDVAIAARAD GVHLTGQHEG LTPSQVRQIY ARAAIVSMSC HSLVEVEQAC ALGASLILFG PVFEKRVGKV VVTEGRGIDS LRQACAVARN IPVLALGGVT PENAGACVEA GAAGIAGIRL FG // ID G8P1T0_GRAMM Unreviewed; 206 AA. AC G8P1T0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AciX8_1564; OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Granulicella. OX NCBI_TaxID=682795; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Rawat S., Mannisto M., Haggblom M., Woyke T.; RT "Complete sequence of Granulicella mallensis MP5ACTX8."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003130; AEU35905.1; -; Genomic_DNA. DR RefSeq; YP_005056935.1; NC_016631.1. DR ProteinModelPortal; G8P1T0; -. DR EnsemblBacteria; AEU35905; AEU35905; AciX8_1564. DR GeneID; 11572663; -. DR KEGG; gma:AciX8_1564; -. DR KO; K00788; -. DR BioCyc; GMAL682795:GHBV-1583-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21639 MW; D126EE789CB1D80A CRC64; MTPLYPIIDK ETFTTRGILV ADFARELRDA GVTLLQYRDK TGTPQEILQA AVEIAAVFAG VEATLILNDR ADLAALAGWN GVHVGHLDLP PAAVRRVLGA GRMIGVSTHN DEQVRVADAS EADYIAVGPV FATSTKLNAE PVVGLEGVQR ARALTAKPIV AIGGINRENA RAVIEAGADS IAVIGGLFSG GESAGKVARD FLEFLR // ID G8P3P0_LACLC Unreviewed; 218 AA. AC G8P3P0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=llh_6955; OS Lactococcus lactis subsp. cremoris A76. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=1104322; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A76; RA Bolotin A., Quinquis B., Ehrlich S.D., Sorokin A.; RT "Complete Genome Sequence of Lactococcus lactis subsp. cremoris A76."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003132; AEU40567.1; -; Genomic_DNA. DR RefSeq; YP_005875990.1; NC_017492.1. DR EnsemblBacteria; AEU40567; AEU40567; llh_6955. DR GeneID; 12484967; -. DR KEGG; llr:llh_6955; -. DR KO; K00788; -. DR BioCyc; LLAC1104322:GLFE-1411-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23608 MW; 931832DC5E93AD94 CRC64; MTNKTLDLSV YFIAGPQNFS ECSLDGATQK IALIIKSGVT VYQFRDKGTI YKEQKQRLSI AQKLQKASEE AGVSFIVNDD VELARELNAD GIHIGQTDES VSKVREKVGQ EMWLGLSVTK ADELKTAQSS GADYLGIGPI YPTNSKNDAA KPIGIKDLRL MLLENQLPIV GIGGITQDSL TELSAIGLDG LAVISLLTEA ENPKKVAQMI RQKITKNG // ID G8PAI8_PEDCP Unreviewed; 216 AA. AC G8PAI8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 14-MAY-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PECL_1559; OS Pediococcus claussenii (strain ATCC BAA-344 / DSM 14800 / JCM 18046 / OS KCTC 3811 / P06). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=701521; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06; RA Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K., RA Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J., RA Kusalik A., Ziola B.; RT "Genome and plasmid sequences for the beer-spoilage organism RT Pediococcus claussenii ATCC BAA-344T."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003137; AEV95777.1; -; Genomic_DNA. DR RefSeq; YP_005005453.1; NC_016605.1. DR EnsemblBacteria; AEV95777; AEV95777; PECL_1559. DR GeneID; 11647715; -. DR KEGG; pce:PECL_1559; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; PCLA701521:GKFD-1519-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23728 MW; C08D69CC45BC32AF CRC64; MKFDEKILKI YLVAGTQDVK DKGQFLQKVE ELLKNGITAF QLREKGINSI QNRSELVILA KQCHELTQKY HIPLIIDDDV DLAIQVGAEG IHVGQKDEQI GSVLNRVGNE MIVGLSCNRM TQVEQANGLV GIDYIGSGTV FETTSKSDAG EAIGVNELHK LVEKSRYPVV AIGGITMSNL AQTMRTGVKG FAAISLFTQM KDPEINMKKI QKIVNA // ID G8PK01_PSEUV Unreviewed; 213 AA. AC G8PK01; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=PSE_4699; OS Pseudovibrio sp. (strain FO-BEG1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudovibrio. OX NCBI_TaxID=911045; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FO-BEG1; RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.; RT "The genus Pseudovibrio contains metabolically versatile and RT symbiotically interacting bacteria."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003147; AEV39201.1; -; Genomic_DNA. DR RefSeq; YP_005083223.1; NC_016642.1. DR EnsemblBacteria; AEV39201; AEV39201; PSE_4699. DR GeneID; 11590003; -. DR KEGG; psf:PSE_4699; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR BioCyc; PSP911045:GJTQ-4767-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 213 AA; 23101 MW; 28A3A64E4F730B5F CRC64; MHPRLYLVTP PTFDLDEFEG QLKQALEGGD IASLLISMPD ANEGELQAAA KRLVPLAQAN EVAVLIENNT QIMGRSGADG LHVSGTDKDL EDVMQSFPED RIIGHAGVKT RHDAMVIASM GVDYMFFGLL SLKQEEEPHR KSLDYGSWWS EVFETPCVVL AGTSVSSVDT VAQTGAEFVA VREAVWNHPE GPKAAVEQAN AILSTHTLAE VED // ID G8PMX8_PSEUV Unreviewed; 213 AA. AC G8PMX8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 14-MAY-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PSE_0621; OS Pseudovibrio sp. (strain FO-BEG1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudovibrio. OX NCBI_TaxID=911045; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FO-BEG1; RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.; RT "The genus Pseudovibrio contains metabolically versatile and RT symbiotically interacting bacteria."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003147; AEV35133.1; -; Genomic_DNA. DR RefSeq; YP_005079155.1; NC_016642.1. DR EnsemblBacteria; AEV35133; AEV35133; PSE_0621. DR GeneID; 11588895; -. DR KEGG; psf:PSE_0621; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; PSP911045:GJTQ-625-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 21971 MW; 590E913795ED75B4 CRC64; MKPLLDLSVY LVLGPQDCPG QDPVDIAVAA SQNGSTVVQL RDKTGSTKEQ IELAERLMQA LKPLNVPLIV NDRVDVALAV HADGVHVGQD DMDATKAREL IGADKLLGLS VSTQDELDAA DIAACDYLGI GACFPTNSKD DAADVGMQNF ADLTAQSQLP VVGIGGISLA NADQVIKAGA DGVAVISAIC GAPSAAEATR KLQEIVKSVK DLG // ID G8PPB0_PSEUV Unreviewed; 200 AA. AC G8PPB0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PSE_3819; OS Pseudovibrio sp. (strain FO-BEG1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudovibrio. OX NCBI_TaxID=911045; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FO-BEG1; RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.; RT "The genus Pseudovibrio contains metabolically versatile and RT symbiotically interacting bacteria."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003147; AEV38323.1; -; Genomic_DNA. DR RefSeq; YP_005082345.1; NC_016642.1. DR EnsemblBacteria; AEV38323; AEV38323; PSE_3819. DR GeneID; 11591073; -. DR KEGG; psf:PSE_3819; -. DR KO; K00788; -. DR OMA; KWRERTN; -. DR BioCyc; PSP911045:GJTQ-3869-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 200 AA; 22542 MW; 57086F36701FA5C1 CRC64; MLDRFYLIID GTQWLPRVLP LGVKFCQLRI KDKSEDEIRS QVREAKQLCD KAGAVLVVND HWQAAYDANV GYVHLGQEDL KTADFRALRS AGIYYGISTH DEAELDTALA LDPEYVALGP IYNSTSKEMH WQPQGLETLK KWRERTNKHL VAIGGITLER ASDVFSAGAD SIATISDVTT ATNPEHRTAQ WLEASKNWQR // ID G8PQK9_PSEUV Unreviewed; 197 AA. AC G8PQK9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 14-MAY-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PSE_0907; OS Pseudovibrio sp. (strain FO-BEG1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudovibrio. OX NCBI_TaxID=911045; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FO-BEG1; RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.; RT "The genus Pseudovibrio contains metabolically versatile and RT symbiotically interacting bacteria."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003147; AEV35419.1; -; Genomic_DNA. DR RefSeq; YP_005079441.1; NC_016642.1. DR EnsemblBacteria; AEV35419; AEV35419; PSE_0907. DR GeneID; 11589437; -. DR KEGG; psf:PSE_0907; -. DR KO; K00788; -. DR OMA; HIANIQK; -. DR BioCyc; PSP911045:GJTQ-921-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 26 30 HMP-PP binding (By similarity). FT REGION 175 176 THZ-P binding (By similarity). FT METAL 59 59 Magnesium (By similarity). FT METAL 78 78 Magnesium (By similarity). FT BINDING 58 58 HMP-PP (By similarity). FT BINDING 97 97 HMP-PP (By similarity). FT BINDING 126 126 HMP-PP (By similarity). FT BINDING 155 155 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 197 AA; 22204 MW; 5AC8DD4DAC4858B7 CRC64; MERFYLITGD LDWIEKLVPH GVRLVQLRIK DQPETEVRRQ VIKARDFCKA HGTQLIINDY WELALELGCD FIHLGQEDMD TADFAALRRA SVRFGLSTHD EAELDRALSH EPEYVALGPV YPTKLKKMKW APQGLDRVRR WKQMVGGTPL VAIGGLTPER LAGVFEAGAD SAAVVTDILQ APDPVARTQE WAEACRL // ID G8PXX4_PSEFL Unreviewed; 208 AA. AC G8PXX4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PSF113_5135; OS Pseudomonas fluorescens F113. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1114970; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F113; RX PubMed=22328765; DOI=10.1128/JB.06601-11; RA Redondo-Nieto M., Barret M., Morrisey J.P., Germaine K., RA Martinez-Granero F., Barahona E., Navazo A., Sanchez-Contreras M., RA Moynihan J.A., Giddens S.R., Coppoolse E.R., Muriel C., Stiekema W.J., RA Rainey P.B., Dowling D., O'Gara F., Martin M., Rivilla R.; RT "Genome Sequence of the Biocontrol Strain Pseudomonas fluorescens RT F113."; RL J. Bacteriol. 194:1273-1274(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003150; AEV65114.1; -; Genomic_DNA. DR RefSeq; YP_005210509.1; NC_016830.1. DR EnsemblBacteria; AEV65114; AEV65114; PSF113_5135. DR GeneID; 11833241; -. DR KEGG; pfe:PSF113_5135; -. DR KO; K00788; -. DR BioCyc; PFLU1114970:GJXA-5168-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22162 MW; CABF6774E993D89C CRC64; MKLRGLYAIT DSQLLAGKFL AYVEAALEGG VTLLQYRDKS SDEARRLREA EALRNLCERY KTQLIINDDA ELAARLGVGV HLGQTDGPLA PVRALLGHKA IVGATCHASL ALAEQAASEG ATYVAFGRFF NSNTKPGAPS ANLELLEQAH LKLHIPVCAI GGITLDNAAP LVAHGVDLLA VVHGLFGADS TTEVTRRARA FNELLQIK // ID G8Q816_PSEFL Unreviewed; 314 AA. AC G8Q816; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 18. DE SubName: Full=MutT; DE EC=2.5.1.3; GN Name=mutT2; ORFNames=PSF113_4633; OS Pseudomonas fluorescens F113. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1114970; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F113; RX PubMed=22328765; DOI=10.1128/JB.06601-11; RA Redondo-Nieto M., Barret M., Morrisey J.P., Germaine K., RA Martinez-Granero F., Barahona E., Navazo A., Sanchez-Contreras M., RA Moynihan J.A., Giddens S.R., Coppoolse E.R., Muriel C., Stiekema W.J., RA Rainey P.B., Dowling D., O'Gara F., Martin M., Rivilla R.; RT "Genome Sequence of the Biocontrol Strain Pseudomonas fluorescens RT F113."; RL J. Bacteriol. 194:1273-1274(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003150; AEV64622.1; -; Genomic_DNA. DR RefSeq; YP_005210017.1; NC_016830.1. DR ProteinModelPortal; G8Q816; -. DR EnsemblBacteria; AEV64622; AEV64622; PSF113_4633. DR GeneID; 11832736; -. DR KEGG; pfe:PSF113_4633; -. DR KO; K03574; -. DR BioCyc; PFLU1114970:GJXA-4663-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Transferase. SQ SEQUENCE 314 AA; 33916 MW; 525490D124CD1DBC CRC64; MKRVHVAAAV IRDAAGKILI ARRADTQHQG GLWEFPGGKV EADESVETAL ARELHEELGI VVDAARPLIK VRHDYPDKQV LLDVWEVSAF TGEPHGAEGQ PLAWVTARDL TNHEFPAANQ PIVAAARLPG EYLITPEGLE TPALLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAVG LCAGKAQLML KGPFEWLGDF PSAGWHITAA QLRKHAAAGR PFGKDRWLAA SCHNAEELSL AQQMDVDFVT LSPVQPTQTH PDAQPLGWAE AARLIEGFNR PVYLLGGVGP GERQKAWETG AQGVAGIRAF WPEA // ID G8QGJ4_AZOSU Unreviewed; 215 AA. AC G8QGJ4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dsui_0663; OS Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma OS suillum). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azospira. OX NCBI_TaxID=640081; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-33 / DSM 13638 / PS; RX PubMed=22535943; DOI=10.1128/JB.00124-12; RA Byrne-Bailey K.G., Coates J.D.; RT "Complete Genome Sequence of the Anaerobic Perchlorate-Reducing RT Bacterium Azospira suillum Strain PS."; RL J. Bacteriol. 194:2767-2768(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003153; AEV25073.1; -; Genomic_DNA. DR RefSeq; YP_005026914.1; NC_016616.1. DR EnsemblBacteria; AEV25073; AEV25073; Dsui_0663. DR GeneID; 11543574; -. DR KEGG; dsu:Dsui_0663; -. DR KO; K00788; -. DR BioCyc; AORY640081:GHAS-663-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22471 MW; 8BAF0693FCB345F0 CRC64; MLKRPRPGLY AVTPDGLETP RLLMLAEAAL AAGIPLLQYR DKSGDDARRR EQATALLALC RRHGTRLIIN DDAALAREVD ADGVHLGGED GDLAAARALL GPDKLIGASC YADFARAQAA AAGANYVAFG AMYASPTKPQ APRAPFNLVT RARQELPGVQ VAAIGGITLD NAAPVIAAGA QFVAVITDLF EAPDVTARAA AYQRLFAESA AHELS // ID G8QK28_AZOSU Unreviewed; 315 AA. AC G8QK28; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 17. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Dsui_1059; OS Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma OS suillum). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azospira. OX NCBI_TaxID=640081; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-33 / DSM 13638 / PS; RX PubMed=22535943; DOI=10.1128/JB.00124-12; RA Byrne-Bailey K.G., Coates J.D.; RT "Complete Genome Sequence of the Anaerobic Perchlorate-Reducing RT Bacterium Azospira suillum Strain PS."; RL J. Bacteriol. 194:2767-2768(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003153; AEV25461.1; -; Genomic_DNA. DR RefSeq; YP_005027302.1; NC_016616.1. DR ProteinModelPortal; G8QK28; -. DR EnsemblBacteria; AEV25461; AEV25461; Dsui_1059. DR GeneID; 11543970; -. DR KEGG; dsu:Dsui_1059; -. DR KO; K03574; -. DR BioCyc; AORY640081:GHAS-1059-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34136 MW; 7B6CA8D8C3C2CAB8 CRC64; MSKVVEVSAA VIERNGGQEF LLACRPEGKV YAGYWEFPGG KVEAGESHRQ ALDRELQEEL GITVTAATPW ISRRFVYPHA TVRLKFFRVT AWEGEIAPIE HSAFAWARIG MDAGVEPILP ANGPILRALA LPPLYALTQA EERGVEAEMA RLERALAGGL KLVQVRDKQL PPAVRADFAA RVVALAHAHG ARALLNAPDE ASDTLARRLG ADGIHLPAAR LQTLTARPDF PLVAASCHSP EELALADRLE LDFSVLGPVR PTPSHPEQAG LGWDVFGEWV FDCAQPVYAL GGMTTAELET ARRHGAQGIA LMRGW // ID G8R4D3_OWEHD Unreviewed; 212 AA. AC G8R4D3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 14-MAY-2014, entry version 15. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Oweho_3282; OS Owenweeksia hongkongensis (strain DSM 17368 / JCM 12287 / NRRL OS B-23963). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Cryomorphaceae; Owenweeksia. OX NCBI_TaxID=926562; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17368 / JCM 12287 / NRRL B-23963; RX PubMed=23450211; DOI=10.4056/sigs.3296896; RA Riedel T., Held B., Nolan M., Lucas S., Lapidus A., Tice H., RA Del Rio T.G., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., RA Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Rohde M., Tindall B.J., Detter J.C., RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Genome sequence of the orange-pigmented seawater bacterium RT Owenweeksia hongkongensis type strain (UST20020801(T))."; RL Stand. Genomic Sci. 7:120-130(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003156; AEV34233.1; -; Genomic_DNA. DR RefSeq; YP_004990878.1; NC_016599.1. DR EnsemblBacteria; AEV34233; AEV34233; Oweho_3282. DR GeneID; 11632487; -. DR KEGG; oho:Oweho_3282; -. DR KO; K00788; -. DR OMA; YLVIDPS; -. DR BioCyc; OHON926562:GHWV-3281-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 212 AA; 23728 MW; 39A367D9429ED5F2 CRC64; MRKLEGIYLV IDPSMEEGKL LHKLESAIDG GIDILQIWNH WAKEAKHEDK LYLIDKITAT AAAKNVPVLI NEEWQLLKET NLDGVHFDII PENWTEVRNT IPKEKIIGFT AGNDLERIRW ANENEIDYLS FCAMFPSSSA ISCEIVKPST VLLARQITTL PLFLSGGINP ENLQSLGLLD FQGVAIISGI MSADNPAKKV KEYKTALAEI KK // ID G8RC36_STAAU Unreviewed; 213 AA. AC G8RC36; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=M013TW_2049; OS Staphylococcus aureus subsp. aureus M013. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1118959; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M013; RA Huang T.-W., Liao T.-L., Chen Y.-T., Tsai S.-F., RA Yang Lauderdale T.-L.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M013; RX PubMed=22328755; DOI=10.1128/JB.06666-11; RA Huang T.W., Chen F.J., Miu W.C., Liao T.L., Lin A.C., Huang I.W., RA Wu K.M., Tsai S.F., Chen Y.T., Lauderdale T.L.; RT "Complete Genome Sequence of Staphylococcus aureus M013, a pvl- RT Positive, ST59-SCCmec Type V Strain Isolated in Taiwan."; RL J. Bacteriol. 194:1256-1257(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003166; AEV79054.1; -; Genomic_DNA. DR RefSeq; YP_005298429.1; NC_016928.1. DR EnsemblBacteria; AEV79054; AEV79054; M013TW_2049. DR GeneID; 11863393; -. DR KEGG; suu:M013TW_2049; -. DR KO; K00788; -. DR BioCyc; SAUR1118959:GJUR-2027-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23374 MW; 8304F05AA899AE8D CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GKDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID G8RX29_MYCRN Unreviewed; 223 AA. AC G8RX29; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MycrhN_1263; OS Mycobacterium rhodesiae (strain NBB3). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=710685; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBB3; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., RA Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.; RT "Complete sequence of Mycobacterium rhodesiae NBB3."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003169; AEV71886.1; -; Genomic_DNA. DR RefSeq; YP_004999101.1; NC_016604.1. DR EnsemblBacteria; AEV71886; AEV71886; MycrhN_1263. DR GeneID; 11642464; -. DR KEGG; mrh:MycrhN_1263; -. DR KO; K00788; -. DR BioCyc; MRHO710685:GI37-1261-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23400 MW; E54426C9B090E7AB CRC64; MPHPRERLAT ASLYLCTDAR RERGDLAQFA EAALAGGVDI IQLRDKGSPG EQQYGPLEAR AELEALAVLA DAARRHDALL AVNDRADIAL AAGADVLHLG QDDLPLTIAR DVIGARPVLG RSTHDEAQVR TAIDEDVDYF CVGPCWPTPT KPGRPAPGLG LVRMAAQSGT SKPWFAIGGI DSARLGQVIE AGARRVVVVR AVTAADDPAS AARSLKDALS AAC // ID G8SH63_ACTS5 Unreviewed; 194 AA. AC G8SH63; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ACPL_817; OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Actinoplanes. OX NCBI_TaxID=134676; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110; RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K., RA Wehmeier U.F., Stoye J., Puehler A.; RT "The complete genome sequence of the acarbose producer Actinoplanes RT sp. SE50/110."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003170; AEV81714.1; -; Genomic_DNA. DR RefSeq; YP_006263782.1; NC_017803.1. DR EnsemblBacteria; AEV81714; AEV81714; ACPL_817. DR GeneID; 12821632; -. DR KEGG; ase:ACPL_817; -. DR KO; K00788; -. DR OMA; PRLHVIT; -. DR BioCyc; ASP134676:GL7H-723-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 30 34 HMP-PP binding (By similarity). FT REGION 126 128 THZ-P binding (By similarity). FT METAL 62 62 Magnesium (By similarity). FT METAL 81 81 Magnesium (By similarity). FT BINDING 61 61 HMP-PP (By similarity). FT BINDING 100 100 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 194 AA; 19221 MW; 75F844742415B1D9 CRC64; MGAVSFPRLH VITDDLDVVR AVAQPGVAVQ IRVKTNDFAA YAVAREAVPR CRTAGALCLV NDRIGVALAT GADGVHLGAD DLPVAAARRV LGPEAVIGAT CRTPEAARAA VADGATYLGV GPAFPTSTKD GLPPPLGPDG VNAVAAAVPG IPVVAIGGIT LERVGLLTTY GVAAVKAFDG DPAGAAAAFL AALQ // ID G8SH67_ACTS5 Unreviewed; 202 AA. AC G8SH67; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 14-MAY-2014, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=ACPL_821; OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Actinoplanes. OX NCBI_TaxID=134676; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110; RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K., RA Wehmeier U.F., Stoye J., Puehler A.; RT "The complete genome sequence of the acarbose producer Actinoplanes RT sp. SE50/110."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003170; AEV81718.1; -; Genomic_DNA. DR RefSeq; YP_006263786.1; NC_017803.1. DR EnsemblBacteria; AEV81718; AEV81718; ACPL_821. DR GeneID; 12821636; -. DR KEGG; ase:ACPL_821; -. DR KO; K00788; -. DR OMA; VMRAEDP; -. DR BioCyc; ASP134676:GL7H-727-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 202 AA; 19958 MW; 21FA45C6195C587E CRC64; MVTPTGLVVL TDRRSAAGPL VETVAAAVRG GAGWVILRER DLPYGDRAAL AAQLRAVVPP GRLIVAGPDP LGGAAVHLAA ADPRPGGVPL VGRSWHGTEP VSEVDYVTLS PIFPTATKPG YGPDLGVDRA ARLAAGMPWL ALGGVDSAAR AASCATAGAD GVAVLGAIMR AANPERVARV LAGAFAAAAA GSPAAADLGG VR // ID G8SRR2_BRUCA Unreviewed; 221 AA. AC G8SRR2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BCA52141_I2463; OS Brucella canis HSK A52141. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1104321; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A52141; RA Kim J.-S., Jeong W., Kim H., Baek J.-H., Vinuselvi P., Lee S.K., RA Kim J.W., Kim J.-Y., Jung S.C., Her M., An D.-J.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A52141; RX PubMed=22933762; DOI=10.1128/JB.01125-12; RA Kim J.S., Jeong W., Jeoung H.Y., Song J.Y., Kim H., Beak J.H., RA Parisutham V., Lee S.K., Kim J.W., Kim J.Y., Jung S.C., Her M., RA An D.J.; RT "Complete Genome Sequence of Brucella canis Strain HSK A52141, RT Isolated from the Blood of an Infected Dog."; RL J. Bacteriol. 194:5134-5134(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003174; AEW14550.1; -; Genomic_DNA. DR RefSeq; YP_005116127.1; NC_016778.1. DR ProteinModelPortal; G8SRR2; -. DR EnsemblBacteria; AEW14550; AEW14550; BCA52141_I2463. DR GeneID; 11683909; -. DR KEGG; bsk:BCA52141_I2463; -. DR KO; K00788; -. DR BioCyc; BCAN1104321:GJV1-1539-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID G8STF7_BRUCA Unreviewed; 203 AA. AC G8STF7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BCA52141_I1346; OS Brucella canis HSK A52141. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1104321; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A52141; RA Kim J.-S., Jeong W., Kim H., Baek J.-H., Vinuselvi P., Lee S.K., RA Kim J.W., Kim J.-Y., Jung S.C., Her M., An D.-J.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A52141; RX PubMed=22933762; DOI=10.1128/JB.01125-12; RA Kim J.S., Jeong W., Jeoung H.Y., Song J.Y., Kim H., Beak J.H., RA Parisutham V., Lee S.K., Kim J.W., Kim J.Y., Jung S.C., Her M., RA An D.J.; RT "Complete Genome Sequence of Brucella canis Strain HSK A52141, RT Isolated from the Blood of an Infected Dog."; RL J. Bacteriol. 194:5134-5134(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003174; AEW13877.1; -; Genomic_DNA. DR RefSeq; YP_005115454.1; NC_016778.1. DR ProteinModelPortal; G8STF7; -. DR EnsemblBacteria; AEW13877; AEW13877; BCA52141_I1346. DR GeneID; 11683236; -. DR KEGG; bsk:BCA52141_I1346; -. DR KO; K00788; -. DR BioCyc; BCAN1104321:GJV1-854-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID G8SXJ2_BRUAO Unreviewed; 221 AA. AC G8SXJ2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAA13334_I01249; OS Brucella abortus A13334. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1104320; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A13334; RX PubMed=22965076; DOI=10.1128/JB.01124-12; RA Kim H., Jeong W., Jeoung H.Y., Song J.Y., Kim J.S., Beak J.H., RA Parisutham V., Lee S.K., Kim J.W., Kim J.Y., Jung S.C., Her M., RA An D.J.; RT "Complete Genome Sequence of Brucella abortus A13334, a New Strain RT Isolated from the Fetal Gastric Fluid of Dairy Cattle."; RL J. Bacteriol. 194:5444-5444(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003176; AEW17143.1; -; Genomic_DNA. DR RefSeq; YP_005151145.1; NC_016795.1. DR ProteinModelPortal; G8SXJ2; -. DR EnsemblBacteria; AEW17143; AEW17143; BAA13334_I01249. DR GeneID; 11724284; -. DR KEGG; baa:BAA13334_I01249; -. DR KO; K00788; -. DR BioCyc; BABO1104320:GKD4-785-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID G8SZI4_BRUAO Unreviewed; 203 AA. AC G8SZI4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=BAA13334_I00119; OS Brucella abortus A13334. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1104320; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A13334; RX PubMed=22965076; DOI=10.1128/JB.01124-12; RA Kim H., Jeong W., Jeoung H.Y., Song J.Y., Kim J.S., Beak J.H., RA Parisutham V., Lee S.K., Kim J.W., Kim J.Y., Jung S.C., Her M., RA An D.J.; RT "Complete Genome Sequence of Brucella abortus A13334, a New Strain RT Isolated from the Fetal Gastric Fluid of Dairy Cattle."; RL J. Bacteriol. 194:5444-5444(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003176; AEW16450.1; -; Genomic_DNA. DR RefSeq; YP_005150452.1; NC_016795.1. DR ProteinModelPortal; G8SZI4; -. DR EnsemblBacteria; AEW16450; AEW16450; BAA13334_I00119. DR GeneID; 11725425; -. DR KEGG; baa:BAA13334_I00119; -. DR KO; K00788; -. DR BioCyc; BABO1104320:GKD4-80-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID G8TNF7_NIAKG Unreviewed; 207 AA. AC G8TNF7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 14-MAY-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Niako_3574; OS Niastella koreensis (strain DSM 17620 / KACC 11465 / GR20-10). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Chitinophagaceae; Niastella. OX NCBI_TaxID=700598; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17620 / KACC 11465 / GR20-10; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Davenport K., Saunders E., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Niastella koreensis GR20-10."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003178; AEV99874.1; -; Genomic_DNA. DR RefSeq; YP_005009278.1; NC_016609.1. DR EnsemblBacteria; AEV99874; AEV99874; Niako_3574. DR GeneID; 11652099; -. DR KEGG; nko:Niako_3574; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR BioCyc; NKOR700598:GHC3-3609-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22660 MW; 5F9E418EDC6C1F49 CRC64; MLERVYFISQ QTAAKTHVTA IEEALEAGCK LVQLRVKNQP ETVVLELAKV AKTLCDRFNA KLIINDYPLV ARSVNAWGVH VGLQDMAVRD VRAIVGRDMI VGGTANTFEH IQQRILEGVD YVGLGPFRFT TTKEKLSPVL GLEGYQRIMD RMRATAYYTP IVAIGGILPD DVPGLRDAGV YGVAVSGALT NAVDQKAQVE KINALYS // ID G8TNF9_NIAKG Unreviewed; 202 AA. AC G8TNF9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Niako_3576; OS Niastella koreensis (strain DSM 17620 / KACC 11465 / GR20-10). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Chitinophagaceae; Niastella. OX NCBI_TaxID=700598; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17620 / KACC 11465 / GR20-10; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Davenport K., Saunders E., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Niastella koreensis GR20-10."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003178; AEV99876.1; -; Genomic_DNA. DR RefSeq; YP_005009280.1; NC_016609.1. DR EnsemblBacteria; AEV99876; AEV99876; Niako_3576. DR GeneID; 11652101; -. DR KEGG; nko:Niako_3576; -. DR KO; K00788; -. DR OMA; ANAVENF; -. DR BioCyc; NKOR700598:GHC3-3611-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 23060 MW; CB33A45471A52A21 CRC64; MFSIVVISHA AAVPNEAAII QQLFAEGLEV FHLRKPEGDE QSVRQLIEAI PAKYHNRIAM HGFFHLMNEY NIHRLHFREE HRQETSKEEM VQLKNKGYTL STSVHDLPTL QRLTSLFSYA FFSPVFDSIS KQQYKGFADD DFYLREEQKP ISVIALGGVD AGNIQSTMAM NFDGVALLGA IWKEPANAVE NFKLCKQHVQ TY // ID G8TVV1_SULAD Unreviewed; 208 AA. AC G8TVV1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 14-MAY-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sulac_1298; OS Sulfobacillus acidophilus (strain ATCC 700253 / DSM 10332 / NAL). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus. OX NCBI_TaxID=679936; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700253 / DSM 10332 / NAL; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Chertkov O., Saunders E., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Pukall R., Gehrich-Schroeter G., Schneider S., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of chromosome of Sulfobacillus acidophilus DSM RT 10332."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003179; AEW04795.1; -; Genomic_DNA. DR RefSeq; YP_005256467.1; NC_016884.1. DR EnsemblBacteria; AEW04795; AEW04795; Sulac_1298. DR GeneID; 11858061; -. DR KEGG; sap:Sulac_1298; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; SACI679936:GHYT-1335-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22249 MW; 6932165FC40C3BEA CRC64; MDLRLMVIID PRQVPVDQLG GFCREVRQGG ATVIQLRGKI RSTRELVTYG RALRVETRRH GLSLIVNDRT DVALAIQADG VHVGQEDMPV RDVRRMAPGL TVGLSVSASE EIPAQPADWP DYFGVGPVYA TSSKDDAGDP LGVEGLRSLW QECRRIAPVV AIGGITPANV GPLWQLPVAG VAVISAVVNA PDKALACRQL ITGKEISG // ID G8TVV4_SULAD Unreviewed; 213 AA. AC G8TVV4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Sulac_1301; OS Sulfobacillus acidophilus (strain ATCC 700253 / DSM 10332 / NAL). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus. OX NCBI_TaxID=679936; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700253 / DSM 10332 / NAL; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Chertkov O., Saunders E., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Pukall R., Gehrich-Schroeter G., Schneider S., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of chromosome of Sulfobacillus acidophilus DSM RT 10332."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003179; AEW04798.1; -; Genomic_DNA. DR RefSeq; YP_005256470.1; NC_016884.1. DR EnsemblBacteria; AEW04798; AEW04798; Sulac_1301. DR GeneID; 11858064; -. DR KEGG; sap:Sulac_1301; -. DR OMA; PCPVIAI; -. DR BioCyc; SACI679936:GHYT-1338-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 213 AA; 23752 MW; E815ED720321A86F CRC64; MIWGLIDAAR FEEPQWAWLP KVAPYLDGVW LRAPTFTLEE WLDWGRRIRG SAPQIPLWVG HLAAATALDA EGVQVSSTGP AAAWLKKRWT RSVAASVHHV AEARYHDAAD VWIWGHAFET RSKPGLAPRP RTHLMELLAE PARPPVLVVG GITVETVGEV AGWGVQGLVV GDGIWRTLAP AEASRKIRQI WDERREKPSY PVSKEGMRFD GFD // ID G8U250_BACCE Unreviewed; 219 AA. AC G8U250; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=bcf_02130; OS Bacillus cereus F837/76. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=347495; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F837/76; RX PubMed=22374959; DOI=10.1128/JB.06719-11; RA Auger S., Galleron N., Segurens B., Dossat C., Bolotin A., Wincker P., RA Sorokin A.; RT "Complete Genome Sequence of the Highly Hemolytic Strain Bacillus RT cereus F837/76."; RL J. Bacteriol. 194:1630-1630(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003187; AEW53591.1; -; Genomic_DNA. DR RefSeq; YP_005117104.1; NC_016779.1. DR ProteinModelPortal; G8U250; -. DR EnsemblBacteria; AEW53591; AEW53591; bcf_02130. DR GeneID; 11677577; -. DR KEGG; bcf:bcf_02130; -. DR KO; K00788; -. DR BioCyc; BCER347495:GHGC-426-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23482 MW; D33A0EEF285CFD9C CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID G8UFH7_BACCE Unreviewed; 206 AA. AC G8UFH7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=bcf_03845; OS Bacillus cereus F837/76. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=347495; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F837/76; RX PubMed=22374959; DOI=10.1128/JB.06719-11; RA Auger S., Galleron N., Segurens B., Dossat C., Bolotin A., Wincker P., RA Sorokin A.; RT "Complete Genome Sequence of the Highly Hemolytic Strain Bacillus RT cereus F837/76."; RL J. Bacteriol. 194:1630-1630(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003187; AEW53892.1; -; Genomic_DNA. DR RefSeq; YP_005117405.1; NC_016779.1. DR EnsemblBacteria; AEW53892; AEW53892; bcf_03845. DR GeneID; 11678244; -. DR KEGG; bcf:bcf_03845; -. DR KO; K10810; -. DR BioCyc; BCER347495:GHGC-769-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 206 AA; 22964 MW; B9CBA35D10713F7A CRC64; MKNELHVISN GNMSFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPPSK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTDC KKDVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID G8UTH3_LEGPN Unreviewed; 495 AA. AC G8UTH3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 18. DE SubName: Full=Phosphomethylpyrimidine kinase ThiD/thiamin-phosphate pyrophosphorylase fused protein ThiE; GN ORFNames=lp12_1506; OS Legionella pneumophila subsp. pneumophila ATCC 43290. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=933093; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43290; RX PubMed=22374950; DOI=10.1128/JB.06626-11; RA Amaro F., Gilbert J.A., Owens S., Trimble W., Shuman H.A.; RT "Whole-Genome Sequence of the Human Pathogen Legionella pneumophila RT Serogroup 12 Strain 570-CO-H."; RL J. Bacteriol. 194:1613-1614(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003192; AEW51771.1; -; Genomic_DNA. DR RefSeq; YP_005185870.1; NC_016811.1. DR ProteinModelPortal; G8UTH3; -. DR EnsemblBacteria; AEW51771; AEW51771; lp12_1506. DR GeneID; 11802684; -. DR KEGG; lpe:lp12_1506; -. DR KO; K14153; -. DR BioCyc; LPNE933093:GH6R-1495-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 495 AA; 55081 MW; 69C8A29273F3E689 CRC64; MASGKQFMKK PIVWTIAGVD SSGLAGVHAD METFSRLNVR ACSVITAVTA QNAHSIIAVE EISRDQVAAQ CRALELNLKP DAIKIGMLCS TPICEEIAYF LKGYEGFVVL DPIITSSSGT NLFFPDLQQH KNNLIQLFPY ITIITPNRIE AEIILNRSIY SYQDIINAAS DLLSLGAKQV LLKGGHVKDN SFSQDYWTDG KESFWIANRR FPETNYRGTG CVLSSALTAC LALGYSIKDA IVIAKMYVNR GIRQSIEIDK DASQLYHDGW PEDEADLPYL SPTPFIKPVP SFKKYSMGFY PIVDSSHWLE MLLPLGIKCI QLRIKEASQE RLEEEIKRSV HLANQYNAAL FINDHWELAI HYGAAGVHLG QEDLEKADVD RINRSGLFLG ISTHCYYEVA RAHALNPSYV ACGPIYETTS KIMPFQAQGI ARLERWRKTL RYPLVAIGGI TLKNLSDVLK TKIDGVSVIS AITKASAPLV AAKQFLTQMN ESHNE // ID G8V3P4_STAAU Unreviewed; 213 AA. AC G8V3P4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MS7_2107; OS Staphylococcus aureus subsp. aureus 11819-97. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1123523; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=11819-97; RX PubMed=22374956; DOI=10.1128/JB.06653-11; RA Stegger M., Price L.B., Larsen A.R., Gillece J.D., Waters A.E., RA Skov R., Andersen P.S.; RT "Genome Sequence of Staphylococcus aureus Strain 11819-97, an ST80-IV RT European Community-Acquired Methicillin-Resistant Isolate."; RL J. Bacteriol. 194:1625-1626(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003194; AEW66070.1; -; Genomic_DNA. DR RefSeq; YP_005758502.1; NC_017351.1. DR ProteinModelPortal; G8V3P4; -. DR EnsemblBacteria; AEW66070; AEW66070; MS7_2107. DR GeneID; 12424894; -. DR KEGG; suz:MS7_2107; -. DR KO; K00788; -. DR BioCyc; SAUR1123523:GLKH-2103-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23428 MW; 72CEFFE40BF6349B CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLET ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PKMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID G8V857_PROAA Unreviewed; 216 AA. AC G8V857; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TIA2EST2_04335; OS Propionibacterium acnes TypeIA2 P.acn33. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1114966; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P.acn33; RX PubMed=22374954; DOI=10.1128/JB.06758-11; RA Voros A., Horvath B., Hunyadkurti J., McDowell A., Barnard E., RA Patrick S., Nagy I.; RT "Complete Genome Sequences of Three Propionibacterium acnes Isolates RT from the Type IA2 Cluster."; RL J. Bacteriol. 194:1621-1622(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003195; AEW78960.1; -; Genomic_DNA. DR RefSeq; YP_004955323.1; NC_016516.1. DR ProteinModelPortal; G8V857; -. DR EnsemblBacteria; AEW78960; AEW78960; TIA2EST2_04335. DR GeneID; 11492579; -. DR KEGG; paz:TIA2EST2_04335; -. DR KO; K00788; -. DR BioCyc; PACN1114966:GJX4-857-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID G8V8Z8_PROAA Unreviewed; 217 AA. AC G8V8Z8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TIA2EST2_00550; OS Propionibacterium acnes TypeIA2 P.acn33. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1114966; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P.acn33; RX PubMed=22374954; DOI=10.1128/JB.06758-11; RA Voros A., Horvath B., Hunyadkurti J., McDowell A., Barnard E., RA Patrick S., Nagy I.; RT "Complete Genome Sequences of Three Propionibacterium acnes Isolates RT from the Type IA2 Cluster."; RL J. Bacteriol. 194:1621-1622(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003195; AEW78223.1; -; Genomic_DNA. DR RefSeq; YP_004954586.1; NC_016516.1. DR EnsemblBacteria; AEW78223; AEW78223; TIA2EST2_00550. DR GeneID; 11491830; -. DR KEGG; paz:TIA2EST2_00550; -. DR KO; K00788; -. DR BioCyc; PACN1114966:GJX4-107-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22432 MW; 973D828880F0910F CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAIRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID G8VDP2_PROAA Unreviewed; 217 AA. AC G8VDP2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TIA2EST22_00550; OS Propionibacterium acnes TypeIA2 P.acn17. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1114967; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P.acn17; RX PubMed=22374954; DOI=10.1128/JB.06758-11; RA Voros A., Horvath B., Hunyadkurti J., McDowell A., Barnard E., RA Patrick S., Nagy I.; RT "Complete Genome Sequences of Three Propionibacterium acnes Isolates RT from the Type IA2 Cluster."; RL J. Bacteriol. 194:1621-1622(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003196; AEW80458.1; -; Genomic_DNA. DR RefSeq; YP_004945648.1; NC_016512.1. DR ProteinModelPortal; G8VDP2; -. DR EnsemblBacteria; AEW80458; AEW80458; TIA2EST22_00550. DR GeneID; 11482269; -. DR KEGG; pav:TIA2EST22_00550; -. DR KO; K00788; -. DR BioCyc; PACN1114967:GJTL-109-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID G8VGI5_PROAA Unreviewed; 216 AA. AC G8VGI5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TIA2EST22_04415; OS Propionibacterium acnes TypeIA2 P.acn17. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1114967; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P.acn17; RX PubMed=22374954; DOI=10.1128/JB.06758-11; RA Voros A., Horvath B., Hunyadkurti J., McDowell A., Barnard E., RA Patrick S., Nagy I.; RT "Complete Genome Sequences of Three Propionibacterium acnes Isolates RT from the Type IA2 Cluster."; RL J. Bacteriol. 194:1621-1622(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003196; AEW81203.1; -; Genomic_DNA. DR RefSeq; YP_004946393.1; NC_016512.1. DR EnsemblBacteria; AEW81203; AEW81203; TIA2EST22_04415. DR GeneID; 11482564; -. DR KEGG; pav:TIA2EST22_04415; -. DR KO; K00788; -. DR BioCyc; PACN1114967:GJTL-867-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22572 MW; 68DE5AAB2FB1D32B CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVVTVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID G8VPP4_PROAA Unreviewed; 217 AA. AC G8VPP4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TIA2EST36_00570; OS Propionibacterium acnes TypeIA2 P.acn31. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1114969; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P.acn31; RX PubMed=22374954; DOI=10.1128/JB.06758-11; RA Voros A., Horvath B., Hunyadkurti J., McDowell A., Barnard E., RA Patrick S., Nagy I.; RT "Complete Genome Sequences of Three Propionibacterium acnes Isolates RT from the Type IA2 Cluster."; RL J. Bacteriol. 194:1621-1622(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003197; AEW82721.1; -; Genomic_DNA. DR RefSeq; YP_004943404.1; NC_016511.1. DR ProteinModelPortal; G8VPP4; -. DR EnsemblBacteria; AEW82721; AEW82721; TIA2EST36_00570. DR GeneID; 11480820; -. DR KEGG; pax:TIA2EST36_00570; -. DR KO; K00788; -. DR BioCyc; PACN1114969:GJUU-109-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID G8VQW8_PROAA Unreviewed; 216 AA. AC G8VQW8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TIA2EST36_04385; OS Propionibacterium acnes TypeIA2 P.acn31. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1114969; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P.acn31; RX PubMed=22374954; DOI=10.1128/JB.06758-11; RA Voros A., Horvath B., Hunyadkurti J., McDowell A., Barnard E., RA Patrick S., Nagy I.; RT "Complete Genome Sequences of Three Propionibacterium acnes Isolates RT from the Type IA2 Cluster."; RL J. Bacteriol. 194:1621-1622(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003197; AEW83467.1; -; Genomic_DNA. DR RefSeq; YP_004944150.1; NC_016511.1. DR ProteinModelPortal; G8VQW8; -. DR EnsemblBacteria; AEW83467; AEW83467; TIA2EST36_04385. DR GeneID; 11480117; -. DR KEGG; pax:TIA2EST36_04385; -. DR KO; K00788; -. DR BioCyc; PACN1114969:GJUU-868-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 141 143 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22602 MW; D04F0C7B366B1021 CRC64; MSRPEFDLSV YLVTDTAQCG GPDEVVETVR HAIAGGVTLV QFRDHDLSDD EFVALGRRVR EICVSGGVPL IIDDRVHLVA EIGADGVHVG QSDMPVDQAR AILGDDLLIG LSAQTPAHVE AALSQGRDIV DYLGVGALHG TGTKPEAGEL GLAEIRDVVN ASPWPVCVIG GVSASDAQDV ARVGCDGLSV VSAICRSTDP KSSARELAEA WRTAKE // ID G8W667_KLEPH Unreviewed; 211 AA. AC G8W667; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=KPHS_02120; OS Klebsiella pneumoniae subsp. pneumoniae (strain HS11286). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=1125630; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HS11286; RX PubMed=22408243; DOI=10.1128/JB.00043-12; RA Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K., RA Ou H.Y.; RT "Complete Genome Sequence of Klebsiella pneumoniae subsp. pneumoniae RT HS11286, a Multidrug-Resistant Strain Isolated from Human Sputum."; RL J. Bacteriol. 194:1841-1842(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003200; AEW58910.1; -; Genomic_DNA. DR RefSeq; YP_005224512.1; NC_016845.1. DR ProteinModelPortal; G8W667; -. DR EnsemblBacteria; AEW58910; AEW58910; KPHS_02120. DR GeneID; 11845196; -. DR KEGG; kpm:KPHS_02120; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; KPNE1125630:GJUV-221-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 21B54D01518D3CB0 CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIERLLE AGVRTLQLRI KDRRDSEVED DVIAAIALGR RYHARLFIND YWQLAIKHQA YGVHLGQEDL ETTDLSAIRQ AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIQRLADYP TVAIGGISLE KAPGVLATGV GSIAVVSAIT QAADWRAATD QLLALAGAGD E // ID G8WEC8_KLEOK Unreviewed; 211 AA. AC G8WEC8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=KOX_07960; OS Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC OS 3318 / NRRL B-199 / KCTC 1686). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=1006551; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / RC KCTC 1686; RA Shin S.H., Kim S., Kim J.Y., Yang K.-S., Seo J.-S.; RT "Complete genome sequence of Klebsiella oxytoca strain KCTC 1686."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003218; AEX03320.1; -; Genomic_DNA. DR RefSeq; YP_005017559.1; NC_016612.1. DR EnsemblBacteria; AEX03320; AEX03320; KOX_07960. DR GeneID; 11663536; -. DR KEGG; kox:KOX_07960; -. DR KO; K00788; -. DR BioCyc; KOXY1006551:GH6O-1621-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23070 MW; A1CD226493FFF341 CRC64; MYQPDFPSVP FRLGLYPVVD SVTWIERLLA AGVRTLQLRI KDKRDSEVEE HVVAAIALGR KYHARLFIND YWRLAIKHQA YGVHLGQEDL ETTDLSAIRN AGLRLGVSTH DDMEIDIALA ARPSYIALGH VFPTQTKQMP SAPQGLDQLA QHIQRLGDYP TVAIGGISLE RAPAVLATGV GSVAVVSAIT QAADWRQATV RLLEIAGAGD E // ID G8X9N6_FLACA Unreviewed; 190 AA. AC G8X9N6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN OrderedLocusNames=FCOL_08950; OS Flavobacterium columnare (strain ATCC 49512 / CIP 103533 / TG 44/87). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1041826; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49512 / CIP 103533 / TG 44/87; RA Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D., Benton N.R., RA Zaitshik J., Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., RA Waldbieser G.C., Lawrence M.L.; RT "Complete genome sequence of Flavobacterium columnare ATCC 49512."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003222; AEW86599.1; -; Genomic_DNA. DR RefSeq; YP_004942392.1; NC_016510.2. DR EnsemblBacteria; AEW86599; AEW86599; FCOL_08950. DR GeneID; 11476876; -. DR KEGG; fco:FCOL_08950; -. DR KO; K00788; -. DR BioCyc; FCOL1041826:GHZN-1820-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 190 AA; 21960 MW; AFBF54D1B66BB420 CRC64; MILLSTEHTI ENEIQTLHQL FDAGLTHFHI RKPNYTLQET KAYLEKIDTY FHPFCVVYYP ELVNEYDLKG IHQTSQNRNS IVKNTKSLST STHSITEFNE LDSAYHYAFL SPVFPSISKV NYQNPEILHQ IAQRTNFNTQ LIALGGISEK NISEVLLYFN SVALLGAIWL HPNPIEQWKK CQNIVLSYSV // ID G8X9N8_FLACA Unreviewed; 210 AA. AC G8X9N8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=FCOL_08960; OS Flavobacterium columnare (strain ATCC 49512 / CIP 103533 / TG 44/87). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1041826; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49512 / CIP 103533 / TG 44/87; RA Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D., Benton N.R., RA Zaitshik J., Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., RA Waldbieser G.C., Lawrence M.L.; RT "Complete genome sequence of Flavobacterium columnare ATCC 49512."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003222; AEW86601.1; -; Genomic_DNA. DR RefSeq; YP_004942394.1; NC_016510.2. DR EnsemblBacteria; AEW86601; AEW86601; FCOL_08960. DR GeneID; 11476878; -. DR KEGG; fco:FCOL_08960; -. DR KO; K00788; -. DR BioCyc; FCOL1041826:GHZN-1822-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22988 MW; 9BA6F3DC152D13DD CRC64; MLPKIQFISQ GATPEKQLNS IRKALDAGIT WTQLRYKNAS KIDVFRLAEK VKKETDQYNA LLTINDFPTI AKAIDAHGLH LGLTDGSIDQ ARELLGNVKI IGGTANTLED VQQRLAERCD YLGLGPLRFT TTKEKLSPPL GFEGYKKIIN TSSNTALVKP IFAIGGIVEN DLPKLVEIGV YGIAVSGLIC NATQPSQIVK QLNETLYTYA // ID G8Y6F0_PICSO Unreviewed; 530 AA. AC G8Y6F0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-APR-2014, entry version 14. DE SubName: Full=Piso0_003721 protein; GN Name=Piso0_003721; GN ORFNames=GNLVRS01_PISO0K01110g, GNLVRS01_PISO0L01111g; OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / OS NBRC 10061 / NRRL Y-12695) (Hybrid yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Millerozyma. OX NCBI_TaxID=559304; RN [1] RP NUCLEOTIDE SEQUENCE. RA Genoscope - CEA; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL RC Y-12695; RX DOI=10.1534/g3.111.001032; RA Wendland J., Walther A.; RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps RT of genome resolution following polyploidization."; RL G3 (Bethesda) 2:299-311(2012). RN [3] RP NUCLEOTIDE SEQUENCE. RX DOI=10.1534/g3.111.000745; RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P., RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A., RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S., RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., RA Mallet S., Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., RA Seret M.L., Talla E., Samson G., Jubin C., Poulain J., Vacherie B., RA Barbe V., Pelletier E., Sherman D.J., Westhof E., Weissenbach J., RA Baret P.V., Wincker P., Gaillardin C., Dujon B., Souciet J.L.; RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps RT of genome resolution following polyploidization."; RL Genetics 0:0-0(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO082049; CCE83149.1; -; Genomic_DNA. DR EMBL; FO082048; CCE84180.1; -; Genomic_DNA. DR RefSeq; XP_004196499.1; XM_004196451.1. DR RefSeq; XP_004197530.1; XM_004197482.1. DR GeneID; 14519504; -. DR GeneID; 14520569; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 530 AA; 57474 MW; 84C36DC1993C046A CRC64; MSSTEYLRLY LVTDSSMVPE GLSFEEQVEK ALDGGATCVQ LREKKLSTRD FIERAKAVHQ KCQAKGVPLI INDRIDVALA IDAEGVHVGQ DDMPAKKARE ILGEKKIIGV SCSTVSEIEE VCEEGIADYV GLGNVYQTNT KKDVKTPNGI GPIGVRKMLH VLQDNSEKYI GSVAIGGINH SNSSKLMYQT AINGRSLDGV AVVSCIMASK EAEKATRKLS ECLSTRATWT SDISNDMITT DLDKQINHLV SNKPLIHHIT NNVVKNYSAN VALSIGASPI MSEFPEEFKD FTTNITNLSL VLNLGTPSVD QMHIFKKALY VYNEDGKHII FDPVAAGATS PRLESCLELL NSGQFSVIKG NLGEIAAIWR LCSNYKNKNA QNDVLMHGVD SVTTLSKDAI IKIGTEVAID FRTVVVITGA TNYIFNGFST YKDTGYHFSN MDTLQYTTVP GGHELMGSIT GTGCSLGTTI AAFVAAKADG RAQKSVNVYQ ATVAAVTLYN KCGKAAGNES KSPGTFMTKF LDHLYLETHK // ID G8ZVY9_TORDC Unreviewed; 539 AA. AC G8ZVY9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-APR-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN Name=TDEL0E05400; ORFNames=TDEL_0E05400; OS Torulaspora delbrueckii (strain ATCC 10662 / CBS 1146 / NBRC 0425 / OS NCYC 2629 / NRRL Y-866) (Yeast) (Candida colliculosa). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Torulaspora. OX NCBI_TaxID=1076872; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10662 / CBS 1146 / NBRC 0425 / NCYC 2629 / NRRL Y-866; RX PubMed=22123960; DOI=10.1073/pnas.1112808108; RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., RA Byrne K.P., Wolfe K.H.; RT "Evolutionary erosion of yeast sex chromosomes by mating-type RT switching accidents."; RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE616746; CCE92783.1; -; Genomic_DNA. DR RefSeq; XP_003681994.1; XM_003681946.1. DR GeneID; 11500983; -. DR KEGG; tdl:TDEL_0E05400; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 539 AA; 58286 MW; 31EDB1C34B8DD7A4 CRC64; MVFDKQKVDY SLYLVTDSSM LPDGTTLYSQ VEAGLKNGVT LVQLREKDCE TKDFIAEALE VQKLCKKFNV PLIINDRIDV ALAIDADGVH VGQDDIPIPM VRKLVGPDRI VGWSVGFREE VETLAKWGPD MVDYIGVGTL FPTLTKKNPK KAPMGPQGAI KVLDALEEFG ANWCRTVGIG GLHPVNIGRV LFQCVSSNGK RALDGICVVS DIMAAKDAGA ATKNLRRIID QGNYHFVNLQ LKNSAITQET FKSVLGQVAL TRPLVQHVTN KVHQNFGANI TLALGSSPIM SEVKDEVHEL ARIPNATLLL NTGSVAPVDM LKEAITCYNN EQRPIIFDPV GYSATETRRL LNDTLLSHGQ FTCIKGNTSE ILSLAKLTVE KMKGVDAFVG NVDEEMLSRA TRIVAYTYKT VAVCSGETDF VADGTENGHF TLSNGPVKTA IDLPCVKINN GPISIMGDIT ASGCSLGSTI ACCLGGANAE SNVFDAVVTA VILYKTAGKL ASTRCQGSGS FHVQLIDALY ELFHANEPAR WTASYRMLN // ID G9A0D3_RHIFH Unreviewed; 217 AA. AC G9A0D3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 11-DEC-2013, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=SFHH103_02837; OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=1117943; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH103; RX PubMed=22374952; DOI=10.1128/JB.06729-11; RA Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., RA Margaret I., Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., RA Szczepanowski R., Vinardell J.M., Zehner S., Gottfert M.; RT "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103."; RL J. Bacteriol. 194:1617-1618(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE616890; CCE97329.1; -; Genomic_DNA. DR RefSeq; YP_005190154.1; NC_016812.1. DR EnsemblBacteria; CCE97329; CCE97329; SFHH103_02837. DR GeneID; 11814837; -. DR KEGG; sfh:SFHH103_02837; -. DR KO; K00788; -. DR BioCyc; SFRE1117943:GJT5-2874-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 217 AA; 22822 MW; 22863D1E50B8B3A8 CRC64; MSNTDNRCRL VLIAPDLPDI AECAKALADA LKGGDVASVI VPQYSLNETD FQRRAEALVP VIQQAGAAAL IEGDTRVAGR AKADGLHIAA GADVLGEAIE RHTPKMIVGG GNATDRHHAL AIGELRPDYV FFGRTDGDIK PEAHPKNLAL AEWWASMIEI PCIVMGGTDP QSALAVAETG AEFVALRLAV FAEPGQAPSV VAAVNALLDE KAPRFED // ID G9AIQ6_RHIFH Unreviewed; 201 AA. AC G9AIQ6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SFHH103_06479; OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii). OG Plasmid pSfHH103e. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=1117943; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH103; RX PubMed=22374952; DOI=10.1128/JB.06729-11; RA Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., RA Margaret I., Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., RA Szczepanowski R., Vinardell J.M., Zehner S., Gottfert M.; RT "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103."; RL J. Bacteriol. 194:1617-1618(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE616899; CCF00938.1; -; Genomic_DNA. DR RefSeq; YP_005193077.1; NC_016815.1. DR EnsemblBacteria; CCF00938; CCF00938; SFHH103_06479. DR GeneID; 11800666; -. DR KEGG; sfh:SFHH103_06479; -. DR KO; K00788; -. DR BioCyc; SFRE1117943:GJT5-5633-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Plasmid; Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22234 MW; B37EBEE2D1A5ECDD CRC64; MKLDPFYLIV DSARWIERLV PLGVKLVQLR IKEQSDEELR GEIRRAKAVC AAHQCQLIVN DYWRLAIEEA CDFVHLGQED LVGADLGAIR AAGLKLGVST HDDKELETAL AAAPDYVALG PIYPTILKQM KWAPQGLARL STWRERVSPL PLVAIGGLNP ERIDGVFAQG ADSAAVVTDI TLNADPEART QEWIRMTAAR R // ID G9AQC4_PANAN Unreviewed; 210 AA. AC G9AQC4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PANA5342_4207; OS Pantoea ananatis LMG 5342. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=1123863; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 5342; RX PubMed=22374951; DOI=10.1128/JB.06715-11; RA De Maayer P., Chan W.Y., Rezzonico F., Buhlmann A., Venter S.N., RA Blom J., Goesmann A., Frey J.E., Smits T.H., Duffy B., Coutinho T.A.; RT "Complete Genome Sequence of Clinical Isolate Pantoea ananatis LMG RT 5342."; RL J. Bacteriol. 194:1615-1616(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE617160; CCF11600.1; -; Genomic_DNA. DR RefSeq; YP_005197637.1; NC_016816.1. DR ProteinModelPortal; G9AQC4; -. DR EnsemblBacteria; CCF11600; CCF11600; PANA5342_4207. DR GeneID; 11798400; -. DR KEGG; plf:PANA5342_4207; -. DR KO; K00788; -. DR BioCyc; PANA1123863:GJWO-4277-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23041 MW; 58C94673C26E3547 CRC64; MDAFPATASR LGLYPVVDSV EWIERLLEAG VRTLQLRIKD QPDEVVEPMI IRAIAAGKRY QARLFINDYW QLAIKHQAYG VHLGQEDLEV ANLQQILHAG LRLGLSTHDD AELDRALALR PSYVALGHIF PTQTKAMPSS PQGVAELKRH LARLHGISTV AIGGISIDRA PEVLATGVGS IAVVSAITQA EDWQEATRVL LRLAEPETAY // ID G9EAJ0_9GAMM Unreviewed; 210 AA. AC G9EAJ0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=KUC_0993; OS Halomonas boliviensis LC1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1072583; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LC1; RA Quillaguamn J., Guzmn D., Balderrama-Subieta A., Cardona-Ortuo C., RA Guevara-Martnez M., Callisaya-Quispe N.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH393257; EHJ94039.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ94039; EHJ94039; KUC_0993. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 21671 MW; C4CE9095E1189DFD CRC64; MPLDLSLYLV TDAALCGDVG LEQTVEAAVR GGVTIVQLRD KHASDEQMIV QAKRLKAVLA GTGVPLIIND RLQVALESQA DGLHVGQSDA AVQAARRLLG EQAIIGLSIN TIAQLQATPF ELLDYVGIGP VFGTQSKQDH AQPIGFGGLA SLVKACPLPS VAIGGLKASH AISVQRAGAN GLAVISAICG QPDPYQAART FQVFQAASAS // ID G9EI55_9GAMM Unreviewed; 318 AA. AC G9EI55; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=KUC_3810; OS Halomonas boliviensis LC1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1072583; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LC1; RA Quillaguamn J., Guzmn D., Balderrama-Subieta A., Cardona-Ortuo C., RA Guevara-Martnez M., Callisaya-Quispe N.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH393260; EHJ91367.1; -; Genomic_DNA. DR ProteinModelPortal; G9EI55; -. DR EnsemblBacteria; EHJ91367; EHJ91367; KUC_3810. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; SQ SEQUENCE 318 AA; 35737 MW; 91FA3D5889DA8095 CRC64; MSIKVKRRVH VAAAAIISAD QKQVLIARRP SNVDHGGLWE FPGGKLAPYE TGLEGLKREL HEELGVEIVC AQPLIRVHHE YPDKHILLDV WQVHEFAGEP FGREGQAVRW VPMSELSKYP FPAANLPILR AVRLPTEYLI TGEEADEARF DAYLERALRE DKVRLVQLRA KQLDEAAYLA RAQRALSLCR EHGARLLLNG EPTLLDHIDA DGIHLTSERL MQLERRPIAE SKWLSASTHN QTQLTQAAVL GCDFVSLSPL RTTPSHPEVF PLGWHDFQQL VERAGMPVFA LGGMTRFDAN HARAVGAQGI ASIRDFWK // ID G9EMC3_9GAMM Unreviewed; 419 AA. AC G9EMC3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=LDG_6389; OS Legionella drancourtii LLAP12. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=658187; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LLAP12; RX PubMed=22047552; DOI=10.1186/1471-2164-12-542; RA Gimenez G., Bertelli C., Moliner C., Robert C., Raoult D., RA Fournier P.E., Greub G.; RT "Insight into cross-talk between intra-amoebal pathogens."; RL BMC Genomics 12:542-542(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH413811; EHL31723.1; -; Genomic_DNA. DR EnsemblBacteria; EHL31723; EHL31723; LDG_6389. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 419 AA; 46094 MW; 077BCF1E6CD5DB74 CRC64; MKTVWAIAGT DADAQTLRGF GLELVHAEGM PAAIKFGALE TANELAATIG FLTNYSGPLV LDVPLIPTAM YGMLHQVDIL VLDIHEAETI LNQAINSHEA IKDAAVELLA FGVKSVLLKG EQMHESLWVH DYWTNGSNSF WLTQRRYSDA KYPVAGAVFS AAITAALALG YPAEDAIVIA KMYLHQAIRL AQTDLYYGGF PEDEADLPYL AAMPLFAAPE AFKHTHYLGL YPVVDSFKWV ETLVEFGVKT IQLRIKERTP TLEEEMKRSI VLAKQHQVTL FINDYWDLAL KLDAEAVHLG QSDLDTADLD AIRRKGLLLG VSTYCYYEVA RAHAICPSYV AIGPIYPTTS KELAFEAQGV EMLRRWMRTL HYPLVAIGGI SLERAPDVVA TGVSGVALIS AITAAEDPRK VTQQLLSLM // ID G9EWV3_CLOSG Unreviewed; 205 AA. AC G9EWV3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IYC_03586; OS Clostridium sporogenes PA 3679. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1075091; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PA3679; RA Bradbury M., Greenfield P., Midgley D., Li D., Tran-Dinh N., Brown J.; RT "Whole genome shotgun sequencing of Clostridium 'sporogenes'."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH470488; EHN16463.1; -; Genomic_DNA. DR EnsemblBacteria; EHN16463; EHN16463; IYC_03586. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22416 MW; A67E9CD2194127C9 CRC64; MDLNYELYLI TDRRFLKGRE LKKVVEDAIL GGVTIVQVRE KDVSTREFYN VAKEVKEVTD HYKVPIIIND RLDIAQAINA HGVHLGQKDM HLNIARRILG KDKIIGISVG NVKEALEAEN NGADYLGIGT IFPTGSKKDV DAIIGIDGLS KIKNNISIPS VAIGGINKTN FKDVLSTGIE GISVISAILD EDDINIAANN LLINK // ID G9F1V5_CLOSG Unreviewed; 200 AA. AC G9F1V5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=IYC_12669; OS Clostridium sporogenes PA 3679. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1075091; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PA3679; RA Bradbury M., Greenfield P., Midgley D., Li D., Tran-Dinh N., Brown J.; RT "Whole genome shotgun sequencing of Clostridium 'sporogenes'."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH470528; EHN14633.1; -; Genomic_DNA. DR EnsemblBacteria; EHN14633; EHN14633; IYC_12669. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 200 AA; 21920 MW; D7F87CF5FBD1D1ED CRC64; MYKLLAITNR HICNNEFLAQ IQDICTLNEK NTVIESVSIV LREKDLSEND YKKLAADVLK ICKKNNTECI LHTYYKVAKE LNCKKIHLPL HILKSNPNIY KDFNEVGVSI HSVNEAIEAM HLGATYITAG HIFATNCKKG LPPRGLGFLS SVCSSVHIPV YAIGGISPAN AEKAIDAGAE GVCIMSGLMA CKSSQLFIAK // ID G9N9R6_HYPVG Unreviewed; 501 AA. AC G9N9R6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-APR-2014, entry version 13. DE SubName: Full=Uncharacterized protein; GN ORFNames=TRIVIDRAFT_40490; OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens) OS (Trichoderma virens). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae; OC Trichoderma. OX NCBI_TaxID=413071; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Gv29-8; RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40; RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A., RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A., RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., RA Antal Z., Atanasova L., Cervantes-Badillo M.G., Challacombe J., RA Chertkov O., McCluskey K., Coulpier F., Deshpande N., von Dohren H., RA Ebbole D.J., Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F., RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R., RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E., RA Lucas S., Lubeck M., Lubeck P.S., Margeot A., Metz B., Misra M., RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E., RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S., RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M., RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.; RT "Comparative genome sequence analysis underscores mycoparasitism as RT the ancestral life style of Trichoderma."; RL Genome Biol. 12:R40-R40(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDF02000090; EHK16684.1; -; Genomic_DNA. DR EnsemblFungi; EHK16684; EHK16684; TRIVIDRAFT_40490. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 501 AA; 51588 MW; 81EB67717782DF26 CRC64; MSKSKVDYGV YLVTDSTPAI LGNKDLTSVV EKALQGGVTI VQYRDKTSDR EAAVKTARAL HEVTRRFGVP LLVNDRVDVA VEVGCEGVHI GQDDMAYEEA RKLLGPDKII GVTASSLEEA LKACEAGADY LGLGTVYATQ TKKDTKSIIG TAGIRSILLG LSSAGHSIPT VCIGGINGSN AISVLAESSA APAKSLDGIA VVSAIVAAQD PAAAARDLLG KVVAGRVPDV IKAVAAATPL SHNMTNLVVQ NFAANVALAV GASPIMANYA EEAADLAKLG GALVINMGTV TPEGLKNHIQ ALQAYNAAGG PVVLDPVGAG ATSIRRNAVK TLLSSGKFTV IKGNEREIQT VYGASVTQRG VDSSSSLTIS QRASLAKSVA RSTGAVVVLT GKTDVVSDGV RTLRVDNGHE FLGRVTGTGC TLGTTISAME AAFRSDPLIA AVAGMVLFEI ASERAAVRDD VRGPGTFVPA FIDELSAIRT ETAKGDVAWL ARSKIETLEV E // ID G9P4P7_HYPAI Unreviewed; 507 AA. AC G9P4P7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-APR-2014, entry version 11. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=TRIATDRAFT_227661; OS Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma OS atroviride). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae; OC Trichoderma. OX NCBI_TaxID=452589; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 20476 / IMI 206040; RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40; RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A., RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A., RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., RA Antal Z., Atanasova L., Cervantes-Badillo M.G., Challacombe J., RA Chertkov O., McCluskey K., Coulpier F., Deshpande N., von Dohren H., RA Ebbole D.J., Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F., RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R., RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E., RA Lucas S., Lubeck M., Lubeck P.S., Margeot A., Metz B., Misra M., RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E., RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S., RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M., RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.; RT "Comparative genome sequence analysis underscores mycoparasitism as RT the ancestral life style of Trichoderma."; RL Genome Biol. 12:R40-R40(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDG02000027; EHK41193.1; -; Genomic_DNA. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 507 AA; 52177 MW; 51D93CFB838F09B5 CRC64; MDKTKVNYGV YLVTDSTPAI LGNKDLTSVV EAAVRGGATI VQYRDKHSDR EAAVRTARAL LAVTRRHGVP LLVNDRVDVA VEVGCEGVHI GQDDMAYEEA RKLLGPDKII GVTASSIQEA LKACEAGADY LGLGTVYATQ TKKDTKSIIG TAGIRSILQA LSAAGHAAIP TVCIGGINSS NATAVLVESS AAPAKSLDGI AVVSALVAAE DPAAAARVLL TNVAMGRVPD VVKAVAAATP LSHNMTNLVV QNFAANVALA VGASPIMANY AEEAADLAKL GGALVINMGT VTPEGLKNHV QALQAYNAAG GPVVYDPVGA GATAIRRNAV KTLLSSGHFT VIKGNEREIQ TVYGSSVSQR GVDSSSSLTI PQRATLARAL ARRTGAVVIL TGKTDIVSDA SRTLRVDNGH EFLSQVTGTG CTLGTTVSAM VAAFRSDVLV AALAGLVLFE IAAERAAVRD DVRGPGTFVP AFIDELSAVR KETAGGNVAW LAKARIEALE VVEEESA // ID G9PN82_9ACTO Unreviewed; 220 AA. AC G9PN82; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0975_01884; OS Actinomyces sp. oral taxon 849 str. F0330. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Actinomycineae; Actinomycetaceae; Actinomyces. OX NCBI_TaxID=653386; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0330; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V., RA Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Actinomyces sp. oral taxon 849 str. F0330."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTB01000102; EHM93595.1; -; Genomic_DNA. DR EnsemblBacteria; EHM93595; EHM93595; HMPREF0975_01884. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22561 MW; 3836F78596ED2EE5 CRC64; MRAAPDLSVY LITDESQCRS RGRDVLDTVE AAVDGGVTCV QLRAKGADGG LFLTQVLEVA EVVGDQVPVI VNDRVDIFLA ARDQGAPVAG VHLGQSDLPA RIARRLVGED AYLGLSAATP DELRTAQEQG ACDHVGIGVV HPTATKADAP KSLGVNGVAR MAALTDLPAV AIGGITASDL PALRAGGLAG AAVVSAICMA EDPRSVAADL HRAWDEGGRR // ID G9PYR3_9BACT Unreviewed; 216 AA. AC G9PYR3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1006_00775; OS Synergistes sp. 3_1_syn1. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Synergistes. OX NCBI_TaxID=457415; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_syn1; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Synergistes sp. 3_1_syn1."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACUH01000059; EHL64490.1; -; Genomic_DNA. DR EnsemblBacteria; EHL64490; EHL64490; HMPREF1006_00775. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22004 MW; 4FCFCCD57425CD2E CRC64; MAADRKKLAE RLRLYLICGE GDSPEAVIKK AAAAIEGGVT AVQLRVKSWT GRECYDTALA LKKICSAHGA LLLINDRLDI ALAAGADGVH LGQKDLPVGA ARRLAGTDFI IGGTARTPEL AREAQQLGAD YVGCGAAFET ATKGDAVVIG PDGIKKVLSA IDIPSVAIGG IELGNVKYLA GCGASGISLS GAIMRADDPK KAATALIKEA GRVLGG // ID G9Q8Y1_9BACI Unreviewed; 206 AA. AC G9Q8Y1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF1014_03123; OS Bacillus sp. 7_6_55CFAA_CT2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=665957; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_6_55CFAA_CT2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacillus sp. 7_6_55CFAA_CT2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWE01000055; EHL71739.1; -; Genomic_DNA. DR EnsemblBacteria; EHL71739; EHL71739; HMPREF1014_03123. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22792 MW; F39530EC7E6959E2 CRC64; MKNELHVISN GHMPFEELVD VAMQIESEID YLHIREREKS TKELYEGVES LLMEGFPASK IVINDRIDIA ILLNIPRVQL GYRSTDVKSV KEKFSYLHVG YSVHSLDEAI VAFKNGADSL VYGHVFPTDC KKGVPARGLE EISDIARCLS IPITAIGGIT PENTVDVLTN GVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID G9QEF2_9BACI Unreviewed; 219 AA. AC G9QEF2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1014_05044; OS Bacillus sp. 7_6_55CFAA_CT2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=665957; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_6_55CFAA_CT2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacillus sp. 7_6_55CFAA_CT2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWE01000086; EHL67404.1; -; Genomic_DNA. DR EnsemblBacteria; EHL67404; EHL67404; HMPREF1014_05044. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23601 MW; 6098F2B475E84197 CRC64; MARIEIDKMS KLLQVYFIMG SNNCTRDPLA VLKEALDGGV TLFQFREKGE GSLIGEDRVR FAKELQTLCK EYSVPFIVND DVELAIELDA DGVHVGQDDE GITSVREKMG DKIIGVSAHT IEEARFAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAY FREQGITVPI VGIGGITIEN TAAVIEAGAD GVSVISAISL AESAYESTRK LAEEVKRSL // ID G9QKP4_9BACI Unreviewed; 204 AA. AC G9QKP4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF1015_01733; OS Bacillus smithii 7_3_47FAA. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=665952; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_3_47FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacillus smithii 7_3_47FAA."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWF01000085; EHL78240.1; -; Genomic_DNA. DR EnsemblBacteria; EHL78240; EHL78240; HMPREF1015_01733. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 204 AA; 22458 MW; 4FDD470D7D2566AE CRC64; MKKALHVIST GKQSFEDWLS ITVRIQPWVD FIHIRERSWS TEMIKKGVAD LEKHGVPLTK IILNSQPDLA LQLGVPGVHF PEKSHEERDH GRFLTKGYSV HSVESAMDKQ KRGAQYLIFG HIYPTKSKPG LPPRGLAALK AVSSAVQIPV IAIGGITPQR VPECLAAGAS GVAVLSGVYE AEFPEQAAKA YKQSLWEGRH HAEI // ID G9QNS2_9BACI Unreviewed; 210 AA. AC G9QNS2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1015_03068; OS Bacillus smithii 7_3_47FAA. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=665952; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_3_47FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacillus smithii 7_3_47FAA."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWF01000142; EHL74994.1; -; Genomic_DNA. DR EnsemblBacteria; EHL74994; EHL74994; HMPREF1015_03068. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22308 MW; 241C6323BBC77623 CRC64; MKFNVKQALS LYLVTSESME LKELLNNVEA AIQGGVTMVQ LREKQSSGKL FLKKALALKS LTEKYEIPLV INDRVDIALA AGADGVHVGQ SDLPAAYVKK IVPPSMFVGV SCSTVEEAKE AEKQGADYLG VGAVFPTNSK KDAERLEKGM LESIVESVNI PVVAIGGINL ENVQQLSHTG IDGIAVVSAI LSSSNPKLAA EMLKSARLKG // ID G9QRF2_9PROT Unreviewed; 204 AA. AC G9QRF2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF1019_00172; OS Campylobacter sp. 10_1_50. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=665939; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=10_1_50; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Campylobacter sp. 10_1_50."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWJ01000004; EHL91401.1; -; Genomic_DNA. DR EnsemblBacteria; EHL91401; EHL91401; HMPREF1019_00172. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 204 AA; 22700 MW; 3ECFB9425D0D94F8 CRC64; MSMFKILCVA DFESYEGDDF LKRIELLCKA GVDEILLRAK GLSEAHFYDL ARVVAQICEN YRKKFIINQF FDVACKLKSD FWLTSAQLDF FKNHGVFLDE FRKTAKIYAP AHDLEQAKIS ASIADVLVAS HIFATSCKAG LEPKGLNFIS EIKSLDKEIY ALGGLDSGNY KEAIKAGANG ICFMSLAMSG DLELIKKIID SKNG // ID G9QU21_9PROT Unreviewed; 203 AA. AC G9QU21; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1019_01091; OS Campylobacter sp. 10_1_50. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=665939; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=10_1_50; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Campylobacter sp. 10_1_50."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWJ01000013; EHL89773.1; -; Genomic_DNA. DR EnsemblBacteria; EHL89773; EHL89773; HMPREF1019_01091. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 22344 MW; A3F4B31368D18B4D CRC64; MAEIYAISDD ILMPENLALD YTREILECGV KFFQFRSKKA VKNEKLASEI LNLCEKFGAK FIVNDDVKFA KKIGTKAVHL GKDDENIKEA FEILGKDAYV GVSCYNDINL AINAAKNWAS YVAFGSIFTS PTKPNAPKCG LEVVKEAKQI LNLPICAIGG INEANIGSLS HAKPDLIAVI SAIYKNGNIK ENIKNLQKII KNF // ID G9R364_9FIRM Unreviewed; 206 AA. AC G9R364; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1021_02358; OS Coprobacillus sp. 3_3_56FAA. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Coprobacillus. OX NCBI_TaxID=665941; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_3_56FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Coprobacillus sp. 3_3_56FAA."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWL01000052; EHM90918.1; -; Genomic_DNA. DR EnsemblBacteria; EHM90918; EHM90918; HMPREF1021_02358. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22317 MW; 7FCE22C13DD7038A CRC64; MLELYLVSDR SWLNDRSLEE DIEQAILGGV TMVQLREKNL TDEEFTIQAK KIKTICSKYH IPFIINDNVA VALAVDSDGI HIGQDDQPVK RVRKIIGPHK IIGVSAHNLK EALAAKEDGA DYLGVGAMFN TSTKDDATAV SFTQLHEITT KIGLPVVAIG GINQDNCLLL KGTKIDGIAV VSAIMSAPDI KEAAAKLKAH ARGIYD // ID G9RMD7_9ENTR Unreviewed; 211 AA. AC G9RMD7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1024_05126; OS Klebsiella sp. 4_1_44FAA. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=665944; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_1_44FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Klebsiella sp. 4_1_44FAA."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWO01000123; EHL84948.1; -; Genomic_DNA. DR ProteinModelPortal; G9RMD7; -. DR EnsemblBacteria; EHL84948; EHL84948; HMPREF1024_05126. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 21B54D01518D3CB0 CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIERLLE AGVRTLQLRI KDRRDSEVED DVIAAIALGR RYHARLFIND YWQLAIKHQA YGVHLGQEDL ETTDLSAIRQ AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIQRLADYP TVAIGGISLE KAPGVLATGV GSIAVVSAIT QAADWRAATD QLLALAGAGD E // ID G9S7L1_9PORP Unreviewed; 209 AA. AC G9S7L1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1033_02747; OS Tannerella sp. 6_1_58FAA_CT1. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Tannerella. OX NCBI_TaxID=665949; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_58FAA_CT1; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Tannerella sp. 6_1_58FAA_CT1."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWX01000054; EHL81853.1; -; Genomic_DNA. DR EnsemblBacteria; EHL81853; EHL81853; HMPREF1033_02747. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 30 34 HMP-PP binding (By similarity). FT REGION 127 129 THZ-P binding (By similarity). FT METAL 63 63 Magnesium (By similarity). FT METAL 82 82 Magnesium (By similarity). FT BINDING 62 62 HMP-PP (By similarity). FT BINDING 101 101 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23073 MW; EE959E9E055D9F8A CRC64; MLQFITHSNE KYDYLTSAIE ALKGGCHWIQ LRMKNIPEQT VMATALQLKE YCRKYNAKLI LDDHVQATLK TGADGVHLGK NDMSPSDARK ILGNGYIIGG TANTLDDIER LIKEGVDYIG LGPFRYTETK KNLSPILGID GYKKILMACK EKGYTIPIVA IGGITKNDIP EIMSTGVTGI ALSGSILRAE NPQVETQLII NLINKYNNE // ID G9S7L2_9PORP Unreviewed; 195 AA. AC G9S7L2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF1033_02748; OS Tannerella sp. 6_1_58FAA_CT1. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Tannerella. OX NCBI_TaxID=665949; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_58FAA_CT1; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Tannerella sp. 6_1_58FAA_CT1."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWX01000054; EHL81854.1; -; Genomic_DNA. DR EnsemblBacteria; EHL81854; EHL81854; HMPREF1033_02748. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 195 AA; 21625 MW; B2B60E97CBCFFE20 CRC64; MKLVGITRPT FFKGEADAIT LLLEGGLDLL HIRKPGSLSE NIASLLSDIP PHLYSQIVIH DHFDLIESFP LKGIHLNKRN PVCPSIHTGS VSRSCHSIEE LDHIEDIDYC FLSPIFDSIS KKGYLSAFSK EELADASRKG IINSKVYALG GITPEHIPLL QEFGFGGVAV LGYLWEDITL HTLQHRINIL KNSIC // ID G9SB68_CITFR Unreviewed; 211 AA. AC G9SB68; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9428_04841; OS Citrobacter freundii 4_7_47CFAA. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex. OX NCBI_TaxID=742730; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_7_47CFAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Citrobacter freundii 4_7_47CFAA."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLG01000005; EHL85790.1; -; Genomic_DNA. DR EnsemblBacteria; EHL85790; EHL85790; HMPREF9428_04841. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23156 MW; 25A994A98019ED33 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLQ AGVRTIQLRI KDKRDEEVEA DVMAAIELGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AELRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLTQLA NHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWQVATA QLLDIAGVGD E // ID G9TG66_SALMO Unreviewed; 211 AA. AC G9TG66; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM031_09962; OS Salmonella enterica subsp. enterica serovar Montevideo str. SARB31. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=749952; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SARB31; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESR01000055; EHL32921.1; -; Genomic_DNA. DR EnsemblBacteria; EHL32921; EHL32921; SEEM031_09962. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G9TN91_SALMO Unreviewed; 211 AA. AC G9TN91; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM710_15603; OS Salmonella enterica subsp. enterica serovar Montevideo str. ATCC OS BAA710. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=749953; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA710; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESS01000106; EHL43381.1; -; Genomic_DNA. DR EnsemblBacteria; EHL43381; EHL43381; SEEM710_15603. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G9U4W1_SALMO Unreviewed; 211 AA. AC G9U4W1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM010_19683; OS Salmonella enterica subsp. enterica serovar Montevideo str. LQC 10. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=749948; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LQC 10; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEST01000049; EHL33707.1; -; Genomic_DNA. DR EnsemblBacteria; EHL33707; EHL33707; SEEM010_19683. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G9UHC2_SALMO Unreviewed; 211 AA. AC G9UHC2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM030_12239; OS Salmonella enterica subsp. enterica serovar Montevideo str. SARB30. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=749947; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SARB30; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESU01000052; EHL44637.1; -; Genomic_DNA. DR EnsemblBacteria; EHL44637; EHL44637; SEEM030_12239. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G9UTJ1_SALMO Unreviewed; 211 AA. AC G9UTJ1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM29N_04953; OS Salmonella enterica subsp. enterica serovar Montevideo str. 29N. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=763920; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=29N; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESW01000068; EHL45488.1; -; Genomic_DNA. DR EnsemblBacteria; EHL45488; EHL45488; SEEM29N_04953. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G9V221_SALMO Unreviewed; 211 AA. AC G9V221; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM42N_13709; OS Salmonella enterica subsp. enterica serovar Montevideo str. 42N. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=763921; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=42N; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESX01000042; EHL58718.1; -; Genomic_DNA. DR EnsemblBacteria; EHL58718; EHL58718; SEEM42N_13709. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G9VAZ1_SALMO Unreviewed; 211 AA. AC G9VAZ1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM41H_10426; OS Salmonella enterica subsp. enterica serovar Montevideo str. 4441 H. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=766761; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4441 H; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AESY01000021; EHL62331.1; -; Genomic_DNA. DR EnsemblBacteria; EHL62331; EHL62331; SEEM41H_10426. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G9VTX6_SALMO Unreviewed; 211 AA. AC G9VTX6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM020_003120; OS Salmonella enterica subsp. enterica serovar Montevideo str. 507440-20. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=859199; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=507440-20; RX PubMed=21345093; DOI=10.1056/NEJMc1100443; RA Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E., RA Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J., RA Stones R.; RT "Identification of a salmonellosis outbreak by means of molecular RT sequencing."; RL N. Engl. J. Med. 364:981-982(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=507440-20; RA Allard M.W., Luo Y., Li C., Keys C.E., San I., Stones R., Musser S.M., RA Brown E.W.; RT "High Resolution Clustering of Salmonella enterica serovar Montevideo RT Strains Using a Next-Generation Sequencing Approach."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AETI02000019; EHN55458.1; -; Genomic_DNA. DR EnsemblBacteria; EHN55458; EHN55458; SEEM020_003120. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G9WD90_SALET Unreviewed; 211 AA. AC G9WD90; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LTSEBAI_5492; OS Salmonella enterica subsp. enterica serovar Baildon str. R6-199. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913069; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R6-199; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCK01001594; EHJ79794.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ79794; EHJ79794; LTSEBAI_5492. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23018 MW; 5F34B5203D5B82C7 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLPQLA RHIERLANYP TVAIGGISVE RAPSVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID G9X030_9FIRM Unreviewed; 305 AA. AC G9X030; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-APR-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9629_01781; OS Peptostreptococcaceae bacterium ACC19a. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=796937; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACC19a; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A., RA Epstein S., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Eubacteriaceae bacterium ACC19a."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFZE01000011; EHL15535.1; -; Genomic_DNA. DR EnsemblBacteria; EHL15535; EHL15535; HMPREF9629_01781. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 305 AA; 33969 MW; F089266410A47C1B CRC64; MKNIDYTMYY VTDEDLLSSN HTLETSVQDA ILGGCTMIQL REKHSSTLDF YNKAVKIKAI CDKYNIPLII NDRIDVALAI NADGVHLGQD DMPLDIARKI MGDGKIIGIS TSTLDEALIA QQGGADYVGV GAMYSTNTKT DANLTTINEL TKIKNNLKIP VVAIGGINLD TIPTLKPAQI DGVAIVSAIS MQEDTVSATR KLKNTFLKQY QTKGVIFDID GTLLETMNIW DNVLLNLMNT LNISYTEYEI QKIWNMGFAE LAQFSIKKFK LDMSVKEFWQ LIKKLSVEEY KNSKIHLKKG AKKTA // ID G9XDZ4_9FIRM Unreviewed; 431 AA. AC G9XDZ4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-APR-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF9628_02017; OS Peptostreptococcaceae bacterium CM5. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=796940; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CM5; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A., RA Epstein S., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Eubacteriaceae bacterium CM5."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFZG01000039; EHL18835.1; -; Genomic_DNA. DR ProteinModelPortal; G9XDZ4; -. DR EnsemblBacteria; EHL18835; EHL18835; HMPREF9628_02017. DR UniPathway; UPA00060; UER00141. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF13419; HAD_2; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00413; HADHALOGNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 431 AA; 48374 MW; 1398300D77049DB5 CRC64; MKNIDYTMYY VTDEDLLSSN HTLETSVQDA ILGGCTMIQL REKHSSTLDF YNKAVKIKAI CDKYNIPLII NDRIDVALAI NADGVHLGQD DMPLDIARKI MGDGKIIGIS TSTLDEALIA QQGGADYVGV GAMYSTNTKT DANLTTIDEL TKIKNNLKIP VVAIGGINLD TIPALKPAQI DGVAIVSAIS MQEDTVSATR KLKNTFLKQY QTKGVIFDID GTLLETMNIW DNVLLNLMNT LNISYTEDEI QKIWNMGFAE LAQFSIKKFK LDMSVKEFWQ LIKKLSVEEY KNSEIHLKKG AKKLLEYLKE KDVKLAIATA LCKEQYETVL TKTGIIDYFD IIASSVDLKM EKSDRQIFDY IAKNLQVPNK NLIFFEDDIN SSTGAKLAGL KLCIVSNKKY NGNSKFDALI DYKIDDFENK LIYDEIIVEK N // ID G9XV96_DESHA Unreviewed; 207 AA. AC G9XV96; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0322_04909; OS Desulfitobacterium hafniense DP7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=537010; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DP7; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFZX01000133; EHL04399.1; -; Genomic_DNA. DR ProteinModelPortal; G9XV96; -. DR EnsemblBacteria; EHL04399; EHL04399; HMPREF0322_04909. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21882 MW; 78E75E75E7596D62 CRC64; MAVDYSLYLV TDRILVGPKD FLLSIRKALE GGVTLLQLRE KETNSREFYD IGVKVKELAA EFGVPLIIND RVDLALALDA DGVHVGQQDL PLAKVRNIIG PDKILGYSVS SLEEALQGER MGADYLGAGP VFPTGSKKDA AEAIGLAKLK EIKAGVSLPV VGIGGIGAAN LRAVKETGID GVSVISAILS QEDPCAAAKG LMDLWRN // ID G9Y190_HAFAL Unreviewed; 220 AA. AC G9Y190; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0454_00305; OS Hafnia alvei ATCC 51873. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Hafnia. OX NCBI_TaxID=1002364; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51873; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGCI01000006; EHM48146.1; -; Genomic_DNA. DR EnsemblBacteria; EHM48146; EHM48146; HMPREF0454_00305. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24211 MW; 3C2A9EE2E4E51286 CRC64; MAPLTHSRTA PFPSTEQRLG LYPVVDSVEW IERLLKAGVR TIQLRIKDQS ENAVETDIAQ AIALGRHYQA RLFINDYWQL AIKHRAYGVH LGQEDLDTAD LSAISAAHLR LGLSTHDDIE MDRALSYRPS YIALGHIFPT QTKLMPSAPQ GLADLKRQVA RIPDYPTVAI GGISIDRVPA VLESGVGSIA VVSAITQAQD WLAATDTLLQ LIENRRANDA // ID G9YH43_9FIRM Unreviewed; 213 AA. AC G9YH43; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0080_00969; OS Anaeroglobus geminatus F0357. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Anaeroglobus. OX NCBI_TaxID=861450; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0357; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGCJ01000038; EHM41098.1; -; Genomic_DNA. DR EnsemblBacteria; EHM41098; EHM41098; HMPREF0080_00969. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22959 MW; 7D868D56172F03B7 CRC64; MTKEEHVRRL AEDPVYVIMG EEFSLGRKNR EVAKELLDAG VKIIQYREKH KTWREKYGEA KEIAAMCEEY GATFIMNDSA DIAVACGADG IHVGQDDAPV PLVRALAGED IFIGLSTNTI AEMKGALADG ADYVGFGPMY PSASKADAGK VVSPEEKAFA LHFALPVVTI GGIGRDNIGE LYKEGFRSFA MISAVVSQPD IAAAVAELRC ACR // ID G9YJX1_9FIRM Unreviewed; 197 AA. AC G9YJX1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF0080_01977; OS Anaeroglobus geminatus F0357. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Anaeroglobus. OX NCBI_TaxID=861450; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0357; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGCJ01000089; EHM37981.1; -; Genomic_DNA. DR EnsemblBacteria; EHM37981; EHM37981; HMPREF0080_01977. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 197 AA; 21953 MW; A761ED4C4B9A22E1 CRC64; MMRKVIAITN RHLVHRDYWD QLEQIVASPV ESLVLREKDL SEDEYIDFKR KALQLCNYHG KECVLHNFGR VAVRLHIPRF QCSLDYLKTH TSISYYMTTL GVSVHTPEEA HQAEKLGATY VIAGHVFPTP SKSKFRPIGV SAVTEICKAV SIPVFALGGV NPGTVEALKN IPVKGIALMS GLMQSSDISS YIASLQK // ID G9YXT8_9ENTR Unreviewed; 211 AA. AC G9YXT8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0880_00021; OS Yokenella regensburgei ATCC 43003. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yokenella. OX NCBI_TaxID=1002368; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43003; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGCL01000002; EHM52027.1; -; Genomic_DNA. DR EnsemblBacteria; EHM52027; EHM52027; HMPREF0880_00021. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22881 MW; F3545A4AACAB1543 CRC64; MYQPDFPSVP FRLGLYPVVD SVEWIERLLQ AGVRTLQLRI KDKRDAEVEA DVAAAIALGR RYDARLFIND YWRLAIKHNA YGVHLGQEDL ETTDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SSPQGLEQLA AHIARLKDYP TVAIGGISLE RAAPVLATGV GSIAVVSAIT QAADWQAATA KLLELAGVGD E // ID G9ZBA7_9GAMM Unreviewed; 204 AA. AC G9ZBA7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9080_00029; OS Cardiobacterium valvarum F0432. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales; OC Cardiobacteriaceae; Cardiobacterium. OX NCBI_TaxID=797473; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0432; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGCM01000003; EHM56124.1; -; Genomic_DNA. DR EnsemblBacteria; EHM56124; EHM56124; HMPREF9080_00029. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 136 138 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 20830 MW; BF61DF815F6D732D CRC64; MNACNLHLYL VLDAAACGER LLAVAEAALQ GGVSVLQLRG HKTAWSKRVW YDTALAVKAR CAAHQVPFII NDQVDIALAV GADGVHIGQS DLPAAVVRRL IGNKRILGLS THSVAQVQAV DSGIVDYIGM GPVFPTRSKA DADPAIGLDG LAAMVAAKRL PGVAIGGINT DNVATVRAAS PDGIAVIGAI CGAANALTAT QALQ // ID G9ZNX7_9LACO Unreviewed; 216 AA. AC G9ZNX7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9103_01431; OS Lactobacillus parafarraginis F0439. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=797515; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0439; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEY01000070; EHL98614.1; -; Genomic_DNA. DR EnsemblBacteria; EHL98614; EHL98614; HMPREF9103_01431. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22981 MW; 1A0AD446D6439C72 CRC64; MGMAFRERLL RAYFIAGTQD VKNPRLTLQQ ILQQALAAGI TAFQYREKGP GSLTGKARVK MALQLREMCA SHAVPFIVDD DVDLAKTTDA DGIHVGQKDE RVTQVIDEVG DSMFVGLSCD TEDQVRAANQ TSGLSYIGSG PVYPTGSKAD ADPAIGVDGL AKLVAVSQLP VVAIGGITEE NVDELPKAKV TGAAVISMIA QSRDINRTVA KMLTTF // ID G9ZP04_9LACO Unreviewed; 225 AA. AC G9ZP04; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9103_01458; OS Lactobacillus parafarraginis F0439. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=797515; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0439; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEY01000072; EHL98564.1; -; Genomic_DNA. DR EnsemblBacteria; EHL98564; EHL98564; HMPREF9103_01458. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 53 57 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 24471 MW; 128388B5B1586548 CRC64; MGRLQCKESN LRRITMKLLN RPLYLVTDHT GLDEADFLQQ IDLACEAGVS LLQLREKDRS SREIYDWAVK VKEIADRHKI PLIVDDRLDI AQAVDAAGVH LGQRDLPVDV ARRILGPRKI IGATAKTLKQ AKLAEQMGAD YLGTGAIFPT QTHVKTVHTS VETLAKIKEA VQIPVYAIGG LKADNVAAIK PAHVDGVAVV SAIMRAKNAW AATSELLSAI EDAIG // ID G9ZVG8_9PROT Unreviewed; 221 AA. AC G9ZVG8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9946_00532; OS Acetobacteraceae bacterium AT-5844. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; unclassified Acetobacteraceae. OX NCBI_TaxID=1054213; RN [1] RP NUCLEOTIDE SEQUENCE. RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEZ01000020; EHM03041.1; -; Genomic_DNA. DR EnsemblBacteria; EHM03041; EHM03041; HMPREF9946_00532. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23170 MW; E64C2829C90545C0 CRC64; MAGGKSQSKQ GKPQDEGCRL YLVTPPALEP RAFADTLARA LDAGDVAAVQ LRLKDVSDDA LKRAVEVLRP VAQSRDVAFL LNDRADLAVQ TGCDGAHLGQ EDGDHAAARE LLGDLMLGIS CHGSRHLAME AGEIGADYVA FGAFFPTSTK VTEHKAEPDV LEWWSEMFEL PSVAIGGITP ENCGPLVRAG ADFLAVVSAV WNHPEGAAAG VRAMNAAIAA A // ID H0A1W9_9PROT Unreviewed; 204 AA. AC H0A1W9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9946_02811; OS Acetobacteraceae bacterium AT-5844. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; unclassified Acetobacteraceae. OX NCBI_TaxID=1054213; RN [1] RP NUCLEOTIDE SEQUENCE. RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEZ01000089; EHL99903.1; -; Genomic_DNA. DR EnsemblBacteria; EHL99903; EHL99903; HMPREF9946_02811. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 30 34 HMP-PP binding (By similarity). FT REGION 179 180 THZ-P binding (By similarity). FT METAL 63 63 Magnesium (By similarity). FT METAL 82 82 Magnesium (By similarity). FT BINDING 62 62 HMP-PP (By similarity). FT BINDING 101 101 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 159 159 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21817 MW; 4BAFFD54C851F32A CRC64; MMPLPSRFYP VVPDAGWVAR LAAAGARLIQ LRIKDATPAE ILRQAAEAAE ACRTHGAHLV LNDHWEAAIA LKLEWLHLGQ EDLDTADLAA IRAAGLRLGV STHSDAELER ALTVDPDYVA LGPIYPTTLK VMPWRPQGLE RLGTWRQRLG GRPLVAIGGI TLERAPGCVA AGADSVAVVS DVTGHPAPEQ RARDWIAQLD AAAA // ID H0AG68_STAAU Unreviewed; 213 AA. AC H0AG68; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21178_1504; OS Staphylococcus aureus subsp. aureus 21178. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904724; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21178; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGRN01000012; EHM64214.1; -; Genomic_DNA. DR ProteinModelPortal; H0AG68; -. DR SMR; H0AG68; 4-209. DR PRIDE; H0AG68; -. DR EnsemblBacteria; EHM64214; EHM64214; SA21178_1504. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H0ATA3_STAAU Unreviewed; 213 AA. AC H0ATA3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21202_2207; OS Staphylococcus aureus subsp. aureus 21202. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904732; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21202; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGRO01000059; EHM59052.1; -; Genomic_DNA. DR ProteinModelPortal; H0ATA3; -. DR EnsemblBacteria; EHM59052; EHM59052; SA21202_2207. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23374 MW; 87C8D3399EE9DFCF CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDEVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H0B2H5_STAAU Unreviewed; 213 AA. AC H0B2H5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21209_1056; OS Staphylococcus aureus subsp. aureus 21209. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904735; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21209; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGRP01000086; EHM57602.1; -; Genomic_DNA. DR ProteinModelPortal; H0B2H5; -. DR SMR; H0B2H5; 4-209. DR PRIDE; H0B2H5; -. DR EnsemblBacteria; EHM57602; EHM57602; SA21209_1056. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H0BCM5_9ACTO Unreviewed; 216 AA. AC H0BCM5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPW_3072; OS Streptomyces sp. W007. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1055352; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=W007; RX PubMed=22374958; DOI=10.1128/JB.06701-11; RA Qin S., Zhang H., Li F., Zhu B., Zheng H.; RT "Draft Genome Sequence of Marine Streptomyces sp. Strain W007, Which RT Produces Angucyclinone Antibiotics with a Benz[a]anthracene RT Skeleton."; RL J. Bacteriol. 194:1628-1629(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSW01000114; EHM28557.1; -; Genomic_DNA. DR EnsemblBacteria; EHM28557; EHM28557; SPW_3072. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22804 MW; 1DC00E15F1894439 CRC64; MSMPREQLSD ARLYLCTDAR KLQGDLPAFL DAVLAAGVDI VQLRDKGMEA AEELEHLAVL ADACRRHGKL LAVNDRADVA HAIAADVLHL GQGDLPVPAA RAIIGADRLI GRSTHAEVEV DAAVAQDGVD YFCTGPCWPT PTKPGRHAPG LDLVRYAASL GGARPWFAIG GIDAGNLDQV LDAGARRVVV VRAITEADDP AAATADLARR IRARAL // ID H0BVR1_9BURK Unreviewed; 306 AA. AC H0BVR1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=KYG_07356; OS Acidovorax sp. NO-1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=512030; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NO-1; RX PubMed=22374962; DOI=10.1128/JB.06814-11; RA Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.; RT "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and RT Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1."; RL J. Bacteriol. 194:1635-1636(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTS01000063; EHL23593.1; -; Genomic_DNA. DR EnsemblBacteria; EHL23593; EHL23593; KYG_07356. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 306 AA; 32116 MW; 266EF5F68CF1B276 CRC64; MHDTTALAHA ILSHHAATFA GFAPEPVPAP TSQEPVYLAA LQACSQLGFI AHDAECLARA WQTRALRTGV AQPETWPDAP EDFGLQPLPR AHQFAPCPHH LGLYAVLPDA AWVGRMARAG VPTVQLRFKS DDPVAIDREV RSAVSAVQGT GALLFINDHW RAAIDAGAYG VHLGQEDLDA LSAPELQALH CSGLRLGVST HGYAEMVRAD AVGPSYVAMG AVFPTTLKKM ATAPQGVGRL GVYARLMRHY PQVAIGGIGA EQFGQVLATG VGSVAVVRAI VNAPDAEVAA AQLMQGLKAG GMPHET // ID H0CBF7_STAAU Unreviewed; 213 AA. AC H0CBF7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21194_0809; OS Staphylococcus aureus subsp. aureus 21194. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904727; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21194; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTU01000208; EHM76900.1; -; Genomic_DNA. DR ProteinModelPortal; H0CBF7; -. DR EnsemblBacteria; EHM76900; EHM76900; SA21194_0809. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23374 MW; 87C8D3399EE9DFCF CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDEVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H0CI57_STAAU Unreviewed; 213 AA. AC H0CI57; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21331_2067; OS Staphylococcus aureus subsp. aureus 21331. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904766; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21331; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTV01000033; EHM75435.1; -; Genomic_DNA. DR ProteinModelPortal; H0CI57; -. DR EnsemblBacteria; EHM75435; EHM75435; SA21331_2067. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23278 MW; 4683C6CD4C160B2C CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLGEY AKSDLTHVDY IGVGPIYPTP SKNDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H0CQC0_STAAU Unreviewed; 213 AA. AC H0CQC0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21334_2091; OS Staphylococcus aureus subsp. aureus 21334. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904768; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21334; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTW01000035; EHM75504.1; -; Genomic_DNA. DR ProteinModelPortal; H0CQC0; -. DR EnsemblBacteria; EHM75504; EHM75504; SA21334_2091. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23384 MW; 8FEFB3993FF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI ENTVNRFKDF FNN // ID H0CVM0_STAAU Unreviewed; 213 AA. AC H0CVM0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21340_1518; OS Staphylococcus aureus subsp. aureus 21340. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904771; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21340; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTX01000020; EHM83128.1; -; Genomic_DNA. DR EnsemblBacteria; EHM83128; EHM83128; SA21340_1518. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23398 MW; 87C7939D6EF62194 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PKMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H0D558_STAAU Unreviewed; 213 AA. AC H0D558; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21232_1309; OS Staphylococcus aureus subsp. aureus 21232. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904737; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21232; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTY01000039; EHM81773.1; -; Genomic_DNA. DR ProteinModelPortal; H0D558; -. DR SMR; H0D558; 4-209. DR PRIDE; H0D558; -. DR EnsemblBacteria; EHM81773; EHM81773; SA21232_1309. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H0D7H5_STAAU Unreviewed; 213 AA. AC H0D7H5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU006_2479; OS Staphylococcus aureus subsp. aureus VCU006. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904313; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU006; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTZ01000005; EHM69600.1; -; Genomic_DNA. DR ProteinModelPortal; H0D7H5; -. DR SMR; H0D7H5; 4-209. DR PRIDE; H0D7H5; -. DR EnsemblBacteria; EHM69600; EHM69600; SEVCU006_2479. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H0DEX6_9STAP Unreviewed; 215 AA. AC H0DEX6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU012_0693; OS Staphylococcus pettenkoferi VCU012. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904314; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU012; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUA01000019; EHM72113.1; -; Genomic_DNA. DR EnsemblBacteria; EHM72113; EHM72113; SEVCU012_0693. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23220 MW; EA7D2038A7FC542E CRC64; MFKATDLKVY FICGTQDIKS ERMIHEVLKD ALEAGITLYQ FREKGPTALR GADKRQLAEE LLALCHQYDV PFIVNDDIEL AKAIDADGVH VGQDDAAVAE FASEFEDKII GLSVGNVEEY QHSDLTHVDY IGVGPMYATQ SKDDANAPVG PEMIPTLREY VGDLPIVAIG GIAINNAQDC FKAGADGVSV ISAIAQSNDI QGTVANFLQS AKESQ // ID H0DJG3_9STAP Unreviewed; 194 AA. AC H0DJG3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU012_1638; OS Staphylococcus pettenkoferi VCU012. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904314; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU012; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUA01000086; EHM68098.1; -; Genomic_DNA. DR EnsemblBacteria; EHM68098; EHM68098; SEVCU012_1638. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 194 AA; 21669 MW; 2FD0A71F7654C2FC CRC64; MFIAITPYRN LTVQDLEHYR ALVTDIDGLI LRTPMSMDQL EQWIEQIVRQ GFPKNKLIAH NDIQLLERQH LSAIHFKESA EELESFVDTH PNIRVSQSTH SAVTIQRAAN LGLDFVLYGH IFPTQSKPGL APRTAEEVRA AVAQPIPVVA LGGIALTNIS QLPKGFAGIA AISLFENVTT SEMKALRKEW SDYV // ID H0DRN2_STAEP Unreviewed; 213 AA. AC H0DRN2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU071_1191; OS Staphylococcus epidermidis VCU071. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904325; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU071; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUB01000039; EHM65351.1; -; Genomic_DNA. DR EnsemblBacteria; EHM65351; EHM65351; SEVCU071_1191. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23761 MW; 3252D2CB7B11E88B CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIH QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H0DS91_STAEP Unreviewed; 197 AA. AC H0DS91; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU071_0865; OS Staphylococcus epidermidis VCU071. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904325; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU071; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUB01000046; EHM64507.1; -; Genomic_DNA. DR EnsemblBacteria; EHM64507; EHM64507; SEVCU071_0865. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 197 AA; 22595 MW; 019E8E297AC4C788 CRC64; MIFIFIAITH HKQLTKDDLQ HYKHIEEAID GLLLRTSMNK EETKDIIQSL LQLGFSKDKI IIHSDVTLLE DLHLKRIHFK ENDSTAFTYK EAHPDICVSM STHDVETVKR CYENGLDSVF FGHIFPTSSH PDVPPRSKEA IQQALNVPIP IYAIGGINEH SIQKMPRGFK GICAISYFNN ASLTDIKQLR REWFAHA // ID H0DTP2_STAEP Unreviewed; 160 AA. AC H0DTP2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF9956_2069; OS Staphylococcus epidermidis 14.1.R1.SE. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1000590; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=14.1.R1.SE; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUC01000027; EHM73688.1; -; Genomic_DNA. DR ProteinModelPortal; H0DTP2; -. DR EnsemblBacteria; EHM73688; EHM73688; HMPREF9956_2069. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18252 MW; D44AF318920FBC36 CRC64; MNNEENKDMI QSLLQLGFSK DKIIIHSDTT LLEELNLKRI HFKSNDTTAF AYKAAHPDIY VSMSTHDVET VKRCYENNLD YVFLGHIFPT ASHPDTPPRS KKTIQQALDV PIPIYAIGGI NEHSIYKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID H0DVK6_STAEP Unreviewed; 213 AA. AC H0DVK6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9956_1713; OS Staphylococcus epidermidis 14.1.R1.SE. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1000590; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=14.1.R1.SE; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUC01000054; EHM73021.1; -; Genomic_DNA. DR ProteinModelPortal; H0DVK6; -. DR EnsemblBacteria; EHM73021; EHM73021; HMPREF9956_1713. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23704 MW; 0E35EA2716A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDVPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H0FAJ5_9BURK Unreviewed; 221 AA. AC H0FAJ5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=KYC_19009; OS Achromobacter arsenitoxydans SY8. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=477184; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SY8; RX PubMed=22328747; DOI=10.1128/JB.06667-11; RA Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.; RT "Genome sequence of the highly efficient arsenite-oxidizing bacterium RT Achromobacter arsenitoxydans SY8."; RL J. Bacteriol. 194:1243-1244(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUF01000058; EHK64659.1; -; Genomic_DNA. DR EnsemblBacteria; EHK64659; EHK64659; KYC_19009. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23269 MW; 611619C474FEF4CB CRC64; MKSLRFPAGL YGVTPEWDDT DRLLQAVRDA AAGGMRALQL RRKDVPDAVR AAQARALAPL CRELGVVFLI NDDWRLALDV GADGAHVGRD DDSLARIRSE AGPDLILGGS SYDDLNRARE LLDAGADYIA FGAMFPSTVK PDTVRAPLSV LTEARRLVQE RDAPRPAVVA IGGITPDNAP LVAQAGADSI AVITSLFGAP SVRAAAAACA APYSANPNRK S // ID H0FAM8_9BURK Unreviewed; 320 AA. AC H0FAM8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Uncharacterized protein; GN ORFNames=KYC_19174; OS Achromobacter arsenitoxydans SY8. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=477184; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SY8; RX PubMed=22328747; DOI=10.1128/JB.06667-11; RA Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.; RT "Genome sequence of the highly efficient arsenite-oxidizing bacterium RT Achromobacter arsenitoxydans SY8."; RL J. Bacteriol. 194:1243-1244(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUF01000058; EHK64692.1; -; Genomic_DNA. DR ProteinModelPortal; H0FAM8; -. DR EnsemblBacteria; EHK64692; EHK64692; KYC_19174. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 320 AA; 34298 MW; 213F404C1FB3A4DC CRC64; MSEKIVDVAA GLILRPDGKL LLGQRPEGKP WSGWWELPGG KLEPGETVLE ALARELQEEI GIRVTQSRPW VTYVHVYPHT TVRLAFCHVT GWEGEPQSLE NQRLEWVDPA NAASVGDLLP ATLPPLRWLQ LPTTYGISSV GSRAGIAPFL GRLEAALARG VKLVQLREPQ WPDGVGASSL HEVLQQALKR CRAAGARLLV NSIHPAAWWK EADGVHLRTA DAARLTARPD LPKTALVGVS AHDNAQVVHA RDLGADFAVL GPVLDTPSHP GAPTLGWDGF VQGNRDAGIP VFALGGQSTQ TVSQALRHGA HGIAGIRGIL // ID H0G0B1_RHIML Unreviewed; 201 AA. AC H0G0B1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SM0020_14479; OS Sinorhizobium meliloti CCNWSX0020. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=1107881; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWSX0020; RX PubMed=22328762; DOI=10.1128/JB.06682-11; RA Li Z., Ma Z., Hao X., Wei G.; RT "Draft Genome Sequence of Sinorhizobium meliloti CCNWSX0020, a RT Nitrogen-Fixing Symbiont with Copper Tolerance Capability Isolated RT from Lead-Zinc Mine Tailings."; RL J. Bacteriol. 194:1267-1268(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVV01000025; EHK77228.1; -; Genomic_DNA. DR EnsemblBacteria; EHK77228; EHK77228; SM0020_14479. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22603 MW; C59BB37F1BFBD60E CRC64; MKLDPFYLIV DSAQWIERLV PLGVKLVQLR IKDRNEEDIR HQIRVARAVC SAHACQLIVN DYWQLAIEEA CDFIHLGQED LAEADLAAIR AAGLKLGVST HDEAELAKAL AAEPDYVALG PIYPTILKKM KWAPQGLERL SWWRERVHPL PLVAIGGLNT ERIEGVFAHG ADSAAVVTDI TLNADPEGRT REWIRKTEAW R // ID H0G9N0_RHIML Unreviewed; 217 AA. AC H0G9N0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=SM0020_31187; OS Sinorhizobium meliloti CCNWSX0020. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=1107881; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWSX0020; RX PubMed=22328762; DOI=10.1128/JB.06682-11; RA Li Z., Ma Z., Hao X., Wei G.; RT "Draft Genome Sequence of Sinorhizobium meliloti CCNWSX0020, a RT Nitrogen-Fixing Symbiont with Copper Tolerance Capability Isolated RT from Lead-Zinc Mine Tailings."; RL J. Bacteriol. 194:1267-1268(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVV01000106; EHK73992.1; -; Genomic_DNA. DR EnsemblBacteria; EHK73992; EHK73992; SM0020_31187. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 217 AA; 22654 MW; 0486726940C4DA94 CRC64; MSNIEDRCRL VLVVPDIADS AERAKLVGEA LKGGDVASVI VPQYALSDAD FQKHAEALVP VIQQAGAAAL IEGDTRVAGR AKADGLHIAG GPDALADAIE RHAPKLIVGG GNATDRHHAL EIGELRPDYV FFGRTDGDIK PEAHPKNLAL AEWWASMIEI PCIVMGGTDP QSALAVAETG AEFVALRLAV FGEAGQAPSV VAAVNALLDE KAPRFEG // ID H0GPB9_9SACH Unreviewed; 540 AA. AC H0GPB9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-APR-2014, entry version 10. DE SubName: Full=Thi6p; GN ORFNames=VIN7_4836; OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii VIN7. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=1095631; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VIN7; RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x; RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H., RA Pretorius I.S., Egholm M., Chambers P.J.; RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid RT hybrid genome with Saccharomyces cerevisiae and Saccharomyces RT kudriavzevii origins."; RL FEMS Yeast Res. 0:0-0(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVY01000049; EHN04238.1; -; Genomic_DNA. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; SQ SEQUENCE 540 AA; 58099 MW; AFA2A1E0B76E2F72 CRC64; MVFTKEEVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDIE TKNFVAEALE VQKICKKYNV PLIINDRIDV AMAIDADGVH VGQDDMPIPM VRKLLGPSKI LGWSVGKPSE VETLAKWGPD MVDYIGVGTL FPTSTKKNPK KSPMGPQGAI AILDALEEFK ATWCRTVGIG GLHPDNIQRV LCQCVASNGK RSLDGISLVS DIMAAPDACA ATKRLRGLLD ATRYQFVECE LNNTFPTTTS IQNVISQVSN NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL ARIPNASLLL NTGSVAPIEM LKAAINAYNE VNRPITFDPV GYSATETRLC LNNTLLTYGQ FACIKGNCSE ILSLAKLNNH KMKGVDSSSG KTNIDTLVRA TQIVAFQYRT VAVCTGEFDC VADGTFGGEY KLSSGTEGIT AEDLPCVIIE DGPIPIMGDI TASGCSLGST IASFIGGLDS TGKLFDAVVG AVLLYKSAGK LXSTRCQGSG SFHVELIDAL YQLFHENKPE KWSASLKKFK // ID H0H1U0_9SACH Unreviewed; 540 AA. AC H0H1U0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-APR-2014, entry version 10. DE SubName: Full=Thi6p; GN ORFNames=VIN7_10257; OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii VIN7. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=1095631; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VIN7; RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x; RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H., RA Pretorius I.S., Egholm M., Chambers P.J.; RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid RT hybrid genome with Saccharomyces cerevisiae and Saccharomyces RT kudriavzevii origins."; RL FEMS Yeast Res. 0:0-0(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVY01000376; EHM99971.1; -; Genomic_DNA. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; SQ SEQUENCE 540 AA; 58021 MW; FB670EFD5FF2AE21 CRC64; MVFAKNDVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDTE TRDFVEEALE VQKICKKYKV PLIINDRIDV AMAIDADGVH VGQSDMPIPM VRRLLGPSKI LGWSVGKPSE VETLAKWGPD MVDYIGVGTL FPTLTKKNPK KSPMGPQGAI AVLDALEEFK AIWCRTVGIG GLHPDNIQRV ICQCVSSNGK RSLDGISLVS DIMAAPDACA ATKRLRGLLD GSKYQFVDCK LNETFPTTAS IQSVISQVSS NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL ARIPNASLLL NTGSVAPIET LKAAINAYNE VNRPITFDPV GYSATETRLC LNNTLLTYGQ FTCIKGNCSE ILSLAKLNKD KMKGVDANSG NMDINLLVRA TQIVAFQYRT IAVCTGEFDC VANGIFDGKY KLSSGTAGIT AEDLPCMIIE DGPIPIMGDI TASGCSLGST IACFIGGLNS TGNLFDAVVG AVLLYKSAGK LASTRCQGSG SFHVQLIDAL YQLFHENKPE SWSASLKKFN // ID H0H394_RHIRD Unreviewed; 220 AA. AC H0H394; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AT5A_00585; OS Agrobacterium tumefaciens 5A. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=1107544; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5A; RX PubMed=22275101; DOI=10.1128/JB.06585-11; RA Hao X., Lin Y., Johnstone L., Liu G., Wang G., Wei G., McDermott T., RA Rensing C.; RT "Genome sequence of the arsenite-oxidizing strain Agrobacterium RT tumefaciens 5A."; RL J. Bacteriol. 194:903-903(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVZ01000001; EHJ99908.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ99908; EHJ99908; AT5A_00585. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22796 MW; 63CBBDCC4FF90451 CRC64; MNKVDYRLNA LVDASLGDVA PLGELALAAA LNGATILQYR DKHASTREMI ENALAIREAI AGTGVPLVIN DRVDVALASG ADGVHLGADD MDAKTARRIL GDKAIIGLTV KNRADGERAA SMPADYACIG GVFETVSKVN PDKPVGLDGF TTLRTLLREL RPGMPVGAIA GIDLARVPNV IAAGADGVAV ISAIFRANDI ASATRDFRAA VDAALKARQS // ID H0H4F1_RHIRD Unreviewed; 217 AA. AC H0H4F1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=AT5A_02620; OS Agrobacterium tumefaciens 5A. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=1107544; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5A; RX PubMed=22275101; DOI=10.1128/JB.06585-11; RA Hao X., Lin Y., Johnstone L., Liu G., Wang G., Wei G., McDermott T., RA Rensing C.; RT "Genome sequence of the arsenite-oxidizing strain Agrobacterium RT tumefaciens 5A."; RL J. Bacteriol. 194:903-903(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVZ01000001; EHK00316.1; -; Genomic_DNA. DR EnsemblBacteria; EHK00316; EHK00316; AT5A_02620. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 217 AA; 22926 MW; F34A5BDB2B0094FD CRC64; MTKVDNRCRL VLIVPQLDDA QKQATELQEA LRGGDVASVI IPQYDLDDAT FQKRAELIVP MVQEAGAAAL IAGDSRVASR VKADGLHVAG NAEALAEAVE NFAPKLIVGG GNADDRHKAL EMGESNPDYV FFGKLEGDIK PEAHPKNLAL GEWWASMIEI PSIVMGGTDI SSVVAVAEAG VEFVAMRSGV FDNASGAAQA VSEINALLDE KAPRFDG // ID H0HLI3_9RHIZ Unreviewed; 207 AA. AC H0HLI3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=MAXJ12_04971; OS Mesorhizobium alhagi CCNWXJ12-2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1107882; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWXJ12-2; RX PubMed=22328758; DOI=10.1128/JB.06635-11; RA Zhou M., Chen W., Chen H., Wei G.; RT "Draft Genome Sequence of Mesorhizobium alhagi CCNWXJ12-2T, a Novel RT Salt-Resistant Species Isolated from the Desert of Northwestern RT China."; RL J. Bacteriol. 194:1261-1262(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHAM01000033; EHK58381.1; -; Genomic_DNA. DR EnsemblBacteria; EHK58381; EHK58381; MAXJ12_04971. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 207 AA; 22020 MW; 62DB1B4C53816489 CRC64; MLIAPSGEDA AAFEPRLRAA ISGGDIASII LPAYELDEAS FQAFAERIVP VAQAANIAAI IADDTRIAGR VGADGLHLET GRAALEEAIE RFQDRMTVGA GGAKTRDDAL NLGEARPDYM FFGRFGYDNK PEPHNRNLAL GHWWAEMIEI PCILMAGSDI ASVETVAETG CEFVALSSAV FGDGVDPAQA IARANAILDE TAPRFEE // ID H0HY94_9RHIZ Unreviewed; 201 AA. AC H0HY94; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MAXJ12_25863; OS Mesorhizobium alhagi CCNWXJ12-2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1107882; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWXJ12-2; RX PubMed=22328758; DOI=10.1128/JB.06635-11; RA Zhou M., Chen W., Chen H., Wei G.; RT "Draft Genome Sequence of Mesorhizobium alhagi CCNWXJ12-2T, a Novel RT Salt-Resistant Species Isolated from the Desert of Northwestern RT China."; RL J. Bacteriol. 194:1261-1262(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHAM01000217; EHK54304.1; -; Genomic_DNA. DR EnsemblBacteria; EHK54304; EHK54304; MAXJ12_25863. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22705 MW; 7D6B5F40F27A865D CRC64; MRLDPFYLIV DSAAWIERLA PLGVRLVQLR IKDLDEARLR AEIRSAKVLC ARHRCQLIIN DYWRLAIEEG CDFIHLGQED MQAADLSRIK AAGLRLGLST HDHFELETAL AARPDYIALG PVYPTVLKQM KWAPQGLERI GEWKRRVATT PLVAIGGLNP ARLESVFAAG ADSAAVVTDI TLNADPEART REWIEKTKRW R // ID H0IFV8_MYCAB Unreviewed; 223 AA. AC H0IFV8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MMAS_41610, MMCCUG48898_4338; OS Mycobacterium abscessus subsp. bolletii CCUG 48898 = JCM 15300. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium abscessus. OX NCBI_TaxID=1001714; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 48898; RA Cho Y.-J., Choi G.E., Cho S.-N., Shin S.J.; RT "Draft Genome Sequence of Mycobacterium abscessus subsp. massiliense RT CCUG 48898."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 48898; RX PubMed=22965080; DOI=10.1128/JB.01200-12; RA Tettelin H., Sampaio E.P., Daugherty S.C., Hine E., Riley D.R., RA Sadzewicz L., Sengamalay N., Shefchek K., Su Q., Tallon L.J., RA Conville P., Olivier K.N., Holland S.M., Fraser C.M., Zelazny A.M.; RT "Genomic Insights into the Emerging Human Pathogen Mycobacterium RT massiliense."; RL J. Bacteriol. 194:5450-5450(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHAR01000015; EHM15781.1; -; Genomic_DNA. DR EMBL; AKVF01000005; EIV65421.1; -; Genomic_DNA. DR EnsemblBacteria; EHM15781; EHM15781; MMAS_41610. DR EnsemblBacteria; EIV65421; EIV65421; MMCCUG48898_4338. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23404 MW; 8D769164DD5CCE4C CRC64; MHSRSARLQS AHLYLCTDAR RERGDLAEFV DAALAGGVDI VQLRDKGSAG ERQFGRLEPT EELEYLAILS EAAARHGALF AVNDRADIAR AAGADVLHLG QDDLPLAVAR EIVGPDVLIG RSTHDAEQAA AAARDDEIDY FCCGPCWPTP TKPGRTAAGL GLVHAAAELG TSKPWFAIGG IDQARVPEVV EAGASRIVVV RAITAAADPR AAAASLRGST HRA // ID H0IU12_MYCAB Unreviewed; 223 AA. AC H0IU12; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MBOL_41030; OS Mycobacterium abscessus subsp. bolletii BD. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium abscessus. OX NCBI_TaxID=1091046; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BD; RX PubMed=22535937; DOI=10.1128/JB.00354-12; RA Choi G.E., Cho Y.J., Koh W.J., Chun J., Cho S.N., Shin S.J.; RT "Draft Genome Sequence of Mycobacterium abscessus subsp. bolletii RT BDT."; RL J. Bacteriol. 194:2756-2757(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHAS01000016; EHM17517.1; -; Genomic_DNA. DR EnsemblBacteria; EHM17517; EHM17517; MBOL_41030. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23503 MW; BE361FDD6D92FA6B CRC64; MHSRSARLQS AHLYLCTDAR RERGDFAEFV DAALAGGVDI VQLRDKGSAG ERQFGRLEPA EELEYLAILS EAAARHGALF AVNDRADIAR AAGADVLHLG QDDLPLAVAR EIVGPDVLIG RSTHDAEQAA AAARDDEIDY FCCGPCWPTP TKPGRTASGL GLVRTAAELG TSKPWFAIGG IDEARVPQVV EAGASRIVVV RAITAAADPR AAATSLRGST HRA // ID H0J2N1_9GAMM Unreviewed; 214 AA. AC H0J2N1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MOY_09457; OS Halomonas sp. GFAJ-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1118153; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GFAJ-1; RA Phung L.T., Silver S., Trimble W.L., Gilbert J.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GFAJ-1; RX PubMed=22408239; DOI=10.1128/JB.06664-11; RA Phung le T., Silver S., Trimble W.L., Gilbert J.A.; RT "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256)."; RL J. Bacteriol. 194:1835-1836(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHBC01000034; EHK60851.1; -; Genomic_DNA. DR EnsemblBacteria; EHK60851; EHK60851; MOY_09457. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 21912 MW; 3DDBA3696DE51963 CRC64; MPFDLSLYLV TDANLCASFG LEQTVAAAVQ GGVTIVQLRD KHASDAQMIA QAKRLKALLA GSGVPLIIND RLNVALESEA DGLHLGQSDT AVQEARQALG PNAIIGLSIN TLPQLQAAPV ELLDYVGLGP VFATGSKQDH AQPIGFDGLA QLAEVCPLPS VAIGGLKAEH AAHVKTAGAN GLAVISAICG QPDPRQAAQA FSAVEQTQEA GIPS // ID H0J2Y5_9GAMM Unreviewed; 318 AA. AC H0J2Y5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=MOY_09975; OS Halomonas sp. GFAJ-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1118153; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GFAJ-1; RA Phung L.T., Silver S., Trimble W.L., Gilbert J.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GFAJ-1; RX PubMed=22408239; DOI=10.1128/JB.06664-11; RA Phung le T., Silver S., Trimble W.L., Gilbert J.A.; RT "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256)."; RL J. Bacteriol. 194:1835-1836(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHBC01000038; EHK60582.1; -; Genomic_DNA. DR ProteinModelPortal; H0J2Y5; -. DR EnsemblBacteria; EHK60582; EHK60582; MOY_09975. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; SQ SEQUENCE 318 AA; 35584 MW; CCBF18F37E7A0CFA CRC64; MSVMVKRRVH VAAAAMISAD QKQVLIARRP SNVDHGGLWE FPGGKLAPYE TGLEGLKREL HEELGVEIVR ARPLIRIHHE YPDKHILLDV WQVQEFAGEP FGREGQAVRW VPMEELANYP FPAANLPILR AVMLPTDYLI TGEEADEERF EALLERALRE DGIRLVQLRA KELDTAAYLA RAERALALCR QHDARLVLNA DPALLDEVDA DGIHLTSERL MNIDRRPIAE SKWLSASTHD QAQLSKAAVL GCDFVTLSPL RTTPSHPEVA PLGWHDFQQL VERAGMPVFA LGGMTRFDAN HARAVGAQGI ASIRDFWK // ID H0JA21_9PSED Unreviewed; 209 AA. AC H0JA21; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PPL19_06320; OS Pseudomonas psychrotolerans L19. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1112217; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L19; RX PubMed=22374955; DOI=10.1128/JB.06786-11; RA Espirito Santo C., Lin Y., Hao X., Wei G., Rensing C., Grass G.; RT "Draft Genome Sequence of Pseudomonas psychrotolerans L19, Isolated RT from Copper Alloy Coins."; RL J. Bacteriol. 194:1623-1624(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHBD01000002; EHK72533.1; -; Genomic_DNA. DR EnsemblBacteria; EHK72533; EHK72533; PPL19_06320. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21837 MW; CF6D54E4B3D69596 CRC64; MSPLRGLYAI TDSALLAEGR LLPYVEAALQ GGTRLVQYRD KSGDASRRQD EAAALAELCR QHGAQLIIND DLALARRLGV GLHLGQEDGS LAAARAELGA DALLGGTCHA SLELAEAAAQ AGVSYLAFGR FFASSTKPDA PPAPLELLDQ ARRRFALPVC AIGGVTLNNA PLLLDHGVDL LAVVHSLFSA ASAGEVERRA RAFAQLFAA // ID H0JIZ2_9PSED Unreviewed; 315 AA. AC H0JIZ2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 13. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=PPL19_21685; OS Pseudomonas psychrotolerans L19. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1112217; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L19; RX PubMed=22374955; DOI=10.1128/JB.06786-11; RA Espirito Santo C., Lin Y., Hao X., Wei G., Rensing C., Grass G.; RT "Draft Genome Sequence of Pseudomonas psychrotolerans L19, Isolated RT from Copper Alloy Coins."; RL J. Bacteriol. 194:1623-1624(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHBD01000018; EHK68876.1; -; Genomic_DNA. DR EnsemblBacteria; EHK68876; EHK68876; PPL19_21685. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34135 MW; DC3BDB1689F8973A CRC64; MTRLHVVAAV IRDPQGRILI AQRPAHKHQG GLWEFPGGKV EAGEAPAAAL ARELAEELGI QVTRARPLLQ VRHDYPDQAV LLDVWQVDAF TGDAHGAEGQ PLAWVAPREL ADYDFPAANR PIVQAARLPE RYLITPGELT TAELLNGLHR ALDSGIRLVQ LRTPDNFDPQ YRDLAGDVQG LCTGRAQLML KGPLEWLGDF PAAGWHLTAE QLRRYAPNGR PFPEHRLLAA SCHDAEELAL AQQMGVDFVT LSPVMPTTSH PGAPTLGWVK AQQLLADCNL PAYLLGGLGE DDLTSAWQAG AQGVAAIRAF WPGGV // ID H0JVI9_9NOCA Unreviewed; 229 AA. AC H0JVI9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AK37_18628; OS Rhodococcus pyridinivorans AK37. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=1114960; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AK37; RA Kriszt B., Tancsics A., Cserhati M., Toth A., Nagy I., Horvath B., RA Tamura T., Kukolya J., Szoboszlay S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHBW01000053; EHK81802.1; -; Genomic_DNA. DR EnsemblBacteria; EHK81802; EHK81802; AK37_18628. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 49 53 HMP-PP binding (By similarity). FT REGION 156 158 THZ-P binding (By similarity). FT METAL 91 91 Magnesium (By similarity). FT METAL 110 110 Magnesium (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 159 159 HMP-PP (By similarity). FT BINDING 187 187 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 24261 MW; DFAB9EDC63EA05D7 CRC64; MTTYRGNHPD PRGRLATARL YLCTDARRDT GDLARFVEEA LAGGVDIVQL RDKDSAGEKK FGRLEAREEL AALEIIGEAC ARHGALLAVN DRADIALASG ADILHLGQGD LPVRHARQIL GDEIVIGRST SSRAQAALAD IEEGVDYFAS GPVWDTPTKP GRTAAGLEVT REVAQSQPAR PWFAIGGIDL ERLPEVLDAG ATRVAVVRAI TKASDPRAAA AALKAALPT // ID H0K4Y8_9PSEU Unreviewed; 229 AA. AC H0K4Y8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SZMC14600_10668; OS Saccharomonospora azurea SZMC 14600. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=1114959; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SZMC 14600; RA Csepregi K., Valasek A., Penzes A., Kiss E.I., Kerepesi I., RA Horvath B., Nagy I., Fekete C.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHBX01000085; EHK87397.1; -; Genomic_DNA. DR EnsemblBacteria; EHK87397; EHK87397; SZMC14600_10668. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 185 185 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 23785 MW; C641FBA47EC1DCC3 CRC64; MPGLDGDQIR KRLDDARLYL CTDARSERGD LAEFVDAALA GGVDIVQLRD KTGGAPLEAA HEIAALEVLA EACARHGALL AVNDRADVAL AVDADVLHLG QDDLPVATAR RVVGDAPVIG RSTHSPAQAR AAATEPGVDY FCVGPCWPTP TKPGRAAPGL DLVRTVATEI DPGLGTTRPW FAIGGIDLDR LDDVVAAGAR RAVVVRAITE ADDPTAAARA LHEGLTRAG // ID H0KLM5_BIFAN Unreviewed; 516 AA. AC H0KLM5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE SubName: Full=Phosphomethylpyrimidine kinase; GN ORFNames=FEM_14468; OS Bifidobacterium animalis subsp. lactis BS 01. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=911598; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BS 01; RA Mogna L., Deidda F.D., Mogna G.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHGW01000005; EHN17302.1; -; Genomic_DNA. DR ProteinModelPortal; H0KLM5; -. DR EnsemblBacteria; EHN17302; EHN17302; FEM_14468. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 516 AA; 54334 MW; BA2BECA74309264A CRC64; MNSFPYPSMR DRFDLRFYFV VGPDDCGNRP ILDVVAKALD GGASFIQLRA KTQDVAEIVS LANDIAEEIA GHHVEHSVAF VVDDRVDAAL EARAKGIKVD GVHIGQDDLD PVVARKLLGP DAIIGLSAKT VDEVREANHL PEGTIDYIGA GPLHMTATKP ESMIVDENGD ITTLNVSSID EMRTMSKYPL IVGGGVKADD IPMLAKTKAD GWFVVSAIAG ATDPEQATRR LVDDWTAIRG DEKPRYTGRK PAATKLPAVL TIATTDSSGG AGIPADLKTM LANDVFGECV VAGITAQNTT GVQAIAAVDP SIVGAQIDSV FDDIRPTAVK IGVIVGVESV KTVARKLRDH QATNIVVDPV MVATSGSSLA ADDTIAEEIS SLFPIATVIT PNIPEAQVLA QMPIGNQADM ETAAVQLAKD YGTCVLVKGG HGVKDADDVL AFPTGAVTWF EGERIANDNT HGTGCTLSSA IASYLAQGED LEDAVRDAKA YLSGALRANL NLGKGHGPMD HAWAMH // ID H0KXK8_9FLAO Unreviewed; 206 AA. AC H0KXK8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-MAR-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EAAG1_17846; OS Elizabethkingia anophelis Ag1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Elizabethkingia. OX NCBI_TaxID=1117646; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ag1; RX PubMed=24309745; RA Kukutla P., Lindberg B.G., Pei D., Rayl M., Yu W., Steritz M., RA Faye I., Xu J.; RT "Draft Genome Sequences of Elizabethkingia anophelis Strains R26T and RT Ag1 from the Midgut of the Malaria Mosquito Anopheles gambiae."; RL Genome Announc. 1:e01030-13(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHHG01000045; EHM96197.1; -; Genomic_DNA. DR EnsemblBacteria; EHM96197; EHM96197; EAAG1_17846. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22834 MW; 2A15813DB55D5954 CRC64; MLSKLQYISQ GVNAEEQERN ILKALLNGAD WIQIRWKNSD VELLQELCIK VQKHCREFGA QCIINDHVSI AKAIDADGVH LGLTDTTVTE ARSILGDHKI IGGTANTIED ICQRIDENCN YIGLGPFRFT TTKEKLSPIL GLEGYKNIFK HFQERQISLP PVFAIGGIQL EDICALKDVG LYGVAVSGLI ADNPELVSTI KIIFNE // ID H0KXK9_9FLAO Unreviewed; 204 AA. AC H0KXK9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-MAR-2014, entry version 12. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=EAAG1_17851; OS Elizabethkingia anophelis Ag1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Elizabethkingia. OX NCBI_TaxID=1117646; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ag1; RX PubMed=24309745; RA Kukutla P., Lindberg B.G., Pei D., Rayl M., Yu W., Steritz M., RA Faye I., Xu J.; RT "Draft Genome Sequences of Elizabethkingia anophelis Strains R26T and RT Ag1 from the Midgut of the Malaria Mosquito Anopheles gambiae."; RL Genome Announc. 1:e01030-13(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHHG01000045; EHM96198.1; -; Genomic_DNA. DR EnsemblBacteria; EHM96198; EHM96198; EAAG1_17851. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 204 AA; 23626 MW; 8D0615F0D61F49FA CRC64; MIIVLSPERE PEQEVYWINE LLAGGLDYFH VRKYWLSEEA MCSYISQINE DYRDRLILHS HYNLAEEFGI VRLHFREESR LNKEQVNFQG KYILSTSTHS IEEFNTLGKE WTYAFLSPVF PSISKQGYGA HCNVLNDLKQ RTNKNVQLVG LGGIDEHNID IVLKSGVDGV AMLGNIWQSS NPLQVFLNCK NKFLNQLQNQ NNVE // ID H0KY34_9FLAO Unreviewed; 212 AA. AC H0KY34; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-MAR-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EAAG1_18746; OS Elizabethkingia anophelis Ag1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Elizabethkingia. OX NCBI_TaxID=1117646; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ag1; RX PubMed=24309745; RA Kukutla P., Lindberg B.G., Pei D., Rayl M., Yu W., Steritz M., RA Faye I., Xu J.; RT "Draft Genome Sequences of Elizabethkingia anophelis Strains R26T and RT Ag1 from the Midgut of the Malaria Mosquito Anopheles gambiae."; RL Genome Announc. 1:e01030-13(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHHG01000051; EHM95984.1; -; Genomic_DNA. DR EnsemblBacteria; EHM95984; EHM95984; EAAG1_18746. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). SQ SEQUENCE 212 AA; 23596 MW; 6BCFC5EEE0F16049 CRC64; MSISSSFPYQ LYLVISEEAC KGKNFLEVAE ESILGGVDII QLREKHCTTA DFLRKAQQLK EITDKYNIPL IINDNSEVAK ALNTHGIHVG NNDISPVELR QQDFWKDKLI GYSIEYTEQL YNKHTQTSDY LGISPVFATA TKTDTVTEWG LEGIVKIRSI TTKPLVAIGN ISLQNAYDIV QAGADCIAVV SAICRANDPQ KAAYELKNKI LK // ID H0KZT5_SALMO Unreviewed; 211 AA. AC H0KZT5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM906_13936; OS Salmonella enterica subsp. enterica serovar Montevideo str. 80959-06. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=763922; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=80959-06; RA Allard M.W., Luo Y., Li C., Keys C.E., San I., Stones R., Musser S.M., RA Brown E.W.; RT "High Resolution Clustering of Salmonella enterica serovar Montevideo RT Strains Using a Next-Generation Sequencing Approach."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHHR01000003; EHN28303.1; -; Genomic_DNA. DR EnsemblBacteria; EHN28303; EHN28303; SEEM906_13936. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID H0LMX7_SALMO Unreviewed; 211 AA. AC H0LMX7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM5278_16481; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS CT_02035278. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=984240; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CT_02035278; RA Allard M.W., Luo Y., Li C., Keys C.E., San I., Stones R., Musser S.M., RA Brown E.W.; RT "High Resolution Clustering of Salmonella enterica serovar Montevideo RT Strains Using a Next-Generation Sequencing Approach."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHHS01000134; EHN18875.1; -; Genomic_DNA. DR EnsemblBacteria; EHN18875; EHN18875; SEEM5278_16481. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID H0LN55_SALMO Unreviewed; 211 AA. AC H0LN55; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM5318_06048; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS CT_02035318. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=984241; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CT_02035318; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHHT01000001; EHN29803.1; -; Genomic_DNA. DR EnsemblBacteria; EHN29803; EHN29803; SEEM5318_06048. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID H0M907_SALMO Unreviewed; 211 AA. AC H0M907; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM5320_14819; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS CT_02035320. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=984242; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CT_02035320; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHHU01000022; EHN33158.1; -; Genomic_DNA. DR EnsemblBacteria; EHN33158; EHN33158; SEEM5320_14819. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID H0MDY7_SALMO Unreviewed; 211 AA. AC H0MDY7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM5321_10382; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS CT_02035321. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=882860; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CT_02035321; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHHV01000002; EHN40002.1; -; Genomic_DNA. DR EnsemblBacteria; EHN40002; EHN40002; SEEM5321_10382. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID H0N1Z5_SALMO Unreviewed; 211 AA. AC H0N1Z5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM5327_07197; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS CT_02035327. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=882862; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CT_02035327; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHHW01000053; EHN41002.1; -; Genomic_DNA. DR EnsemblBacteria; EHN41002; EHN41002; SEEM5327_07197. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID H0NEE3_SALET Unreviewed; 211 AA. AC H0NEE3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEPO729_14979; OS Salmonella enterica subsp. enterica serovar Pomona str. ATCC 10729. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=941188; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10729; RX PubMed=22260654; DOI=10.1186/1471-2164-13-32; RA Allard M.W., Luo Y., Strain E., Li C., Keys C.E., Son I., Stones R., RA Musser S.M., Brown E.W.; RT "High resolution clustering of Salmonella enterica serovar Montevideo RT strains using a next-generation sequencing approach."; RL BMC Genomics 13:32-32(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHIA01000081; EHN42078.1; -; Genomic_DNA. DR ProteinModelPortal; H0NEE3; -. DR EnsemblBacteria; EHN42078; EHN42078; SEEPO729_14979. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22997 MW; 53EBA33604968A81 CRC64; MYQPDFPTVP FRLGLYPVVD SVQWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPSVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID H0NM96_BACCE Unreviewed; 219 AA. AC H0NM96; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BCN_0409; OS Bacillus cereus NC7401. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=334406; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NC7401; RX PubMed=22887669; DOI=10.1128/JB.01015-12; RA Takeno A., Okamoto A., Tori K., Oshima K., Hirakawa H., Toh H., RA Agata N., Yamada K., Ogasawara N., Hayashi T., Shimizu T., Kuhara S., RA Hattori M., Ohta M.; RT "Complete Genome Sequence of Bacillus cereus NC7401, Which Produces RT High Levels of the Emetic Toxin Cereulide."; RL J. Bacteriol. 194:4767-4768(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP007209; BAL16202.1; -; Genomic_DNA. DR RefSeq; YP_005102942.1; NC_016771.1. DR ProteinModelPortal; H0NM96; -. DR EnsemblBacteria; BAL16202; BAL16202; BCN_0409. DR GeneID; 11692179; -. DR KEGG; bnc:BCN_0409; -. DR KO; K00788; -. DR BioCyc; BCER334406:GJ71-475-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23583 MW; 9EF4BB9B5967DB91 CRC64; MSRISKSEMS RLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTEEKRIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKR LVEEVSNSL // ID H0NP18_BACCE Unreviewed; 206 AA. AC H0NP18; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Regulatory protein TenI; GN ORFNames=BCN_0707; OS Bacillus cereus NC7401. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=334406; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NC7401; RX PubMed=22887669; DOI=10.1128/JB.01015-12; RA Takeno A., Okamoto A., Tori K., Oshima K., Hirakawa H., Toh H., RA Agata N., Yamada K., Ogasawara N., Hayashi T., Shimizu T., Kuhara S., RA Hattori M., Ohta M.; RT "Complete Genome Sequence of Bacillus cereus NC7401, Which Produces RT High Levels of the Emetic Toxin Cereulide."; RL J. Bacteriol. 194:4767-4768(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP007209; BAL16500.1; -; Genomic_DNA. DR RefSeq; YP_005103240.1; NC_016771.1. DR ProteinModelPortal; H0NP18; -. DR EnsemblBacteria; BAL16500; BAL16500; BCN_0707. DR GeneID; 11692476; -. DR KEGG; bnc:BCN_0707; -. DR KO; K10810; -. DR BioCyc; BCER334406:GJ71-814-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22777 MW; 767D7D7B15B3A27E CRC64; MKNELHVISN GHMSFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK IVINDRIDIA ILLNIPRVQL GYRSADVRSV KEKFSYLHVG YSVHSLEEAI DAFKNGADSL VYGHVFPTDC KKGVPARGLE EISDIARCLS IPITAIGGIT PENTGDVLTN GVSGIAVMSG IISSSNPYSK AKSYKESIRK WAEKHV // ID H0P1K7_9SYNC Unreviewed; 343 AA. AC H0P1K7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SYNGTI_0407; OS Synechocystis sp. PCC 6803 substr. GT-I. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechocystis. OX NCBI_TaxID=1080228; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=22193367; DOI=10.1093/dnares/dsr042; RA Kanesaki Y., Shiwa Y., Tajima N., Suzuki M., Watanabe S., Sato N., RA Ikeuchi M., Yoshikawa H.; RT "Identification of substrain-specific mutations by massively parallel RT whole-genome resequencing of Synechocystis sp. PCC 6803."; RL DNA Res. 19:67-79(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012276; BAL28154.1; -; Genomic_DNA. DR RefSeq; YP_005382169.1; NC_017038.1. DR ProteinModelPortal; H0P1K7; -. DR EnsemblBacteria; BAL28154; BAL28154; SYNGTI_0407. DR GeneID; 11972820; -. DR KEGG; syt:SYNGTI_0407; -. DR KO; K00788; -. DR BioCyc; SSP1080228:GLM4-412-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 123 Unknown (By similarity). FT REGION 124 343 Thiamine-phosphate synthase (By FT similarity). FT REGION 171 175 HMP-PP binding (By similarity). FT REGION 268 270 THZ-P binding (By similarity). FT METAL 204 204 Magnesium (By similarity). FT METAL 223 223 Magnesium (By similarity). FT BINDING 203 203 HMP-PP (By similarity). FT BINDING 242 242 HMP-PP (By similarity). FT BINDING 271 271 HMP-PP (By similarity). FT BINDING 298 298 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 343 AA; 37883 MW; 84BE7074EC082056 CRC64; MQQASPTAIA RILDANLNRA REGLRTVEEW CRFALENREL AEECKQLRQA LAPWHQDDLR AARDTPNDVG TQLTHAQEAL RTDVRALLQA NLCRVEEALR VLEEYGKLRD PAMGACCKQL RYRVYALESG LLGSKLVQRL QQCSLYLVTS PQENLLATVE AALQGGLKLV QYRDKDAEDQ LRWQRAKDLR ELCRQYEALF LVNDRVDLAL AVDADGVHLG QQDLPIAVAR QLLGPDKIIG RSTTNPEEMA KAIAEGADYI GVGPVYATPT KAGKKPAGLE YVQYAVTNSP VPWFAIGGID GENLGEVMEA GATQVAIVRA IMETTNPTQA TAQLLTQLSR INP // ID H0PDX2_9SYNC Unreviewed; 343 AA. AC H0PDX2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SYNPCCN_0407; OS Synechocystis sp. PCC 6803 substr. PCC-N. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechocystis. OX NCBI_TaxID=1080229; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=22193367; DOI=10.1093/dnares/dsr042; RA Kanesaki Y., Shiwa Y., Tajima N., Suzuki M., Watanabe S., Sato N., RA Ikeuchi M., Yoshikawa H.; RT "Identification of substrain-specific mutations by massively parallel RT whole-genome resequencing of Synechocystis sp. PCC 6803."; RL DNA Res. 19:67-79(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012277; BAL31324.1; -; Genomic_DNA. DR RefSeq; YP_005408046.1; NC_017052.1. DR ProteinModelPortal; H0PDX2; -. DR EnsemblBacteria; BAL31324; BAL31324; SYNPCCN_0407. DR GeneID; 12013006; -. DR KEGG; sys:SYNPCCN_0407; -. DR KO; K00788; -. DR BioCyc; SSP1080229:GLM2-412-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 123 Unknown (By similarity). FT REGION 124 343 Thiamine-phosphate synthase (By FT similarity). FT REGION 171 175 HMP-PP binding (By similarity). FT REGION 268 270 THZ-P binding (By similarity). FT METAL 204 204 Magnesium (By similarity). FT METAL 223 223 Magnesium (By similarity). FT BINDING 203 203 HMP-PP (By similarity). FT BINDING 242 242 HMP-PP (By similarity). FT BINDING 271 271 HMP-PP (By similarity). FT BINDING 298 298 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 343 AA; 37883 MW; 84BE7074EC082056 CRC64; MQQASPTAIA RILDANLNRA REGLRTVEEW CRFALENREL AEECKQLRQA LAPWHQDDLR AARDTPNDVG TQLTHAQEAL RTDVRALLQA NLCRVEEALR VLEEYGKLRD PAMGACCKQL RYRVYALESG LLGSKLVQRL QQCSLYLVTS PQENLLATVE AALQGGLKLV QYRDKDAEDQ LRWQRAKDLR ELCRQYEALF LVNDRVDLAL AVDADGVHLG QQDLPIAVAR QLLGPDKIIG RSTTNPEEMA KAIAEGADYI GVGPVYATPT KAGKKPAGLE YVQYAVTNSP VPWFAIGGID GENLGEVMEA GATQVAIVRA IMETTNPTQA TAQLLTQLSR INP // ID H0PJP1_9SYNC Unreviewed; 343 AA. AC H0PJP1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SYNPCCP_0407; OS Synechocystis sp. PCC 6803 substr. PCC-P. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechocystis. OX NCBI_TaxID=1080230; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=22193367; DOI=10.1093/dnares/dsr042; RA Kanesaki Y., Shiwa Y., Tajima N., Suzuki M., Watanabe S., Sato N., RA Ikeuchi M., Yoshikawa H.; RT "Identification of substrain-specific mutations by massively parallel RT whole-genome resequencing of Synechocystis sp. PCC 6803."; RL DNA Res. 19:67-79(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012278; BAL34493.1; -; Genomic_DNA. DR RefSeq; YP_005385339.1; NC_017039.1. DR ProteinModelPortal; H0PJP1; -. DR EnsemblBacteria; BAL34493; BAL34493; SYNPCCP_0407. DR GeneID; 11976042; -. DR KEGG; syq:SYNPCCP_0407; -. DR KO; K00788; -. DR BioCyc; SSP1080230:GLM3-412-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 123 Unknown (By similarity). FT REGION 124 343 Thiamine-phosphate synthase (By FT similarity). FT REGION 171 175 HMP-PP binding (By similarity). FT REGION 268 270 THZ-P binding (By similarity). FT METAL 204 204 Magnesium (By similarity). FT METAL 223 223 Magnesium (By similarity). FT BINDING 203 203 HMP-PP (By similarity). FT BINDING 242 242 HMP-PP (By similarity). FT BINDING 271 271 HMP-PP (By similarity). FT BINDING 298 298 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 343 AA; 37883 MW; 84BE7074EC082056 CRC64; MQQASPTAIA RILDANLNRA REGLRTVEEW CRFALENREL AEECKQLRQA LAPWHQDDLR AARDTPNDVG TQLTHAQEAL RTDVRALLQA NLCRVEEALR VLEEYGKLRD PAMGACCKQL RYRVYALESG LLGSKLVQRL QQCSLYLVTS PQENLLATVE AALQGGLKLV QYRDKDAEDQ LRWQRAKDLR ELCRQYEALF LVNDRVDLAL AVDADGVHLG QQDLPIAVAR QLLGPDKIIG RSTTNPEEMA KAIAEGADYI GVGPVYATPT KAGKKPAGLE YVQYAVTNSP VPWFAIGGID GENLGEVMEA GATQVAIVRA IMETTNPTQA TAQLLTQLSR INP // ID H0PT74_9RHOO Unreviewed; 218 AA. AC H0PT74; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AZKH_3832; OS Azoarcus sp. KH32C. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azoarcus. OX NCBI_TaxID=748247; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KH32C; RA Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S., RA Senoo K.; RT "Complete genome sequence of Azoarcus sp. KH32C."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012304; BAL26116.1; -; Genomic_DNA. DR RefSeq; YP_007553092.1; NC_020516.1. DR EnsemblBacteria; BAL26116; BAL26116; AZKH_3832. DR GeneID; 14788206; -. DR KEGG; aza:AZKH_3832; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 22892 MW; 554892D7389A1C2B CRC64; MKRQRKRKAM TERKLRGLYL VTPDLADTAT LVELARRALE GRPALLQYRS KQPDAALRRE QAAALVQPCR DAGVPLIVND DLQLALAIGA DGAHLGRDDG DIAAARAALG PKRILGVTCY NEWARAETGL VAGADYVAFG AVFSSPTKPA AVHAPLALLT RAHLELRCPV AAIGGITLEN ASAVVAAGAD LLAVISDVFD APDPGARVAA YAALFEPV // ID H0PX14_9RHOO Unreviewed; 314 AA. AC H0PX14; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-JAN-2014, entry version 15. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=AZKH_0665; OS Azoarcus sp. KH32C. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azoarcus. OX NCBI_TaxID=748247; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KH32C; RA Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S., RA Senoo K.; RT "Complete genome sequence of Azoarcus sp. KH32C."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012304; BAL23006.1; -; Genomic_DNA. DR RefSeq; YP_007549982.1; NC_020516.1. DR ProteinModelPortal; H0PX14; -. DR EnsemblBacteria; BAL23006; BAL23006; AZKH_0665. DR GeneID; 14785178; -. DR KEGG; aza:AZKH_0665; -. DR KO; K03574; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 34429 MW; DC8FFFA21CA22508 CRC64; MKKRVDVAAG VIVRPDGRFL LGQRAPDTFY AGYWEFPGGK VEAGESPAAA LVRELDEELG IRVGKVYPWV TREHLYEHAH VRLHFFEVAE WEGTVSDHVH SALSWESMDR PAVGPMLPAN GPILKALRLP RWMGITQCAE MGVEGQLERL DAAFARGLRL VQVREPQMTT GDRLQLLQRV LERARSCDAT VVVNRDLEAA ARAGAHGVHL SADQLGELAE RPDFEWVGAS CHTRAELERA AALGLDYAVL GAVLPTRTHP GQPALGWERF EELVRDLPIP VLALGGVGPA DMDVARSHGA HGVAAIRASW DQSF // ID H0QFL1_ECOLI Unreviewed; 211 AA. AC H0QFL1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 14-MAY-2014, entry version 19. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECMDS42_3431; OS Escherichia coli str. K-12 substr. MDS42. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1110693; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K-12; RA Ying B.W., Seno S., Suzuki S., Yomo T.; RT "genome sequence of Escherichia coli str. K-12 substr. MDS42."; RL Submitted (NOV-2100) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012306; BAL40554.1; -; Genomic_DNA. DR RefSeq; YP_007558947.1; NC_020518.1. DR ProteinModelPortal; H0QFL1; -. DR SMR; H0QFL1; 20-202. DR EnsemblBacteria; BAL40554; BAL40554; ECMDS42_3431. DR GeneID; 14968318; -. DR KEGG; ecok:ECMDS42_3431; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H0QS34_ARTGO Unreviewed; 236 AA. AC H0QS34; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ARGLB_085_02040; OS Arthrobacter globiformis NBRC 12137. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1077972; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 12137; RA Miyazawa S., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Arthrobacter globiformis NBRC RT 12137."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAEG01000085; GAB15520.1; -; Genomic_DNA. DR EnsemblBacteria; GAB15520; GAB15520; ARGLB_085_02040. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 187 187 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 236 AA; 24768 MW; 1F5D738F192F323C CRC64; MVAMTQHSAH TAARLYLCTD ARKDRGDFAD FVDAAFAGGV DIIQLRDKSI EAAEELELLE VVHAAARRHG RLWAVNDRAD IASIAGAPVF HIGQKDLPLR AARKLLHDAT VIGLSTHSTD QVDAAIGAAH GRSGLDYFCV GPLWATPTKP GRAAVGLDLV RYAAEAVRTA NEERVGGLLL PWFAIGGIDR TNVEQVLAAG ASRIVVVRAI TDAADPAAAA AELLDALDAT APAAIS // ID H0QXT4_9ACTO Unreviewed; 222 AA. AC H0QXT4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GOEFS_036_00740; OS Gordonia effusa NBRC 100432. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1077974; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100432; RA Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., RA Yamazaki S., Fujita N.; RT "Whole genome shotgun sequence of Gordonia effusa NBRC 100432."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAEH01000036; GAB17635.1; -; Genomic_DNA. DR EnsemblBacteria; GAB17635; GAB17635; GOEFS_036_00740. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23523 MW; 34773BEE6DD6CA1A CRC64; MDLRARLSRA RLYLCTDARR ERGDLIEFVS AAIAGGVDIV QLRDKGSPGE REFGALEAGE ELQLLAKLRE VTEASGALLS VNDRADIAAA ARADVLHLGQ GDLPIAVARD IVGDDMIVGL STHDAEQARA AATAPGVDYF CVGPCWPTPT KPDRSAPGLG LVRTAASLDT DRPWFAIGGI DERRLPEVLD AGARRIVVVR AITHAPDAQV AARQLRSATA SV // ID H0RCP5_9ACTO Unreviewed; 233 AA. AC H0RCP5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GOPIP_031_04690; OS Gordonia polyisoprenivorans NBRC 16320. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1077976; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 16320; RA Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Gordonia polyisoprenivorans NBRC RT 16320."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAEI01000031; GAB22846.1; -; Genomic_DNA. DR EnsemblBacteria; GAB22846; GAB22846; GOPIP_031_04690. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 56 60 HMP-PP binding (By similarity). FT REGION 163 165 THZ-P binding (By similarity). FT METAL 98 98 Magnesium (By similarity). FT METAL 117 117 Magnesium (By similarity). FT BINDING 97 97 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 166 166 HMP-PP (By similarity). FT BINDING 192 192 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 24541 MW; 455F73E81AEEF5F1 CRC64; MPRENRIARD GDPTDDPRRA RLRAARLYLC TDARRERGDL LEFVDAALAG GVDLIQLRDK GSPGEREFGA LEAGEELAIL AEMRGVVDAH GALLSVNDRA DIALLAGADV LHLGQGDLRP EQARRIVGDD VIVGVSTHDP DQAHAAIADD AVDYFCVGPC WPTPTKPGRA APGLGLVREV AGVSKPWFAI GGIDSARLPE VRDAGARRAV VVRAITAADD PAAAAAQLRA GLA // ID H0S4Y7_9BRAD Unreviewed; 224 AA. AC H0S4Y7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase (Thiamin phosphate synthase/diphosphorylase); DE EC=2.5.1.3; GN ORFNames=BRAO285_590006; OS Bradyrhizobium sp. ORS 285. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=115808; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORS285; RA Rouy Z.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORS285; RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D., RA Smith A.A.T., Giraud E., Medigue C., Moulin L.; RT "Comparative Genomics of Aeschynomene Symbionts: Insights into the RT Ecological Lifestyle of Nod-Independent Photosynthetic RT Bradyrhizobia."; RL Genes (Basel) 3:35-61(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFH01000257; CCD89264.1; -; Genomic_DNA. DR EnsemblBacteria; CCD89264; CCD89264; BRAO285_590006. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 224 AA; 22855 MW; A8E95BAB15C215B8 CRC64; MSGKTTPARP EPRLYLATPV VTDAAALAAS LPAILASADV AAVLVRLKDS DPRSMITTVK TLAPAIQGTG AALLIDGHPD IVARAGADGA HLTGIAALEE ALPGLKPDRI AGGGGLSTRH DSMRAGEVGA DYVLFGERDA QGRRPSPDAV NERLAWWAEL FEPPCVGYAI SLKEAADFVA AGADFVLVDD LVWNDARGPA AALAEIGATI RQAHAAAPVA IAGS // ID H0S774_9BRAD Unreviewed; 202 AA. AC H0S774; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BRAO285_920006; OS Bradyrhizobium sp. ORS 285. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=115808; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORS285; RA Rouy Z.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORS285; RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D., RA Smith A.A.T., Giraud E., Medigue C., Moulin L.; RT "Comparative Genomics of Aeschynomene Symbionts: Insights into the RT Ecological Lifestyle of Nod-Independent Photosynthetic RT Bradyrhizobia."; RL Genes (Basel) 3:35-61(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFH01000294; CCD90051.1; -; Genomic_DNA. DR EnsemblBacteria; CCD90051; CCD90051; BRAO285_920006. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 29 33 HMP-PP binding (By similarity). FT REGION 178 179 THZ-P binding (By similarity). FT METAL 62 62 Magnesium (By similarity). FT METAL 81 81 Magnesium (By similarity). FT BINDING 61 61 HMP-PP (By similarity). FT BINDING 100 100 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 202 AA; 21574 MW; 3D275631032A3B72 CRC64; MPYPDRFYPV VDSLAWVERL TRLGVGTVQL RAKNLDDGQA LQIVTDALAI TKGTATKLIV NDYWRAAIVA GAEHVHLGQE DLAEADVKAI KDAGLTLGLS THDDAELETA LAAEPDYVAL GPIFPTTLKA MRFAPQGIPK ISVWKQRIGQ IPLVAIGGIK LEQAAEIFAA GADSIAVVSD VTQNADPDAR VRAWLDAAKE PA // ID H0SS96_9BRAD Unreviewed; 225 AA. AC H0SS96; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase (Thiamin phosphate synthase/diphosphorylase); DE EC=2.5.1.3; GN ORFNames=BRAO375_880001; OS Bradyrhizobium sp. ORS 375. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=566679; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORS375; RA Rouy Z.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORS375; RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D., RA Smith A.A.T., Giraud E., Medigue C., Moulin L.; RT "Comparative Genomics of Aeschynomene Symbionts: Insights into the RT Ecological Lifestyle of Nod-Independent Photosynthetic RT Bradyrhizobia."; RL Genes (Basel) 3:35-61(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFI01000485; CCD97073.1; -; Genomic_DNA. DR EnsemblBacteria; CCD97073; CCD97073; BRAO375_880001. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 225 AA; 23023 MW; 059E134B27DF7680 CRC64; MSGKTSPARP APRLYLATPV VTDAAALAAS LPAILASADV AAVLVRLKES DPRSMITAVK TMAPAIQSTG AALLIDGHAD IVARAGADGA HLTGIAALEE AMPGLKPDRI AGCGGLSTRH DSMRAGELGA DYVLFGERDA QGRRPSPDAV NERLAWWAEL FEPPCVGYAI SLKEAADFVA AGADFVLVDD LVWNDPRGPA AALAEIGATI RQAHATAPAA LAGQS // ID H0SSH3_9BRAD Unreviewed; 202 AA. AC H0SSH3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BRAO375_940001; OS Bradyrhizobium sp. ORS 375. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=566679; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORS375; RA Rouy Z.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORS375; RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D., RA Smith A.A.T., Giraud E., Medigue C., Moulin L.; RT "Comparative Genomics of Aeschynomene Symbionts: Insights into the RT Ecological Lifestyle of Nod-Independent Photosynthetic RT Bradyrhizobia."; RL Genes (Basel) 3:35-61(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFI01000492; CCD97150.1; -; Genomic_DNA. DR EnsemblBacteria; CCD97150; CCD97150; BRAO375_940001. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 29 33 HMP-PP binding (By similarity). FT REGION 178 179 THZ-P binding (By similarity). FT METAL 62 62 Magnesium (By similarity). FT METAL 81 81 Magnesium (By similarity). FT BINDING 61 61 HMP-PP (By similarity). FT BINDING 100 100 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 202 AA; 21577 MW; 3EDB5B9924013EC5 CRC64; MPYPDRFYPV VDSLAWVERL TKLGVGTVQL RAKDLNDGEA LQIVTDALAI TKGTATRLIV NDYWRAAIVA GAEHVHLGQE DLADADVKAI KDAGLTLGLS THDDAELETA LAAEPDYVAL GPIFPTTLKA MRFAPQGIPK IAVWKQRVGN IPLVAIGGIK LEQATEIFAA GADSIAVVSD VTQNADPDAR VRAWLDATKE PA // ID H0SUH7_9BRAD Unreviewed; 72 AA. AC H0SUH7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine phosphate pyrophosphorylase (Thiamin phosphate synthase/diphosphorylase); DE EC=2.5.1.3; GN ORFNames=BRAS3809_1420009; OS Bradyrhizobium sp. STM 3809. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=551936; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STM 3809; RA Rouy Z.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STM 3809; RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D., RA Smith A.A.T., Giraud E., Medigue C., Moulin L.; RT "Comparative Genomics of Aeschynomene Symbionts: Insights into the RT Ecological Lifestyle of Nod-Independent Photosynthetic RT Bradyrhizobia."; RL Genes (Basel) 3:35-61(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFJ01000049; CCD97854.1; -; Genomic_DNA. DR EnsemblBacteria; CCD97854; CCD97854; BRAS3809_1420009. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 72 AA; 7631 MW; A33E639C66945D19 CRC64; MRFAPQGIAK ISVWKQRVGK IPLVAIGGIK LDQAAEIFAA GADSIAVVSD VTQNADPDSR VRAWLDATKE PA // ID H0T8R7_9BRAD Unreviewed; 224 AA. AC H0T8R7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase (Thiamin phosphate synthase/diphosphorylase); DE EC=2.5.1.3; GN ORFNames=BRAS3809_6640015; OS Bradyrhizobium sp. STM 3809. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=551936; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STM 3809; RA Rouy Z.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STM 3809; RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D., RA Smith A.A.T., Giraud E., Medigue C., Moulin L.; RT "Comparative Genomics of Aeschynomene Symbionts: Insights into the RT Ecological Lifestyle of Nod-Independent Photosynthetic RT Bradyrhizobia."; RL Genes (Basel) 3:35-61(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFJ01000628; CCE02844.1; -; Genomic_DNA. DR EnsemblBacteria; CCE02844; CCE02844; BRAS3809_6640015. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 224 AA; 23054 MW; 269DD816D1883F74 CRC64; MSGKTTPARP EPRLYLATPV VTDAAALAAS LPAILASADV AAVLVRLEES DPRSMITAVK TLAPAIQKTG AALLIDGHPD IVARSGADGA HLTGIAALEE ALPGLKPDRI AGGGGLSTRH DSMRAGEIGA DYVLFGERDA QGRRPSPDAV NERLAWWAEL FEPPCVGYAI SLKEAADFVA AGADFVLVDD LVWNDERGPA AALADIGATI RQAYATAPVA VAGN // ID H0TEU9_9BRAD Unreviewed; 202 AA. AC H0TEU9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BRAS3843_1210018; OS Bradyrhizobium sp. STM 3843. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=551947; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STM 3843; RA Rouy Z.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STM 3843; RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D., RA Smith A.A.T., Giraud E., Medigue C., Moulin L.; RT "Comparative Genomics of Aeschynomene Symbionts: Insights into the RT Ecological Lifestyle of Nod-Independent Photosynthetic RT Bradyrhizobia."; RL Genes (Basel) 3:35-61(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFK01000026; CCE04987.1; -; Genomic_DNA. DR EnsemblBacteria; CCE04987; CCE04987; BRAS3843_1210018. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 29 33 HMP-PP binding (By similarity). FT REGION 178 179 THZ-P binding (By similarity). FT METAL 62 62 Magnesium (By similarity). FT METAL 81 81 Magnesium (By similarity). FT BINDING 61 61 HMP-PP (By similarity). FT BINDING 100 100 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 202 AA; 21720 MW; 2C55BA1D11CAFBDE CRC64; MPYPDKFYPV VDTLAWVERL TKLGVGTVQL RAKNLNDGEA LQIVTDALAI TKGTKTKLIV NDYWRAAVVA GAEHLHLGQE DLADADVVAI RQAGLTLGLS THDDEELATA LAAEPDYIAL GPIFPTTLKS MRFAPQGIPK ITEWKRRIGN IPLVAIGGIK LEQAADIFAA GADSIAVVSD VTQNPDPDAR VRAWLELTAE TA // ID H0TLI3_9BRAD Unreviewed; 225 AA. AC H0TLI3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase (Thiamin phosphate synthase/diphosphorylase); DE EC=2.5.1.3; GN ORFNames=BRAS3843_2050013; OS Bradyrhizobium sp. STM 3843. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=551947; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STM 3843; RA Rouy Z.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=STM 3843; RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D., RA Smith A.A.T., Giraud E., Medigue C., Moulin L.; RT "Comparative Genomics of Aeschynomene Symbionts: Insights into the RT Ecological Lifestyle of Nod-Independent Photosynthetic RT Bradyrhizobia."; RL Genes (Basel) 3:35-61(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFK01000119; CCE07321.1; -; Genomic_DNA. DR EnsemblBacteria; CCE07321; CCE07321; BRAS3843_2050013. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 225 AA; 23365 MW; 68E37BAEC36E818B CRC64; MAGKTTPPRP APRLYLATPV ITDPAPLAAE LPSILRGGDV AAVLVRLKES DPRSMIRCVK ALAPAIQDAG AALLVEGHAD IVARAGADGA HLNGLAALDE ALPGLKPDRI AGIGGLATRH DSMTAGERGT DYVLFGEKDA AGRRPSVDAI VERLSWWAEL FEPPCVGYAA TREEATEFVA AGADFILVDD LVWNDPRGPA AALADIDSAI KQAYMAVPTA AAGQE // ID H0U7G4_BRELA Unreviewed; 227 AA. AC H0U7G4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BLGI_1322; OS Brevibacillus laterosporus GI-9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=1118154; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GI-9; RA Sharma V., Singh P.K., Midha S., Ranjan M., Korpole S., Patil P.B.; RT "Genome Sequence of Brevibacillus laterosporus Strain GI-9."; RL J. Bacteriol. 194:1279-1279(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGD01000004; CCF13408.1; -; Genomic_DNA. DR EnsemblBacteria; CCF13408; CCF13408; BLGI_1322. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 24638 MW; 248C111E314DB1D9 CRC64; MKLARLALLS QKWSIYLVIG SQDCGNSVEN MFRILTEALQ AGVGCVQWRE KGAGSISDVI QREQIAIRMK KLCHTYDAIF LINDDVSLAC KVQADGVHVG HEDMPFVQVK QLVPPEMIIG ISAGNIEEAR LALTYGADYL GVGPMYTSKS KTDAGEPIGP NGLSAIRKFV GGYPIVAIGG IKLEHVSCLR KNGADAIAVI SAITQAPDTK KAVQDFIYHV HKNHNYT // ID H0U7G8_BRELA Unreviewed; 229 AA. AC H0U7G8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI family protein; GN Name=tenI; ORFNames=BLGI_1326; OS Brevibacillus laterosporus GI-9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=1118154; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GI-9; RA Sharma V., Singh P.K., Midha S., Ranjan M., Korpole S., Patil P.B.; RT "Genome Sequence of Brevibacillus laterosporus Strain GI-9."; RL J. Bacteriol. 194:1279-1279(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGD01000004; CCF13412.1; -; Genomic_DNA. DR EnsemblBacteria; CCF13412; CCF13412; BLGI_1326. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 229 AA; 25395 MW; 6A4FB2AC81A415D3 CRC64; MRARSLHLIT TGRQALREVL PIIEKADQAG VDYLHIREKQ RTARELAEWI RLLSDVFPRD RIIVNDRVDV AMAYHCGGVQ LGQQSLHASL AGRMLASHQL LGCSVHNDQE CLSLQSLQPS DQYDSLTEHD FVPSRPPTFV IAGHVFVTEC KPGLEPRGLP FVTRMRKLLA PSISLLAIGG ITPNRVKDVI AAGADGIAVM SGIMQSAQPK ERMKEYRDQL DKTAENAIQ // ID H0UN21_9BACT Unreviewed; 214 AA. AC H0UN21; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TheveDRAFT_0112; OS Thermanaerovibrio velox DSM 12556. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Thermanaerovibrio. OX NCBI_TaxID=926567; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 12556; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Teshima H., Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Brambilla E.-M., Klenk H.-P., Eisen J.A.; RT "The Noncontiguous Finished genome of Thermanaerovibrio velox DSM RT 12556."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001377; EHM09300.1; -; Genomic_DNA. DR EnsemblBacteria; EHM09300; EHM09300; TheveDRAFT_0112. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 21897 MW; 81CBFA557EE91D16 CRC64; MLNRGDLGRR LAVYGILDSS LGGAEELVRL GALGAAKGVK ALQLRCKGFD GMDMYRIARD LVEACGPFGC LILVNDRLDV ALAAKAHGVH LGHRDIPIGE ARRIAPEGFI IGATARTPEE AARAEADGAS YIGSGAAFPS STKNDTVLIG PSGIARVARA VRIPCVAIGG INEDNLRALE GTGIAGIAMC GGLFGAGGMR GEAIAGALEV LGHR // ID H1APC6_9FIRM Unreviewed; 206 AA. AC H1APC6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0978_02774; OS Coprobacillus sp. 8_2_54BFAA. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Coprobacillus. OX NCBI_TaxID=469597; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=8_2_54BFAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Coprobacillus sp. 8_2_54BFAA."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTG01000010; EHQ45428.1; -; Genomic_DNA. DR ProteinModelPortal; H1APC6; -. DR EnsemblBacteria; EHQ45428; EHQ45428; HMPREF0978_02774. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22313 MW; C0B809C8F5673F8B CRC64; MLELYLVSDR SWLNDRPLEE DIEQAILGGV TMVQLREKNL TDEEFTIQAK KVKTICSKYH IPFIINDNVA VALAVDSDGI HIGQDDQPVK RVRKIIGPHK IIGVSAHNLK EALAAKEDGA DYLGVGAMFN TSTKDDATAV SFTQLHEITT KIGLPVVAIG GINQDNCLLL KGTKIDGIAV VSAIMSAPDI KEAAAKLKAH ARGIYD // ID H1AYF1_9FIRM Unreviewed; 209 AA. AC H1AYF1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0982_02308; OS Erysipelotrichaceae bacterium 21_3. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=658657; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21_3; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Erysipelotrichaceae bacterium 21_3."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTI01000023; EHO26110.1; -; Genomic_DNA. DR EnsemblBacteria; EHO26110; EHO26110; HMPREF0982_02308. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22591 MW; 18EAD723C8CEC452 CRC64; MRFDLTLYLV SDSTGLSEDE FLRRLEQALR GGVTLLQLRE KNRTTLEYYE LARKVKKLTD AYGVPLMIDD RVDIALAVDA AGVHVGAEDM PVREARRLMG PDKIVGATAK RVDTAMQAEA DGADYLGVGA IYPTTTKVKT VLTSVETLQD ICAHVSIPVG AIGGLNAENC EILKGTGIKG ICVVSAIMKQ ENSYDAAKAL KAKIMTICK // ID H1BBR3_9FIRM Unreviewed; 209 AA. AC H1BBR3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0981_02646; OS Erysipelotrichaceae bacterium 6_1_45. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=469614; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_45; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Erysipelotrichaceae bacterium 6_1_45."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTK01000043; EHO26256.1; -; Genomic_DNA. DR EnsemblBacteria; EHO26256; EHO26256; HMPREF0981_02646. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22591 MW; 18EAD723C8CEC452 CRC64; MRFDLTLYLV SDSTGLSEDE FLRRLEQALR GGVTLLQLRE KNRTTLEYYE LARKVKKLTD AYGVPLMIDD RVDIALAVDA AGVHVGAEDM PVREARRLMG PDKIVGATAK RVDTAMQAEA DGADYLGVGA IYPTTTKVKT VLTSVETLQD ICAHVSIPVG AIGGLNAENC EILKGTGIKG ICVVSAIMKQ ENSYDAAKAL KAKIMTICK // ID H1C613_ECOLX Unreviewed; 211 AA. AC H1C613; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0986_05197; OS Escherichia coli 4_1_47FAA. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1127356; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_1_47FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli 4_1_47FAA."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTQ01000086; EHP62785.1; -; Genomic_DNA. DR EnsemblBacteria; EHP62785; EHP62785; HMPREF0986_05197. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23034 MW; 4EC571B19EAAAE13 CRC64; MYQPDFPPVP FRLGLYPVVD SAQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAITLGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVMATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H1CLG6_9FIRM Unreviewed; 199 AA. AC H1CLG6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF0995_05294; OS Lachnospiraceae bacterium 7_1_58FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658087; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_1_58FAA; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 7_1_58FAA."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTW01000120; EHO23260.1; -; Genomic_DNA. DR EnsemblBacteria; EHO23260; EHO23260; HMPREF0995_05294. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 21463 MW; ECAACC56CC363D6E CRC64; MSDILCVTSR SLCREDFLTR LERVAAAGPA GVILREKDLP PEDYRALAER ALALCRARGV PCILHSFPET AEALGERAIH LPLPLLRALP PERRGAFRVL GTSCHSVEDA REAEKLGCTY ITAGHVFATD CKKGLAPRGL DFLRAVCRAV DLPVWAIGGI TPENFPSVRA AGARGGCVMS GLMTCADPAA LLERFARRD // ID H1CR17_CLOPF Unreviewed; 207 AA. AC H1CR17; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9476_00988; OS Clostridium perfringens WAL-14572. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=742739; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-14572; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., RA Summanen P.H., Molitoris D.R., Daigneault M., Vaisanen M.-L., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium perfringens WAL-14572."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLP01000004; EHP49535.1; -; Genomic_DNA. DR ProteinModelPortal; H1CR17; -. DR EnsemblBacteria; EHP49535; EHP49535; HMPREF9476_00988. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22794 MW; ADE9A2301814122F CRC64; MSNKDTKKLY LVTDYRIPFN ELLEKTKEAL IGGVSIVQYR AKNKKTKEMC KEAKELKKLC DDFGALFLVN DRIDVALAVK ANGVHIGQDD MEVSIAREIM PKDAVIGVTV HNKEEALKAI KEGADNLGVG ALFSTNSKDD ATLMTLETLR EIKSVSNIPL YGIGGIAPEK LNKDILENLD GVAVISSLLN SDNIREKSNE FLNILSK // ID H1CRJ4_CLOPF Unreviewed; 193 AA. AC H1CRJ4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF9476_01254; OS Clostridium perfringens WAL-14572. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=742739; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-14572; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., RA Summanen P.H., Molitoris D.R., Daigneault M., Vaisanen M.-L., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium perfringens WAL-14572."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLP01000005; EHP49211.1; -; Genomic_DNA. DR EnsemblBacteria; EHP49211; EHP49211; HMPREF9476_01254. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 193 AA; 21957 MW; DC9CAB0EA5262A41 CRC64; MFLITNRKLV NRERYFNTIE EAGKYGVKNI ILREKDLSTE ELIEVYIKIK ELVPEETNII INSNIEAARI LKEKFIHLSF NDFKRNLEEI KSLKVGVSVH SILEALEADR LGASYILVSP IFETQCKKGV IPKGVDFIKE IKEKVNCKVI ALGGINEHNF KEVLGAGADD FACMSLLFMS NNIKKSLDTF KAF // ID H1D2A0_9FIRM Unreviewed; 211 AA. AC H1D2A0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9453_01738; OS Dialister succinatiphilus YIT 11850. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Dialister. OX NCBI_TaxID=742743; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11850; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Dunbar C., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Dialister succinatiphilus YIT 11850."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLT01000054; EHO62366.1; -; Genomic_DNA. DR EnsemblBacteria; EHO62366; EHO62366; HMPREF9453_01738. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23011 MW; 831EF43D4F9CFA2A CRC64; MRKIDYRLYL VTDRKQPAPG TFEKVVEEAL KGGVTLVQLR EKEGDTGLLY ERAVKLKQIT KAYHVPLIID DRIDIMMAAD ADGVHLGQSD MPAALARKLI GEDKIMGVSA GTLEEAVKAE KDGADYLGVG AMFPTATKKD ADITTPETLR KIMDTVHIPV VTIGGMNERT IPLFKGYGLS GFAVVSAIMA SREPEKAAKN LKRIIDDIVG R // ID H1D455_9FUSO Unreviewed; 212 AA. AC H1D455; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9466_00283; OS Fusobacterium necrophorum subsp. funduliforme 1_1_36S. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=742814; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_36S; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium necrophorum 1_1_36S."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLZ01000003; EHO21908.1; -; Genomic_DNA. DR ProteinModelPortal; H1D455; -. DR EnsemblBacteria; EHO21908; EHO21908; HMPREF9466_00283. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23831 MW; 1361BA57B2490DF2 CRC64; MRKRIEIPKG IYGITGDNFS HGKSNLECVK AMIEGGIRII QYRDKIKSMR EKYQEAKEIA KLCKENKVLF IVNDHVDLAL LVDADGVHIG QDDYPVEEVR SLLGPDKIIG LSTHSPKQGL EAFQNENVDY IGVGPIFPTT TKDTKAVGLE YLDFAIKNLS LPFVAIGGIH EHNLQEILTR NVSRFCMVSG IVGAENIMKT VKKLYKQWEE TQ // ID H1DF19_9PORP Unreviewed; 652 AA. AC H1DF19; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF9449_00855; OS Odoribacter laneus YIT 12061. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Odoribacter. OX NCBI_TaxID=742817; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12061; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G., RA Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., RA Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Odoribacter laneus YIT 12061."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMC01000014; EHP49337.1; -; Genomic_DNA. DR EnsemblBacteria; EHP49337; EHP49337; HMPREF9449_00855. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 652 AA; 73877 MW; 2064DD35548D8EAD CRC64; MLTILITSPF FISEETTICN LLFDYGLDLL HLRKPGADRT VFENFIQKIR PCYRNRIVLH DFYELVAIYH LRGIHLKSTQ RDKIGMYENF SHISISCHTV AEIKTLPATV TYCFLSPVFD SLSKPDYYSP FRELPEITEA KLPLPVIALG GITPDKIRLC QRAGFAGVAV LGYIWERPQE AVMRFRDLKT PTVFSIAGFD PSGGAGITAD LKTFESCSVY GRGILSALTF QNEKEYLATK NFCLEEIIRQ LELQFRYAIP SFIKIGLLPD QEILFSLTRY LTQKVPDIKI IWDPILRTSS GFTFHTSLSL PDHFLRQLFL ITPNTEELHQ LFGENLCISD LQKLCKKYQF HLLWKGGHNA EEISVDRLIG PDTLHCFPVE RSIYQKHGTG CILSAAITAY LARGISLVEA CRKAQVYVSR FMDSNDSLLG YHLPVPLKNI PLPSTLRLQY ITDYKEGWTI GEQVEAVCQG GVRWIQLRMK KNSKAEILQT GRLIKEICRY YNALFIVNDQ VEIARQLDAD GVHLGLEDMN PEEARKILGP DKIIGATCNT MEDIRLRAIQ KVDYIGLGPF RYTTTKQKLS PVLGVEGYQK ILHSMSREGI SIPVFAIGGI QDADFIPLLQ TGIQGIALSG LIKNSPDIKQ KVREIRKELE SI // ID H1DZ08_ECOLX Unreviewed; 211 AA. AC H1DZ08; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ESNG_04391; OS Escherichia coli B093. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=550674; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B093; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli B093."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXF01000101; EHO04523.1; -; Genomic_DNA. DR EnsemblBacteria; EHO04523; EHO04523; ESNG_04391. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23112 MW; 3AEB04EE6C1929DE CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLDAIRT AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLVDYP TVAIGGISLP RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGAGD E // ID H1DZL0_ECOLX Unreviewed; 78 AA. AC H1DZL0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 14-MAY-2014, entry version 10. DE SubName: Full=Uncharacterized protein; DE Flags: Fragment; GN ORFNames=ESNG_04593; OS Escherichia coli B093. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=550674; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B093; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli B093."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXF01000112; EHO04274.1; -; Genomic_DNA. DR EnsemblBacteria; EHO04274; EHO04274; ESNG_04593. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. PE 4: Predicted; FT NON_TER 1 1 SQ SEQUENCE 78 AA; 8083 MW; F547B85278FDAFE6 CRC64; FPSSAFGPQY IKALKAVLPP DIAVFAVGGV TPENLAQWID AGCAGAGLGS DLYRAGQSVE RTAQQAAAFV KAYREAVQ // ID H1E0D8_ECOLX Unreviewed; 75 AA. AC H1E0D8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 14-MAY-2014, entry version 8. DE SubName: Full=Uncharacterized protein; DE Flags: Fragment; GN ORFNames=ESNG_04871; OS Escherichia coli B093. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=550674; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B093; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli B093."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXF01000160; EHO03524.1; -; Genomic_DNA. DR EnsemblBacteria; EHO03524; EHO03524; ESNG_04871. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. PE 4: Predicted; FT NON_TER 1 1 SQ SEQUENCE 75 AA; 7780 MW; 51C99F34A421722B CRC64; SAFGPQYIKA LKAVLPPDIA VFAVGGVTPE NLAQWIDAGC AGAGLGSDLY RAGQSVERTA RQAAAFVKAY REAVQ // ID H1ECX3_ECOLX Unreviewed; 211 AA. AC H1ECX3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ESOG_04352; OS Escherichia coli E101. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=550685; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E101; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli E101."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXG01000031; EHN96137.1; -; Genomic_DNA. DR EnsemblBacteria; EHN96137; EHN96137; ESOG_04352. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23045 MW; 95B3B23110333A9C CRC64; MYQPDFPPVP FRLGLYPVVD SVHWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR HYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H1ETK1_ECOLX Unreviewed; 211 AA. AC H1ETK1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ESPG_04915; OS Escherichia coli H397. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656398; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H397; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli H397."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXH01000088; EHN90378.1; -; Genomic_DNA. DR ProteinModelPortal; H1ETK1; -. DR SMR; H1ETK1; 9-208. DR EnsemblBacteria; EHN90378; EHN90378; ESPG_04915. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H1FD41_ECOLX Unreviewed; 211 AA. AC H1FD41; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ESQG_04814; OS Escherichia coli H494. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656405; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H494; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J., Griggs A., RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli H494."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQH01000088; EHN80505.1; -; Genomic_DNA. DR ProteinModelPortal; H1FD41; -. DR SMR; H1FD41; 20-202. DR EnsemblBacteria; EHN80505; EHN80505; ESQG_04814. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H1FQT3_ECOLX Unreviewed; 211 AA. AC H1FQT3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ESRG_04395; OS Escherichia coli TA124. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656435; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA124; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J., Griggs A., RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli TA124."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQI01000072; EHN81304.1; -; Genomic_DNA. DR EnsemblBacteria; EHN81304; EHN81304; ESRG_04395. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22924 MW; FB7070BF941936B8 CRC64; MYQPDFPPVP FHLGLYPVVD SVQWIERLLD AGVLTLQLRI KDRRDEEAEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H1G0T4_9GAMM Unreviewed; 315 AA. AC H1G0T4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Mutator MutT protein; GN ORFNames=ECTPHS_01934; OS Ectothiorhodospira sp. PHS-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Ectothiorhodospira. OX NCBI_TaxID=519989; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PHS-1; RA Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V., RA Hoeft S., Oremland R.S., Stolz J.; RT "ArxA, a new clade of arsenite oxidase within the DMSO family of RT molybdenum oxidoreductases."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGBG01000003; EHQ51421.1; -; Genomic_DNA. DR ProteinModelPortal; H1G0T4; -. DR EnsemblBacteria; EHQ51421; EHQ51421; ECTPHS_01934. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 33977 MW; E55C2837F546C907 CRC64; MAVAAITNAR DEYLIARRPA HVHQGGLWEF PGGKIESGES LADALRRELR EELDITPLRH HPLITLNHDY PDRRVCLEVV KVDRFEGEPR GMEGQPLRWV AADHLHALAF PAANRAIIQA LTLPDRLLIT PDLRCPDTLL NGLHRTLETA GPALLQLRAP RLSREAFAAL AEAVIPLCRS RGTRVVLNAD PELAVSLGAD GVHLNARRLA TLAGRPDVLD RLTLVGASAH HRDELAHAAR LGAHFVLVSP VAPTRTHPGT SVLGWPGFAA LAREAGRPAY ALGGMTVDDI ATARHHGGQG IAGIRGLWQG ATEAD // ID H1G112_9GAMM Unreviewed; 195 AA. AC H1G112; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECTPHS_02334; OS Ectothiorhodospira sp. PHS-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Ectothiorhodospira. OX NCBI_TaxID=519989; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PHS-1; RA Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V., RA Hoeft S., Oremland R.S., Stolz J.; RT "ArxA, a new clade of arsenite oxidase within the DMSO family of RT molybdenum oxidoreductases."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGBG01000003; EHQ51499.1; -; Genomic_DNA. DR EnsemblBacteria; EHQ51499; EHQ51499; ECTPHS_02334. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 27 31 HMP-PP binding (By similarity). FT REGION 125 127 THZ-P binding (By similarity). FT METAL 60 60 Magnesium (By similarity). FT METAL 79 79 Magnesium (By similarity). FT BINDING 59 59 HMP-PP (By similarity). FT BINDING 98 98 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 155 155 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 195 AA; 20543 MW; 72F24D3DD0FA0E87 CRC64; MITPQDAGDT LLEQAAAALT GGARILQYRD KSRDHDRRLA ESRALCRLCR HHQALFIVND DVALAARVEA DGVHIGSDDG DIATARALIG PERIIGVSCY NRLELARRAE AAGADYVAFG ALFPSGTKPA AVHAPLSLIR EARQSLAVPI TAIGGITQDN ADTVIQAGAH MLAVIQGVFS APDIRAAAAD LSARF // ID H1GAC0_LISIO Unreviewed; 214 AA. AC H1GAC0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0557_00955; OS Listeria innocua ATCC 33091. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1002366; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33091; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGCN01000017; EHN61936.1; -; Genomic_DNA. DR EnsemblBacteria; EHN61936; EHN61936; HMPREF0557_00955. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22531 MW; 577F29D2BC8C3B52 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALKCQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAA EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRQA GIKLPIVGIG GINETNSAEV LTAGAEGVSV ISAITRSEDC QSVIKQLKNP GYPS // ID H1GPC5_9FLAO Unreviewed; 210 AA. AC H1GPC5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF9712_02898; OS Myroides odoratimimus CCUG 10230. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Myroides. OX NCBI_TaxID=883150; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 10230; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Myroides odoratimimus CCUG 10230."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEC02000027; EHO06693.1; -; Genomic_DNA. DR EnsemblBacteria; EHO06693; EHO06693; HMPREF9712_02898. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 210 AA; 24485 MW; 14F8AD363393A39E CRC64; MVVITYPTPI ENETSLINKM FEKGLPLLHV RKPNMSYEEL VKWVNNIDNY YHPYLVIHIP TIVINNNEHV FKQYKALINK INSTYTHLST TDCLYVNNYS VELPKLSTSV HCISEVNKLS TNIDRAFISP IYPSISKRGY VSTIDWTEEL KQRTNNRVTL VALGGITPFH IESIHTMGFD DYALLGTIWE AEQPLKQFEL CQYYDQLHWQ // ID H1GPC7_9FLAO Unreviewed; 206 AA. AC H1GPC7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9712_02900; OS Myroides odoratimimus CCUG 10230. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Myroides. OX NCBI_TaxID=883150; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 10230; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Myroides odoratimimus CCUG 10230."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEC02000027; EHO06695.1; -; Genomic_DNA. DR EnsemblBacteria; EHO06695; EHO06695; HMPREF9712_02900. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22954 MW; E20D1EC49578F167 CRC64; MLNKIQYISH GDTPQEQLYH IETVLGAGQQ WIQYRFKNTT NTTLWQTAEQ VKKLCEQYQA TLIINDHVDL AKAIEADGVH LGLTDLSITQ AKAYLPNKII GGTANTIEDI QLRHAEGCDY IGLGPYRFTT TKQKLSPILG LAGYQQLLKQ MQELDINIPV VAIGGIQLED VEDLKQAGLH GIAISGLLQN STDKKTLLQQ LNYILK // ID H1H149_9FLAO Unreviewed; 210 AA. AC H1H149; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF9714_03427; OS Myroides odoratimimus CCUG 12901. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Myroides. OX NCBI_TaxID=883152; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 12901; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J., Griggs A., RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Myroides odoratimimus CCUG 12901."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGED01000052; EHO05064.1; -; Genomic_DNA. DR EnsemblBacteria; EHO05064; EHO05064; HMPREF9714_03427. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 210 AA; 24482 MW; 75715E95C6BD8C28 CRC64; MVVITYPTPI ENETSLINKM FEKGLPLLHV RKPNMPFEEL VKWVNNIDNY YHQYLVIHIP TIVINNNEHV FKQYKALINK INSTYTHLST TNCLYVNNYS VELPKLSTSV HCISEVNKLS TSIDRAFISP IYPSISKRGY VSTIDWTEEL KQRTNNRVTL VALGGITPFH IESIHTMGFD DYALLGTIWE AEQPLKQFEL CQYYDQLHWQ // ID H1H151_9FLAO Unreviewed; 206 AA. AC H1H151; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9714_03429; OS Myroides odoratimimus CCUG 12901. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Myroides. OX NCBI_TaxID=883152; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 12901; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J., Griggs A., RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Myroides odoratimimus CCUG 12901."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGED01000052; EHO05066.1; -; Genomic_DNA. DR EnsemblBacteria; EHO05066; EHO05066; HMPREF9714_03429. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22954 MW; 19ED1EC49578EAC6 CRC64; MLNKIQYISH GDTPQEQLYH IETVLGAGQQ WIQYRFKNTT NTTLWQTAEQ VKKLCEQYQA TLIINDHVDL AKAIEADGVH LGLTDLSITQ AKAYLPNKII GGTANTIEDI QLRHAEGCDY IGLGPYRFTT TKQKLSPILG LAGYQQLLKQ MQELDINIPV VAIGGIQLED VEDLKKAGLH GIAISGLLQN STDKKTLLQQ LNYILK // ID H1HB73_9FLAO Unreviewed; 206 AA. AC H1HB73; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9715_03361; OS Myroides odoratimimus CIP 101113. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Myroides. OX NCBI_TaxID=883154; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 101113; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J., Griggs A., RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Myroides odoratimimus CIP 101113."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEE01000058; EHO05291.1; -; Genomic_DNA. DR EnsemblBacteria; EHO05291; EHO05291; HMPREF9715_03361. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22917 MW; 4802EB39C415500C CRC64; MLNKIQYISH GDTPQEQLYH IENVLGAGQQ WIQYRFKNTT NTTLWQTAEQ VKKLCEQYQA TLIINDHVDL AKAIEADGVH LGLTDLSITQ AKAYLPNKII GGTANTIEDI QLRHAEGCDY IGLGPYRFTT TKQKLSPILG LAGYQQLLKQ MQELNINIPV VAIGGIQLED VEDLKQAGLH GIAISGLLQN STDKKTLLQQ LNNILK // ID H1HB75_9FLAO Unreviewed; 210 AA. AC H1HB75; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-MAR-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=HMPREF9715_03363; OS Myroides odoratimimus CIP 101113. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Myroides. OX NCBI_TaxID=883154; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 101113; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J., Griggs A., RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Myroides odoratimimus CIP 101113."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEE01000058; EHO05293.1; -; Genomic_DNA. DR EnsemblBacteria; EHO05293; EHO05293; HMPREF9715_03363. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 210 AA; 24508 MW; 87A6F251F1FE4A22 CRC64; MVVITYPTPI ENETSLINKM FEKGLPLLHV RKPNMPFEEL VKWVNNIDNY YHPYLVIHIP TIVINNNEHV FKQYKALINK INSTYTHLST TNCLYVNNYS VELPKLSTSV HCISEVNKLS TNIDRAFISP IYPSISKRGY VSTIDWTEEL KQRTNNRVTL VALGGITPFH IESIHTMGFD DYTLLGTIWE AEQPLKQFEL CQYYDQLHWQ // ID H1HGS7_FUSNU Unreviewed; 206 AA. AC H1HGS7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9942_01678; OS Fusobacterium nucleatum subsp. animalis F0419. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=999414; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OT 420; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M., RA Mathney J., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., RA Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., RA Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium nucleatum subsp. animalis OT RT 420."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEH01000023; EHO76548.1; -; Genomic_DNA. DR EnsemblBacteria; EHO76548; EHO76548; HMPREF9942_01678. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22761 MW; 01E1724308467D77 CRC64; MDLKDCKIYL VTDEKSCNGK DFYKCIEEAI KGGVKIVQLR EKTLSTKDFF IKALKIKEIC KSYGVLFIIN DRLDIAQAVE ADGVHLGQSD MPIEKAREIL KDKFLIGATA RNIEEAKKAE LLGADYIGSG AIFGTSTKDN AKKLEIEDLK KIVNSVKIPV FAIGGININN VWMLKNIGLQ GVCSVSGILS EKDCKKAVEN ILKNFN // ID H1HGT3_FUSNU Unreviewed; 206 AA. AC H1HGT3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 13-NOV-2013, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HMPREF9942_01684; OS Fusobacterium nucleatum subsp. animalis F0419. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=999414; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OT 420; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M., RA Mathney J., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., RA Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., RA Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium nucleatum subsp. animalis OT RT 420."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEH01000023; EHO76554.1; -; Genomic_DNA. DR EnsemblBacteria; EHO76554; EHO76554; HMPREF9942_01684. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 24022 MW; ADF93866473BAADF CRC64; MIENKIKLNI ISNRKLCENE NLEKQIEKIF SAYQRKIILE NFEIVALTLR EKDLYKNEYL KLVEKIYPIC QKYRIDLILH QNYNLRLDNK YNIKGLHLSY NTFKSLNKNI REELIRKYKK IGVSIHSINE AKEVENLGAN YVVAGHIFKT DCKKDLEPRG LKFIQELSVI LTIPIFAIGG INQENSHLVI NSGAFGVCMM SSLMKD // ID H1HS42_9FIRM Unreviewed; 208 AA. AC H1HS42; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9623_00412; OS Stomatobaculum longum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Stomatobaculum. OX NCBI_TaxID=796942; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACC2; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A., RA Epstein S., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium ACC2."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEL01000003; EHO18228.1; -; Genomic_DNA. DR EnsemblBacteria; EHO18228; EHO18228; HMPREF9623_00412. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22182 MW; D144D9A3DC2D8E37 CRC64; MRLYAVTDRT WVGKQSLAGQ VAAALRGGVT CVQLREKELD EEQFLREAEE IFSLCKGYRV PFFINDNVAL ALRCHADGVH VGQDDMDVAA VRRLVGQEMM IGVSVHTVEE ARAAAEGGAD YLGVGAMFAT STKTDASLVT KETLRAICDA VSIPVVAIGG INKSNLLELA GTGVDGVALV SAIFSAADIT AECRLLYGLS QEMTELEK // ID H1KJL3_METEX Unreviewed; 167 AA. AC H1KJL3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN ORFNames=MetexDRAFT_2825; OS Methylobacterium extorquens DSM 13060. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=882800; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13060; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Koskimaki J., Halonen O., RA Pirttila A., Frank C., Woyke T.J.; RT "The draft genome of Methylobacterium extorquens DSM 13060."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGJK01000068; EHP92309.1; -; Genomic_DNA. DR EnsemblBacteria; EHP92309; EHP92309; MetexDRAFT_2825. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; FT NON_TER 1 1 SQ SEQUENCE 167 AA; 17376 MW; 9795DFE5305966A1 CRC64; SLVALVKRLA PPAQERGAAV LVSVPGFTGD IVSVAARGGA DGVHLDRADE EALRDLRGRL RDGRILGTGG VLGSRNAAMV AGETGVDYLM VGGLFPDGVA PDAEEVRERA AWWAEIFETP CIAVATSAED VAALVLTGSE FVGLESALWL DDPEGVRAAQ AQLDRAR // ID H1KLQ1_METEX Unreviewed; 241 AA. AC H1KLQ1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MetexDRAFT_3563; OS Methylobacterium extorquens DSM 13060. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=882800; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13060; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Koskimaki J., Halonen O., RA Pirttila A., Frank C., Woyke T.J.; RT "The draft genome of Methylobacterium extorquens DSM 13060."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGJK01000103; EHP91566.1; -; Genomic_DNA. DR ProteinModelPortal; H1KLQ1; -. DR EnsemblBacteria; EHP91566; EHP91566; MetexDRAFT_3563. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT METAL 87 87 Magnesium (By similarity). FT METAL 106 106 Magnesium (By similarity). FT BINDING 86 86 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 241 AA; 24468 MW; 0265DCCA37059A80 CRC64; MGSGTGLGLS RPSAGVALDL RLYGILDVGV LGGDATALAT LAAEAVAGGA TLLQYRDKDL TDARAALARI RAIHAALAGR APLLVNDRVD LALAAGVEGV HLGQSDLHPE DARRLLGPRA IIGLTVKTGA QADELYRLPI DYACIGGVFA TTSKDNPDPP VGLDGLQRIV FRARLARGQS LPLGAIAGID ASNTASVIRA GADGVALIGA LFKGGATEAK ARDLLARVDE ALGQRGSTGT R // ID H1KQV1_METEX Unreviewed; 205 AA. AC H1KQV1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MetexDRAFT_5014; OS Methylobacterium extorquens DSM 13060. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=882800; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13060; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Koskimaki J., Halonen O., RA Pirttila A., Frank C., Woyke T.J.; RT "The draft genome of Methylobacterium extorquens DSM 13060."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGJK01000211; EHP90111.1; -; Genomic_DNA. DR ProteinModelPortal; H1KQV1; -. DR EnsemblBacteria; EHP90111; EHP90111; MetexDRAFT_5014. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT REGION 134 136 THZ-P binding (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 20364 MW; 801781346B1F380C CRC64; MTLPPLLVVT DRHGAARPLT ETVRAAVAGG ARFVWLRDRD LDRDARRDLA RDLIGLLQPV GGRLVVGGDT DLAAEIGAQG VHLSSSAGID GIRAARMALG AAALIGFSAH SVAEIAAAGA AGADYATLSP IFPTASKPGY GPALGLASLR AAAAHGVPVF ALGGIDGGNA RACREAGAAG VAVMGGVMRG SDPRAATGRF VAALT // ID H1L618_GEOME Unreviewed; 497 AA. AC H1L618; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE SubName: Full=Phosphomethylpyrimidine kinase; GN ORFNames=GeomeDRAFT_1465; OS Geobacter metallireducens RCH3. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=691164; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RCH3; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Chakraborty R., Arkin A., Dehal P., RA Wall J., Hazen T., Woyke T.J.; RT "The draft genome of Geobacter metallireducens RCH3."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGJM01000011; EHP87126.1; -; Genomic_DNA. DR ProteinModelPortal; H1L618; -. DR EnsemblBacteria; EHP87126; EHP87126; GeomeDRAFT_1465. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 497 AA; 52391 MW; D89049C6DDF85AD1 CRC64; MGSNGHNLRL VVNRDKQDSP IRGVYLVTDH GDRLAERVEA AIDGGVRIVQ YRNKGKDRAQ RYAVGEELRD LCSRRGVIFI VNDDLDLALQ LKADGIHLGQ EDGDPRIARR ELGPGRIIGV STHTMEEALA AQAAGADYIG FGAMFPTNSK EIGHLAGPEG LAAIRSRIMI PIVAIGGISR DNGPRVVDAG ADALAVISAV LAHPDPFLAA TELGLLFNRR APHPRGAVLT IAGSDSGGGA GIQADLKTAT LLGSYGSSVI TALTAQNTRG VSGIHGVPPS FVAEQLDAVL SDIPVDTVKT GMLFSAEIIA TVADKLAEYR KRIVVVDPVM VAKGGAPLID RGAVNVLKDR LMPRTYLLTP NIPEAERLTG LTIVDEEGMQ EAARRLFRLG ARNVLVKGGH LVAGDAVDIL FDGSAFHRFT APRILSKNTH GTGCTYAAAI ATYLAQGEPL REAVGRAKEF VTAAIRLGQP LGRGHGPVNH LLAALEVGDQ GPGTGDR // ID H1L644_GEOME Unreviewed; 213 AA. AC H1L644; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GeomeDRAFT_1491; OS Geobacter metallireducens RCH3. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=691164; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RCH3; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Chakraborty R., Arkin A., Dehal P., RA Wall J., Hazen T., Woyke T.J.; RT "The draft genome of Geobacter metallireducens RCH3."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGJM01000011; EHP87152.1; -; Genomic_DNA. DR ProteinModelPortal; H1L644; -. DR EnsemblBacteria; EHP87152; EHP87152; GeomeDRAFT_1491. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22401 MW; E17325CD5B0F037E CRC64; MSKVDFSLYL ITDRRQTTGR DLPAVVEEAL AGGVRAVQLR EKDLSSRELL ELARVMRELT GRYGAKLIIN DRVDIALATD ADGVHLGEAS IPADAARRIL GAHRLIGVSC HNREGALAAE KSGADFITFG PVYPTPSKAA YGAPVGVERL AEAAALLTIP VFALGGIKGD NIPEVLATGA AGVALISAVI AAVNPNEEAR AILTLLEQGR RTE // ID H1LDY5_9LACO Unreviewed; 217 AA. AC H1LDY5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9104_00811; OS Lactobacillus kisonensis F0435. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=797516; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0435; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGRJ01000083; EHO52897.1; -; Genomic_DNA. DR EnsemblBacteria; EHO52897; EHO52897; HMPREF9104_00811. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23399 MW; 09B4BFB959DD69EE CRC64; MEMKFETAML RSYFIAGTQD IKDERPLEEV LKQALEAGIT AFQYREKGPT SLTGSQKLEL GQRLKVLCAD YQIPFIVDDD VDLAIKTRAD GIHVGQKDER VTSVIDQVGN QMFVGLSCDT PDQIQVANQI AGISYIGSGP VFPTGSKADA DPVIGVDGLA QLVKVSKLPV VAIGGITEDN ITELPKTGVA GTSVISMIAQ SDDIFRTVKT MNQTFSD // ID H1LQS4_9PAST Unreviewed; 226 AA. AC H1LQS4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9096_01650; OS Haemophilus sp. oral taxon 851 str. F0397. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=762965; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0397; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGRK01000033; EHO45795.1; -; Genomic_DNA. DR EnsemblBacteria; EHO45795; EHO45795; HMPREF9096_01650. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24849 MW; 65320BBB2DEFEEBD CRC64; MKNIQEILPL YFVAGTQDCR HLGDNPADNL LSVLRQALEG GITCFQFRDK GKFSLENSPD EQRSLAIKCR DLCRQYNVPF IVDDNVDLAL EIEADGIHVG QSDTPVKTIR AKTNKPLIIG WSVNRLDEAR IGEELSEIDY FGVGPIFTTQ SKENPSPTLG MEFIQTLRNG GITKPLVAIG GIKLEHVKPL RKYGADGVAV ITAITQANNI KSATQALKEE SNIVNS // ID H1PKG1_9FIRM Unreviewed; 184 AA. AC H1PKG1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=HMPREF0380_00669; OS Eubacterium infirmum F0142. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XIII. Incertae Sedis. OX NCBI_TaxID=883109; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0142; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A., RA Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G., RA Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., RA Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Eubacterium infirmum F0142."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGWI01000008; EHO86377.1; -; Genomic_DNA. DR EnsemblBacteria; EHO86377; EHO86377; HMPREF0380_00669. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 184 AA; 20386 MW; 9E7F3F84C5ED0650 CRC64; MSTFKKIAVT NRSLCSAGLE EQVEKICRSS LCDALILREK DLGEQEYMNL AMPIKGICDK HRVDFFCNSM PKVSDELGCG LQLSYQSFLE QNGEKDAYIW VSIHTVEEAV NAEKLGANAL IAGHIFMTDC KKGLAPRGLD FLKDICRAVS IPVFAIGGID DSNSEAVKLA GAQGECRMSW YMRY // ID H1PKW9_9FIRM Unreviewed; 213 AA. AC H1PKW9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0380_00827; OS Eubacterium infirmum F0142. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XIII. Incertae Sedis. OX NCBI_TaxID=883109; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0142; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A., RA Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G., RA Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., RA Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Eubacterium infirmum F0142."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGWI01000011; EHO85703.1; -; Genomic_DNA. DR EnsemblBacteria; EHO85703; EHO85703; HMPREF0380_00827. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23121 MW; 9E2C8BA2E3520572 CRC64; MKFDKRDLLV YAITDEKRRS NKEWEKLLIP IFEAGIRILQ LRQKHASHEE FVNSARELVE ICHRFGAKLI VNDDAGTCIE AGADGVHLGQ DDMPIAEARK LLGDEYIIGA TAHNLDEAEK AEADGADYVG VGAAFGSNSK LDARPIELAD YRKISDKITI PMVAIGGINP ENIDLLSGSG ADGVAVISAL FANDDIREAA DVLMAKSRSL FGN // ID H1PSZ0_9FUSO Unreviewed; 211 AA. AC H1PSZ0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF0402_01533; OS Fusobacterium ulcerans 12-1B. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=457404; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=12_1B; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium ulcerans 12_1B."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGWJ02000012; EHO81681.1; -; Genomic_DNA. DR EnsemblBacteria; EHO81681; EHO81681; HMPREF0402_01533. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23380 MW; CB099C3C72455AF0 CRC64; MRNRIDIPEG LYGITGDNFA NGKSNYQCVE EMIKGGIKIV QYRDKRKNSR EKVEEAGAIR ELCRKNNVLF IVNDDVAIAM LVDADGVHVG QEDMKPSDVR KLLGENKIIG LSTHSEEQGM AAYNDIDVDY IGVGPIFPTT TKDTAPVGLG YLEFAVKNLH LPFIAIGGIK DYNIDEIIKR GAKRICLVSD IVGAEDICKK IIDLNNKILK K // ID H1QDA8_9ACTO Unreviewed; 113 AA. AC H1QDA8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase/TENI subfamily; DE Flags: Fragment; GN ORFNames=SMCF_2886; OS Streptomyces coelicoflavus ZG0656. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1120227; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZG0656; RX PubMed=22691180; DOI=10.1111/j.1472-765X.2012.03274.x; RA Guo X., Geng P., Bai F., Bai G., Sun T., Li X., Shi L., Zhong Q.; RT "Draft genome sequence of Streptomyces coelicoflavus ZG0656 reveals RT the putative biosynthetic gene cluster of acarviostatin family ?- RT amylase inhibitors."; RL Lett. Appl. Microbiol. 55:162-169(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHGS01000326; EHN77588.1; -; Genomic_DNA. DR EnsemblBacteria; EHN77588; EHN77588; SMCF_2886. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; FT NON_TER 113 113 SQ SEQUENCE 113 AA; 11990 MW; CD4E6FBEE10BA540 CRC64; MILPAGYSDD ARMIWDAATA LNRAAAAVSP AAARLPPLLF FTDPARTPRP WETAARLPPG SAVVYRAFGA DQALEIGRRL RAVTREAGVE LLVGKDADLA DAVSADGLHL PER // ID H1QPL3_9ACTO Unreviewed; 223 AA. AC H1QPL3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SMCF_6932; OS Streptomyces coelicoflavus ZG0656. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1120227; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZG0656; RX PubMed=22691180; DOI=10.1111/j.1472-765X.2012.03274.x; RA Guo X., Geng P., Bai F., Bai G., Sun T., Li X., Shi L., Zhong Q.; RT "Draft genome sequence of Streptomyces coelicoflavus ZG0656 reveals RT the putative biosynthetic gene cluster of acarviostatin family ?- RT amylase inhibitors."; RL Lett. Appl. Microbiol. 55:162-169(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHGS01001425; EHN73639.1; -; Genomic_DNA. DR EnsemblBacteria; EHN73639; EHN73639; SMCF_6932. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23392 MW; 3CFAE3823985EE32 CRC64; MPDTAPTTAR ARLAGARLYL CTDARRSQGD LPEFLDAVLA GGVDIVQLRD KGMEAAEELE HLKVFADACA RHGKLLAVND RADVAHAARA DVLHLGQGDL PVPAARAILG DDVLVGRSTH AESEAAAAAV QHGVDYFCTG PCWPTPTKPG RHAPGLDLVR YTAALGTDRP WFAIGGIDLG NLDEVLDAGA RRVVVVRAIT AAEDPGAAAA EFAKRLRQAP ARG // ID H1QV91_ALIFS Unreviewed; 219 AA. AC H1QV91; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VFSR5_0037; OS Vibrio fischeri SR5. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=1088719; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SR5; RX PubMed=22374964; DOI=10.1128/JB.06825-11; RA Gyllborg M.C., Sahl J.W., Cronin D.C.III., Rasko D.A., Mandel M.J.; RT "Draft Genome Sequence of Vibrio fischeri SR5, a Strain Isolated from RT the Light Organ of the Mediterranean Squid Sepiola robusta."; RL J. Bacteriol. 194:1639-1639(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHIH01000001; EHN71414.1; -; Genomic_DNA. DR EnsemblBacteria; EHN71414; EHN71414; VFSR5_0037. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006162; PPantetheine_attach_site. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24226 MW; D938677684CA0456 CRC64; MFAFPNIDKS KFGLYPVVDD VSWIEKLLKL DVKTIQLRIK NPEQADLEQQ IIKAIRLGRE YDAQVFINDY WQLAIKHNAF GIHLGQEDIE VADLQAIAEA NICLGLSTHD DSELLKVKAL NPSYLALGHI FPTPTKEMPS QPQGLTNLAK NQQLAGDTPT VAIGGIDLSV ANDVWQTGVD SIAVVRAITE AEDTEQAVAK FNDIISEPRR GNLSEVVHE // ID H1REI7_SALMO Unreviewed; 211 AA. AC H1REI7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEM8286_00080; OS Salmonella enterica subsp. enterica serovar Montevideo str. OS IA_2010008286. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=882868; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IA_2010008286; RA Allard M.W., Luo Y., Li C., Keys C.E., San I., Stones R., Musser S.M., RA Brown E.W.; RT "High Resolution Clustering of Salmonella enterica serovar Montevideo RT Strains Using a Next-Generation Sequencing Approach."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHIK01000018; EHP18968.1; -; Genomic_DNA. DR EnsemblBacteria; EHP18968; EHP18968; SEEM8286_00080. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23006 MW; 4610A3395E9E6602 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID H1RSJ7_COMTE Unreviewed; 313 AA. AC H1RSJ7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CTATCC11996_16065; OS Comamonas testosteroni ATCC 11996. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=1009852; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11996; RX PubMed=22374961; DOI=10.1128/JB.06795-11; RA Gong W., Kisiela M., Schilhabel M.B., Xiong G., Maser E.; RT "Genome Sequence of Comamonas testosteroni ATCC 11996, a RT Representative Strain Involved in Steroid Degradation."; RL J. Bacteriol. 194:1633-1634(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHIL01000035; EHN64759.1; -; Genomic_DNA. DR EnsemblBacteria; EHN64759; EHN64759; CTATCC11996_16065. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 137 141 HMP-PP binding (By similarity). FT METAL 170 170 Magnesium (By similarity). FT METAL 189 189 Magnesium (By similarity). FT BINDING 169 169 HMP-PP (By similarity). FT BINDING 211 211 HMP-PP (By similarity). FT BINDING 240 240 HMP-PP (By similarity). FT BINDING 269 269 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 313 AA; 33454 MW; 91FF5F553C7682B5 CRC64; MDSAEIKALA QAIIHQHSAN FGAQLHHDAN SVELTPQPVP PALRQDPAYL AALEACSELG FIAVDAQTLA QAWQRQSERT DQFDVTHWPD DPRDFGLGKA DPALAFAHCP RELGLYGVLP TAEWVGRMAR AGVPTVQLRF KSGDRAAVAQ EVKAAVEAVK GTQARLFIND HWQAALDAGA YGIHVGQEDL DVIGQRDLQT IRSSGTRLGV STHGYAEMVR AHAVQPSYIA LGAVFPTTLK KMATAPQGLA RLAAYVRLMQ QYPLVAIGGI SEDLFPAVRA TGVGSVAVVR ALVNAPDPEA AARHLLARMQ AAA // ID H1SF01_9BURK Unreviewed; 377 AA. AC H1SF01; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=OR16_34503; OS Cupriavidus basilensis OR16. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=1127483; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OR16; RX PubMed=22461549; DOI=10.1128/JB.06752-11; RA Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A., RA Nagy I., Horvath B., Nagy I., Kukolya J.; RT "De Novo Genome Project of Cupriavidus basilensis OR16."; RL J. Bacteriol. 194:2109-2110(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHJE01000103; EHP38946.1; -; Genomic_DNA. DR EnsemblBacteria; EHP38946; EHP38946; OR16_34503. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 377 AA; 39674 MW; A9332618A7EE7F1F CRC64; MTRNLLPAGI DAALRDTLLA RYGATFGISD KTWRAWARGD VPAALGDADV ALFDGEADAA TLARIAAAGA IAIESDREGG QWSDTVRSPM GTWVFSAHAD DDTAHSPAFV AVLLACLALH FPAHDALCLA RAWQPGSLDW PVDFARFPHV RHAALVAPEQ RAEPFAPCPP LGLYAVVPSA EWIERLVALA LPTVQLRFKS DDAQAVRSEI ERAAKAARGS ASRLFINDHW RAAIDYHASQ GGDSGIYGIH LGQEDLDDAD LDALRACGLR LGVSTHGYAE MLRVATIGPS YLALGAIFPT TTKVMPTAPQ GLGRFHAYVK LMQPVVPSLV GIGGVDAARL PEVLAAGVGS AAVVRAITEA ADVPAAVTNL LGMFPAA // ID H1SQE3_STAAU Unreviewed; 213 AA. AC H1SQE3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21252_1722; OS Staphylococcus aureus subsp. aureus 21252. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904743; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21252; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHJV01000045; EHO88577.1; -; Genomic_DNA. DR EnsemblBacteria; EHO88577; EHO88577; SA21252_1722. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23325 MW; 8756AC9C9EE9DE8A CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF LNN // ID H1STQ9_STAAU Unreviewed; 213 AA. AC H1STQ9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21262_1471; OS Staphylococcus aureus subsp. aureus 21262. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904745; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21262; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHJW01000027; EHO92168.1; -; Genomic_DNA. DR EnsemblBacteria; EHO92168; EHO92168; SA21262_1471. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23374 MW; 5FCFB1B12D19C187 CRC64; MFNQSYLNVY FICGTSDVPS HRTVHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHRYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H1SZ77_STAAU Unreviewed; 213 AA. AC H1SZ77; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21264_2743; OS Staphylococcus aureus subsp. aureus 21264. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904746; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21264; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHJX01000001; EHO94729.1; -; Genomic_DNA. DR ProteinModelPortal; H1SZ77; -. DR EnsemblBacteria; EHO94729; EHO94729; SA21264_2743. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H1TB57_STAAU Unreviewed; 213 AA. AC H1TB57; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21272_2063; OS Staphylococcus aureus subsp. aureus 21272. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904750; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21272; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHJY01000021; EHO97653.1; -; Genomic_DNA. DR ProteinModelPortal; H1TB57; -. DR SMR; H1TB57; 4-209. DR PRIDE; H1TB57; -. DR EnsemblBacteria; EHO97653; EHO97653; SA21272_2063. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H1TJT6_STAAU Unreviewed; 213 AA. AC H1TJT6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21283_1560; OS Staphylococcus aureus subsp. aureus 21283. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904754; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21283; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHJZ01000099; EHO97710.1; -; Genomic_DNA. DR ProteinModelPortal; H1TJT6; -. DR SMR; H1TJT6; 4-209. DR PRIDE; H1TJT6; -. DR EnsemblBacteria; EHO97710; EHO97710; SA21283_1560. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H1TNM0_STAAU Unreviewed; 213 AA. AC H1TNM0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21333_0032; OS Staphylococcus aureus subsp. aureus 21333. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904767; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21333; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKA01000008; EHP01190.1; -; Genomic_DNA. DR ProteinModelPortal; H1TNM0; -. DR EnsemblBacteria; EHP01190; EHP01190; SA21333_0032. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23428 MW; 72CEFFE40BF6349B CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLET ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PKMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H1UF02_ACEPA Unreviewed; 201 AA. AC H1UF02; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APT_0723; OS Acetobacter pasteurianus NBRC 101655. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=1006554; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 101655; RA Matsutani M., Hirakawa H., Saichana N., Soemphol W., Yakushi T., RA Matsushita K.; RT "Genome-wide phylogenetic analysis of differences in thermotolerance RT among closely related Acetobacter pasteurianus strains."; RL Microbiology (Mosc.) 158:229-239(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BACF01000005; GAB27233.1; -; Genomic_DNA. DR ProteinModelPortal; H1UF02; -. DR EnsemblBacteria; GAB27233; GAB27233; APT_0723. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 22025 MW; 95A7C6BC567B0FD6 CRC64; MTALPQKIYP VVDSATWVDR LGGAGARFIQ LRLKDMEEDA LRAEIRQGHA YAKQHGVCLV LNDYWQIALD EGIDYIHLGQ EDLDTADLAA IRKGGIRLGI STHCHEELDR ALSCNPDYVA LGPIWETKLK KMAFGPQGPL KLTEWRKLIG NLPLVAIGGI TLERAWACIE AGADSVSAVS AFIRQPDPEG QVKAWLAAVE G // ID H1UHR4_ACEPA Unreviewed; 190 AA. AC H1UHR4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APT_1685; OS Acetobacter pasteurianus NBRC 101655. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=1006554; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 101655; RA Matsutani M., Hirakawa H., Saichana N., Soemphol W., Yakushi T., RA Matsushita K.; RT "Genome-wide phylogenetic analysis of differences in thermotolerance RT among closely related Acetobacter pasteurianus strains."; RL Microbiology (Mosc.) 158:229-239(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BACF01000020; GAB28195.1; -; Genomic_DNA. DR ProteinModelPortal; H1UHR4; -. DR EnsemblBacteria; GAB28195; GAB28195; APT_1685. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 190 AA; 20113 MW; B0E8B42A9EF2C9A0 CRC64; MSDLYLVTPA VSDAQAFLPV LEAGLAHHQP AAVLLRLVDM PASAARQAVL LLKPVIQARD IALMLENAPT LAQETGCDGV HLSASYTAAS VKDVRRIIGP DLQLGVAVGE SRDAAMCAGE DGADYICFGA EDGASLETVS ALTRWWSLMM ELPVVAQAQT PADLAVLNAS GADFVMPSEQ WWQQPDAWQG // ID H1UMR0_ACEPA Unreviewed; 201 AA. AC H1UMR0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APS_0543; OS Acetobacter pasteurianus subsp. pasteurianus LMG 1262 = NBRC 106471. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=940265; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3191; RA Matsutani M., Hirakawa H., Saichana N., Soemphol W., Yakushi T., RA Matsushita K.; RT "Genome-wide phylogenetic analysis of differences in thermotolerance RT among closely related Acetobacter pasteurianus strains."; RL Microbiology (Mosc.) 158:229-239(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BACG01000003; GAB29941.1; -; Genomic_DNA. DR ProteinModelPortal; H1UMR0; -. DR EnsemblBacteria; GAB29941; GAB29941; APS_0543. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 22025 MW; 95A7C6BC567B0FD6 CRC64; MTALPQKIYP VVDSATWVDR LGGAGARFIQ LRLKDMEEDA LRAEIRQGHA YAKQHGVCLV LNDYWQIALD EGIDYIHLGQ EDLDTADLAA IRKGGIRLGI STHCHEELDR ALSCNPDYVA LGPIWETKLK KMAFGPQGPL KLTEWRKLIG NLPLVAIGGI TLERAWACIE AGADSVSAVS AFIRQPDPEG QVKAWLAAVE G // ID H1UTF8_ACEPA Unreviewed; 190 AA. AC H1UTF8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN ORFNames=APS_2541; OS Acetobacter pasteurianus subsp. pasteurianus LMG 1262 = NBRC 106471. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=940265; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3191; RA Matsutani M., Hirakawa H., Saichana N., Soemphol W., Yakushi T., RA Matsushita K.; RT "Genome-wide phylogenetic analysis of differences in thermotolerance RT among closely related Acetobacter pasteurianus strains."; RL Microbiology (Mosc.) 158:229-239(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BACG01000064; GAB31939.1; -; Genomic_DNA. DR EnsemblBacteria; GAB31939; GAB31939; APS_2541. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 190 AA; 20135 MW; 368FABD85618B377 CRC64; MSDLYPVTPA VSDAQAFLPV LEAGLVHHQP AAVLLRLVDM PASAARQAVL LLKPVIQARD IALMLENAPT LAQETGCDGV HLSASYTAAS VKDVRRIIGP DLQLGVAVGE SRDAAMCAGE DGADYICFGA EDGASLETVS ALTRWWSLMM ELPVVAQAQT PADLAVLNAS GADFVMPPEQ WWQQPDAWQG // ID H1VS82_COLHI Unreviewed; 53 AA. AC H1VS82; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 11-DEC-2013, entry version 10. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN ORFNames=CH063_12896; OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose OS fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae; OC mitosporic Glomerellaceae; Colletotrichum. OX NCBI_TaxID=759273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMI 349063; RX PubMed=22885923; DOI=10.1038/ng.2372; RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J., RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., RA Altmueller J., Alvarado-Balderrama L., Bauser C.A., Becker C., RA Birren B.W., Chen Z., Choi J., Crouch J.A., Duvick J.P., Farman M.A., RA Gan P., Heiman D., Henrissat B., Howard R.J., Kabbage M., Koch C., RA Kracher B., Kubo Y., Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., RA Moore N., Neumann U., Nordstroem K., Panaccione D.G., Panstruga R., RA Place M., Proctor R.H., Prusky D., Rech G., Reinhardt R., RA Rollins J.A., Rounsley S., Schardl C.L., Schwartz D.C., Shenoy N., RA Shirasu K., Sikhakolli U.R., Stueber K., Sukno S.A., Sweigard J.A., RA Takano Y., Takahara H., Trail F., van der Does H.C., Voll L.M., RA Will I., Young S., Zeng Q., Zhang J., Zhou S., Dickman M.B., RA Schulze-Lefert P., Ver Loren van Themaat E., Ma L.-J., RA Vaillancourt L.J.; RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi RT deciphered by genome and transcriptome analyses."; RL Nat. Genet. 44:1060-1065(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CACQ02005851; CCF43089.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. FT NON_TER 53 53 SQ SEQUENCE 53 AA; 5583 MW; E0745D59DE0730DA CRC64; MPQPTVDYSL YLVTDSTPAI LGDRDLADVV AAAVRGGVTV VQYRDKTSDT GAL // ID H1W651_9CYAN Unreviewed; 365 AA. AC H1W651; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ARTHRO_10086; OS Arthrospira sp. PCC 8005. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Arthrospira. OX NCBI_TaxID=376219; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 8005; RA Rouy Z.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 8005; RA Genoscope C.E.A.; RT "Arthrospira sp. PCC 8005 whole genome shotgun sequence."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFN01000001; CCE15036.1; -; Genomic_DNA. DR EnsemblBacteria; CCE15036; CCE15036; ARTHRO_10086. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 129 Unknown (By similarity). FT REGION 130 365 Thiamine-phosphate synthase (By FT similarity). FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 365 AA; 41279 MW; 97F346057AB60A23 CRC64; MGDLNHKTKL GQPALYRILD ANLDRAREGI RTIEEWFRFG LDNSEMAAEC KNLRQQLAQW HSNELRMSRD TTTDVGTQLS HPSEENRESL EQVIQVNFCR VEEALRVLEE YGKVYHPNMG AAVKQMRYRV YTLESNLLAY GRHQTLQRAN LYLVTSPSER LMSVVEAALQ GGLKVVQYRD KDTDDHQRWK NARQLCQLCH RYNALFLVND RVDIAIAVNA DGVHLGQQDL PIAVAKQLLG PQKIVGKSTT NPEEMKLAIA EGADYIGVGP VYATPTKPDK QAAGLEYVRH ATRHASVPWF AIGGINMNNF DDVLMAGATR VAVVRSLMQA EQPTLVTQYF LSQFTRVQTL RDRQIVPENT PADFS // ID H1WQB4_LEUCI Unreviewed; 212 AA. AC H1WQB4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LEUCOC10_04340; OS Leuconostoc citreum LBAE C10. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=1108974; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LBAE C10; RA Laguerre S., Amari M., Gabriel V., Moulis C., Loux V., Klopp C., RA Robert H., Gabriel B., Vuillemin M., Morel S., Remaud-Simeon M., RA Fontagne-Faucher C.; RT "Genome sequences of three Leuconostoc citreum strains (LBAE C10, C11 RT and E16) isolated from wheat sourdoughs."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGE01000008; CCF24513.1; -; Genomic_DNA. DR EnsemblBacteria; CCF24513; CCF24513; LEUCOC10_04340. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23025 MW; 7A894A6C27EDE146 CRC64; MIFDKTMLAR YFIMGTQDVA DEAEFLRILN QALRSGITLF QYREKGQGAL VGQKKLQLAK QVRALTAQYH VPLVIDDDMA LAHAIAADGI HFGQDDGRPV DNIKQSGNLF VGVSVSNQQE YQRIAHVAGI DHIGVGPIFA TTSKSDAKPP IGISGLSQLI RIAHHPIVAI GGIQRDNLSK VLSTGVDGAA VISMISQSED IQKTLADWRN RT // ID H1WUF6_LEUCI Unreviewed; 212 AA. AC H1WUF6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LEUCOC11_01615; OS Leuconostoc citreum LBAE C11. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=1127128; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LBAE C11; RA Laguerre S., Amari M., Gabriel V., Moulis C., Loux V., Klopp C., RA Robert H., Gabriel B., Vuillemin M., Morel S., Remaud-Simeon M., RA Fontagne-Faucher C.; RT "Genome sequences of three Leuconostoc citreum strains (LBAE C10, C11 RT and E16) isolated from wheat sourdoughs."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGF01000003; CCF25955.1; -; Genomic_DNA. DR EnsemblBacteria; CCF25955; CCF25955; LEUCOC11_01615. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23025 MW; 7A894A6C27EDE146 CRC64; MIFDKTMLAR YFIMGTQDVA DEAEFLRILN QALRSGITLF QYREKGQGAL VGQKKLQLAK QVRALTAQYH VPLVIDDDMA LAHAIAADGI HFGQDDGRPV DNIKQSGNLF VGVSVSNQQE YQRIAHVAGI DHIGVGPIFA TTSKSDAKPP IGISGLSQLI RIAHHPIVAI GGIQRDNLSK VLSTGVDGAA VISMISQSED IQKTLADWRN RT // ID H1X138_LEUCI Unreviewed; 212 AA. AC H1X138; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LEUCOE16_03130; OS Leuconostoc citreum LBAE E16. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=1127129; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LBAE E16; RA Laguerre S., Amari M., Gabriel V., Moulis C., Loux V., Klopp C., RA Robert H., Gabriel B., Vuillemin M., Morel S., Remaud-Simeon M., RA Fontagne-Faucher C.; RT "Genome sequences of three Leuconostoc citreum strains (LBAE C10, C11 RT and E16) isolated from wheat sourdoughs."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGG01000003; CCF28287.1; -; Genomic_DNA. DR ProteinModelPortal; H1X138; -. DR EnsemblBacteria; CCF28287; CCF28287; LEUCOE16_03130. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22953 MW; 7A894A6C27EF6B46 CRC64; MIFDKTMLAR YFIMGTQDVA DEAEFLRILN QALRSGITLF QYREKGQGAL VGQKKLQLAK QVRALTAQYH VPLVIDDDMA LAHAIAADGI HFGQDDGRPV DNIKQSGNLF VGVSVSNQQE YQRIAHVAGI DHIGVGPIFA TTSKSDAKPP IGISGLSQLI RIAHHPIVAI GGIQRDNLSK VLSTGVDGAA VISMISQSGD IQKTLADWRN RT // ID H1X992_WEICO Unreviewed; 237 AA. AC H1X992; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 11-DEC-2013, entry version 12. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE1; ORFNames=WEISSC39_08410; OS Weissella confusa LBAE C39-2. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Weissella. OX NCBI_TaxID=1127131; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LBAE C39-2; RA Amari M., Laguerre S., Gabriel V., Moulis C., Loux V., Klopp C., RA Robert H., Gabriel B., Vuillemin M., Morel S., Remaud-Simeon M., RA Fontagne-Faucher C.; RT "Genome sequence of Weissella confusa LBAE C39-2 isolated from a wheat RT sourdough."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGH01000022; CCF31145.1; -; Genomic_DNA. DR EnsemblBacteria; CCF31145; CCF31145; WEISSC39_08410. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 237 AA; 24984 MW; A84801EE52DDFC91 CRC64; MTFKAEQLAS TLVIGSQYVD DVAGFVAQAV KAGVSMVILN EAQLTGVEKQ NLAEYIRDVT RAADVAFMIA DDVALAAAVG ADGVYITDRH QVNELTAQAQ AADLYTGVSI NNRTELLEEE PAGLAFYSVS PVYPSRHVTE ESPIEHLAGL TTVVQNSDLP VVAMGGITVA RLKDIVRMGV YGAAAIDAFV DADDLIAAVT AFNDTFAGMT VDQALGNTRY GLAIPGKHTN AVQGELH // ID H1XAF0_WEICO Unreviewed; 217 AA. AC H1XAF0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; ORFNames=WEISSC39_10585; OS Weissella confusa LBAE C39-2. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Weissella. OX NCBI_TaxID=1127131; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LBAE C39-2; RA Amari M., Laguerre S., Gabriel V., Moulis C., Loux V., Klopp C., RA Robert H., Gabriel B., Vuillemin M., Morel S., Remaud-Simeon M., RA Fontagne-Faucher C.; RT "Genome sequence of Weissella confusa LBAE C39-2 isolated from a wheat RT sourdough."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGH01000035; CCF31553.1; -; Genomic_DNA. DR EnsemblBacteria; CCF31553; CCF31553; WEISSC39_10585. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23430 MW; 95AD66DC928C62E0 CRC64; MNKEFLQRYF VAGSQNFPDL TLPEYEERIA LIMQSGITAY QFREKNPTLS FDEKQALAMR LREKARELAV PFIVDDDVAL AIAVEADGIH VGQDDMPITD VVAQVAGQMI VGLSVRNKAE MVAAQSVMGI DYLGVGPVFA TTTKADAATP LGLDGLATTL NANAKQLPTV AIGGITLEDL PALHQSGVDG VSVISLLSEA PDVRTVIDEM KEQWRTL // ID H1XEB6_9XANT Unreviewed; 212 AA. AC H1XEB6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=XAPC_1238; OS Xanthomonas axonopodis pv. punicae str. LMG 859. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=1085630; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 859; RX PubMed=22493202; DOI=10.1128/JB.00181-12; RA Sharma V., Midha S., Ranjan M., Pinnaka A.K., Patil P.B.; RT "Genome Sequence of Xanthomonas axonopodis pv. punicae Strain LMG RT 859."; RL J. Bacteriol. 194:2395-2395(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGJ01000013; CCF67546.1; -; Genomic_DNA. DR EnsemblBacteria; CCF67546; CCF67546; XAPC_1238. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22018 MW; DFBBCECE610D5526 CRC64; MPNRLNVRGV YLITPDEPNT QRLLLRTAPL LGSITWLQYR NKQADAALRL RQAGALREAC AAHGVPLIIN DDAQLAAQVG AQGVHLGEDD GDVAAARALL GEQAIIGVSC YDDIERARAA AASGASYVAF GAFFPTTTKQ TTRRATPALL QQAAELDVPR VAIGGIAPAQ VPALVTAGAD LIAVVSGVYA APDPVAAVQG YRAGFAAQRG KL // ID H1XF65_9XANT Unreviewed; 302 AA. AC H1XF65; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-OCT-2013, entry version 14. DE SubName: Full=Mutator MutT family protein; GN Name=mutT; ORFNames=XAPC_1540; OS Xanthomonas axonopodis pv. punicae str. LMG 859. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=1085630; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 859; RX PubMed=22493202; DOI=10.1128/JB.00181-12; RA Sharma V., Midha S., Ranjan M., Pinnaka A.K., Patil P.B.; RT "Genome Sequence of Xanthomonas axonopodis pv. punicae Strain LMG RT 859."; RL J. Bacteriol. 194:2395-2395(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGJ01000018; CCF67845.1; -; Genomic_DNA. DR ProteinModelPortal; H1XF65; -. DR EnsemblBacteria; CCF67845; CCF67845; XAPC_1540. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 302 AA; 33539 MW; 978020494A8FF058 CRC64; MITDPRGRIL LTRRTETRDM PGLWEFPGGK REPGETSEQA LVRELNEELG IEAQVGDWVM DVPQLYPDKR LRLEVRHITI WKGSPRGREG QAMTWVAADK LARYSMPPAD VPVVGALRQP DRYLITPDPE DDARWLESLE LALQNGITRI QLRARQLAPA RWQALLQQVM RLRGRARAQL LLNRDIALAA DLGIGVHLGS EQLAGLQERP LPAEQLVAAS CHGLDDLRHA QRTGCDFAVL GPVQATASHP GATPIGWDGF ETLREQVSLP IYALGGMQVE DVRQARSHGA QGIAAIRALW PQ // ID H1Y3N3_9SPHI Unreviewed; 216 AA. AC H1Y3N3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Mucpa_6239; OS Mucilaginibacter paludis DSM 18603. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Mucilaginibacter. OX NCBI_TaxID=714943; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18603; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001403; EHQ30295.1; -; Genomic_DNA. DR ProteinModelPortal; H1Y3N3; -. DR EnsemblBacteria; EHQ30295; EHQ30295; Mucpa_6239. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23792 MW; 0981AF0796E70513 CRC64; MGNFPYRLYL VTDEAACLGR DFFWVIEQAI KGGVDMVQLR EKNLSDQAFL NKALLLKDLL DRYNVPLIIN DNLPVAVHCG AAGIHVGNSD SPPTKIRLQH PDTKFLGYSI EYEAQLETED ARVSDYLALS PVYATNTKTD TVTEWKTEGI HRVRQITNKP LVAIGGINEA NAASIITAGA DCLAIVSAIC SAENPALAAE RLRNLIDRSM NSYEKI // ID H1Y4Q3_9SPHI Unreviewed; 206 AA. AC H1Y4Q3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 22-JAN-2014, entry version 12. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Mucpa_4006; OS Mucilaginibacter paludis DSM 18603. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Mucilaginibacter. OX NCBI_TaxID=714943; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18603; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001403; EHQ28097.1; -; Genomic_DNA. DR EnsemblBacteria; EHQ28097; EHQ28097; Mucpa_4006. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22973 MW; 4C20339B31EBA028 CRC64; MKKYISRFHY LTQDLPNRSH AEQTLMACQA GVNWIQYRCL TKPDDEMIPE INEVASICDE WGATLILTDH YHLLNRVDAQ GVHIEDFDAD LVVIREVITD EKTLGASATN IERILALQQS GVVDYCGYGP FAHTDTKPNN FPLLGYKGYR ELEKYPITIP VIAVGGILLA DVEHLMKTPI TGIAVSGAVN HSVDPKAMLK AFYQAV // ID H1Y609_9SPHI Unreviewed; 204 AA. AC H1Y609; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 22-JAN-2014, entry version 12. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Mucpa_6919; OS Mucilaginibacter paludis DSM 18603. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Mucilaginibacter. OX NCBI_TaxID=714943; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18603; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001403; EHQ30968.1; -; Genomic_DNA. DR EnsemblBacteria; EHQ30968; EHQ30968; Mucpa_6919. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 204 AA; 22584 MW; 5F9363E511D5E854 CRC64; MELIVISNPV AVADESILIN NLFEAGLQCF HIRKPESDVR TVRELIGGIA PLFYNRISLH QFHEIAPDYG IQRLHYTEHY RAGTSPKNRE VQKANGYILS TSVHDATLLP GLTDFDYVFF GPVFNSLSKS GYQSTLTTDF KLKKNEITTK VIALGGVDQF NLIKIEKMGF DGAAVLGAIW NAPSSAVASF LTLSEIYTPQ NITS // ID H1Y610_9SPHI Unreviewed; 215 AA. AC H1Y610; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Mucpa_6920; OS Mucilaginibacter paludis DSM 18603. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Mucilaginibacter. OX NCBI_TaxID=714943; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18603; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001403; EHQ30969.1; -; Genomic_DNA. DR EnsemblBacteria; EHQ30969; EHQ30969; Mucpa_6920. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23529 MW; 8FE49976488DAB4F CRC64; MIDQLHYISQ QPENGSHLTA IQQALEAGCR WIQLRVKNQP QDVILKYAFI AKRMCNLHGA KLIVDDHPEI ALAVGAHGVH LGLQDMPVSQ ARRMVGDQMI IGGTANTFQH IRQRADEGVD YIGCGPYRFT TTKQKLSPIV GLSGYEILAG QMDAAGIHIP VIAIGGILPE DVPLIRQTGL YGVAISGAIT FSGNREQTVA QIYRQLKTPC LKRVI // ID H1YJY2_9GAMM Unreviewed; 646 AA. AC H1YJY2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN ORFNames=Sbal183_2217; OS Shewanella baltica OS183. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=693971; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OS183; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Held B., Land M.L., Hauser L., RA Konstantinidis K., Deng J., Brettar I., Hofle M., Tiedje J., RA Auchtung J., Woyke T.J.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=OS183; RX PubMed=22328742; DOI=10.1128/JB.06468-11; RA Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M., RA Tiedje J.M., Konstantinidis K.T.; RT "Genome Sequencing of Five Shewanella baltica Strains Recovered from RT the Oxic-Anoxic Interface of the Baltic Sea."; RL J. Bacteriol. 194:1236-1236(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001435; EHQ15117.1; -; Genomic_DNA. DR ProteinModelPortal; H1YJY2; -. DR EnsemblBacteria; EHQ15117; EHQ15117; Sbal183_2217. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 646 AA; 68280 MW; 69576481957ED8AE CRC64; MLGIHGDNVP MNTERPAFVW TIAGSDSGGG AGIQADLATI QDLGCHGCSV VTTVTAQSSV AVTLVEPVSA AMLMAQLTTL LSDLPPKAIK IGLLADQTQV ALLADWIASF KINYPSVPVI VDPVMVASCG DALAVDNCQD IKSAAKSALD FKPFKGLIEL ITPNVLELGR LTHSDVSTKA QFAAAALALS QSLDCSVLAK GGDVSFGCTD ILDDTHAKTH DNTHAQTHDN TYAETQANAY KSNGWDLELA EDYLVCRQVR ASSKLHQNGR FWLASQRVNT HHNHGSGCTL SSAIAAVLAQ GFVLQDAVVV AKAYVSQGLS AAIGLGQGPG PLARTGWPND VSHYAKIRLC CDNGINQHLD VGNDLVATVL SATDQATAQV RIASTPPQNI LSHCFKVLDA DLGVYPVVSD LTMLESLLAA GVKTVQLRIK TDISELTTTT APAEFDLGKS ALGRCESGEP ELIGSELEAQ IQTAIALGKH FNAQLFINDH WQLAIKYHAF GVHLGQEDLA VTDLAAIQAA GLALGISSHS YFELLLAHQY SPSYIALGHI FPTTTKQMPS APQGLAKLKH YVALLQGHYP LVAIGGIDLT NLAKVKATGV GNIAVVRAIT KAKEPLAAFA ELSQAWEQCS LSEELAVKHE LVAKHE // ID H1Z1T9_9EURY Unreviewed; 209 AA. AC H1Z1T9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Metlim_1297; OS Methanoplanus limicola DSM 2279. OC Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales; OC Methanomicrobiaceae; Methanoplanus. OX NCBI_TaxID=937775; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2279; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Wirth R., RA Brambilla E.-M., Klenk H.-P., Eisen J.A.; RT "The Improved High-Quality Draft genome of Methanoplanus limicola DSM RT 2279."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001436; EHQ35406.1; -; Genomic_DNA. DR EnsemblBacteria; EHQ35406; EHQ35406; Metlim_1297. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21169 MW; DA034BC2850C5DD7 CRC64; MAYGLYIVTD RVIGRGMTHA DMAALAVAGG ADVVQLRDKD MPAADLTAEA VNIREITEDS GTLFIVNDRI DIALASGADG VHLGQSDIPA EYARKIVPDD FIIGISVSTP DEALKARNSG ADYVSPGPVF TTATKSDAGD ALGLDTVFTI SAAVEIPVVP IGGISGKNAA SVIGAGADGV AVISAVFGRE DAVSAAADLK KIIEGAKTA // ID H1Z4Z9_MYROD Unreviewed; 210 AA. AC H1Z4Z9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Myrod_1414; OS Myroides odoratus DSM 2801. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Myroides. OX NCBI_TaxID=929704; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2801; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The draft genome of Myroides odoratus DSM 2801."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001437; EHQ42247.1; -; Genomic_DNA. DR EnsemblBacteria; EHQ42247; EHQ42247; Myrod_1414. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 210 AA; 24407 MW; A64CED49159BA843 CRC64; MVVITPPYHH PKEISLANTM LERGLPLLHI RKPDFTFEQL QQWVENISYQ HHDKLVIHIP SLVINNYPKV FKQYVQLINS LRAQYAHLST DNCSFVNNYA QKLPYLSTSV HNSTECEKLS TRHQRVFLSP VFDSISKIAY QPTLHWPSFL ADWKYPWIQT VALGGITPDH LATVRNMGFD DFAVLGAIWQ AADPLKIFDL CYKQDQLLFR // ID H1Z501_MYROD Unreviewed; 206 AA. AC H1Z501; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Myrod_1416; OS Myroides odoratus DSM 2801. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Myroides. OX NCBI_TaxID=929704; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2801; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The draft genome of Myroides odoratus DSM 2801."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001437; EHQ42249.1; -; Genomic_DNA. DR EnsemblBacteria; EHQ42249; EHQ42249; Myrod_1416. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22822 MW; BB7801DEAE558EC3 CRC64; MFNPIQYISQ GDTPQEQLYH IESVLDAGQR WIQFRFKDTL TSIRWKTAEQ VKLLCDSYQA TLLINDDPDL ALAIDADGVH LGLQDRSIAE ARVLLPHKII GGTANTLQDV KQRLGESCDY IGLGPLRYTP TKKKLSPLLG FEGYQQLLTA LTPEEKQTPI VAIGGITLAD VPVLQKIGLS GIAVSSLLHQ AQSPQQLIQQ LNTYFL // ID H2A6M5_STRMD Unreviewed; 127 AA. AC H2A6M5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 11-DEC-2013, entry version 14. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=SMA_1100; OS Streptococcus macedonicus (strain ACA-DC 198). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1116231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACA-DC 198; RX PubMed=22408241; DOI=10.1128/JB.06804-11; RA Papadimitriou K., Ferreira S., Papandreou N.C., Mavrogonatou E., RA Supply P., Pot B., Tsakalidou E.; RT "Complete genome sequence of the dairy isolate Streptococcus RT macedonicus ACA-DC 198."; RL J. Bacteriol. 194:1838-1839(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE613569; CCF02391.1; -; Genomic_DNA. DR RefSeq; YP_005094744.1; NC_016749.1. DR EnsemblBacteria; CCF02391; CCF02391; SMA_1100. DR GeneID; 11602009; -. DR KEGG; smn:SMA_1100; -. DR KO; K00788; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 127 AA; 13362 MW; 1556C836CAE806C5 CRC64; MIINDDVDLA LELDADGIHL GQDDLPITKA RQLFPNKIID LSVGLIIEYQ RSAVELVDYI GVGPIFSTSS KNGAGEVIGL KGLNNVRDYD KEIPIVAIGG ITFGDVAAIK QTGADGVAVI SAIAQSK // ID H2AG98_BACAM Unreviewed; 224 AA. AC H2AG98; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BACAU_3577; OS Bacillus amyloliquefaciens subsp. plantarum CAU B946. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1114958; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CAU B946; RX PubMed=22408246; DOI=10.1128/JB.06762-11; RA Blom J., Rueckert C., Niu B., Wang Q., Borriss R.; RT "The Complete Genome of Bacillus amyloliquefaciens subsp. plantarum RT CAU B946 Contains a Gene Cluster for Nonribosomal Synthesis of Iturin RT A."; RL J. Bacteriol. 194:1845-1846(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE617159; CCF07111.1; -; Genomic_DNA. DR RefSeq; YP_005132306.1; NC_016784.1. DR EnsemblBacteria; CCF07111; CCF07111; BACAU_3577. DR GeneID; 11699482; -. DR KEGG; baq:BACAU_3577; -. DR KO; K00788; -. DR BioCyc; BAMY1114958:GJW0-3698-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23838 MW; DCA2A0F849E2DD51 CRC64; MTRISREMMK NMLSVYFIMG SNNTSADPVS VVKKAIEGGA TLFQFREKGS GSLTGDERVL FAKRVQDVCR QAGIPFIIND DVELALRLEA DGVHIGQDDA DAEETRAAIG DMILGVSAHN VSEVKRAEEA GADYVGMGPV YPTETKKDAE AVQGVTLIEE VRRQGITIPI VGIGGITADN AAPVIEAGAD GVSMISAISQ AEDPKAAARK FSEEIRRSKA GLSR // ID H2AGV6_BACAM Unreviewed; 230 AA. AC H2AGV6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 22-JAN-2014, entry version 16. DE SubName: Full=Transcriptional regulator TenI; DE EC=2.5.1.3; GN Name=tenI; ORFNames=BACAU_1128; OS Bacillus amyloliquefaciens subsp. plantarum CAU B946. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1114958; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CAU B946; RX PubMed=22408246; DOI=10.1128/JB.06762-11; RA Blom J., Rueckert C., Niu B., Wang Q., Borriss R.; RT "The Complete Genome of Bacillus amyloliquefaciens subsp. plantarum RT CAU B946 Contains a Gene Cluster for Nonribosomal Synthesis of Iturin RT A."; RL J. Bacteriol. 194:1845-1846(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE617159; CCF04662.1; -; Genomic_DNA. DR RefSeq; YP_005129857.1; NC_016784.1. DR EnsemblBacteria; CCF04662; CCF04662; BACAU_1128. DR GeneID; 11697644; -. DR KEGG; baq:BACAU_1128; -. DR KO; K10810; -. DR BioCyc; BAMY1114958:GJW0-1218-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 230 AA; 25884 MW; 759ADAA8EE09CA29 CRC64; MNINFGEWLI KKKAGPRRTE KRWNPLELHA VTDNRKPVAE LAEDILSIQR EVSFIHIRER DKTAGEIMQL LSLLKKGGAD KDKLIINDRA DIALFANIHR VQLPSRSFSV KQVRSRFPHL HIGRSVHSLE EAIQAEKEDA DYVVFGHIFE TECKQGLEAR GISLLSEIKR TLSIPVIAIG GMTLQTIGHT KQAKPDGIAV MSGIFSAENP EEAAKRYARA VREADYEEAL // ID H2B178_KAZAF Unreviewed; 540 AA. AC H2B178; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-APR-2014, entry version 16. DE SubName: Full=Uncharacterized protein; GN Name=KAFR0K00230; ORFNames=KAFR_0K00230; OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / OS CECT 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces OS africanus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kazachstania. OX NCBI_TaxID=1071382; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 / RC NRRL Y-8276; RX PubMed=22123960; DOI=10.1073/pnas.1112808108; RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., RA Byrne K.P., Wolfe K.H.; RT "Evolutionary erosion of yeast sex chromosomes by mating-type RT switching accidents."; RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE650831; CCF60378.1; -; Genomic_DNA. DR RefSeq; XP_003959513.1; XM_003959464.1. DR GeneID; 13886567; -. DR KEGG; kaf:KAFR_0K00230; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 540 AA; 58328 MW; B116217F74C1BC4A CRC64; MICNKNAVDY SLYLVTDSSM LPPNTSLYSQ IEAGLKNGVT VVQVREKDSD TGAFIDEAVR IKELCTKYQV PLMINDRVDV AMAIDADGVH VGQDDMPIPM VRKLLGPDKI IGWSVGKVEE VETLAYWGPE MVDYIGVGTV FPTETKKNTK IPMGPRGVAR ILTALEDNKA EWCRTVAIGG LHPTNIERVL YQSFSQNGKR SLDGIAVVSD IMAAPDAGAA TKRLQGLLKQ NAYHFIPPCS VEKSDLSLHS KIKTVISNVN DKAPLIHHIT NKVHQNFGAN VTLSLGSSPI MSEIESEAQD LAELPHAALL LNTGSVAPVQ MVKTAIAAYN KVKKPIVFDP VGYSATETRL LLNNTLLSHG QFTCIKGNIG EILSLANMSK NKMKGVDSGD HIVDKKYLAL ATKTVAYNFR TVAVCTGEDD FIADGTFGGE YKLGHGLNKH SLDDVPCLRV ENGPIPIMGQ ITASGCSLGT TIACFLGGYD SRISVFETVT AAVMLYKSAG FKAASLCQGT ASFQVHLVDT LYNLFQENSP ETWTAKVSVV // ID H2CFV3_9LEPT Unreviewed; 250 AA. AC H2CFV3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=Lepil_2124; OS Leptonema illini DSM 21528. OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptonema. OX NCBI_TaxID=929563; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 21528; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Held B., Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., RA Brambilla E.-M., Klenk H.-P., Eisen J.A.; RT "The Improved High-Quality Draft genome of Leptonema illini DSM RT 21528."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH597773; EHQ06802.1; -; Genomic_DNA. DR EnsemblBacteria; EHQ06802; EHQ06802; Lepil_2124. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 250 AA; 28861 MW; 042769C94AD3F3FC CRC64; MSKKETSSES LRIRAYPILD EDFLQMAGLQ PMDLIDLWAD EGITIFQYRN KQKPTKARLE EVERNARRRR LRWILNDYDQ LFCDGVADGI HLGWEDWHGL PEERRQALLR RLNGVQSLQA ESTPLCGIST HTPDQWSEAL TLHRSGVLPL SYIAFGPCFK TTSKKSGLHP QLQKEAFEEL ERRRDEARKK GELPDAVFIG GIDPDNLPVL VQTLSNTKKK EERTIFVASI RALSDPLDIR RFRSIPNWKP // ID H2FYS8_OCESG Unreviewed; 502 AA. AC H2FYS8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-APR-2014, entry version 18. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=GU3_01680; OS Oceanimonas sp. (strain GK1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Oceanimonas. OX NCBI_TaxID=511062; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GK1; RX PubMed=22461556; DOI=10.1128/JB.00023-12; RA Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., RA Ramezani M., Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.; RT "Complete Genome Sequence of Oceanimonas sp. GK1, a Halotolerant RT Bacterium from Gavkhouni Wetland in Iran."; RL J. Bacteriol. 194:2123-2124(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003171; AEY00093.1; -; Genomic_DNA. DR RefSeq; YP_005090843.1; NC_016745.1. DR EnsemblBacteria; AEY00093; AEY00093; GU3_01680. DR GeneID; 11597433; -. DR KEGG; oce:GU3_01680; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR BioCyc; OSP511062:GI6E-341-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 502 AA; 53315 MW; EB79239EE6835994 CRC64; MTKPIVWTIA GSDSGGGAGI QADLHTIQAL GGHGCSVISA ITAQNSVSVS MVEPVLMQAF TSQLVSLATD MQAAAIKIGL LPGGLRAEVL ARYLKEYRRQ WQPWVVLDPV AIASTGQSMA EANLLPAIKT HLLPEVDLIT PNAVELEALS GIAPDSPQAL RAGAAALREM GVGAVLVKGG HLDWTGDQAI DFYSDGEREI WLASPRLDTQ HGHGTGCTLS SAIATAVALD YPIEDALVLA KAYVNQGLKG AEGIGAGAGP VAHLGWPTNL ADFPAVVMPG SKLAEQLGIS GPHPQGAFAA MDTNQLGLYP VVTTVAWLER LLKQGVRTLQ LRIKDKTDAE VEADVRAAVE LGKRYNARLF INDYWRLAIK HGAYGVHLGQ EDIEVADLEA IRAAGLKLGL STHGYYEMLR ARELKPSYLA LGHIFPTRTK DMPSRPQGLE RLHRYVALMQ DEFPLVAIGG ISKDRVPLVA QTGVGSIALV TAITEAADPD AATRELLQMV EG // ID H2G087_OCESG Unreviewed; 204 AA. AC H2G087; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GU3_01640; OS Oceanimonas sp. (strain GK1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Oceanimonas. OX NCBI_TaxID=511062; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GK1; RX PubMed=22461556; DOI=10.1128/JB.00023-12; RA Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., RA Ramezani M., Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.; RT "Complete Genome Sequence of Oceanimonas sp. GK1, a Halotolerant RT Bacterium from Gavkhouni Wetland in Iran."; RL J. Bacteriol. 194:2123-2124(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003171; AEY00085.1; -; Genomic_DNA. DR RefSeq; YP_005090835.1; NC_016745.1. DR EnsemblBacteria; AEY00085; AEY00085; GU3_01640. DR GeneID; 11597425; -. DR KEGG; oce:GU3_01640; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; OSP511062:GI6E-333-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21982 MW; B55F765E39E30C0A CRC64; MNPYRLYLVT DDRQPIDTLQ TVVREAVAGG VTLVQVREKH GDVRAFIERA EAVKAVLQGT GVPLIINDRV DVALAVDADG VHLGQSDMPA THARRLLGPD RLLGLSVETE QQLFESESLP VDYLGLSAIF ATPTKTDLKR HWGIDGLQRA LSHSSRPIVA IGGIHADNLQ QVVQTGVHGV ALVSAICAAS CPRTAAKKLR QMMA // ID H2G3H4_CORD3 Unreviewed; 222 AA. AC H2G3H4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CD31A_0029; OS Corynebacterium diphtheriae (strain 31A). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=31A; RX PubMed=22505676; DOI=10.1128/JB.00183-12; RA Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., RA Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., RA Santos C.S., Santos L.S., Hirata R.Jr., Mattos-Guaraldi A.L., RA Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.; RT "Pangenomic Study of Corynebacterium diphtheriae That Provides RT Insights into the Genomic Diversity of Pathogenic Isolates from Cases RT of Classical Diphtheria, Endocarditis, and Pneumonia."; RL J. Bacteriol. 194:3199-3215(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003206; AEX40715.1; -; Genomic_DNA. DR RefSeq; YP_005156742.1; NC_016799.1. DR EnsemblBacteria; AEX40715; AEX40715; CD31A_0029. DR GeneID; 11731161; -. DR KEGG; cdz:CD31A_0029; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; CDIP698962:GH9X-34-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). SQ SEQUENCE 222 AA; 23497 MW; FE29E5F246E61099 CRC64; MLPTPRWGRD FDPRCYFVTG TGSVDHIVDV ARQAARAGAG LIQVRSKPIA ARDLYILGRE VARAVAEVNP RTRVLIDDRV DVALALMNNG EHIHGVHVGQ DDLPVRHVRA LLGDNAIIGL TTGTLELVRA SRQVAEVIDY IGAGPFRPTP TKDSGRAPVG LVGYPPLVAE SLVPVVAIGD VRPEDAADLA ATGVAGVAIV RALMNSQDVA ADVKLVLKGF AQ // ID H2GBC0_CORD2 Unreviewed; 222 AA. AC H2GBC0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-APR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CD241_0028; OS Corynebacterium diphtheriae (strain 241). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698966; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=241; RX PubMed=22505676; DOI=10.1128/JB.00183-12; RA Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., RA Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., RA Santos C.S., Santos L.S., Hirata R.Jr., Mattos-Guaraldi A.L., RA Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.; RT "Pangenomic Study of Corynebacterium diphtheriae That Provides RT Insights into the Genomic Diversity of Pathogenic Isolates from Cases RT of Classical Diphtheria, Endocarditis, and Pneumonia."; RL J. Bacteriol. 194:3199-3215(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003207; AEX43095.1; -; Genomic_DNA. DR RefSeq; YP_005124297.1; NC_016782.1. DR EnsemblBacteria; AEX43095; AEX43095; CD241_0028. DR GeneID; 11674475; -. DR KEGG; cdp:CD241_0028; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). SQ SEQUENCE 222 AA; 23400 MW; 96AFB4B751E541C4 CRC64; MLPTPRWGRD FDPRCYFVTG TGSVDHIVDV ARQAARAGAG LIQVRSKPIA ARDLYILGRE VARAVAEVNP GTRVLIDDRV DVALALMNNG EHIHGVHVGQ DDLPVRHVRA LLGDNAIIGL TTGTLELVRA SRQVAEVIDY IGAGPFRPTP TKDSGRAPVG LAGYPPLVAE SLVPVVAIGD VRPEDAADLA ATGVAGVAIV RALMNSQDVA ADVKLVLKGF TQ // ID H2GHJ0_CORDN Unreviewed; 222 AA. AC H2GHJ0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-APR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CDB402_0028; OS Corynebacterium diphtheriae (strain INCA 402). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698972; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=INCA 402; RX PubMed=22505676; DOI=10.1128/JB.00183-12; RA Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., RA Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., RA Santos C.S., Santos L.S., Hirata R.Jr., Mattos-Guaraldi A.L., RA Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.; RT "Pangenomic Study of Corynebacterium diphtheriae That Provides RT Insights into the Genomic Diversity of Pathogenic Isolates from Cases RT of Classical Diphtheria, Endocarditis, and Pneumonia."; RL J. Bacteriol. 194:3199-3215(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003208; AEX45340.1; -; Genomic_DNA. DR RefSeq; YP_005126542.1; NC_016783.1. DR EnsemblBacteria; AEX45340; AEX45340; CDB402_0028. DR GeneID; 11670050; -. DR KEGG; cdh:CDB402_0028; -. DR KO; K00788; -. DR BioCyc; CDIP698972:GI1X-33-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). SQ SEQUENCE 222 AA; 23529 MW; 8A49F85482669AAF CRC64; MLPTPRWGRD FDPRCYFVTG TGSVDHIVDV ARQAARAGAG LIQVRSKPIA ARDLYILGRE VARAVTEVNP RTRVLIDDRV DVALALMNNG EHIHGVHVGQ DDLPVRHVRA LLGDNAIIGL TTGTLELVRA SRQVAEVIDY IGAGPFRPTP TKDSGRAPVG LAGYPPLVAE SLVPVVAIGD VRPEDAADLA ATGVAGVAIV RALMNSQDVA TDVKLVLKGF AQ // ID H2GRK0_CORDB Unreviewed; 222 AA. AC H2GRK0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-APR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CDBH8_0032; OS Corynebacterium diphtheriae (strain BH8). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698973; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BH8; RX PubMed=22505676; DOI=10.1128/JB.00183-12; RA Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., RA Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., RA Santos C.S., Santos L.S., Hirata R.Jr., Mattos-Guaraldi A.L., RA Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.; RT "Pangenomic Study of Corynebacterium diphtheriae That Provides RT Insights into the Genomic Diversity of Pathogenic Isolates from Cases RT of Classical Diphtheria, Endocarditis, and Pneumonia."; RL J. Bacteriol. 194:3199-3215(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003209; AEX47559.1; -; Genomic_DNA. DR RefSeq; YP_005159126.1; NC_016800.1. DR EnsemblBacteria; AEX47559; AEX47559; CDBH8_0032. DR GeneID; 11734437; -. DR KEGG; cdb:CDBH8_0032; -. DR KO; K00788; -. DR BioCyc; CDIP698973:GHAI-37-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). SQ SEQUENCE 222 AA; 23440 MW; 1617249258B8A563 CRC64; MLPTPRWGRD FDPRCYFVTG TGSVEHIVDV ARQAARAGAG LIQVRSKPIA ARDLYILGRE VARAVAEVNP GTRVLIDDRV DVALALMNNG EHIHGVHVGQ DDLPVRHVRA LLGDNAIIGL TTGTLELVRA SRQVAEVIDY IGAGPFRPTP TKDSGRVPVG LVGYPPLVAE SLVPVVAIGD VRPEDAADLA ATGVAGVAIV RALMNSQDVA ADVKLVLKGF AQ // ID H2GTC5_CORD7 Unreviewed; 222 AA. AC H2GTC5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CDC7B_0028; OS Corynebacterium diphtheriae (strain ATCC 27012 / C7 (beta)). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27012 / C7 (beta); RX PubMed=22505676; DOI=10.1128/JB.00183-12; RA Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., RA Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., RA Santos C.S., Santos L.S., Hirata R.Jr., Mattos-Guaraldi A.L., RA Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.; RT "Pangenomic Study of Corynebacterium diphtheriae That Provides RT Insights into the Genomic Diversity of Pathogenic Isolates from Cases RT of Classical Diphtheria, Endocarditis, and Pneumonia."; RL J. Bacteriol. 194:3199-3215(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003210; AEX66229.1; -; Genomic_DNA. DR RefSeq; YP_005161483.1; NC_016801.1. DR EnsemblBacteria; AEX66229; AEX66229; CDC7B_0028. DR GeneID; 11737351; -. DR KEGG; cds:CDC7B_0028; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; CDIP698963:GHGE-33-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). SQ SEQUENCE 222 AA; 23529 MW; 8A49F85482669AAF CRC64; MLPTPRWGRD FDPRCYFVTG TGSVDHIVDV ARQAARAGAG LIQVRSKPIA ARDLYILGRE VARAVTEVNP RTRVLIDDRV DVALALMNNG EHIHGVHVGQ DDLPVRHVRA LLGDNAIIGL TTGTLELVRA SRQVAEVIDY IGAGPFRPTP TKDSGRAPVG LAGYPPLVAE SLVPVVAIGD VRPEDAADLA ATGVAGVAIV RALMNSQDVA TDVKLVLKGF AQ // ID H2H0P7_CORDD Unreviewed; 222 AA. AC H2H0P7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-APR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CDCE8392_0026; OS Corynebacterium diphtheriae (strain CDCE 8392). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698965; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDCE 8392; RX PubMed=22505676; DOI=10.1128/JB.00183-12; RA Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., RA Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., RA Santos C.S., Santos L.S., Hirata R.Jr., Mattos-Guaraldi A.L., RA Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.; RT "Pangenomic Study of Corynebacterium diphtheriae That Provides RT Insights into the Genomic Diversity of Pathogenic Isolates from Cases RT of Classical Diphtheria, Endocarditis, and Pneumonia."; RL J. Bacteriol. 194:3199-3215(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003211; AEX71030.1; -; Genomic_DNA. DR RefSeq; YP_005132578.1; NC_016785.1. DR EnsemblBacteria; AEX71030; AEX71030; CDCE8392_0026. DR GeneID; 11707757; -. DR KEGG; cdd:CDCE8392_0026; -. DR KO; K00788; -. DR BioCyc; CDIP698965:GHJP-31-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). SQ SEQUENCE 222 AA; 23499 MW; E139E5E250F1108E CRC64; MLPTPRWGRD FDPRCYFVTG TGSVDHIVDV ARQAARAGAG LIQVRSKPIA ARDLYILGRE VARAVAEVNP RTRVLIDDRV DVALALMNNG EHIHGVHVGQ DDLPVRHVRA LLGDNAIIGL TTGTLELVRA SRQVAEVIDY IGAGPFRPTP TKDSGRAPVG LAGYPPLVAE SLVPVVAIGD VRPEDAADLA ATGVAGVAIV RALMNSQDVA TDVKLVLKGF AQ // ID H2H7C5_CORDH Unreviewed; 222 AA. AC H2H7C5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-APR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CDHC01_0028; OS Corynebacterium diphtheriae (strain HC01). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698967; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HC01; RX PubMed=22505676; DOI=10.1128/JB.00183-12; RA Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., RA Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., RA Santos C.S., Santos L.S., Hirata R.Jr., Mattos-Guaraldi A.L., RA Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.; RT "Pangenomic Study of Corynebacterium diphtheriae That Provides RT Insights into the Genomic Diversity of Pathogenic Isolates from Cases RT of Classical Diphtheria, Endocarditis, and Pneumonia."; RL J. Bacteriol. 194:3199-3215(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003212; AEX73281.1; -; Genomic_DNA. DR RefSeq; YP_005134829.1; NC_016786.1. DR EnsemblBacteria; AEX73281; AEX73281; CDHC01_0028. DR GeneID; 11708312; -. DR KEGG; cdt:CDHC01_0028; -. DR KO; K00788; -. DR BioCyc; CDIP698967:GHQ6-33-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). SQ SEQUENCE 222 AA; 23400 MW; 96AFB4B751E541C4 CRC64; MLPTPRWGRD FDPRCYFVTG TGSVDHIVDV ARQAARAGAG LIQVRSKPIA ARDLYILGRE VARAVAEVNP GTRVLIDDRV DVALALMNNG EHIHGVHVGQ DDLPVRHVRA LLGDNAIIGL TTGTLELVRA SRQVAEVIDY IGAGPFRPTP TKDSGRAPVG LAGYPPLVAE SLVPVVAIGD VRPEDAADLA ATGVAGVAIV RALMNSQDVA ADVKLVLKGF TQ // ID H2HDZ3_CORDJ Unreviewed; 222 AA. AC H2HDZ3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-APR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CDHC02_0031; OS Corynebacterium diphtheriae (strain HC02). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698968; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HC02; RX PubMed=22505676; DOI=10.1128/JB.00183-12; RA Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., RA Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., RA Santos C.S., Santos L.S., Hirata R.Jr., Mattos-Guaraldi A.L., RA Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.; RT "Pangenomic Study of Corynebacterium diphtheriae That Provides RT Insights into the Genomic Diversity of Pathogenic Isolates from Cases RT of Classical Diphtheria, Endocarditis, and Pneumonia."; RL J. Bacteriol. 194:3199-3215(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003213; AEX75532.1; -; Genomic_DNA. DR RefSeq; YP_005163823.1; NC_016802.1. DR EnsemblBacteria; AEX75532; AEX75532; CDHC02_0031. DR GeneID; 11739113; -. DR KEGG; cde:CDHC02_0031; -. DR KO; K00788; -. DR BioCyc; CDIP698968:GI5N-36-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). SQ SEQUENCE 222 AA; 23557 MW; BF4984E337961E70 CRC64; MLPTPRWGRD FDPRCYFVTG TGSVDHIVDV TRQAARAGAG LIQVRSKPIA ARDLYILGRE VARAVAEVNP RTRVLIDDRV DVALALMNNG EHIHGVHVGQ DDLPVRHVRA LLGDNAIIGL TTGTLELVRA SRQVAEVIDY IGAGPFRPTP TKDSGRAPVG LVGYPLLVAE SLVPVVAIGD VRPEDAADLA ATGVAGVAIV RALMNSQDVA ADVKLILKGF AQ // ID H2HLL1_CORDK Unreviewed; 222 AA. AC H2HLL1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-APR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CDHC03_0030; OS Corynebacterium diphtheriae (strain HC03). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698969; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HC03; RX PubMed=22505676; DOI=10.1128/JB.00183-12; RA Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., RA Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., RA Santos C.S., Santos L.S., Hirata R.Jr., Mattos-Guaraldi A.L., RA Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.; RT "Pangenomic Study of Corynebacterium diphtheriae That Provides RT Insights into the Genomic Diversity of Pathogenic Isolates from Cases RT of Classical Diphtheria, Endocarditis, and Pneumonia."; RL J. Bacteriol. 194:3199-3215(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003214; AEX77761.1; -; Genomic_DNA. DR RefSeq; YP_005137079.1; NC_016787.1. DR EnsemblBacteria; AEX77761; AEX77761; CDHC03_0030. DR GeneID; 11710774; -. DR KEGG; cdr:CDHC03_0030; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). SQ SEQUENCE 222 AA; 23499 MW; E139E5E250F1108E CRC64; MLPTPRWGRD FDPRCYFVTG TGSVDHIVDV ARQAARAGAG LIQVRSKPIA ARDLYILGRE VARAVAEVNP RTRVLIDDRV DVALALMNNG EHIHGVHVGQ DDLPVRHVRA LLGDNAIIGL TTGTLELVRA SRQVAEVIDY IGAGPFRPTP TKDSGRAPVG LAGYPPLVAE SLVPVVAIGD VRPEDAADLA ATGVAGVAIV RALMNSQDVA TDVKLVLKGF AQ // ID H2HTF7_CORDL Unreviewed; 222 AA. AC H2HTF7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-APR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CDHC04_0026; OS Corynebacterium diphtheriae (strain HC04). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698970; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HC04; RX PubMed=22505676; DOI=10.1128/JB.00183-12; RA Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., RA Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., RA Santos C.S., Santos L.S., Hirata R.Jr., Mattos-Guaraldi A.L., RA Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.; RT "Pangenomic Study of Corynebacterium diphtheriae That Provides RT Insights into the Genomic Diversity of Pathogenic Isolates from Cases RT of Classical Diphtheria, Endocarditis, and Pneumonia."; RL J. Bacteriol. 194:3199-3215(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003215; AEX80019.1; -; Genomic_DNA. DR RefSeq; YP_005139337.1; NC_016788.1. DR EnsemblBacteria; AEX80019; AEX80019; CDHC04_0026. DR GeneID; 11714434; -. DR KEGG; cda:CDHC04_0026; -. DR KO; K00788; -. DR BioCyc; CDIP698970:GHZI-31-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). SQ SEQUENCE 222 AA; 23499 MW; E139E5E250F1108E CRC64; MLPTPRWGRD FDPRCYFVTG TGSVDHIVDV ARQAARAGAG LIQVRSKPIA ARDLYILGRE VARAVAEVNP RTRVLIDDRV DVALALMNNG EHIHGVHVGQ DDLPVRHVRA LLGDNAIIGL TTGTLELVRA SRQVAEVIDY IGAGPFRPTP TKDSGRAPVG LAGYPPLVAE SLVPVVAIGD VRPEDAADLA ATGVAGVAIV RALMNSQDVA TDVKLVLKGF AQ // ID H2HZC8_CORDW Unreviewed; 199 AA. AC H2HZC8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-APR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CDPW8_0023; OS Corynebacterium diphtheriae (strain PW8). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PW8; RX PubMed=22505676; DOI=10.1128/JB.00183-12; RA Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., RA Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., RA Santos C.S., Santos L.S., Hirata R.Jr., Mattos-Guaraldi A.L., RA Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.; RT "Pangenomic Study of Corynebacterium diphtheriae That Provides RT Insights into the Genomic Diversity of Pathogenic Isolates from Cases RT of Classical Diphtheria, Endocarditis, and Pneumonia."; RL J. Bacteriol. 194:3199-3215(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003216; AEX68705.1; -; Genomic_DNA. DR RefSeq; YP_005141610.1; NC_016789.1. DR EnsemblBacteria; AEX68705; AEX68705; CDPW8_0023. DR GeneID; 11715156; -. DR KEGG; cdw:CDPW8_0023; -. DR KO; K00788; -. DR BioCyc; CDIP698964:GHZP-26-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 126 128 THZ-P binding (By similarity). FT METAL 55 55 Magnesium (By similarity). FT METAL 79 79 Magnesium (By similarity). FT BINDING 54 54 HMP-PP (By similarity). FT BINDING 98 98 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). SQ SEQUENCE 199 AA; 20847 MW; 26E973364CC13238 CRC64; MEHIVDVARQ AARAGAGLIQ VRSKPIAARD LYILGREVAR AVAEANPRTR VLIDDRVDVA LALMNNGEHI HGVHVGQDDL PVRHVRALLG DNAIIGLTTG TLELVRASRQ VAEAIDYIGA GPFRPTPTKD SGRAPVGLAG YPPLVAESLV PVVAIGDVRP EDAADLAATG VAGVAIVRAL MNSQDVATDV KLVLKGFAQ // ID H2I7G8_CORDV Unreviewed; 222 AA. AC H2I7G8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 16-APR-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CDVA01_0027; OS Corynebacterium diphtheriae (strain VA01). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698971; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VA01; RX PubMed=22505676; DOI=10.1128/JB.00183-12; RA Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., RA Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., RA Santos C.S., Santos L.S., Hirata R.Jr., Mattos-Guaraldi A.L., RA Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.; RT "Pangenomic Study of Corynebacterium diphtheriae That Provides RT Insights into the Genomic Diversity of Pathogenic Isolates from Cases RT of Classical Diphtheria, Endocarditis, and Pneumonia."; RL J. Bacteriol. 194:3199-3215(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003217; AEX82296.1; -; Genomic_DNA. DR RefSeq; YP_005143936.1; NC_016790.1. DR EnsemblBacteria; AEX82296; AEX82296; CDVA01_0027. DR GeneID; 11717702; -. DR KEGG; cdv:CDVA01_0027; -. DR KO; K00788; -. DR BioCyc; CDIP698971:GHYD-32-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). SQ SEQUENCE 222 AA; 23531 MW; B2C684FC3A060170 CRC64; MLPTPRWGRD FDPRCYFVTG TGSVDHIVDV TRQAARAGAG LIQVRSKPIA ARDLYILGRE VARAVAEVNP RTRVLIDDRV DVALALMNNG EHIHGIHVGQ DDLPVRHVRA LLGDNAIIGL TTGTLELVRA SRQVAEVIDY IGAGPFRPTP TKDSGRAPVG LVGYPSLVAE SLVPVVAIGD VRPEDAADLA ATGVAGVAIV RALMNSQDVA ADVKLVLKGF AQ // ID H2IFJ4_9VIBR Unreviewed; 441 AA. AC H2IFJ4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=VEJY3_15245; OS Vibrio sp. EJY3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1116375; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EJY3; RX PubMed=22535948; DOI=10.1128/JB.00303-12; RA Roh H., Yun E.J., Lee S., Ko H.J., Kim S., Kim B.Y., Song H., RA Lim K.I., Kim K.H., Choi I.G.; RT "Genome Sequence of Vibrio sp. Strain EJY3, an Agarolytic Marine RT Bacterium Metabolizing 3,6-Anhydro-L-Galactose as a Sole Carbon RT Source."; RL J. Bacteriol. 194:2773-2774(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003241; AEX23519.1; -; Genomic_DNA. DR RefSeq; YP_005024498.1; NC_016613.1. DR EnsemblBacteria; AEX23519; AEX23519; VEJY3_15245. DR GeneID; 11664950; -. DR KEGG; vej:VEJY3_15245; -. DR KO; K00788; -. DR BioCyc; VSP1116375:GJV8-3151-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 441 AA; 48767 MW; 80AA5F91C5EEF5C9 CRC64; MTKILIPSPL IELTGFVQQS LLLAKEQGFS TEKFELGISP THLIQLVLDP NKTLSVGTDL VDGFDEALTG DFTLYYQSNL SLKETSQQSS SAIFIGITDT SPTPNSDGNN ALLDIWRHPI TDEVRALSAN LSASNTFQAE HHLAWTVTLL ALEFPIEDAL TLARAMTNVS RETLFNGETC TLHEWASHFT DFPTPILEDA RLGIQVGWSS QSEAVSFPCL DKESLGLYPV VDDVSWIERL LPLGIKTIQL RIKNPDQSDL EEQIIRAIEL GRQYDAQVFI NDYWQLAIQH GAFGVHLGQE DIEESNLIQL SEAGIHLGLS THGYYELLRI VQINPSYIAL GHIFPTTTKQ MPSKPQGLIR LALYQKLIDS IPYGKQVGYP TVAIGGIDQS NAELVWRCGV SSLAVVRAIT LSESPKSVIE FFNQLMGSAQ PLQVVENESA Y // ID H2IJA9_9VIBR Unreviewed; 204 AA. AC H2IJA9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VEJY3_16181; OS Vibrio sp. EJY3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1116375; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EJY3; RX PubMed=22535948; DOI=10.1128/JB.00303-12; RA Roh H., Yun E.J., Lee S., Ko H.J., Kim S., Kim B.Y., Song H., RA Lim K.I., Kim K.H., Choi I.G.; RT "Genome Sequence of Vibrio sp. Strain EJY3, an Agarolytic Marine RT Bacterium Metabolizing 3,6-Anhydro-L-Galactose as a Sole Carbon RT Source."; RL J. Bacteriol. 194:2773-2774(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003242; AEX23657.1; -; Genomic_DNA. DR RefSeq; YP_005024631.1; NC_016614.1. DR EnsemblBacteria; AEX23657; AEX23657; VEJY3_16181. DR GeneID; 11668090; -. DR KEGG; vej:VEJY3_16181; -. DR KO; K00788; -. DR BioCyc; VSP1116375:GJV8-3293-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21940 MW; 1BA846ADE497D96F CRC64; MNAYRLYLVT DDQQDLATLK HVVSKAVEGG VTMVQVREKH GDVRAFIERA QAVKDILKNT NVPLIINDRV DVALAVDADG VHLGQSDMPA HIARELIGPN KILGLSIEDE QQLAEVDTLP IDYIGLSAIY ATPTKTNTQK HWDIDGLKMA LNTTSLPIVA IGGINESTIP ALSATGVHGL ALVSAICHAD DPKLACEYLL SLMA // ID H2IVU3_RAHAC Unreviewed; 217 AA. AC H2IVU3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rahaq2_4236; OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC OS 105701 / NCIMB 13365 / CIP 78.65). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Rahnella. OX NCBI_TaxID=745277; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / RC CIP 78.65; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P., RA Martinez R., Woyke T.; RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003244; AEX53998.1; -; Genomic_DNA. DR RefSeq; YP_005202138.1; NC_016818.1. DR EnsemblBacteria; AEX53998; AEX53998; Rahaq2_4236. DR GeneID; 11793446; -. DR KEGG; raq:Rahaq2_4236; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23355 MW; 05931863C236C49F CRC64; MNQSAQPFPA VPFHLGLYPV VDTVEWIARL LDAGVKTLQL RVKDLSDEEV EPAIIDAIAL GKKYQARLFI NDYWRLAVKH QAYGVHLGQE DLDTADLEAI RQAGLRLGVS THDDTELARA VAVNPSYIAL GHIFPTQTKD MPSAPQGLAE LTRHIKKLDG NFPTVAIGGI SIDRAPSVLD CGVGSIAVVS AITQAADWRA ATAQLLALCA SKVPEDA // ID H2JBJ2_9CLOT Unreviewed; 215 AA. AC H2JBJ2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Clo1100_2987; OS Clostridium sp. BNL1100. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=755731; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BNL1100; RX PubMed=23209234; DOI=10.1128/JB.01908-12; RA Li L.L., Taghavi S., Izquierdo J.A., van der Lelie D.; RT "Complete Genome Sequence of Clostridium sp. Strain BNL1100, a RT Cellulolytic Mesophile Isolated from Corn Stover."; RL J. Bacteriol. 194:6982-6983(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003259; AEY67138.1; -; Genomic_DNA. DR RefSeq; YP_005148943.1; NC_016791.1. DR EnsemblBacteria; AEY67138; AEY67138; Clo1100_2987. DR GeneID; 11720859; -. DR KEGG; clb:Clo1100_2987; -. DR KO; K00788; -. DR BioCyc; CSP755731:GJVM-2985-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 215 AA; 23324 MW; 3C96CBAA8E82E3DB CRC64; MLIYVTNRNL CRDDFLNRIA CLASGKPHAI ILREKDLSPE DYQTLAEKVK VICDSAGVQL IVNKYITAAK NLGVSSVHVS MEDFLKYRDA LQSFSKVWVS VHSAKEAQEA CNSGASTLIA GHIYETDCKK GVSPRGLDFL REVCSSVSIP VFGIGGITQD RIKGVTGAGA KGVCMMSEAM TCLSPTSLSS RILAFTLEDS CYTVTDCYYN KNGGK // ID H2JEE4_9CLOT Unreviewed; 210 AA. AC H2JEE4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Clo1100_2344; OS Clostridium sp. BNL1100. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=755731; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BNL1100; RX PubMed=23209234; DOI=10.1128/JB.01908-12; RA Li L.L., Taghavi S., Izquierdo J.A., van der Lelie D.; RT "Complete Genome Sequence of Clostridium sp. Strain BNL1100, a RT Cellulolytic Mesophile Isolated from Corn Stover."; RL J. Bacteriol. 194:6982-6983(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003259; AEY66518.1; -; Genomic_DNA. DR RefSeq; YP_005148323.1; NC_016791.1. DR EnsemblBacteria; AEY66518; AEY66518; Clo1100_2344. DR GeneID; 11722685; -. DR KEGG; clb:Clo1100_2344; -. DR KO; K00788; -. DR BioCyc; CSP755731:GJVM-2342-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22438 MW; 1D13F2E4FEE0429B CRC64; MNSKIDYTLY LVTDRDLMST KTLEEAVEQA IMGGCTLVQL REKTASSREF YQTALKVKAI TDNYKVPLII NDRVDIALAI GADGVHVGQS DLPAVVVRKI IGKDRILGVS AGSVEKAIEA QRDGADYIGV GALFSTSTKT DAKSVSKETL MKILKEVSIP IVGIGGINAQ NAVELKNTGI DGIAVVSAII AQKDIKLSAE KMLEIFGKKA // ID H2JWV6_STRHJ Unreviewed; 216 AA. AC H2JWV6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SHJG_3587; OS Streptomyces hygroscopicus subsp. jinggangensis (strain 5008). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1133850; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5008; RA Wu H., Bai L.; RT "Genomic analysis of Streptomyces hygroscopicus subsp. jinggangensis RT 5008."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003275; AEY88859.1; -; Genomic_DNA. DR RefSeq; YP_006244732.1; NC_017765.1. DR EnsemblBacteria; AEY88859; AEY88859; SHJG_3587. DR GeneID; 12809858; -. DR KEGG; shy:SHJG_3587; -. DR KO; K00788; -. DR BioCyc; SHYG1133850:GLLU-3593-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22849 MW; B5E254F070BA0AE9 CRC64; MSDTARAALA DARLYLCTDA RERQGDLPEF LDAVLAGGVD IVQLRDKGME AAEELEHLEV FADACARHGK LLAVNDRADV AHAARADVLH LGQGDLPVPA ARAILGDRVL IGRSTHAEAE AAAAAVQEGV DYFCTGPCWP TPTKPGRHAP GLDLVRYAAG LGTDRPWFAI GGIDLGNLDQ VLDAGARRVV VVRAITEADD PGAAATEFAK RLRDAR // ID H2VFR1_ZYMMO Unreviewed; 238 AA. AC H2VFR1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ZMO0332; OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=264203; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31821 / ZM4 / CP4; RX PubMed=15592456; DOI=10.1038/nbt1045; RA Seo J.S., Chong H., Park H.S., Yoon K.O., Jung C., Kim J.J., RA Hong J.H., Kim H., Kim J.H., Kil J.I., Park C.J., Oh H.M., Lee J.S., RA Jin S.J., Um H.W., Lee H.J., Oh S.J., Kim J.Y., Kang H.L., Lee S.Y., RA Lee K.J., Kang H.S.; RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis RT ZM4."; RL Nat. Biotechnol. 23:63-68(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008692; AAV88956.1; -; Genomic_DNA. DR RefSeq; YP_162067.1; NC_006526.2. DR ProteinModelPortal; H2VFR1; -. DR EnsemblBacteria; AAV88956; AAV88956; ZMO0332. DR GeneID; 3188243; -. DR KEGG; zmo:ZMO0332; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 158 160 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 161 161 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 238 AA; 25614 MW; B79C390DBF103D9D CRC64; MAENEILTDN DEALDAFTNN YQRPSENPCG LYLISPPEID EHFVERLKKA FDGGDVSAFQ LRLKGLNEHA IARLAEPLQK VCADRDVAFI VNDSVSLAKR LGADGVHLGQ GDGDAAEARV ILGPSAQIGV TCHNSRHLAM IAGEKGADYV AFGAFYPTTS KDVRYYARPE ILSWWATLFE LPSVAIGGIT TENVAPIVKA GADFVAVCAG IWKAKEGEDK AVAHFNTVLD QAVKGEIA // ID H3K8L7_9FIRM Unreviewed; 216 AA. AC H3K8L7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9454_01590; OS Megamonas funiformis YIT 11815. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megamonas. OX NCBI_TaxID=742816; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11815; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G., RA Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., RA Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Megamonas funiformis YIT 11815."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMB01000072; EHR35892.1; -; Genomic_DNA. DR EnsemblBacteria; EHR35892; EHR35892; HMPREF9454_01590. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23970 MW; A45E7505F59C7C4C CRC64; MRKEMEHFIN NPIYTITAEA MSNGRNNIEV VGKMLEAGIK FIQYREKEKP ALERYQECMQ LVKMTKEAGA IFIIDDFVDL AMAVNADGVH IGQTDLPPQV VRQLIGEDKI LGLSTHEESQ LQKANELGDI IDYIGVGPVY ATQTKKDAVP VGFSYVDYAS KYAKHPFVAI GGIKEHNICE VASHGAKTFA IVSEIVSADD IVNKIKSIEK TLQNKL // ID H3KG10_9BURK Unreviewed; 213 AA. AC H3KG10; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9440_01684; OS Sutterella parvirubra YIT 11816. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Sutterellaceae; Sutterella. OX NCBI_TaxID=762967; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11816; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBQ01000257; EHY30936.1; -; Genomic_DNA. DR EnsemblBacteria; EHY30936; EHY30936; HMPREF9440_01684. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 21822 MW; 29ABDA5AD83DCC48 CRC64; MKTFDLSLYL VLDPDLCGGA EGMLRTTEEA LEGGVTIVQL RAPTWKKRAL AACARDLLEI LRPRGIPLII NDHADVAAAV GADGLHVGQD DLSPADARRI IGPDMILGLS AGCMAEVRGA DPALVDYLGI GPVWATATKK DAGEAVGLDG LAALRAATPL PVVAIGGIGA SNAADVMRTG VDGIAVVSAI CGQASPRTAA ENLLVQLRIA DRS // ID H3KWT3_ECOLX Unreviewed; 211 AA. AC H3KWT3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC2B_4829; OS Escherichia coli DEC2B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868139; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFJB01000039; EHU34612.1; -; Genomic_DNA. DR EnsemblBacteria; EHU34612; EHU34612; ECDEC2B_4829. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23000 MW; CC43679342B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H3L324_BIFBR Unreviewed; 917 AA. AC H3L324; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE SubName: Full=Thiamine biosynthesis; GN ORFNames=CECT7263_19632; OS Bifidobacterium breve CECT 7263. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=1036735; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CECT 7263; RX PubMed=22740680; DOI=10.1128/JB.00691-12; RA Jimenez E., Villar-Tajadura M.A., Marin M., Fontecha J., Requena T., RA Arroyo R., Fernandez L., Rodriguez J.M.; RT "Complete Genome Sequence of Bifidobacterium breve CECT 7263, a Strain RT Isolated from Human Milk."; RL J. Bacteriol. 194:3762-3763(2012). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFVV01000033; EHS84639.1; -; Genomic_DNA. DR EnsemblBacteria; EHS84639; EHS84639; CECT7263_19632. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. SQ SEQUENCE 917 AA; 100206 MW; 30F82904651CF3EB CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVQLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLAGTKA AGWFAVSAIA GAENPEGATR AMVEGWKAVR GDKKHGYAPR VVAHTPAADT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AQDRDDAISK ARFEFRWLDQ FNLSYDPDTA IAFHDETLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LAKAKANVDN DVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID H3LFZ7_KLEOX Unreviewed; 211 AA. AC H3LFZ7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9686_04482; OS Klebsiella oxytoca 10-5242. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=883117; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-5242; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Taylor N., Fox J., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Klebsiella oxytoca 10-5242."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGDI01000024; EHS92489.1; -; Genomic_DNA. DR EnsemblBacteria; EHS92489; EHS92489; HMPREF9686_04482. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23008 MW; 09B1F3A41ADFD0D7 CRC64; MYQPDFPSVP FRLGLYPVVD SVTWIERLLA AGVRTLQLRI KDKRDSEVEE HVVAAIALGR IYHARLFIND YWRLAIKHQA YGVHLGQEDL ETTDLSAIRN AGLRLGVSTH DDMEIDIALA ARPSYIALGH VFPTQTKQMP SAPQGLDQLA QHIQRLGDYP TVAIGGISLE HAPAVLATGV GSVAVVSAIT QAADWRQATA RLLEIAGAGD E // ID H3LYS3_KLEOX Unreviewed; 211 AA. AC H3LYS3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9687_05355; OS Klebsiella oxytoca 10-5243. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=883118; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-5243; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Taylor N., Fox J., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Klebsiella oxytoca 10-5243."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGDJ01000037; EHS87964.1; -; Genomic_DNA. DR EnsemblBacteria; EHS87964; EHS87964; HMPREF9687_05355. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23142 MW; 1DE5E317DB2164FB CRC64; MYQPDFPSVP FRLGLYPVVD SVAWIERLLA AGVRTLQLRI KDKRDSDVED DVVAAITLGR KYHARLFIND YWRLAIKHQA YGVHLGQEDL ETTDLSAIRN AGLRLGVSTH DDMEMDIALA ARPSYIALGH VFPTQTKQMP SSPQGLDQLA QHIQRLEDYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QATDWRQATA RLLEIAGAGD E // ID H3MDT0_KLEOX Unreviewed; 211 AA. AC H3MDT0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9689_05118; OS Klebsiella oxytoca 10-5245. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=883120; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-5245; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Taylor N., Fox J., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Klebsiella oxytoca 10-5245."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGDL01000043; EHS88898.1; -; Genomic_DNA. DR EnsemblBacteria; EHS88898; EHS88898; HMPREF9689_05118. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23112 MW; 00533180510021FB CRC64; MYQPDFPSVP FRLGLYPVVD SVAWIERLLA AGVRTLQLRI KDKRDSDVED DVVAAIALGR KYHARLFIND YWRLAIKHQA YGVHLGQEDL ETTDLSAIRN AGLRLGVSTH DDMEMDIALA ARPSYIALGH VFPTQTKQMP SSPQGLDQLA QHIQRLEDYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QATDWRQATA RLLEIAGAGD E // ID H3MFL9_KLEOX Unreviewed; 211 AA. AC H3MFL9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9690_00022; OS Klebsiella oxytoca 10-5246. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=883121; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-5246; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Taylor N., Fox J., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Klebsiella oxytoca 10-5246."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGDM01000002; EHT15057.1; -; Genomic_DNA. DR EnsemblBacteria; EHT15057; EHT15057; HMPREF9690_00022. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23079 MW; 528B51AC453BD969 CRC64; MYQPDFPSVP FRLGLYPVVD SVVWIERLLK AGVRTLQLRI KDKRDSDVED DVIAAIALGR QYHARLFIND YWQLAIKHQA YGVHLGQEDL ETTDLSAIRN AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIQRLEDYP TVAIGGISLE RAPAVLGTGV GSIAVVSAIT QTADWQQATA QLLTIAGAGD E // ID H3N5M2_KLEOX Unreviewed; 211 AA. AC H3N5M2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9694_03480; OS Klebsiella oxytoca 10-5250. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=883125; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-5250; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Taylor N., Fox J., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Klebsiella oxytoca 10-5250."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGDP01000016; EHT09422.1; -; Genomic_DNA. DR EnsemblBacteria; EHT09422; EHT09422; HMPREF9694_03480. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23051 MW; 353EC08FD96CA623 CRC64; MYQPDFPSVP FRLGLYPVVD SVAWIERLLD AGVRTVQLRI KDKHDSEVED DVVAAIALGR KYDARLFIND YWRLAIKHQA YGVHLGQEDL ETTDLRAIRN AGLRLGVSTH DDMEIDIALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA QHILRLDDYP TVAIGGISLE RAAGVLATGV GSVAVVSAIT QAADWRQATA RLLEIAGAGD E // ID H3NER9_9LACT Unreviewed; 210 AA. AC H3NER9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9703_01050; OS Dolosigranulum pigrum ATCC 51524. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Dolosigranulum. OX NCBI_TaxID=883103; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51524; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G., RA Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., RA Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Dolosigranulum pigrum ATCC 51524."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEF01000009; EHR32934.1; -; Genomic_DNA. DR EnsemblBacteria; EHR32934; EHR32934; HMPREF9703_01050. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22834 MW; FD8DF5D9BF7D0AA9 CRC64; MKTDIYTLYL VTDRFDYTDD EFFSIIEEAC QAGVTLVQLR EKKATTNRFF HLAQKVKTIT DKYDVPLIIN DRVDICLAVD AAGVHIGDDE LPIDVARSLI GPNKLLGVSA DTLERANEAQ QLGADYLGIG AVFPSSTKAD CETVSLDTVR QINDRSALPS VAIGGINQDN IIQLEKTGIT GISLVSAIMQ ADNVSETTGQ LLQQVRAITT // ID H3P0J8_LACPN Unreviewed; 217 AA. AC H3P0J8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=nc8_0114; OS Lactobacillus plantarum subsp. plantarum NC8. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1036177; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=22493200; DOI=10.1128/JB.00141-12; RA Axelsson L., Rud I., Naterstad K., Blom H., Renckens B., Boekhorst J., RA Kleerebezem M., van Hijum S., Siezen R.J.; RT "Genome Sequence of the Naturally Plasmid-Free Lactobacillus plantarum RT Strain NC8 (CCUG 61730)."; RL J. Bacteriol. 194:2391-2392(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGRI01000002; EHS83812.1; -; Genomic_DNA. DR ProteinModelPortal; H3P0J8; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22751 MW; 485246DDAE17215A CRC64; MTLKFEPTQL RAYFVCGTQD VPGQDLNVVV QTALDAGITA FQYRDKGNSQ LTTAERFALG QQLRERCAQA HVPFIVDDDV ELALALQADG IHVGQKDDRV TQVIQRVANQ MFVGLSCSTL AEVQIANQLE GIAYLGSGPI FPTTSKADAD PVVGLTGLRQ LVVTATCPVV AIGGITVAQL PAIAATGAAG AAVISMLTRS PDMAATVKAM LTATEGH // ID H3PAE8_BRUAO Unreviewed; 203 AA. AC H3PAE8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M17_01339; OS Brucella abortus bv. 1 str. NI435a. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051055; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI435a; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI435a."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVF01000009; EHR12582.1; -; Genomic_DNA. DR ProteinModelPortal; H3PAE8; -. DR EnsemblBacteria; EHR12582; EHR12582; M17_01339. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID H3PF64_BRUAO Unreviewed; 221 AA. AC H3PF64; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 11. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M17_02999; OS Brucella abortus bv. 1 str. NI435a. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051055; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI435a; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI435a."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVF01000015; EHR07019.1; -; Genomic_DNA. DR ProteinModelPortal; H3PF64; -. DR EnsemblBacteria; EHR07019; EHR07019; M17_02999. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID H3PGZ6_BRUAO Unreviewed; 203 AA. AC H3PGZ6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M19_00508; OS Brucella abortus bv. 1 str. NI474. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051056; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI474; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI474."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVG01000003; EHR13700.1; -; Genomic_DNA. DR ProteinModelPortal; H3PGZ6; -. DR EnsemblBacteria; EHR13700; EHR13700; M19_00508. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID H3PPA9_BRUAO Unreviewed; 221 AA. AC H3PPA9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 11. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M19_03071; OS Brucella abortus bv. 1 str. NI474. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051056; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI474; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI474."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVG01000015; EHR06829.1; -; Genomic_DNA. DR ProteinModelPortal; H3PPA9; -. DR EnsemblBacteria; EHR06829; EHR06829; M19_03071. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID H3PWE9_BRUAO Unreviewed; 203 AA. AC H3PWE9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M1A_02430; OS Brucella abortus bv. 1 str. NI486. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051057; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI486; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI486."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVH01000015; EHR08778.1; -; Genomic_DNA. DR ProteinModelPortal; H3PWE9; -. DR EnsemblBacteria; EHR08778; EHR08778; M1A_02430. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID H3PY32_BRUAO Unreviewed; 221 AA. AC H3PY32; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M1A_03071; OS Brucella abortus bv. 1 str. NI486. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051057; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI486; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI486."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVH01000021; EHR06637.1; -; Genomic_DNA. DR ProteinModelPortal; H3PY32; -. DR EnsemblBacteria; EHR06637; EHR06637; M1A_03071. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID H3Q556_BRUAO Unreviewed; 203 AA. AC H3Q556; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M1E_02356; OS Brucella abortus bv. 1 str. NI488. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051058; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI488; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI488."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVI01000021; EHR19053.1; -; Genomic_DNA. DR ProteinModelPortal; H3Q556; -. DR EnsemblBacteria; EHR19053; EHR19053; M1E_02356. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID H3Q705_BRUAO Unreviewed; 221 AA. AC H3Q705; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M1E_03005; OS Brucella abortus bv. 1 str. NI488. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051058; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI488; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI488."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVI01000027; EHR16122.1; -; Genomic_DNA. DR ProteinModelPortal; H3Q705; -. DR EnsemblBacteria; EHR16122; EHR16122; M1E_03005. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID H3Q8U5_BRUAO Unreviewed; 203 AA. AC H3Q8U5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M1G_00508; OS Brucella abortus bv. 1 str. NI010. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051059; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI010; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI010."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVJ01000003; EHR22362.1; -; Genomic_DNA. DR ProteinModelPortal; H3Q8U5; -. DR EnsemblBacteria; EHR22362; EHR22362; M1G_00508. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID H3QFY3_BRUAO Unreviewed; 221 AA. AC H3QFY3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M1G_02996; OS Brucella abortus bv. 1 str. NI010. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051059; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI010; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI010."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVJ01000012; EHR16285.1; -; Genomic_DNA. DR ProteinModelPortal; H3QFY3; -. DR EnsemblBacteria; EHR16285; EHR16285; M1G_02996. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID H3QHS1_BRUAO Unreviewed; 203 AA. AC H3QHS1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M1I_00507; OS Brucella abortus bv. 1 str. NI016. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051060; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI016; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI016."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVK01000002; EHR22818.1; -; Genomic_DNA. DR ProteinModelPortal; H3QHS1; -. DR EnsemblBacteria; EHR22818; EHR22818; M1I_00507. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID H3QQ32_BRUAO Unreviewed; 221 AA. AC H3QQ32; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 11. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M1I_03068; OS Brucella abortus bv. 1 str. NI016. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051060; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI016; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI016."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVK01000012; EHR16542.1; -; Genomic_DNA. DR ProteinModelPortal; H3QQ32; -. DR EnsemblBacteria; EHR16542; EHR16542; M1I_03068. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID H3QTR3_BRUAO Unreviewed; 203 AA. AC H3QTR3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M1K_01337; OS Brucella abortus bv. 1 str. NI021. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051061; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI021; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI021."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVL01000008; EHR29592.1; -; Genomic_DNA. DR ProteinModelPortal; H3QTR3; -. DR EnsemblBacteria; EHR29592; EHR29592; M1K_01337. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID H3QZ13_BRUAO Unreviewed; 221 AA. AC H3QZ13; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M1K_03071; OS Brucella abortus bv. 1 str. NI021. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051061; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI021; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI021."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVL01000017; EHR24328.1; -; Genomic_DNA. DR ProteinModelPortal; H3QZ13; -. DR EnsemblBacteria; EHR24328; EHR24328; M1K_03071. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID H3R741_BRUAO Unreviewed; 203 AA. AC H3R741; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M1M_02723; OS Brucella abortus bv. 1 str. NI259. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051062; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI259; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI259."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVM01000011; EHR25147.1; -; Genomic_DNA. DR ProteinModelPortal; H3R741; -. DR EnsemblBacteria; EHR25147; EHR25147; M1M_02723. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID H3R7Z8_BRUAO Unreviewed; 221 AA. AC H3R7Z8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=M1M_03074; OS Brucella abortus bv. 1 str. NI259. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=1051062; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI259; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Ward D., Whatmore A., Skuce R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Brucella abortus bv. 1 NI259."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVM01000013; EHR24521.1; -; Genomic_DNA. DR ProteinModelPortal; H3R7Z8; -. DR EnsemblBacteria; EHR24521; EHR24521; M1M_03074. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID H3RJ24_PANSE Unreviewed; 210 AA. AC H3RJ24; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-APR-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CKS_0011; OS Pantoea stewartii subsp. stewartii DC283. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=660596; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DC283; RX PubMed=22111898; DOI=10.1111/j.1365-2958.2011.07926.x; RA Wang X., Yang F., von Bodman S.B.; RT "The genetic and structural basis of two distinct terminal side branch RT residues in stewartan and amylovoran exopolysaccharides and their RT potential role in host adaptation."; RL Mol. Microbiol. 83:195-207(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DC283; RA Biehl B.S., Ding Y., Dugan-Rocha S.P., Gibbs R.A., Glasner J.D., RA Kovar C., Muzny D.M., Neeno-Eckwall E.C., Perna N.T., Qin X., RA von Bodman S.B., Weinstock G.M.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHIE01000036; EHT98619.1; -; Genomic_DNA. DR EnsemblBacteria; EHT98619; EHT98619; CKS_0011. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23062 MW; 19FD2DBF6305111D CRC64; MNAFPATAPR LGLYPVVDSV EWIERLLDAG VRTIQLRIKD LPDEIVEPTI IQAIATGQRY QARLFINDYW QLAIKHKAYG VHLGQEDLAV ANVQRILDAG LRLGISTHDD AELDRALALR PSYIALGHIF PTQTKVMPSS PQGLSELKRH LSRLQGISTV AIGGISIDRV PAVLETGVGS IAVVSAITQA EDWRAATREL LRLVEHESGH // ID H3RPB5_9LACO Unreviewed; 207 AA. AC H3RPB5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LBLM1_07550; OS Lactobacillus mucosae LM1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1130798; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LM1; RX PubMed=22887668; DOI=10.1128/JB.01011-12; RA Lee J.H., Valeriano V.D., Shin Y.R., Chae J.P., Kim G.B., Ham J.S., RA Chun J., Kang D.K.; RT "Genome Sequence of Lactobacillus mucosae LM1, Isolated from Piglet RT Feces."; RL J. Bacteriol. 194:4766-4766(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHIT01000020; EHT16352.1; -; Genomic_DNA. DR EnsemblBacteria; EHT16352; EHT16352; LBLM1_07550. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22375 MW; 56CCFFABC93EF60C CRC64; MLHCYLVGGT QDVNHDPKRF LNDVSIAMDS GITAFQYREK GTSQLNQEQR VQLGLKLRRL ADQHHIPLIV DDDVELAQAI NADGIHVGQK DQRVEQVLAA VGNTMFVGYS CNQPAQIKHA NQLPVAYVGS GPIFPTSSKN DADPAMGLEK LHGLVTISTH PIVAIGGITE ANMIQTLAAG VAGLSMISMI LQSADIQKTV QHINSLY // ID H3S0M0_STAAU Unreviewed; 213 AA. AC H3S0M0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1114_2663; OS Staphylococcus aureus subsp. aureus CIG1114. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931433; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1114; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKD01000013; EHT17725.1; -; Genomic_DNA. DR ProteinModelPortal; H3S0M0; -. DR SMR; H3S0M0; 4-209. DR PRIDE; H3S0M0; -. DR EnsemblBacteria; EHT17725; EHT17725; SACIG1114_2663. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3S8U9_STAAU Unreviewed; 213 AA. AC H3S8U9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1605_2843; OS Staphylococcus aureus subsp. aureus CIG1605. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931438; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1605; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKE01000014; EHT33415.1; -; Genomic_DNA. DR ProteinModelPortal; H3S8U9; -. DR EnsemblBacteria; EHT33415; EHT33415; SACIG1605_2843. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3S9P1_9BACL Unreviewed; 217 AA. AC H3S9P1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PDENDC454_01100; OS Paenibacillus dendritiformis C454. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1131935; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C454; RX PubMed=22461558; DOI=10.1128/JB.00158-12; RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A., RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., RA Nikolaev V., Gutnick D.L., Lancet D., Ben-Jacob E.; RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus RT dendritiformis C454 Chiral Morphotype."; RL J. Bacteriol. 194:2127-2128(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKH01000002; EHQ64159.1; -; Genomic_DNA. DR EnsemblBacteria; EHQ64159; EHQ64159; PDENDC454_01100. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22781 MW; A6E40D81ECA9FAB5 CRC64; MSRLRPEEIR AHLRLYLVMG SVNCRMDPVQ VAEEALAGGV SVLQYREKGT GALTGDDKRR LGAELQAVCK RHGVPFIVND DLELALELGA DGIHIGQQDE RADRVRSRIG DLMLGVSAHT VEEARLAIEQ GADYLGIGPI YPTQSKEDAL EAQGPSIIVD IRAAGINVPL VGIGGITLAN AGAVLEAGAD GIAVISALTG SDDIRAAAAS FRRLGPG // ID H3SST2_PSEAE Unreviewed; 315 AA. AC H3SST2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=O1O_04856; OS Pseudomonas aeruginosa MPAO1/P1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1131757; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MPAO1/P1; RX PubMed=22952955; DOI=10.1371/journal.pone.0044326; RA Olivas A.D., Shogan B.D., Valuckaite V., Zaborin A., Belogortseva N., RA Musch M., Meyer F., L Trimble W., An G., Gilbert J., Zaborina O., RA Alverdy J.C.; RT "Intestinal Tissues Induce an SNP Mutation in Pseudomonas aeruginosa RT That Enhances Its Virulence: Possible Role in Anastomotic Leak."; RL PLoS ONE 7:E44326-E44326(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKM01000006; EHS39001.1; -; Genomic_DNA. DR ProteinModelPortal; H3SST2; -. DR SMR; H3SST2; 6-123, 127-313. DR EnsemblBacteria; EHS39001; EHS39001; O1O_04856. DR OMA; RWLAASC; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34055 MW; 9165F7469596B47A CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EDGEPVRAAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEAHGAEGQ PLAWVEPREL ADYEFPAANA PIVQAARLPA HYLITPDGLE PGELISGVRK AVEAGIRLIQ LRAPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDAEELAL AASMGVEFVT LSPVQPTESH PGEPALGWDK AAELIAGFNQ PVYLLGGLGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID H3T278_PSEAE Unreviewed; 209 AA. AC H3T278; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=O1O_21075; OS Pseudomonas aeruginosa MPAO1/P1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1131757; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MPAO1/P1; RX PubMed=22952955; DOI=10.1371/journal.pone.0044326; RA Olivas A.D., Shogan B.D., Valuckaite V., Zaborin A., Belogortseva N., RA Musch M., Meyer F., L Trimble W., An G., Gilbert J., Zaborina O., RA Alverdy J.C.; RT "Intestinal Tissues Induce an SNP Mutation in Pseudomonas aeruginosa RT That Enhances Its Virulence: Possible Role in Anastomotic Leak."; RL PLoS ONE 7:E44326-E44326(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKM01000038; EHS34883.1; -; Genomic_DNA. DR ProteinModelPortal; H3T278; -. DR SMR; H3T278; 24-200. DR EnsemblBacteria; EHS34883; EHS34883; O1O_21075. DR OMA; CTGPVWA; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22146 MW; 898DA261D0AFA265 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER HGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAQ LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID H3T8Y3_PSEAE Unreviewed; 315 AA. AC H3T8Y3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=O1Q_03698; OS Pseudomonas aeruginosa MPAO1/P2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1131758; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MPAO1/P2; RA Olivas A.D., Zaborina O., Valuckaite V., Poroyko V., Zaborin A., RA Musch M., Umaskiy K., Shogan B., Trimble W.L., Gilbert J., RA Alverdy J.C.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKN01000009; EHS43988.1; -; Genomic_DNA. DR ProteinModelPortal; H3T8Y3; -. DR SMR; H3T8Y3; 6-123, 127-313. DR EnsemblBacteria; EHS43988; EHS43988; O1Q_03698. DR OMA; RWLAASC; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34055 MW; 9165F7469596B47A CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EDGEPVRAAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEAHGAEGQ PLAWVEPREL ADYEFPAANA PIVQAARLPA HYLITPDGLE PGELISGVRK AVEAGIRLIQ LRAPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDAEELAL AASMGVEFVT LSPVQPTESH PGEPALGWDK AAELIAGFNQ PVYLLGGLGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID H3TFK2_PSEAE Unreviewed; 209 AA. AC H3TFK2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=O1Q_15485; OS Pseudomonas aeruginosa MPAO1/P2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1131758; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MPAO1/P2; RA Olivas A.D., Zaborina O., Valuckaite V., Poroyko V., Zaborin A., RA Musch M., Umaskiy K., Shogan B., Trimble W.L., Gilbert J., RA Alverdy J.C.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKN01000051; EHS41585.1; -; Genomic_DNA. DR ProteinModelPortal; H3TFK2; -. DR SMR; H3TFK2; 24-200. DR EnsemblBacteria; EHS41585; EHS41585; O1Q_15485. DR OMA; CTGPVWA; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22146 MW; 898DA261D0AFA265 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER HGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAQ LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID H3TR19_STAAU Unreviewed; 213 AA. AC H3TR19; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21342_2616; OS Staphylococcus aureus subsp. aureus 21342. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904772; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21342; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKU01000046; EHQ70292.1; -; Genomic_DNA. DR ProteinModelPortal; H3TR19; -. DR EnsemblBacteria; EHQ70292; EHQ70292; SA21342_2616. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3TZM1_STAAU Unreviewed; 213 AA. AC H3TZM1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21343_1865; OS Staphylococcus aureus subsp. aureus 21343. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904773; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21343; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKV01000021; EHQ69368.1; -; Genomic_DNA. DR ProteinModelPortal; H3TZM1; -. DR SMR; H3TZM1; 4-209. DR PRIDE; H3TZM1; -. DR EnsemblBacteria; EHQ69368; EHQ69368; SA21343_1865. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3U4U1_STAAU Unreviewed; 213 AA. AC H3U4U1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SA21345_2186; OS Staphylococcus aureus subsp. aureus 21345. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904774; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=21345; RA Jones M., Durkin A.S., Kim M., Kreiswirth B., Mishra P., Singh I., RA Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKW01000006; EHQ71504.1; -; Genomic_DNA. DR ProteinModelPortal; H3U4U1; -. DR EnsemblBacteria; EHQ71504; EHQ71504; SA21345_2186. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3UBX1_STAEP Unreviewed; 160 AA. AC H3UBX1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU041_1718; OS Staphylococcus epidermidis VCU041. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904320; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU041; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKX01000003; EHQ78089.1; -; Genomic_DNA. DR ProteinModelPortal; H3UBX1; -. DR EnsemblBacteria; EHQ78089; EHQ78089; SEVCU041_1718. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID H3UDF8_STAEP Unreviewed; 213 AA. AC H3UDF8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU041_0479; OS Staphylococcus epidermidis VCU041. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904320; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU041; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKX01000019; EHQ76758.1; -; Genomic_DNA. DR ProteinModelPortal; H3UDF8; -. DR EnsemblBacteria; EHQ76758; EHQ76758; SEVCU041_0479. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3UJ12_STAEP Unreviewed; 160 AA. AC H3UJ12; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU057_2133; OS Staphylococcus epidermidis VCU057. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904323; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU057; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKY01000003; EHQ80186.1; -; Genomic_DNA. DR ProteinModelPortal; H3UJ12; -. DR EnsemblBacteria; EHQ80186; EHQ80186; SEVCU057_2133. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID H3UN06_STAEP Unreviewed; 213 AA. AC H3UN06; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU057_0028; OS Staphylococcus epidermidis VCU057. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904323; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU057; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKY01000068; EHQ75359.1; -; Genomic_DNA. DR ProteinModelPortal; H3UN06; -. DR EnsemblBacteria; EHQ75359; EHQ75359; SEVCU057_0028. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3USY8_STAEP Unreviewed; 213 AA. AC H3USY8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU065_1202; OS Staphylococcus epidermidis VCU065. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904324; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU065; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKZ01000035; EHQ78667.1; -; Genomic_DNA. DR ProteinModelPortal; H3USY8; -. DR EnsemblBacteria; EHQ78667; EHQ78667; SEVCU065_1202. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3UXA4_STAEP Unreviewed; 160 AA. AC H3UXA4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU065_0509; OS Staphylococcus epidermidis VCU065. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904324; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU065; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKZ01000083; EHQ74320.1; -; Genomic_DNA. DR ProteinModelPortal; H3UXA4; -. DR EnsemblBacteria; EHQ74320; EHQ74320; SEVCU065_0509. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID H3V1F4_STAEP Unreviewed; 160 AA. AC H3V1F4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU117_1745; OS Staphylococcus epidermidis VCU117. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904335; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU117; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLA01000060; EHR83277.1; -; Genomic_DNA. DR ProteinModelPortal; H3V1F4; -. DR EnsemblBacteria; EHR83277; EHR83277; SEVCU117_1745. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID H3V3I6_STAEP Unreviewed; 213 AA. AC H3V3I6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU117_0813; OS Staphylococcus epidermidis VCU117. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904335; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU117; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLA01000084; EHR80853.1; -; Genomic_DNA. DR ProteinModelPortal; H3V3I6; -. DR EnsemblBacteria; EHR80853; EHR80853; SEVCU117_0813. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3V4U9_STAEP Unreviewed; 166 AA. AC H3V4U9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU118_0889; OS Staphylococcus epidermidis VCU118. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904336; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU118; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLB01000006; EHR87088.1; -; Genomic_DNA. DR EnsemblBacteria; EHR87088; EHR87088; SEVCU118_0889. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 166 AA; 18953 MW; 7F6F0AF1D7186AC2 CRC64; MLFRTSMNNE ENKDMIQSLL QLGFSKDKII IHSDTTLLEE LNLKRIHFKS NDTTAFAYKA AHPDIYVSMS THDVETVKRC YENNLDYVFL GHIFPTASHP DTPPRSKKTI QQALDVPIPI YAIGGINEHS IQKMPPGFKG ICAISYFNNA SLEEIKQLRK EWSTHA // ID H3V7F1_STAEP Unreviewed; 213 AA. AC H3V7F1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU118_1568; OS Staphylococcus epidermidis VCU118. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904336; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU118; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLB01000045; EHR83645.1; -; Genomic_DNA. DR ProteinModelPortal; H3V7F1; -. DR EnsemblBacteria; EHR83645; EHR83645; SEVCU118_1568. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23704 MW; 0E35EA2716A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDVPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3VGL8_STAEP Unreviewed; 213 AA. AC H3VGL8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU120_1765; OS Staphylococcus epidermidis VCU120. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904337; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU120; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLC01000046; EHR81399.1; -; Genomic_DNA. DR ProteinModelPortal; H3VGL8; -. DR EnsemblBacteria; EHR81399; EHR81399; SEVCU120_1765. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3VH15_STAEP Unreviewed; 160 AA. AC H3VH15; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU120_1390; OS Staphylococcus epidermidis VCU120. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904337; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU120; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLC01000051; EHR80958.1; -; Genomic_DNA. DR ProteinModelPortal; H3VH15; -. DR EnsemblBacteria; EHR80958; EHR80958; SEVCU120_1390. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID H3VJH3_STAHO Unreviewed; 212 AA. AC H3VJH3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU122_1838; OS Staphylococcus hominis VCU122. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904339; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU122; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLD01000027; EHR89730.1; -; Genomic_DNA. DR ProteinModelPortal; H3VJH3; -. DR EnsemblBacteria; EHR89730; EHR89730; SEVCU122_1838. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23190 MW; 7FB8A445669AF2A9 CRC64; MFDSKSLQVY FICGTQDIIG DQNIKDVLKA ALESGITLFQ FREKGPNALV GDEKEALAKE LKTLCHEYKV PFLINDDVDL AEKIDADGIH VGQDDEIIAS FANRFKNKII GLSVGNVKEY QQSDLEHVDY IGVGPMYETS SKSDASAPVG PEMIATLKNI NPSLPMVAIG GITEDNCELI AKEGADGVSV ISVITHSQNI DKTVNKLKHY FK // ID H3VPI5_STAHO Unreviewed; 196 AA. AC H3VPI5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU122_1088; OS Staphylococcus hominis VCU122. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904339; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU122; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLD01000070; EHR86202.1; -; Genomic_DNA. DR EnsemblBacteria; EHR86202; EHR86202; SEVCU122_1088. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 22420 MW; 677E7CD060ED16FA CRC64; MFIFIAITKY KDLTNDDVQH FLDISDGIDG LLFRTPMSSS DLSSFLTSLI EKGFPKSKII IHSDVHLLEQ LHLSHIHFRE MDEDAFSYKS THPEIEVSMS THSIESVKAA YEHDLDYVFF GHIFKTPSKP NQLPRSKAEI QRVLEIPIPI YAIGGITEKT ILQLPHGFKG ICAISFFMNA SLQQIELLRK EWLKDA // ID H3VTV9_STAEP Unreviewed; 213 AA. AC H3VTV9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU123_2394; OS Staphylococcus epidermidis VCU123. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904340; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU123; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLE01000046; EHR90817.1; -; Genomic_DNA. DR ProteinModelPortal; H3VTV9; -. DR EnsemblBacteria; EHR90817; EHR90817; SEVCU123_2394. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3VVC5_STAEP Unreviewed; 160 AA. AC H3VVC5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU123_1653; OS Staphylococcus epidermidis VCU123. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904340; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU123; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLE01000065; EHR89464.1; -; Genomic_DNA. DR ProteinModelPortal; H3VVC5; -. DR EnsemblBacteria; EHR89464; EHR89464; SEVCU123_1653. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID H3W051_STAEP Unreviewed; 213 AA. AC H3W051; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU125_1783; OS Staphylococcus epidermidis VCU125. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904341; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU125; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLF01000044; EHR91026.1; -; Genomic_DNA. DR ProteinModelPortal; H3W051; -. DR EnsemblBacteria; EHR91026; EHR91026; SEVCU125_1783. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3W2Q1_STAEP Unreviewed; 199 AA. AC H3W2Q1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU125_0578; OS Staphylococcus epidermidis VCU125. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904341; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU125; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLF01000070; EHR88699.1; -; Genomic_DNA. DR EnsemblBacteria; EHR88699; EHR88699; SEVCU125_0578. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 22868 MW; 28DCE9FC38622427 CRC64; MGGIFIFIAI TYHKQLTRDD LQHYKHIEEA IDGLLFRTSM NNEENKDMIQ SLLQLGFSKD KIIIHSDVTL LEDLHLKRIH FKENDTTAFT YKEAHPDICV SMSTHDVETV KRCYENNLDY VFLGHIFPTA SHPDTPPRSK KTIQQALDVP IPIYAIGGIN EHSIQKMPPG FKGICAISYF NNASLEEIKQ LRKEWSTHA // ID H3W886_STAEP Unreviewed; 160 AA. AC H3W886; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU126_0908; OS Staphylococcus epidermidis VCU126. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904342; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU126; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLG01000071; EHR93057.1; -; Genomic_DNA. DR ProteinModelPortal; H3W886; -. DR EnsemblBacteria; EHR93057; EHR93057; SEVCU126_0908. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID H3W8M1_STAEP Unreviewed; 213 AA. AC H3W8M1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU126_0866; OS Staphylococcus epidermidis VCU126. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904342; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU126; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLG01000074; EHR92896.1; -; Genomic_DNA. DR ProteinModelPortal; H3W8M1; -. DR EnsemblBacteria; EHR92896; EHR92896; SEVCU126_0866. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3WEX7_STAEP Unreviewed; 213 AA. AC H3WEX7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU127_0988; OS Staphylococcus epidermidis VCU127. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904343; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU127; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLH01000072; EHR96170.1; -; Genomic_DNA. DR ProteinModelPortal; H3WEX7; -. DR EnsemblBacteria; EHR96170; EHR96170; SEVCU127_0988. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3WFH3_STAEP Unreviewed; 199 AA. AC H3WFH3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU127_0547; OS Staphylococcus epidermidis VCU127. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904343; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU127; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLH01000077; EHR95542.1; -; Genomic_DNA. DR EnsemblBacteria; EHR95542; EHR95542; SEVCU127_0547. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 22735 MW; BA8D10C9E4F009B0 CRC64; MGGIFIFIAI TYHKQLTRDD LQHYKHIEEA IDGLLFRTSM NKEETKDIIQ SLLQLGFSKD KIIIHSDVTL LEDLHLKRIH FKENDTTAFT YKEAHPDICV SMSTHDVETV KRCYENGLDS VFFGHIFPTS SHPNVPPRSK EAIQQALNVP IPIYAIGGIN EHSLQKMPPG FKGICAISYF NNASLEEIKQ LRKEWSTHA // ID H3WLH6_STAEP Unreviewed; 160 AA. AC H3WLH6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU128_1390; OS Staphylococcus epidermidis VCU128. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904344; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU128; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLI01000051; EHR96233.1; -; Genomic_DNA. DR EnsemblBacteria; EHR96233; EHR96233; SEVCU128_1390. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18217 MW; D44AFE40478FBC36 CRC64; MNNEENKDMI QSLLQLGFSK DKIIIHSDTT LLEELNLKRI HFKSNDTTAF AYKAAHPDIY VSMSTHDVET VKRCYENNLD YVFLGHIFPT ASHPDTPPRS KKTIQQALDV PIPIYAIGGI NEHSIQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID H3WLU5_STAEP Unreviewed; 213 AA. AC H3WLU5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU128_2431; OS Staphylococcus epidermidis VCU128. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904344; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU128; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLI01000052; EHR96092.1; -; Genomic_DNA. DR ProteinModelPortal; H3WLU5; -. DR EnsemblBacteria; EHR96092; EHR96092; SEVCU128_2431. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23704 MW; 0E35EA2716A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDVPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3WP44_STAEP Unreviewed; 160 AA. AC H3WP44; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU129_0062; OS Staphylococcus epidermidis VCU129. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904345; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU129; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLJ01000008; EHS03153.1; -; Genomic_DNA. DR EnsemblBacteria; EHS03153; EHS03153; SEVCU129_0062. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18187 MW; D45AFF4C3693CC36 CRC64; MNNEENKDMI QSLLQLGFSK DKIIIHSDAT LLEELNLKRI HFKSNDTTAF AYKAAHPDIY VSMSTHDVET VKRCYENNLD YVFLGHIFPT ASHPDTPPRS KKTIQQALDV PIPIYAIGGI NEHSIQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID H3WQ51_STAEP Unreviewed; 213 AA. AC H3WQ51; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU129_1977; OS Staphylococcus epidermidis VCU129. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904345; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU129; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLJ01000016; EHS02477.1; -; Genomic_DNA. DR ProteinModelPortal; H3WQ51; -. DR EnsemblBacteria; EHS02477; EHS02477; SEVCU129_1977. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23704 MW; 0E35EA2716A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDVPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3WVQ7_STALU Unreviewed; 212 AA. AC H3WVQ7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU139_2417; OS Staphylococcus lugdunensis VCU139. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904346; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU139; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLK01000013; EHS05168.1; -; Genomic_DNA. DR EnsemblBacteria; EHS05168; EHS05168; SEVCU139_2417. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23263 MW; 28D0FABBD5366612 CRC64; MFKSTDLKVY FICGTQDIHE GKSLEQVVTQ ALESGVTMFQ FREKGSKVSQ DKEIEQLALK LKELCHNYQV PFIVNDNVAL ALKVQADGIH VGQDDAKVED FFEQFHDKII GLSVSNLDEL KHSDLTHVDY IGVGPIYQTP SKSDASTPVG PEMILTLRKE IGNFPIVAIG GVTENNAQAV VDAGADGISV ISAIARSQNI DSTVNKFLSY YN // ID H3WXU4_STALU Unreviewed; 196 AA. AC H3WXU4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU139_1657; OS Staphylococcus lugdunensis VCU139. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904346; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU139; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLK01000036; EHS04553.1; -; Genomic_DNA. DR EnsemblBacteria; EHS04553; EHS04553; SEVCU139_1657. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 196 AA; 22561 MW; 30B343BBA6F39656 CRC64; MFIFIAITEY KFLDNNDLQH FLTIEQDIDF LLFRTSMSQK ELQHFIQQLI YQGFPKSKMM IHSDVKLLNT LGLQNIHFRE NDAQAFQLKS KYPDIHVSMS THHLSSVIRA YEAGLDAVFF GHIFPTPSKP NLPPRSQVEI DSVLEVPIPV YAIGGITTDT IRKLSPKFAG ICAISFFMKS SASVIHQFRK EWHHHA // ID H3X4B0_STAAU Unreviewed; 213 AA. AC H3X4B0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS3_2251; OS Staphylococcus aureus subsp. aureus IS-3. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904775; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-3; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLL01000033; EHS14230.1; -; Genomic_DNA. DR ProteinModelPortal; H3X4B0; -. DR SMR; H3X4B0; 4-209. DR PRIDE; H3X4B0; -. DR EnsemblBacteria; EHS14230; EHS14230; IS3_2251. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3XB11_STAAU Unreviewed; 213 AA. AC H3XB11; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS24_2324; OS Staphylococcus aureus subsp. aureus IS-24. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904776; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-24; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLM01000010; EHS13437.1; -; Genomic_DNA. DR ProteinModelPortal; H3XB11; -. DR SMR; H3XB11; 4-209. DR PRIDE; H3XB11; -. DR EnsemblBacteria; EHS13437; EHS13437; IS24_2324. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3XN48_STAAU Unreviewed; 213 AA. AC H3XN48; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS55_2053; OS Staphylococcus aureus subsp. aureus IS-55. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904777; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-55; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLN01000045; EHS16510.1; -; Genomic_DNA. DR ProteinModelPortal; H3XN48; -. DR SMR; H3XN48; 4-209. DR PRIDE; H3XN48; -. DR EnsemblBacteria; EHS16510; EHS16510; IS55_2053. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3XR53_STAAU Unreviewed; 213 AA. AC H3XR53; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS88_1555; OS Staphylococcus aureus subsp. aureus IS-88. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904778; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-88; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLO01000010; EHS25937.1; -; Genomic_DNA. DR ProteinModelPortal; H3XR53; -. DR SMR; H3XR53; 4-209. DR PRIDE; H3XR53; -. DR EnsemblBacteria; EHS25937; EHS25937; IS88_1555. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3XYF2_STAAU Unreviewed; 213 AA. AC H3XYF2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS91_2497; OS Staphylococcus aureus subsp. aureus IS-91. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904779; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-91; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLP01000002; EHS23702.1; -; Genomic_DNA. DR ProteinModelPortal; H3XYF2; -. DR SMR; H3XYF2; 4-209. DR PRIDE; H3XYF2; -. DR EnsemblBacteria; EHS23702; EHS23702; IS91_2497. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3Y6C4_STAAU Unreviewed; 213 AA. AC H3Y6C4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS99_0960; OS Staphylococcus aureus subsp. aureus IS-99. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904780; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-99; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLQ01000001; EHS16565.1; -; Genomic_DNA. DR ProteinModelPortal; H3Y6C4; -. DR SMR; H3Y6C4; 4-209. DR PRIDE; H3Y6C4; -. DR EnsemblBacteria; EHS16565; EHS16565; IS99_0960. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3YH50_STAAU Unreviewed; 213 AA. AC H3YH50; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS105_1001; OS Staphylococcus aureus subsp. aureus IS-105. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904781; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-105; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLR01000057; EHS28400.1; -; Genomic_DNA. DR ProteinModelPortal; H3YH50; -. DR SMR; H3YH50; 4-209. DR PRIDE; H3YH50; -. DR EnsemblBacteria; EHS28400; EHS28400; IS105_1001. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3YPP6_STAAU Unreviewed; 213 AA. AC H3YPP6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS111_0798; OS Staphylococcus aureus subsp. aureus IS-111. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904782; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-111; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLS01000048; EHS30834.1; -; Genomic_DNA. DR ProteinModelPortal; H3YPP6; -. DR SMR; H3YPP6; 4-209. DR PRIDE; H3YPP6; -. DR EnsemblBacteria; EHS30834; EHS30834; IS111_0798. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3Z2C9_STAAU Unreviewed; 213 AA. AC H3Z2C9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS122_0851; OS Staphylococcus aureus subsp. aureus IS-122. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904783; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-122; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLT01000090; EHS27667.1; -; Genomic_DNA. DR ProteinModelPortal; H3Z2C9; -. DR SMR; H3Z2C9; 4-209. DR PRIDE; H3Z2C9; -. DR EnsemblBacteria; EHS27667; EHS27667; IS122_0851. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H3Z3H8_STAEP Unreviewed; 213 AA. AC H3Z3H8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEVCU081_0675; OS Staphylococcus epidermidis VCU081. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904326; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU081; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLU01000006; EHQ81963.1; -; Genomic_DNA. DR ProteinModelPortal; H3Z3H8; -. DR EnsemblBacteria; EHQ81963; EHQ81963; SEVCU081_0675. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID H3Z8X3_STAEP Unreviewed; 160 AA. AC H3Z8X3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=SEVCU081_0413; OS Staphylococcus epidermidis VCU081. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904326; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU081; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHLU01000074; EHQ79053.1; -; Genomic_DNA. DR EnsemblBacteria; EHQ79053; EHQ79053; SEVCU081_0413. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18169 MW; 1CFC64416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTNA // ID H3ZAF4_9ALTE Unreviewed; 553 AA. AC H3ZAF4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=AJE_01464; OS Alishewanella jeotgali KCTC 22429. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alishewanella. OX NCBI_TaxID=1129374; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KCTC 22429; RX PubMed=22461542; DOI=10.1128/JB.00153-12; RA Jung J., Chun J., Park W.; RT "Genome Sequence of Extracellular-Protease-Producing Alishewanella RT jeotgali Isolated from Traditional Korean Fermented Seafood."; RL J. Bacteriol. 194:2097-2097(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHTH01000004; EHR42508.1; -; Genomic_DNA. DR EnsemblBacteria; EHR42508; EHR42508; AJE_01464. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 553 AA; 57947 MW; 41F376F162DC545A CRC64; MPPHFELMPQ AAKVSSNKTE ATKAIVWSIA GSDSGGGAGI QADLLTMRAF GVHGCSLITA ITAQSSVEVA RVELVSEQML AAQWQTLLAD LPPVAIKIGL VASRAQQQQL ATLLATLPTT IPVIIDPVLI ASCGDTLTLD PGSDALPELP ALYRFASLLT PNLPELAALT GLAVTTPEQI ITATECLLTQ GVRAVLVKGG HASGCKQLAL DYLASTRQQY WLASPRIDTE HNHGTGCSLA SAITSGLALG YPLDDAVVLA KAYLNRGLSA AYATGQGPGT LSHLPLPVAV EHFPLWLNTA QVQALYQGAS LADLTPPSAA FAPLAQAEMG LYPVVDSVAW LTRLLPLGVN TIQLRIKTAD QQQLSAEIAA AIALAKQYQA QLFINDHWQL ALQLGAYGVH LGQEDLATAD LHALQQAGIR LGVSSHGYAE LLRAKALQPS YIALGHIFPT KTKQMPSQPQ GVARLAQYVA LAAPYPTVAI GGINAERIAA VAATGVNSIA VVTAITEAAD PEQATQLLMA LLAKAKQEAH VRQLAQAKEF AQAINEVNAV CLN // ID H3ZJJ7_THELN Unreviewed; 207 AA. AC H3ZJJ7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=OCC_04974; OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / OS NS-C). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=523849; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C; RX PubMed=22493191; DOI=10.1128/JB.00123-12; RA Gardner A.F., Kumar S., Perler F.B.; RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus RT litoralis NS-C."; RL J. Bacteriol. 194:2375-2376(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006670; EHR79860.1; -; Genomic_DNA. DR RefSeq; YP_008428443.1; NC_022084.1. DR EnsemblBacteria; EHR79860; EHR79860; OCC_04974. DR GeneID; 16548773; -. DR KEGG; tlt:OCC_04974; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22595 MW; C221CE7ADCEC564E CRC64; MNLRKKLKLY VITDRRLRPE VESVKEALEG GATSIQLRIK NAPTREMIEI GKEIRKLTEE YDALYFVDDR LDVALATNAD GVQLGSEDMP ISIAKEIAPN LIIGASVYSL EEALQAEKEG ADYLGAGSVF PTPTKKDVKI IGIEGLSRIV ESVKIPVVAI GGIKHENVRE VLKAGVDGIA VISAIMGAEN VREATERMRK IIEEVIG // ID H3ZSX4_STAAU Unreviewed; 213 AA. AC H3ZSX4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS125_1166; OS Staphylococcus aureus subsp. aureus IS-125. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904784; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-125; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVC01000025; EHS72912.1; -; Genomic_DNA. DR ProteinModelPortal; H3ZSX4; -. DR SMR; H3ZSX4; 4-209. DR PRIDE; H3ZSX4; -. DR EnsemblBacteria; EHS72912; EHS72912; IS125_1166. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4A6C9_STAAU Unreviewed; 213 AA. AC H4A6C9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIGC93_2123; OS Staphylococcus aureus subsp. aureus CIGC93. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931460; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIGC93; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVD01000025; EHT92164.1; -; Genomic_DNA. DR ProteinModelPortal; H4A6C9; -. DR SMR; H4A6C9; 4-209. DR PRIDE; H4A6C9; -. DR EnsemblBacteria; EHT92164; EHT92164; SACIGC93_2123. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4AEV5_STAAU Unreviewed; 213 AA. AC H4AEV5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1165_2625; OS Staphylococcus aureus subsp. aureus CIG1165. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931434; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1165; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVE01000012; EHT17241.1; -; Genomic_DNA. DR ProteinModelPortal; H4AEV5; -. DR SMR; H4AEV5; 4-209. DR PRIDE; H4AEV5; -. DR EnsemblBacteria; EHT17241; EHT17241; SACIG1165_2625. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4AMX4_STAAU Unreviewed; 213 AA. AC H4AMX4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1213_2663; OS Staphylococcus aureus subsp. aureus CIG1213. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931446; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1213; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVF01000014; EHT53866.1; -; Genomic_DNA. DR EnsemblBacteria; EHT53866; EHT53866; SACIG1213_2663. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23359 MW; 80EE2B9D7779BD79 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQPLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4AVF3_STAAU Unreviewed; 213 AA. AC H4AVF3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1769_2442; OS Staphylococcus aureus subsp. aureus CIG1769. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931440; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1769; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVG01000019; EHT37459.1; -; Genomic_DNA. DR ProteinModelPortal; H4AVF3; -. DR SMR; H4AVF3; 4-209. DR PRIDE; H4AVF3; -. DR EnsemblBacteria; EHT37459; EHT37459; SACIG1769_2442. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4B2Y9_STAAU Unreviewed; 213 AA. AC H4B2Y9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1150_2363; OS Staphylococcus aureus subsp. aureus CIG1150. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931444; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1150; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVH01000038; EHT47971.1; -; Genomic_DNA. DR ProteinModelPortal; H4B2Y9; -. DR SMR; H4B2Y9; 4-209. DR PRIDE; H4B2Y9; -. DR EnsemblBacteria; EHT47971; EHT47971; SACIG1150_2363. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4BAT0_STAAU Unreviewed; 213 AA. AC H4BAT0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1524_2552; OS Staphylococcus aureus subsp. aureus CIG1524. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931454; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1524; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVI01000012; EHT75148.1; -; Genomic_DNA. DR ProteinModelPortal; H4BAT0; -. DR EnsemblBacteria; EHT75148; EHT75148; SACIG1524_2552. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23374 MW; 87C8D3399EE9DFCF CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDEVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4BIJ1_STAAU Unreviewed; 213 AA. AC H4BIJ1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1176_2692; OS Staphylococcus aureus subsp. aureus CIG1176. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931445; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1176; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVJ01000016; EHT53831.1; -; Genomic_DNA. DR ProteinModelPortal; H4BIJ1; -. DR EnsemblBacteria; EHT53831; EHT53831; SACIG1176_2692. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4BS88_STAAU Unreviewed; 213 AA. AC H4BS88; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1057_2817; OS Staphylococcus aureus subsp. aureus CIG1057. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931432; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1057; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVK01000015; EHT17362.1; -; Genomic_DNA. DR ProteinModelPortal; H4BS88; -. DR SMR; H4BS88; 4-209. DR PRIDE; H4BS88; -. DR EnsemblBacteria; EHT17362; EHT17362; SACIG1057_2817. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4C0S0_STAAU Unreviewed; 213 AA. AC H4C0S0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIGC341D_2915; OS Staphylococcus aureus subsp. aureus CIGC341D. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931456; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIGC341D; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVL01000023; EHT82123.1; -; Genomic_DNA. DR ProteinModelPortal; H4C0S0; -. DR EnsemblBacteria; EHT82123; EHT82123; SACIGC341D_2915. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4C8Q5_STAAU Unreviewed; 213 AA. AC H4C8Q5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1214_2766; OS Staphylococcus aureus subsp. aureus CIG1214. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931435; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1214; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVM01000014; EHT25049.1; -; Genomic_DNA. DR ProteinModelPortal; H4C8Q5; -. DR EnsemblBacteria; EHT25049; EHT25049; SACIG1214_2766. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4CH43_STAAU Unreviewed; 213 AA. AC H4CH43; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1770_2767; OS Staphylococcus aureus subsp. aureus CIG1770. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931449; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1770; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVN01000011; EHT63867.1; -; Genomic_DNA. DR ProteinModelPortal; H4CH43; -. DR SMR; H4CH43; 4-209. DR PRIDE; H4CH43; -. DR EnsemblBacteria; EHT63867; EHT63867; SACIG1770_2767. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4CPG9_STAAU Unreviewed; 213 AA. AC H4CPG9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIGC345D_2541; OS Staphylococcus aureus subsp. aureus CIGC345D. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931457; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIGC345D; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVO01000012; EHT85350.1; -; Genomic_DNA. DR ProteinModelPortal; H4CPG9; -. DR SMR; H4CPG9; 4-209. DR PRIDE; H4CPG9; -. DR EnsemblBacteria; EHT85350; EHT85350; SACIGC345D_2541. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4CXN2_STAAU Unreviewed; 213 AA. AC H4CXN2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG149_2826; OS Staphylococcus aureus subsp. aureus CIG149. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931453; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG149; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVP01000029; EHT73819.1; -; Genomic_DNA. DR ProteinModelPortal; H4CXN2; -. DR EnsemblBacteria; EHT73819; EHT73819; SACIG149_2826. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4D5E3_STAAU Unreviewed; 213 AA. AC H4D5E3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG547_2699; OS Staphylococcus aureus subsp. aureus CIG547. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931442; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG547; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVQ01000012; EHT45289.1; -; Genomic_DNA. DR ProteinModelPortal; H4D5E3; -. DR SMR; H4D5E3; 4-209. DR PRIDE; H4D5E3; -. DR EnsemblBacteria; EHT45289; EHT45289; SACIG547_2699. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4DCR5_STAAU Unreviewed; 213 AA. AC H4DCR5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIGC340D_2533; OS Staphylococcus aureus subsp. aureus CIGC340D. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931455; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIGC340D; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVR01000009; EHT78573.1; -; Genomic_DNA. DR ProteinModelPortal; H4DCR5; -. DR SMR; H4DCR5; 4-209. DR PRIDE; H4DCR5; -. DR EnsemblBacteria; EHT78573; EHT78573; SACIGC340D_2533. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4DL16_STAAU Unreviewed; 213 AA. AC H4DL16; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1267_2915; OS Staphylococcus aureus subsp. aureus CIG1267. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931452; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1267; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVS01000012; EHT72363.1; -; Genomic_DNA. DR ProteinModelPortal; H4DL16; -. DR EnsemblBacteria; EHT72363; EHT72363; SACIG1267_2915. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4DTX3_STAAU Unreviewed; 213 AA. AC H4DTX3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIGC348_2736; OS Staphylococcus aureus subsp. aureus CIGC348. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931458; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIGC348; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVT01000022; EHT86328.1; -; Genomic_DNA. DR ProteinModelPortal; H4DTX3; -. DR SMR; H4DTX3; 4-209. DR PRIDE; H4DTX3; -. DR EnsemblBacteria; EHT86328; EHT86328; SACIGC348_2736. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4E242_STAAU Unreviewed; 213 AA. AC H4E242; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1233_2832; OS Staphylococcus aureus subsp. aureus CIG1233. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931447; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1233; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVU01000013; EHT57033.1; -; Genomic_DNA. DR ProteinModelPortal; H4E242; -. DR EnsemblBacteria; EHT57033; EHT57033; SACIG1233_2832. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4E9S5_STAAU Unreviewed; 213 AA. AC H4E9S5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG2018_2653; OS Staphylococcus aureus subsp. aureus CIG2018. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931450; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG2018; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVV01000014; EHT65344.1; -; Genomic_DNA. DR ProteinModelPortal; H4E9S5; -. DR SMR; H4E9S5; 4-209. DR PRIDE; H4E9S5; -. DR EnsemblBacteria; EHT65344; EHT65344; SACIG2018_2653. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4EI44_STAAU Unreviewed; 213 AA. AC H4EI44; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1612_2746; OS Staphylococcus aureus subsp. aureus CIG1612. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931448; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1612; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVW01000007; EHT60642.1; -; Genomic_DNA. DR ProteinModelPortal; H4EI44; -. DR SMR; H4EI44; 4-209. DR PRIDE; H4EI44; -. DR EnsemblBacteria; EHT60642; EHT60642; SACIG1612_2746. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4ERG2_STAAU Unreviewed; 213 AA. AC H4ERG2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1750_2856; OS Staphylococcus aureus subsp. aureus CIG1750. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931439; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1750; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVX01000043; EHT35722.1; -; Genomic_DNA. DR ProteinModelPortal; H4ERG2; -. DR SMR; H4ERG2; 4-209. DR PRIDE; H4ERG2; -. DR EnsemblBacteria; EHT35722; EHT35722; SACIG1750_2856. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4EZ14_STAAU Unreviewed; 213 AA. AC H4EZ14; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIGC128_2638; OS Staphylococcus aureus subsp. aureus CIGC128. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIGC128; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHVY01000010; EHT93079.1; -; Genomic_DNA. DR ProteinModelPortal; H4EZ14; -. DR EnsemblBacteria; EHT93079; EHT93079; SACIGC128_2638. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23384 MW; 8FEFB3993FF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI ENTVNRFKDF FNN // ID H4F7Q2_9RHIZ Unreviewed; 207 AA. AC H4F7Q2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=PDO_2022; OS Rhizobium sp. PDO1-076. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1125979; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PDO-076; RX PubMed=22493196; DOI=10.1128/JB.00198-12; RA Brown S.D., Klingeman D.M., Lu T.Y., Johnson C.M., Utturkar S.M., RA Land M.L., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Draft Genome Sequence of Rhizobium sp. Strain PDO1-076, a Bacterium RT Isolated from Populus deltoides."; RL J. Bacteriol. 194:2383-2384(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHZC01000255; EHS51203.1; -; Genomic_DNA. DR EnsemblBacteria; EHS51203; EHS51203; PDO_2022. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 207 AA; 23018 MW; 6169CEDEB08D24AB CRC64; MKLDPFYLIV DSADWIERLV PCGVKLVQLR MKNIDPPTLI DHVRRARQIC VRHGCQLIIN DYWQTAIDEG CDFIHLGQED LAGADINAIR KANLKIGIST HDEVELETAL ALAPDYVALG PIYPTILKKM KWSAQGPEKL ARWKSRIGTM PLVAIGGLRV DRLAGVFANG ADIAAVVTDI TQNQDPKAQT KRWIEQTSAI RQNSGPE // ID H4FC50_9RHIZ Unreviewed; 218 AA. AC H4FC50; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=PDO_0523; OS Rhizobium sp. PDO1-076. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1125979; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PDO-076; RX PubMed=22493196; DOI=10.1128/JB.00198-12; RA Brown S.D., Klingeman D.M., Lu T.Y., Johnson C.M., Utturkar S.M., RA Land M.L., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Draft Genome Sequence of Rhizobium sp. Strain PDO1-076, a Bacterium RT Isolated from Populus deltoides."; RL J. Bacteriol. 194:2383-2384(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHZC01000408; EHS49550.1; -; Genomic_DNA. DR EnsemblBacteria; EHS49550; EHS49550; PDO_0523. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 218 AA; 22936 MW; 802E72D43E5F8447 CRC64; MTKKKQDRCR LVLIVPDMAD AAEQARVLGD ALRGGDVASV IIPQYGLDDA TFQKHAELLV PVIQEAGAAA LIVDNSRVAG RVKADGLHIS GNSAALAEAV GNHTPKMIVG GGNAMDRHHA LEMGEAQPDY IFFGRLDGDI KPEAHSKNIA LGEWWSAMIA IPCIVMGGID PSSAVVVAES GSEFVALGKA VFDDPATAAT IVSQVNAELD EKAPRFED // ID H4FW64_STAAU Unreviewed; 213 AA. AC H4FW64; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS157_0378; OS Staphylococcus aureus subsp. aureus IS-157. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904785; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-157; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICH01000086; EHS77765.1; -; Genomic_DNA. DR ProteinModelPortal; H4FW64; -. DR SMR; H4FW64; 4-209. DR PRIDE; H4FW64; -. DR EnsemblBacteria; EHS77765; EHS77765; IS157_0378. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4G5C3_STAAU Unreviewed; 213 AA. AC H4G5C3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS160_2403; OS Staphylococcus aureus subsp. aureus IS-160. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904786; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-160; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICI01000131; EHS77094.1; -; Genomic_DNA. DR EnsemblBacteria; EHS77094; EHS77094; IS160_2403. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23374 MW; 8304F05AA899AE8D CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GKDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4GHH9_STAAU Unreviewed; 213 AA. AC H4GHH9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS189_1962; OS Staphylococcus aureus subsp. aureus IS-189. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904787; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-189; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICJ01000081; EHS74316.1; -; Genomic_DNA. DR ProteinModelPortal; H4GHH9; -. DR SMR; H4GHH9; 4-209. DR PRIDE; H4GHH9; -. DR EnsemblBacteria; EHS74316; EHS74316; IS189_1962. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4GIX5_9LACO Unreviewed; 217 AA. AC H4GIX5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PS3_6732; OS Lactobacillus gastricus PS3. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1144300; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PS3; RX PubMed=23846278; RA Martin V., Cardenas N., Jimenez E., Maldonado A., Rodriguez J.M., RA Fernandez L.; RT "Genome Sequence of Lactobacillus gastricus PS3, a Strain Isolated RT from Human Milk."; RL Genome Announc. 1:E00489-13(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICN01000024; EHS87147.1; -; Genomic_DNA. DR EnsemblBacteria; EHS87147; EHS87147; PS3_6732. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23229 MW; CFFD0EDEAB4ADEFE CRC64; MQFKPEMLHC YLIGGSQDVD HDPTKFLLKL TTACQAGITA FQFREKSDLV EYDVYALGFQ VRTICSQFQV PLFVDDNLEL AQKINADGIH VGQKDQPIEE VIQAAGDDLM IGYSCNTVAQ VEHANQVQVD YIGSGPIYPT KSKADADPAL GVKELGHLVQ ISQHPVVAIG GITPAKVPEV LTSGCAGISA IAGIFDNLAA GMPAGPDNPV SQILNCY // ID H4GSJ0_STAAU Unreviewed; 213 AA. AC H4GSJ0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1242_2139; OS Staphylococcus aureus subsp. aureus CIG1242. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931436; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1242; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIEO01000052; EHT26985.1; -; Genomic_DNA. DR ProteinModelPortal; H4GSJ0; -. DR EnsemblBacteria; EHT26985; EHT26985; SACIG1242_2139. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4H2T7_STAAU Unreviewed; 213 AA. AC H4H2T7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1500_2769; OS Staphylococcus aureus subsp. aureus CIG1500. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931437; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1500; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIEP01000018; EHT27092.1; -; Genomic_DNA. DR ProteinModelPortal; H4H2T7; -. DR EnsemblBacteria; EHT27092; EHT27092; SACIG1500_2769. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4H9X4_STAAU Unreviewed; 213 AA. AC H4H9X4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1835_2460; OS Staphylococcus aureus subsp. aureus CIG1835. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931441; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1835; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIEQ01000010; EHT39873.1; -; Genomic_DNA. DR ProteinModelPortal; H4H9X4; -. DR EnsemblBacteria; EHT39873; EHT39873; SACIG1835_2460. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23384 MW; 8FEFB3993FF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI ENTVNRFKDF FNN // ID H4HI14_STAAU Unreviewed; 213 AA. AC H4HI14; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG1096_2717; OS Staphylococcus aureus subsp. aureus CIG1096. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931443; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG1096; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIER01000007; EHT45548.1; -; Genomic_DNA. DR ProteinModelPortal; H4HI14; -. DR SMR; H4HI14; 4-209. DR PRIDE; H4HI14; -. DR EnsemblBacteria; EHT45548; EHT45548; SACIG1096_2717. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H4HQX2_STAAU Unreviewed; 213 AA. AC H4HQX2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SACIG290_2717; OS Staphylococcus aureus subsp. aureus CIG290. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=931451; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIG290; RA Gill S., Fowler V., Tallon L., Sadzewicz L., Hine E., Daugherty S.C., RA Chibucos M.C., Mongodin E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIES01000019; EHT65710.1; -; Genomic_DNA. DR EnsemblBacteria; EHT65710; EHT65710; SACIG290_2717. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23325 MW; 8756AC9C9EE9DE8A CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF LNN // ID H4I472_ECOLX Unreviewed; 194 AA. AC H4I472; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC1A_4574; OS Escherichia coli DEC1A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868133; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIEV01000060; EHU03586.1; -; Genomic_DNA. DR EnsemblBacteria; EHU03586; EHU03586; ECDEC1A_4574. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 117 119 THZ-P binding (By similarity). FT REGION 169 170 THZ-P binding (By similarity). FT METAL 53 53 Magnesium (By similarity). FT METAL 72 72 Magnesium (By similarity). FT BINDING 52 52 HMP-PP (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 194 AA; 20999 MW; EFFD4AD132E7FA47 CRC64; MVDSVQWIER LLDAGVRTLQ LRIKDQRDEE VEADVVAAIA LGRRYNARLF INDYWRLAIK HQAYGVHLGQ EDLQATDLSA IRAAGLRLGV STHDDMEIDV ALAARPSYIA LGHVFPTQTK QMPSAPQGLE QLARHVERLA DYPTVAIGGI SLARAPAVIA TGVGSIAVVS AITQAADWRL ATAQLLEIAG VGDE // ID H4IJ79_ECOLX Unreviewed; 211 AA. AC H4IJ79; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC1B_4789; OS Escherichia coli DEC1B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868134; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIEW01000064; EHU06003.1; -; Genomic_DNA. DR EnsemblBacteria; EHU06003; EHU06003; ECDEC1B_4789. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23000 MW; CC43679342B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4J063_ECOLX Unreviewed; 211 AA. AC H4J063; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC1C_4870; OS Escherichia coli DEC1C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868135; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIEX01000075; EHU03565.1; -; Genomic_DNA. DR EnsemblBacteria; EHU03565; EHU03565; ECDEC1C_4870. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23000 MW; CC43679342B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4JGA6_ECOLX Unreviewed; 211 AA. AC H4JGA6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC1D_5124; OS Escherichia coli DEC1D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868136; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIEY01000065; EHU17303.1; -; Genomic_DNA. DR EnsemblBacteria; EHU17303; EHU17303; ECDEC1D_5124. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; CC43645C43A8F6D7 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4JV81_ECOLX Unreviewed; 194 AA. AC H4JV81; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC1E_4922; OS Escherichia coli DEC1E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868137; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIEZ01000036; EHU20453.1; -; Genomic_DNA. DR EnsemblBacteria; EHU20453; EHU20453; ECDEC1E_4922. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 117 119 THZ-P binding (By similarity). FT REGION 169 170 THZ-P binding (By similarity). FT METAL 53 53 Magnesium (By similarity). FT METAL 72 72 Magnesium (By similarity). FT BINDING 52 52 HMP-PP (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 194 AA; 20999 MW; EFFD4AD132E7FA47 CRC64; MVDSVQWIER LLDAGVRTLQ LRIKDQRDEE VEADVVAAIA LGRRYNARLF INDYWRLAIK HQAYGVHLGQ EDLQATDLSA IRAAGLRLGV STHDDMEIDV ALAARPSYIA LGHVFPTQTK QMPSAPQGLE QLARHVERLA DYPTVAIGGI SLARAPAVIA TGVGSIAVVS AITQAADWRL ATAQLLEIAG VGDE // ID H4KAJ9_ECOLX Unreviewed; 211 AA. AC H4KAJ9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC2A_4785; OS Escherichia coli DEC2A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868138; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFA01000070; EHU21847.1; -; Genomic_DNA. DR EnsemblBacteria; EHU21847; EHU21847; ECDEC2A_4785. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23000 MW; CC43679342B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4KQ46_ECOLX Unreviewed; 211 AA. AC H4KQ46; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC2C_4844; OS Escherichia coli DEC2C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868140; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFB01000071; EHU36190.1; -; Genomic_DNA. DR EnsemblBacteria; EHU36190; EHU36190; ECDEC2C_4844. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23000 MW; CC43679342B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4L5V8_ECOLX Unreviewed; 211 AA. AC H4L5V8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC2D_4739; OS Escherichia coli DEC2D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868141; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFC01000043; EHU37731.1; -; Genomic_DNA. DR EnsemblBacteria; EHU37731; EHU37731; ECDEC2D_4739. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23000 MW; CC43679342B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4LKA4_ECOLX Unreviewed; 211 AA. AC H4LKA4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC2E_4821; OS Escherichia coli DEC2E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868142; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFD01000053; EHU49693.1; -; Genomic_DNA. DR EnsemblBacteria; EHU49693; EHU49693; ECDEC2E_4821. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23000 MW; CC43679342B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4LYY6_ECOLX Unreviewed; 211 AA. AC H4LYY6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC3A_4217; OS Escherichia coli DEC3A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868143; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC3A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC3A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFE01000053; EHU55171.1; -; Genomic_DNA. DR ProteinModelPortal; H4LYY6; -. DR SMR; H4LYY6; 10-209. DR EnsemblBacteria; EHU55171; EHU55171; ECDEC3A_4217. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4M365_ECOLX Unreviewed; 211 AA. AC H4M365; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC3B_0082; OS Escherichia coli DEC3B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868144; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC3B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC3B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFF01000004; EHU67143.1; -; Genomic_DNA. DR ProteinModelPortal; H4M365; -. DR SMR; H4M365; 10-209. DR EnsemblBacteria; EHU67143; EHU67143; ECDEC3B_0082. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4MZL1_ECOLX Unreviewed; 211 AA. AC H4MZL1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC3C_5565; OS Escherichia coli DEC3C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868145; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC3C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC3C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFG01000067; EHU65682.1; -; Genomic_DNA. DR ProteinModelPortal; H4MZL1; -. DR SMR; H4MZL1; 10-209. DR EnsemblBacteria; EHU65682; EHU65682; ECDEC3C_5565. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4NGE1_ECOLX Unreviewed; 211 AA. AC H4NGE1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC3D_5754; OS Escherichia coli DEC3D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868146; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC3D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC3D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFH01000096; EHU67172.1; -; Genomic_DNA. DR ProteinModelPortal; H4NGE1; -. DR SMR; H4NGE1; 10-209. DR EnsemblBacteria; EHU67172; EHU67172; ECDEC3D_5754. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4NWK8_ECOLX Unreviewed; 211 AA. AC H4NWK8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC3E_5447; OS Escherichia coli DEC3E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868147; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC3E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC3E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFI01000088; EHU70376.1; -; Genomic_DNA. DR ProteinModelPortal; H4NWK8; -. DR SMR; H4NWK8; 10-209. DR EnsemblBacteria; EHU70376; EHU70376; ECDEC3E_5447. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4PD65_ECOLX Unreviewed; 211 AA. AC H4PD65; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC3F_5381; OS Escherichia coli DEC3F. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868148; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC3F; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC3F; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFJ01000091; EHU80535.1; -; Genomic_DNA. DR ProteinModelPortal; H4PD65; -. DR SMR; H4PD65; 10-209. DR EnsemblBacteria; EHU80535; EHU80535; ECDEC3F_5381. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4PSL7_ECOLX Unreviewed; 211 AA. AC H4PSL7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC4A_5025; OS Escherichia coli DEC4A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868149; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC4A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC4A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFK01000050; EHU86695.1; -; Genomic_DNA. DR ProteinModelPortal; H4PSL7; -. DR SMR; H4PSL7; 10-209. DR EnsemblBacteria; EHU86695; EHU86695; ECDEC4A_5025. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4Q9E6_ECOLX Unreviewed; 211 AA. AC H4Q9E6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC4B_5288; OS Escherichia coli DEC4B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868150; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC4B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC4B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFL01000074; EHU89795.1; -; Genomic_DNA. DR ProteinModelPortal; H4Q9E6; -. DR SMR; H4Q9E6; 10-209. DR EnsemblBacteria; EHU89795; EHU89795; ECDEC4B_5288. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4QT10_ECOLX Unreviewed; 211 AA. AC H4QT10; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC4C_5878; OS Escherichia coli DEC4C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868151; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC4C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC4C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFM01000055; EHU99171.1; -; Genomic_DNA. DR ProteinModelPortal; H4QT10; -. DR SMR; H4QT10; 10-209. DR EnsemblBacteria; EHU99171; EHU99171; ECDEC4C_5878. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4QT84_ECOLX Unreviewed; 211 AA. AC H4QT84; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC4D_5668; OS Escherichia coli DEC4D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868152; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC4D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC4D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFN01000007; EHV15771.1; -; Genomic_DNA. DR ProteinModelPortal; H4QT84; -. DR SMR; H4QT84; 10-209. DR EnsemblBacteria; EHV15771; EHV15771; ECDEC4D_5668. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4RNA7_ECOLX Unreviewed; 211 AA. AC H4RNA7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC4E_4995; OS Escherichia coli DEC4E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868153; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC4E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC4E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFO01000062; EHV07068.1; -; Genomic_DNA. DR ProteinModelPortal; H4RNA7; -. DR SMR; H4RNA7; 10-209. DR EnsemblBacteria; EHV07068; EHV07068; ECDEC4E_4995. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4RPX0_ECOLX Unreviewed; 211 AA. AC H4RPX0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC4F_0016; OS Escherichia coli DEC4F. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868154; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC4F; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC4F; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFP01000001; EHV31181.1; -; Genomic_DNA. DR ProteinModelPortal; H4RPX0; -. DR SMR; H4RPX0; 10-209. DR EnsemblBacteria; EHV31181; EHV31181; ECDEC4F_0016. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4SJ72_ECOLX Unreviewed; 194 AA. AC H4SJ72; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC5A_4788; OS Escherichia coli DEC5A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868155; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC5A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC5A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFQ01000034; EHV20174.1; -; Genomic_DNA. DR EnsemblBacteria; EHV20174; EHV20174; ECDEC5A_4788. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 117 119 THZ-P binding (By similarity). FT REGION 169 170 THZ-P binding (By similarity). FT METAL 53 53 Magnesium (By similarity). FT METAL 72 72 Magnesium (By similarity). FT BINDING 52 52 HMP-PP (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 194 AA; 21070 MW; 03FE69A0FF85508F CRC64; MVDSVQWIER LLDAGVRTLQ LRIKDRRDEE VEADVVAAIA LGRRYNARLF INDYWRLAIK HQAYGVHLGQ EDLQATDLNA IRAAGLRLGV STHDDMEIDV ALAARPSYIA LGHVFPTQTK QMPSAPQGLE QLARHVERLS DYPTVAIGGI SLARAPAVIA TGVGSIAVVS AITQAADWRL ATAQLLEIAG VGDE // ID H4T1U1_ECOLX Unreviewed; 211 AA. AC H4T1U1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC5B_5693; OS Escherichia coli DEC5B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868156; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC5B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC5B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFR01000071; EHV21790.1; -; Genomic_DNA. DR ProteinModelPortal; H4T1U1; -. DR SMR; H4T1U1; 10-209. DR EnsemblBacteria; EHV21790; EHV21790; ECDEC5B_5693. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4TFX3_ECOLX Unreviewed; 211 AA. AC H4TFX3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC5C_4911; OS Escherichia coli DEC5C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868157; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC5C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC5C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFS01000051; EHV31901.1; -; Genomic_DNA. DR ProteinModelPortal; H4TFX3; -. DR SMR; H4TFX3; 10-209. DR EnsemblBacteria; EHV31901; EHV31901; ECDEC5C_4911. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4TW00_ECOLX Unreviewed; 211 AA. AC H4TW00; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC5D_4929; OS Escherichia coli DEC5D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868158; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC5D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC5D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFT01000040; EHV33528.1; -; Genomic_DNA. DR ProteinModelPortal; H4TW00; -. DR SMR; H4TW00; 10-209. DR EnsemblBacteria; EHV33528; EHV33528; ECDEC5D_4929. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4UAZ9_ECOLX Unreviewed; 211 AA. AC H4UAZ9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC5E_4994; OS Escherichia coli DEC5E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868159; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC5E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC5E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFU01000026; EHV42996.1; -; Genomic_DNA. DR ProteinModelPortal; H4UAZ9; -. DR SMR; H4UAZ9; 10-209. DR EnsemblBacteria; EHV42996; EHV42996; ECDEC5E_4994. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4US28_ECOLX Unreviewed; 211 AA. AC H4US28; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC6A_4812; OS Escherichia coli DEC6A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868160; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFV01000038; EHV51846.1; -; Genomic_DNA. DR ProteinModelPortal; H4US28; -. DR SMR; H4US28; 20-202. DR EnsemblBacteria; EHV51846; EHV51846; ECDEC6A_4812. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4V8Q3_ECOLX Unreviewed; 211 AA. AC H4V8Q3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC6B_5094; OS Escherichia coli DEC6B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868161; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFW01000047; EHV51191.1; -; Genomic_DNA. DR ProteinModelPortal; H4V8Q3; -. DR SMR; H4V8Q3; 20-202. DR EnsemblBacteria; EHV51191; EHV51191; ECDEC6B_5094. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4VP65_ECOLX Unreviewed; 211 AA. AC H4VP65; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC6C_4749; OS Escherichia coli DEC6C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868162; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFX01000070; EHV54284.1; -; Genomic_DNA. DR ProteinModelPortal; H4VP65; -. DR SMR; H4VP65; 20-202. DR EnsemblBacteria; EHV54284; EHV54284; ECDEC6C_4749. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4W4A2_ECOLX Unreviewed; 211 AA. AC H4W4A2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC6D_4734; OS Escherichia coli DEC6D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868163; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFY01000056; EHV66374.1; -; Genomic_DNA. DR ProteinModelPortal; H4W4A2; -. DR SMR; H4W4A2; 20-202. DR EnsemblBacteria; EHV66374; EHV66374; ECDEC6D_4734. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4WIQ2_ECOLX Unreviewed; 211 AA. AC H4WIQ2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC6E_4762; OS Escherichia coli DEC6E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868164; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIFZ01000039; EHV68597.1; -; Genomic_DNA. DR ProteinModelPortal; H4WIQ2; -. DR SMR; H4WIQ2; 20-202. DR EnsemblBacteria; EHV68597; EHV68597; ECDEC6E_4762. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4WZ78_ECOLX Unreviewed; 211 AA. AC H4WZ78; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC7A_4685; OS Escherichia coli DEC7A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868165; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC7A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC7A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGA01000061; EHV72595.1; -; Genomic_DNA. DR ProteinModelPortal; H4WZ78; -. DR SMR; H4WZ78; 10-208. DR EnsemblBacteria; EHV72595; EHV72595; ECDEC7A_4685. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4XCI8_ECOLX Unreviewed; 211 AA. AC H4XCI8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC7B_4376; OS Escherichia coli DEC7B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868166; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC7B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC7B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGB01000040; EHV90235.1; -; Genomic_DNA. DR ProteinModelPortal; H4XCI8; -. DR SMR; H4XCI8; 20-202. DR EnsemblBacteria; EHV90235; EHV90235; ECDEC7B_4376. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4XTM1_ECOLX Unreviewed; 211 AA. AC H4XTM1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC7C_4734; OS Escherichia coli DEC7C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868167; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC7C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC7C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGC01000026; EHV83462.1; -; Genomic_DNA. DR ProteinModelPortal; H4XTM1; -. DR SMR; H4XTM1; 10-208. DR EnsemblBacteria; EHV83462; EHV83462; ECDEC7C_4734. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4Y9E8_ECOLX Unreviewed; 211 AA. AC H4Y9E8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC7D_4934; OS Escherichia coli DEC7D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868168; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC7D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC7D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGD01000029; EHV85739.1; -; Genomic_DNA. DR ProteinModelPortal; H4Y9E8; -. DR SMR; H4Y9E8; 10-208. DR EnsemblBacteria; EHV85739; EHV85739; ECDEC7D_4934. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4YNU2_ECOLX Unreviewed; 211 AA. AC H4YNU2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC7E_4608; OS Escherichia coli DEC7E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868169; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC7E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC7E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGE01000039; EHV96412.1; -; Genomic_DNA. DR ProteinModelPortal; H4YNU2; -. DR SMR; H4YNU2; 10-208. DR EnsemblBacteria; EHV96412; EHV96412; ECDEC7E_4608. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4Z480_ECOLX Unreviewed; 211 AA. AC H4Z480; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC8A_4876; OS Escherichia coli DEC8A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868170; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGF01000052; EHW04482.1; -; Genomic_DNA. DR ProteinModelPortal; H4Z480; -. DR SMR; H4Z480; 10-208. DR EnsemblBacteria; EHW04482; EHW04482; ECDEC8A_4876. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H4ZJQ9_ECOLX Unreviewed; 211 AA. AC H4ZJQ9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC8B_4273; OS Escherichia coli DEC8B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868171; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGG01000069; EHW07419.1; -; Genomic_DNA. DR ProteinModelPortal; H4ZJQ9; -. DR SMR; H4ZJQ9; 10-208. DR EnsemblBacteria; EHW07419; EHW07419; ECDEC8B_4273. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5A4Z7_ECOLX Unreviewed; 211 AA. AC H5A4Z7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC8C_5825; OS Escherichia coli DEC8C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868172; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGH01000073; EHW09880.1; -; Genomic_DNA. DR ProteinModelPortal; H5A4Z7; -. DR SMR; H5A4Z7; 10-208. DR EnsemblBacteria; EHW09880; EHW09880; ECDEC8C_5825. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5ALB6_ECOLX Unreviewed; 211 AA. AC H5ALB6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC8D_5147; OS Escherichia coli DEC8D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868173; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGI01000050; EHW19596.1; -; Genomic_DNA. DR ProteinModelPortal; H5ALB6; -. DR SMR; H5ALB6; 10-208. DR EnsemblBacteria; EHW19596; EHW19596; ECDEC8D_5147. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5AN63_ECOLX Unreviewed; 211 AA. AC H5AN63; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC8E_5492; OS Escherichia coli DEC8E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868174; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGJ01000004; EHW37285.1; -; Genomic_DNA. DR ProteinModelPortal; H5AN63; -. DR SMR; H5AN63; 10-208. DR EnsemblBacteria; EHW37285; EHW37285; ECDEC8E_5492. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5BI70_ECOLX Unreviewed; 211 AA. AC H5BI70; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC9A_5113; OS Escherichia coli DEC9A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868175; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC9A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC9A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGK01000072; EHW29651.1; -; Genomic_DNA. DR ProteinModelPortal; H5BI70; -. DR SMR; H5BI70; 10-208. DR EnsemblBacteria; EHW29651; EHW29651; ECDEC9A_5113. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5BYX3_ECOLX Unreviewed; 211 AA. AC H5BYX3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC9B_4747; OS Escherichia coli DEC9B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868176; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC9B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC9B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGL01000060; EHW34583.1; -; Genomic_DNA. DR ProteinModelPortal; H5BYX3; -. DR SMR; H5BYX3; 10-208. DR EnsemblBacteria; EHW34583; EHW34583; ECDEC9B_4747. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5CE06_ECOLX Unreviewed; 211 AA. AC H5CE06; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC9C_4832; OS Escherichia coli DEC9C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868177; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC9C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC9C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGM01000056; EHW40288.1; -; Genomic_DNA. DR ProteinModelPortal; H5CE06; -. DR SMR; H5CE06; 10-208. DR EnsemblBacteria; EHW40288; EHW40288; ECDEC9C_4832. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5CUS6_ECOLX Unreviewed; 211 AA. AC H5CUS6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC9D_4790; OS Escherichia coli DEC9D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868178; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC9D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC9D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGN01000062; EHW47797.1; -; Genomic_DNA. DR ProteinModelPortal; H5CUS6; -. DR SMR; H5CUS6; 10-208. DR EnsemblBacteria; EHW47797; EHW47797; ECDEC9D_4790. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5DB86_ECOLX Unreviewed; 211 AA. AC H5DB86; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC9E_5264; OS Escherichia coli DEC9E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868179; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC9E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC9E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGO01000060; EHW50363.1; -; Genomic_DNA. DR ProteinModelPortal; H5DB86; -. DR SMR; H5DB86; 10-208. DR EnsemblBacteria; EHW50363; EHW50363; ECDEC9E_5264. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5DTV3_ECOLX Unreviewed; 211 AA. AC H5DTV3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC10A_5801; OS Escherichia coli DEC10A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868180; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGP01000075; EHW55051.1; -; Genomic_DNA. DR ProteinModelPortal; H5DTV3; -. DR SMR; H5DTV3; 10-208. DR EnsemblBacteria; EHW55051; EHW55051; ECDEC10A_5801. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5DU06_ECOLX Unreviewed; 211 AA. AC H5DU06; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC10B_6002; OS Escherichia coli DEC10B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868181; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGQ01000001; EHW81888.1; -; Genomic_DNA. DR ProteinModelPortal; H5DU06; -. DR SMR; H5DU06; 10-208. DR EnsemblBacteria; EHW81888; EHW81888; ECDEC10B_6002. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5EB40_ECOLX Unreviewed; 211 AA. AC H5EB40; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC10C_6014; OS Escherichia coli DEC10C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868182; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGR01000001; EHW82120.1; -; Genomic_DNA. DR ProteinModelPortal; H5EB40; -. DR SMR; H5EB40; 10-208. DR EnsemblBacteria; EHW82120; EHW82120; ECDEC10C_6014. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5F596_ECOLX Unreviewed; 211 AA. AC H5F596; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC10D_4448; OS Escherichia coli DEC10D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868183; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGS01000047; EHW75405.1; -; Genomic_DNA. DR ProteinModelPortal; H5F596; -. DR SMR; H5F596; 10-208. DR EnsemblBacteria; EHW75405; EHW75405; ECDEC10D_4448. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5FML7_ECOLX Unreviewed; 211 AA. AC H5FML7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC10E_4814; OS Escherichia coli DEC10E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868184; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGT01000040; EHW84301.1; -; Genomic_DNA. DR ProteinModelPortal; H5FML7; -. DR SMR; H5FML7; 10-208. DR EnsemblBacteria; EHW84301; EHW84301; ECDEC10E_4814. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5G516_ECOLX Unreviewed; 211 AA. AC H5G516; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC10F_5680; OS Escherichia coli DEC10F. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868185; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10F; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10F; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGU01000071; EHW85490.1; -; Genomic_DNA. DR ProteinModelPortal; H5G516; -. DR SMR; H5G516; 10-208. DR EnsemblBacteria; EHW85490; EHW85490; ECDEC10F_5680. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5GJU7_ECOLX Unreviewed; 211 AA. AC H5GJU7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC11A_4635; OS Escherichia coli DEC11A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868186; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC11A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC11A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGV01000055; EHW85458.1; -; Genomic_DNA. DR ProteinModelPortal; H5GJU7; -. DR SMR; H5GJU7; 10-208. DR EnsemblBacteria; EHW85458; EHW85458; ECDEC11A_4635. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5GZX1_ECOLX Unreviewed; 211 AA. AC H5GZX1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC11B_4672; OS Escherichia coli DEC11B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868187; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC11B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC11B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGW01000046; EHW99046.1; -; Genomic_DNA. DR ProteinModelPortal; H5GZX1; -. DR SMR; H5GZX1; 10-208. DR EnsemblBacteria; EHW99046; EHW99046; ECDEC11B_4672. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5HFH2_ECOLX Unreviewed; 211 AA. AC H5HFH2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC11C_4997; OS Escherichia coli DEC11C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868188; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC11C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC11C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGX01000040; EHX06575.1; -; Genomic_DNA. DR ProteinModelPortal; H5HFH2; -. DR SMR; H5HFH2; 10-208. DR EnsemblBacteria; EHX06575; EHX06575; ECDEC11C_4997. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5HXG2_ECOLX Unreviewed; 211 AA. AC H5HXG2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC11D_4722; OS Escherichia coli DEC11D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868189; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC11D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC11D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGY01000053; EHX04830.1; -; Genomic_DNA. DR ProteinModelPortal; H5HXG2; -. DR SMR; H5HXG2; 10-208. DR EnsemblBacteria; EHX04830; EHX04830; ECDEC11D_4722. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5IBJ1_ECOLX Unreviewed; 211 AA. AC H5IBJ1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC11E_4626; OS Escherichia coli DEC11E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868190; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC11E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC11E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIGZ01000028; EHX14997.1; -; Genomic_DNA. DR ProteinModelPortal; H5IBJ1; -. DR SMR; H5IBJ1; 10-208. DR EnsemblBacteria; EHX14997; EHX14997; ECDEC11E_4626. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5IRZ2_ECOLX Unreviewed; 211 AA. AC H5IRZ2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC12A_4878; OS Escherichia coli DEC12A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868191; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHA01000043; EHX24936.1; -; Genomic_DNA. DR ProteinModelPortal; H5IRZ2; -. DR SMR; H5IRZ2; 10-208. DR EnsemblBacteria; EHX24936; EHX24936; ECDEC12A_4878. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5J9J5_ECOLX Unreviewed; 211 AA. AC H5J9J5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC12B_5331; OS Escherichia coli DEC12B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868192; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHB01000072; EHX21695.1; -; Genomic_DNA. DR ProteinModelPortal; H5J9J5; -. DR SMR; H5J9J5; 10-208. DR EnsemblBacteria; EHX21695; EHX21695; ECDEC12B_5331. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5JRA1_ECOLX Unreviewed; 211 AA. AC H5JRA1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC12C_4984; OS Escherichia coli DEC12C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868193; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHC01000086; EHX25427.1; -; Genomic_DNA. DR ProteinModelPortal; H5JRA1; -. DR SMR; H5JRA1; 10-208. DR EnsemblBacteria; EHX25427; EHX25427; ECDEC12C_4984. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5K6Q6_ECOLX Unreviewed; 211 AA. AC H5K6Q6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC12D_5005; OS Escherichia coli DEC12D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868194; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHD01000077; EHX39379.1; -; Genomic_DNA. DR ProteinModelPortal; H5K6Q6; -. DR SMR; H5K6Q6; 10-208. DR EnsemblBacteria; EHX39379; EHX39379; ECDEC12D_5005. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5KLZ0_ECOLX Unreviewed; 211 AA. AC H5KLZ0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC12E_4776; OS Escherichia coli DEC12E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868195; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHE01000045; EHX42457.1; -; Genomic_DNA. DR ProteinModelPortal; H5KLZ0; -. DR SMR; H5KLZ0; 10-208. DR EnsemblBacteria; EHX42457; EHX42457; ECDEC12E_4776. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5L1N6_ECOLX Unreviewed; 211 AA. AC H5L1N6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC13A_4449; OS Escherichia coli DEC13A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868196; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC13A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC13A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHF01000033; EHX42420.1; -; Genomic_DNA. DR ProteinModelPortal; H5L1N6; -. DR SMR; H5L1N6; 10-208. DR EnsemblBacteria; EHX42420; EHX42420; ECDEC13A_4449. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5LEA8_ECOLX Unreviewed; 211 AA. AC H5LEA8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC13B_4299; OS Escherichia coli DEC13B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868197; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC13B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC13B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHG01000035; EHX55600.1; -; Genomic_DNA. DR ProteinModelPortal; H5LEA8; -. DR SMR; H5LEA8; 10-208. DR EnsemblBacteria; EHX55600; EHX55600; ECDEC13B_4299. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5LUR1_ECOLX Unreviewed; 211 AA. AC H5LUR1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC13C_4870; OS Escherichia coli DEC13C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868198; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC13C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC13C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHH01000063; EHX55352.1; -; Genomic_DNA. DR ProteinModelPortal; H5LUR1; -. DR SMR; H5LUR1; 10-208. DR EnsemblBacteria; EHX55352; EHX55352; ECDEC13C_4870. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5M8T4_ECOLX Unreviewed; 211 AA. AC H5M8T4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC13D_4578; OS Escherichia coli DEC13D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868199; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC13D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC13D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHI01000033; EHX57797.1; -; Genomic_DNA. DR ProteinModelPortal; H5M8T4; -. DR SMR; H5M8T4; 10-208. DR EnsemblBacteria; EHX57797; EHX57797; ECDEC13D_4578. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5MN70_ECOLX Unreviewed; 211 AA. AC H5MN70; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC13E_4602; OS Escherichia coli DEC13E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868200; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC13E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC13E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHJ01000050; EHX68350.1; -; Genomic_DNA. DR ProteinModelPortal; H5MN70; -. DR SMR; H5MN70; 10-208. DR EnsemblBacteria; EHX68350; EHX68350; ECDEC13E_4602. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5N1T7_ECOLX Unreviewed; 211 AA. AC H5N1T7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC14A_4436; OS Escherichia coli DEC14A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868201; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC14A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC14A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHK01000036; EHX72106.1; -; Genomic_DNA. DR ProteinModelPortal; H5N1T7; -. DR SMR; H5N1T7; 10-208. DR EnsemblBacteria; EHX72106; EHX72106; ECDEC14A_4436. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5NHE4_ECOLX Unreviewed; 211 AA. AC H5NHE4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC14B_4826; OS Escherichia coli DEC14B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868202; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC14B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC14B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHL01000079; EHX73782.1; -; Genomic_DNA. DR ProteinModelPortal; H5NHE4; -. DR SMR; H5NHE4; 10-208. DR EnsemblBacteria; EHX73782; EHX73782; ECDEC14B_4826. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5NXL0_ECOLX Unreviewed; 211 AA. AC H5NXL0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC14C_4789; OS Escherichia coli DEC14C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868203; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC14C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC14C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHM01000070; EHX83696.1; -; Genomic_DNA. DR ProteinModelPortal; H5NXL0; -. DR SMR; H5NXL0; 10-208. DR EnsemblBacteria; EHX83696; EHX83696; ECDEC14C_4789. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5PCD0_ECOLX Unreviewed; 211 AA. AC H5PCD0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC14D_4690; OS Escherichia coli DEC14D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868204; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC14D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC14D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHN01000071; EHX86400.1; -; Genomic_DNA. DR ProteinModelPortal; H5PCD0; -. DR SMR; H5PCD0; 10-208. DR EnsemblBacteria; EHX86400; EHX86400; ECDEC14D_4690. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5PSV2_ECOLX Unreviewed; 211 AA. AC H5PSV2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC15A_4974; OS Escherichia coli DEC15A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868206; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC15A; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC15A; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHO01000058; EHX92610.1; -; Genomic_DNA. DR ProteinModelPortal; H5PSV2; -. DR SMR; H5PSV2; 10-208. DR EnsemblBacteria; EHX92610; EHX92610; ECDEC15A_4974. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5Q7F0_ECOLX Unreviewed; 211 AA. AC H5Q7F0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC15B_4814; OS Escherichia coli DEC15B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868207; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC15B; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC15B; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHP01000034; EHX99389.1; -; Genomic_DNA. DR ProteinModelPortal; H5Q7F0; -. DR SMR; H5Q7F0; 10-208. DR EnsemblBacteria; EHX99389; EHX99389; ECDEC15B_4814. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5QM98_ECOLX Unreviewed; 211 AA. AC H5QM98; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC15C_4685; OS Escherichia coli DEC15C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868208; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC15C; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC15C; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHQ01000031; EHY02135.1; -; Genomic_DNA. DR ProteinModelPortal; H5QM98; -. DR SMR; H5QM98; 10-208. DR EnsemblBacteria; EHY02135; EHY02135; ECDEC15C_4685. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5R1X8_ECOLX Unreviewed; 211 AA. AC H5R1X8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC15D_4625; OS Escherichia coli DEC15D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868209; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC15D; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC15D; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHR01000030; EHY10385.1; -; Genomic_DNA. DR ProteinModelPortal; H5R1X8; -. DR SMR; H5R1X8; 10-208. DR EnsemblBacteria; EHY10385; EHY10385; ECDEC15D_4625. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5RHN9_ECOLX Unreviewed; 211 AA. AC H5RHN9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECDEC15E_4987; OS Escherichia coli DEC15E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868210; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC15E; RX PubMed=22582382; DOI=10.1128/JB.00426-12; RA Hazen T.H., Sahl J.W., Redman J.C., Morris C.R., Daugherty S.C., RA Chibucos M.C., Sengamalay N.A., Fraser-Liggett C.M., Steinsland H., RA Whittam T.S., Whittam B., Manning S.D., Rasko D.A.; RT "Draft Genome Sequences of the Diarrheagenic Escherichia coli RT Collection."; RL J. Bacteriol. 194:3026-3027(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC15E; RA Rasko D., Redman J., Daugherty S.C., Chibucos M.C., Tallon L., RA Sadzewicz L., Jones K., Santana-Cruz I., Liu X.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHS01000051; EHY14748.1; -; Genomic_DNA. DR ProteinModelPortal; H5RHN9; -. DR SMR; H5RHN9; 10-208. DR EnsemblBacteria; EHY14748; EHY14748; ECDEC15E_4987. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H5SDS9_9BACT Unreviewed; 206 AA. AC H5SDS9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HGMM_F14E04C06; OS uncultured Aquificae bacterium. OC Bacteria; Aquificae; environmental samples. OX NCBI_TaxID=453415; RN [1] RP NUCLEOTIDE SEQUENCE. RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S., RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.; RT "Genetic and functional properties of uncultivated thermophilic RT crenarchaeotes from a subsurface gold mine as revealed by analysis of RT genome fragments."; RL Environ. Microbiol. 7:1967-1984(2005). RN [2] RP NUCLEOTIDE SEQUENCE. RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S., RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.; RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA RT Pathway Dominates a Subsurface Ecosystem."; RL PLoS ONE 7:e30559-e30559(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011685; BAL54315.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 125 127 THZ-P binding (By similarity). FT REGION 175 176 THZ-P binding (By similarity). FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 155 155 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22848 MW; 0B2A1C79A9F6D882 CRC64; MTDDKYFTDR DLVDTIEKAL QGGVTALQYR FKNKSTRQMY EELLVLRELT RRYGADLVVN DRVDLAMAVG ADGVHVGKED LPPDVVRKIV GDSMYIGYSV NSVEDLREVD HLPIDYIGFG SVYETTTKEN YKLVGIEGLR QAVKLTSKPV VAIGGITSYR MKEVLQTGVK GVAVVSAILG FEDVKSAAQT LAQIYKSVVK EKFFAP // ID H5SDV1_9BACT Unreviewed; 154 AA. AC H5SDV1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HGMM_F14E04C28; OS uncultured Aquificae bacterium. OC Bacteria; Aquificae; environmental samples. OX NCBI_TaxID=453415; RN [1] RP NUCLEOTIDE SEQUENCE. RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S., RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.; RT "Genetic and functional properties of uncultivated thermophilic RT crenarchaeotes from a subsurface gold mine as revealed by analysis of RT genome fragments."; RL Environ. Microbiol. 7:1967-1984(2005). RN [2] RP NUCLEOTIDE SEQUENCE. RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S., RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.; RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA RT Pathway Dominates a Subsurface Ecosystem."; RL PLoS ONE 7:e30559-e30559(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011685; BAL54337.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 154 AA; 17022 MW; D55C2CE64AFF6F16 CRC64; MVQLREKSLS AKEYYQKALK AREITREYSA LLLINERVDI ALAVGADGVH LPQNGLPPSA VRRLKKDLIV GFSAHDLKSA LYAQEEGADF ITLSPIFKTP SHPEREPLGL EALKDISKRV SIPVYALGGI TWEKIKLCYK NGAYGIAGIS LFLK // ID H5SEC0_9GAMM Unreviewed; 205 AA. AC H5SEC0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HGMM_F01C09C32, HGMM_F16E07C13; OS uncultured gamma proteobacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=86473; RN [1] RP NUCLEOTIDE SEQUENCE. RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S., RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.; RT "Genetic and functional properties of uncultivated thermophilic RT crenarchaeotes from a subsurface gold mine as revealed by analysis of RT genome fragments."; RL Environ. Microbiol. 7:1967-1984(2005). RN [2] RP NUCLEOTIDE SEQUENCE. RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S., RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.; RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA RT Pathway Dominates a Subsurface Ecosystem."; RL PLoS ONE 7:e30559-e30559(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011628; BAL52438.1; -; Genomic_DNA. DR EMBL; AP011691; BAL54506.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21491 MW; A981DBD9662486A8 CRC64; MVHPFPRRGL YAITPDCEDF ARLLTQVEAV LTGGAKAVQL RDKQRHLNQT QAAQLVKLCH AYQVPLIVND DLALAERIGA DGVHLGREDT DACQARNRLG PDAIVGVSCY ADLSRAVCAA QAGATYVAFG AFFSSATKPN ASPAPIELLS AAKKVLACPI VAIGGITPEN GACLLAAGAD LLAAISGVFG HPDPEQAARR YADLF // ID H5SHV8_9GAMM Unreviewed; 310 AA. AC H5SHV8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=7,8-dihydro-8-oxoguanine triphosphatase; GN ORFNames=HGMM_F07C12C20, HGMM_F31D07C18; OS uncultured gamma proteobacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=86473; RN [1] RP NUCLEOTIDE SEQUENCE. RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S., RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.; RT "Genetic and functional properties of uncultivated thermophilic RT crenarchaeotes from a subsurface gold mine as revealed by analysis of RT genome fragments."; RL Environ. Microbiol. 7:1967-1984(2005). RN [2] RP NUCLEOTIDE SEQUENCE. RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S., RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.; RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA RT Pathway Dominates a Subsurface Ecosystem."; RL PLoS ONE 7:e30559-e30559(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011660; BAL53535.1; -; Genomic_DNA. DR EMBL; AP011728; BAL55744.1; -; Genomic_DNA. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 310 AA; 34088 MW; 5889FF1EF86AFBCD CRC64; MPFLHVAAGA ICNAHGQVLI AQRRAGGPQG GRWEFPGGKL KPGESAYAAL VRELKEELGI SVTAARPLIQ IRHAYADRKV HLEVFAVTAF RGRPKARENQ PLAWVAIAEL ARYELLEANR PVVTALELPP FYPVLERAGS EKAYRERFKR LVWQGHRLLY WRARDLPEAA YLRLAEEFSR VLAQAGGCLM VRDLPYPEPW GAPVGLHLSA RQLAALPARP PGWRWVGAAC HSLAELRRAS QLGLDFAVLS PVRSTSTHPD AVPLGWQTVR AWIAWVNLPV YLLGGLGRLD LAQAWDCGAQ GIAGIGAFCA // ID H5SLW3_9ZZZZ Unreviewed; 216 AA. AC H5SLW3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=HGMM_F47C12C26; OS uncultured prokaryote. OC unclassified sequences; environmental samples. OX NCBI_TaxID=198431; RN [1] RP NUCLEOTIDE SEQUENCE. RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S., RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.; RT "Genetic and functional properties of uncultivated thermophilic RT crenarchaeotes from a subsurface gold mine as revealed by analysis of RT genome fragments."; RL Environ. Microbiol. 7:1967-1984(2005). RN [2] RP NUCLEOTIDE SEQUENCE. RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S., RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.; RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA RT Pathway Dominates a Subsurface Ecosystem."; RL PLoS ONE 7:e30559-e30559(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011767; BAL57149.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; SQ SEQUENCE 216 AA; 22487 MW; 24D7371471ABB987 CRC64; MGLDLRVYVI TDRTFRGRSH EDVARAALVG GATVVQLRDK QAGGRELVEW ARQLRALTRR ARVTFVVNDR VDVALAAEAD GAHVGEDDLP VADARRLLGP GRIVGASAGT VEEALRAQAE GADYLGVGPV FATSTKPDAG GAIGPEGLRR IVQAVRIPVV GIGGITLDNA AEVIRAGAAG VAVISAVAAA DDMVEATRRL REVVDAALQE RGGAER // ID H5SZD6_LACLL Unreviewed; 215 AA. AC H5SZD6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=lilo_1201; OS Lactococcus lactis subsp. lactis IO-1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=1046624; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IO-1; RX PubMed=22461545; DOI=10.1128/JB.00074-12; RA Kato H., Shiwa Y., Oshima K., Machii M., Araya-kojima T., Zendo T., RA Shimizu-kadota M., Hattori M., Sonomoto K., Yoshikawa H.; RT "Complete Genome Sequence of Lactococcus lactis IO-1, a Lactic Acid RT Bacterium That Utilizes Xylose and Produces High Levels of L-Lactic RT Acid."; RL J. Bacteriol. 194:2102-2103(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012281; BAL51200.1; -; Genomic_DNA. DR RefSeq; YP_007508526.1; NC_020450.1. DR EnsemblBacteria; BAL51200; BAL51200; lilo_1201. DR GeneID; 14678701; -. DR KEGG; lls:lilo_1201; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23571 MW; B53D417E72C5E42E CRC64; MKNKILDLRA YFIAGPQDFP KLSIDDAVDK ISVIIKSGVT VYQFRDKGTI YKNNNQRLEV AKRLQGVAQK AAVSFIVNDD VELARELSAD GIHVGQDDDS VSKIRELIGQ EMWVGLSVSN DMELESAQKS GADYLGIGPI YPTNSKSDAA EPIGIDHLRK MLEHNQLPTV GIGGITENSL TELSKIGLGG VAVISLLTES ENYKNMVQKI KQNIR // ID H5T4V2_MELPD Unreviewed; 216 AA. AC H5T4V2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MPD5_0964; OS Melissococcus plutonius (strain DAT561). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Melissococcus. OX NCBI_TaxID=1090974; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DAT561; RX PubMed=22582373; DOI=10.1128/JB.00437-12; RA Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M., RA Miyoshi-Akiyama T.; RT "Complete genome sequence of Melissococcus plutonius DAT561, a strain RT that shows an unusual growth profile and is representative of an RT endemic cluster in Japan."; RL J. Bacteriol. 194:3014-3014(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012282; BAL62195.1; -; Genomic_DNA. DR RefSeq; YP_005319690.1; NC_016938.1. DR EnsemblBacteria; BAL62195; BAL62195; MPD5_0964. DR GeneID; 11879464; -. DR KEGG; mpx:MPD5_0964; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23733 MW; A6C985FCDA819F5A CRC64; MLTSQQLKKA LQIYFIAGTQ DTNGSSLQLL NVLDKALTAG ITCFQYREKG ANSLKKSLER KRMARACQRL CRKHQVPFII NDDIELALEI DADGIHVGQN DEAISKVIQK NPNKIIGLSC HNVTEITYAN TFKEISYYGI GPIFPTSSKL DADKPLGLDQ LKTMVAVAKK PTVAIGGISI KNAVDIWQSN ADGLAIISAI TQAENLEETI ELLKFN // ID H5TCP9_9ALTE Unreviewed; 530 AA. AC H5TCP9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Hydroxymethylpyrimidine kinase; GN ORFNames=GPUN_1961; OS Glaciecola punicea DSM 14233 = ACAM 611. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Glaciecola. OX NCBI_TaxID=1121923; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACAM 611; RX PubMed=22628500; DOI=10.1128/JB.00463-12; RA Qin Q.-L., Xie B.-B., Shu Y.-L., Rong J.-C., Zhao D.-L., Zhang X.-Y., RA Chen X.-L., Zhou B.-C., Zhanga Y.-Z.; RT "Genome sequence of proteorhodopsin-containing sea ice bacterium RT Glaciecola punicea ACAM 611T."; RL J. Bacteriol. 194:3267-3267(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACAM 611; RA Qin Q.L., Xie B.B., Shu Y.L., Zhang Y.Z.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAET01000020; GAB56076.1; -; Genomic_DNA. DR EnsemblBacteria; GAB56076; GAB56076; GPUN_1961. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 530 AA; 56939 MW; 4437C591947A8096 CRC64; MSNQHKIFAR TQPAKPIVWS IAGSDSGGGA GIQADSLTIH DLGGHACNVV TAITAQNSHQ VIDVAPTCAM VLLNQLNGLL DDLPPSAIKI GVLANAEQFQ LISHWLSNTL RPYQQQHDLL IPVIWDPVMV STSGQSLTLA NNSPTVDDYI SLANHVTLIT PNAFELQVLA RLLQAQGNTS QEPLECLANA VLSGVLVTGG ADIDTFAIDW LMAKSIAHTS VFHAHQRIGF QSSRVDTRHN HGTGCALSAA IATAMAFGHP LLDATVIAKA YVHQGLSSGY GLGKGAGVLG RNGWPHDLVH FPEILMPHYA SLSINHGLVF AKVIQPLGVY TVTKSVSVLE QVLKSGARTV QLRIKNNSVD KRPLNEIEKD IIQAISLGHK YKAQVFINDH WEIALKHGAF GVHLGQEDVL QANLLQIANA GLASGLSSHG YFEMLLAQQL NPSYLAIGHI FSTPTKQMPS KPQGLLKLSC YCKLLKNKMP LVAIGGVDLQ NLAQLKATAV HDVAVVRGIE STENPGQSWQ ALQQKWQALT // ID H5TJX8_9ACTO Unreviewed; 230 AA. AC H5TJX8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GOOTI_082_00160; OS Gordonia otitidis NBRC 100426. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1108044; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100426; RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Gordonia otitidis NBRC 100426."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFB01000082; GAB33786.1; -; Genomic_DNA. DR EnsemblBacteria; GAB33786; GAB33786; GOOTI_082_00160. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT METAL 87 87 Magnesium (By similarity). FT METAL 106 106 Magnesium (By similarity). FT BINDING 86 86 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 189 189 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 230 AA; 24472 MW; CE73C93506CF8EE2 CRC64; MAIHSHRHAR LATALLYLCT DARRERGDLV EFVDAALAGG VDIVQLRDKG SAGEKQFGTL EAREELEILA LLREVTSARN ALLAVNDRAD IATLADADIL HIGQDDLPPA AARRIVGKHV IVGRSTHDVE QAAAAAADPD VDYFCVGPCW PTPTKPGRHA PGLELVREVA ANESADDVRH RKPWFAIGGI DATRLPEVTA AGAQRIVVVR AITAASDPAA AATELRDPLA // ID H5U725_9ACTO Unreviewed; 236 AA. AC H5U725; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GOSPT_133_00300; OS Gordonia sputi NBRC 100414. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1089453; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100414; RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Gordonia sputi NBRC 100414."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFC01000131; GAB41533.1; -; Genomic_DNA. DR EnsemblBacteria; GAB41533; GAB41533; GOSPT_133_00300. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 51 55 HMP-PP binding (By similarity). FT REGION 158 160 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 161 161 HMP-PP (By similarity). FT BINDING 195 195 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 236 AA; 24850 MW; 4FAECFC18EFBED31 CRC64; MATLAIVTAH HARAKRLESA TLYLCTDARR ERGDLAEFVD AALAGGVDIV QLRDKGSAGE KRFGALEARE ELEILAVLRE ITQSRGALLA VNDRADIAAL AGADVLHVGQ DDLPPAAARR IVGKDVLVGK STHDVDQAAA AEADPDVDYF CVGPCWPTPT KPGRPAPGLD LVREVAANES AENPRRRKPW FAIGGVDADR LPEVTEAGAR RIVVVRAITS ASGPSAAASQ LRAGLT // ID H5UB60_9ACTO Unreviewed; 260 AA. AC H5UB60; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GOTRE_034_00090; OS Gordonia terrae NBRC 100016. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1089454; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100016; RA Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Gordonia terrae NBRC 100016."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFD01000034; GAB42968.1; -; Genomic_DNA. DR EnsemblBacteria; GAB42968; GAB42968; GOTRE_034_00090. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 77 81 HMP-PP binding (By similarity). FT REGION 184 186 THZ-P binding (By similarity). FT METAL 119 119 Magnesium (By similarity). FT METAL 138 138 Magnesium (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 157 157 HMP-PP (By similarity). FT BINDING 187 187 HMP-PP (By similarity). FT BINDING 220 220 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 260 AA; 26742 MW; A2ACC76D30066E7B CRC64; MFVRSTLRPG LGRPVSLVGV TTPNPTTSAS ADSGRAADRC RRLSAARLYL CTDARRERGD LLDFVDAALA GGVDIVQLRD KNSPGEREFG TLEAGEELEI LAGLRAVADA HGALLAVNDR ADIAALSGAD VLHVGQGDLA PSAARRIIGP GVIIGASTHD PEQAAAAIAD EDVDYFCVGP CWTTPTKPGR AAAGLDLVSA TSEMLSRTPQ STKPWFAIGG IDAGRVGEVT ALGARRIVVV RAITAAADPA AAARDLAGML // ID H5USN5_9MICO Unreviewed; 216 AA. AC H5USN5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MOPEL_080_00220; OS Mobilicoccus pelagius NBRC 104925. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Dermatophilaceae; Mobilicoccus. OX NCBI_TaxID=1089455; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 104925; RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Mobilicoccus pelagius NBRC 104925."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFE01000058; GAB48743.1; -; Genomic_DNA. DR EnsemblBacteria; GAB48743; GAB48743; MOPEL_080_00220. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22810 MW; 1CC64ADDA6AF1BE7 CRC64; MTTTSQAVRE RLAASRLYLC TDTRAERGDL RGFVRAAFAG GVDIVQIREK GIEAAQELAA LEIVAEEARA AEALVAANDR ADVAALAGVD VLHVGQDDLT PAQVRRFCPD AVVGLSTHSP EQLAAALAEP DVDYFCTGPI WATPTKPGRP GVGLDLVRAA AESGTETPWF AIGGVSHETI GEVVDAGATR VVVVREITES HDPEAAARRL RHVLPD // ID H5UUF3_9MICO Unreviewed; 217 AA. AC H5UUF3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MOPEL_129_00040; OS Mobilicoccus pelagius NBRC 104925. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Dermatophilaceae; Mobilicoccus. OX NCBI_TaxID=1089455; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 104925; RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Mobilicoccus pelagius NBRC 104925."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFE01000088; GAB49361.1; -; Genomic_DNA. DR EnsemblBacteria; GAB49361; GAB49361; MOPEL_129_00040. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 192 193 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22379 MW; CC249FD4A1F72E2A CRC64; MTRPACDLTL YLVTDTPMAG GPERVADVVR AAVDGGATLV QVRDPHASDD ELVRIARSVV TALRGSGVPV LLNDRVHLVE EAGADGAHVG QSDTDPITAR RLLGPDRLLG LSCQTLAHVE TARALPEGTI DHVGLGPVFD QTTKPDAAAA SGLDTLTALV AESPWPTVAI GGITVDRIGL LPVTGVDGAA VVSAICATPD PREAAATLLT RWKDAPR // ID H5V7L1_ESCHE Unreviewed; 211 AA. AC H5V7L1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=EH105704_25_00110; OS Escherichia hermannii NBRC 105704. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1115512; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 105704; RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Escherichia hermannii NBRC 105704."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFF01000025; GAB53969.1; -; Genomic_DNA. DR EnsemblBacteria; GAB53969; GAB53969; EH105704_25_00110. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22599 MW; 59415A9152141920 CRC64; MIQPLFPPVP KRLGLYPVVD SVEWIARLLD AGVRTLQLRI KDKSEEDAEG AVIDAIALGH RYQARLFIND YWRLAIKHQA YGVHLGQEDL AGADLEAIHA AGLRLGISTH DDMEIDVALT VRPSYVALGH VFPTRTKNMP SSPQGLEQLT AHVQRLGDYP TVAIGGISLD RAPAVLATGV GSIAVVSAIT QAADWQSATA QLLALAGAGN E // ID H5V952_HELBI Unreviewed; 209 AA. AC H5V952; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HBZS_102290; OS Helicobacter bizzozeronii CCUG 35545. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1002805; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 35545; RA Schott T., Rossi M., Paulin L., Auvinen P., Hanninen M.-L.; RT "The genome of the canine-derived Helicobacter bizzozeronii CCUG RT 35545."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGP01000008; CCF79781.1; -; Genomic_DNA. DR EnsemblBacteria; CCF79781; CCF79781; HBZS_102290. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22743 MW; E056E7F5B563A20F CRC64; MGIELKGLYA LSDELLTPYD QLPHMLSLAI QGGVKIFQFR DKSHSDSELF SLAKDLAKIC QKHSVGFVIN DRLDLALKCH AWGLHVGSDD VPLSQARRLF KGHLGVSCYG NLDQALQAQQ ARASYAAFGA CFPSSTKPKA PCISLDTLQH AKAHLNIPIC AIGGINPQNA PQLKNADMIA VISSLWSGDI VQNARKLLNC WQGKTSNLH // ID H5VEK6_HELBI Unreviewed; 198 AA. AC H5VEK6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=HBZS_121360; OS Helicobacter bizzozeronii CCUG 35545. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1002805; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 35545; RA Schott T., Rossi M., Paulin L., Auvinen P., Hanninen M.-L.; RT "The genome of the canine-derived Helicobacter bizzozeronii CCUG RT 35545."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGP01000129; CCF81685.1; -; Genomic_DNA. DR EnsemblBacteria; CCF81685; CCF81685; HBZS_121360. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 198 AA; 21692 MW; 4027ADC4277DF29E CRC64; MSSLETYWIT PQLSSDPQIF QATLQATLQA HTIHKAALRG ANFSAQLLDL FARTCHAHHT TSFLNLPTLK LSVQKALEHG FQGVHVKGAQ ILEIPTIPPP LQIFYSAHNA REVLQALDLG AHFCTISPIC ATPNKPPPLG LDYLDQFPQE VKARLFALGG MGYELASLLE KKGLKGFAGI RCFAPNVAFL QTHTPTRT // ID H5VUF5_SALSE Unreviewed; 211 AA. AC H5VUF5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SS209_04877; OS Salmonella enterica subsp. enterica serovar Senftenberg str. SS209. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1147753; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS209; RA Grepinet O., Boumart Z., Virlogeux-Payant I., Loux V., Chiapello H., RA Gendrault A., Gibrat J.-F., Chemaly M., Velge P.; RT "Genome sequence of the persistent Salmonella Senftenberg strain RT SS209."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGQ01000108; CCF91161.1; -; Genomic_DNA. DR EnsemblBacteria; CCF91161; CCF91161; SS209_04877. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22923 MW; AC2D24D5365B3705 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHNA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIDRLADYP TVAIGGISVE RAPSVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGVGD E // ID H5WG48_RALSL Unreviewed; 210 AA. AC H5WG48; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RSK60_80001; OS Ralstonia solanacearum K60-1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=1091042; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K60; RA LABGeM C.E.A.; RT "Ralstonia solanacearum K60, WGS."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K60; RA MicroScope M.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGT01000326; CCF98769.1; -; Genomic_DNA. DR EnsemblBacteria; CCF98769; CCF98769; RSK60_80001. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 210 AA; 21908 MW; 3C140D1A57B6586D CRC64; MVPDAAWVER LVALGVPTVQ LRVKSDDTPA VAGHVRRAAA AARGSQTRLF INDHWRVALD VHAARSDSAP DSGVYGIHLG QEDIDDADLP AIRASGLRLG ISTHGYAEML RVAPLNPSYL ALGAVFATPT KTMPTVPQGL GRLFAHAAAM RTRVPAPPLV AIGGIDLAAM PRVLQSGVGC VAVVRALTQA EDVPAAVQAL QATFAAHVRA // ID H5X000_9PSEU Unreviewed; 225 AA. AC H5X000; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SacmaDRAFT_4822; OS Saccharomonospora marina XMU15. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882083; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XMU15; RX PubMed=22768369; DOI=10.4056/sigs.2655905; RA Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S., RA Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M., RA Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C., RA Woyke T.; RT "Genome sequence of the ocean sediment bacterium Saccharomonospora RT marina type strain (XMU15(T))."; RL Stand. Genomic Sci. 6:265-275(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001439; EHR52996.1; -; Genomic_DNA. DR EnsemblBacteria; EHR52996; EHR52996; SacmaDRAFT_4822. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 23911 MW; 1893547ADB7B5315 CRC64; MPGLNGDQIR QRLAEARLYL CTDARRDRGD LAEFADAALA GGVDIIQLRD KNDGTLEAGE EIEALEVLAR ACAKHGALLS VNDRADIALA VQADVLHLGQ DDLPVSVARR ILGDDPVIGR STHSLEEARL AATEDGVDYF CVGPCWPTPT KPGRPAPGLE LIRAVAQGID TTRPWFAIGG IDERRVGEVV AAGARRAVVV RAITEAEDPA AAATALRQAL QPDSR // ID H5XR95_9PSEU Unreviewed; 225 AA. AC H5XR95; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SaccyDRAFT_4568; OS Saccharomonospora cyanea NA-134. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882082; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NA-134; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Brambilla E.-M., Klenk H.-P., Woyke T.; RT "The Noncontiguous Finished sequence of Saccharomonospora cyanea NA- RT 134."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001440; EHR63376.1; -; Genomic_DNA. DR EnsemblBacteria; EHR63376; EHR63376; SaccyDRAFT_4568. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 23705 MW; 474D6CFB70915B30 CRC64; MPGLDGDRIR KRLDEARLYL CTDARTQRGD LAEFVDAALA GGVDIVQLRD KTGGAPLEAA QEIAALEVLA EACARHGALL AVNDRADVAL AVDADVLHLG QDDLPVRVAR RIVGEEPVIG RSTHSPDQAR AAATEAGVDY FCVGPCWPTP TKPGRPAPGL DLVRSVASEV ETARPWFAIG GIDLPRLDDV LAAGARRAVV VRAITEADDP AAAARALREG LTRAD // ID H5Y5Z2_9FIRM Unreviewed; 208 AA. AC H5Y5Z2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=DesyoDRAFT_3958; OS Desulfosporosinus youngiae DSM 17734. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=768710; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17734; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Lu M., Land M.L., Hauser L., Pester M., RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A., RA Woyke T.J.; RT "The Noncontiguous Finished genome of Desulfosporosinus youngiae DSM RT 17734."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001441; EHQ90931.1; -; Genomic_DNA. DR EnsemblBacteria; EHQ90931; EHQ90931; DesyoDRAFT_3958. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22367 MW; 2AA560A57E0E89CC CRC64; MAVDYTLYLV TDRKLVGSKD FLTSVKRALE GGVTLIQLRE KDAGSKEFYE LGLQVKKIAA EFGVPLIIND RVDLALVLDA DGVHIGQNDL PIEHVRRMIG KDKLLGYSVA NQEEAVYGEA MGADYLGAGP VFPTGSKKDA SEPIGLEGLK TIKQCVNIPV VGIGGIGTAN LSQLKSIGIN GISVISAILS EEDPYCAARE LKNLWKDH // ID H5YEV2_9BRAD Unreviewed; 229 AA. AC H5YEV2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 22-JAN-2014, entry version 11. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=Bra471DRAFT_01305; OS Bradyrhizobium sp. WSM471. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=319017; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WSM471; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., RA Rui T., Howieson J., Reeve W., Woyke T.; RT "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001442; EHR00731.1; -; Genomic_DNA. DR EnsemblBacteria; EHR00731; EHR00731; Bra471DRAFT_01305. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 229 AA; 23953 MW; 7C7B2A23ACD807A2 CRC64; MSNKSPPPRP APRLYLATPV VDDPASLLAE LPGLLAAADV AAVLLRLKET DQRTMISRIK ALAPPVQKAG AALLVDGHPE LVARGGADGA HLPGIAALKE ALPSLKPDRI AGVGGLTTRH HSMDAGEIGA DYLLFGEPDA KGQRPSSQAI AERLDWWAEL FEPPCVGFAM SLEEAHEFAA NGADFVLVDD FIWADPRGPK AALVEIDAAI KKAHATALAG QNPAGQEHG // ID H5YQQ6_9BRAD Unreviewed; 202 AA. AC H5YQQ6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 22-JAN-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=Bra471DRAFT_05975; OS Bradyrhizobium sp. WSM471. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=319017; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WSM471; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., RA Rui T., Howieson J., Reeve W., Woyke T.; RT "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001442; EHR05162.1; -; Genomic_DNA. DR EnsemblBacteria; EHR05162; EHR05162; Bra471DRAFT_05975. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 202 AA; 21804 MW; BEEE3DA58EBFEDF6 CRC64; MPYPDRFYPV VDSLAWVERL TKLGVGTIQL RAKDLDDSQS LQMVTDALAI TAGTQAKLVV NDYWRAAIVA GAKYLHLGQE DLADADLAAI REAGLSLGVS THDDAELDTA LAAEPDYVAL GPIFFTTLKS MRFEPQGIPK ITEWKKRIGN IPLVAIGGIK FEHAAEIFAA GADSIAVVSD ITQNADPDAR VRQWLGQAKE AA // ID H6CB87_EXODN Unreviewed; 533 AA. AC H6CB87; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 11. DE SubName: Full=Thiamine-phosphate dipyrophosphorylase/hydroxyethylthiazole kinase; GN ORFNames=HMPREF1120_08974; OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) OS (Black yeast) (Wangiella dermatitidis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; OC Exophiala. OX NCBI_TaxID=858893; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 34100 / CBS 525.76 / NIH/UT8656; RX PubMed=24496724; DOI=10.1534/g3.113.009241; RA Chen Z., Martinez D.A., Gujja S., Sykes S.M., Zeng Q., Szaniszlo P.J., RA Wang Z., Cuomo C.A.; RT "Comparative genomic and transcriptomic analysis of Wangiella RT dermatitidis, a major cause of phaeohyphomycosis and a model black RT yeast human pathogen."; RL G3 (Bethesda) 0:0-0(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH226137; EHY61034.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 533 AA; 55714 MW; 4A7CB8A298BBC5BF CRC64; MAQKRTTIDW SLYLVTDSTP AILGDKDIVK VVEQAIQGGV TVVQYRDKHA DTGVMVDTAS KIHSITRKYN VPLLINDRFD VCQAVGAEGV HIGQDDMECV EARRILGPDA IIGVTASSVI EAQKAIDDGA DYLGIGTTFA TPTKTDTKSI IGTRGLQEIL ASCSTGTEKS IPCVAIGSIN ASNVQRVLHQ SAHGSNRLNG VAVVSAIMAS TDPQASARSL LELIKATPAK YYAAIPPQAT LVTNLDKLVA QVPGIIQSHV SSSVLCHNMT NTVVQNFAAN VCLATGASPI MSENGVEAPD LARLGGALVI NMGTATPAKM EAFTAGMRAY NAVGASVLFD PVGGGATASR RNAVKTLLAA GFFSVIKGNE REIGAVAGTS TTQQRGVDSG PSASTAEEKA NLVKDIALRE HCIVLMTGKT DYLSDGVRTV AINNGSRWLG NITGSGCALG SIIASYVAVH PQDKFLAALA GILHYEIAAE RAEARQDCKG PGSFIPAFLD ELYLLGEDIK EGTGIGGHGE FARHVRVEML TSA // ID H6CJY2_9BACL Unreviewed; 200 AA. AC H6CJY2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Regulatory protein tenI; GN ORFNames=WG8_2650; OS Paenibacillus sp. Aloe-11. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1050222; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Aloe-11; RA Peng Y., Li N., Xia T., Xu Y., Du H., He D., Long Q., Xiang H.; RT "Genome Sequence of the Endophytic Bacteria Paenibacillus sp. Aloe- RT 11."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH601055; EHS57281.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 200 AA; 21505 MW; E93AB7FC49549A51 CRC64; MITMESGYHA DVPQVAAAIY PYVHYVHARL KQKGASELLA LIRSMVEQGV PLQQIAVNDR VDVALLTLAG AVQLPANGLP VRDVKSLLPK GTRCGVSVHS LEEAQMAEQA GADYVLYGHV YVTRCKPGVV PRGIAQLERI CSLSNIPVIA LGGIQPHHIP ELYHAGASGI AVMSGIWEAE SPIAAAMEYR QLVDQVVRNL // ID H6CN44_9BACL Unreviewed; 103 AA. AC H6CN44; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN ORFNames=WG8_3783; OS Paenibacillus sp. Aloe-11. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1050222; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Aloe-11; RA Peng Y., Li N., Xia T., Xu Y., Du H., He D., Long Q., Xiang H.; RT "Genome Sequence of the Endophytic Bacteria Paenibacillus sp. Aloe- RT 11."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH601059; EHS56162.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; FT NON_TER 103 103 SQ SEQUENCE 103 AA; 11302 MW; 53E624F468FA3146 CRC64; MSSRMLPETV RRHLQMYLVL GSVNCLAEPG WVVQEALAGG ATMVQFREKG RGALTGAPRL ELARRLQDQC RRVGVPFIVN DDVELALELD ADGVHIGQDD ESA // ID H6CN45_9BACL Unreviewed; 119 AA. AC H6CN45; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN ORFNames=WG8_3783; OS Paenibacillus sp. Aloe-11. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1050222; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Aloe-11; RA Peng Y., Li N., Xia T., Xu Y., Du H., He D., Long Q., Xiang H.; RT "Genome Sequence of the Endophytic Bacteria Paenibacillus sp. Aloe- RT 11."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH601059; EHS56163.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; FT NON_TER 1 1 SQ SEQUENCE 119 AA; 12450 MW; 4B4301658B835F5A CRC64; GNRMLGVSAH TIEEARRAIL QGADYLGVGP IYPTISKDDA NAVQGPVILH ELRKAGMDVP IVGIGGITVD RVEEVVRAGA DGVAVISAVT QAEQIRTAVE ELKKKVALSI KSPGVSQKL // ID H6CN47_9BACL Unreviewed; 59 AA. AC H6CN47; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=WG8_3786; OS Paenibacillus sp. Aloe-11. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1050222; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Aloe-11; RA Peng Y., Li N., Xia T., Xu Y., Du H., He D., Long Q., Xiang H.; RT "Genome Sequence of the Endophytic Bacteria Paenibacillus sp. Aloe- RT 11."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH601059; EHS56165.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 59 AA; 6214 MW; B5B3C7DE73EC9EDA CRC64; MRKVGIHVPI VGIGGITKDR VEEVVHAGAD GVAVISAVTR AERIRAAAEE LKKKVVLSL // ID H6L7W6_SAPGL Unreviewed; 218 AA. AC H6L7W6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-APR-2014, entry version 14. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=SGRA_1452; OS Saprospira grandis (strain Lewin). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Saprospiraceae; Saprospira. OX NCBI_TaxID=984262; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lewin; RX PubMed=22675601; DOI=10.4056/sigs.2445005; RA Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.; RT "Complete genome sequencing and analysis of Saprospira grandis str. RT Lewin, a predatory marine bacterium."; RL Stand. Genomic Sci. 6:84-93(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002831; AFC24187.1; -; Genomic_DNA. DR RefSeq; YP_005321771.1; NC_016940.1. DR EnsemblBacteria; AFC24187; AFC24187; SGRA_1452. DR GeneID; 11922085; -. DR KEGG; sgn:SGRA_1452; -. DR KO; K00788; -. DR BioCyc; SGRA984262:GLJW-1460-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 218 AA; 24156 MW; 0DA764DF7E181682 CRC64; MGPLAFEIAK MKIRLLTHPE LLTDEIQLIN ALFAEGLACL NLRKPNFTAQ QYEDFLAQID AQYHPKIILH DHYELCDKYK VQGIHLGEAR RRSYKPAELL ALRQKLQKAG LALGSSVHER ATLDELAPKH FDYIFVSPVF SSISKQGYGP KEDWTISGYK AQYDFNIVGL GGIDLDSLGA AAEKGFEEVG ALGSVWLKGE AAPAYFAKML AACQALLS // ID H6L7W8_SAPGL Unreviewed; 218 AA. AC H6L7W8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-APR-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SGRA_1454; OS Saprospira grandis (strain Lewin). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Saprospiraceae; Saprospira. OX NCBI_TaxID=984262; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lewin; RX PubMed=22675601; DOI=10.4056/sigs.2445005; RA Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.; RT "Complete genome sequencing and analysis of Saprospira grandis str. RT Lewin, a predatory marine bacterium."; RL Stand. Genomic Sci. 6:84-93(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002831; AFC24189.1; -; Genomic_DNA. DR RefSeq; YP_005321773.1; NC_016940.1. DR EnsemblBacteria; AFC24189; AFC24189; SGRA_1454. DR GeneID; 11922087; -. DR KEGG; sgn:SGRA_1454; -. DR KO; K00788; -. DR BioCyc; SGRA984262:GLJW-1462-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23908 MW; B0CBD099A161A844 CRC64; MSKKEIAALQ YVSSGQRIQE HLDQIADFLA AGGRWVQLRL KEVSTADYLA AGKTARALCD QYQAQLIIND QIEVAQAVAA DGLHLGRSDM PLEEARAILG PDFILGGTAN SWEDIREVYL AGADYIGLGP FRFTPTKKKL SPILGMKGYR ERLQQLERKG WEIPVVGIGG IKLADIEGLL RTGLHGVALS GLINQTTDKK TLVKEIYQLL EMAPSGYK // ID H6LEF3_ACEWD Unreviewed; 206 AA. AC H6LEF3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase ThiE1; DE EC=2.5.1.3; GN Name=thiE1; OrderedLocusNames=Awo_c00530; OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC OS 1655). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Acetobacterium. OX NCBI_TaxID=931626; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655; RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J., RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.; RT "Complte genome sequence of Acetobacterium woodii."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002987; AFA46867.1; -; Genomic_DNA. DR RefSeq; YP_005267756.1; NC_016894.1. DR EnsemblBacteria; AFA46867; AFA46867; Awo_c00530. DR GeneID; 11870718; -. DR KEGG; awo:Awo_c00530; -. DR KO; K00788; -. DR OMA; ASHIFAT; -. DR BioCyc; AWOO931626:GI4Q-53-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 206 AA; 23142 MW; 5BB41BC0AB48B54C CRC64; MLICITNRKL CQDDFLNRID QLAQGKPAAI MLREKDLERA AFQDLAIKVK EICDQHQVSL IINQNLEIAK QLKVGNIQLS IEKLRENKEF IREFEQVGVS VHSVDQAKEA EAAGADYLIA GHVFPTECKK GLPARGLRFL KEVCDAVKIP VWGIGGIDQN NYKVTLMTGA KGVCVMSEAM TCRDPAGFSQ RFTVGKEQTR MEENRY // ID H6LID8_ACEWD Unreviewed; 212 AA. AC H6LID8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; OrderedLocusNames=Awo_c05130; OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC OS 1655). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Acetobacterium. OX NCBI_TaxID=931626; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655; RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J., RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.; RT "Complte genome sequence of Acetobacterium woodii."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002987; AFA47312.1; -; Genomic_DNA. DR RefSeq; YP_005268201.1; NC_016894.1. DR EnsemblBacteria; AFA47312; AFA47312; Awo_c05130. DR GeneID; 11871067; -. DR KEGG; awo:Awo_c05130; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; AWOO931626:GI4Q-512-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22789 MW; 240502810ECCC27B CRC64; MKLDKQAMLL YAVTDRSWLG TRTLVEQVEE TLKGGATFIQ LREKDLDFLD FVDEAKEIKK LTDTYQIPFV INDNVEVALA VDADGVHVGQ DDLDAGELRK RLGDKIIGVS ADTVALALKA EADGADYIGV GAIYSTATKT DAEVVDFETI AAICKSVTIP VVAIGGLNEN NILSLRGTGV DGVALVSAIF SKTDIVKATQ VLRRLSEDMV KA // ID H6LM56_STAAU Unreviewed; 213 AA. AC H6LM56; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAVC_09335; OS Staphylococcus aureus subsp. aureus VC40. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1028799; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VC40; RX PubMed=22461548; DOI=10.1128/JB.06631-11; RA Sass P., Berscheid A., Jansen A., Oedenkoven M., Szekat C., RA Strittmatter A., Gottschalk G., Bierbaum G.; RT "Genome Sequence of Staphylococcus aureus VC40, a Vancomycin- and RT Daptomycin-Resistant Strain, To Study the Genetics of Development of RT Resistance to Currently Applied Last-Resort Antibiotics."; RL J. Bacteriol. 194:2107-2108(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003033; AEZ38020.1; -; Genomic_DNA. DR RefSeq; YP_005291454.1; NC_016912.1. DR ProteinModelPortal; H6LM56; -. DR SMR; H6LM56; 4-209. DR PRIDE; H6LM56; -. DR EnsemblBacteria; AEZ38020; AEZ38020; SAVC_09335. DR GeneID; 11870050; -. DR KEGG; suv:SAVC_09335; -. DR KO; K00788; -. DR BioCyc; SAUR1028799:GH9Q-1921-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID H6MI50_ECOLX Unreviewed; 211 AA. AC H6MI50; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECO55CA74_23025; OS Escherichia coli O55:H7 str. RM12579. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1048689; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RM12579; RX PubMed=22328665; DOI=10.1128/JB.00120-12; RA Kyle J.L., Cummings C.A., Parker C.T., Quinones B., Vatta P., RA Newton E., Huynh S., Swimley M., Degoricija L., Barker M., RA Fontanoz S., Nguyen K., Patel R., Fang R., Tebbs R., Petrauskene O., RA Furtado M., Mandrell R.E.; RT "Escherichia coli Serotype O55:H7 Diversity Supports Parallel RT Acquisition of Bacteriophage at Shiga Toxin Phage Insertion Sites RT during Evolution of the O157:H7 Lineage."; RL J. Bacteriol. 194:1885-1896(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003109; AEZ43144.1; -; Genomic_DNA. DR RefSeq; YP_006161699.1; NC_017656.1. DR ProteinModelPortal; H6MI50; -. DR SMR; H6MI50; 10-209. DR EnsemblBacteria; AEZ43144; AEZ43144; ECO55CA74_23025. DR GeneID; 12662152; -. DR KEGG; elr:ECO55CA74_23025; -. DR KO; K00788; -. DR BioCyc; ECOL1048689:GLD6-4621-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H6MW20_GORPV Unreviewed; 177 AA. AC H6MW20; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-APR-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GPOL_c06460; OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1112204; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44266 / VH2; RX PubMed=22327575; DOI=10.1128/AEM.07969-11; RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., RA Angelov A., Liebl W., Daniel R., Steinbuchel A.; RT "Involvement of Two Latex-Clearing Proteins during Rubber Degradation RT and Insights into the Subsequent Degradation Pathway Revealed by the RT Genome Sequence of Gordonia polyisoprenivorans Strain VH2."; RL Appl. Environ. Microbiol. 78:2874-2887(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003119; AFA71715.1; -; Genomic_DNA. DR RefSeq; YP_005281081.1; NC_016906.1. DR EnsemblBacteria; AFA71715; AFA71715; GPOL_c06460. DR GeneID; 11780657; -. DR KEGG; gpo:GPOL_c06460; -. DR KO; K00788; -. DR BioCyc; GPOL1112204:GJWY-645-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 177 AA; 18257 MW; B7F7636D5E767285 CRC64; MRDKGSPGER EFGALEAGEE LAMLAEMRGV VDAHGALLSV NDRADIALLA GADVLHLGQG DLRPEQARRI VGDDVIVGVS THDPDQAHAA IADDAVDYFC VGPCWPTPTK PGRAAPGLGL VREVAGVSKP WFAIGGIDSA RLPEVRDAGA RRAVVVRAIT AADDPAAAAA QLRAGLA // ID H6NR15_9BACL Unreviewed; 214 AA. AC H6NR15; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PM3016_5303; OS Paenibacillus mucilaginosus 3016. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1116391; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3016; RX PubMed=22535950; DOI=10.1128/JB.00323-12; RA Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X., RA Shen D., Du B., Li J.; RT "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a RT Bacterium Functional as Microbial Fertilizer."; RL J. Bacteriol. 194:2777-2778(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003235; AFC32008.1; -; Genomic_DNA. DR RefSeq; YP_005315157.1; NC_016935.1. DR ProteinModelPortal; H6NR15; -. DR EnsemblBacteria; AFC32008; AFC32008; PM3016_5303. DR GeneID; 11887293; -. DR KEGG; pmq:PM3016_5303; -. DR KO; K00788; -. DR BioCyc; PMUC1116391:GLI5-5330-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22495 MW; 5CD2F1779A30FAC0 CRC64; MYRSSLHDTL SVYLVTDTAG YEHRSAAEIV RAAVAGGVTL VQLRDKQAQL RDVLPAGREI RELCRSAGIP FVVNDRADLA LLLEADGVHV GQDDLPAQEA RRLLGPDAII GVSAGTMEEA EWAVAQGADY LGVGPVYATA SKKDAGEAIG TDLIARIRSR WPQLPLVGIG GIHQGNAAPV LASGAQGVAV ISAITRQSDP QSAARGLADV CRRR // ID H6P6K7_SALTI Unreviewed; 211 AA. AC H6P6K7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=STBHUCCB_36470; OS Salmonella enterica subsp. enterica serovar Typhi str. P-stx-12. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1132507; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P-stx-12; RX PubMed=22461552; DOI=10.1128/JB.00121-12; RA Ong S.Y., Pratap C.B., Wan X., Hou S., Abdul Rahman A.Y., Saito J.A., RA Nath G., Alam M.; RT "Complete Genome Sequence of Salmonella enterica subsp. enterica RT Serovar Typhi P-stx-12."; RL J. Bacteriol. 194:2115-2116(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003278; AEZ47267.1; -; Genomic_DNA. DR RefSeq; YP_005219120.1; NC_016832.1. DR ProteinModelPortal; H6P6K7; -. DR EnsemblBacteria; AEZ47267; AEZ47267; STBHUCCB_36470. DR OMA; AVRPSYI; -. DR BioCyc; SENT1132507:GKDO-3646-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22839 MW; B535027E2F10C309 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR CYDARLFIND YWRLAIKHNA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLAIAGVGD E // ID H6PBI9_STRIC Unreviewed; 203 AA. AC H6PBI9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-APR-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sinf_1011; OS Streptococcus infantarius (strain CJ18). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1069533; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CJ18; RX PubMed=22461547; DOI=10.1128/JB.00160-12; RA Jans C., Follador R., Lacroix C., Meile L., Stevens M.J.; RT "Complete Genome Sequence of the African Dairy Isolate Streptococcus RT infantarius subsp. infantarius Strain CJ18."; RL J. Bacteriol. 194:2105-2106(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003295; AEZ62341.1; -; Genomic_DNA. DR RefSeq; YP_005203812.1; NC_016826.1. DR EnsemblBacteria; AEZ62341; AEZ62341; Sinf_1011. DR GeneID; 11877538; -. DR KEGG; sif:Sinf_1011; -. DR KO; K00788; -. DR BioCyc; SINF1069533:GLL3-1088-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21984 MW; DFE3A71BBAA13671 CRC64; MNKEQLQVYF ICGTPNCPKG KFLDILEAAF KSGVTCFQFR EKGQGALSGQ EKKELALNVK SLCRKYHVLF FINDDIDLAL EIGVDGVHLG QDDMPVREAR KLFPDKLIGL SVGNAKEYHL SAIDVVDYIG VGPIFPTSSK SDAGQVIGLN GLREMRELDK DIPIVAIGGI TFGDVAAIRQ SGADGVAIIS AIAQSKEVEL DTQ // ID H6Q4N1_WIGGL Unreviewed; 212 AA. AC H6Q4N1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=WIGMOR_0249; OS Wigglesworthia glossinidia endosymbiont of Glossina morsitans OS morsitans (Yale colony). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Wigglesworthia. OX NCBI_TaxID=1142511; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=22334516; RA Rio R.V., Symula R.E., Wang J., Lohs C., Wu Y.N., Snyder A.K., RA Bjornson R.D., Oshima K., Biehl B.S., Perna N.T., Hattori M., RA Aksoy S.; RT "Insight into the transmission biology and species-specific functional RT capabilities of tsetse (Diptera: glossinidae) obligate symbiont RT wigglesworthia."; RL MBio 3:E00240-11(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003315; AFA41091.1; -; Genomic_DNA. DR RefSeq; YP_005267314.1; NC_016893.1. DR EnsemblBacteria; AFA41091; AFA41091; WIGMOR_0249. DR GeneID; 11874249; -. DR KEGG; wgl:WIGMOR_0249; -. DR KO; K00788; -. DR BioCyc; WGLO1142511:GJU3-250-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 212 AA; 24366 MW; 09FE1ED414700656 CRC64; MKINQIFFPK FSKKIGLYPI VDSIEWLIKI LSTGIKIIQL RIKNMSEIKL DENIKKSVML GKKYKAYIII NDYWELAIKH QAHGIHLGQE DMQNANRKKI YDSGLYLGLS THNDIEIKHA LSWNPSYIAF GHIFHTTTKI MHSQPQGIQK LKELCKKKYN CQKVAIGGIG LKEIDEVLSC NVDGVSMISA IKNSKNWKNT ISRIQKKIRS VL // ID H6R645_NOCCG Unreviewed; 212 AA. AC H6R645; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NOCYR_5185; OS Nocardia cyriacigeorgica (strain GUH-2). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Nocardia. OX NCBI_TaxID=1127134; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GUH-2; RX PubMed=22461543; DOI=10.1128/JB.00161-12; RA Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L., RA Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S., RA Nazaret S., Neto M., Petit S., Roche D., Vallenet D., RA Rodriguez-Nava V., Richard Y., Cournoyer B., Blaha D.; RT "Genome sequence of the human- and animal-pathogenic strain Nocardia RT cyriacigeorgica GUH-2."; RL J. Bacteriol. 194:2098-2099(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO082843; CCF65935.1; -; Genomic_DNA. DR RefSeq; YP_005266565.1; NC_016887.1. DR EnsemblBacteria; CCF65935; CCF65935; NOCYR_5185. DR GeneID; 11930080; -. DR KEGG; ncy:NOCYR_5185; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; NCYR1127134:GLHX-5178-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 30 34 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22388 MW; 1FAB54C532658046 CRC64; MYLCTDARRE KGDLAKFAEA ALAGGVDIIQ LRDKGSPGEQ KFGPLEAKAE LGALAELKAA ARRHGALVAV NDRADLALAA GADVLHLGQG DLPPWYARRI LGPDVVIGRS THNRAQAGLA AIDEHIDYFC TGPVWATPTK PNRQAAGIDL VRSTAEAHPT RPWFAIGGID TQNLPEVLAA GADRVVVVRA ITEARDPEAA ARELKAALLA NV // ID H6RI86_9BACT Unreviewed; 220 AA. AC H6RI86; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=VIS_S18BMA40020; OS uncultured Flavobacteriia bacterium. OC Bacteria; Bacteroidetes; Flavobacteriia; environmental samples. OX NCBI_TaxID=212695; RN [1] RP NUCLEOTIDE SEQUENCE. RA Gomez-Pereira PR, Schuler M, Fuchs BM, Bennke C, Teeling H, RA Waldmann J, Richter M, Barbe V, Bataille E, Glockner FO, Amann R.; RT "Genomic content of uncultured Bacteroidetes from contrasting oceanic RT provinces in the North Atlantic Ocean."; RL Environ. Microbiol. 14:52-66(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RA Genoscope - CEA; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO117617; CCG00798.1; -; Genomic_DNA. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24114 MW; 4419E08E5345B86A CRC64; MSISTTSVTL KKEISSLHYI SQGVGGDAHL EHIERVLNAG CNWVQLRMKN TPYEEVLETA YKVKIRCDEY NAQLIINDNV SIVQEVGAAG VHLGQHDMST AEARKILGES KIIGGTANTL EQCIDHLKNG VDYIGVGPLR FTSTKEKLSP LLGFAGYSNL HQSYKQNQHK VPLIAIGGIT SSDFEKLKDC GVDGIAVSGL LTQPNPEEII KQVFSLWQTH // ID H6RI87_9BACT Unreviewed; 199 AA. AC H6RI87; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine-phosphate pyrophosphorylase protein 2; GN ORFNames=VIS_S18BMA40021; OS uncultured Flavobacteriia bacterium. OC Bacteria; Bacteroidetes; Flavobacteriia; environmental samples. OX NCBI_TaxID=212695; RN [1] RP NUCLEOTIDE SEQUENCE. RA Gomez-Pereira PR, Schuler M, Fuchs BM, Bennke C, Teeling H, RA Waldmann J, Richter M, Barbe V, Bataille E, Glockner FO, Amann R.; RT "Genomic content of uncultured Bacteroidetes from contrasting oceanic RT provinces in the North Atlantic Ocean."; RL Environ. Microbiol. 14:52-66(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RA Genoscope - CEA; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO117617; CCG00799.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 199 AA; 23005 MW; 694949074B8390DB CRC64; MLIVITSEAF LSAEITQIKQ MIDLGLKHVH VRKPQATLEE LRNWFQNFEP RFLATMMLHQ HHVLGEELSC KGVHFKEHER NTQDKTFKKK LMNFRSNGFQ VSTSFHKLDD LKSNAVFFDY AFLSPVFTSI SKVGYEGKQF EVHDIPENCI ALGGITSEKI EEAYPLGFCG VAVLGAIWMS KNPVNEFIKI KNQYEYIYH // ID H6RK73_BLASD Unreviewed; 200 AA. AC H6RK73; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE SubName: Full=Thiamine monophosphate synthase; GN Name=thiE; OrderedLocusNames=BLASA_0097; OS Blastococcus saxobsidens (strain DD2). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Geodermatophilaceae; Blastococcus. OX NCBI_TaxID=1146883; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD2; RA Genoscope.; RT "Complete genome sequence of Blastococcus saxobsidens strain DD2."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO117623; CCG01096.1; -; Genomic_DNA. DR RefSeq; YP_005327145.1; NC_016943.1. DR EnsemblBacteria; CCG01096; CCG01096; BLASA_0097. DR GeneID; 11915782; -. DR KEGG; bsd:BLASA_0097; -. DR KO; K00788; -. DR OMA; VMRAEDP; -. DR BioCyc; BSAX1146883:GL9E-92-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 200 AA; 20502 MW; E5DCABBD6AA9E5C1 CRC64; MNLPRLVLVT DRTQCARPLV DVVATAVAHG ARAVVLRDKD LPAAERTALV ADLRSVLQPV GGLLVHGGAR GAPLDTPVHL AAAEPFPAVR PPLVGRSCHS ATELARAARE GCDWVTLSPV FPTVSKPGYG PALGLEGLAA LVPGAPPVLA LGGIRPDHVA DCLAAGAYGV AVMGPVMRDP TLVAEYLAAD VAEQPGPHRD // ID H6RK77_BLASD Unreviewed; 208 AA. AC H6RK77; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE2; Synonyms=thiE; OrderedLocusNames=BLASA_0101; OS Blastococcus saxobsidens (strain DD2). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Geodermatophilaceae; Blastococcus. OX NCBI_TaxID=1146883; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD2; RA Genoscope.; RT "Complete genome sequence of Blastococcus saxobsidens strain DD2."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO117623; CCG01100.1; -; Genomic_DNA. DR RefSeq; YP_005327149.1; NC_016943.1. DR EnsemblBacteria; CCG01100; CCG01100; BLASA_0101. DR GeneID; 11915786; -. DR KEGG; bsd:BLASA_0101; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR BioCyc; BSAX1146883:GL9E-96-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 20010 MW; EA8DEAC9AB139893 CRC64; MSRALGGLHV LTDAAGGPRA LAAVAAAVSA GAPVVQVRAK DCTDRVLVEF AGQVVDICAP TGVTCLVNDR VDVALAVGAH GTHLGATDLP VAAARRVAGP GHLLGGTARD PETARRLVAE GADYLGVGPA WPTTTKTGLP DALGPAGVAA VAAAVDVPVI AIGGVTAERV AALLAAGAAG VAVVGAVTGA PDPTAATREL LRALAGAP // ID H6S6Y1_MYCTX Unreviewed; 222 AA. AC H6S6Y1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-MAY-2014, entry version 18. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=UDA_0414c; OS Mycobacterium tuberculosis UT205. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1097669; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UT205; RA Alzate J.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UT205; RX PubMed=22404577; DOI=10.1111/j.1574-6968.2012.02540.x; RA Isaza J.P., Duque C., Gomez V., Robledo J., Barrera L.F., Alzate J.F.; RT "Whole genome shotgun sequencing of one Colombian clinical isolate of RT Mycobacterium tuberculosis reveals DosR regulon gene deletions."; RL FEMS Microbiol. Lett. 330:113-120(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE608151; CCE35952.1; -; Genomic_DNA. DR RefSeq; YP_005306759.1; NC_016934.1. DR ProteinModelPortal; H6S6Y1; -. DR SMR; H6S6Y1; 1-221. DR EnsemblBacteria; CCE35952; CCE35952; UDA_0414c. DR GeneID; 13111247; -. DR KEGG; mtd:UDA_0414c; -. DR KO; K00788; -. DR OMA; YEVINRS; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID H6SN36_RHOPH Unreviewed; 239 AA. AC H6SN36; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=RSPPHO_00286; OS Rhodospirillum photometricum DSM 122. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=1150469; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 122; RA Duquesne K., Sturgis J.; RT "Shotgun genome sequence of Phaeospirillum photometricum DSM 122."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE663493; CCG06912.1; -; Genomic_DNA. DR RefSeq; YP_005415882.1; NC_017059.1. DR EnsemblBacteria; CCG06912; CCG06912; RSPPHO_00286. DR GeneID; 12210986; -. DR KEGG; rpm:RSPPHO_00286; -. DR KO; K00788; -. DR BioCyc; RPHO1150469:GLJ6-358-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 239 AA; 25281 MW; E2F6668CD2A50DF9 CRC64; MTASLSCRAE RVHRRAGRPK APAAVLVTDE RRLPDPRPVL PALPRGARVV LRAYGDPTRA GAVVAAARRR RIGVILALAA PRLPPLPRDL AGIHLPQGRA CRGLMAGVLL WRRAAAGRSL SMAAHDGRAL ARARALRLTF VLLSPVFPTR SHPGAPALGP LRATLLARTS QVPVLALGGI TPTTAARLPP RPWSGLAALE SWTKNRGVRG GPASPPSLPL PFPLPLPPEE NMEKLDSPG // ID H6SNI1_RHOPH Unreviewed; 256 AA. AC H6SNI1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RSPPHO_02686; OS Rhodospirillum photometricum DSM 122. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=1150469; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 122; RA Duquesne K., Sturgis J.; RT "Shotgun genome sequence of Phaeospirillum photometricum DSM 122."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE663493; CCG09312.1; -; Genomic_DNA. DR RefSeq; YP_005418282.1; NC_017059.1. DR EnsemblBacteria; CCG09312; CCG09312; RSPPHO_02686. DR GeneID; 12212132; -. DR KEGG; rpm:RSPPHO_02686; -. DR KO; K00788; -. DR BioCyc; RPHO1150469:GLJ6-2817-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 75 79 HMP-PP binding (By similarity). FT REGION 173 175 THZ-P binding (By similarity). FT METAL 108 108 Magnesium (By similarity). FT METAL 127 127 Magnesium (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 176 176 HMP-PP (By similarity). FT BINDING 203 203 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 256 AA; 27774 MW; 4957E8A1D7895F7A CRC64; MARRHRSPGN RGSCLADGLG LTHPDRVVPF VKDPTVTDDD ACRLYLITPP RLDDLRAFAE RLARTLDAGD VPCVQLRLKE ADDTAIRRAV EALRPVCHAR EVALILNDRP DLAKDTGCDG VHVGQKDMPY AKARKVVGDN AIVGVTCHDS RHLGMEAGEA GADYVAFGAF YPTATKEAPT QADTDLLRWW SEMMVVPSVA IGGITPENAR PLIEAGADFL AVCSGVWEHP EGPEAAVRAF DALFREVSPL DLPDEK // ID H7CIG2_LISMN Unreviewed; 214 AA. AC H7CIG2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMIV_0101; OS Listeria monocytogenes FSL J1-208. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393119; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL J1-208; RX PubMed=22247147; DOI=10.1128/AEM.06969-11; RA den Bakker H.C., Bowen B.M., Rodriguez-Rivera L.D., Wiedmann M.; RT "FSL J1-208, a Virulent Uncommon Phylogenetic Lineage IV Listeria RT monocytogenes Strain with a Small Chromosome Size and a Putative RT Virulence Plasmid Carrying Internalin-Like Genes."; RL Appl. Environ. Microbiol. 78:1876-1889(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEIS01000001; EHY64063.1; -; Genomic_DNA. DR EnsemblBacteria; EHY64063; EHY64063; LMIV_0101. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22495 MW; BBC0499335B06401 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAI EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAA EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRT GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC HSVIKQLKNP GSPS // ID H7CW16_CLOPF Unreviewed; 207 AA. AC H7CW16; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HA1_08227; OS Clostridium perfringens F262. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=883064; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F262; RX PubMed=22412860; DOI=10.1371/journal.pone.0032271; RA Nowell V.J., Kropinski A.M., Songer J.G., Macinnes J.I., RA Parreira V.R., Prescott J.F.; RT "Genome Sequencing and Analysis of a Type A Clostridium perfringens RT Isolate from a Case of Bovine Clostridial Abomasitis."; RL PLoS ONE 7:E32271-E32271(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFES01000022; EIA17110.1; -; Genomic_DNA. DR EnsemblBacteria; EIA17110; EIA17110; HA1_08227. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22957 MW; B4A41E9BC9BCFD54 CRC64; MSNKDYKKLY LVTDYRISFN ELLEKTKEAL IGGVSIVQYR AKNKKTKEMC KEAKELKKLC DEFGALFLVN DRIDVALAVK ANGVHIGQDD MEVSIAREIM PKDAVIGVTV HNKEEALKAM KEGADNLGVG ALFSTNSKDD ATLMTLETLR EIKSVSNIPL YGIGGITPYN LNKDILENLE GVAVISSLLN SDNIREKSKE FLNILSK // ID H7CWX9_CLOPF Unreviewed; 193 AA. AC H7CWX9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 22-JAN-2014, entry version 13. DE SubName: Full=Thiamine monophosphate synthase family protein; GN ORFNames=HA1_09806; OS Clostridium perfringens F262. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=883064; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F262; RX PubMed=22412860; DOI=10.1371/journal.pone.0032271; RA Nowell V.J., Kropinski A.M., Songer J.G., Macinnes J.I., RA Parreira V.R., Prescott J.F.; RT "Genome Sequencing and Analysis of a Type A Clostridium perfringens RT Isolate from a Case of Bovine Clostridial Abomasitis."; RL PLoS ONE 7:E32271-E32271(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFES01000025; EIA16880.1; -; Genomic_DNA. DR EnsemblBacteria; EIA16880; EIA16880; HA1_09806. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 193 AA; 21943 MW; 86DBCA6E7AE5E34E CRC64; MFLITNRKLV NREKYFNTIK EAGKYGVKNI ILREKDLSTE ELIEVYIKIR DLVPEETNII INSNIEAARI LKEKFIHLSF KDFKRNLEEV KSLQVGVSVH SILEALEADR LGASYILVSP IFETQCKKDV TPKGINFIKE IKEKVNCKVI ALGGINELNF KEVLGAGADD FACMSLLFMS NNIKKSLDTF KAL // ID H7EFC5_SALHO Unreviewed; 211 AA. AC H7EFC5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEHO0A_04252; OS Salmonella enterica subsp. houtenae str. ATCC BAA-1581. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=523831; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1581; RA McClelland M., Clifton S., Porwollik S., Cheng P., Wollam A., RA Rotter K., Pepin K., Bhonagiri V., Fulton R., Fulton L.F., RA Delehaunty K., Fronick C., O'Laughlin M., Godfrey J., Waligorski J., RA Appelbaum E., Farmer C., Strong C., Tomlinson C., Hou S., Minx P., RA Warren W., Wilson R.K.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGRM01000005; EHY67136.1; -; Genomic_DNA. DR EnsemblBacteria; EHY67136; EHY67136; SEHO0A_04252. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23046 MW; 2B0ED2AEFD0B6C81 CRC64; MYQPDFPPVP FRLGLYPVVD SVTWVERLLA TGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHNA YGVHLGQEDL ETTDLNAIRA AGLRLGVSTH DDMEIDIALA ARPSYIALGH VFPTQTKQMP SAPQGLEPLA WHIERLADYP TVAIGGISLD RAHSVLATGV GSIAVVSAIT QAADWRAATQ QLLAIAGAGD E // ID H7ELN5_9SPIO Unreviewed; 237 AA. AC H7ELN5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TresaDRAFT_1185; OS Treponema saccharophilum DSM 2985. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=907348; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2985; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Kyrpides N., RA Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E., Klenk H.-P., RA Eisen J.A.; RT "The draft genome of Treponema saccharophilum DSM 2985."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGRW01000049; EIC01576.1; -; Genomic_DNA. DR EnsemblBacteria; EIC01576; EIC01576; TresaDRAFT_1185. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT REGION 210 211 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 190 190 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 237 AA; 24796 MW; 428E098B8AD03F4C CRC64; MGKNRVDVSA YLVVGPENTL GRPVRDVVSD AVRAGFTAVQ IRSKTASARE LIGICRESAI AIGQLGKSDS VSLLVDDRLD IVLAAREEGI KVDGIHVGQK DIPVSVCRKY LGEDAVVGLS ARTFDLLEYA RGLSADEYGM IDYFGAGPLH KTQSKADAGL DLSGNFHTRN MGELSELARI SRVPVVVGGG VTVDDIPALR STGVAGFFVI SAVAGAENPF SAASALVSAW RACGCSS // ID H7EMD5_9SPIO Unreviewed; 188 AA. AC H7EMD5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=TresaDRAFT_0357; OS Treponema saccharophilum DSM 2985. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=907348; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2985; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Kyrpides N., RA Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E., Klenk H.-P., RA Eisen J.A.; RT "The draft genome of Treponema saccharophilum DSM 2985."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGRW01000051; EIC01220.1; -; Genomic_DNA. DR EnsemblBacteria; EIC01220; EIC01220; TresaDRAFT_0357. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 188 AA; 20058 MW; 02726388D3ED07DB CRC64; MNFGGNTIVV TNRNLCGTDF LARIREICMG DAIAIILREK DLPEDDYARL ARSVNGICGI YGKKFIAHNF PDAARSLGIK SIHLPLPVFL SATENRRLDF FDEIGTSVHS VEDAVAAEKA GASYITAGHI FDTDCKKGIP GRGLPFLRDV CAAVRIPVYA IGGIKPQNIG SVIECGAAGG CVMSLAMS // ID H7EZB8_PSEST Unreviewed; 313 AA. AC H7EZB8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=PstZobell_16853; OS Pseudomonas stutzeri ATCC 14405 = CCUG 16156. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=32042; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 16156; RX PubMed=22328767; DOI=10.1128/JB.06648-11; RA Pena A., Busquets A., Gomila M., Bosch R., Nogales B., RA Garcia-Valdes E., Lalucat J., Bennasar A.; RT "Draft Genome of Pseudomonas stutzeri Strain ZoBell (CCUG 16156), a RT Marine Isolate and Model Organism for Denitrification Studies."; RL J. Bacteriol. 194:1277-1278(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSL01000101; EHY79092.1; -; Genomic_DNA. DR ProteinModelPortal; H7EZB8; -. DR EnsemblBacteria; EHY79092; EHY79092; PstZobell_16853. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 313 AA; 33673 MW; A454DDD2F36DEC64 CRC64; MKRIHVAAAV IRGADARVLI AKRPLDKHQG GLWEFPGGKV EADERVEAAL ARELLEELGI VVTAAQPLIQ VRHDYPDKQV LLDVWEVQAF TGEPHGAEGQ PLMWVTADQL TNYSFPAANQ PIVAAARLPH RYLITPDGIA PQRLLEGLAR ALDDGIRLIQ LRVPSLPPAA YRALAERALA LCEGQAQLML KGPLQWACDY PGAGWHLTAG QLREQAGRER PIAASRWLAA SCHDAEELAL AAVLGVDFVT LSPVLATASH PDASPLGWPQ VADLLLGFDR PAYLLGGLQA SDLSAARQAG AQGVAAIRAF WPD // ID H7F016_PSEST Unreviewed; 213 AA. AC H7F016; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PstZobell_18135; OS Pseudomonas stutzeri ATCC 14405 = CCUG 16156. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=32042; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 16156; RX PubMed=22328767; DOI=10.1128/JB.06648-11; RA Pena A., Busquets A., Gomila M., Bosch R., Nogales B., RA Garcia-Valdes E., Lalucat J., Bennasar A.; RT "Draft Genome of Pseudomonas stutzeri Strain ZoBell (CCUG 16156), a RT Marine Isolate and Model Organism for Denitrification Studies."; RL J. Bacteriol. 194:1277-1278(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSL01000112; EHY79340.1; -; Genomic_DNA. DR EnsemblBacteria; EHY79340; EHY79340; PstZobell_18135. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22768 MW; 8C41DBB19D3C3E83 CRC64; MKESTRLRGL YAITDSKLLA EGRLLPYVEA ALKGGARLLQ YRDKSSDEAR RLREADALRE LCAQYGAQLI INDDAELAAR LGVGLHLGQE DGSLSAARAL LGRQAIIGAT CHAQLTLAEQ AAREGASYVA FGRFFQSQTK PGAPSADREL LREARARVGL PIAGIGGITL DTAPSLIADG VQMIAVVHAL FAAENAAEVE RRARAFSQLF LTP // ID H7FEJ5_STASA Unreviewed; 195 AA. AC H7FEJ5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Uncharacterized protein; GN ORFNames=SSME_00650; OS Staphylococcus saprophyticus subsp. saprophyticus KACC 16562. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1131257; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KACC 16562; RX PubMed=22843581; DOI=10.1128/JB.00848-12; RA Kim B.S., Kim C.T., Park B.H., Kwon S., Cho Y.J., Kim N., Kim C.J., RA Chun J., Kwak J., Maeng J.S.; RT "Draft Genome Sequence of Staphylococcus saprophyticus subsp. RT saprophyticus M1-1, Isolated from the Gills of a Korean Rockfish, RT Sebastes schlegeli Hilgendorf, after High Hydrostatic Pressure RT Processing."; RL J. Bacteriol. 194:4441-4442(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KACC 16562; RA Maeng J.-S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKB01000003; EHY93764.1; -; Genomic_DNA. DR EnsemblBacteria; EHY93764; EHY93764; SSME_00650. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 195 AA; 22757 MW; 324EDC8067D936BF CRC64; MFIAITEFEN LDSDDIQHYT TIASVIDYLM IRTPMSQQQL INWINRLIQA GFPKNKIIIH SHITVLEQCY LSAIHFREAD ARIKDFKKSH PHIQISMSTH HEESVKQAQA LNLDFILFSH IFRTNSKPNQ PPRTQSEINK VLQYPMPNVA LGGVNEQTLN DLPKGFDGIA GITLFRRKNR ETMELLRERW NEYQI // ID H7FGL9_STASA Unreviewed; 212 AA. AC H7FGL9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SSME_07870; OS Staphylococcus saprophyticus subsp. saprophyticus KACC 16562. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1131257; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KACC 16562; RX PubMed=22843581; DOI=10.1128/JB.00848-12; RA Kim B.S., Kim C.T., Park B.H., Kwon S., Cho Y.J., Kim N., Kim C.J., RA Chun J., Kwak J., Maeng J.S.; RT "Draft Genome Sequence of Staphylococcus saprophyticus subsp. RT saprophyticus M1-1, Isolated from the Gills of a Korean Rockfish, RT Sebastes schlegeli Hilgendorf, after High Hydrostatic Pressure RT Processing."; RL J. Bacteriol. 194:4441-4442(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KACC 16562; RA Maeng J.-S.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKB01000013; EHY93112.1; -; Genomic_DNA. DR EnsemblBacteria; EHY93112; EHY93112; SSME_07870. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23162 MW; F66DAF3A9404A3B8 CRC64; MFDKNNLKLY FICGTQDIES KTTIIDVVTE ALESGITMFQ FREKGNGALI GDEKEDLARK LLALCHDYAV PFIVNDDVAL ANKIGADGIH VGQDDMDVKV FAEQFKGKII GLSISNIDEY KTSNLAHVDY IGVGPMYATT SKDDANLPVG PEMITKLRAH VNHFPIVAIG GINVENTREV MQAGADGISI ISAITKSENI SNTVRQFLQN VE // ID H7G5E2_STAA5 Unreviewed; 229 AA. AC H7G5E2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ST398NM02_2134; OS Staphylococcus aureus subsp. aureus DR10. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1155079; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DR10; RX PubMed=22375071; RA Uhlemann A.C., Porcella S.F., Trivedi S., Sullivan S.B., Hafer C., RA Kennedy A.D., Barbian K.D., McCarthy A.J., Street C., Hirschberg D.L., RA Lipkin W.I., Lindsay J.A., DeLeo F.R., Lowy F.D.; RT "Identification of a highly transmissible animal-independent RT Staphylococcus aureus ST398 clone with distinct genomic and cell RT adhesion properties."; RL MBio 3:e00027-12(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DR10; RA Uhlemann A.-C., Porcella S.F., Trivedi S., Sullivan S.B., Hafer C., RA Kennedy A.D., Barbian K.D., McCarthy A.J., Street C., Hirschberg D.L., RA Lipkin W.I., Lindsay J.A., DeLeo F.R., Lowy F.D.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIDT01000006; EIA14251.1; -; Genomic_DNA. DR EnsemblBacteria; EIA14251; EIA14251; ST398NM02_2134. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 56 60 HMP-PP binding (By similarity). FT REGION 155 157 THZ-P binding (By similarity). FT REGION 207 208 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 HMP-PP (By similarity). FT BINDING 187 187 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 25199 MW; 86460FFBE17E260B CRC64; MKQPINNGFA FKRWNSMFNQ SYLNVYFICG TSDVPSHRTI HEVLEAALKA GITLFQFREK GESALKGNDK LVLAKELQHL CHQYDVPFIV NDDVSLAKEI NADGIHVGQD DAKVKEIAQY FTDKIIGLSI SDLGEYAKSD LTHVDYIGVG PIYPTPSKND AHTPVGPEMI ATFKEMNPQL PIVAIGGINT SNVAPIVEAG ANGISVISAI SKSENIEKTV NRFKDFFNN // ID H7GAM4_PROAA Unreviewed; 217 AA. AC H7GAM4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TICEST70_03986; OS Propionibacterium acnes PRP-38. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1136877; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PRP-38; RX PubMed=22628495; DOI=10.1128/JB.00479-12; RA McDowell A., Hunyadkurti J., Horvath B., Voros A., Barnard E., RA Patrick S., Nagy I.; RT "Draft Genome Sequence of an Antibiotic-Resistant Propionibacterium RT acnes Strain, PRP-38, from the Novel Type IC Cluster."; RL J. Bacteriol. 194:3260-3261(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJP01000005; EIA12040.1; -; Genomic_DNA. DR ProteinModelPortal; H7GAM4; -. DR EnsemblBacteria; EIA12040; EIA12040; TICEST70_03986. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID H7GG20_9DEIN Unreviewed; 206 AA. AC H7GG20; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RLTM_05004; OS Thermus sp. RL. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=456163; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RL; RA Lal R., Dwivedi V., Sangwan N., Lata P., Nigam A., Niharika N., RA Khurana J.P., Khurana P., Raghuvanshi S., Raman R.R.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJQ01000005; EIA39251.1; -; Genomic_DNA. DR EnsemblBacteria; EIA39251; EIA39251; RLTM_05004. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22655 MW; 77A4EBE6F24B48B2 CRC64; MQGRLYLVVT PRPHWSMGET LDRTERALGG GVEVLQLRAK DWEARPILEL GERMLALARR YGVPFFLNDR PDLAALLGAD GVHLGQGDLT PLEARRFFSG LVGRSTHAPE QALKALEEGA DYLSVGPVWE TPTKPGRKAA GLGYVRWAAE NLKEKPWFAI GGIDLENLDQ VLEAGARRIV VVRAILDAPD PEXAAXAFRE RLYGVA // ID H7GL51_STREE Unreviewed; 209 AA. AC H7GL51; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR76_0700; OS Streptococcus pneumoniae GA43264. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760817; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA43264; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA43264."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJS01000002; EHZ54348.1; -; Genomic_DNA. DR ProteinModelPortal; H7GL51; -. DR EnsemblBacteria; EHZ54348; EHZ54348; SPAR76_0700. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7GL58_STREE Unreviewed; 210 AA. AC H7GL58; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR76_0707; OS Streptococcus pneumoniae GA43264. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760817; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA43264; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA43264."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJS01000002; EHZ54216.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ54216; EHZ54216; SPAR76_0707. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22728 MW; E8F9319141D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGAGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7GSC8_STREE Unreviewed; 209 AA. AC H7GSC8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR131_0677; OS Streptococcus pneumoniae 7533-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760872; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7533-05; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 7533-05."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJT01000007; EHZ85062.1; -; Genomic_DNA. DR ProteinModelPortal; H7GSC8; -. DR EnsemblBacteria; EHZ85062; EHZ85062; SPAR131_0677. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7GSD5_STREE Unreviewed; 210 AA. AC H7GSD5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR131_0684; OS Streptococcus pneumoniae 7533-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760872; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7533-05; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 7533-05."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJT01000007; EHZ85069.1; -; Genomic_DNA. DR ProteinModelPortal; H7GSD5; -. DR EnsemblBacteria; EHZ85069; EHZ85069; SPAR131_0684. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7GYQ4_STREE Unreviewed; 209 AA. AC H7GYQ4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR130_0670; OS Streptococcus pneumoniae 5652-06. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760871; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5652-06; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 5652-06."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJU01000007; EHZ83004.1; -; Genomic_DNA. DR ProteinModelPortal; H7GYQ4; -. DR EnsemblBacteria; EHZ83004; EHZ83004; SPAR130_0670. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7GYR1_STREE Unreviewed; 210 AA. AC H7GYR1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR130_0677; OS Streptococcus pneumoniae 5652-06. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760871; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=5652-06; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 5652-06."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJU01000007; EHZ83011.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ83011; EHZ83011; SPAR130_0677. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22786 MW; B30A9754D1308511 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLVKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7H448_STREE Unreviewed; 209 AA. AC H7H448; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR25_0660; OS Streptococcus pneumoniae GA11856. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760766; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA11856; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA11856."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJV01000007; EHZ17327.1; -; Genomic_DNA. DR ProteinModelPortal; H7H448; -. DR EnsemblBacteria; EHZ17327; EHZ17327; SPAR25_0660. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7H455_STREE Unreviewed; 210 AA. AC H7H455; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR25_0667; OS Streptococcus pneumoniae GA11856. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760766; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA11856; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA11856."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJV01000007; EHZ17334.1; -; Genomic_DNA. DR ProteinModelPortal; H7H455; -. DR EnsemblBacteria; EHZ17334; EHZ17334; SPAR25_0667. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7HAG7_STREE Unreviewed; 209 AA. AC H7HAG7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR140_0663; OS Streptococcus pneumoniae EU-NP05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760881; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EU-NP05; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae EU-NP05."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJW01000002; EHZ96938.1; -; Genomic_DNA. DR ProteinModelPortal; H7HAG7; -. DR EnsemblBacteria; EHZ96938; EHZ96938; SPAR140_0663. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7HAH4_STREE Unreviewed; 210 AA. AC H7HAH4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR140_0670; OS Streptococcus pneumoniae EU-NP05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760881; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EU-NP05; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae EU-NP05."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJW01000002; EHZ96945.1; -; Genomic_DNA. DR ProteinModelPortal; H7HAH4; -. DR EnsemblBacteria; EHZ96945; EHZ96945; SPAR140_0670. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7HGS3_STREE Unreviewed; 209 AA. AC H7HGS3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR63_0737; OS Streptococcus pneumoniae GA40183. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760804; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA40183; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA40183."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJX01000004; EHZ42426.1; -; Genomic_DNA. DR ProteinModelPortal; H7HGS3; -. DR EnsemblBacteria; EHZ42426; EHZ42426; SPAR63_0737. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7HGT0_STREE Unreviewed; 210 AA. AC H7HGT0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR63_0744; OS Streptococcus pneumoniae GA40183. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760804; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA40183; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA40183."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJX01000004; EHZ42433.1; -; Genomic_DNA. DR ProteinModelPortal; H7HGT0; -. DR EnsemblBacteria; EHZ42433; EHZ42433; SPAR63_0744. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7HN17_STREE Unreviewed; 209 AA. AC H7HN17; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR126_0663; OS Streptococcus pneumoniae 8190-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760867; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=8190-05; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 8190-05."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJY01000018; EHZ81068.1; -; Genomic_DNA. DR ProteinModelPortal; H7HN17; -. DR EnsemblBacteria; EHZ81068; EHZ81068; SPAR126_0663. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7HN24_STREE Unreviewed; 210 AA. AC H7HN24; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR126_0670; OS Streptococcus pneumoniae 8190-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760867; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=8190-05; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 8190-05."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJY01000018; EHZ81075.1; -; Genomic_DNA. DR ProteinModelPortal; H7HN24; -. DR EnsemblBacteria; EHZ81075; EHZ81075; SPAR126_0670. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7HTX5_STREE Unreviewed; 209 AA. AC H7HTX5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR6_0608; OS Streptococcus pneumoniae GA13499. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760747; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13499; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13499."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJZ01000008; EHZ05304.1; -; Genomic_DNA. DR ProteinModelPortal; H7HTX5; -. DR EnsemblBacteria; EHZ05304; EHZ05304; SPAR6_0608. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7HTY2_STREE Unreviewed; 210 AA. AC H7HTY2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR6_0615; OS Streptococcus pneumoniae GA13499. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760747; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13499; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13499."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIJZ01000008; EHZ05311.1; -; Genomic_DNA. DR ProteinModelPortal; H7HTY2; -. DR EnsemblBacteria; EHZ05311; EHZ05311; SPAR6_0615. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7I0B6_STREE Unreviewed; 209 AA. AC H7I0B6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR64_0675; OS Streptococcus pneumoniae GA40410. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760805; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA40410; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA40410."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKA01000007; EHZ45430.1; -; Genomic_DNA. DR ProteinModelPortal; H7I0B6; -. DR EnsemblBacteria; EHZ45430; EHZ45430; SPAR64_0675. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7I0H1_STREE Unreviewed; 210 AA. AC H7I0H1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR64_0682; OS Streptococcus pneumoniae GA40410. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760805; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA40410; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA40410."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKA01000007; EHZ45437.1; -; Genomic_DNA. DR ProteinModelPortal; H7I0H1; -. DR EnsemblBacteria; EHZ45437; EHZ45437; SPAR64_0682. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7I7I0_STREE Unreviewed; 209 AA. AC H7I7I0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR26_0765; OS Streptococcus pneumoniae GA13224. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760767; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13224; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13224."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKB01000008; EHZ19257.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ19257; EHZ19257; SPAR26_0765. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23316 MW; 31F264436DD7A478 CRC64; MFHKELLKLY FICGTTTCQE KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7I7I8_STREE Unreviewed; 210 AA. AC H7I7I8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR26_0773; OS Streptococcus pneumoniae GA13224. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760767; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13224; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13224."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKB01000008; EHZ19265.1; -; Genomic_DNA. DR ProteinModelPortal; H7I7I8; -. DR EnsemblBacteria; EHZ19265; EHZ19265; SPAR26_0773. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7IES7_STREE Unreviewed; 209 AA. AC H7IES7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR60_0672; OS Streptococcus pneumoniae GA19923. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760801; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA19923; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA19923."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKC01000004; EHZ36981.1; -; Genomic_DNA. DR ProteinModelPortal; H7IES7; -. DR EnsemblBacteria; EHZ36981; EHZ36981; SPAR60_0672. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7IET4_STREE Unreviewed; 210 AA. AC H7IET4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR60_0679; OS Streptococcus pneumoniae GA19923. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760801; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA19923; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA19923."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKC01000004; EHZ36988.1; -; Genomic_DNA. DR ProteinModelPortal; H7IET4; -. DR EnsemblBacteria; EHZ36988; EHZ36988; SPAR60_0679. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7IKT3_STREE Unreviewed; 209 AA. AC H7IKT3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR129_0683; OS Streptococcus pneumoniae 7879-04. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760870; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7879-04; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 7879-04."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKD01000005; EHZ78704.1; -; Genomic_DNA. DR ProteinModelPortal; H7IKT3; -. DR EnsemblBacteria; EHZ78704; EHZ78704; SPAR129_0683. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7IKU1_STREE Unreviewed; 210 AA. AC H7IKU1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR129_0691; OS Streptococcus pneumoniae 7879-04. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760870; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7879-04; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 7879-04."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKD01000005; EHZ78712.1; -; Genomic_DNA. DR ProteinModelPortal; H7IKU1; -. DR EnsemblBacteria; EHZ78712; EHZ78712; SPAR129_0691. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7IQT8_STREE Unreviewed; 210 AA. AC H7IQT8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR132_1165; OS Streptococcus pneumoniae 4075-00. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760873; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4075-00; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 4075-00."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKE01000003; EHZ88776.1; -; Genomic_DNA. DR ProteinModelPortal; H7IQT8; -. DR EnsemblBacteria; EHZ88776; EHZ88776; SPAR132_1165. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7IQU5_STREE Unreviewed; 209 AA. AC H7IQU5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR132_1172; OS Streptococcus pneumoniae 4075-00. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760873; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4075-00; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae 4075-00."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKE01000003; EHZ88783.1; -; Genomic_DNA. DR ProteinModelPortal; H7IQU5; -. DR EnsemblBacteria; EHZ88783; EHZ88783; SPAR132_1172. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7IVG2_STREE Unreviewed; 209 AA. AC H7IVG2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR137_0670; OS Streptococcus pneumoniae EU-NP02. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760878; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EU-NP02; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae EU-NP02."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKF01000004; EHZ89224.1; -; Genomic_DNA. DR ProteinModelPortal; H7IVG2; -. DR EnsemblBacteria; EHZ89224; EHZ89224; SPAR137_0670. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7IVG9_STREE Unreviewed; 210 AA. AC H7IVG9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR137_0677; OS Streptococcus pneumoniae EU-NP02. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760878; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EU-NP02; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae EU-NP02."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKF01000004; EHZ89231.1; -; Genomic_DNA. DR ProteinModelPortal; H7IVG9; -. DR EnsemblBacteria; EHZ89231; EHZ89231; SPAR137_0677. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7J1Y6_STREE Unreviewed; 209 AA. AC H7J1Y6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR138_0675; OS Streptococcus pneumoniae EU-NP03. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760879; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EU-NP03; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae EU-NP03."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKG01000003; EHZ92141.1; -; Genomic_DNA. DR ProteinModelPortal; H7J1Y6; -. DR EnsemblBacteria; EHZ92141; EHZ92141; SPAR138_0675. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7J1Z3_STREE Unreviewed; 210 AA. AC H7J1Z3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR138_0682; OS Streptococcus pneumoniae EU-NP03. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760879; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EU-NP03; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae EU-NP03."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKG01000003; EHZ92006.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ92006; EHZ92006; SPAR138_0682. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22728 MW; E8F9319141D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGAGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7J8W8_STREE Unreviewed; 209 AA. AC H7J8W8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR139_0817; OS Streptococcus pneumoniae EU-NP04. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760880; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EU-NP04; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae EU-NP04."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKH01000006; EHZ94176.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ94176; EHZ94176; SPAR139_0817. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23352 MW; 24457EFDA912E780 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KYDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7J8X5_STREE Unreviewed; 210 AA. AC H7J8X5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR139_0824; OS Streptococcus pneumoniae EU-NP04. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760880; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=EU-NP04; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae EU-NP04."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKH01000006; EHZ94183.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ94183; EHZ94183; SPAR139_0824. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; 2BE4904FBC77D49C CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID H7JE94_STREE Unreviewed; 209 AA. AC H7JE94; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR1_0542; OS Streptococcus pneumoniae GA02254. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760742; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA02254; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA02254."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKI01000007; EHY97803.1; -; Genomic_DNA. DR ProteinModelPortal; H7JE94; -. DR EnsemblBacteria; EHY97803; EHY97803; SPAR1_0542. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7JEA1_STREE Unreviewed; 210 AA. AC H7JEA1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR1_0549; OS Streptococcus pneumoniae GA02254. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760742; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA02254; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA02254."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKI01000007; EHY97810.1; -; Genomic_DNA. DR EnsemblBacteria; EHY97810; EHY97810; SPAR1_0549. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22800 MW; A1CC2790D72571EC CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GLEKILGITA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID H7JK90_STREE Unreviewed; 209 AA. AC H7JK90; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR2_0743; OS Streptococcus pneumoniae GA02270. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760743; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA02270; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA02270."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKJ01000002; EHY99649.1; -; Genomic_DNA. DR ProteinModelPortal; H7JK90; -. DR EnsemblBacteria; EHY99649; EHY99649; SPAR2_0743. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7JK97_STREE Unreviewed; 210 AA. AC H7JK97; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR2_0750; OS Streptococcus pneumoniae GA02270. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760743; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA02270; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA02270."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKJ01000002; EHY99656.1; -; Genomic_DNA. DR EnsemblBacteria; EHY99656; EHY99656; SPAR2_0750. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22728 MW; E8F9319141D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGAGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7JS11_STREE Unreviewed; 209 AA. AC H7JS11; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR3_0743; OS Streptococcus pneumoniae GA02714. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760744; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA02714; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA02714."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKK01000004; EHY99946.1; -; Genomic_DNA. DR ProteinModelPortal; H7JS11; -. DR EnsemblBacteria; EHY99946; EHY99946; SPAR3_0743. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7JS18_STREE Unreviewed; 210 AA. AC H7JS18; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR3_0750; OS Streptococcus pneumoniae GA02714. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760744; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA02714; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA02714."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKK01000004; EHY99953.1; -; Genomic_DNA. DR ProteinModelPortal; H7JS18; -. DR EnsemblBacteria; EHY99953; EHY99953; SPAR3_0750. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7JZ74_STREE Unreviewed; 209 AA. AC H7JZ74; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR4_0703; OS Streptococcus pneumoniae GA04175. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760745; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA04175; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA04175."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKL01000004; EHZ04385.1; -; Genomic_DNA. DR ProteinModelPortal; H7JZ74; -. DR EnsemblBacteria; EHZ04385; EHZ04385; SPAR4_0703. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7JZ81_STREE Unreviewed; 210 AA. AC H7JZ81; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR4_0710; OS Streptococcus pneumoniae GA04175. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760745; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA04175; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA04175."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKL01000004; EHZ04574.1; -; Genomic_DNA. DR ProteinModelPortal; H7JZ81; -. DR EnsemblBacteria; EHZ04574; EHZ04574; SPAR4_0710. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7K765_STREE Unreviewed; 209 AA. AC H7K765; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR8_1177; OS Streptococcus pneumoniae GA05248. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760749; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA05248; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA05248."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKM01000005; EHZ08708.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ08708; EHZ08708; SPAR8_1177. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23302 MW; 094F9E0E007A2FA0 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGESALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7K772_STREE Unreviewed; 210 AA. AC H7K772; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR8_1184; OS Streptococcus pneumoniae GA05248. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760749; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA05248; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA05248."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKM01000005; EHZ08715.1; -; Genomic_DNA. DR ProteinModelPortal; H7K772; -. DR EnsemblBacteria; EHZ08715; EHZ08715; SPAR8_1184. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7KB55_STREE Unreviewed; 209 AA. AC H7KB55; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR9_0658; OS Streptococcus pneumoniae GA06083. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760750; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA06083; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA06083."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKN01000005; EHZ11831.1; -; Genomic_DNA. DR ProteinModelPortal; H7KB55; -. DR EnsemblBacteria; EHZ11831; EHZ11831; SPAR9_0658. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7KB62_STREE Unreviewed; 192 AA. AC H7KB62; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR9_0665; OS Streptococcus pneumoniae GA06083. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760750; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA06083; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA06083."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKN01000005; EHZ11838.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ11838; EHZ11838; SPAR9_0665. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 117 119 THZ-P binding (By similarity). FT METAL 53 53 Magnesium (By similarity). FT METAL 72 72 Magnesium (By similarity). FT BINDING 52 52 HMP-PP (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 147 147 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 192 AA; 20566 MW; 06E056B1121AD04F CRC64; MESFLAKVET ACRSGVTIVQ LREKNLTTNQ YYQLAKQVKE ITDAYQVPLI IDDRLDVCLA VDAAGLHIGD DELPVSVARQ VLGPEKILGV TAKTVKRALE AEKSGADYLG TGAIFPTTTK ENAPITLIST LKTICQTVAI PIVAIGGLTS ENIDQLMGTG IAGVAVVRDL MQAEDIEAKT QAFLTKLHDI LS // ID H7KJV4_STREE Unreviewed; 209 AA. AC H7KJV4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR15_0628; OS Streptococcus pneumoniae GA07914. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760756; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA07914; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA07914."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKO01000004; EHZ10538.1; -; Genomic_DNA. DR ProteinModelPortal; H7KJV4; -. DR EnsemblBacteria; EHZ10538; EHZ10538; SPAR15_0628. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7KJW1_STREE Unreviewed; 210 AA. AC H7KJW1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR15_0635; OS Streptococcus pneumoniae GA07914. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760756; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA07914; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA07914."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKO01000004; EHZ10545.1; -; Genomic_DNA. DR ProteinModelPortal; H7KJW1; -. DR EnsemblBacteria; EHZ10545; EHZ10545; SPAR15_0635. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; AEAC90751A95738D CRC64; MNREALRLYL VTNRYQDSVE SFLAKIETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7KMP4_STREE Unreviewed; 209 AA. AC H7KMP4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR29_0633; OS Streptococcus pneumoniae GA13430. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760770; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13430; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13430."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKP01000001; EHZ18751.1; -; Genomic_DNA. DR ProteinModelPortal; H7KMP4; -. DR EnsemblBacteria; EHZ18751; EHZ18751; SPAR29_0633. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23275 MW; 54691E8B38ED4ED4 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LRGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7KMQ1_STREE Unreviewed; 210 AA. AC H7KMQ1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR29_0640; OS Streptococcus pneumoniae GA13430. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760770; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13430; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13430."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKP01000001; EHZ18758.1; -; Genomic_DNA. DR ProteinModelPortal; H7KMQ1; -. DR EnsemblBacteria; EHZ18758; EHZ18758; SPAR29_0640. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7KV78_STREE Unreviewed; 209 AA. AC H7KV78; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR36_0711; OS Streptococcus pneumoniae GA14688. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760777; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA14688; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA14688."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKQ01000002; EHZ26465.1; -; Genomic_DNA. DR ProteinModelPortal; H7KV78; -. DR EnsemblBacteria; EHZ26465; EHZ26465; SPAR36_0711. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23376 MW; 2FA03125014CC79F CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYL GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7KV85_STREE Unreviewed; 210 AA. AC H7KV85; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR36_0718; OS Streptococcus pneumoniae GA14688. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760777; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA14688; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA14688."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKQ01000002; EHZ26472.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ26472; EHZ26472; SPAR36_0718. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22785 MW; 20B55C47CB70B024 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVRLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7L2E0_STREE Unreviewed; 209 AA. AC H7L2E0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR53_0710; OS Streptococcus pneumoniae GA18068. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760794; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA18068; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA18068."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKR01000002; EHZ31754.1; -; Genomic_DNA. DR ProteinModelPortal; H7L2E0; -. DR EnsemblBacteria; EHZ31754; EHZ31754; SPAR53_0710. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7L2E7_STREE Unreviewed; 210 AA. AC H7L2E7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR53_0717; OS Streptococcus pneumoniae GA18068. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760794; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA18068; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA18068."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKR01000002; EHZ31761.1; -; Genomic_DNA. DR ProteinModelPortal; H7L2E7; -. DR PRIDE; H7L2E7; -. DR EnsemblBacteria; EHZ31761; EHZ31761; SPAR53_0717. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; 60239DF9671A7380 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID H7L7U3_STREE Unreviewed; 209 AA. AC H7L7U3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR57_0622; OS Streptococcus pneumoniae GA19101. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760798; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA19101; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA19101."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKS01000010; EHZ38168.1; -; Genomic_DNA. DR ProteinModelPortal; H7L7U3; -. DR EnsemblBacteria; EHZ38168; EHZ38168; SPAR57_0622. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7L7V0_STREE Unreviewed; 210 AA. AC H7L7V0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR57_0629; OS Streptococcus pneumoniae GA19101. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760798; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA19101; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA19101."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKS01000010; EHZ38175.1; -; Genomic_DNA. DR ProteinModelPortal; H7L7V0; -. DR EnsemblBacteria; EHZ38175; EHZ38175; SPAR57_0629. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7LE13_STREE Unreviewed; 209 AA. AC H7LE13; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR65_0660; OS Streptococcus pneumoniae GA40563. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760806; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA40563; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA40563."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKT01000006; EHZ46306.1; -; Genomic_DNA. DR ProteinModelPortal; H7LE13; -. DR EnsemblBacteria; EHZ46306; EHZ46306; SPAR65_0660. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7LE20_STREE Unreviewed; 210 AA. AC H7LE20; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR65_0667; OS Streptococcus pneumoniae GA40563. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760806; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA40563; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA40563."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKT01000006; EHZ46313.1; -; Genomic_DNA. DR ProteinModelPortal; H7LE20; -. DR EnsemblBacteria; EHZ46313; EHZ46313; SPAR65_0667. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7LKA5_STREE Unreviewed; 210 AA. AC H7LKA5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR75_1142; OS Streptococcus pneumoniae GA43257. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760816; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA43257; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA43257."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKU01000004; EHZ48796.1; -; Genomic_DNA. DR ProteinModelPortal; H7LKA5; -. DR EnsemblBacteria; EHZ48796; EHZ48796; SPAR75_1142. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7LKB2_STREE Unreviewed; 209 AA. AC H7LKB2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR75_1149; OS Streptococcus pneumoniae GA43257. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760816; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA43257; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA43257."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKU01000004; EHZ48803.1; -; Genomic_DNA. DR ProteinModelPortal; H7LKB2; -. DR EnsemblBacteria; EHZ48803; EHZ48803; SPAR75_1149. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23247 MW; 9D63833774B28637 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7LQU6_STREE Unreviewed; 209 AA. AC H7LQU6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR79_0729; OS Streptococcus pneumoniae GA44128. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760820; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44128; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44128."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKV01000001; EHZ53970.1; -; Genomic_DNA. DR ProteinModelPortal; H7LQU6; -. DR EnsemblBacteria; EHZ53970; EHZ53970; SPAR79_0729. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23376 MW; 2FA03125014CC79F CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYL GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7LR27_STREE Unreviewed; 210 AA. AC H7LR27; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR79_0736; OS Streptococcus pneumoniae GA44128. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760820; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44128; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44128."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKV01000001; EHZ53977.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ53977; EHZ53977; SPAR79_0736. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22785 MW; 20B55C47CB70B024 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVRLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7LYB2_STREE Unreviewed; 209 AA. AC H7LYB2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR83_0708; OS Streptococcus pneumoniae GA44386. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760824; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44386; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44386."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKW01000005; EHZ54882.1; -; Genomic_DNA. DR ProteinModelPortal; H7LYB2; -. DR EnsemblBacteria; EHZ54882; EHZ54882; SPAR83_0708. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7LYB9_STREE Unreviewed; 192 AA. AC H7LYB9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR83_0715; OS Streptococcus pneumoniae GA44386. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760824; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA44386; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA44386."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKW01000005; EHZ55292.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ55292; EHZ55292; SPAR83_0715. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 117 119 THZ-P binding (By similarity). FT METAL 53 53 Magnesium (By similarity). FT METAL 72 72 Magnesium (By similarity). FT BINDING 52 52 HMP-PP (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 147 147 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 192 AA; 20536 MW; 06FDE06A621AD04F CRC64; MESFLAKVET ACRSGVTIVQ LREKNLTTNQ YYQLAKQVKE ITDAYQVPLI IDDRLDVCLA VDAAGLHIGD DELPVSVARQ VLGPEKILGV TAKTVKRALE AEKSGADYLG TGAIFPTTTK ENAPITLIST LKTICQTVAI PIVAIGGLTS ENIDQLMGAG IAGVAVVRDL MQAEDIEAKT QAFLTKLHDI LS // ID H7M4M6_STREE Unreviewed; 209 AA. AC H7M4M6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR88_0639; OS Streptococcus pneumoniae GA47179. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760829; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47179; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47179."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKX01000004; EHZ59039.1; -; Genomic_DNA. DR ProteinModelPortal; H7M4M6; -. DR EnsemblBacteria; EHZ59039; EHZ59039; SPAR88_0639. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7M4N3_STREE Unreviewed; 210 AA. AC H7M4N3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR88_0646; OS Streptococcus pneumoniae GA47179. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760829; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47179; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47179."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKX01000004; EHZ59046.1; -; Genomic_DNA. DR ProteinModelPortal; H7M4N3; -. DR EnsemblBacteria; EHZ59046; EHZ59046; SPAR88_0646. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22744 MW; A3239DF7871A7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7MB51_STREE Unreviewed; 209 AA. AC H7MB51; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR89_0669; OS Streptococcus pneumoniae GA47210. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760830; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47210; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47210."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKY01000002; EHZ59699.1; -; Genomic_DNA. DR ProteinModelPortal; H7MB51; -. DR EnsemblBacteria; EHZ59699; EHZ59699; SPAR89_0669. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7MB58_STREE Unreviewed; 210 AA. AC H7MB58; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR89_0676; OS Streptococcus pneumoniae GA47210. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760830; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47210; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47210."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKY01000002; EHZ59706.1; -; Genomic_DNA. DR ProteinModelPortal; H7MB58; -. DR EnsemblBacteria; EHZ59706; EHZ59706; SPAR89_0676. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7MFN7_STREE Unreviewed; 209 AA. AC H7MFN7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR97_0649; OS Streptococcus pneumoniae GA47461. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760838; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47461; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47461."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKZ01000001; EHZ62183.1; -; Genomic_DNA. DR ProteinModelPortal; H7MFN7; -. DR EnsemblBacteria; EHZ62183; EHZ62183; SPAR97_0649. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7MFP4_STREE Unreviewed; 210 AA. AC H7MFP4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR97_0656; OS Streptococcus pneumoniae GA47461. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760838; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47461; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47461."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIKZ01000001; EHZ62190.1; -; Genomic_DNA. DR ProteinModelPortal; H7MFP4; -. DR PRIDE; H7MFP4; -. DR EnsemblBacteria; EHZ62190; EHZ62190; SPAR97_0656. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; 60239DF9671A7380 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID H7MPA0_STREE Unreviewed; 209 AA. AC H7MPA0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR99_1226; OS Streptococcus pneumoniae GA47522. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760840; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47522; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47522."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILA01000005; EHZ64711.1; -; Genomic_DNA. DR ProteinModelPortal; H7MPA0; -. DR EnsemblBacteria; EHZ64711; EHZ64711; SPAR99_1226. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7MPA7_STREE Unreviewed; 210 AA. AC H7MPA7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR99_1233; OS Streptococcus pneumoniae GA47522. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760840; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47522; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47522."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILA01000005; EHZ64718.1; -; Genomic_DNA. DR ProteinModelPortal; H7MPA7; -. DR EnsemblBacteria; EHZ64718; EHZ64718; SPAR99_1233. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7MT91_STREE Unreviewed; 210 AA. AC H7MT91; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR101_0631; OS Streptococcus pneumoniae GA47597. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760842; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47597; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47597."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILB01000002; EHZ67082.1; -; Genomic_DNA. DR ProteinModelPortal; H7MT91; -. DR EnsemblBacteria; EHZ67082; EHZ67082; SPAR101_0631. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7MUJ0_STREE Unreviewed; 209 AA. AC H7MUJ0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR101_0624; OS Streptococcus pneumoniae GA47597. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760842; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47597; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47597."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILB01000002; EHZ67075.1; -; Genomic_DNA. DR ProteinModelPortal; H7MUJ0; -. DR EnsemblBacteria; EHZ67075; EHZ67075; SPAR101_0624. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7MZR1_STREE Unreviewed; 209 AA. AC H7MZR1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR102_0698; OS Streptococcus pneumoniae GA47628. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760843; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47628; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47628."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILC01000004; EHZ66592.1; -; Genomic_DNA. DR ProteinModelPortal; H7MZR1; -. DR EnsemblBacteria; EHZ66592; EHZ66592; SPAR102_0698. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7MZS3_STREE Unreviewed; 210 AA. AC H7MZS3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR102_0705; OS Streptococcus pneumoniae GA47628. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760843; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47628; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47628."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILC01000004; EHZ66599.1; -; Genomic_DNA. DR ProteinModelPortal; H7MZS3; -. DR EnsemblBacteria; EHZ66599; EHZ66599; SPAR102_0705. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7N5S6_STREE Unreviewed; 209 AA. AC H7N5S6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR105_0610; OS Streptococcus pneumoniae GA47760. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760846; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47760; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47760."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILD01000006; EHZ73871.1; -; Genomic_DNA. DR ProteinModelPortal; H7N5S6; -. DR EnsemblBacteria; EHZ73871; EHZ73871; SPAR105_0610. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7N5T3_STREE Unreviewed; 210 AA. AC H7N5T3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR105_0617; OS Streptococcus pneumoniae GA47760. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760846; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47760; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47760."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILD01000006; EHZ73878.1; -; Genomic_DNA. DR ProteinModelPortal; H7N5T3; -. DR EnsemblBacteria; EHZ73878; EHZ73878; SPAR105_0617. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; AEAC90751A95738D CRC64; MNREALRLYL VTNRYQDSVE SFLAKIETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7NBA8_STREE Unreviewed; 209 AA. AC H7NBA8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR111_0694; OS Streptococcus pneumoniae GA49194. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760852; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA49194; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA49194."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILE01000001; EHZ72324.1; -; Genomic_DNA. DR ProteinModelPortal; H7NBA8; -. DR EnsemblBacteria; EHZ72324; EHZ72324; SPAR111_0694. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7NBB5_STREE Unreviewed; 210 AA. AC H7NBB5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR111_0701; OS Streptococcus pneumoniae GA49194. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760852; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA49194; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA49194."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILE01000001; EHZ72331.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ72331; EHZ72331; SPAR111_0701. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22728 MW; E8F9319141D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGAGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7NIF5_STREE Unreviewed; 209 AA. AC H7NIF5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR114_0670; OS Streptococcus pneumoniae GA49542. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760855; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA49542; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA49542."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILF01000003; EHZ77347.1; -; Genomic_DNA. DR ProteinModelPortal; H7NIF5; -. DR EnsemblBacteria; EHZ77347; EHZ77347; SPAR114_0670. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23247 MW; 9D63833774B28637 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7NIG2_STREE Unreviewed; 210 AA. AC H7NIG2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR114_0677; OS Streptococcus pneumoniae GA49542. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760855; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA49542; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA49542."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILF01000003; EHZ77354.1; -; Genomic_DNA. DR ProteinModelPortal; H7NIG2; -. DR EnsemblBacteria; EHZ77354; EHZ77354; SPAR114_0677. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7NPN2_STREE Unreviewed; 210 AA. AC H7NPN2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR142_0775; OS Streptococcus pneumoniae NP141. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760883; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NP141; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae NP141."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILG01000003; EHZ97873.1; -; Genomic_DNA. DR ProteinModelPortal; H7NPN2; -. DR EnsemblBacteria; EHZ97873; EHZ97873; SPAR142_0775. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7NPN9_STREE Unreviewed; 209 AA. AC H7NPN9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR142_0782; OS Streptococcus pneumoniae NP141. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760883; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NP141; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae NP141."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILG01000003; EHZ97880.1; -; Genomic_DNA. DR ProteinModelPortal; H7NPN9; -. DR EnsemblBacteria; EHZ97880; EHZ97880; SPAR142_0782. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23244 MW; 69798D236EB6C679 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7NWU0_STREE Unreviewed; 209 AA. AC H7NWU0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR149_0664; OS Streptococcus pneumoniae GA05578. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1069623; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA05578; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA05578."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILH01000003; EIA01145.1; -; Genomic_DNA. DR EnsemblBacteria; EIA01145; EIA01145; SPAR149_0664. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23302 MW; 094F9E0E007A2FA0 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGESALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7NWU7_STREE Unreviewed; 210 AA. AC H7NWU7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR149_0671; OS Streptococcus pneumoniae GA05578. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1069623; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA05578; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA05578."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILH01000003; EIA01152.1; -; Genomic_DNA. DR ProteinModelPortal; H7NWU7; -. DR EnsemblBacteria; EIA01152; EIA01152; SPAR149_0671. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7P1Y2_STREE Unreviewed; 209 AA. AC H7P1Y2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR152_0636; OS Streptococcus pneumoniae England14-9. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1069625; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=England14-9; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae England14-9."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILI01000001; EIA03311.1; -; Genomic_DNA. DR EnsemblBacteria; EIA03311; EIA03311; SPAR152_0636. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23362 MW; A51A41EFBB2CC783 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKDEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7P1Y9_STREE Unreviewed; 210 AA. AC H7P1Y9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR152_0643; OS Streptococcus pneumoniae England14-9. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1069625; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=England14-9; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae England14-9."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILI01000001; EIA03318.1; -; Genomic_DNA. DR EnsemblBacteria; EIA03318; EIA03318; SPAR152_0643. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22772 MW; FD46268D3AB58688 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIIQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7P5T4_STREE Unreviewed; 209 AA. AC H7P5T4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR154_0655; OS Streptococcus pneumoniae GA02506. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1069626; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA02506; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA02506."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILJ01000002; EIA04943.1; -; Genomic_DNA. DR EnsemblBacteria; EIA04943; EIA04943; SPAR154_0655. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23302 MW; 094F9E0E007A2FA0 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGESALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7P5U1_STREE Unreviewed; 210 AA. AC H7P5U1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR154_0662; OS Streptococcus pneumoniae GA02506. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1069626; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA02506; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA02506."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILJ01000002; EIA04950.1; -; Genomic_DNA. DR ProteinModelPortal; H7P5U1; -. DR EnsemblBacteria; EIA04950; EIA04950; SPAR154_0662. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7PDL0_STREE Unreviewed; 209 AA. AC H7PDL0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR156_0671; OS Streptococcus pneumoniae GA08825. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1069628; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA08825; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA08825."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILK01000004; EIA06040.1; -; Genomic_DNA. DR ProteinModelPortal; H7PDL0; -. DR EnsemblBacteria; EIA06040; EIA06040; SPAR156_0671. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7PDL7_STREE Unreviewed; 210 AA. AC H7PDL7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR156_0678; OS Streptococcus pneumoniae GA08825. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1069628; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA08825; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA08825."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILK01000004; EIA06047.1; -; Genomic_DNA. DR ProteinModelPortal; H7PDL7; -. DR EnsemblBacteria; EIA06047; EIA06047; SPAR156_0678. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7PJN3_STREE Unreviewed; 209 AA. AC H7PJN3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR7_0675; OS Streptococcus pneumoniae GA05245. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760748; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA05245; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA05245."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILL01000003; EHZ05734.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ05734; EHZ05734; SPAR7_0675. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23271 MW; B351214742E856CB CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVKYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7PJP0_STREE Unreviewed; 210 AA. AC H7PJP0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR7_0682; OS Streptococcus pneumoniae GA05245. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760748; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA05245; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA05245."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILL01000003; EHZ05741.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ05741; EHZ05741; SPAR7_0682. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22740 MW; E8E4874C9DBCC48E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7PR80_STREE Unreviewed; 209 AA. AC H7PR80; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR33_0746; OS Streptococcus pneumoniae GA13723. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760774; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13723; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13723."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILM01000005; EHZ24373.1; -; Genomic_DNA. DR ProteinModelPortal; H7PR80; -. DR EnsemblBacteria; EHZ24373; EHZ24373; SPAR33_0746. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7PR87_STREE Unreviewed; 210 AA. AC H7PR87; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR33_0753; OS Streptococcus pneumoniae GA13723. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760774; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA13723; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA13723."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILM01000005; EHZ24411.1; -; Genomic_DNA. DR EnsemblBacteria; EHZ24411; EHZ24411; SPAR33_0753. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; E8E496ABC1C7E57E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APIILISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7PYA0_STREE Unreviewed; 209 AA. AC H7PYA0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR35_0725; OS Streptococcus pneumoniae GA14373. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760776; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA14373; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA14373."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILN01000003; EHZ24881.1; -; Genomic_DNA. DR ProteinModelPortal; H7PYA0; -. DR EnsemblBacteria; EHZ24881; EHZ24881; SPAR35_0725. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23261 MW; 9D79329C74B6C673 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7PYA7_STREE Unreviewed; 210 AA. AC H7PYA7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR35_0732; OS Streptococcus pneumoniae GA14373. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760776; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA14373; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA14373."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILN01000003; EHZ24888.1; -; Genomic_DNA. DR ProteinModelPortal; H7PYA7; -. DR EnsemblBacteria; EHZ24888; EHZ24888; SPAR35_0732. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7Q477_STREE Unreviewed; 209 AA. AC H7Q477; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR51_0551; OS Streptococcus pneumoniae GA17719. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760792; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17719; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA17719."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILO01000005; EHZ31489.1; -; Genomic_DNA. DR ProteinModelPortal; H7Q477; -. DR EnsemblBacteria; EHZ31489; EHZ31489; SPAR51_0551. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7Q484_STREE Unreviewed; 210 AA. AC H7Q484; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR51_0558; OS Streptococcus pneumoniae GA17719. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760792; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17719; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA17719."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILO01000005; EHZ31496.1; -; Genomic_DNA. DR ProteinModelPortal; H7Q484; -. DR EnsemblBacteria; EHZ31496; EHZ31496; SPAR51_0558. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7QBF0_STREE Unreviewed; 209 AA. AC H7QBF0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR62_0637; OS Streptococcus pneumoniae GA40028. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760803; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA40028; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA40028."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILP01000005; EHZ39715.1; -; Genomic_DNA. DR ProteinModelPortal; H7QBF0; -. DR EnsemblBacteria; EHZ39715; EHZ39715; SPAR62_0637. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23244 MW; 69798D236EB6C679 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H7QBF7_STREE Unreviewed; 210 AA. AC H7QBF7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR62_0644; OS Streptococcus pneumoniae GA40028. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760803; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA40028; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA40028."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILP01000005; EHZ39653.1; -; Genomic_DNA. DR ProteinModelPortal; H7QBF7; -. DR EnsemblBacteria; EHZ39653; EHZ39653; SPAR62_0644. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7QGT1_STREE Unreviewed; 209 AA. AC H7QGT1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR107_0638; OS Streptococcus pneumoniae GA47794. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760848; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47794; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47794."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILQ01000003; EHZ73459.1; -; Genomic_DNA. DR ProteinModelPortal; H7QGT1; -. DR EnsemblBacteria; EHZ73459; EHZ73459; SPAR107_0638. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7QGT8_STREE Unreviewed; 210 AA. AC H7QGT8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR107_0645; OS Streptococcus pneumoniae GA47794. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760848; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA47794; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA47794."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILQ01000003; EHZ73466.1; -; Genomic_DNA. DR ProteinModelPortal; H7QGT8; -. DR EnsemblBacteria; EHZ73466; EHZ73466; SPAR107_0645. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22744 MW; A3239DF7871A7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7QMR3_STREE Unreviewed; 209 AA. AC H7QMR3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR46_0699; OS Streptococcus pneumoniae GA17457. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760787; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17457; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA17457."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILS01000004; EHZ33172.1; -; Genomic_DNA. DR ProteinModelPortal; H7QMR3; -. DR EnsemblBacteria; EHZ33172; EHZ33172; SPAR46_0699. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23304 MW; BD457EEC48E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID H7QMS1_STREE Unreviewed; 210 AA. AC H7QMS1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPAR46_0707; OS Streptococcus pneumoniae GA17457. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=760787; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GA17457; RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., RA Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P., RA Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L., RA Stephens D.S., Tettelin H.; RT "Genomic Sequence of Streptococcus pneumoniae GA17457."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AILS01000004; EHZ33180.1; -; Genomic_DNA. DR ProteinModelPortal; H7QMS1; -. DR EnsemblBacteria; EHZ33180; EHZ33180; SPAR46_0707. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22758 MW; E8E4874A31D6048E CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPI VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID H7QT65_CAMCO Unreviewed; 210 AA. AC H7QT65; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco1_01174; OS Campylobacter coli 111-3. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887280; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=111-3; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=111-3; RX PubMed=23279811; RA Richards V.P., Lefebure T., Pavinski Bitar P.D., Stanhope M.J.; RT "Comparative characterization of the virulence gene clusters RT (lipooligosaccharide [LOS] and capsular polysaccharide [CPS]) for RT Campylobacter coli, Campylobacter jejuni subsp. jejuni and related RT Campylobacter species."; RL Infect. Genet. Evol. 14:200-213(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMI01000006; EIA45379.1; -; Genomic_DNA. DR ProteinModelPortal; H7QT65; -. DR EnsemblBacteria; EIA45379; EIA45379; cco1_01174. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23256 MW; F7221F023DA3BA7E CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7QTA5_CAMCO Unreviewed; 201 AA. AC H7QTA5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco1_01389; OS Campylobacter coli 111-3. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887280; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=111-3; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=111-3; RX PubMed=23279811; RA Richards V.P., Lefebure T., Pavinski Bitar P.D., Stanhope M.J.; RT "Comparative characterization of the virulence gene clusters RT (lipooligosaccharide [LOS] and capsular polysaccharide [CPS]) for RT Campylobacter coli, Campylobacter jejuni subsp. jejuni and related RT Campylobacter species."; RL Infect. Genet. Evol. 14:200-213(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMI01000006; EIA45419.1; -; Genomic_DNA. DR EnsemblBacteria; EIA45419; EIA45419; cco1_01389. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7QYX5_CAMCO Unreviewed; 201 AA. AC H7QYX5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco10_02172; OS Campylobacter coli 90-3. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887286; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=90-3; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=90-3; RX PubMed=23279811; RA Richards V.P., Lefebure T., Pavinski Bitar P.D., Stanhope M.J.; RT "Comparative characterization of the virulence gene clusters RT (lipooligosaccharide [LOS] and capsular polysaccharide [CPS]) for RT Campylobacter coli, Campylobacter jejuni subsp. jejuni and related RT Campylobacter species."; RL Infect. Genet. Evol. 14:200-213(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMJ01000008; EIA45041.1; -; Genomic_DNA. DR EnsemblBacteria; EIA45041; EIA45041; cco10_02172. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7QZ13_CAMCO Unreviewed; 210 AA. AC H7QZ13; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco10_02392; OS Campylobacter coli 90-3. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887286; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=90-3; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=90-3; RX PubMed=23279811; RA Richards V.P., Lefebure T., Pavinski Bitar P.D., Stanhope M.J.; RT "Comparative characterization of the virulence gene clusters RT (lipooligosaccharide [LOS] and capsular polysaccharide [CPS]) for RT Campylobacter coli, Campylobacter jejuni subsp. jejuni and related RT Campylobacter species."; RL Infect. Genet. Evol. 14:200-213(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMJ01000008; EIA45079.1; -; Genomic_DNA. DR EnsemblBacteria; EIA45079; EIA45079; cco10_02392. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7R642_CAMCO Unreviewed; 201 AA. AC H7R642; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco100_05324; OS Campylobacter coli Z163. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887314; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Z163; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMK01000016; EIA42175.1; -; Genomic_DNA. DR EnsemblBacteria; EIA42175; EIA42175; cco100_05324. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7R6Q5_CAMCO Unreviewed; 210 AA. AC H7R6Q5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco100_06410; OS Campylobacter coli Z163. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887314; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Z163; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMK01000025; EIA41608.1; -; Genomic_DNA. DR EnsemblBacteria; EIA41608; EIA41608; cco100_06410. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23316 MW; F72204038DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NTYLATKELR QEMNENLSFK // ID H7RAH2_CAMCO Unreviewed; 210 AA. AC H7RAH2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco105_04034; OS Campylobacter coli 2548. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887315; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2548; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIML01000016; EIA48921.1; -; Genomic_DNA. DR ProteinModelPortal; H7RAH2; -. DR EnsemblBacteria; EIA48921; EIA48921; cco105_04034. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23256 MW; F7221F023DA3BA7E CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7RAM1_CAMCO Unreviewed; 201 AA. AC H7RAM1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco105_04289; OS Campylobacter coli 2548. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887315; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2548; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIML01000018; EIA48774.1; -; Genomic_DNA. DR EnsemblBacteria; EIA48774; EIA48774; cco105_04289. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23248 MW; 80BA6AB950692189 CRC64; MWGKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLESRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7RFN4_CAMCO Unreviewed; 201 AA. AC H7RFN4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=cco106_03514; OS Campylobacter coli 2553. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887316; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2553; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2553; RX PubMed=23279811; RA Richards V.P., Lefebure T., Pavinski Bitar P.D., Stanhope M.J.; RT "Comparative characterization of the virulence gene clusters RT (lipooligosaccharide [LOS] and capsular polysaccharide [CPS]) for RT Campylobacter coli, Campylobacter jejuni subsp. jejuni and related RT Campylobacter species."; RL Infect. Genet. Evol. 14:200-213(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMM01000018; EIA50783.1; -; Genomic_DNA. DR EnsemblBacteria; EIA50783; EIA50783; cco106_03514. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23315 MW; F910A58699E1C260 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7RHN6_CAMCO Unreviewed; 210 AA. AC H7RHN6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco106_07174; OS Campylobacter coli 2553. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887316; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2553; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2553; RX PubMed=23279811; RA Richards V.P., Lefebure T., Pavinski Bitar P.D., Stanhope M.J.; RT "Comparative characterization of the virulence gene clusters RT (lipooligosaccharide [LOS] and capsular polysaccharide [CPS]) for RT Campylobacter coli, Campylobacter jejuni subsp. jejuni and related RT Campylobacter species."; RL Infect. Genet. Evol. 14:200-213(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMM01000052; EIA49480.1; -; Genomic_DNA. DR EnsemblBacteria; EIA49480; EIA49480; cco106_07174. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7RK84_CAMCO Unreviewed; 201 AA. AC H7RK84; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco111_02050; OS Campylobacter coli 2680. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887317; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2680; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMN01000009; EIA48567.1; -; Genomic_DNA. DR EnsemblBacteria; EIA48567; EIA48567; cco111_02050. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23298 MW; 470352B423B863A2 CRC64; MWDKKIIAIS DRKCVEIGFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7RKW0_CAMCO Unreviewed; 210 AA. AC H7RKW0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco111_03227; OS Campylobacter coli 2680. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887317; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2680; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMN01000014; EIA48105.1; -; Genomic_DNA. DR EnsemblBacteria; EIA48105; EIA48105; cco111_03227. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7RSG6_CAMCO Unreviewed; 201 AA. AC H7RSG6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco112_05607; OS Campylobacter coli 2685. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887318; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2685; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMO01000029; EIA52265.1; -; Genomic_DNA. DR EnsemblBacteria; EIA52265; EIA52265; cco112_05607. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7RSK9_CAMCO Unreviewed; 210 AA. AC H7RSK9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco112_05832; OS Campylobacter coli 2685. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887318; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2685; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMO01000029; EIA52308.1; -; Genomic_DNA. DR ProteinModelPortal; H7RSK9; -. DR EnsemblBacteria; EIA52308; EIA52308; cco112_05832. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23256 MW; F7221F023DA3BA7E CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7RUS9_CAMCO Unreviewed; 210 AA. AC H7RUS9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco113_00350; OS Campylobacter coli 2688. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887319; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2688; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMP01000003; EIA57513.1; -; Genomic_DNA. DR ProteinModelPortal; H7RUS9; -. DR EnsemblBacteria; EIA57513; EIA57513; cco113_00350. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23256 MW; F7221F023DA3BA7E CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7RYK7_CAMCO Unreviewed; 201 AA. AC H7RYK7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco113_07222; OS Campylobacter coli 2688. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887319; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2688; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMP01000072; EIA54222.1; -; Genomic_DNA. DR ProteinModelPortal; H7RYK7; -. DR EnsemblBacteria; EIA54222; EIA54222; cco113_07222. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23386 MW; 3EB32B7F410860B3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YTFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7S1G6_CAMCO Unreviewed; 201 AA. AC H7S1G6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco115_02407; OS Campylobacter coli 2692. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887320; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2692; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMQ01000017; EIA56836.1; -; Genomic_DNA. DR EnsemblBacteria; EIA56836; EIA56836; cco115_02407. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7S2V3_CAMCO Unreviewed; 210 AA. AC H7S2V3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco115_04858; OS Campylobacter coli 2692. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887320; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2692; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMQ01000041; EIA55477.1; -; Genomic_DNA. DR ProteinModelPortal; H7S2V3; -. DR EnsemblBacteria; EIA55477; EIA55477; cco115_04858. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23256 MW; F7221F023DA3BA7E CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7S877_CAMCO Unreviewed; 210 AA. AC H7S877; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco117_05754; OS Campylobacter coli 2698. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887321; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2698; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMR01000035; EIA56647.1; -; Genomic_DNA. DR EnsemblBacteria; EIA56647; EIA56647; cco117_05754. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7S948_CAMCO Unreviewed; 201 AA. AC H7S948; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco117_07424; OS Campylobacter coli 2698. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887321; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2698; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMR01000061; EIA55368.1; -; Genomic_DNA. DR EnsemblBacteria; EIA55368; EIA55368; cco117_07424. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23223 MW; 5D00A58A36F499E8 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKC KTTCFLHFFD RECLKLGHRY FHTPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLAECKRNL L // ID H7SAD3_CAMCO Unreviewed; 201 AA. AC H7SAD3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco12_01214; OS Campylobacter coli 84-2. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887287; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=84-2; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMS01000008; EIA60342.1; -; Genomic_DNA. DR EnsemblBacteria; EIA60342; EIA60342; cco12_01214. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7SCZ5_CAMCO Unreviewed; 210 AA. AC H7SCZ5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco12_05921; OS Campylobacter coli 84-2. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887287; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=84-2; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMS01000038; EIA59230.1; -; Genomic_DNA. DR EnsemblBacteria; EIA59230; EIA59230; cco12_05921. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23320 MW; 736EFF0CD949AE91 CRC64; MKNDLDLSLY LVASRGKKSD EFFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7SHU6_CAMCO Unreviewed; 201 AA. AC H7SHU6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco14_06040; OS Campylobacter coli 80352. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887288; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=80352; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMT01000058; EIA63566.1; -; Genomic_DNA. DR EnsemblBacteria; EIA63566; EIA63566; cco14_06040. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7SIG6_CAMCO Unreviewed; 210 AA. AC H7SIG6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco14_07180; OS Campylobacter coli 80352. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887288; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=80352; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMT01000069; EIA63194.1; -; Genomic_DNA. DR ProteinModelPortal; H7SIG6; -. DR EnsemblBacteria; EIA63194; EIA63194; cco14_07180. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23256 MW; F7221F023DA3BA7E CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7SMD7_CAMCO Unreviewed; 201 AA. AC H7SMD7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=cco16_03236; OS Campylobacter coli 86119. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887289; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=86119; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMU01000011; EIA61836.1; -; Genomic_DNA. DR EnsemblBacteria; EIA61836; EIA61836; cco16_03236. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23315 MW; F910A58699E1C260 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7SP23_CAMCO Unreviewed; 210 AA. AC H7SP23; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco16_06211; OS Campylobacter coli 86119. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887289; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=86119; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMU01000022; EIA61145.1; -; Genomic_DNA. DR EnsemblBacteria; EIA61145; EIA61145; cco16_06211. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7SSP5_CAMCO Unreviewed; 201 AA. AC H7SSP5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco19_03118; OS Campylobacter coli 1091. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887290; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1091; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMV01000018; EIA65594.1; -; Genomic_DNA. DR EnsemblBacteria; EIA65594; EIA65594; cco19_03118. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7SSS8_CAMCO Unreviewed; 210 AA. AC H7SSS8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco19_03283; OS Campylobacter coli 1091. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887290; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1091; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMV01000019; EIA65505.1; -; Genomic_DNA. DR EnsemblBacteria; EIA65505; EIA65505; cco19_03283. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23320 MW; 736EFF0CD949AE91 CRC64; MKNDLDLSLY LVASRGKKSD EFFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7SW08_CAMCO Unreviewed; 201 AA. AC H7SW08; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco23_00395; OS Campylobacter coli 1098. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887291; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1098; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMW01000002; EIA67913.1; -; Genomic_DNA. DR EnsemblBacteria; EIA67913; EIA67913; cco23_00395. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7SW40_CAMCO Unreviewed; 210 AA. AC H7SW40; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco23_00160; OS Campylobacter coli 1098. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887291; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1098; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMW01000002; EIA67868.1; -; Genomic_DNA. DR EnsemblBacteria; EIA67868; EIA67868; cco23_00160. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7T3N1_CAMCO Unreviewed; 210 AA. AC H7T3N1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco25_04329; OS Campylobacter coli 1148. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887292; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1148; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMX01000014; EIA70567.1; -; Genomic_DNA. DR EnsemblBacteria; EIA70567; EIA70567; cco25_04329. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23320 MW; 736EFF0CD949AE91 CRC64; MKNDLDLSLY LVASRGKKSD EFFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7T3S4_CAMCO Unreviewed; 201 AA. AC H7T3S4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco25_04554; OS Campylobacter coli 1148. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887292; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1148; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMX01000014; EIA70610.1; -; Genomic_DNA. DR EnsemblBacteria; EIA70610; EIA70610; cco25_04554. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7TAJ5_CAMCO Unreviewed; 201 AA. AC H7TAJ5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco37_07556; OS Campylobacter coli 1417. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887293; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1417; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMY01000034; EIA68623.1; -; Genomic_DNA. DR EnsemblBacteria; EIA68623; EIA68623; cco37_07556. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7TAN9_CAMCO Unreviewed; 210 AA. AC H7TAN9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco37_07796; OS Campylobacter coli 1417. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887293; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1417; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMY01000034; EIA68667.1; -; Genomic_DNA. DR EnsemblBacteria; EIA68667; EIA68667; cco37_07796. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7TE80_CAMCO Unreviewed; 210 AA. AC H7TE80; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco4_04814; OS Campylobacter coli 7--1. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887281; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7--1; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMZ01000014; EIA71497.1; -; Genomic_DNA. DR EnsemblBacteria; EIA71497; EIA71497; cco4_04814. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23350 MW; 667AAE49CD0CAE8A CRC64; MKNDLDLSLY LVASRGKKSD EFFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGTDYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7TF37_CAMCO Unreviewed; 201 AA. AC H7TF37; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco4_06236; OS Campylobacter coli 7--1. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887281; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=7--1; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMZ01000026; EIA70346.1; -; Genomic_DNA. DR EnsemblBacteria; EIA70346; EIA70346; cco4_06236. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7THK5_CAMCO Unreviewed; 210 AA. AC H7THK5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco5_02292; OS Campylobacter coli 132-6. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887282; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=132-6; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINA01000013; EIA76790.1; -; Genomic_DNA. DR ProteinModelPortal; H7THK5; -. DR EnsemblBacteria; EIA76790; EIA76790; cco5_02292. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23256 MW; F7221F023DA3BA7E CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7THP6_CAMCO Unreviewed; 201 AA. AC H7THP6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco5_02497; OS Campylobacter coli 132-6. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887282; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=132-6; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINA01000013; EIA76831.1; -; Genomic_DNA. DR EnsemblBacteria; EIA76831; EIA76831; cco5_02497. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7TP41_CAMCO Unreviewed; 210 AA. AC H7TP41; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco54_05564; OS Campylobacter coli 1891. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887294; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1891; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINB01000038; EIA73971.1; -; Genomic_DNA. DR EnsemblBacteria; EIA73971; EIA73971; cco54_05564. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23320 MW; 736EFF0CD949AE91 CRC64; MKNDLDLSLY LVASRGKKSD EFFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7TUD4_CAMCO Unreviewed; 210 AA. AC H7TUD4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco55_06873; OS Campylobacter coli 1909. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887295; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1909; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINC01000034; EIA75724.1; -; Genomic_DNA. DR EnsemblBacteria; EIA75724; EIA75724; cco55_06873. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7TUL0_CAMCO Unreviewed; 201 AA. AC H7TUL0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco55_07273; OS Campylobacter coli 1909. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887295; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1909; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINC01000036; EIA75525.1; -; Genomic_DNA. DR EnsemblBacteria; EIA75525; EIA75525; cco55_07273. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7TW00_CAMCO Unreviewed; 210 AA. AC H7TW00; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco6_00497; OS Campylobacter coli 59-2. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887283; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=59-2; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIND01000002; EIA82505.1; -; Genomic_DNA. DR EnsemblBacteria; EIA82505; EIA82505; cco6_00497. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23320 MW; 736EFF0CD949AE91 CRC64; MKNDLDLSLY LVASRGKKSD EFFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7TW42_CAMCO Unreviewed; 201 AA. AC H7TW42; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco6_00727; OS Campylobacter coli 59-2. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887283; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=59-2; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIND01000002; EIA82547.1; -; Genomic_DNA. DR EnsemblBacteria; EIA82547; EIA82547; cco6_00727. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7U1U5_CAMCO Unreviewed; 201 AA. AC H7U1U5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco61_01216; OS Campylobacter coli 1948. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887296; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1948; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINE01000007; EIA81759.1; -; Genomic_DNA. DR EnsemblBacteria; EIA81759; EIA81759; cco61_01216. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23357 MW; 24028A65570ECD15 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH ETTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7U1Y4_CAMCO Unreviewed; 210 AA. AC H7U1Y4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco61_01431; OS Campylobacter coli 1948. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887296; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1948; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINE01000007; EIA81798.1; -; Genomic_DNA. DR EnsemblBacteria; EIA81798; EIA81798; cco61_01431. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7U8U7_CAMCO Unreviewed; 210 AA. AC H7U8U7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco65_05043; OS Campylobacter coli 1957. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887297; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1957; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINF01000022; EIA82729.1; -; Genomic_DNA. DR EnsemblBacteria; EIA82729; EIA82729; cco65_05043. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7U9W9_CAMCO Unreviewed; 201 AA. AC H7U9W9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco65_06937; OS Campylobacter coli 1957. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887297; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1957; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINF01000035; EIA81480.1; -; Genomic_DNA. DR EnsemblBacteria; EIA81480; EIA81480; cco65_06937. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7UCK6_CAMCO Unreviewed; 201 AA. AC H7UCK6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco67_02191; OS Campylobacter coli 1961. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887298; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1961; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AING01000007; EIA87217.1; -; Genomic_DNA. DR EnsemblBacteria; EIA87217; EIA87217; cco67_02191. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7UCQ2_CAMCO Unreviewed; 210 AA. AC H7UCQ2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco67_02431; OS Campylobacter coli 1961. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887298; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1961; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AING01000007; EIA87263.1; -; Genomic_DNA. DR EnsemblBacteria; EIA87263; EIA87263; cco67_02431. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7UGM6_CAMCO Unreviewed; 210 AA. AC H7UGM6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco69_00090; OS Campylobacter coli 202/04. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887299; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=202/04; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINH01000001; EIA86990.1; -; Genomic_DNA. DR EnsemblBacteria; EIA86990; EIA86990; cco69_00090. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7UJX9_CAMCO Unreviewed; 201 AA. AC H7UJX9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco69_06000; OS Campylobacter coli 202/04. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887299; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=202/04; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINH01000019; EIA84856.1; -; Genomic_DNA. DR EnsemblBacteria; EIA84856; EIA84856; cco69_06000. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7UMF1_CAMCO Unreviewed; 210 AA. AC H7UMF1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco7_01313; OS Campylobacter coli 67-8. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887284; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=67-8; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINI01000005; EIA88767.1; -; Genomic_DNA. DR EnsemblBacteria; EIA88767; EIA88767; cco7_01313. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23283 MW; FF9B04881E7E8CD9 CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELNSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7UMJ2_CAMCO Unreviewed; 201 AA. AC H7UMJ2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco7_01538; OS Campylobacter coli 67-8. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887284; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=67-8; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINI01000005; EIA88808.1; -; Genomic_DNA. DR EnsemblBacteria; EIA88808; EIA88808; cco7_01538. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7URT0_CAMCO Unreviewed; 210 AA. AC H7URT0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco71_00905; OS Campylobacter coli 317/04. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887300; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=317/04; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINJ01000003; EIA93021.1; -; Genomic_DNA. DR EnsemblBacteria; EIA93021; EIA93021; cco71_00905. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23264 MW; 676290D455F84271 CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELNSREI YKLGLKVQKL CKEYEIPFLI NDRIDIALTL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKNI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPVGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7URX0_CAMCO Unreviewed; 201 AA. AC H7URX0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco71_01115; OS Campylobacter coli 317/04. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887300; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=317/04; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINJ01000003; EIA93061.1; -; Genomic_DNA. DR EnsemblBacteria; EIA93061; EIA93061; cco71_01115. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23223 MW; 5D00A58A36F499E8 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKC KTTCFLHFFD RECLKLGHRY FHTPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLAECKRNL L // ID H7UZG1_CAMCO Unreviewed; 210 AA. AC H7UZG1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco74_04937; OS Campylobacter coli 37/05. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887301; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=37/05; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINK01000019; EIA90996.1; -; Genomic_DNA. DR EnsemblBacteria; EIA90996; EIA90996; cco74_04937. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7V1G9_CAMCO Unreviewed; 201 AA. AC H7V1G9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco74_08589; OS Campylobacter coli 37/05. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887301; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=37/05; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINK01000048; EIA89469.1; -; Genomic_DNA. DR EnsemblBacteria; EIA89469; EIA89469; cco74_08589. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7V4S2_CAMCO Unreviewed; 210 AA. AC H7V4S2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco75_04868; OS Campylobacter coli LMG 9854. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887302; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9854; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINL01000024; EIA93493.1; -; Genomic_DNA. DR EnsemblBacteria; EIA93493; EIA93493; cco75_04868. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23320 MW; 736EFF0CD949AE91 CRC64; MKNDLDLSLY LVASRGKKSD EFFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7V5K6_CAMCO Unreviewed; 201 AA. AC H7V5K6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco75_06389; OS Campylobacter coli LMG 9854. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887302; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9854; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINL01000036; EIA92155.1; -; Genomic_DNA. DR EnsemblBacteria; EIA92155; EIA92155; cco75_06389. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7V9J9_CAMCO Unreviewed; 210 AA. AC H7V9J9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco76_04157; OS Campylobacter coli LMG 23336. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887303; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23336; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINM01000017; EIA96427.1; -; Genomic_DNA. DR EnsemblBacteria; EIA96427; EIA96427; cco76_04157. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7V9N9_CAMCO Unreviewed; 201 AA. AC H7V9N9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco76_04357; OS Campylobacter coli LMG 23336. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887303; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23336; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINM01000018; EIA96355.1; -; Genomic_DNA. DR EnsemblBacteria; EIA96355; EIA96355; cco76_04357. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7VCB1_CAMCO Unreviewed; 201 AA. AC H7VCB1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco77_00125; OS Campylobacter coli LMG 23341. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887304; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23341; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINN01000001; EIA98832.1; -; Genomic_DNA. DR EnsemblBacteria; EIA98832; EIA98832; cco77_00125. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7VDF2_CAMCO Unreviewed; 210 AA. AC H7VDF2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco77_02156; OS Campylobacter coli LMG 23341. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887304; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23341; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINN01000009; EIA97763.1; -; Genomic_DNA. DR ProteinModelPortal; H7VDF2; -. DR EnsemblBacteria; EIA97763; EIA97763; cco77_02156. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23256 MW; F7221F023DA3BA7E CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7VIM4_CAMCO Unreviewed; 210 AA. AC H7VIM4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco78_02692; OS Campylobacter coli LMG 23342. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887305; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23342; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINO01000010; EIA99109.1; -; Genomic_DNA. DR ProteinModelPortal; H7VIM4; -. DR EnsemblBacteria; EIA99109; EIA99109; cco78_02692. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23256 MW; F7221F023DA3BA7E CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7VIS0_CAMCO Unreviewed; 201 AA. AC H7VIS0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco78_02937; OS Campylobacter coli LMG 23342. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887305; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23342; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINO01000010; EIA99155.1; -; Genomic_DNA. DR EnsemblBacteria; EIA99155; EIA99155; cco78_02937. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7VPP1_CAMCO Unreviewed; 210 AA. AC H7VPP1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco79_04773; OS Campylobacter coli LMG 23344. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887306; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23344; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINP01000034; EIB04243.1; -; Genomic_DNA. DR EnsemblBacteria; EIB04243; EIB04243; cco79_04773. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23316 MW; B6320E033DA3A612 CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESF VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7VPT8_CAMCO Unreviewed; 201 AA. AC H7VPT8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco79_05020; OS Campylobacter coli LMG 23344. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887306; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23344; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINP01000036; EIB04177.1; -; Genomic_DNA. DR EnsemblBacteria; EIB04177; EIB04177; cco79_05020. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7VSS3_CAMCO Unreviewed; 201 AA. AC H7VSS3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco8_00325; OS Campylobacter coli 151-9. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887285; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=151-9; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINQ01000002; EIB03584.1; -; Genomic_DNA. DR EnsemblBacteria; EIB03584; EIB03584; cco8_00325. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7VSW2_CAMCO Unreviewed; 210 AA. AC H7VSW2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco8_00540; OS Campylobacter coli 151-9. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887285; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=151-9; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINQ01000002; EIB03623.1; -; Genomic_DNA. DR ProteinModelPortal; H7VSW2; -. DR EnsemblBacteria; EIB03623; EIB03623; cco8_00540. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23256 MW; F7221F023DA3BA7E CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7VZB1_CAMCO Unreviewed; 201 AA. AC H7VZB1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco81_02650; OS Campylobacter coli LMG 9853. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887307; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9853; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINR01000012; EIB01913.1; -; Genomic_DNA. DR EnsemblBacteria; EIB01913; EIB01913; cco81_02650. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7VZF1_CAMCO Unreviewed; 210 AA. AC H7VZF1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco81_02880; OS Campylobacter coli LMG 9853. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887307; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9853; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINR01000012; EIB01953.1; -; Genomic_DNA. DR ProteinModelPortal; H7VZF1; -. DR EnsemblBacteria; EIB01953; EIB01953; cco81_02880. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23256 MW; F7221F023DA3BA7E CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7W3P7_CAMCO Unreviewed; 210 AA. AC H7W3P7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco88_02088; OS Campylobacter coli LMG 9860. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887308; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9860; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINS01000011; EIB08625.1; -; Genomic_DNA. DR EnsemblBacteria; EIB08625; EIB08625; cco88_02088. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23317 MW; 985CC680B9BC847D CRC64; MKNDLDLSLY FVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELNSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7W3U1_CAMCO Unreviewed; 201 AA. AC H7W3U1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco88_02308; OS Campylobacter coli LMG 9860. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887308; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9860; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINS01000011; EIB08669.1; -; Genomic_DNA. DR EnsemblBacteria; EIB08669; EIB08669; cco88_02308. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7WAU6_CAMCO Unreviewed; 210 AA. AC H7WAU6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco91_04404; OS Campylobacter coli H6. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887309; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H6; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINT01000021; EIB06364.1; -; Genomic_DNA. DR EnsemblBacteria; EIB06364; EIB06364; cco91_04404. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7WAY8_CAMCO Unreviewed; 201 AA. AC H7WAY8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco91_04634; OS Campylobacter coli H6. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887309; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H6; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINT01000021; EIB06406.1; -; Genomic_DNA. DR EnsemblBacteria; EIB06406; EIB06406; cco91_04634. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7WDY7_CAMCO Unreviewed; 210 AA. AC H7WDY7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco93_01137; OS Campylobacter coli H8. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887310; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H8; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINU01000006; EIB12147.1; -; Genomic_DNA. DR EnsemblBacteria; EIB12147; EIB12147; cco93_01137. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7WE27_CAMCO Unreviewed; 201 AA. AC H7WE27; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco93_01347; OS Campylobacter coli H8. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887310; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H8; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINU01000007; EIB12099.1; -; Genomic_DNA. DR EnsemblBacteria; EIB12099; EIB12099; cco93_01347. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7WL50_CAMCO Unreviewed; 210 AA. AC H7WL50; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco94_04072; OS Campylobacter coli H9. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887311; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H9; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINV01000017; EIB10853.1; -; Genomic_DNA. DR EnsemblBacteria; EIB10853; EIB10853; cco94_04072. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23316 MW; B6320E033DA3A612 CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESF VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID H7WL92_CAMCO Unreviewed; 201 AA. AC H7WL92; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco94_04297; OS Campylobacter coli H9. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887311; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H9; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINV01000017; EIB10895.1; -; Genomic_DNA. DR EnsemblBacteria; EIB10895; EIB10895; cco94_04297. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7WPX0_CAMCO Unreviewed; 201 AA. AC H7WPX0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco96_02371; OS Campylobacter coli H56. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887312; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H56; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINW01000008; EIB14082.1; -; Genomic_DNA. DR EnsemblBacteria; EIB14082; EIB14082; cco96_02371. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7WQ14_CAMCO Unreviewed; 210 AA. AC H7WQ14; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco96_02601; OS Campylobacter coli H56. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887312; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H56; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINW01000008; EIB14126.1; -; Genomic_DNA. DR EnsemblBacteria; EIB14126; EIB14126; cco96_02601. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23286 MW; F7221F023DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLATKELR QEMNENLSFK // ID H7WXP3_CAMCO Unreviewed; 201 AA. AC H7WXP3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cco99_06788; OS Campylobacter coli Z156. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887313; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Z156; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINX01000030; EIB15408.1; -; Genomic_DNA. DR EnsemblBacteria; EIB15408; EIB15408; cco99_06788. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23356 MW; 24028065F0B860A3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YAFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID H7WXT5_CAMCO Unreviewed; 210 AA. AC H7WXT5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cco99_07018; OS Campylobacter coli Z156. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=887313; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Z156; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINX01000030; EIB15450.1; -; Genomic_DNA. DR EnsemblBacteria; EIB15450; EIB15450; cco99_07018. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23316 MW; F72204038DA3AA7F CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NTYLATKELR QEMNENLSFK // ID H7X136_CAMJU Unreviewed; 210 AA. AC H7X136; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje1_03746; OS Campylobacter jejuni subsp. jejuni 129-258. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889213; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=129-258; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINY01000024; EIB16038.1; -; Genomic_DNA. DR ProteinModelPortal; H7X136; -. DR EnsemblBacteria; EIB16038; EIB16038; cje1_03746. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22980 MW; 25138187D1AAA731 CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKAVLD ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLPLK // ID H7X1K7_CAMJU Unreviewed; 201 AA. AC H7X1K7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=cje1_04683; OS Campylobacter jejuni subsp. jejuni 129-258. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889213; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=129-258; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINY01000030; EIB15721.1; -; Genomic_DNA. DR ProteinModelPortal; H7X1K7; -. DR EnsemblBacteria; EIB15721; EIB15721; cje1_04683. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23461 MW; 48AC77B39ECB01F4 CRC64; MWDKKIIAIS DRKCVQIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7X3V2_CAMJU Unreviewed; 201 AA. AC H7X3V2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje10_00125; OS Campylobacter jejuni subsp. jejuni 51494. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889216; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=51494; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINZ01000001; EIB23077.1; -; Genomic_DNA. DR EnsemblBacteria; EIB23077; EIB23077; cje10_00125. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23404 MW; FCB55F8B19041BEC CRC64; MWGKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7X4C6_CAMJU Unreviewed; 210 AA. AC H7X4C6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje10_01057; OS Campylobacter jejuni subsp. jejuni 51494. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889216; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=51494; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AINZ01000005; EIB22872.1; -; Genomic_DNA. DR ProteinModelPortal; H7X4C6; -. DR EnsemblBacteria; EIB22872; EIB22872; cje10_01057. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7X9Z8_CAMJU Unreviewed; 210 AA. AC H7X9Z8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje100_01033; OS Campylobacter jejuni subsp. jejuni LMG 23216. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889239; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23216; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOA01000005; EIB21939.1; -; Genomic_DNA. DR EnsemblBacteria; EIB21939; EIB21939; cje100_01033. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22898 MW; 70FA731CCE25EA11 CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYEIPFLI NDRVDIALAL GADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK CKIYENLPLK // ID H7XA36_CAMJU Unreviewed; 203 AA. AC H7XA36; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje100_01223; OS Campylobacter jejuni subsp. jejuni LMG 23216. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889239; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23216; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOA01000005; EIB21977.1; -; Genomic_DNA. DR EnsemblBacteria; EIB21977; EIB21977; cje100_01223. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 203 AA; 23529 MW; DA0B47C57BFDFD38 CRC64; MWDKKIIAIS DRKCVQIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICTKQ KVTCFLHSFD KVCLKLGHRY FHAPLSLLRK ESKLVKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNMENFK DINIAGVCMR EILMKEKDLK TYIQVCKERL SYE // ID H7XES9_CAMJU Unreviewed; 201 AA. AC H7XES9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje102_01930; OS Campylobacter jejuni subsp. jejuni LMG 23218. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889240; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23218; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOB01000006; EIB21327.1; -; Genomic_DNA. DR EnsemblBacteria; EIB21327; EIB21327; cje102_01930. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23432 MW; 4E08626647C7C0A5 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHGKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7XEW7_CAMJU Unreviewed; 210 AA. AC H7XEW7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje102_02120; OS Campylobacter jejuni subsp. jejuni LMG 23218. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889240; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23218; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOB01000006; EIB21365.1; -; Genomic_DNA. DR ProteinModelPortal; H7XEW7; -. DR EnsemblBacteria; EIB21365; EIB21365; cje102_02120. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7XKK1_CAMJU Unreviewed; 201 AA. AC H7XKK1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Transferase; GN ORFNames=cje104_02942; OS Campylobacter jejuni subsp. jejuni LMG 23223. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889241; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23223; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOC01000013; EIB24607.1; -; Genomic_DNA. DR EnsemblBacteria; EIB24607; EIB24607; cje104_02942. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23427 MW; 095C9E503C92E91D CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG IDFLKSLLKF SQIPLYAIGG INAQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID H7XKP2_CAMJU Unreviewed; 210 AA. AC H7XKP2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje104_03157; OS Campylobacter jejuni subsp. jejuni LMG 23223. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889241; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23223; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOC01000013; EIB24648.1; -; Genomic_DNA. DR EnsemblBacteria; EIB24648; EIB24648; cje104_03157. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23032 MW; 9DEB1B6CAF4C53B1 CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIMQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKEALV ELKGINLSGV AVVRAIMDAK DAFLSAKELK RKIYENLSLK // ID H7XPS5_CAMJU Unreviewed; 210 AA. AC H7XPS5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje109_01969; OS Campylobacter jejuni subsp. jejuni LMG 23263. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889242; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23263; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOD01000010; EIB27024.1; -; Genomic_DNA. DR ProteinModelPortal; H7XPS5; -. DR EnsemblBacteria; EIB27024; EIB27024; cje109_01969. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7XPW7_CAMJU Unreviewed; 201 AA. AC H7XPW7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje109_02209; OS Campylobacter jejuni subsp. jejuni LMG 23263. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889242; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23263; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOD01000010; EIB27066.1; -; Genomic_DNA. DR EnsemblBacteria; EIB27066; EIB27066; cje109_02209. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5565A3BA4302D5F4 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7XU74_CAMJU Unreviewed; 201 AA. AC H7XU74; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje11_00240; OS Campylobacter jejuni subsp. jejuni 60004. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889217; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=60004; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOE01000002; EIB28491.1; -; Genomic_DNA. DR ProteinModelPortal; H7XU74; -. DR EnsemblBacteria; EIB28491; EIB28491; cje11_00240. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7XUB1_CAMJU Unreviewed; 210 AA. AC H7XUB1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje11_00425; OS Campylobacter jejuni subsp. jejuni 60004. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889217; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=60004; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOE01000002; EIB28528.1; -; Genomic_DNA. DR ProteinModelPortal; H7XUB1; -. DR EnsemblBacteria; EIB28528; EIB28528; cje11_00425. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7XZY3_CAMJU Unreviewed; 210 AA. AC H7XZY3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje110_01570; OS Campylobacter jejuni subsp. jejuni LMG 23264. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889243; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23264; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOF01000005; EIB31284.1; -; Genomic_DNA. DR ProteinModelPortal; H7XZY3; -. DR EnsemblBacteria; EIB31284; EIB31284; cje110_01570. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7Y322_CAMJU Unreviewed; 201 AA. AC H7Y322; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje110_07294; OS Campylobacter jejuni subsp. jejuni LMG 23264. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889243; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23264; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOF01000044; EIB29066.1; -; Genomic_DNA. DR ProteinModelPortal; H7Y322; -. DR EnsemblBacteria; EIB29066; EIB29066; cje110_07294. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7Y5S5_CAMJU Unreviewed; 210 AA. AC H7Y5S5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje114_02531; OS Campylobacter jejuni subsp. jejuni LMG 23269. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889244; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23269; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOG01000016; EIB32286.1; -; Genomic_DNA. DR ProteinModelPortal; H7Y5S5; -. DR EnsemblBacteria; EIB32286; EIB32286; cje114_02531. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7Y5W2_CAMJU Unreviewed; 201 AA. AC H7Y5W2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje114_02716; OS Campylobacter jejuni subsp. jejuni LMG 23269. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889244; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23269; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOG01000016; EIB32323.1; -; Genomic_DNA. DR EnsemblBacteria; EIB32323; EIB32323; cje114_02716. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23404 MW; FCB55F8B19041BEC CRC64; MWGKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7YCS7_CAMJU Unreviewed; 201 AA. AC H7YCS7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Transferase; GN ORFNames=cje12_06252; OS Campylobacter jejuni subsp. jejuni 55037. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889218; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=55037; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOH01000035; EIB31193.1; -; Genomic_DNA. DR ProteinModelPortal; H7YCS7; -. DR EnsemblBacteria; EIB31193; EIB31193; cje12_06252. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23486 MW; 61622900362A43FB CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICVKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG IDFLKSLLEF SQIPLYAIGG INTQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID H7YCW3_CAMJU Unreviewed; 210 AA. AC H7YCW3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje12_06442; OS Campylobacter jejuni subsp. jejuni 55037. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889218; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=55037; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOH01000035; EIB31229.1; -; Genomic_DNA. DR EnsemblBacteria; EIB31229; EIB31229; cje12_06442. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22955 MW; 3DA973D7D1B83EBA CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKVTPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKAVLD ELKGINLSGV AVVRAIMDAK DAFLAAKELK CKIYENLPLK // ID H7YF58_CAMJU Unreviewed; 201 AA. AC H7YF58; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje120_02105; OS Campylobacter jejuni subsp. jejuni LMG 9879. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889245; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9879; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOI01000009; EIB35981.1; -; Genomic_DNA. DR ProteinModelPortal; H7YF58; -. DR EnsemblBacteria; EIB35981; EIB35981; cje120_02105. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7YF94_CAMJU Unreviewed; 210 AA. AC H7YF94; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje120_02295; OS Campylobacter jejuni subsp. jejuni LMG 9879. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889245; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9879; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOI01000009; EIB36017.1; -; Genomic_DNA. DR ProteinModelPortal; H7YF94; -. DR EnsemblBacteria; EIB36017; EIB36017; cje120_02295. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7YJT0_CAMJU Unreviewed; 201 AA. AC H7YJT0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Transferase; GN ORFNames=cje13_01395; OS Campylobacter jejuni subsp. jejuni 86605. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889219; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=86605; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOJ01000007; EIB37685.1; -; Genomic_DNA. DR EnsemblBacteria; EIB37685; EIB37685; cje13_01395. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23428 MW; E75C9E503632E917 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID H7YMT2_CAMJU Unreviewed; 210 AA. AC H7YMT2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje13_06975; OS Campylobacter jejuni subsp. jejuni 86605. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889219; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=86605; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOJ01000041; EIB35138.1; -; Genomic_DNA. DR ProteinModelPortal; H7YMT2; -. DR EnsemblBacteria; EIB35138; EIB35138; cje13_06975. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7YQW6_CAMJU Unreviewed; 201 AA. AC H7YQW6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje133_03643; OS Campylobacter jejuni subsp. jejuni LMG 23357. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889246; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23357; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOK01000022; EIB38021.1; -; Genomic_DNA. DR EnsemblBacteria; EIB38021; EIB38021; cje133_03643. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23406 MW; 1056F2DFF632DA47 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD KVCLKLGHRY FHTPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVAGVCMR EILMKEKDLK KYLLECRQNL R // ID H7YR03_CAMJU Unreviewed; 210 AA. AC H7YR03; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje133_03838; OS Campylobacter jejuni subsp. jejuni LMG 23357. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889246; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23357; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOK01000022; EIB38058.1; -; Genomic_DNA. DR ProteinModelPortal; H7YR03; -. DR EnsemblBacteria; EIB38058; EIB38058; cje133_03838. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22980 MW; 25138187D1AAA731 CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKAVLD ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLPLK // ID H7YVU0_CAMJU Unreviewed; 210 AA. AC H7YVU0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje135_03660; OS Campylobacter jejuni subsp. jejuni ATCC 33560. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889247; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33560; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOL01000030; EIB42855.1; -; Genomic_DNA. DR EnsemblBacteria; EIB42855; EIB42855; cje135_03660. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22917 MW; 25069657D1AAA731 CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKAVLD ELKGINLSGV AVVRAIMDAK DAFLAAKELK CKIYENLSLK // ID H7YVY0_CAMJU Unreviewed; 203 AA. AC H7YVY0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje135_03880; OS Campylobacter jejuni subsp. jejuni ATCC 33560. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889247; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33560; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOL01000030; EIB42895.1; -; Genomic_DNA. DR EnsemblBacteria; EIB42895; EIB42895; cje135_03880. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 203 AA; 23689 MW; 1E4EB0B25E2F6494 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICTKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLVKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG LDFLKSLLKF SQIPLYAIGG INAQNIENFK DINIAGVCMR EILMKEKDLK TYIQVCKERL YHE // ID H7Z227_CAMJU Unreviewed; 201 AA. AC H7Z227; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=cje139_05301; OS Campylobacter jejuni subsp. jejuni LMG 9081. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889248; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9081; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOM01000030; EIB39805.1; -; Genomic_DNA. DR ProteinModelPortal; H7Z227; -. DR EnsemblBacteria; EIB39805; EIB39805; cje139_05301. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23390 MW; 081449B92607D5F2 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RGCLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7Z2U8_CAMJU Unreviewed; 210 AA. AC H7Z2U8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje139_06760; OS Campylobacter jejuni subsp. jejuni LMG 9081. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889248; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9081; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOM01000041; EIB39426.1; -; Genomic_DNA. DR ProteinModelPortal; H7Z2U8; -. DR EnsemblBacteria; EIB39426; EIB39426; cje139_06760. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7Z5Y9_CAMJU Unreviewed; 201 AA. AC H7Z5Y9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje14_04165; OS Campylobacter jejuni subsp. jejuni 53161. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889220; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=53161; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AION01000019; EIB42147.1; -; Genomic_DNA. DR EnsemblBacteria; EIB42147; EIB42147; cje14_04165. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23404 MW; FCB55F8B19041BEC CRC64; MWGKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7Z626_CAMJU Unreviewed; 210 AA. AC H7Z626; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje14_04350; OS Campylobacter jejuni subsp. jejuni 53161. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889220; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=53161; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AION01000019; EIB42184.1; -; Genomic_DNA. DR ProteinModelPortal; H7Z626; -. DR EnsemblBacteria; EIB42184; EIB42184; cje14_04350. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7ZB12_CAMJU Unreviewed; 201 AA. AC H7ZB12; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje140_04573; OS Campylobacter jejuni subsp. jejuni LMG 9217. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889249; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9217; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOO01000020; EIB44866.1; -; Genomic_DNA. DR ProteinModelPortal; H7ZB12; -. DR EnsemblBacteria; EIB44866; EIB44866; cje140_04573. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23390 MW; 081449B92607D5F2 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RGCLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7ZB51_CAMJU Unreviewed; 210 AA. AC H7ZB51; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje140_04778; OS Campylobacter jejuni subsp. jejuni LMG 9217. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889249; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9217; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOO01000020; EIB44905.1; -; Genomic_DNA. DR ProteinModelPortal; H7ZB51; -. DR EnsemblBacteria; EIB44905; EIB44905; cje140_04778. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7ZF48_CAMJU Unreviewed; 201 AA. AC H7ZF48; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje145_02940; OS Campylobacter jejuni subsp. jejuni 2008-1025. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889250; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2008-1025; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOP01000010; EIB47471.1; -; Genomic_DNA. DR ProteinModelPortal; H7ZF48; -. DR EnsemblBacteria; EIB47471; EIB47471; cje145_02940. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7ZF84_CAMJU Unreviewed; 210 AA. AC H7ZF84; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje145_03135; OS Campylobacter jejuni subsp. jejuni 2008-1025. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889250; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2008-1025; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOP01000010; EIB47507.1; -; Genomic_DNA. DR ProteinModelPortal; H7ZF84; -. DR EnsemblBacteria; EIB47507; EIB47507; cje145_03135. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7ZJM5_CAMJU Unreviewed; 210 AA. AC H7ZJM5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje146_01946; OS Campylobacter jejuni subsp. jejuni 2008-894. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889251; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2008-894; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOQ01000009; EIB49131.1; -; Genomic_DNA. DR EnsemblBacteria; EIB49131; EIB49131; cje146_01946. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22947 MW; 25069657CDB766F1 CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKAVLD ELKSINLSGV AVVRAIMDAK DAFLAAKELK CKIYENLSLK // ID H7ZJR1_CAMJU Unreviewed; 201 AA. AC H7ZJR1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Transferase; GN ORFNames=cje146_02136; OS Campylobacter jejuni subsp. jejuni 2008-894. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889251; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2008-894; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOQ01000009; EIB49167.1; -; Genomic_DNA. DR ProteinModelPortal; H7ZJR1; -. DR EnsemblBacteria; EIB49167; EIB49167; cje146_02136. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23486 MW; 61622900362A43FB CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICVKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG IDFLKSLLEF SQIPLYAIGG INTQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID H7ZQ95_CAMJU Unreviewed; 210 AA. AC H7ZQ95; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje147_03388; OS Campylobacter jejuni subsp. jejuni 2008-872. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889252; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2008-872; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOR01000022; EIB50273.1; -; Genomic_DNA. DR EnsemblBacteria; EIB50273; EIB50273; cje147_03388. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22998 MW; C812FDED06C6616C CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7ZQN2_CAMJU Unreviewed; 201 AA. AC H7ZQN2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=cje147_04083; OS Campylobacter jejuni subsp. jejuni 2008-872. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889252; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2008-872; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOR01000027; EIB50129.1; -; Genomic_DNA. DR ProteinModelPortal; H7ZQN2; -. DR EnsemblBacteria; EIB50129; EIB50129; cje147_04083. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23461 MW; 48AC77B39ECB01F4 CRC64; MWDKKIIAIS DRKCVQIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H7ZTW3_CAMJU Unreviewed; 210 AA. AC H7ZTW3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje154_01160; OS Campylobacter jejuni subsp. jejuni 2008-988. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889253; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2008-988; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOS01000011; EIB55088.1; -; Genomic_DNA. DR ProteinModelPortal; H7ZTW3; -. DR EnsemblBacteria; EIB55088; EIB55088; cje154_01160. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H7ZU00_CAMJU Unreviewed; 201 AA. AC H7ZU00; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje154_01345; OS Campylobacter jejuni subsp. jejuni 2008-988. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889253; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2008-988; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOS01000011; EIB55125.1; -; Genomic_DNA. DR ProteinModelPortal; H7ZU00; -. DR EnsemblBacteria; EIB55125; EIB55125; cje154_01345. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8A1U9_CAMJU Unreviewed; 201 AA. AC H8A1U9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Transferase; GN ORFNames=cje16_05489; OS Campylobacter jejuni subsp. jejuni 1997-1. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889221; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1997-1; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOT01000025; EIB51659.1; -; Genomic_DNA. DR EnsemblBacteria; EIB51659; EIB51659; cje16_05489. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23428 MW; E75C9E503632E917 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID H8A1Y9_CAMJU Unreviewed; 210 AA. AC H8A1Y9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje16_05709; OS Campylobacter jejuni subsp. jejuni 1997-1. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889221; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1997-1; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOT01000025; EIB51699.1; -; Genomic_DNA. DR EnsemblBacteria; EIB51699; EIB51699; cje16_05709. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23010 MW; 9509512237033192 CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKAVLD ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLPLK // ID H8A4K0_CAMJU Unreviewed; 210 AA. AC H8A4K0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje160_01622; OS Campylobacter jejuni subsp. jejuni 2008-979. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889254; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2008-979; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOU01000010; EIB57490.1; -; Genomic_DNA. DR ProteinModelPortal; H8A4K0; -. DR EnsemblBacteria; EIB57490; EIB57490; cje160_01622. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8A4N8_CAMJU Unreviewed; 201 AA. AC H8A4N8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje160_01812; OS Campylobacter jejuni subsp. jejuni 2008-979. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889254; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2008-979; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOU01000010; EIB57528.1; -; Genomic_DNA. DR EnsemblBacteria; EIB57528; EIB57528; cje160_01812. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23404 MW; FCB55F8B19041BEC CRC64; MWGKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8A9X4_CAMJU Unreviewed; 210 AA. AC H8A9X4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje161_01039; OS Campylobacter jejuni subsp. jejuni 2008-831. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889255; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2008-831; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOV01000004; EIB57814.1; -; Genomic_DNA. DR ProteinModelPortal; H8A9X4; -. DR EnsemblBacteria; EIB57814; EIB57814; cje161_01039. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8AA10_CAMJU Unreviewed; 201 AA. AC H8AA10; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje161_01234; OS Campylobacter jejuni subsp. jejuni 2008-831. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889255; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2008-831; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOV01000004; EIB57850.1; -; Genomic_DNA. DR ProteinModelPortal; H8AA10; -. DR EnsemblBacteria; EIB57850; EIB57850; cje161_01234. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8AGF6_CAMJU Unreviewed; 210 AA. AC H8AGF6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje19_04202; OS Campylobacter jejuni subsp. jejuni 1997-4. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889222; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1997-4; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOW01000019; EIB59670.1; -; Genomic_DNA. DR ProteinModelPortal; H8AGF6; -. DR EnsemblBacteria; EIB59670; EIB59670; cje19_04202. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23001 MW; 753C83D43B0EB44A CRC64; MKNKLDLSLY LVATKGSKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8AGJ4_CAMJU Unreviewed; 201 AA. AC H8AGJ4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje19_04392; OS Campylobacter jejuni subsp. jejuni 1997-4. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889222; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1997-4; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOW01000019; EIB59708.1; -; Genomic_DNA. DR EnsemblBacteria; EIB59708; EIB59708; cje19_04392. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23504 MW; 4E08610646A7C2A5 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLEHRY FHAPLSLLRK EPKLTKYFHI LGTSVHGKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8AJ87_CAMJU Unreviewed; 201 AA. AC H8AJ87; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=cje21_08200; OS Campylobacter jejuni subsp. jejuni 1997-7. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889223; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1997-7; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOX01000001; EIB61643.1; -; Genomic_DNA. DR ProteinModelPortal; H8AJ87; -. DR EnsemblBacteria; EIB61643; EIB61643; cje21_08200. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23461 MW; 48AC77B39ECB01F4 CRC64; MWDKKIIAIS DRKCVQIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8AJD0_CAMJU Unreviewed; 210 AA. AC H8AJD0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje21_08425; OS Campylobacter jejuni subsp. jejuni 1997-7. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889223; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1997-7; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOX01000001; EIB61686.1; -; Genomic_DNA. DR EnsemblBacteria; EIB61686; EIB61686; cje21_08425. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22998 MW; C812FDED06C6616C CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8AQS2_CAMJU Unreviewed; 210 AA. AC H8AQS2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje22_03791; OS Campylobacter jejuni subsp. jejuni 1997-10. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889224; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1997-10; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOY01000023; EIB63377.1; -; Genomic_DNA. DR ProteinModelPortal; H8AQS2; -. DR EnsemblBacteria; EIB63377; EIB63377; cje22_03791. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8AQV8_CAMJU Unreviewed; 201 AA. AC H8AQV8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje22_03971; OS Campylobacter jejuni subsp. jejuni 1997-10. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889224; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1997-10; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOY01000023; EIB63413.1; -; Genomic_DNA. DR EnsemblBacteria; EIB63413; EIB63413; cje22_03971. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23404 MW; FCB55F8B19041BEC CRC64; MWGKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8AW10_CAMJU Unreviewed; 210 AA. AC H8AW10; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje23_03169; OS Campylobacter jejuni subsp. jejuni 1997-11. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889225; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1997-11; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOZ01000015; EIB64741.1; -; Genomic_DNA. DR EnsemblBacteria; EIB64741; EIB64741; cje23_03169. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23008 MW; 2513819473209C31 CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKVVLD ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLPLK // ID H8AX00_CAMJU Unreviewed; 201 AA. AC H8AX00; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=cje23_04918; OS Campylobacter jejuni subsp. jejuni 1997-11. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889225; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1997-11; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIOZ01000027; EIB63972.1; -; Genomic_DNA. DR ProteinModelPortal; H8AX00; -. DR EnsemblBacteria; EIB63972; EIB63972; cje23_04918. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23461 MW; 48AC77B39ECB01F4 CRC64; MWDKKIIAIS DRKCVQIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8B1J1_CAMJU Unreviewed; 210 AA. AC H8B1J1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje25_04478; OS Campylobacter jejuni subsp. jejuni 1997-14. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889226; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1997-14; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPA01000022; EIB66291.1; -; Genomic_DNA. DR ProteinModelPortal; H8B1J1; -. DR EnsemblBacteria; EIB66291; EIB66291; cje25_04478. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8B1M8_CAMJU Unreviewed; 201 AA. AC H8B1M8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje25_04663; OS Campylobacter jejuni subsp. jejuni 1997-14. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889226; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1997-14; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPA01000022; EIB66328.1; -; Genomic_DNA. DR EnsemblBacteria; EIB66328; EIB66328; cje25_04663. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23404 MW; FCB55F8B19041BEC CRC64; MWGKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8B6H3_CAMJU Unreviewed; 210 AA. AC H8B6H3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje28_03584; OS Campylobacter jejuni subsp. jejuni 51037. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889227; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=51037; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPB01000018; EIB70628.1; -; Genomic_DNA. DR ProteinModelPortal; H8B6H3; -. DR EnsemblBacteria; EIB70628; EIB70628; cje28_03584. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8B828_CAMJU Unreviewed; 201 AA. AC H8B828; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje28_06528; OS Campylobacter jejuni subsp. jejuni 51037. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889227; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=51037; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPB01000041; EIB69609.1; -; Genomic_DNA. DR EnsemblBacteria; EIB69609; EIB69609; cje28_06528. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23404 MW; FCB55F8B19041BEC CRC64; MWGKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8BA30_CAMJU Unreviewed; 201 AA. AC H8BA30; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje3_00275; OS Campylobacter jejuni subsp. jejuni 110-21. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889214; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=110-21; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPC01000001; EIB69353.1; -; Genomic_DNA. DR ProteinModelPortal; H8BA30; -. DR EnsemblBacteria; EIB69353; EIB69353; cje3_00275. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8BA69_CAMJU Unreviewed; 210 AA. AC H8BA69; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje3_00470; OS Campylobacter jejuni subsp. jejuni 110-21. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889214; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=110-21; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPC01000001; EIB69392.1; -; Genomic_DNA. DR ProteinModelPortal; H8BA69; -. DR EnsemblBacteria; EIB69392; EIB69392; cje3_00470. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23001 MW; 753C83D43B0EB44A CRC64; MKNKLDLSLY LVATKGSKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8BHM3_CAMJU Unreviewed; 201 AA. AC H8BHM3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje33_05227; OS Campylobacter jejuni subsp. jejuni 87330. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889228; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=87330; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPD01000024; EIB70692.1; -; Genomic_DNA. DR ProteinModelPortal; H8BHM3; -. DR EnsemblBacteria; EIB70692; EIB70692; cje33_05227. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8BHQ8_CAMJU Unreviewed; 210 AA. AC H8BHQ8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje33_05427; OS Campylobacter jejuni subsp. jejuni 87330. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889228; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=87330; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPD01000024; EIB70727.1; -; Genomic_DNA. DR ProteinModelPortal; H8BHQ8; -. DR EnsemblBacteria; EIB70727; EIB70727; cje33_05427. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8BL84_CAMJU Unreviewed; 210 AA. AC H8BL84; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje34_03067; OS Campylobacter jejuni subsp. jejuni 87459. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889229; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=87459; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPE01000031; EIB75223.1; -; Genomic_DNA. DR ProteinModelPortal; H8BL84; -. DR EnsemblBacteria; EIB75223; EIB75223; cje34_03067. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8BLC0_CAMJU Unreviewed; 201 AA. AC H8BLC0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje34_03257; OS Campylobacter jejuni subsp. jejuni 87459. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889229; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=87459; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPE01000031; EIB75259.1; -; Genomic_DNA. DR EnsemblBacteria; EIB75259; EIB75259; cje34_03257. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23404 MW; FCB55F8B19041BEC CRC64; MWGKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8BRI5_CAMJU Unreviewed; 201 AA. AC H8BRI5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje4_02881; OS Campylobacter jejuni subsp. jejuni 140-16. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889215; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=140-16; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPF01000012; EIB75483.1; -; Genomic_DNA. DR EnsemblBacteria; EIB75483; EIB75483; cje4_02881. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5565A3BA4302D5F4 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8BRM5_CAMJU Unreviewed; 210 AA. AC H8BRM5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje4_03081; OS Campylobacter jejuni subsp. jejuni 140-16. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889215; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=140-16; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPF01000012; EIB75523.1; -; Genomic_DNA. DR ProteinModelPortal; H8BRM5; -. DR EnsemblBacteria; EIB75523; EIB75523; cje4_03081. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8BVZ9_CAMJU Unreviewed; 210 AA. AC H8BVZ9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje52_01732; OS Campylobacter jejuni subsp. jejuni 1213. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889230; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1213; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPG01000008; EIB77347.1; -; Genomic_DNA. DR EnsemblBacteria; EIB77347; EIB77347; cje52_01732. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22933 MW; BF749645DC4AAADC CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENS IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKAVLD ELKGINLSGV AVVRAIMDAK DAFLAAKELK CKIYENLSLK // ID H8BW39_CAMJU Unreviewed; 201 AA. AC H8BW39; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Transferase; GN ORFNames=cje52_01932; OS Campylobacter jejuni subsp. jejuni 1213. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889230; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1213; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPG01000008; EIB77387.1; -; Genomic_DNA. DR EnsemblBacteria; EIB77387; EIB77387; cje52_01932. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23428 MW; E75C9E503632E917 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID H8C0S2_CAMJU Unreviewed; 210 AA. AC H8C0S2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje68_01464; OS Campylobacter jejuni subsp. jejuni 1577. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889231; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1577; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPH01000011; EIB82647.1; -; Genomic_DNA. DR ProteinModelPortal; H8C0S2; -. DR EnsemblBacteria; EIB82647; EIB82647; cje68_01464. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8C382_CAMJU Unreviewed; 201 AA. AC H8C382; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje68_05996; OS Campylobacter jejuni subsp. jejuni 1577. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889231; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1577; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPH01000046; EIB80690.1; -; Genomic_DNA. DR ProteinModelPortal; H8C382; -. DR EnsemblBacteria; EIB80690; EIB80690; cje68_05996. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8C5F1_CAMJU Unreviewed; 210 AA. AC H8C5F1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje75_00490; OS Campylobacter jejuni subsp. jejuni 1798. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889232; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1798; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPI01000003; EIB80892.1; -; Genomic_DNA. DR EnsemblBacteria; EIB80892; EIB80892; cje75_00490. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22998 MW; C812FDED06C6616C CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8C9Q6_CAMJU Unreviewed; 201 AA. AC H8C9Q6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=cje75_08515; OS Campylobacter jejuni subsp. jejuni 1798. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889232; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1798; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPI01000080; EIB77808.1; -; Genomic_DNA. DR ProteinModelPortal; H8C9Q6; -. DR EnsemblBacteria; EIB77808; EIB77808; cje75_08515. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23461 MW; 48AC77B39ECB01F4 CRC64; MWDKKIIAIS DRKCVQIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8CB19_CAMJU Unreviewed; 210 AA. AC H8CB19; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje77_02072; OS Campylobacter jejuni subsp. jejuni 1854. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889233; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1854; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPJ01000009; EIB81586.1; -; Genomic_DNA. DR ProteinModelPortal; H8CB19; -. DR EnsemblBacteria; EIB81586; EIB81586; cje77_02072. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23001 MW; 753C83D43B0EB44A CRC64; MKNKLDLSLY LVATKGSKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8CB55_CAMJU Unreviewed; 201 AA. AC H8CB55; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje77_02262; OS Campylobacter jejuni subsp. jejuni 1854. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889233; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1854; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPJ01000009; EIB81622.1; -; Genomic_DNA. DR ProteinModelPortal; H8CB55; -. DR EnsemblBacteria; EIB81622; EIB81622; cje77_02262. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8CGI5_CAMJU Unreviewed; 210 AA. AC H8CGI5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje79_03320; OS Campylobacter jejuni subsp. jejuni 1893. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889234; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1893; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1893; RX PubMed=23279811; RA Richards V.P., Lefebure T., Pavinski Bitar P.D., Stanhope M.J.; RT "Comparative characterization of the virulence gene clusters RT (lipooligosaccharide [LOS] and capsular polysaccharide [CPS]) for RT Campylobacter coli, Campylobacter jejuni subsp. jejuni and related RT Campylobacter species."; RL Infect. Genet. Evol. 14:200-213(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPK01000013; EIB84526.1; -; Genomic_DNA. DR ProteinModelPortal; H8CGI5; -. DR EnsemblBacteria; EIB84526; EIB84526; cje79_03320. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8CGM4_CAMJU Unreviewed; 201 AA. AC H8CGM4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje79_03515; OS Campylobacter jejuni subsp. jejuni 1893. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889234; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1893; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1893; RX PubMed=23279811; RA Richards V.P., Lefebure T., Pavinski Bitar P.D., Stanhope M.J.; RT "Comparative characterization of the virulence gene clusters RT (lipooligosaccharide [LOS] and capsular polysaccharide [CPS]) for RT Campylobacter coli, Campylobacter jejuni subsp. jejuni and related RT Campylobacter species."; RL Infect. Genet. Evol. 14:200-213(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPK01000013; EIB84565.1; -; Genomic_DNA. DR EnsemblBacteria; EIB84565; EIB84565; cje79_03515. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5565A3BA4302D5F4 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8CKG5_CAMJU Unreviewed; 201 AA. AC H8CKG5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=cje84_01648; OS Campylobacter jejuni subsp. jejuni 1928. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889235; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1928; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1928; RX PubMed=23279811; RA Richards V.P., Lefebure T., Pavinski Bitar P.D., Stanhope M.J.; RT "Comparative characterization of the virulence gene clusters RT (lipooligosaccharide [LOS] and capsular polysaccharide [CPS]) for RT Campylobacter coli, Campylobacter jejuni subsp. jejuni and related RT Campylobacter species."; RL Infect. Genet. Evol. 14:200-213(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPL01000010; EIB87001.1; -; Genomic_DNA. DR ProteinModelPortal; H8CKG5; -. DR EnsemblBacteria; EIB87001; EIB87001; cje84_01648. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23461 MW; 48AC77B39ECB01F4 CRC64; MWDKKIIAIS DRKCVQIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG LDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8CKK4_CAMJU Unreviewed; 210 AA. AC H8CKK4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje84_01843; OS Campylobacter jejuni subsp. jejuni 1928. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889235; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1928; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1928; RX PubMed=23279811; RA Richards V.P., Lefebure T., Pavinski Bitar P.D., Stanhope M.J.; RT "Comparative characterization of the virulence gene clusters RT (lipooligosaccharide [LOS] and capsular polysaccharide [CPS]) for RT Campylobacter coli, Campylobacter jejuni subsp. jejuni and related RT Campylobacter species."; RL Infect. Genet. Evol. 14:200-213(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPL01000010; EIB87040.1; -; Genomic_DNA. DR ProteinModelPortal; H8CKK4; -. DR EnsemblBacteria; EIB87040; EIB87040; cje84_01843. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23001 MW; 753C83D43B0EB44A CRC64; MKNKLDLSLY LVATKGSKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8CQT2_CAMJU Unreviewed; 210 AA. AC H8CQT2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje89_02395; OS Campylobacter jejuni subsp. jejuni LMG 9872. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889236; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9872; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPM01000011; EIB87465.1; -; Genomic_DNA. DR EnsemblBacteria; EIB87465; EIB87465; cje89_02395. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23130 MW; 4570D9F61BA1FB06 CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKIQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKTTPTKESS LLSLEFLSQI CDKSPIGVVA IGGIDKEVLD ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLPLK // ID H8CQW8_CAMJU Unreviewed; 201 AA. AC H8CQW8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje89_02575; OS Campylobacter jejuni subsp. jejuni LMG 9872. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889236; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 9872; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPM01000011; EIB87501.1; -; Genomic_DNA. DR EnsemblBacteria; EIB87501; EIB87501; cje89_02575. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23496 MW; 0215A9BA41B1032A CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPFSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8CV07_CAMJU Unreviewed; 201 AA. AC H8CV07; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 9. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=cje95_01312; OS Campylobacter jejuni subsp. jejuni LMG 23210. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889237; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23210; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPN01000006; EIB94320.1; -; Genomic_DNA. DR ProteinModelPortal; H8CV07; -. DR EnsemblBacteria; EIB94320; EIB94320; cje95_01312. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID H8CV44_CAMJU Unreviewed; 210 AA. AC H8CV44; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje95_01507; OS Campylobacter jejuni subsp. jejuni LMG 23210. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889237; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23210; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPN01000006; EIB94357.1; -; Genomic_DNA. DR ProteinModelPortal; H8CV44; -. DR EnsemblBacteria; EIB94357; EIB94357; cje95_01507. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID H8D0M2_CAMJU Unreviewed; 201 AA. AC H8D0M2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Transferase; GN ORFNames=cje96_00969; OS Campylobacter jejuni subsp. jejuni LMG 23211. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889238; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23211; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23211; RX PubMed=23279811; RA Richards V.P., Lefebure T., Pavinski Bitar P.D., Stanhope M.J.; RT "Comparative characterization of the virulence gene clusters RT (lipooligosaccharide [LOS] and capsular polysaccharide [CPS]) for RT Campylobacter coli, Campylobacter jejuni subsp. jejuni and related RT Campylobacter species."; RL Infect. Genet. Evol. 14:200-213(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPO01000004; EIB93197.1; -; Genomic_DNA. DR EnsemblBacteria; EIB93197; EIB93197; cje96_00969. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 201 AA; 23428 MW; E75C9E503632E917 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLIKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKVGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINIAGVCMR EILMKEKDLK KYLLECRQNL R // ID H8D0Q9_CAMJU Unreviewed; 210 AA. AC H8D0Q9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=cje96_01174; OS Campylobacter jejuni subsp. jejuni LMG 23211. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=889238; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23211; RA Richards V., Lefebure T., Suzuki H., Pavinski Bitar P., Stanhope M.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 23211; RX PubMed=23279811; RA Richards V.P., Lefebure T., Pavinski Bitar P.D., Stanhope M.J.; RT "Comparative characterization of the virulence gene clusters RT (lipooligosaccharide [LOS] and capsular polysaccharide [CPS]) for RT Campylobacter coli, Campylobacter jejuni subsp. jejuni and related RT Campylobacter species."; RL Infect. Genet. Evol. 14:200-213(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIPO01000004; EIB93234.1; -; Genomic_DNA. DR EnsemblBacteria; EIB93234; EIB93234; cje96_01174. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23036 MW; DF04995A1E85F892 CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAVKELK RKIYENLPLK // ID H8DFW7_ECOLX Unreviewed; 211 AA. AC H8DFW7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=OQA_20034; OS Escherichia coli SCI-07. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1144302; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SCI-07; RX PubMed=22582380; DOI=10.1128/JB.00394-12; RA Rojas T.C., Parizzi L.P., Tiba M.R., Chen L., Pereira G.A., Sangal V., RA Yang J., Yu J., Dias da Silveira W.; RT "Draft Genome of a Brazilian Avian-Pathogenic Escherichia coli Strain RT and In Silico Characterization of Virulence-Related Genes."; RL J. Bacteriol. 194:3023-3023(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJFG01000042; EIA34290.1; -; Genomic_DNA. DR ProteinModelPortal; H8DFW7; -. DR SMR; H8DFW7; 9-208. DR EnsemblBacteria; EIA34290; EIA34290; OQA_20034. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23030 MW; D9436839F2B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSTIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H8DNB1_9ENTR Unreviewed; 208 AA. AC H8DNB1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=S7A_17605; OS Pantoea sp. Sc1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=593105; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sc1; RX PubMed=22582377; DOI=10.1128/JB.00450-12; RA Medrano E.G., Bell A.A.; RT "Genome Sequence of Pantoea sp. Strain Sc 1, an Opportunistic Cotton RT Pathogen."; RL J. Bacteriol. 194:3019-3019(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJFP01000001; EIC00349.1; -; Genomic_DNA. DR EnsemblBacteria; EIC00349; EIC00349; S7A_17605. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22556 MW; 98C1E984BF8E212A CRC64; MSAFPATAPR LGLYPVVDSP AWIERLLTAG VRTLQLRIKD QPDEIAEPAI AQAIALGKRY DARLFINDYW ELAIRHDAYG VHLGQEDLDV ADLARIRQAG LRLGISTHDD TELDRALAIQ PSYIALGHIF PTQTKAMPSA PQGVEQLKRH LARLTHIPTV AIGGISIARA PEVLATGVGS IAVVSAITQA DDWREATRTL LALAEPHG // ID H8EFF1_CLOTM Unreviewed; 356 AA. AC H8EFF1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=AD2_2304; OS Clostridium thermocellum AD2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1138384; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AD2; RX PubMed=22628515; DOI=10.1128/JB.00473-12; RA Brown S.D., Lamed R., Morag E., Borovok I., Shoham Y., Klingeman D.M., RA Johnson C.M., Yang Z., Land M.L., Utturkar S.M., Keller M., RA Bayer E.A.; RT "Draft Genome Sequences for Clostridium thermocellum Wild-Type Strain RT YS and Derived Cellulose Adhesion-Defective Mutant Strain AD2."; RL J. Bacteriol. 194:3290-3291(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGS01000067; EIC10439.1; -; Genomic_DNA. DR ProteinModelPortal; H8EFF1; -. DR EnsemblBacteria; EIC10439; EIC10439; AD2_2304. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 183 187 HMP-PP binding (By similarity). FT REGION 280 282 THZ-P binding (By similarity). FT REGION 331 332 THZ-P binding (By similarity). FT METAL 216 216 Magnesium (By similarity). FT METAL 235 235 Magnesium (By similarity). FT BINDING 215 215 HMP-PP (By similarity). FT BINDING 254 254 HMP-PP (By similarity). FT BINDING 283 283 HMP-PP (By similarity). FT BINDING 311 311 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 356 AA; 40444 MW; 3C88F277A3F463FC CRC64; MGLDNLYRVL DANVNRTSEG LRVLEDLARF CYNDRLLSKR IKELRHSVRK NIAGLVPNLI SSRDSVNDVG LKTSMEMDID RKASLLDLAR ANFKRVQEAL RTVEESLKVL NENDLSKFYE SCRFETYSIE KEYFKVLTFE NKKGRLNEII TGLYCITSEE HSKGRSNIEV VEKMIKAGVK IIQYREKKKS LLEKYNECKK IREMTLDSGV TFIVNDNIDI AMMVKADGVH IGQDDLPIEK VRELVGDEMI IGISTHSPTQ AEDAVRRGAD YIGVGPLYRT YTKEDVCEPV GLEYLDYVVK NINIPYVAIG GIKEHNMDEV LARGARCIAM VTEIVGADDI EEKISKVKSK FSRGVL // ID H8EKW6_CLOTM Unreviewed; 356 AA. AC H8EKW6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=YSBL_0954; OS Clostridium thermocellum YS. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1094188; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YS; RX PubMed=22628515; DOI=10.1128/JB.00473-12; RA Brown S.D., Lamed R., Morag E., Borovok I., Shoham Y., Klingeman D.M., RA Johnson C.M., Yang Z., Land M.L., Utturkar S.M., Keller M., RA Bayer E.A.; RT "Draft Genome Sequences for Clostridium thermocellum Wild-Type Strain RT YS and Derived Cellulose Adhesion-Defective Mutant Strain AD2."; RL J. Bacteriol. 194:3290-3291(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGT01000015; EIC05572.1; -; Genomic_DNA. DR ProteinModelPortal; H8EKW6; -. DR EnsemblBacteria; EIC05572; EIC05572; YSBL_0954. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 183 187 HMP-PP binding (By similarity). FT REGION 280 282 THZ-P binding (By similarity). FT REGION 331 332 THZ-P binding (By similarity). FT METAL 216 216 Magnesium (By similarity). FT METAL 235 235 Magnesium (By similarity). FT BINDING 215 215 HMP-PP (By similarity). FT BINDING 254 254 HMP-PP (By similarity). FT BINDING 283 283 HMP-PP (By similarity). FT BINDING 311 311 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 356 AA; 40444 MW; 3C88F277A3F463FC CRC64; MGLDNLYRVL DANVNRTSEG LRVLEDLARF CYNDRLLSKR IKELRHSVRK NIAGLVPNLI SSRDSVNDVG LKTSMEMDID RKASLLDLAR ANFKRVQEAL RTVEESLKVL NENDLSKFYE SCRFETYSIE KEYFKVLTFE NKKGRLNEII TGLYCITSEE HSKGRSNIEV VEKMIKAGVK IIQYREKKKS LLEKYNECKK IREMTLDSGV TFIVNDNIDI AMMVKADGVH IGQDDLPIEK VRELVGDEMI IGISTHSPTQ AEDAVRRGAD YIGVGPLYRT YTKEDVCEPV GLEYLDYVVK NINIPYVAIG GIKEHNMDEV LARGARCIAM VTEIVGADDI EEKISKVKSK FSRGVL // ID H8EVP8_MYCTE Unreviewed; 222 AA. AC H8EVP8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ERDMAN_0456; OS Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=652616; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35801 / TMC 107 / Erdman; RX PubMed=22535945; DOI=10.1128/JB.00353-12; RA Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.; RT "Complete annotated genome sequence of Mycobacterium tuberculosis RT Erdman."; RL J. Bacteriol. 194:2770-2770(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012340; BAL64272.1; -; Genomic_DNA. DR RefSeq; YP_007608949.1; NC_020559.1. DR ProteinModelPortal; H8EVP8; -. DR SMR; H8EVP8; 1-221. DR EnsemblBacteria; BAL64272; BAL64272; ERDMAN_0456. DR GeneID; 14963814; -. DR KEGG; mtn:ERDMAN_0456; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID H8FEG2_XANCI Unreviewed; 315 AA. AC H8FEG2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 13-NOV-2013, entry version 11. DE SubName: Full=Mutator MutT family protein; GN Name=mutT; ORFNames=XMIN_1706; OS Xanthomonas citri pv. mangiferaeindicae LMG 941. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=1156940; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 941; RA Midha S., Ranjan M., Sharma V., Pinnaka A.K., Patil P.B.; RT "Genome Sequence of Xanthomonas citri pv. mangiferaeindicae Strain LMG RT 941."; RL J. Bacteriol. 194:3031-3031(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 941; RA Patil P.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAHO01000016; CCG36732.1; -; Genomic_DNA. DR ProteinModelPortal; H8FEG2; -. DR EnsemblBacteria; CCG36732; CCG36732; XMIN_1706. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34887 MW; 4DEBDBFC8B5A6A34 CRC64; MPDSLRSIHV VAGVITDPRG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIEAQVGD WVMDVPQLYP DKRLRLEVRH ITSWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGAL RQPDRYLITP DPEDDTRWLE SLELALQNGI TRIQLRARQL APARWQALLQ QVMRLRGRAR AQLLLNRDIA LAADLGIGVH LGSEQLAGLQ ERPLPAEQLV AASCHGLDDL RHAQRIGCDF AVLGPVQATA SHPGATPIGW DGFETLREQV SLPIYALGGM QVEDVRQARS HGAQGIAAIR ALWPQ // ID H8FFK0_XANCI Unreviewed; 212 AA. AC H8FFK0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=XMIN_2117; OS Xanthomonas citri pv. mangiferaeindicae LMG 941. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=1156940; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 941; RA Midha S., Ranjan M., Sharma V., Pinnaka A.K., Patil P.B.; RT "Genome Sequence of Xanthomonas citri pv. mangiferaeindicae Strain LMG RT 941."; RL J. Bacteriol. 194:3031-3031(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 941; RA Patil P.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAHO01000022; CCG37137.1; -; Genomic_DNA. DR EnsemblBacteria; CCG37137; CCG37137; XMIN_2117. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22032 MW; 2FF6925A758DC9B4 CRC64; MPNRPNVRGV YLITPDEPNT QRLLLRTAPL LGSITWLQYR NKQADAALRL RQASALREAC AAHGVPLIIN DDAQLAAQVG AQGVHLGEDD GDVAAARALL GEQAIIGVSC YDDIERARAA AASGASYVAF GAFFPTTTKQ TTRRATPALL QQAAELDVPR VAIGGIAPAQ VPALVTAGAD LIAVVSGVYA APDPVAAVQG YRAGFAAQRG KL // ID H8FMV5_PHAMO Unreviewed; 222 AA. AC H8FMV5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 11-DEC-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=PHAMO_10118; OS Phaeospirillum molischianum DSM 120. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Phaeospirillum. OX NCBI_TaxID=1150626; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 120; RX PubMed=22689244; DOI=10.1128/JB.00605-12; RA Duquesne K., Prima V., Ji B., Rouy Z., Medigue C., Talla E., RA Sturgis J.N.; RT "Draft Genome Sequence of the Purple Photosynthetic Bacterium RT Phaeospirillum molischianum DSM120, a Particularly Versatile RT Bacterium."; RL J. Bacteriol. 194:3559-3560(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAHP01000001; CCG39693.1; -; Genomic_DNA. DR EnsemblBacteria; CCG39693; CCG39693; PHAMO_10118. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 222 AA; 22772 MW; 36D1CAE2CCD11E52 CRC64; MTLANPSRRL NSTVCGLSAW AGPPLILVTD DVRLPDPLAA AAALPSGSGV LLRHYGDPAR AARAAALAAL CRRRRLVLLV AGDWRLAARL GAAGLHLPEG IARHGVLAPA LGWLRRRHAL LTVAAHSPLA LGRAAALGAD AALVSPVFPS RSHPGAPVVG PLRLGGWRRR ARLPLIALGG VSAATARRLP RGSVCGLAAI EGLSGVSRSG QGERDVLTLG ID // ID H8FSF6_PHAMO Unreviewed; 233 AA. AC H8FSF6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PHAMO_270135; OS Phaeospirillum molischianum DSM 120. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Phaeospirillum. OX NCBI_TaxID=1150626; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 120; RX PubMed=22689244; DOI=10.1128/JB.00605-12; RA Duquesne K., Prima V., Ji B., Rouy Z., Medigue C., Talla E., RA Sturgis J.N.; RT "Draft Genome Sequence of the Purple Photosynthetic Bacterium RT Phaeospirillum molischianum DSM120, a Particularly Versatile RT Bacterium."; RL J. Bacteriol. 194:3559-3560(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAHP01000020; CCG41294.1; -; Genomic_DNA. DR EnsemblBacteria; CCG41294; CCG41294; PHAMO_270135. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 61 65 HMP-PP binding (By similarity). FT REGION 159 161 THZ-P binding (By similarity). FT METAL 94 94 Magnesium (By similarity). FT METAL 113 113 Magnesium (By similarity). FT BINDING 93 93 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 162 162 HMP-PP (By similarity). FT BINDING 189 189 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 233 AA; 25291 MW; A268EE919EC2D846 CRC64; MPRCRHPCFK WQFPPRTPTR STIPPRHSRL YLITPPVIET PAQWVHTLEQ ALDAGDVACL QIRAKGLDDD SLARLVDILR PPAQRRGVAV LLNDRPDLAF ETGCDGVHIG QGDMPYAQAR EAVGPDGIIG VTCHDSRHLA MEAGEAGADY VAFGAFFPTE TKDAPARADL DLLYWWSELF TVPCVAIGGI TVDNCRPLVE AGTDFLAVSS GVWTHPDGPA AAVAAFDRIL TGR // ID H8G1U7_PEDPE Unreviewed; 216 AA. AC H8G1U7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PCPN_1240; OS Pediococcus pentosaceus IE-3. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=1133596; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IE-3; RA Midha S., Ranjan M., Sharma V., Kumari A., Singh P.K., Korpole S., RA Patil P.B.; RT "Genome Sequence of Pediococcus pentosaceus Strain IE-3."; RL J. Bacteriol. 194:4468-4468(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IE-3; RA Patil P.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAHU01000010; CCG90614.1; -; Genomic_DNA. DR EnsemblBacteria; CCG90614; CCG90614; PCPN_1240. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23380 MW; BD6B2B6ABFB05DF0 CRC64; MKFNSDMLKI YFVAGTQDVA NKADFLPKVE EILQAGATAF QLREKGYNSI DNPAELTELA EKCHQLTQKY HVPFFIDDDV DLALAIHAEG IHVGQKDEKI ESVLKRVQGS MIVGLSCNTE AQVKQANQLD GIDYLGTGTV FETTSKADAG AALGVAKLQE LVELSRYPIV AIGGITLDNL PETMATGVKG FAAISMFTQM TAVPTQMQKI KAIVKG // ID H8G4P0_9PSEU Unreviewed; 229 AA. AC H8G4P0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SacazDRAFT_02232; OS Saccharomonospora azurea NA-128. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882081; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NA-128; RX PubMed=22768365; DOI=10.4056/sigs.2635833; RA Klenk H.P., Held B., Lucas S., Lapidus A., Copeland A., Hammon N., RA Pitluck S., Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., RA Land M., Ivanova N., Rohde M., Goker M., Detter J.C., Kyrpides N.C., RA Woyke T.; RT "Genome sequence of the soil bacterium Saccharomonospora azurea type RT strain (NA-128(T))."; RL Stand. Genomic Sci. 6:220-229(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001466; EHY89143.1; -; Genomic_DNA. DR EnsemblBacteria; EHY89143; EHY89143; SacazDRAFT_02232. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 185 185 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 23818 MW; E441FBBB7EC9C0B0 CRC64; MPGLDGDQIR KRLDDARLYL CTDARSERGD LAEFVDAALA GGVDIVQLRD KTGGAPLEAA HEIAALEVLA EACARHGALL AVNDRADVAL AVDADVLHLG QDDLPVATAR RIVGDAPVIG RSTHSPAQAR AAATEPGVDY FCVGPCWPTP TKPGRAAPGL DLVRTVATEI DPGLGTTRPW FAIGGIDLDR LDDVVAAGAR RAVVVRAITE ADDPTAAARA LREGLTRAG // ID H8GI75_METAL Unreviewed; 316 AA. AC H8GI75; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 22-JAN-2014, entry version 12. DE SubName: Full=Mutator mutT protein; GN ORFNames=Metal_2500; OS Methylomicrobium album BG8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomicrobium. OX NCBI_TaxID=686340; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BG8; RX PubMed=23580712; RA Kits K.D., Kalyuzhnaya M.G., Klotz M.G., Jetten M.S., RA Op den Camp H.J., Vuilleumier S., Bringel F., Dispirito A.A., RA Murrell J.C., Bruce D., Cheng J.F., Copeland A., Goodwin L., RA Hauser L., Lajus A., Land M.L., Lapidus A., Lucas S., Medigue C., RA Pitluck S., Woyke T., Zeytun A., Stein L.Y.; RT "Genome Sequence of the Obligate Gammaproteobacterial Methanotroph RT Methylomicrobium album Strain BG8."; RL Genome Announc. 1:E0017013-E0017013(2013). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001475; EIC30219.1; -; Genomic_DNA. DR EnsemblBacteria; EIC30219; EIC30219; Metal_2500. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01401; MUTATORMUTT. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 316 AA; 34484 MW; 5FCA0795F8895E5F CRC64; MNHFRTTAQK FLQVAAGVIK NADGRILIAR RDESLHQGGL WEFPGGKIEA GETPEQALFR ELKEELDIDT LSAAPLITIH HRYPDRDVTL RVFLVDRFSG TAKGCQEQPI RWVEPNELNR FAFPAANRPI IAAAQLPPFY AILDDQVSSN PMEDLHKLLA QGIDLIQARL KTSPHDRIDE FLAIASPLCS KHGAALLINS AVDFGQHRTH GLHLTARDLL ALSERPSGYR WIGASCHNLQ ELEHAQKIGA DFAVLAPVLP TLTHPETAAL GWKRFAALAE GSNIPVYALG GLTKKDLSAA RDAGAQGIAG ISAFLG // ID H8GQG7_METAL Unreviewed; 206 AA. AC H8GQG7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Metal_2034; OS Methylomicrobium album BG8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomicrobium. OX NCBI_TaxID=686340; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BG8; RX PubMed=23580712; RA Kits K.D., Kalyuzhnaya M.G., Klotz M.G., Jetten M.S., RA Op den Camp H.J., Vuilleumier S., Bringel F., Dispirito A.A., RA Murrell J.C., Bruce D., Cheng J.F., Copeland A., Goodwin L., RA Hauser L., Lajus A., Land M.L., Lapidus A., Lucas S., Medigue C., RA Pitluck S., Woyke T., Zeytun A., Stein L.Y.; RT "Genome Sequence of the Obligate Gammaproteobacterial Methanotroph RT Methylomicrobium album Strain BG8."; RL Genome Announc. 1:E0017013-E0017013(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001475; EIC29794.1; -; Genomic_DNA. DR EnsemblBacteria; EIC29794; EIC29794; Metal_2034. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22002 MW; C634FF3A3801C761 CRC64; MRFPPRGLYA ITQTDGKSPA TVIAEIEAAI RGGAVVVQYR DKHPHDALTL ARELVKVCHR HRVPLLINDN IELTLEAGAD GVHLGKNDGH IREARERLGT DAIIGISCYD SLERALEAQA HGATYAAFGR FFPSGTKPLA SPAHPDTLRQ AKQALSIPIV AIGGILPENG AALLAAGADL LAVIGGIFDH DPELSAHAYQ RLFDSQ // ID H8H453_HELPX Unreviewed; 216 AA. AC H8H453; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HPELS_02300; OS Helicobacter pylori ELS37. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1055527; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ELS37; RA Bertoli M.T., Kersulyte D., Pascasio M.A., Berg D.E.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002953; AFF20020.1; -; Genomic_DNA. DR RefSeq; YP_005424596.1; NC_017063.1. DR EnsemblBacteria; AFF20020; AFF20020; HPELS_02300. DR GeneID; 12019719; -. DR KEGG; hpe:HPELS_02300; -. DR KO; K00788; -. DR BioCyc; HPYL1055527:GLEB-452-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23633 MW; C141DE2ECD50B65E CRC64; MFDANCLKLM FVAGSQDFYH IKGDRTNALL DTLELALKSQ ITAFQFRQKG DLALQDPVEI KQLALECQKL CQKYGAPFIV NDETQLALEL KADGVHVGQE DMVIEEVVTL CKKRLFIGLS VNTLEQALKA RHLDGVAYLG VGPIFPTPSK KDAKEVVGVE LLKKIRDSGV KKPLIAIGGI TIHNASKLCE YGGIAVISAI TQAKDKALVI ETLLKK // ID H8HIV3_MYCTX Unreviewed; 222 AA. AC H8HIV3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 14-MAY-2014, entry version 17. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MRGA327_02630; OS Mycobacterium tuberculosis RGTB327. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1091500; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RGTB327; RX PubMed=22843573; DOI=10.1128/JB.00453-12; RA Madhavilatha G.K., Joseph B.V., Paul L.K., Kumar R.A., Hariharan R., RA Mundayoor S.; RT "Whole-Genome Sequences of Two Clinical Isolates of Mycobacterium RT tuberculosis from Kerala, South India."; RL J. Bacteriol. 194:4430-4430(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RGTB327; RA Madhavilatha K.G., Joseph B.V., Paul L.K., Kumar A.R., Hariharan R., RA Mundayoor S.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003233; AFE15392.1; -; Genomic_DNA. DR ProteinModelPortal; H8HIV3; -. DR SMR; H8HIV3; 1-221. DR EnsemblBacteria; AFE15392; AFE15392; MRGA327_02630. DR OMA; YEVINRS; -. DR BioCyc; MTUB1091500:GLGW-401-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID H8HZH2_MYCTX Unreviewed; 222 AA. AC H8HZH2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 14-MAY-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MRGA423_02605; OS Mycobacterium tuberculosis RGTB423. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1091501; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RGTB423; RX PubMed=22843573; DOI=10.1128/JB.00453-12; RA Madhavilatha G.K., Joseph B.V., Paul L.K., Kumar R.A., Hariharan R., RA Mundayoor S.; RT "Whole-Genome Sequences of Two Clinical Isolates of Mycobacterium RT tuberculosis from Kerala, South India."; RL J. Bacteriol. 194:4430-4430(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RGTB423; RA Madhavilatha K.G., Joseph B.V., Paul L.K., Kumar A.R., Hariharan R., RA Mundayoor S.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003234; AFE11745.1; -; Genomic_DNA. DR ProteinModelPortal; H8HZH2; -. DR SMR; H8HZH2; 1-221. DR EnsemblBacteria; AFE11745; AFE11745; MRGA423_02605. DR OMA; YEVINRS; -. DR BioCyc; MTUB1091501:GLGZ-376-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID H8I6Y5_METCZ Unreviewed; 218 AA. AC H8I6Y5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mtc_1059; OS Methanocella conradii (strain DSM 24694 / JCM 17849 / CGMCC 1.5162 / OS HZ254). OC Archaea; Euryarchaeota; Methanomicrobia; Methanocellales; OC Methanocellaceae; Methanocella. OX NCBI_TaxID=1041930; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 24694 / JCM 17849 / CGMCC 1.5162 / HZ254; RX PubMed=22493204; DOI=10.1128/JB.00207-12; RA Lu Z., Lu Y.; RT "Complete genome sequence of a thermophilic methanogen, Methanocella RT conradii HZ254, isolated from Chinese rice field soil."; RL J. Bacteriol. 194:2398-2399(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003243; AFC99815.1; -; Genomic_DNA. DR RefSeq; YP_005380334.1; NC_017034.1. DR EnsemblBacteria; AFC99815; AFC99815; Mtc_1059. DR GeneID; 11971184; -. DR KEGG; mez:Mtc_1059; -. DR KO; K00788; -. DR OMA; GLGPICH; -. DR BioCyc; MCON1041930:GLGC-1084-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 22365 MW; 095DA0EEC0385E28 CRC64; MSRTLRYDLY VITDEALSHG LSHVEIARRA VEGGADVIQL RDKGMSGKGL TKCALEIREV TRKAGALFIV NDRLDVALAS GADGVHLGQD DIPASSARAI SPPGFIIGVS VGNVEEAVQA ERDGADYVGL GPICHTASKS DAGPACGFDV IASVKKAVSI PVVAIGGLGP QNAGKAIEAG ADGIAVISAV VGQADIAGAA RRLKYIIVEA KHRKGYQG // ID H8IBS5_PASMH Unreviewed; 221 AA. AC H8IBS5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PMCN06_1924; OS Pasteurella multocida (strain HN06). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=1132496; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HN06; RA Liu W., Xu Z., Liang W., Wu B.; RT "Complete genome sequence of Pasteurella multocida HN06, a toxigenic RT strain of serogroup D."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003313; AFF25150.1; -; Genomic_DNA. DR RefSeq; YP_005364321.1; NC_017027.1. DR EnsemblBacteria; AFF25150; AFF25150; PMCN06_1924. DR GeneID; 11961042; -. DR KEGG; pmv:PMCN06_1924; -. DR KO; K00788; -. DR BioCyc; PMUL1132496:GLIB-1969-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23678 MW; ADC6E7ECF5E63FB2 CRC64; MKPVHAFMRL YFIAGTQDCL HLDGDPAQNL LNILQQALQS GITCYQFREK GKKALQDPDK IKALAIQCRD LCRQYQVPFV VNDDVQLAID IGADGIHVGQ TDMAVADVAA LCHSHCFIGT SVNTLEQGIA AQANPLIDYF GTGPIFPTQS KEDPKPVVGV DFVSTIRAHG IDKPIVAIGG VTAQTAEELR QRGANGVAVI SAITQSADIA KTVKELLGNA Q // ID H8IV74_MYCIA Unreviewed; 223 AA. AC H8IV74; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=OCU_46320; OS Mycobacterium intracellulare (strain ATCC 13950 / DSM 43223 / JCM 6384 OS / NCTC 13025 / 3600). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=487521; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600; RX PubMed=22535933; DOI=10.1128/JB.00295-12; RA Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., RA Kook Y.H., Kim B.J.; RT "Complete genome sequence of Mycobacterium intracellulare strain ATCC RT 13950T."; RL J. Bacteriol. 194:2750-2750(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003322; AFC45851.1; -; Genomic_DNA. DR RefSeq; YP_005340172.1; NC_016946.1. DR ProteinModelPortal; H8IV74; -. DR EnsemblBacteria; AFC45851; AFC45851; OCU_46320. DR GeneID; 11911395; -. DR KEGG; mia:OCU_46320; -. DR KO; K00788; -. DR BioCyc; MINT487521:GLGN-4679-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23111 MW; 77A3920AAF0A496E CRC64; MDRRLSVLAT ARLYLCTDAR RERGDLAEFA DAALAGGVDI IQLRDKGSAG EQRFGPLEAR EELAACEILA DAARRHGALF AVNDRADIAR AAGADVLHLG QGDLPLDVAR DIVGPDVLLG LSSHSADQAG AAAVSEADYF CVGPCWPTPT KPDRAAPGLG LVRAAAGLGT DKPWFAIGGI DAQRLPEVLD SGARRVVVVR AITAASDPRA AARRLSSALA AAS // ID H8J581_MYCIT Unreviewed; 223 AA. AC H8J581; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=OCO_46610; OS Mycobacterium intracellulare MOTT-02. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=1138382; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MOTT-02; RX PubMed=22535946; DOI=10.1128/JB.00365-12; RA Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., RA Kook Y.H., Kim B.J.; RT "Complete Genome Sequence of Mycobacterium intracellulare Clinical RT Strain MOTT-02."; RL J. Bacteriol. 194:2771-2771(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MOTT-02; RA Kim B.-J., Lee J.H., Lim J.-S., Choi I.-Y., Choi B.-S., Lim J.-S.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003323; AFC51024.1; -; Genomic_DNA. DR RefSeq; YP_005345345.1; NC_016947.1. DR EnsemblBacteria; AFC51024; AFC51024; OCO_46610. DR GeneID; 11906225; -. DR KEGG; mit:OCO_46610; -. DR KO; K00788; -. DR BioCyc; MINT1138382:GLGO-4708-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23083 MW; 6CBC820AAF155966 CRC64; MDRRLSVLAT ARLYLCTDAR RERGDLAEFA DAALAGGVDI IQLRDKGSAG EQRFGPLEAR EELAACEILA DAARRHGALF AVNDRADIAR AAGADALHLG QGDLPLDVAR DIVGPDVLLG LSSHSADQAG AAAVSEADYF CVGPCWPTPT KPDRAAPGLG LVRAAAGLGT DKPWFAIGGI DAQRLPEVLD SGARRVVVVR AITAASDPRA AARRLSSALA AAS // ID H8JJ98_MYCIT Unreviewed; 223 AA. AC H8JJ98; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=OCQ_47650; OS Mycobacterium intracellulare MOTT-64. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=1138383; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MOTT-64; RX PubMed=22628501; DOI=10.1128/JB.00471-12; RA Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Kook Y.H., Kim B.J.; RT "Complete Genome Sequence of Mycobacterium intracellulare Clinical RT Strain MOTT-64, Belonging to the INT1 Genotype."; RL J. Bacteriol. 194:3268-3268(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MOTT-64; RA Kim B.-J., Lee J.H., Lim J.-S., Choi I.-Y., Choi B.-S., Lim J.-S.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003324; AFC56277.1; -; Genomic_DNA. DR RefSeq; YP_005350598.1; NC_016948.1. DR ProteinModelPortal; H8JJ98; -. DR EnsemblBacteria; AFC56277; AFC56277; OCQ_47650. DR GeneID; 11901030; -. DR KEGG; mir:OCQ_47650; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23111 MW; 77A3920AAF0A496E CRC64; MDRRLSVLAT ARLYLCTDAR RERGDLAEFA DAALAGGVDI IQLRDKGSAG EQRFGPLEAR EELAACEILA DAARRHGALF AVNDRADIAR AAGADVLHLG QGDLPLDVAR DIVGPDVLLG LSSHSADQAG AAAVSEADYF CVGPCWPTPT KPDRAAPGLG LVRAAAGLGT DKPWFAIGGI DAQRLPEVLD SGARRVVVVR AITAASDPRA AARRLSSALA AAS // ID H8JUH7_VIBCL Unreviewed; 440 AA. AC H8JUH7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=O3Y_00290; OS Vibrio cholerae IEC224. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1134456; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IEC224; RX PubMed=22535947; DOI=10.1128/JB.00300-12; RA Morais L.L., Garza D.R., Loureiro E.C., Nunes K.N., Vellasco R.S., RA da Silva C.P., Nunes M.R., Thompson C.C., Vicente A.C., Santos E.C.; RT "Complete Genome Sequence of a Sucrose-Nonfermenting Epidemic Strain RT of Vibrio cholerae O1 from Brazil."; RL J. Bacteriol. 194:2772-2772(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IEC224; RX PubMed=22662140; DOI=10.1371/journal.pone.0037283; RA Garza D.R., Thompson C.C., Loureiro E.C., Dutilh B.E., Inada D.T., RA Junior E.C., Cardoso J.F., Nunes M.R., de Lima C.P., Silvestre R.V., RA Nunes K.N., Santos E.C., Edwards R.A., Vicente A.C., RA de Sa Morais L.L.; RT "Genome-Wide Study of the Defective Sucrose Fermenter Strain of Vibrio RT cholerae from the Latin American Cholera Epidemic."; RL PLoS ONE 7:E37283-E37283(2012). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IEC224; RA Garza D.R.Jr., Thompson C.C., Loureiro E.C.B., Dutilh B.E., RA Inada D.T., Junior E.C.S., Cardoso J.F., Nunes M.R.T., de Lima C.P.S., RA Vellasco R.S., Nunes K.N.B., Santos E.C.O., Edwards R.A., RA Vicente A.C.P., Morais L.L.C.S.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003330; AFC56947.1; -; Genomic_DNA. DR RefSeq; YP_005331935.1; NC_016944.1. DR ProteinModelPortal; H8JUH7; -. DR EnsemblBacteria; AFC56947; AFC56947; O3Y_00290. DR GeneID; 11912999; -. DR KEGG; vci:O3Y_00290; -. DR KO; K00788; -. DR BioCyc; VCHO1134456:GLMN-64-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID H8KKZ4_SOLCM Unreviewed; 210 AA. AC H8KKZ4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 14-MAY-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Solca_3812; OS Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / OS NCIMB 12057 / USAM 9D) (Flexibacter canadensis). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Solitalea. OX NCBI_TaxID=929556; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., RA Kopitz M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Solitalea canadensis DSM 3403."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003349; AFD08811.1; -; Genomic_DNA. DR RefSeq; YP_006257987.1; NC_017770.1. DR EnsemblBacteria; AFD08811; AFD08811; Solca_3812. DR GeneID; 12906322; -. DR KEGG; scn:Solca_3812; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; SCAN929556:GLKC-3813-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). SQ SEQUENCE 210 AA; 23188 MW; 71CFBB1D1D093BC9 CRC64; MNKFPYRLYL VTDMKACLGR DLLWVTEEAV KGGVDVVQIR EKEISDKEFL GKAIQLKEML DHYKVPLIVN DRLAIAMKCR AAGIHVGVND LSPLTIKEQW DTCEILGYSL EWIEQLKSNE VAASDYIALS PVFSTTTKTN TITEWGLEGV QKVRGLTEKP IVAIGNMNKG NISAVIKSGA DCISVVSAIC SANEPYRAAA EIRALIEQSL // ID H8KLH8_SOLCM Unreviewed; 204 AA. AC H8KLH8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 11-DEC-2013, entry version 14. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Solca_3868; OS Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / OS NCIMB 12057 / USAM 9D) (Flexibacter canadensis). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Solitalea. OX NCBI_TaxID=929556; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., RA Kopitz M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Solitalea canadensis DSM 3403."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003349; AFD08865.1; -; Genomic_DNA. DR RefSeq; YP_006258041.1; NC_017770.1. DR EnsemblBacteria; AFD08865; AFD08865; Solca_3868. DR GeneID; 12906379; -. DR KEGG; scn:Solca_3868; -. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR BioCyc; SCAN929556:GLKC-3869-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 204 AA; 23466 MW; 1F59B7315740579C CRC64; MFKLFVISPE ETKNHEAKIF TSLLNEGVHY IYLRKRADYS IDAIKELVEN IPVDLHPRII VSSSHYTLKR EFAVQLHLKG IDRNKLAVGN NWFSTSVHSV NDWLNLKEQY NYTFLSPVFN SISKANYYSA FNLRELTKEI RQHKFEKDNL SKLVALGGID AESITKLKNS GFDGAAILGS IWQSKDPVEA FKQIRKALNE AFQE // ID H8KLI2_SOLCM Unreviewed; 217 AA. AC H8KLI2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 14-MAY-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Solca_3872; OS Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / OS NCIMB 12057 / USAM 9D) (Flexibacter canadensis). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Solitalea. OX NCBI_TaxID=929556; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., RA Kopitz M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Solitalea canadensis DSM 3403."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003349; AFD08869.1; -; Genomic_DNA. DR RefSeq; YP_006258045.1; NC_017770.1. DR EnsemblBacteria; AFD08869; AFD08869; Solca_3872. DR GeneID; 12906383; -. DR KEGG; scn:Solca_3872; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR BioCyc; SCAN929556:GLKC-3873-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 125 127 THZ-P binding (By similarity). FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23911 MW; E86E1892F2876A51 CRC64; MKIDKLQYIC TTAAQAEDAC RSGIKWIQLR LKNTPFPEWK QVALDIQAVC KKYGATFIVN DHVHLAKEIN ADGVHLGKED MPPAEAREIL GDAFIIGSTA NTIEDIEQLT VALPDYIGLG PYRFTSTKEK LSPILGLNGY QTILKRCEER KIHIPVIAIG GLQPEDLPDL MKTGVWGIAV SGTITHAENR EVLIKKLLAL STTTELLTVH PSETPTT // ID H8KSI8_SOLCM Unreviewed; 212 AA. AC H8KSI8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Solca_3535; OS Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / OS NCIMB 12057 / USAM 9D) (Flexibacter canadensis). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Solitalea. OX NCBI_TaxID=929556; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., RA Kopitz M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Solitalea canadensis DSM 3403."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003349; AFD08539.1; -; Genomic_DNA. DR RefSeq; YP_006257715.1; NC_017770.1. DR EnsemblBacteria; AFD08539; AFD08539; Solca_3535. DR GeneID; 12906043; -. DR KEGG; scn:Solca_3535; -. DR KO; K00788; -. DR OMA; GAKWIQY; -. DR BioCyc; SCAN929556:GLKC-3536-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23743 MW; 61AD68C173E5D596 CRC64; MKKHIEKFHY LTLDMENFSH LQQAEMACKA GAKWIQYRTK NKRSTEAWIV EATQIANICD DWGATLIVCS NVDVVEKVDD AQGVHIEMAD MSVEQAREIL GDAKIIGGSA HTFEQIKAVY HSGADYVGVG PYKPTKTIMY SVDHLTLDDY RNIIERMKEE GIDLPVIAAG GIKPEHVDEL MKTGIHGVAV CSAINLAENP EAVYKEIYKK LY // ID H8L4F5_FRAAD Unreviewed; 315 AA. AC H8L4F5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 14-MAY-2014, entry version 12. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Fraau_1170; OS Frateuria aurantia (strain ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB OS 13370) (Acetobacter aurantius). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Frateuria. OX NCBI_TaxID=767434; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB 13370; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., RA Teshima H., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "The complete genome of Frateuria aurantia DSM 6220."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003350; AFC85629.1; -; Genomic_DNA. DR RefSeq; YP_005377311.1; NC_017033.1. DR EnsemblBacteria; AFC85629; AFC85629; Fraau_1170. DR GeneID; 11969056; -. DR KEGG; fau:Fraau_1170; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR BioCyc; FAUR767434:GLDK-1170-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 315 AA; 33807 MW; D180FEBCD1BF4AE5 CRC64; MHVVAAILKD AAGRVLLAQR PPGKHLAGQW EFAGGKLEPG EGRLQGLVRE IEEELGVTVQ AAHPWIWLPW RYGDRSLQLD VWMVDSWQGL PRGREGQAIA WRDPASMDPG LMAGADRMVL RRLQLPPRYL ITSAEAAPQD RPRIERQLRE WLAGGQSLIQ LRLPLWSVAQ IRALAAELLP VARSVGASLL LNADVEGARM LGAGTGVQLR SSQLAQWSQR PLPWGQRVGA SCHDVDELAA AVALDVDFAT LSPVRATASH PGVPGMGWER FAEQVAAAAV PVYALGGVGP DDGARAAEAG AQGVAGIRAF VDRGD // ID H8L691_FRAAD Unreviewed; 204 AA. AC H8L691; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 14-MAY-2014, entry version 12. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Fraau_1518; OS Frateuria aurantia (strain ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB OS 13370) (Acetobacter aurantius). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Frateuria. OX NCBI_TaxID=767434; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB 13370; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., RA Teshima H., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "The complete genome of Frateuria aurantia DSM 6220."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003350; AFC85937.1; -; Genomic_DNA. DR RefSeq; YP_005377619.1; NC_017033.1. DR EnsemblBacteria; AFC85937; AFC85937; Fraau_1518. DR GeneID; 11969403; -. DR KEGG; fau:Fraau_1518; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; FAUR767434:GLDK-1517-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 204 AA; 22146 MW; D6B9513D4D3467E7 CRC64; MIVLPRFYPL TDSAAGVERL AAAGARLIQL RIKSASHATL RQEVLASQAS CRRHGAGLVL NDYWALAIEL GVEWVHLGQE DLDQADWSAC RRCGLKLGLS THDDAELERA LAHAPDYLAL GPVWPSRLKP MHWAAQGVER IAEWKRRVGE RPLVAIGGIT LERAPICLAA GADVLAVSTD ISAASDPAAR TRDWVRLVQR APAA // ID H8LJU5_STRET Unreviewed; 209 AA. AC H8LJU5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MYY_0754; OS Streptococcus pneumoniae (strain ST556). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1130804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST556; RX PubMed=22628517; DOI=10.1128/JB.00363-12; RA Li G., Hu F.Z., Yang X., Cui Y., Yang J., Qu F., Gao G.F., Zhang J.R.; RT "Complete Genome Sequence of Streptococcus pneumoniae Strain ST556, a RT Multidrug-Resistant Isolate from an Otitis Media Patient."; RL J. Bacteriol. 194:3294-3295(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003357; AFC94415.1; -; Genomic_DNA. DR RefSeq; YP_006252950.1; NC_017769.1. DR ProteinModelPortal; H8LJU5; -. DR EnsemblBacteria; AFC94415; AFC94415; MYY_0754. DR GeneID; 12900188; -. DR KEGG; snd:MYY_0754; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR BioCyc; SPNE1130804:GLLC-758-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23272 MW; BD5FCF4748E2F661 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID H8LJV2_STRET Unreviewed; 192 AA. AC H8LJV2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=MYY_0761; OS Streptococcus pneumoniae (strain ST556). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1130804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST556; RX PubMed=22628517; DOI=10.1128/JB.00363-12; RA Li G., Hu F.Z., Yang X., Cui Y., Yang J., Qu F., Gao G.F., Zhang J.R.; RT "Complete Genome Sequence of Streptococcus pneumoniae Strain ST556, a RT Multidrug-Resistant Isolate from an Otitis Media Patient."; RL J. Bacteriol. 194:3294-3295(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003357; AFC94422.1; -; Genomic_DNA. DR RefSeq; YP_006252957.1; NC_017769.1. DR EnsemblBacteria; AFC94422; AFC94422; MYY_0761. DR GeneID; 12900195; -. DR KEGG; snd:MYY_0761; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; SPNE1130804:GLLC-765-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 117 119 THZ-P binding (By similarity). FT METAL 53 53 Magnesium (By similarity). FT METAL 72 72 Magnesium (By similarity). FT BINDING 52 52 HMP-PP (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 147 147 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 192 AA; 20566 MW; 06E056B1121AD04F CRC64; MESFLAKVET ACRSGVTIVQ LREKNLTTNQ YYQLAKQVKE ITDAYQVPLI IDDRLDVCLA VDAAGLHIGD DELPVSVARQ VLGPEKILGV TAKTVKRALE AEKSGADYLG TGAIFPTTTK ENAPITLIST LKTICQTVAI PIVAIGGLTS ENIDQLMGTG IAGVAVVRDL MQAEDIEAKT QAFLTKLHDI LS // ID H8M267_SALTM Unreviewed; 211 AA. AC H8M267; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=UMN798_4510; OS Salmonella enterica subsp. enterica serovar Typhimurium str. 798. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1008297; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=798; RX PubMed=22937065; DOI=10.1371/journal.pone.0043592; RA Patterson S.K., Borewicz K., Johnson T., Xu W., Isaacson R.E.; RT "Characterization and Differential Gene Expression between Two RT Phenotypic Phase Variants in Salmonella enterica Serovar RT Typhimurium."; RL PLoS ONE 7:E43592-E43592(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003386; AFD60974.1; -; Genomic_DNA. DR RefSeq; YP_005399439.1; NC_017046.1. DR ProteinModelPortal; H8M267; -. DR EnsemblBacteria; AFD60974; AFD60974; UMN798_4510. DR BioCyc; SENT1008297:GLJT-4062-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22983 MW; 803CF861FC550D88 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE SGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID H8MPF5_CORCM Unreviewed; 219 AA. AC H8MPF5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=COCOR_02402; OS Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 OS / M2) (Myxococcus coralloides). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Corallococcus. OX NCBI_TaxID=1144275; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2; RA Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., RA Sogaard-Andersen L.; RT "Genome sequence of the fruiting myxobacterium Corallococcus RT coralloides DSM 2259."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003389; AFE10476.1; -; Genomic_DNA. DR RefSeq; YP_005368389.1; NC_017030.1. DR EnsemblBacteria; AFE10476; AFE10476; COCOR_02402. DR GeneID; 11981565; -. DR KEGG; ccx:COCOR_02402; -. DR KO; K00788; -. DR BioCyc; CCOR1144275:GLBO-2404-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22319 MW; E2FEA37CA8826780 CRC64; MNVSPRPPLP QGPYLLCDDS IRPELPLVDK AGRLLEGGAR VIQLRMKHAP PREALAAARA VVALCRRAGA VCLINDRVDL ALLSDAHGVH VGDEDLPPEA ARELLGPGRY VGVTARGTEG AKAARAAGAD YVGVGPLFGT TTKVVAAPVL GLEAFRRVVA DSPLPVVGIG GVGLSNIASV AATGAHGAAV VSDALLAQDI AERVRQLAAA FDSARGTGL // ID H8N0D2_CORCM Unreviewed; 204 AA. AC H8N0D2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN Name=thiE1; OrderedLocusNames=COCOR_03011; OS Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 OS / M2) (Myxococcus coralloides). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Corallococcus. OX NCBI_TaxID=1144275; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2; RA Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., RA Sogaard-Andersen L.; RT "Genome sequence of the fruiting myxobacterium Corallococcus RT coralloides DSM 2259."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003389; AFE10477.1; -; Genomic_DNA. DR RefSeq; YP_005368987.1; NC_017030.1. DR EnsemblBacteria; AFE10477; AFE10477; COCOR_03011. DR GeneID; 11986835; -. DR KEGG; ccx:COCOR_03011; -. DR KO; K00788; -. DR BioCyc; CCOR1144275:GLBO-3015-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 204 AA; 21710 MW; 5A8220CB5B13D314 CRC64; MPALPRLVVI TDWRLPRARL LTALERALEA GPDVAVQHRH PEASGRLFLE EARLLADVCR GRTLFVNGRL DVALLVGAHL HLPASGPSPR DVRPFLPADR WVSMAVHDAR EAERAVGADL ALVSPVFAPG SKPGDTRDTL GPHGFSVLAE RLPCPALALG GMTPERAREV PGAWGVAVIS AVLEAGDPLA AARALLDACR PPRD // ID H8NQS8_RAHAQ Unreviewed; 217 AA. AC H8NQS8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Q7S_20970; OS Rahnella aquatilis HX2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Rahnella. OX NCBI_TaxID=1151116; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HX2; RX PubMed=23144397; DOI=10.1128/JB.01769-12; RA Guo Y., Jiao Z., Li L., Wu D., Crowley D.E., Wang Y., Wu W.; RT "Draft Genome Sequence of Rahnella aquatilis Strain HX2, a Plant RT Growth-Promoting Rhizobacterium Isolated from Vineyard Soil in RT Beijing, China."; RL J. Bacteriol. 194:6646-6647(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003403; AFE60403.1; -; Genomic_DNA. DR RefSeq; YP_005403970.1; NC_017047.1. DR EnsemblBacteria; AFE60403; AFE60403; Q7S_20970. DR GeneID; 12002652; -. DR KEGG; raa:Q7S_20970; -. DR KO; K00788; -. DR BioCyc; RAQU1151116:GLJ4-4206-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23231 MW; 82F0B08770C9E16D CRC64; MNPSSQSFPA VPFHLGLYPV VDTVEWIARL LDAGVKTLQL RVKDLPDEQA EPAIIDAIAL GKKYQARLFI NDYWRLAVKH QAYGVHLGQE DLDTADLEAI RQAGLRLGVS THDDAEMARA VAVNPSYIAL GHIFPTQTKD MPSAPQGLAE LTRHVKKLDG SFPTVAIGGI SIDRAASVLD CGVGSIAVVS AITQAADWRA ATAQLLALCA SKVPQDA // ID H8W438_MARHY Unreviewed; 222 AA. AC H8W438; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MARHY0542; OS Marinobacter hydrocarbonoclasticus ATCC 49840. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=1163748; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49840; RX PubMed=22689231; DOI=10.1128/JB.00500-12; RA Grimaud R., Ghiglione J.F., Cagnon C., Lauga B., Vaysse P.J., RA Rodriguez-Blanco A., Mangenot S., Cruveiller S., Barbe V., Duran R., RA Wu L.F., Talla E., Bonin P., Michotey V.; RT "Genome Sequence of the Marine Bacterium Marinobacter RT hydrocarbonoclasticus SP17, Which Forms Biofilms on Hydrophobic RT Organic Compounds."; RL J. Bacteriol. 194:3539-3540(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49840; RA Genoscope - CEA; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO203363; CCG94038.1; -; Genomic_DNA. DR RefSeq; YP_005428461.1; NC_017067.1. DR EnsemblBacteria; CCG94038; CCG94038; MARHY0542. DR GeneID; 12921173; -. DR KEGG; mhc:MARHY0542; -. DR KO; K00788; -. DR BioCyc; MHYD1163748:GLG7-538-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23153 MW; 110230D9EAB010DA CRC64; MGTVKSQLRP GLYAITDNRL TPADILIASV EAALAGGARL VQYRDKGSTA SERLVQARNL NSLCQGFDVP LLINDDPELA VRVGAAGVHL GQDDCSLVDA RRLLGEHAII GITCHHSLNL AQTAADGGAD YLAFGRFYDS TTKPGAPPAS PDVLTEAKGL GLPITAIGGI TGNNAEALIR AGADLVAVVG GLFGGQPSDI EARARAFHRL FARHHPLFSL SE // ID H8W672_MARHY Unreviewed; 329 AA. AC H8W672; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE SubName: Full=Uncharacterized protein; GN ORFNames=MARHY0804; OS Marinobacter hydrocarbonoclasticus ATCC 49840. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=1163748; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49840; RX PubMed=22689231; DOI=10.1128/JB.00500-12; RA Grimaud R., Ghiglione J.F., Cagnon C., Lauga B., Vaysse P.J., RA Rodriguez-Blanco A., Mangenot S., Cruveiller S., Barbe V., Duran R., RA Wu L.F., Talla E., Bonin P., Michotey V.; RT "Genome Sequence of the Marine Bacterium Marinobacter RT hydrocarbonoclasticus SP17, Which Forms Biofilms on Hydrophobic RT Organic Compounds."; RL J. Bacteriol. 194:3539-3540(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49840; RA Genoscope - CEA; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO203363; CCG94288.1; -; Genomic_DNA. DR RefSeq; YP_005428711.1; NC_017067.1. DR ProteinModelPortal; H8W672; -. DR EnsemblBacteria; CCG94288; CCG94288; MARHY0804. DR GeneID; 12921433; -. DR KEGG; mhc:MARHY0804; -. DR KO; K03574; -. DR BioCyc; MHYD1163748:GLG7-798-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 329 AA; 35048 MW; 4F33DFAB0039FF8B CRC64; MPNTVPESVE GLSANRKTVH VAVGVIVRDG RVLIARRPDK AHQGGLLEFP GGKVEPGETV QQALCREIAE ETGLVLTEDS LEPVIGIRHD YGDKCVFLDV WSSHSAQGEP EGKEGQPVSW LAPEALKDEE FPAANRPIIR ALRLPHRLAV TGTIEDAPAG LARLGAALDR GQPDSLVVLR APTLSGAAYL ELAAAALGGC RERGVGLILH GTADLCRAVP DVQGVHLPWR EAQQHSERPV SDDYWLGVSC HSAEQLRHAE RLEADYVVLG NVLETPSHPG QPGIGWAAFQ ALAATANVPV YGIGGLGPEH QFRARALGGQ GVAGIGFWW // ID H8X1D7_CANO9 Unreviewed; 512 AA. AC H8X1D7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE SubName: Full=Thi6 thiamin-phosphate pyrophosphorylase, hydroxyethylthiazole kinase; GN ORFNames=CORT_0B04690; OS Candida orthopsilosis (strain 90-125) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; OC Candida. OX NCBI_TaxID=1136231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=90-125; RX PubMed=22563396; DOI=10.1371/journal.pone.0035750; RA Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.; RT "Sequence and analysis of the genome of the pathogenic yeast Candida RT orthopsilosis."; RL PLoS ONE 7:E35750-E35750(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE681720; CCG22177.1; -; Genomic_DNA. DR RefSeq; XP_003867614.1; XM_003867566.1. DR GeneID; 14538545; -. DR KEGG; cot:CORT_0B04690; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 512 AA; 55092 MW; 473811DAE8F4DFD8 CRC64; MAVDYSLYLV TDSTMIPSSS TFLKQVEDAV NNGVTLIQLR EKEISTLDFI ERAKEVHKLT KPKNIPLIIN DRVDVALAVD AEGVHVGQDD MPATLARKLL GPNKILGVTC SNPEEVKQVV REGVADYVGL GTTFATNTKK DVKTPGGVGP IGIRKQMHEL SKDIRCVAIG GINHSNANRV IHQCRVGNKR LDGIAVVSCI MASEDAAEAT RTLRAELEYI PDWAVTKLFE KDISVHSIIE NMTGSHPLVH HITNNVVKNF SANVTLAIGA SPIMSELPEE FEEFASGIPN IGLVINLGTP NTELMKVFSK ALTVYNRYNK PIVFDPVACG ASKARLESCR KLLNQGFVTV IKGNVGEIMS IWKLTPYYLE GGDGESQMRG VDSISNAQEA EVTEKGFQVA STFGCTVVIT GKRNYILSSD KRSVVVTGGD PVMGSITGTG CSLGSTIAAF LAAEKANPAV GGDVWKATEV AVRLYNSAGA DAARKSQSPG SFMITFLDKL SELSQNFEAK NT // ID H8XIU3_BACAM Unreviewed; 230 AA. AC H8XIU3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE SubName: Full=Transcriptional regulator TenI; DE EC=2.5.1.3; GN Name=tenI; ORFNames=BANAU_1073; OS Bacillus amyloliquefaciens subsp. plantarum YAU B9601-Y2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1155777; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YAU B9601-Y2; RX PubMed=22628498; DOI=10.1128/JB.00545-12; RA Hao K., He P., Blom J., Rueckert C., Mao Z., Wu Y., He Y., Borriss R.; RT "The Genome of Plant Growth-Promoting Bacillus amyloliquefaciens RT subsp. plantarum Strain YAU B9601-Y2 Contains a Gene Cluster for RT Mersacidin Synthesis."; RL J. Bacteriol. 194:3264-3265(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE774679; CCG49095.1; -; Genomic_DNA. DR RefSeq; YP_005420411.1; NC_017061.1. DR EnsemblBacteria; CCG49095; CCG49095; BANAU_1073. DR GeneID; 12207844; -. DR KEGG; bya:BANAU_1073; -. DR KO; K10810; -. DR BioCyc; BAMY1155777:GL8E-1159-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 230 AA; 25857 MW; 2E2FFB57E999D6AB CRC64; MNINFGEWPI KKKAGPRRAE KRWNLLELHA VTDNRKPVAE LAEDILSIQR EVSFIHIRER DKTAGEIMQL LSLLKKGGAD KDKLIINDRA DIALFANIHR VQLPSRSFSV KQVRSRFPHL HIGRSVHSLK EAIQAEKEDA DYVVFGHVFE TECKQGLEAR GISLLSEIKR TLSIPVIAIG GMTMQTIGHT KQAKPDGIAV MSGIFSAENP EEAAKRYARA VREADYEEAL // ID H8XK54_BACAM Unreviewed; 224 AA. AC H8XK54; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BANAU_3734; OS Bacillus amyloliquefaciens subsp. plantarum YAU B9601-Y2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1155777; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YAU B9601-Y2; RX PubMed=22628498; DOI=10.1128/JB.00545-12; RA Hao K., He P., Blom J., Rueckert C., Mao Z., Wu Y., He Y., Borriss R.; RT "The Genome of Plant Growth-Promoting Bacillus amyloliquefaciens RT subsp. plantarum Strain YAU B9601-Y2 Contains a Gene Cluster for RT Mersacidin Synthesis."; RL J. Bacteriol. 194:3264-3265(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE774679; CCG51755.1; -; Genomic_DNA. DR RefSeq; YP_005423071.1; NC_017061.1. DR EnsemblBacteria; CCG51755; CCG51755; BANAU_3734. DR GeneID; 12207358; -. DR KEGG; bya:BANAU_3734; -. DR KO; K00788; -. DR BioCyc; BAMY1155777:GL8E-3850-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23850 MW; 2AD3E6E42696A96F CRC64; MTRISREMMK DMLSVYFIMG SNNTSADPVS VVKKAIEGGA TLFQFREKGS GSLTGDERVL FAKQVQDVCR QAGIPFIIND DVELALRLEA DGVHIGQDDA DAEETREAIG DMILGVSAHN VSEVKRAEEA GADYVGMGPV YPTETKKDAE AVQGVTLIEE VRRQGITIPI VGIGGITADN AAPVIEAGAD GVSMISAISQ AEDPKAAARK FSEEIRHSKA GLSR // ID H8Z3H1_9GAMM Unreviewed; 333 AA. AC H8Z3H1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 13-NOV-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN ORFNames=Thi970DRAFT_02114; OS Thiorhodovibrio sp. 970. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiorhodovibrio. OX NCBI_TaxID=631362; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=970; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., RA Liu Z., Overmann J., Frigaard N.-U., Bryant D., Woyke T.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH603169; EIC21879.1; -; Genomic_DNA. DR ProteinModelPortal; H8Z3H1; -. DR EnsemblBacteria; EIC21879; EIC21879; Thi970DRAFT_02114. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase; Signal. FT SIGNAL 1 17 Potential. FT CHAIN 18 333 Potential. FT /FTId=PRO_5000879971. SQ SEQUENCE 333 AA; 35173 MW; 76D343064AA50DD7 CRC64; MVGVLHVVAG ALIDAQGRVL IARRPEQVHQ GGRWEFPGGK LEPGESAINA LSRELQEELG IRPRSSRPLI QIEHDYRERR ILLDLYRVSA WDGEPRGCEG QPLAWEFPQA LDPALFPPAD GPAILALRLP ALYLITPPAA PDPTQAGGRA QLPGYLTRLR AALAAGAGAV QLRAHDLSAP AYAALSCAVA PICAAAGVPL VLNRAPEELT KLPADGWHLS SAHLHQLAAR PPQAPSLLGA SCHTEADLCL AARLGLDYAL LSPVQQTRSH PHSHPLGWEG FAQLTRAARL PVYALGGLGP ADLEPAWAHG AQGVAAIGGL WGAQLAEALS LTH // ID H8Z602_9GAMM Unreviewed; 214 AA. AC H8Z602; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Thi970DRAFT_04306; OS Thiorhodovibrio sp. 970. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiorhodovibrio. OX NCBI_TaxID=631362; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=970; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., RA Liu Z., Overmann J., Frigaard N.-U., Bryant D., Woyke T.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH603170; EIC20652.1; -; Genomic_DNA. DR EnsemblBacteria; EIC20652; EIC20652; Thi970DRAFT_04306. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 21869 MW; 3E27C8424EFFDCA5 CRC64; MKPFDLGVYL VTDPHLCGPR GVLATATAAV EGGATMVQLR DKTASDAELI ALGKALKAAI STHAALLIVN DRIDVALAID ADGLHLGQRD ADPAQARARL GTQAIIGLSV ETPALARAAN PELIDYLGVG PVFATATKAD HATPLSFDGL RAICREAPEL PKVAIGGLHA EHAGDVIRAG AQGLAVVSAI FTAGDPQAAA RAIRTQVDLA RAIS // ID H9UZH5_ECOLX Unreviewed; 211 AA. AC H9UZH5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 14-MAY-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=P12B_c4105; OS Escherichia coli P12b. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=910348; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P12b; RX PubMed=22287625; DOI=10.1093/nar/gks040; RA Liu B., Hu B., Zhou Z., Guo D., Guo X., Ding P., Feng L., Wang L.; RT "A novel non-homologous recombination-mediated mechanism for RT Escherichia coli unilateral flagellar phase variation."; RL Nucleic Acids Res. 40:4530-4538(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002291; AFG42918.1; -; Genomic_DNA. DR RefSeq; YP_006171088.1; NC_017663.1. DR ProteinModelPortal; H9UZH5; -. DR SMR; H9UZH5; 20-202. DR EnsemblBacteria; AFG42918; AFG42918; P12B_c4105. DR GeneID; 12757826; -. DR KEGG; elp:P12B_c4105; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; ECOL910348:GI9X-4197-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID H9ZSH1_THETH Unreviewed; 206 AA. AC H9ZSH1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=TtJL18_1397; OS Thermus thermophilus JL-18. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=798128; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JL-18; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lam J., RA McDonald A., Dodsworth J., Hedlund B., Woyke T.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JL-18; RX PubMed=23405355; RA Murugapiran S.K., Huntemann M., Wei C.L., Han J., Detter J.C., RA Han C.S., Erkkila T.H., Teshima H., Chen A., Kyrpides N., RA Mavrommatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Lam J., RA McDonald A.I., Dodsworth J.A., Pati A., Goodwin L., Peters L., RA Pitluck S., Woyke T., Hedlund B.P.; RT "Whole Genome Sequencing of Thermus oshimai JL-2 and Thermus RT thermophilus JL-18, Incomplete Denitrifiers from the United States RT Great Basin."; RL Genome Announc. 1:E00106-E00112(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003252; AFH39281.1; -; Genomic_DNA. DR RefSeq; YP_006059067.1; NC_017587.1. DR EnsemblBacteria; AFH39281; AFH39281; TtJL18_1397. DR GeneID; 12654071; -. DR KEGG; ttl:TtJL18_1397; -. DR KO; K00788; -. DR BioCyc; TTHE798128:GLMF-1396-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22719 MW; 83D1875D7C7A0B5C CRC64; MLGRLYLVVT PRPGWSLEAT LDRTERALAG GVEVVQLRAK DWEARPTLAL GERMLALARR YGVPFFLNDR PDLAALLGAD GVHLGQNDLT PEEARRFFRG MVGRSTHAPE QALRALEEGV DYLSVGPVWE TPTKPGRPAA GLAYVRWAAE NLKEKPWFAI GGIDLENLDQ VLEAGARRIV VVRAILDAPD PEKAAKAFRE RLYGVA // ID I0A3R2_SALET Unreviewed; 211 AA. AC I0A3R2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SU5_0242; OS Salmonella enterica subsp. enterica serovar Heidelberg str. B182. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1160717; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=B182; RX PubMed=22689230; DOI=10.1128/JB.00498-12; RA Le Bars H., Bousarghin L., Bonnaure-Mallet M., Jolivet-Gougeon A., RA Barloy-Hubler F.; RT "Complete Genome Sequence of the Strong Mutator Salmonella enterica RT subsp. enterica Serotype Heidelberg Strain B182."; RL J. Bacteriol. 194:3537-3538(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003416; AFH43619.1; -; Genomic_DNA. DR RefSeq; YP_006085893.1; NC_017623.1. DR ProteinModelPortal; I0A3R2; -. DR EnsemblBacteria; AFH43619; AFH43619; SU5_0242. DR BioCyc; SENT1160717:GLJS-276-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22950 MW; A495042EC6FEDE33 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIDRLADYP TVAIGGISVE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID I0BEW2_9BACL Unreviewed; 237 AA. AC I0BEW2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 2. DT 22-JAN-2014, entry version 15. DE SubName: Full=Regulatory protein; GN ORFNames=B2K_09275; OS Paenibacillus mucilaginosus K02. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=997761; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K02; RA Xiao B., Sun L., Xiao L., Lian B.; RT "Complete genome sequence of Paenibacillus mucilaginosus K02."; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003422; AFH60909.2; -; Genomic_DNA. DR RefSeq; YP_006188674.2; NC_017672.3. DR EnsemblBacteria; AFH60909; AFH60909; B2K_09275. DR GeneID; 12740159; -. DR KEGG; pmw:B2K_09275; -. DR BioCyc; PMUC997761:GLI6-1913-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 237 AA; 24843 MW; 3536BA9D2CD0237F CRC64; MQKGFVRAMT HEHPGAAAPP PAGRTHALHV LTTGRLELDA AASILSIIPA GMIDMLHIRE KHRSAHELAA WYRRLKPLLP PGAALAVNDR LDAALAVRAD AVQLTGASLS PAEARELAPP GRMRIGCSVH SPEEAAEAAA GGADYVLYGH VYETGSKPGL APRGLQALAD TVEACPVPVI AIGGIEPALV DEVLSTGAAG IAVLSSVFGH PDPAGQLRAF RFGLDRTRHK PRKGWTF // ID I0BPT0_9BACL Unreviewed; 214 AA. AC I0BPT0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=B2K_27405; OS Paenibacillus mucilaginosus K02. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=997761; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K02; RA Xiao B., Sun L., Xiao L., Lian B.; RT "Complete genome sequence of Paenibacillus mucilaginosus K02."; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003422; AFH64377.1; -; Genomic_DNA. DR RefSeq; YP_006192142.1; NC_017672.3. DR ProteinModelPortal; I0BPT0; -. DR EnsemblBacteria; AFH64377; AFH64377; B2K_27405. DR GeneID; 12740430; -. DR KEGG; pmw:B2K_27405; -. DR KO; K00788; -. DR BioCyc; PMUC997761:GLI6-5424-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22495 MW; 5CD2F1779A30FAC0 CRC64; MYRSSLHDTL SVYLVTDTAG YEHRSAAEIV RAAVAGGVTL VQLRDKQAQL RDVLPAGREI RELCRSAGIP FVVNDRADLA LLLEADGVHV GQDDLPAQEA RRLLGPDAII GVSAGTMEEA EWAVAQGADY LGVGPVYATA SKKDAGEAIG TDLIARIRSR WPQLPLVGIG GIHQGNAAPV LASGAQGVAV ISAITRQSDP QSAARGLADV CRRR // ID I0C692_STAA5 Unreviewed; 229 AA. AC I0C692; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ST398NM01_2134; OS Staphylococcus aureus subsp. aureus 71193. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1155084; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=71193; RX PubMed=22375071; RA Uhlemann A.C., Porcella S.F., Trivedi S., Sullivan S.B., Hafer C., RA Kennedy A.D., Barbian K.D., McCarthy A.J., Street C., Hirschberg D.L., RA Lipkin W.I., Lindsay J.A., DeLeo F.R., Lowy F.D.; RT "Identification of a highly transmissible animal-independent RT Staphylococcus aureus ST398 clone with distinct genomic and cell RT adhesion properties."; RL MBio 3:e00027-12(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003045; AFH70321.1; -; Genomic_DNA. DR RefSeq; YP_006196164.1; NC_017673.1. DR EnsemblBacteria; AFH70321; AFH70321; ST398NM01_2134. DR GeneID; 12731237; -. DR KEGG; sud:ST398NM01_2134; -. DR KO; K00788; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 56 60 HMP-PP binding (By similarity). FT REGION 155 157 THZ-P binding (By similarity). FT REGION 207 208 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 129 129 HMP-PP (By similarity). FT BINDING 158 158 HMP-PP (By similarity). FT BINDING 187 187 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 25199 MW; 86460FFBE17E260B CRC64; MKQPINNGFA FKRWNSMFNQ SYLNVYFICG TSDVPSHRTI HEVLEAALKA GITLFQFREK GESALKGNDK LVLAKELQHL CHQYDVPFIV NDDVSLAKEI NADGIHVGQD DAKVKEIAQY FTDKIIGLSI SDLGEYAKSD LTHVDYIGVG PIYPTPSKND AHTPVGPEMI ATFKEMNPQL PIVAIGGINT SNVAPIVEAG ANGISVISAI SKSENIEKTV NRFKDFFNN // ID I0CNH9_LISMN Unreviewed; 214 AA. AC I0CNH9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MUO_01765; OS Listeria monocytogenes 07PF0776. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1126011; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=07PF0776; RX PubMed=22689239; DOI=10.1128/JB.00616-12; RA McMullen P.D., Gillaspy A.F., Gipson J., Bobo L.D., Skiest D.J., RA Freitag N.E.; RT "Genome Sequence of Listeria monocytogenes 07PF0776, a Cardiotropic RT Serovar 4b Strain."; RL J. Bacteriol. 194:3552-3552(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003414; AFH78910.1; -; Genomic_DNA. DR RefSeq; YP_006204578.1; NC_017728.1. DR ProteinModelPortal; I0CNH9; -. DR EnsemblBacteria; AFH78910; AFH78910; MUO_01765. DR GeneID; 12793649; -. DR KEGG; lmp:MUO_01765; -. DR KO; K00788; -. DR BioCyc; LMON1126011:GLFQ-337-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22595 MW; 10E4ADFD02F4711D CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAE EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GYPS // ID I0CWL1_BACAN Unreviewed; 219 AA. AC I0CWL1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 14-MAY-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=H9401_0356; OS Bacillus anthracis str. H9401. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=768494; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H9401; RX PubMed=22815438; DOI=10.1128/JB.00159-12; RA Chun J.H., Hong K.J., Cha S.H., Cho M.H., Lee K.J., Jeong D.H., RA Yoo C.K., Rhie G.E.; RT "Complete genome sequence of Bacillus anthracis H9401, an isolate from RT a Korean patient with anthrax."; RL J. Bacteriol. 194:4116-4117(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002091; AFH81742.1; -; Genomic_DNA. DR RefSeq; YP_006207410.1; NC_017729.1. DR ProteinModelPortal; I0CWL1; -. DR SMR; I0CWL1; 1-215. DR EnsemblBacteria; AFH81742; AFH81742; H9401_0356. DR GeneID; 12790015; -. DR KEGG; bax:H9401_0356; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; BANT768494:GL8F-406-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23600 MW; 6D85F0FE3EFD3046 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGFI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWVIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID I0CXK3_BACAN Unreviewed; 208 AA. AC I0CXK3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-APR-2014, entry version 15. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN ORFNames=H9401_0698; OS Bacillus anthracis str. H9401. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=768494; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H9401; RX PubMed=22815438; DOI=10.1128/JB.00159-12; RA Chun J.H., Hong K.J., Cha S.H., Cho M.H., Lee K.J., Jeong D.H., RA Yoo C.K., Rhie G.E.; RT "Complete genome sequence of Bacillus anthracis H9401, an isolate from RT a Korean patient with anthrax."; RL J. Bacteriol. 194:4116-4117(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002091; AFH82084.1; -; Genomic_DNA. DR RefSeq; YP_006207752.1; NC_017729.1. DR EnsemblBacteria; AFH82084; AFH82084; H9401_0698. DR GeneID; 12790399; -. DR KEGG; bax:H9401_0698; -. DR KO; K10810; -. DR BioCyc; BANT768494:GL8F-790-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 23136 MW; D5FD7481E4D90BC3 CRC64; MNMKNELHVI SNGHMSFEEL VSVAMQIESE IDYLHIRERE KSTKELYEGV ESLLKKGFPA SKLVINDRID IAILLNIPRV QLGYRSTDVR SVKEKFSYLH VGYSVHSLEE AIEAFKNGAD SLVYGHVFPT ECKKGVPARG LEEISDIARS LSIPIIAIGG ITPENTKDIL ASEVSGIAVM SGIVSSSNPY SKAKSYKESI RKWAEKHV // ID I0DTA7_PROSM Unreviewed; 212 AA. AC I0DTA7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 14-MAY-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=S70_08565; OS Providencia stuartii (strain MRSN 2154). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Providencia. OX NCBI_TaxID=1157951; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MRSN 2154; RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A., RA Lesho E.P., Waterman P.E.; RT "Complete genome sequence of Providencia stuartii clinical isolate RT MRSN 2154."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003488; AFH93575.1; -; Genomic_DNA. DR RefSeq; YP_006216266.1; NC_017731.1. DR ProteinModelPortal; I0DTA7; -. DR EnsemblBacteria; AFH93575; AFH93575; S70_08565. DR GeneID; 12784434; -. DR KEGG; psi:S70_08565; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR BioCyc; PSTU1157951:GLIN-1703-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23340 MW; 377D1FF142665E6C CRC64; MKKLPSTPFA PTEQRLGLYP VVDSVEWIER LLNAGVTTIQ LRIKDKHDDE VRDDIQQAIA LGEKHHARLF INDYWRLAIE LGAYGVHLGQ EDLETTDLLA IHQAGLRLGI STHDQHELAI AKSVRPSYIA MGHIFPTETK KMPSAPQGLE TLKTMVEATP DYPTVAIGGI SIDRVPAVLA TGVGSVALVS AITKADDWLE ATKTLLRLVE NH // ID I0E4U5_HELPX Unreviewed; 219 AA. AC I0E4U5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HPSH417_04125; OS Helicobacter pylori Shi417. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1163739; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Shi417; RA Kersulyte D., Cabrera L., Pacheco R., Herrera P., Rodriguez C., RA Gilman R.H., Berg D.E.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003472; AFH97963.1; -; Genomic_DNA. DR RefSeq; YP_006224457.1; NC_017739.1. DR EnsemblBacteria; AFH97963; AFH97963; HPSH417_04125. DR GeneID; 12775212; -. DR KEGG; hhr:HPSH417_04125; -. DR KO; K00788; -. DR BioCyc; HPYL1163739:GLEQ-807-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23886 MW; E6924E4E371F129F CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLALQDP IEIKQLALEC QKLCQKYGVP FIVNDEVKLA LELKADGVHV GQEDTAIEEV MALCKKRLFI GLSVNTLEQA LKVRHLDAVA YFGVGPIFPT QSKKDKQVVG VELLKKIKDS GVKKPLVAIG GITVHNASKL REYGGIAVIS AITQAKDKAL AVGKLLNNA // ID I0ECU9_HELPX Unreviewed; 219 AA. AC I0ECU9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HPSH112_02770; OS Helicobacter pylori Shi112. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1163740; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Shi112; RA Kersulyte D., Cabrera L., Pacheco R., Herrera P., Rodriguez C., RA Gilman R.H., Berg D.E.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003474; AFI00768.1; -; Genomic_DNA. DR RefSeq; YP_006227261.1; NC_017741.1. DR EnsemblBacteria; AFI00768; AFI00768; HPSH112_02770. DR GeneID; 12771713; -. DR KEGG; hhp:HPSH112_02770; -. DR KO; K00788; -. DR BioCyc; HPYL1163740:GLEO-536-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23938 MW; C3116E96EAAB8926 CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLSLQDP IEIKQLALKC QKLCQKYGAP FIVNDEVQLA LELKADGVHV GQEDMAIEEV MTLCKKCLFI GLSVNTLEQA LKARHLDGVA YFGVGPIFPT QSKKDKQVVG VELLKKIKDR GIKKPLIAIG GITTHNASKL REYGGIAVIS AITQAKDKAL AVGKLLNDA // ID I0EI10_HELPX Unreviewed; 217 AA. AC I0EI10; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HPPC18_04160; OS Helicobacter pylori PeCan18. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1163742; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PeCan18; RA Kersulyte D., Ramirez Ramos A., Recarvarren S., Barua R.L., RA Watanabe J., Gilman R.H., Berg D.E.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003475; AFI02579.1; -; Genomic_DNA. DR RefSeq; YP_006229072.1; NC_017742.1. DR EnsemblBacteria; AFI02579; AFI02579; HPPC18_04160. DR GeneID; 12770788; -. DR KEGG; hca:HPPC18_04160; -. DR KO; K00788; -. DR BioCyc; HPYL1163742:GLEK-785-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23866 MW; 4BB65F5A35F1C857 CRC64; MFDANCLKLM FVAGSQDFYH IKGDRTNALL DTLELALQSK ITAFQFRQKG DLALQDPVEI KRLALECQKL CKKYGAPFII NDEVRLALEL KADGVHVGQE DMAIEEVITL CQKRLFIGLS VNTLEQALKA RHLDHIAYLG VGPIFPTPSK KDAKEVVGVN LLKKIHDSGV KKPLIAIGGI TTDNASKLWE YGGIAVISAI TQAKDKALAV ERLLKNA // ID I0EK83_HELC0 Unreviewed; 212 AA. AC I0EK83; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HCW_00275; OS Helicobacter cetorum (strain ATCC BAA-429 / MIT 00-7128). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=182217; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-429 / MIT 00-7128; RA Kersulyte D., Berg D.E.; RT "Complete genome sequence of Helicobacter cetorum strain MIT 00- RT 7128."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003479; AFI03352.1; -; Genomic_DNA. DR RefSeq; YP_006221982.1; NC_017737.1. DR EnsemblBacteria; AFI03352; AFI03352; HCW_00275. DR GeneID; 12777006; -. DR KEGG; hce:HCW_00275; -. DR KO; K00788; -. DR BioCyc; HCET182217:GLDW-51-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23484 MW; 9D3A44A5386D8C9F CRC64; MTNLYGIYAI SDESLTPYTT LIAQLKSAIK GGIKIFQLRD KHNNDAKLLP IVQELNALCK QHNVAFFLND RLELAIKAQV FGVHLGKEDA TILQAKKYFK GKIGISCYGS LKEAQKMQDL GASYVAFGAC FNSPSKPLAP IIDLNLLKNA RESLKIPICA IGGITLSLLK THHSLKYAHM LAFISDLWGL KNERSLDEIT NHANQLNQAF NI // ID I0EP30_HELC0 Unreviewed; 195 AA. AC I0EP30; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=HCW_07205; OS Helicobacter cetorum (strain ATCC BAA-429 / MIT 00-7128). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=182217; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-429 / MIT 00-7128; RA Kersulyte D., Berg D.E.; RT "Complete genome sequence of Helicobacter cetorum strain MIT 00- RT 7128."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003479; AFI04699.1; -; Genomic_DNA. DR RefSeq; YP_006223329.1; NC_017737.1. DR EnsemblBacteria; AFI04699; AFI04699; HCW_07205. DR GeneID; 12777238; -. DR KEGG; hce:HCW_07205; -. DR KO; K00788; -. DR BioCyc; HCET182217:GLDW-1417-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 195 AA; 22576 MW; 456A3792A63BB3C1 CRC64; MQGYFIVPPL LYSSNPTKIF IKTLEKIFST HVINKACLRN DCNLIQNYLK PFVEICKTYE VESYINCEEA FLSVKIALDY SFEGVHFKDR FYPNFEPLKR LLNTLKAHNK RCFYSAHSIE CARYMLKNKI DYVTLSPIFL TPNKGKPLGL EVFKHFNDME KSRLFALGGI ITQGQIDCLR GQGIGGFSAI RYFLQ // ID I0ER03_HELCM Unreviewed; 219 AA. AC I0ER03; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HCD_01700; OS Helicobacter cetorum (strain ATCC BAA-540 / MIT 99-5656). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1163745; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-540 / MIT 99-5656; RA Kersulyte D., Berg D.E.; RT "Complete genome sequence of Helicobacter cetorum strain MIT 99- RT 5656."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003481; AFI05372.1; -; Genomic_DNA. DR RefSeq; YP_006220582.1; NC_017735.1. DR EnsemblBacteria; AFI05372; AFI05372; HCD_01700. DR GeneID; 12778432; -. DR KEGG; hcm:HCD_01700; -. DR KO; K00788; -. DR BioCyc; HCET1163745:GLDY-347-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24262 MW; E6BBB0486CF74601 CRC64; MFDVNCLKLM FVAGSQDFYH IKGDRVKSLL YTLELALQSK ITAFQFRQKG DLDLQDNTEI KKLAIECQRL CEKYGVPFII NDDVHLALEL KACGVHIGQE DMALEKAITL CKNRLFIGLS VNTLEQALKV YKMDGVAYLG IGSIFPTQSK KDVKQVVGAD FLKQLQAFKI QKPLVAIGGI TTDNVSELRM CGASGVAVIS AITQARDIST AIREILLNF // ID I0EW80_HELPX Unreviewed; 219 AA. AC I0EW80; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HPB14_02450; OS Helicobacter pylori HUP-B14. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1163743; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HUP-B14; RA Kersulyte D., Berg D.E.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003486; AFI07199.1; -; Genomic_DNA. DR RefSeq; YP_006219219.1; NC_017733.1. DR EnsemblBacteria; AFI07199; AFI07199; HPB14_02450. DR GeneID; 12780290; -. DR KEGG; hcn:HPB14_02450; -. DR KO; K00788; -. DR BioCyc; HPYL1163743:GLEH-488-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23965 MW; F14030480EF52A8F CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLETLELAL QSQITVFQFR QKGDLALQDP VEIKQLALEC QKLCQKYGTP FIVNDEVQLA LELKADGVHV GQEDMAIEEV ITLCKKRLFI GLSVNTLEQA LKARHLDGVA YLGVGPIFPT PSKKDAKEVV GVNLLKKIHD SGVKKPLIAI GGITTDNASK LHEYGGIAVI SAITQAKDKA LAIEKLLKK // ID I0F2V3_9BACI Unreviewed; 205 AA. AC I0F2V3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE SubName: Full=Transcriptional regulator TenI; GN ORFNames=MY9_1271; OS Bacillus sp. JS. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1127744; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JS; RX PubMed=22740679; DOI=10.1128/JB.00676-12; RA Song J.Y., Kim H.A., Kim J.S., Kim S.Y., Jeong H., Kang S.G., RA Kim B.K., Kwon S.K., Lee C.H., Yu D.S., Kim B.S., Kim S.H., Kwon S.Y., RA Kim J.F.; RT "Genome Sequence of the Plant Growth-Promoting Rhizobacterium Bacillus RT sp. Strain JS."; RL J. Bacteriol. 194:3760-3761(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003492; AFI27809.1; -; Genomic_DNA. DR RefSeq; YP_006231065.1; NC_017743.1. DR EnsemblBacteria; AFI27809; AFI27809; MY9_1271. DR GeneID; 12768950; -. DR KEGG; bjs:MY9_1271; -. DR KO; K10810; -. DR BioCyc; BSP1127744:GL8I-1353-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 205 AA; 22986 MW; 0D34D6C0C86FFBA8 CRC64; MELHAITDDS KPVEELARII IKIQNEVDFI HIRERSKSAA DILKLLELIF EGGIDKRKLV MNGRVDIALF STIHRVQLPS TSFSPKQVRA RFPHLHIGRS VHSLEEAVQA EKEDADYVLF GHVFETDCKK GLEGRGVSLL SDIKQRISIP VIAIGGMTPE RLKDVKQAGA DGIAVMSGIF SSAEPLEAAR RYSRKLKEMR YEKAL // ID I0FAF0_9BACI Unreviewed; 222 AA. AC I0FAF0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MY9_3924; OS Bacillus sp. JS. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1127744; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JS; RX PubMed=22740679; DOI=10.1128/JB.00676-12; RA Song J.Y., Kim H.A., Kim J.S., Kim S.Y., Jeong H., Kang S.G., RA Kim B.K., Kwon S.K., Lee C.H., Yu D.S., Kim B.S., Kim S.H., Kwon S.Y., RA Kim J.F.; RT "Genome Sequence of the Plant Growth-Promoting Rhizobacterium Bacillus RT sp. Strain JS."; RL J. Bacteriol. 194:3760-3761(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003492; AFI30456.1; -; Genomic_DNA. DR RefSeq; YP_006233712.1; NC_017743.1. DR EnsemblBacteria; AFI30456; AFI30456; MY9_3924. DR GeneID; 12767275; -. DR KEGG; bjs:MY9_3924; -. DR KO; K00788; -. DR BioCyc; BSP1127744:GL8I-4035-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23762 MW; 29D7E4D328297665 CRC64; MTRISREMMK ELLSVYFIMG SNNTKADPVT VVQKALKGGA TLYQFREKGG DALTGEARAE FAEKVQAACR EAGVPFIVND DVELALKLKA DGIHIGQEDA NAKEVRAAIG DMILGVSAHT MSEVKQAEED GADYVGLGPI YPTETKKDTR AVQGVSLIEA VRRQGISIPI VGIGGITIDN ASPIIQAGAD GVSMISAISQ AEDPEGAARK FHEEIQTYKT RR // ID I0G0M7_9BRAD Unreviewed; 229 AA. AC I0G0M7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=S23_10950; OS Bradyrhizobium sp. S23321. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=335659; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S23321; RX PubMed=22452844; DOI=10.1264/jsme2.ME11321; RA Okubo T., Tsukui T., Maita H., Okamoto S., Oshima K., Fujisawa T., RA Saito A., Futamata H., Hattori R., Shimomura Y., Haruta S., RA Morimoto S., Wang Y., Sakai Y., Hattori M., Aizawa S., RA Nagashima K.V.P., Masuda S., Hattori T., Yamashita A., Bao Z., RA Hayatsu M., Kajiya-Kanegae H., Yoshinaga I., Sakamoto K., Toyota K., RA Nakao M., Kohara M., Anda M., Niwa R., Jung-Hwan P., RA Sameshima-Saito R., Tokuda S., Yamamoto S., Yamamoto S., Yokoyama T., RA Akutsu T., Nakamura Y., Nakahira-Yanaka Y., Takada Hoshino Y., RA Hirakawa H., Mitsui H., Terasawa K., Itakura M., Sato S., RA Ikeda-Ohtsubo W., Sakakura N., Kaminuma E., Minamisawa K.; RT "Complete genome sequence of Bradyrhizobium sp. S23321: insights into RT symbiosis evolution in soil oligotrophs."; RL Microbes Environ. 27:306-315(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012279; BAL74314.1; -; Genomic_DNA. DR RefSeq; YP_005448426.1; NC_017082.1. DR EnsemblBacteria; BAL74314; BAL74314; S23_10950. DR GeneID; 12045730; -. DR KEGG; brs:S23_10950; -. DR KO; K00788; -. DR BioCyc; BSP335659:GL9K-1095-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 229 AA; 23856 MW; 8C78F37F6A3F440A CRC64; MSNKSPPPRP APRLYLATPV VDDPAALQAE LPALLAAADV AAVLLRLKET DQRTMITRIK ALAPVVQKAG AALLVEGHPD LVARGGADGA HLPGIAALKE ALPSLKPDRI AGVGGLTTRH HSMDAGEIGA DYVLFGEPDG KGQRPSSQAI AERLDWWAEL FEPPCVGFAT SLEEAHDFAA SGADFVLVGE FIWADPRGPK AALVEADAAI KKAHATALAE QNPVSGEHG // ID I0G283_9BRAD Unreviewed; 202 AA. AC I0G283; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=S23_16530; OS Bradyrhizobium sp. S23321. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=335659; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=S23321; RX PubMed=22452844; DOI=10.1264/jsme2.ME11321; RA Okubo T., Tsukui T., Maita H., Okamoto S., Oshima K., Fujisawa T., RA Saito A., Futamata H., Hattori R., Shimomura Y., Haruta S., RA Morimoto S., Wang Y., Sakai Y., Hattori M., Aizawa S., RA Nagashima K.V.P., Masuda S., Hattori T., Yamashita A., Bao Z., RA Hayatsu M., Kajiya-Kanegae H., Yoshinaga I., Sakamoto K., Toyota K., RA Nakao M., Kohara M., Anda M., Niwa R., Jung-Hwan P., RA Sameshima-Saito R., Tokuda S., Yamamoto S., Yamamoto S., Yokoyama T., RA Akutsu T., Nakamura Y., Nakahira-Yanaka Y., Takada Hoshino Y., RA Hirakawa H., Mitsui H., Terasawa K., Itakura M., Sato S., RA Ikeda-Ohtsubo W., Sakakura N., Kaminuma E., Minamisawa K.; RT "Complete genome sequence of Bradyrhizobium sp. S23321: insights into RT symbiosis evolution in soil oligotrophs."; RL Microbes Environ. 27:306-315(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012279; BAL74870.1; -; Genomic_DNA. DR RefSeq; YP_005448982.1; NC_017082.1. DR EnsemblBacteria; BAL74870; BAL74870; S23_16530. DR GeneID; 12039991; -. DR KEGG; brs:S23_16530; -. DR KO; K00788; -. DR BioCyc; BSP335659:GL9K-1653-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 202 AA; 21811 MW; 8ED27AF2F278A3B2 CRC64; MPYPDRFYPV VDSLAWVERL TKLGVGTIQL RAKELNDSQA LQLVTDALAI TEGTQAKLVV NDYWRAAIVA GAKYLHLGQE DLAEADLAAI REAGLLLGIS THDDAELETA LAAKPDYVAL GPIFFTTLKS MRFEPQGIPK ITEWKKRIGS IPLVAIGGIK FEHAAEIFAA GADSIAVVSD VTQNADPDAR VRQWLGLSAE AA // ID I0GNI4_SELRL Unreviewed; 200 AA. AC I0GNI4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 12. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=SELR_06130; OS Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / OS TAM6421). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=927704; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 103574 / TAM6421; RA Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., RA Takahashi M., Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., RA Yamazaki S., Fujita N.; RT "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica RT TAM6421."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012292; BAL82321.1; -; Genomic_DNA. DR RefSeq; YP_005432344.1; NC_017068.1. DR EnsemblBacteria; BAL82321; BAL82321; SELR_06130. DR GeneID; 12023618; -. DR KEGG; sri:SELR_06130; -. DR KO; K00788; -. DR BioCyc; SRUM927704:GLJZ-650-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 200 AA; 22082 MW; 7964D619846FBE58 CRC64; MIMSMSDMDW KDILAVTNRH LCTGNFLQQV EKVARRKPKA LILREKDLPE QDYRQLATEV QKICRQYDVP LHLHNFPQAA AGLSAVGLHL PLPKLRERTT EARQRWKVLG TSCHSVAEVQ EAVALGCTYI VAGHIYATDC KRGLPGRGLD FLRAACQAAS TVPVYAIGGI TPERLPAVLA AGAAGACVMS GMMKDSEWWR // ID I0GTQ8_SELRL Unreviewed; 481 AA. AC I0GTQ8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase/hydroxymethylpyrimidine/ phosphomethylpyrimidine kinase; DE EC=2.5.1.3; DE EC=2.7.1.49; DE EC=2.7.4.7; GN Name=thiED; OrderedLocusNames=SELR_24370; OS Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / OS TAM6421). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=927704; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 103574 / TAM6421; RA Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., RA Takahashi M., Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., RA Yamazaki S., Fujita N.; RT "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica RT TAM6421."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012292; BAL84145.1; -; Genomic_DNA. DR RefSeq; YP_005434168.1; NC_017068.1. DR EnsemblBacteria; BAL84145; BAL84145; SELR_24370. DR GeneID; 12025659; -. DR KEGG; sri:SELR_24370; -. DR KO; K14153; -. DR BioCyc; SRUM927704:GLJZ-2511-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 481 AA; 50611 MW; 8E8057AE36E775FD CRC64; MLKAQDLQLY AVTDRRWLRG TSLASAVEQA LQGGVTCVQL REKDLPFAEF LASAREIKAL CQRHHVPFIV DDDLDIALAA DADGLHIGQK DMPAAEARKL LGPDKILGVT AKTVEQAIAA WQAGADYLGS GAVFPTGTKK DTIPLPLTEL QKITAAVPIP VVAIGGIDAG NISQLEGTGI AGVAVVSGIF AQAEIKKAAS DLRQLIPASS KRFAPTFPAR GRLPAVLTIA GSDSSGGAGI QADLKTMLAN GVYGMSAITA LTAQNTTGVT AVAKTEPDIL AAQLDSVFTD IFPDAVKTGM VFDSDLIAVI ADKLTHYQAN NIVIDPVMVA TSGARLLNEN AISALQEKLL PLATLITPNL LEAEVLADRK IHSHEDMVQA AQKLYDRYGC NVLCKGGHRL QDADDLLYTA EGAHWLKAEH IDNPNTHGTG CTLSSAIASQ LAKGETLPRA VQQAKAYITG ALKANLNLGK GSGPLHHGWN L // ID I0GYM1_ACTM4 Unreviewed; 196 AA. AC I0GYM1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AMIS_6380; OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 OS / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Actinoplanes. OX NCBI_TaxID=512565; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / RC NBRC 102363 / 431; RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H., RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.; RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC RT 102363)."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012319; BAL85858.1; -; Genomic_DNA. DR RefSeq; YP_005460374.1; NC_017093.1. DR EnsemblBacteria; BAL85858; BAL85858; AMIS_6380. DR GeneID; 12049565; -. DR KEGG; ams:AMIS_6380; -. DR KO; K00788; -. DR OMA; PRLHVIT; -. DR BioCyc; AMIS512565:GL7J-658-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 128 130 THZ-P binding (By similarity). FT METAL 64 64 Magnesium (By similarity). FT METAL 83 83 Magnesium (By similarity). FT BINDING 63 63 HMP-PP (By similarity). FT BINDING 102 102 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 196 AA; 19560 MW; 950CA185E972EC08 CRC64; MHGSLSFPRL HVITDSLDVV RGVAGQPDVA VQIRVKTSDA QAYALTVAAL EILRPAGTMC LVNDRVAVAL AAGADGVHVG ADDLPVDAAR RILGPDAVIG ATCRNPTDAR AAVAAGASYL GTGPAFATST KDGLPPPIGP AGVAAVVDAV PGTPVLAIGG ITADRVPVLP SHGVAAIGAF VTDPKRAVAE FLEALR // ID I0GYM5_ACTM4 Unreviewed; 200 AA. AC I0GYM5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 14-MAY-2014, entry version 14. DE SubName: Full=Putative thiamine monophosphate synthase; GN Name=thiE2; OrderedLocusNames=AMIS_6420; OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 OS / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Actinoplanes. OX NCBI_TaxID=512565; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / RC NBRC 102363 / 431; RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H., RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.; RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC RT 102363)."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012319; BAL85862.1; -; Genomic_DNA. DR RefSeq; YP_005460378.1; NC_017093.1. DR EnsemblBacteria; BAL85862; BAL85862; AMIS_6420. DR GeneID; 12049569; -. DR KEGG; ams:AMIS_6420; -. DR KO; K00788; -. DR OMA; VMRAEDP; -. DR BioCyc; AMIS512565:GL7J-662-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 200 AA; 19758 MW; E1C200E7472FE90E CRC64; MVTPGGLVVL TDRRSAAGPL VEVVAAAVRG GADWVILRER DLGYEERAAL AAQLRPLLPP GRLIVAGPDP LGGTAVHLSA ADPLPSGVPL VGRSWHGAEP PSDVDYVTLS PIYPTATKPG YGPALGAAGA AALAGRVPWL ALGGVDSAAR AAECARAGAE GIAVLGAIMR AANPARVASE LAGAFAAAQR AAASAGAGAW // ID I0HWW8_RUBGI Unreviewed; 214 AA. AC I0HWW8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=RGE_41690; OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Rubrivivax. OX NCBI_TaxID=983917; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 100245 / IL144; RA Nagashima S., Sekine M., Takami A., Shimizu T., Nakamura S., Aono E., RA Sakamoto K., Nakazawa H., Yamazaki S., Fujita N., Shimada K., RA Hanada S., Nagashima K.; RT "Complete genome sequence of phototrophic betaproteobacterium RT Rubrivivax gelatinosus IL144."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012320; BAL97505.1; -; Genomic_DNA. DR RefSeq; YP_005439004.1; NC_017075.1. DR EnsemblBacteria; BAL97505; BAL97505; RGE_41690. DR GeneID; 12028960; -. DR KEGG; rge:RGE_41690; -. DR KO; K00788; -. DR BioCyc; RGEL983917:GLJR-4221-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22191 MW; C3A36C1684E46FA3 CRC64; MQGWGVEALR LMLVTDETLC GGRSLEAIVA AAVRGGVRCV QLREKRLGTR AFVERARALK ALLAPLRVPL VVNDRVDVAL AIGADGVHLG QSDMPVEDAR RLLPAEVFIG WSVETLDDVR RAAALPLDYL GTSPVFATAT KTDAAPPWGL EGLRAAREAT ALPLVAIGGL HAGNAALAIA HGADSVAVVS AICAAADPEA AARELARVVG EGAR // ID I0I501_CALAS Unreviewed; 215 AA. AC I0I501; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CLDAP_22990; OS Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 / OS STL-6-O1). OC Bacteria; Chloroflexi; Caldilineae; Caldilineales; Caldilineaceae; OC Caldilinea. OX NCBI_TaxID=926550; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1; RA Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S., RA Hanada S., Yamazaki S., Fujita N.; RT "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC RT 102666)."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012337; BAM00339.1; -; Genomic_DNA. DR RefSeq; YP_005442236.1; NC_017079.1. DR EnsemblBacteria; BAM00339; BAM00339; CLDAP_22990. DR GeneID; 12034189; -. DR KEGG; cap:CLDAP_22990; -. DR KO; K00788; -. DR BioCyc; CAER926550:GLA5-2340-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22396 MW; C54D84B40A1F74CF CRC64; MDWSVYVITD RRMAGERDLL AVMQAAIEGG ATVVQLRDKH ATTRELLEFG NALQRLTRSA GIPLIINDRV DIALALDADG VHLGDDDMPP ELARRLIGPD RLLGVSADSE QAARRAEQAG ADYLGVGDIF GTRTKPDAGA PIGLEKLAAI ARSVKIPVVG IGGITLANAP AVIQAGAAGV AVVSAVLGAP EPAAAARALR STLKNSIRKS SQLRL // ID I0I502_CALAS Unreviewed; 211 AA. AC I0I502; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CLDAP_23000; OS Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 / OS STL-6-O1). OC Bacteria; Chloroflexi; Caldilineae; Caldilineales; Caldilineaceae; OC Caldilinea. OX NCBI_TaxID=926550; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1; RA Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S., RA Hanada S., Yamazaki S., Fujita N.; RT "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC RT 102666)."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012337; BAM00340.1; -; Genomic_DNA. DR RefSeq; YP_005442237.1; NC_017079.1. DR EnsemblBacteria; BAM00340; BAM00340; CLDAP_23000. DR GeneID; 12034190; -. DR KEGG; cap:CLDAP_23000; -. DR KO; K00788; -. DR BioCyc; CAER926550:GLA5-2341-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 133 135 THZ-P binding (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22332 MW; 374DB08EF4D15DCF CRC64; MTLPEPPLLV ITDRHMARRP LSAMVAETLV GGCRWILVRE KDLPRPALIA LVKELLDLAR PYNAWVGVSA DVQAMMAAQA HGLHLPQGMD VRAVRRQVDA TRWIGVSAHS VVEVEAAATS GADYVTFSPV FPTPSKPGYG PALGLEALRQ ATQASPIPVV ALGGITAENA ARCIQAGAAG VAVMGEVMRA ADPAAVTHRL VQSIQEGRLK Q // ID I0IFK7_PHYMF Unreviewed; 357 AA. AC I0IFK7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PSMK_18860; OS Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / OS FYK2301M01). OC Bacteria; Planctomycetes; Phycisphaerae; Phycisphaerales; OC Phycisphaeraceae; Phycisphaera. OX NCBI_TaxID=1142394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01; RA Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., RA Nakamura S., Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., RA Fujita N.; RT "Complete genome sequence of Phycisphaera mikurensis NBRC 102666."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012338; BAM04045.1; -; Genomic_DNA. DR RefSeq; YP_005445942.1; NC_017080.1. DR EnsemblBacteria; BAM04045; BAM04045; PSMK_18860. DR GeneID; 12035691; -. DR KEGG; phm:PSMK_18860; -. DR KO; K00788; -. DR BioCyc; PMIK1142394:GLIF-1916-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 188 192 HMP-PP binding (By similarity). FT REGION 284 286 THZ-P binding (By similarity). FT METAL 220 220 Magnesium (By similarity). FT METAL 239 239 Magnesium (By similarity). FT BINDING 219 219 HMP-PP (By similarity). FT BINDING 258 258 HMP-PP (By similarity). FT BINDING 287 287 HMP-PP (By similarity). FT BINDING 315 315 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 357 AA; 36488 MW; 571621A709299D5C CRC64; MSVPHREDRG PLRILDANAN RAREALRVME EAARFLLDDS RLAGTLKSDR HALRAALAGA GDLAAGRDVG GDVGRTLTTP AEGERDTVVA VVAAAGGRAS EALRALEEYG KAVPGVDAAA IEAIRYRGYA VAAELATRLR VAAQAKDRRA QLQAHPWRVC VLLDRAACRL PWERLLAAVL DAGADAIQVR EKQTPSGPLL AHAREVVRRV ERRAAVVVND RPDLALLSGA DGVHLGQDDV GVADARRVLG PAALVGVSTT SLCELAAAVA DGADTVGLGP MFPTATKPGK AVAGVAYAEA ALRRHPGLPH LAIGGITPAN AGGLAAAGVR GVAVAASVTG AADPAAAVHG LLEALAA // ID I0IKN7_LEPFC Unreviewed; 208 AA. AC I0IKN7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LFE_0107; OS Leptospirillum ferrooxidans (strain C2-3). OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=1162668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C2-3; RA Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M., RA Kamijo T., Ohta H.; RT "The complete genome sequence of the pioneer microbe on fresh volcanic RT deposit, Leptospirillum ferrooxidans strain C2-3."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012342; BAM05836.1; -; Genomic_DNA. DR RefSeq; YP_005467966.1; NC_017094.1. DR EnsemblBacteria; BAM05836; BAM05836; LFE_0107. DR GeneID; 12054917; -. DR KEGG; lfc:LFE_0107; -. DR KO; K00788; -. DR BioCyc; LFER1162668:GLFM-107-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 131 133 THZ-P binding (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22380 MW; 4367C7D109B2BA65 CRC64; MEILPLLFVT PEDLPAKVIV SRVQEAVSGG VSAVVLRRKN GPVRDFLDLG YLLRDSLGEE FPIIVNTRLD MALSIHAIGL HLPEDHIPMD VIRKKKPDNF LLGVSCHSRE SVMRAQAEGA DYVFFGPVFE TPSKLAYGPP QGLKLLEQVV AEAEIPVVAI GGIHQGNIES VRKTGASGVA MIGDLAYSAD PKAKAFSLRG GWTRGGSV // ID I0IN09_LEPFC Unreviewed; 207 AA. AC I0IN09; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LFE_0954; OS Leptospirillum ferrooxidans (strain C2-3). OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=1162668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C2-3; RA Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M., RA Kamijo T., Ohta H.; RT "The complete genome sequence of the pioneer microbe on fresh volcanic RT deposit, Leptospirillum ferrooxidans strain C2-3."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012342; BAM06658.1; -; Genomic_DNA. DR RefSeq; YP_005468788.1; NC_017094.1. DR EnsemblBacteria; BAM06658; BAM06658; LFE_0954. DR GeneID; 12055761; -. DR KEGG; lfc:LFE_0954; -. DR KO; K00788; -. DR BioCyc; LFER1162668:GLFM-951-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22837 MW; F1AA62AF687F92AC CRC64; MTFPKLLYIA GSQDFPDKTS FFSHLESLLS EGLSWFQFRE KALTEKALFS WALEIRELTS SYKALLTIND RPDIAYLIEA DGVHLGQEDI PSMTSELIPL ELKNLHIGIS THNPYEVKRS VILSPSYLGV GPINPTKTKD LEHPPRGIQG IIETKKITAL PLVAIGGITP DMAGDIFRAG AQTIAVSGAL TKSPDPIKTM KDFLNHH // ID I0JF34_STAAU Unreviewed; 213 AA. AC I0JF34; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAEMRSA15_20000; OS Staphylococcus aureus subsp. aureus HO 5096 0412. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=1074252; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HO 5096 0412; RA Aslett M.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HO 5096 0412; RX PubMed=23299977; DOI=10.1101/gr.147710.112; RA Holden M.T., Hsu L.Y., Kurt K., Weinert L.A., Mather A.E., RA Harris S.R., Strommenger B., Layer F., Witte W., de Lencastre H., RA Skov R., Westh H., Zemlickova H., Coombs G., Kearns A.M., Hill R.L., RA Edgeworth J., Gould I., Gant V., Cooke J., Edwards G.F., McAdam P.R., RA Templeton K.E., McCann A., Zhou Z., Castillo-Ramirez S., Feil E.J., RA Hudson L.O., Enright M.C., Balloux F., Aanensen D.M., Spratt B.G., RA Fitzgerald J.R., Parkhill J., Achtman M., Bentley S.D., Nubel U.; RT "A genomic portrait of the emergence, evolution, and global spread of RT a methicillin-resistant Staphylococcus aureus pandemic."; RL Genome Res. 23:653-664(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE681097; CCG16711.1; -; Genomic_DNA. DR RefSeq; YP_006238328.1; NC_017763.1. DR ProteinModelPortal; I0JF34; -. DR SMR; I0JF34; 4-209. DR PRIDE; I0JF34; -. DR EnsemblBacteria; CCG16711; CCG16711; SAEMRSA15_20000. DR GeneID; 12801115; -. DR KEGG; sux:SAEMRSA15_20000; -. DR KO; K00788; -. DR BioCyc; SAUR1074252:GLKL-2087-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID I0JNP6_HALH3 Unreviewed; 207 AA. AC I0JNP6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 11-DEC-2013, entry version 17. DE SubName: Full=TenI family protein; GN OrderedLocusNames=HBHAL_3422; OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / OS NBRC 102448/ NCIMB 2269) (Sporosarcina halophila). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Halobacillus. OX NCBI_TaxID=866895; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / NBRC 102448/ NCIMB 2269; RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x; RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V., RA Oesterhelt D.; RT "Chloride and organic osmolytes: a hybrid strategy to cope with RT elevated salinities by the moderately halophilic, chloride-dependent RT bacterium Halobacillus halophilus."; RL Environ. Microbiol. 15:1619-1633(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE717023; CCG45766.1; -; Genomic_DNA. DR RefSeq; YP_006181040.1; NC_017668.1. DR EnsemblBacteria; CCG45766; CCG45766; HBHAL_3422. DR GeneID; 12749225; -. DR KEGG; hhd:HBHAL_3422; -. DR KO; K10810; -. DR BioCyc; HHAL866895:GLDT-2454-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 207 AA; 22847 MW; 1EE799EFB4705BC2 CRC64; MSLKRELHVL SDGKKELDEF CQTALSIQSS VTAIHLREKH REEEEIERWV YTLIKEGISS TKIIVNSYYS VAGKWGAAGV QLPECGPSPE KVKRLYPNLR VGCSIHGLEA GCQKEREGAD YLLFGNVYQT ESKSGLKGKG VKSLASLTEA VSIPVIAIGG IHLSNLERVL QTKVSGIAVM SSIAEAHHPG EKAWRFQSRI QRSCYHA // ID I0JSY7_HALH3 Unreviewed; 205 AA. AC I0JSY7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 16. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HBHAL_4922; OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / OS NBRC 102448/ NCIMB 2269) (Sporosarcina halophila). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Halobacillus. OX NCBI_TaxID=866895; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / NBRC 102448/ NCIMB 2269; RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x; RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V., RA Oesterhelt D.; RT "Chloride and organic osmolytes: a hybrid strategy to cope with RT elevated salinities by the moderately halophilic, chloride-dependent RT bacterium Halobacillus halophilus."; RL Environ. Microbiol. 15:1619-1633(2013). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE717023; CCG47259.1; -; Genomic_DNA. DR RefSeq; YP_006182530.1; NC_017668.1. DR EnsemblBacteria; CCG47259; CCG47259; HBHAL_4922. DR GeneID; 12746607; -. DR KEGG; hhd:HBHAL_4922; -. DR KO; K00788; -. DR BioCyc; HHAL866895:GLDT-3958-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22220 MW; 06A0BBC83243CF59 CRC64; MTLSKQLRKY FVMGSQDTDR DPEAVLEEAI EAGITAFQYR EKGTGSLEGE AKHELGWKLR SLCREKGILF IVNDDLDMVE PLDADGIHVG QEDIGVEVIR SQFPDKILGL SVSTEQEVIQ SSLEKVDYLG AGPIFQTSTK EDAKPVVGTV WIKQLREAYP DLPIVGIGGI NTENALLVVE AGAAGVAVVS AITHAESIAE AVKRL // ID I0JXW0_9BACT Unreviewed; 222 AA. AC I0JXW0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MFUM_300033; OS Methylacidiphilum fumariolicum SolV. OC Bacteria; Verrucomicrobia; unclassified Verrucomicrobia; OC Methylacidiphilales; Methylacidiphilaceae; Methylacidiphilum. OX NCBI_TaxID=1156937; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SolV; RX PubMed=22740660; DOI=10.1128/JB.00501-12; RA Khadem A.F., Wieczorek A.S., Pol A., Vuilleumier S., Harhangi H.R., RA Dunfield P.F., Kalyuzhnaya M.G., Murrell J.C., Francoijs K.-J., RA Stunnenberg H.G., Stein L.Y., DiSpirito A.A., Semrau J.D., Lajus A., RA Medigue C., Klotz M.G., Jetten M.S.M., Op den Camp H.J.M.; RT "Draft Genome Sequence of the Volcano-Inhabiting Thermoacidophilic RT Methanotroph Methylacidiphilum fumariolicum Strain SolV."; RL J. Bacteriol. 194:3729-3730(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SolV; RA Op den Camp H.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAHT01000034; CCG92079.1; -; Genomic_DNA. DR EnsemblBacteria; CCG92079; CCG92079; MFUM_300033. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 24743 MW; FBB62FD8001AD1FD CRC64; MKLDNLKKKF LLSQARFYGI LDLGYVPAEK LKAYSEQLAE GRVDILQLRA KNLEKRKIAE LAREIQSSLV EKEILFIIND YPDIALEIGA DGVHLGQEDM PIEQARKYLS EEFLIGKSTH TLSQALAAAQ EPVDYIAFGP IFKTPTKPDY LPVGIESIAT IKERIKKPVF FIGGINKENI SLVLSAGADR IVMVSALLGA KDIPEFCRQM RNLLSLKGLL AN // ID I0KJJ8_STEMA Unreviewed; 307 AA. AC I0KJJ8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE SubName: Full=Mutator mutT protein (7,8-dihydro-8-oxoguanine-triphosphatase); DE EC=3.6.1.-; GN Name=mutT; ORFNames=SMD_0652; OS Stenotrophomonas maltophilia D457. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=1163399; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D457; RX PubMed=22689246; DOI=10.1128/JB.00602-12; RA Lira F., Hernandez A., Belda E., Sanchez M.B., Moya A., Silva F.J., RA Martinez J.L.; RT "Whole-genome sequence of Stenotrophomonas maltophilia D457, a RT clinical isolate and a model strain."; RL J. Bacteriol. 194:3563-3564(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D457; RA Silva F.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE798556; CCH11237.1; -; Genomic_DNA. DR RefSeq; YP_006183418.1; NC_017671.1. DR ProteinModelPortal; I0KJJ8; -. DR EnsemblBacteria; CCH11237; CCH11237; SMD_0652. DR GeneID; 12744112; -. DR KEGG; smz:SMD_0652; -. DR KO; K03574; -. DR BioCyc; SMAL1163399:GLKX-652-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 307 AA; 33636 MW; 6D6F19F73EAFC239 CRC64; MAAVITDARG RVLLNRRTEN RDMAGLWEFP GGKRESGETS EQALVRELRE ELGIEADVGP WLMDVPQRYP DKHLTLEVRH VRSWKGTPRG REGQAITWVA QDKLGRYSMP PADLPVVAAL RQPDRYLITP APAEDAGGVQ HWHERLQQAV AAGQHRIQLR LPPEHPQRQA MIEQAVRAHR RGVQWLLNRD VALARTLGVG VHLGSEQLLA LQERPLPEGQ LVAASCHDLE QLQAAQQLGC DFAVLGPVQA TASHPGAVPL GWEAFAALRA QVSLPIYALG GMAAGHIAEA RRHGGQGIAA IRGLWPA // ID I0KSE5_STEMA Unreviewed; 208 AA. AC I0KSE5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 14. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SMD_3473; OS Stenotrophomonas maltophilia D457. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=1163399; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D457; RX PubMed=22689246; DOI=10.1128/JB.00602-12; RA Lira F., Hernandez A., Belda E., Sanchez M.B., Moya A., Silva F.J., RA Martinez J.L.; RT "Whole-genome sequence of Stenotrophomonas maltophilia D457, a RT clinical isolate and a model strain."; RL J. Bacteriol. 194:3563-3564(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=D457; RA Silva F.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE798556; CCH13987.1; -; Genomic_DNA. DR RefSeq; YP_006186151.1; NC_017671.1. DR EnsemblBacteria; CCH13987; CCH13987; SMD_3473. DR GeneID; 12744965; -. DR KEGG; smz:SMD_3473; -. DR KO; K00788; -. DR BioCyc; SMAL1163399:GLKX-3473-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21022 MW; 00CB4FED43791E46 CRC64; MTSASPAPRG VYLITPDEPD TACLLARTAP LLAAGATWLQ YRNKTASDAL RREQATALQA LCAEHGVPLI VNDDPALAKA VGAAGVHLGG TDGDIPSARA LLGAEAIIGA SCYDQLANAE KAVAAGASYV AFGAFFPTTT KVTSSRAHTG LLRQSAALGV PRVAIGGLTP DNVGPIIDAG ADLVAVVSSV FAAEDPVATQ RAYLAQFA // ID I0LC31_9ACTO Unreviewed; 277 AA. AC I0LC31; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 13-NOV-2013, entry version 13. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=MILUP08_46275; OS Micromonospora lupini str. Lupac 08. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Micromonospora. OX NCBI_TaxID=1150864; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Lupac 08; RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., RA Vallenet D., Carro L., Coll P., Trujillo M.E.; RT "Genome sequence of Micromonospora lupini str. Lupac 08 isolated from RT root nodules of Lupinus angustifolius."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Lupac 08; RA Trujillo M.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAIE01000041; CCH21378.1; -; Genomic_DNA. DR EnsemblBacteria; CCH21378; CCH21378; MILUP08_46275. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 277 AA; 28496 MW; E4D16D07B9453412 CRC64; MTGWTGAAGP AGSPAPDLGT KRPLEGRFLT KISAIGGIVV LTDRWQARRP LAEIVAAAVA GGVRAVLLRE KDLPRAERAA LAADLRPILA EAGGTLIVAG PDPLDGDAVH LPAAGPYPAP RCRLVGRSCH DEAELLRLTR EDYATLSPVF PSRSKPGYGP PLRPDGLASL IRRSPVPVLA LGGVETPDRV TACVEAGAAG VAVLGAIMRA TDPAEIVASL TSAYVKAVSS KPPESGHGRT EVSRSGLRPT VPTQGSSLTA RSGHGRPQPP TATRESP // ID I0LC35_9ACTO Unreviewed; 207 AA. AC I0LC35; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MILUP08_46279; OS Micromonospora lupini str. Lupac 08. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Micromonospora. OX NCBI_TaxID=1150864; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Lupac 08; RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., RA Vallenet D., Carro L., Coll P., Trujillo M.E.; RT "Genome sequence of Micromonospora lupini str. Lupac 08 isolated from RT root nodules of Lupinus angustifolius."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Lupac 08; RA Trujillo M.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAIE01000041; CCH21382.1; -; Genomic_DNA. DR EnsemblBacteria; CCH21382; CCH21382; MILUP08_46279. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 20381 MW; 07D2DFE53F14AB9A CRC64; MPSLGRLHLV TDTRPGRDPL TVVRAALTAA RADLVVQVRV EDSATDREAY DLAGRVLALC ARYGATCLVN DRLHVALAVG AAGGHVGADD LPVAAARHVL GPTGVLGATA RAPETAVAAV TAGASYLGVG PCHATSTKDG LPDPIGPTGV RAVADAVDVP VIAIGGVTAA RVPALRAAGA YGVAVVGALS AATDPAAATA ELLRALA // ID I0LX85_SALET Unreviewed; 211 AA. AC I0LX85; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEH1573_23830; OS Salmonella enterica subsp. enterica serovar Heidelberg str. 41573. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1128959; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=41573; RX PubMed=22628505; DOI=10.1128/JB.00419-12; RA Hoffmann M., Zhao S., Luo Y., Li C., Folster J.P., Whichard J., RA Allard M.W., Brown E.W., McDermott P.F.; RT "Genome Sequences of Five Salmonella enterica Serovar Heidelberg RT Isolates Associated with a 2011 Multistate Outbreak in the United RT States."; RL J. Bacteriol. 194:3274-3275(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=41573; RA Strain E.A., Timme R.E., Brown E., Allard M.W., Luo Y.L.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGY01000112; EIC34505.1; -; Genomic_DNA. DR ProteinModelPortal; I0LX85; -. DR EnsemblBacteria; EIC34505; EIC34505; SEEH1573_23830. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22950 MW; A495042EC6FEDE33 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIDRLADYP TVAIGGISVE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID I0M1E0_SALET Unreviewed; 211 AA. AC I0M1E0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEH1579_12001; OS Salmonella enterica subsp. enterica serovar Heidelberg str. 41579. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1124937; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=41579; RX PubMed=22628505; DOI=10.1128/JB.00419-12; RA Hoffmann M., Zhao S., Luo Y., Li C., Folster J.P., Whichard J., RA Allard M.W., Brown E.W., McDermott P.F.; RT "Genome Sequences of Five Salmonella enterica Serovar Heidelberg RT Isolates Associated with a 2011 Multistate Outbreak in the United RT States."; RL J. Bacteriol. 194:3274-3275(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=41579; RA Strain E.A., Timme R.E., Brown E., Allard M.W., Luo Y.L.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGW01000019; EIC35960.1; -; Genomic_DNA. DR ProteinModelPortal; I0M1E0; -. DR EnsemblBacteria; EIC35960; EIC35960; SEEH1579_12001. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22950 MW; A495042EC6FEDE33 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIDRLADYP TVAIGGISVE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID I0M2D5_SALET Unreviewed; 211 AA. AC I0M2D5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEH1563_00775; OS Salmonella enterica subsp. enterica serovar Heidelberg str. 41563. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1124941; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=41563; RX PubMed=22628505; DOI=10.1128/JB.00419-12; RA Hoffmann M., Zhao S., Luo Y., Li C., Folster J.P., Whichard J., RA Allard M.W., Brown E.W., McDermott P.F.; RT "Genome Sequences of Five Salmonella enterica Serovar Heidelberg RT Isolates Associated with a 2011 Multistate Outbreak in the United RT States."; RL J. Bacteriol. 194:3274-3275(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=41563; RA Strain E.A., Timme R.E., Brown E., Allard M.W., Luo Y.L.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGX01000026; EIC36305.1; -; Genomic_DNA. DR ProteinModelPortal; I0M2D5; -. DR EnsemblBacteria; EIC36305; EIC36305; SEEH1563_00775. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22950 MW; A495042EC6FEDE33 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIDRLADYP TVAIGGISVE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID I0N127_SALET Unreviewed; 211 AA. AC I0N127; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEH1566_01335; OS Salmonella enterica subsp. enterica serovar Heidelberg str. 41566. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1124942; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=41566; RX PubMed=22628505; DOI=10.1128/JB.00419-12; RA Hoffmann M., Zhao S., Luo Y., Li C., Folster J.P., Whichard J., RA Allard M.W., Brown E.W., McDermott P.F.; RT "Genome Sequences of Five Salmonella enterica Serovar Heidelberg RT Isolates Associated with a 2011 Multistate Outbreak in the United RT States."; RL J. Bacteriol. 194:3274-3275(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=41566; RA Strain E.A., Timme R.E., Brown E., Allard M.W., Luo Y.L.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGZ01000032; EIC48097.1; -; Genomic_DNA. DR ProteinModelPortal; I0N127; -. DR EnsemblBacteria; EIC48097; EIC48097; SEEH1566_01335. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22950 MW; A495042EC6FEDE33 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIDRLADYP TVAIGGISVE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID I0N340_SALET Unreviewed; 211 AA. AC I0N340; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SEEH1565_01523; OS Salmonella enterica subsp. enterica serovar Heidelberg str. 41565. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1128963; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=41565; RX PubMed=22628505; DOI=10.1128/JB.00419-12; RA Hoffmann M., Zhao S., Luo Y., Li C., Folster J.P., Whichard J., RA Allard M.W., Brown E.W., McDermott P.F.; RT "Genome Sequences of Five Salmonella enterica Serovar Heidelberg RT Isolates Associated with a 2011 Multistate Outbreak in the United RT States."; RL J. Bacteriol. 194:3274-3275(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=41565; RA Strain E.A., Timme R.E., Brown E., Allard M.W., Luo Y.L.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJHA01000107; EIC48810.1; -; Genomic_DNA. DR ProteinModelPortal; I0N340; -. DR EnsemblBacteria; EIC48810; EIC48810; SEEH1565_01523. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22950 MW; A495042EC6FEDE33 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIDRLADYP TVAIGGISVE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID I0N7G7_STREE Unreviewed; 209 AA. AC I0N7G7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpSV36_0531; OS Streptococcus pneumoniae SV36. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=497739; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SV36; RA Hiller N.L., Eutsey R.A., Powell E., Earl J., Janto B., Martin D., RA David S., Ahmed A., Longwell M., Dahlgren M.E., Ezzo S., Tettelin H., RA Daugherty S.C., Mitchell T., Hillman T., Buchinsky F.J., Tomasz A., RA de Lencastre H., Sa-Leao R., Post J.C., Hu F.Z., Ehrlich G.D.; RT "Differences in Genotype and Virulence among Four Multidrug-Resistant RT Streptococcus pneumoniae Isolates belonging to the PMEN1 clone."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNO01000007; EIC50337.1; -; Genomic_DNA. DR ProteinModelPortal; I0N7G7; -. DR EnsemblBacteria; EIC50337; EIC50337; CGSSpSV36_0531. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23275 MW; 54691E8B38ED4ED4 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LRGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID I0N7H4_STREE Unreviewed; 210 AA. AC I0N7H4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpSV36_0538; OS Streptococcus pneumoniae SV36. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=497739; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SV36; RA Hiller N.L., Eutsey R.A., Powell E., Earl J., Janto B., Martin D., RA David S., Ahmed A., Longwell M., Dahlgren M.E., Ezzo S., Tettelin H., RA Daugherty S.C., Mitchell T., Hillman T., Buchinsky F.J., Tomasz A., RA de Lencastre H., Sa-Leao R., Post J.C., Hu F.Z., Ehrlich G.D.; RT "Differences in Genotype and Virulence among Four Multidrug-Resistant RT Streptococcus pneumoniae Isolates belonging to the PMEN1 clone."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNO01000007; EIC50344.1; -; Genomic_DNA. DR ProteinModelPortal; I0N7H4; -. DR EnsemblBacteria; EIC50344; EIC50344; CGSSpSV36_0538. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID I0NUS5_STREE Unreviewed; 209 AA. AC I0NUS5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpSV35_0813; OS Streptococcus pneumoniae SV35. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=497738; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SV35; RA Hiller N.L., Eutsey R.A., Powell E., Earl J., Janto B., Martin D., RA David S., Ahmed A., Longwell M., Dahlgren M.E., Ezzo S., Tettelin H., RA Daugherty S.C., Mitchell T., Hillman T., Buchinsky F.J., Tomasz A., RA de Lencastre H., Sa-Leao R., Post J.C., Hu F.Z., Ehrlich G.D.; RT "Differences in Genotype and Virulence among Four Multidrug-Resistant RT Streptococcus pneumoniae Isolates belonging to the PMEN1 clone."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNN01000007; EIC58145.1; -; Genomic_DNA. DR ProteinModelPortal; I0NUS5; -. DR EnsemblBacteria; EIC58145; EIC58145; CGSSpSV35_0813. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23275 MW; 54691E8B38ED4ED4 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LRGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID I0NUT2_STREE Unreviewed; 210 AA. AC I0NUT2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSpSV35_0820; OS Streptococcus pneumoniae SV35. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=497738; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SV35; RA Hiller N.L., Eutsey R.A., Powell E., Earl J., Janto B., Martin D., RA David S., Ahmed A., Longwell M., Dahlgren M.E., Ezzo S., Tettelin H., RA Daugherty S.C., Mitchell T., Hillman T., Buchinsky F.J., Tomasz A., RA de Lencastre H., Sa-Leao R., Post J.C., Hu F.Z., Ehrlich G.D.; RT "Differences in Genotype and Virulence among Four Multidrug-Resistant RT Streptococcus pneumoniae Isolates belonging to the PMEN1 clone."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNN01000007; EIC58152.1; -; Genomic_DNA. DR ProteinModelPortal; I0NUT2; -. DR EnsemblBacteria; EIC58152; EIC58152; CGSSpSV35_0820. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID I0NZV4_STREE Unreviewed; 209 AA. AC I0NZV4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp4595_0632; OS Streptococcus pneumoniae 459-5. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=497980; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=459-5; RA Hiller N.L., Eutsey R.A., Powell E., Earl J., Janto B., Martin D., RA David S., Ahmed A., Longwell M., Dahlgren M.E., Ezzo S., Tettelin H., RA Daugherty S.C., Mitchell T., Hillman T., Buchinsky F.J., Tomasz A., RA de Lencastre H., Sa-Leao R., Post J.C., Hu F.Z., Ehrlich G.D.; RT "Differences in Genotype and Virulence among Four Multidrug-Resistant RT Streptococcus pneumoniae Isolates Belonging to the PMEN1 Clone."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXO01000011; EIC59924.1; -; Genomic_DNA. DR ProteinModelPortal; I0NZV4; -. DR EnsemblBacteria; EIC59924; EIC59924; CGSSp4595_0632. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23275 MW; 54691E8B38ED4ED4 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LRGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGVKLMRKLL PQMPLVAIGG IQTKHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID I0NZW1_STREE Unreviewed; 210 AA. AC I0NZW1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CGSSp4595_0639; OS Streptococcus pneumoniae 459-5. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=497980; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=459-5; RA Hiller N.L., Eutsey R.A., Powell E., Earl J., Janto B., Martin D., RA David S., Ahmed A., Longwell M., Dahlgren M.E., Ezzo S., Tettelin H., RA Daugherty S.C., Mitchell T., Hillman T., Buchinsky F.J., Tomasz A., RA de Lencastre H., Sa-Leao R., Post J.C., Hu F.Z., Ehrlich G.D.; RT "Differences in Genotype and Virulence among Four Multidrug-Resistant RT Streptococcus pneumoniae Isolates Belonging to the PMEN1 Clone."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXO01000011; EIC59931.1; -; Genomic_DNA. DR ProteinModelPortal; I0NZW1; -. DR EnsemblBacteria; EIC59931; EIC59931; CGSSp4595_0639. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22802 MW; A3239F0AA8CA7392 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDILS // ID I0P5X8_MYCAB Unreviewed; 223 AA. AC I0P5X8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=OUW_23001; OS Mycobacterium abscessus M93. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium abscessus. OX NCBI_TaxID=1149134; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M93; RX PubMed=22628507; DOI=10.1128/JB.00492-12; RA Choo S.W., Wong Y.L., Yusoff A.M., Leong M.L., Wong G.J., Ong C.S., RA Ng K.P., Ngeow Y.F.; RT "Genome Sequence of the Mycobacterium abscessus Strain M93."; RL J. Bacteriol. 194:3278-3278(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGF01000013; EIC62048.1; -; Genomic_DNA. DR EnsemblBacteria; EIC62048; EIC62048; OUW_23001. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23492 MW; BE260B3D6D92FA6B CRC64; MHSRSARLQS AHLYLCTDAR RERGDFAEFV DAALAGGVDI VQLRDKGSAG ERQFGRLEPA EELEYLAILS EAAARHGALF AVNDRADIAR AAGADVLHLG QDDLPLAVAR EIVGPDVLIG RSTHDAEQAA AAARDDEIDY FCCGPCWPTP TKPGRTASGL GLVRTAAELG TSKPWFAIGG IDEARVPQVV EAGASRIVVV RAITAAADPR AAAASLRGST RRA // ID I0PXN1_MYCAB Unreviewed; 223 AA. AC I0PXN1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=S7W_01250; OS Mycobacterium abscessus M94. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium abscessus. OX NCBI_TaxID=1158135; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M94; RA Ngeow Y.F., Choo S.W., Wong Y.L.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGG01000001; EIC71401.1; -; Genomic_DNA. DR EnsemblBacteria; EIC71401; EIC71401; S7W_01250. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23492 MW; BE260B3D6D92FA6B CRC64; MHSRSARLQS AHLYLCTDAR RERGDFAEFV DAALAGGVDI VQLRDKGSAG ERQFGRLEPA EELEYLAILS EAAARHGALF AVNDRADIAR AAGADVLHLG QDDLPLAVAR EIVGPDVLIG RSTHDAEQAA AAARDDEIDY FCCGPCWPTP TKPGRTASGL GLVRTAAELG TSKPWFAIGG IDEARVPQVV EAGASRIVVV RAITAAADPR AAAASLRGST RRA // ID I0Q109_STROR Unreviewed; 210 AA. AC I0Q109; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1115_0902; OS Streptococcus oralis SK610. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1095741; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK610; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJKQ01000026; EIC74961.1; -; Genomic_DNA. DR EnsemblBacteria; EIC74961; EIC74961; HMPREF1115_0902. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22734 MW; 38BF1F95FA5441C1 CRC64; MNREALRLYL VTNRYQDSLE NFLEKVETAC RSGVTMIQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDICLAVD AAGLHIGDDE LPVSVARQVL GPDKILGVTA KTVERALEAE EGGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLAATGIA GVAVVRDLMQ AKDIEAKAQA FLTKLDDIVS // ID I0Q6L3_STROR Unreviewed; 210 AA. AC I0Q6L3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1114_1922; OS Streptococcus oralis SK100. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1095740; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK100; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJKP01000037; EIC76915.1; -; Genomic_DNA. DR EnsemblBacteria; EIC76915; EIC76915; HMPREF1114_1922. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22831 MW; 81127CE26B3DBB97 CRC64; MNREAFRLYL VTNRYQDSLE SFLEKVETAC RSGVTIIQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDICLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE TSGADYLGTG AIFPTTTKEN APITLISTLK TICQMVAIPV VAIGGLTSEN IDQLAATGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDDMIS // ID I0QBK6_STROR Unreviewed; 210 AA. AC I0QBK6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1113_0083; OS Streptococcus oralis SK10. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1095739; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK10; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJKO01000035; EIC78658.1; -; Genomic_DNA. DR EnsemblBacteria; EIC78658; EIC78658; HMPREF1113_0083. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22682 MW; 32DE539BAFAD8BA8 CRC64; MNREVLKLYL VTNRYQDSLG SFLEKVETAC RSGVTIIQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDICLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE TSGADYLGTG AIFPTTTKEN APITPISTLK TICQTIAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKAHA FLTKLDDIIS // ID I0QJX9_STRSL Unreviewed; 210 AA. AC I0QJX9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PS4_48839; OS Streptococcus salivarius PS4. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1157946; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PS4; RX PubMed=22843595; DOI=10.1128/JB.00896-12; RA Martin V., Maldonado-Barragan A., Jimenez E., Ruas-Madiedo P., RA Fernandez L., Rodriguez J.M.; RT "Complete Genome Sequence of Streptococcus salivarius PS4, a Strain RT Isolated from Human Milk."; RL J. Bacteriol. 194:4466-4467(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJFW01000012; EIC81589.1; -; Genomic_DNA. DR EnsemblBacteria; EIC81589; EIC81589; PS4_48839. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23061 MW; D5A8EDFC255A7565 CRC64; MLKETLRLYL VTNRYQDSLE TFLKKVEQAC QSGVTMVQLR EKQLTTNQYY ELAKIVKQIT DTYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GTEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK DICQTVGIPV VAIGGLTCEN IHQLSGTDIA GIAVVRDLMQ ARDIEARTQE FLTKLDQIIP // ID I0QLX5_9ENTR Unreviewed; 219 AA. AC I0QLX5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPM24T3_22606; OS Serratia sp. M24T3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=932213; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M24T3; RX PubMed=22740681; DOI=10.1128/JB.00670-12; RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.; RT "Draft Genome Sequence of Serratia sp. Strain M24T3, Isolated from RT Pinewood Disease Nematode Bursaphelenchus xylophilus."; RL J. Bacteriol. 194:3764-3764(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJHJ01000049; EIC82298.1; -; Genomic_DNA. DR EnsemblBacteria; EIC82298; EIC82298; SPM24T3_22606. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24272 MW; E68C93BD24F9EFF9 CRC64; MNIPSTPFPA VPYYLGLYPV VDSVEWVRRL LEAGVKTLQL RIKDLPDAEV EPAIIEAIKL GRQYEARLFI NDYWRLAVKH QAYGIHLGQE DLDTTDLLAI HQAGLRLGVS THDEAELERA ISVHPSYIAL GHVFPTQTKD MPSAPQGLAE LAHHIKQLNG RFPTVAIGGI SLERVQPVME CGVGSVAVVS AITKAADWRA ATQQLIELCP YRDDNHAQR // ID I0RAT8_9FIRM Unreviewed; 211 AA. AC I0RAT8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF9970_1968; OS Lachnoanaerobaculum saburreum F0468. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Lachnoanaerobaculum. OX NCBI_TaxID=1095750; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0468; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGH01000027; EIC96796.1; -; Genomic_DNA. DR EnsemblBacteria; EIC96796; EIC96796; HMPREF9970_1968. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23086 MW; 26E02A0CB03ECB8B CRC64; MRLDKKYMHL YAVSDRAWTG EKTLYEQINE ALKNGVTCVQ LREKNLDEIS FIEEAKKISE LCKQYSIPFI VNDNVKVAVA SNADGVHIGQ DDMKLKDVRK LVGENMIIGV SVHTVDEAKS AQEDGADYIG IGAVFETSTK NDVDIIPYEK VKSICEAVDI PKVAIGGINA ENILKLKGSK IDGVAVVSAI FGAKDIGKAT KELDTLVNEL I // ID I0REK7_MYCXE Unreviewed; 223 AA. AC I0REK7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MXEN_20285; OS Mycobacterium xenopi RIVM700367. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1150591; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RIVM700367; RX PubMed=22628510; DOI=10.1128/JB.00482-12; RA Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S., RA van Soolingen D., Bitter W., Pain A.; RT "Complete Genome Sequence of Mycobacterium xenopi Type Strain RT RIVM700367."; RL J. Bacteriol. 194:3282-3283(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJFI01000108; EID09560.1; -; Genomic_DNA. DR EnsemblBacteria; EID09560; EID09560; MXEN_20285. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23523 MW; EC65D6D292765729 CRC64; MHETRSRLAA ARLYLCTDAR RERGDLAEFA EAALAGGVDI IQLRDKGSVG EQRFGPLEAR DELAALEILA EAARRHAALV AVNDRADIAR AAGADVLHLG QNDLPLAVAR EIVGRHTLIG RSTHDVEQVA AAVAEDADYF CVGPCWPTPT KPGRPAPGLQ LVRVAAETAG EKPWFAIGGI DAARLPQVLE AGARRIVVVR AIAAADDPKA AAKRLSSALA AAR // ID I0RTV9_MYCPH Unreviewed; 223 AA. AC I0RTV9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MPHLEI_10995; OS Mycobacterium phlei RIVM601174. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1150599; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RIVM601174; RX PubMed=22628511; DOI=10.1128/JB.00485-12; RA Abdallah A.M., Rashid M., Adroub S.A., Arnoux M., Ali S., RA van Soolingen D., Bitter W., Pain A.; RT "Complete Genome Sequence of Mycobacterium phlei Type Strain RT RIVM601174."; RL J. Bacteriol. 194:3284-3285(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJFJ01000048; EID14562.1; -; Genomic_DNA. DR EnsemblBacteria; EID14562; EID14562; MPHLEI_10995. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23584 MW; 7353D496347DA929 CRC64; MHKPRHRLAT ASLYLCTDAR RERGDLAEFA DAALAGGVDL IQLRDKGSPG EQRFGPLEAR QELEALEVLA DAARRHGALL AVNDRADIAR AAGADVLHLG QDDLPLAVAR EIIGADPVIG RSTHDTAQVD AAVDEPVDYF CVGPCWPTPT KPGRPAPGLD LVRYAAGLAT DKPWFAIGGI DAERLPEVLA AGARRIVVVR AITGADDPRA AAEQLKRALS TAG // ID I0SFQ6_STRMT Unreviewed; 210 AA. AC I0SFQ6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_1; Synonyms=thiE; ORFNames=HMPREF1045_0102; OS Streptococcus mitis SK616. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1095735; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK616; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICR01000076; EID22209.1; -; Genomic_DNA. DR EnsemblBacteria; EID22209; EID22209; HMPREF1045_0102. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22849 MW; AC775D7C9EF932C5 CRC64; MNREALRLYL VTNRYQDSLE SFLEKLETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVTRALEAE EGGADYLGTG AIFPTTTKEN APITLISTLK TICQRVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDDIIF // ID I0SFW8_STRMT Unreviewed; 209 AA. AC I0SFW8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_2; Synonyms=thiE; ORFNames=HMPREF1045_0110; OS Streptococcus mitis SK616. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1095735; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK616; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICR01000076; EID22271.1; -; Genomic_DNA. DR EnsemblBacteria; EID22271; EID22271; HMPREF1045_0110. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23290 MW; D307C0C824F31072 CRC64; MFHKELLKLY FICGTTTCRG KDLYTVVEEA LKGGITLFQF REKGEGALEG KEKVELAMKL QDLCKKYNVP FIVNDDIELA LEIDADGVHV GQDDLGVDEI RKLMPAKIIG LSIKNEKEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLKLMRKLL PQMPLVAIGG IQTQHIKDIM KINMDGVSII SAISYAKNIE KTVREMSEQ // ID I0SKN1_9STRE Unreviewed; 209 AA. AC I0SKN1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1046_2026; OS Streptococcus pseudopneumoniae ATCC BAA-960. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=889205; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-960; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICS01000239; EID23934.1; -; Genomic_DNA. DR EnsemblBacteria; EID23934; EID23934; HMPREF1046_2026. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23215 MW; 1230EBA553285D3B CRC64; MFHKELLKLY FICGTATCQG KDLYRVVEEA LKGGITLFQF REKGEGALEG KEKVEVAIKL QDLCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDLGVDEI RKLMPAKIIG LSIKNEKEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLKLMRKLL PQMPLVAIGG IQTQHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID I0SSJ6_STROR Unreviewed; 210 AA. AC I0SSJ6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1047_0299; OS Streptococcus oralis SK1074. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1095738; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK1074; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICT01000005; EID26349.1; -; Genomic_DNA. DR EnsemblBacteria; EID26349; EID26349; HMPREF1047_0299. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22778 MW; EC6C92D324953D92 CRC64; MNRESLKLYL VTNRYQDSLE NFLEKVETAC RSGVTIIQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPKKILGVTA KTVKRALEAE TSGADYLGTG AIFPTTTKEN APITQISTLK TICQTVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDDIVS // ID I0SUP6_STRMT Unreviewed; 210 AA. AC I0SUP6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1048_0363; OS Streptococcus mitis SK575. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1095736; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK575; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICU01000086; EID27099.1; -; Genomic_DNA. DR EnsemblBacteria; EID27099; EID27099; HMPREF1048_0363. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22907 MW; A69EF713B2660480 CRC64; MNREALRLYL VTNRYQDSVE SFLEKVEMAC RSGVTIVQLR EKNLTTNQYY QLAKKVKEIT DAYQVPLIID DRLDICLAVD AAGLHIGDDE LPVSVARQVL GPEKILGVTA KTVKRALEAE EGGANYLGTG AIFPTTTKEN APITLISTLK TICQRVAIPV VAIGGLTSEN IDQLIGTGIA GVAVVRDLMQ SEDIEAKTQA FLTKLDDIIF // ID I0SVR5_9STRE Unreviewed; 210 AA. AC I0SVR5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HMPREF1046_1115; OS Streptococcus pseudopneumoniae ATCC BAA-960. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=889205; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-960; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICS01000170; EID27468.1; -; Genomic_DNA. DR EnsemblBacteria; EID27468; EID27468; HMPREF1046_1115. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22788 MW; F554FECD23B385CB CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPDKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDIIS // ID I0T7M8_STRMT Unreviewed; 209 AA. AC I0T7M8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_2; Synonyms=thiE; ORFNames=HMPREF1110_1926; OS Streptococcus mitis SK579. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1095737; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK579; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJL01000031; EID31631.1; -; Genomic_DNA. DR EnsemblBacteria; EID31631; EID31631; HMPREF1110_1926. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23228 MW; FA7554AC92468FE6 CRC64; MFHKELLKLY FICGTTTCQG KDLYTVVEEA LKGGITLFQF REKGEGALEG KEKVELAIKL QDLCKKYNVP FIVNDDIELA LEIDADGVHV GQDDLGVDEI RKLMPAKIIG LSIKNEEEFQ QSKVEYVDYV GVGPVFDTQS KEDAGGAIGY EGLKLMRKLL PQLPLVAIGG IQTQHIKDIM KTNMDGVSII SAISYAKNIE KTVRKMSEQ // ID I0T7Z4_STRMT Unreviewed; 210 AA. AC I0T7Z4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_1; Synonyms=thiE; ORFNames=HMPREF1110_0865; OS Streptococcus mitis SK579. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1095737; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK579; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJL01000022; EID31747.1; -; Genomic_DNA. DR EnsemblBacteria; EID31747; EID31747; HMPREF1110_0865. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22834 MW; 55335E401A94C819 CRC64; MNREALRLYL VTNRYQDSLE SFLEKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPDKILGVTA KTVKRALEAE EGGADYLGTG AIFPTTTKEN APITLISTLK TICQRVAIPV VAIGGLTSEN VDQLIGTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLDDIIF // ID I0TAE5_9BACT Unreviewed; 202 AA. AC I0TAE5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=HMPREF9969_1481; OS Prevotella sp. oral taxon 306 str. F0472. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1095752; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0472; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJIN01000067; EID32598.1; -; Genomic_DNA. DR EnsemblBacteria; EID32598; EID32598; HMPREF9969_1481. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 23287 MW; D06DD6CB7BAC82E3 CRC64; MKLVIMTKST FFVEEDKIIS MLFEEGLDCL HISKVDPSPL YLERLLALIP SHYHSKIVVH QHFQMKSEYG LGGIHLDNPS LATPHGYRGH ISRSCDDVMK LKAIKKQSDY VFLKNIHQPR ENTAATEHIL SDIELEEARK QGLLGKHVYA MGGITIDDFP RLHDLDFGGV VVRNDLWDQF CIHSEQNFNP IIKYFRKLRT IC // ID I0TI82_STAEP Unreviewed; 160 AA. AC I0TI82; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=IS250_1028; OS Staphylococcus epidermidis IS-250. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904789; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-250; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJR01000052; EID35335.1; -; Genomic_DNA. DR ProteinModelPortal; I0TI82; -. DR EnsemblBacteria; EID35335; EID35335; IS250_1028. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID I0TNT8_STAEP Unreviewed; 213 AA. AC I0TNT8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=IS250_1649; OS Staphylococcus epidermidis IS-250. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904789; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-250; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJR01000021; EID37291.1; -; Genomic_DNA. DR ProteinModelPortal; I0TNT8; -. DR EnsemblBacteria; EID37291; EID37291; IS250_1649. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23752 MW; 12585CE016A733F5 CRC64; MMFDSKQLSV YFICGTQDIP KNKSIEQVLK EALEAGITLY QFREKGPNAL KGEKKKQLAL KLKQLCHSYH VPMIVNDDVQ LAQEINADGI HVGQDDMEIQ QFASQFKNKI IGLSVGNLKE YQQSDLSKVD YIGVGPMYTT SSKDDASKPV GPSMISQLRL YIHDFPIVAI GGINETNVQP IVDEGADGIS VISAITRSTN IDKTVKYFLR YFT // ID I0TPF6_STAEP Unreviewed; 160 AA. AC I0TPF6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine monophosphate synthase/TENI; GN ORFNames=ISK_1032; OS Staphylococcus epidermidis IS-K. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904791; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-K; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJS01000033; EID37509.1; -; Genomic_DNA. DR ProteinModelPortal; I0TPF6; -. DR EnsemblBacteria; EID37509; EID37509; ISK_1032. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID I0TS80_STAEP Unreviewed; 215 AA. AC I0TS80; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ISK_2072; OS Staphylococcus epidermidis IS-K. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904791; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-K; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJS01000025; EID38483.1; -; Genomic_DNA. DR ProteinModelPortal; I0TS80; -. DR EnsemblBacteria; EID38483; EID38483; ISK_2072. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23998 MW; 87DCB45162513A97 CRC64; MNMMFDSKQL SVYFICGTQD IPKNKSIEQV LKEALEAGIT LYQFREKGPN ALKGEKKKQL ALKLKQLCHS YHVPMIVNDD VQLAQEINAD GIHVGQDDME IQQFASQFKN KIIGLSVGNL KEYQQSDLSK VDYIGVGPMY TTSSKDDASK PVGPSMISQL RLYIHDFPIV AIGGINETNV QPIVDEGADG ISVISAITRS TNIDKTVKYF LRYFT // ID I0U2U6_STAAU Unreviewed; 213 AA. AC I0U2U6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAISM_2146; OS Staphylococcus aureus subsp. aureus IS-M. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904792; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IS-M; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJLD01000001; EID42199.1; -; Genomic_DNA. DR ProteinModelPortal; I0U2U6; -. DR SMR; I0U2U6; 4-209. DR PRIDE; I0U2U6; -. DR EnsemblBacteria; EID42199; EID42199; SAISM_2146. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID I0U730_GEOTM Unreviewed; 204 AA. AC I0U730; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 22-JAN-2014, entry version 14. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN Name=tenI; ORFNames=GT20_2816; OS Geobacillus thermoglucosidans TNO-09.020. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1136178; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TNO-09.020; RX PubMed=22815439; DOI=10.1128/JB.00318-12; RA Zhao Y., Caspers M.P., Abee T., Siezen R.J., Kort R.; RT "Complete genome sequence of Geobacillus thermoglucosidans TNO-09.020, RT a thermophilic sporeformer associated with a dairy-processing RT environment."; RL J. Bacteriol. 194:4118-4118(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJN01000019; EID43683.1; -; Genomic_DNA. DR EnsemblBacteria; EID43683; EID43683; GT20_2816. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 204 AA; 22235 MW; BE4DB890D4C99391 CRC64; MKVERQLHII STGKQPLEQF VAICARVHPY VDAIHVREKR KTAREISEFL TELIGRGIPP KKIIVNDRID VAVVFGVKGV QLAHHSLSVH QTKRHFPSLS VGCSVHSLEE AMEAEKSGAD YCIYGHIFPT ASKLGAPPRG IESLRNIVHH VNIPVIAIGG IHSDNAEQVL QAGAHGIAVM SAVFCAKDPV SEAKKLAKIV KKMA // ID I0UA11_GEOTM Unreviewed; 219 AA. AC I0UA11; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 15. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=GT20_1454; OS Geobacillus thermoglucosidans TNO-09.020. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1136178; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TNO-09.020; RX PubMed=22815439; DOI=10.1128/JB.00318-12; RA Zhao Y., Caspers M.P., Abee T., Siezen R.J., Kort R.; RT "Complete genome sequence of Geobacillus thermoglucosidans TNO-09.020, RT a thermophilic sporeformer associated with a dairy-processing RT environment."; RL J. Bacteriol. 194:4118-4118(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJN01000007; EID44714.1; -; Genomic_DNA. DR EnsemblBacteria; EID44714; EID44714; GT20_1454. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23205 MW; 00D05884CA6EAC10 CRC64; MARIAREEMK QRLKVYFIMG SVNCKKSPFE VLTEAIDGGI TLFQFREKGS GALVGEQKYE FAKQLQAICQ KRGIPFIVND DVELALAIDA DGVHIGQDDE DARIVREKIG DKILGVSAHN LAEAQAAATA GADYIGVGPI YPTKSKADAK QAQGPGMIRL LRDNGIDIPI VGIGGITAEN ASEVMNAGAD GVSVISAIAS APSPLLATKQ LVQTVLNNE // ID I0UE90_BACLI Unreviewed; 203 AA. AC I0UE90; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 13-NOV-2013, entry version 12. DE SubName: Full=Transcriptional regulator TenI; GN ORFNames=MUY_01470; OS Bacillus licheniformis WX-02. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1126218; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WX-02; RA Yangtse W., Chen S.; RT "Genome sequence of Bacillus licheniformis WX-02."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHIF01000002; EID46193.1; -; Genomic_DNA. DR ProteinModelPortal; I0UE90; -. DR SMR; I0UE90; 1-191. DR EnsemblBacteria; EID46193; EID46193; MUY_01470. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 203 AA; 22376 MW; 3BE3AB481BF14203 CRC64; MHLHAITDDK HSVEELSAKI ISIHDAVDFI HIRERSKKVS EISSLIDRLA EEGVDKRKLI INDRVDIALF HHIHRVQLPS HGFSVKSVRS RFPHLKIGKS VHSPEEAVQA ETEGADYVLF GHIFETDCKK GRKGRGALSL AEVKAAVRIP VIAIGGITEQ RLAEVKMADG IAVMSGIFSH DRPNEAAARL ASLAKGDSYE KAL // ID I0UM00_BACLI Unreviewed; 224 AA. AC I0UM00; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MUY_04207; OS Bacillus licheniformis WX-02. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1126218; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WX-02; RA Yangtse W., Chen S.; RT "Genome sequence of Bacillus licheniformis WX-02."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHIF01000002; EID48903.1; -; Genomic_DNA. DR EnsemblBacteria; EID48903; EID48903; MUY_04207. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23606 MW; 14AA6FB9424CAB58 CRC64; MTRVSEEAMK DLLSVYFIMG SNNTAGDPLT VIEKALKGGA TLFQFREKGE GALKAGDQTA FARQVQALCK QFNVPFIIND DVELALELDA DGVHIGQDDD KAADVRARIG DKVLGVSAHT LEEVLKAEKD GADYIGAGPV YPTETKRDTK AVQGVSLIQE IRRQGIGIPV VGIGGITVEN CVPVIEAGAD GISVISAISK AADPKQAAEA FSEKVQAAKQ SAHS // ID I0URC7_9MICC Unreviewed; 204 AA. AC I0URC7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=HMPREF1324_2235; OS Rothia aeria F0474. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Rothia. OX NCBI_TaxID=1125724; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0474; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJQ01000042; EID50430.1; -; Genomic_DNA. DR EnsemblBacteria; EID50430; EID50430; HMPREF1324_2235. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 204 AA; 21963 MW; 0F3FD4748F0FC10F CRC64; MTTNSTAKTT TPLDLSLYLV TGENPVETVR RARHATCIQV RSKPISARDL YALAEEIACT ALPHQKILID DRVDVALALR ARGVRIDGVH IGQDDLPVAD ARRLLGEHAI IGLTTGTREL VERANTVAHL IDYIGAGPFR PSPTKASNRP PLGVEGLREL AELSKVPVVA IGDIWPQDCP SIRETGVAGV AMARAFVENP ELQA // ID I0V400_9PSEU Unreviewed; 225 AA. AC I0V400; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SacxiDRAFT_2633; OS Saccharomonospora xinjiangensis XJ-54. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882086; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XJ-54; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Brambilla E.-M., Klenk H.-P., Woyke T.; RT "Improved High-Quality Draft sequence of Saccharomonospora RT xinjiangensis XJ-54."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH636049; EID54853.1; -; Genomic_DNA. DR EnsemblBacteria; EID54853; EID54853; SacxiDRAFT_2633. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 23556 MW; 08E7352CC0E8056D CRC64; MPGLDGDRIR KRLDDARLYL CTDARARQGD LAEFADAALA GGVDIVQLRD KTGGKPLEAA QEIAALEILA EACARHGALL AVNDRADVAV AVDADVLHLG QDDLPVAVAR RIVGDDVVIG RSTHSWEQAA AAATEEGVDY FCVGPCWPTP TKPGRAAPGL DLVRAVSSGI ETTRPWFAIG GIDLARLDDV LAAGAERAVV VRAITEAGDP AEAARELRHG LTRAG // ID I0VJH2_SHIFL Unreviewed; 211 AA. AC I0VJH2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 14-MAY-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SF5M90T_3976; OS Shigella flexneri 5a str. M90T. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=1086030; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M90T; RA Onodera N.T., Ryu J., Corey N., Archibald J.M., Rohde J.R.; RT "The whole genome sequence of Shigella flexneri serotype 5a strain RT M90T Sm."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001474; EID64288.1; -; Genomic_DNA. DR ProteinModelPortal; I0VJH2; -. DR SMR; I0VJH2; 10-208. DR EnsemblBacteria; EID64288; EID64288; SF5M90T_3976. DR OMA; AVRPSYI; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID I0VXM2_ECOLX Unreviewed; 194 AA. AC I0VXM2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECW26_05950; OS Escherichia coli W26. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1090926; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=W26; RX PubMed=22933771; DOI=10.1128/JB.01180-12; RA Kim M., Yi H., Cho Y.J., Jang J., Hur H.G., Chun J.; RT "Draft Genome Sequence of Escherichia coli W26, an Enteric Strain RT Isolated from Cow Feces."; RL J. Bacteriol. 194:5149-5150(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGIA01000013; EID68888.1; -; Genomic_DNA. DR EnsemblBacteria; EID68888; EID68888; ECW26_05950. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 20 24 HMP-PP binding (By similarity). FT REGION 117 119 THZ-P binding (By similarity). FT REGION 169 170 THZ-P binding (By similarity). FT METAL 53 53 Magnesium (By similarity). FT METAL 72 72 Magnesium (By similarity). FT BINDING 52 52 HMP-PP (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 194 AA; 21082 MW; 816B02DA346B5F71 CRC64; MVDSVQWIER LLDAGVRTLQ LRIKDRRDEE VEVDVVAAIA LGRRYNARLF INDYWRLAIK HQAYGVHLGQ EDLQATDLNA IRAAGLRLGV STHDDMEIDV ALAARPSYIA LGHVFPTQTK QMPSAPQGLE QLARHVERLA DYPTVAIGGI SLARAPAVIA TGVGSIAVVS AITQAADWRL ATAQLLEIAG VGDE // ID I0VZV0_9STRE Unreviewed; 209 AA. AC I0VZV0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_1; Synonyms=thiE; ORFNames=HMPREF1112_0641; OS Streptococcus pseudopneumoniae SK674. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1095734; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK674; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJKE01000100; EID69666.1; -; Genomic_DNA. DR EnsemblBacteria; EID69666; EID69666; HMPREF1112_0641. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23215 MW; 1230EBA553285D3B CRC64; MFHKELLKLY FICGTATCQG KDLYRVVEEA LKGGITLFQF REKGEGALEG KEKVEVAIKL QDLCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDLGVDEI RKLMPAKIIG LSIKNEKEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLKLMRKLL PQMPLVAIGG IQTQHIKDIM KTNVDGVSII SAISYAKNIE KTVREMSEQ // ID I0VZV8_9STRE Unreviewed; 210 AA. AC I0VZV8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE_2; Synonyms=thiE; ORFNames=HMPREF1112_0650; OS Streptococcus pseudopneumoniae SK674. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1095734; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK674; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJKE01000100; EID69674.1; -; Genomic_DNA. DR EnsemblBacteria; EID69674; EID69674; HMPREF1112_0650. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22788 MW; F554FECD23B385CB CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARQVL GPDKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMDTGIA GVAVVRDLMQ AEDIEAKTQA FLTKLHDIIS // ID I0W880_9NOCA Unreviewed; 232 AA. AC I0W880; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=W59_36658; OS Rhodococcus imtechensis RKJ300 = JCM 13270. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=1165867; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RKJ300; RX PubMed=22689233; DOI=10.1128/JB.00532-12; RA Vikram S., Kumar S., Subramanian S., Raghava G.P.; RT "Draft Genome Sequence of the Nitrophenol-Degrading Actinomycete RT Rhodococcus imtechensis RKJ300."; RL J. Bacteriol. 194:3543-3543(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJH01000175; EID72596.1; -; Genomic_DNA. DR EnsemblBacteria; EID72596; EID72596; W59_36658. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 157 159 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 160 160 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 232 AA; 24463 MW; A058C65910550549 CRC64; MTTSHHSNLT DRRRRLGTAR LYLCTDARRE KGDLAQFAEA ALSGGVDIIQ LRDKGSAGEK KFGTMDARDE LAALSVLAAA ARRHGALLAV NDRADMALAA GADVLHLGQG DLPVPYARTV VGSDVLIGRS THSRAQASLA AIEDGVDYFC TGPVWATPTK PGRTASGIDL VRSTADSEPN RPWFAIGGID ESRVPEILAA GASRIVVVRA ITEARDPQAA ARSLSALLQQ NA // ID I0WDF4_9FLAO Unreviewed; 468 AA. AC I0WDF4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=W5A_09299; OS Imtechella halotolerans K1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Imtechella. OX NCBI_TaxID=946077; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K1; RX PubMed=22740661; DOI=10.1128/JB.00506-12; RA Kumar S., Vikram S., Subramanian S., Raghava G.P., Pinnaka A.K.; RT "Genome Sequence of the Halotolerant Bacterium Imtechella halotolerans RT K1T."; RL J. Bacteriol. 194:3731-3731(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJU01000011; EID74420.1; -; Genomic_DNA. DR EnsemblBacteria; EID74420; EID74420; W5A_09299. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 468 AA; 51612 MW; EAB60129BB421C79 CRC64; MKTFYILTIA GHDPSGGAGL TADINTIQNY GLTALSVCTG VTVQNESIFK KCYWSNPNSI KEQLTLLLST YPIKAIKIGI IENLTLLEEL LFIIYSSDPT IKIIWDPILK SGTGYAFHEE LSKQKLLNIV KLCYLVTPNY DELKAISKEE NIENIISEIS SRCHLFLKGG HREDSFKGTD TLYLKNGDSI NFHPPTILNV NRHGTGCALS SSITSLLGQG YSLNESCLLA KEYVYRLLLH TNLVTEKKMT LQYISDGETS EEHLKNIQNA CVSGVKWIQL RMKEFPEKIV LNTAKNALKI CRDHGALLII DDYVSIAKIS GADGVHLGKN DLPPNEARYI LGPEFIIGAT ANTIDDIEDL ANKNIDYVGL GPFKYTPTKK NLSPILGLKG YSSIMKWVKL NNISIPIIAI GGISMEDIAP ILKTGISGIA VSGLLSKQRN NVDLKNTVSS IQKCLLHNSQ PKEIISID // ID I0WDF5_9FLAO Unreviewed; 209 AA. AC I0WDF5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=W5A_09304; OS Imtechella halotolerans K1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Imtechella. OX NCBI_TaxID=946077; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K1; RX PubMed=22740661; DOI=10.1128/JB.00506-12; RA Kumar S., Vikram S., Subramanian S., Raghava G.P., Pinnaka A.K.; RT "Genome Sequence of the Halotolerant Bacterium Imtechella halotolerans RT K1T."; RL J. Bacteriol. 194:3731-3731(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJU01000011; EID74421.1; -; Genomic_DNA. DR EnsemblBacteria; EID74421; EID74421; W5A_09304. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 209 AA; 23909 MW; 9E1F4152E33228D1 CRC64; MKVYQPELIV ITKPENSTNE TYQIIEMFQK GLAVLHLRKP TLSEDETIEF LNTIPEQYHE RIVIHQHYKC INTYNLKGIH FPEAIRKDSS LMQGYLNYFG DKGISISTSF HSPEALLGKQ EAIFQYAFLG PVFNSISKPG YNGKFFNIHK ELLPFPVYAI GGITPEHISK IPKMGFSGVA ALGYIWNNPN PVKAFEQLSN YKNYFSKPL // ID I0X9J9_9SPIO Unreviewed; 216 AA. AC I0X9J9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MSI_11710; OS Treponema sp. JC4. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=1124982; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=JC4; RX PubMed=22815447; DOI=10.1128/JB.00754-12; RA Rosewarne C.P., Cheung J.L., Smith W.J., Evans P.N., Tomkins N.W., RA Denman S.E., O Cuiv P., Morrison M.; RT "Draft genome sequence of Treponema sp. strain JC4, a novel spirochete RT isolated from the bovine rumen."; RL J. Bacteriol. 194:4130-4130(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGU01000009; EID85315.1; -; Genomic_DNA. DR EnsemblBacteria; EID85315; EID85315; MSI_11710. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23540 MW; 9D8A23A704E7F87D CRC64; MKSDKDFDLR KSLLLYAVTD RHWTGEKTLY QQTEEAILGG TTFLQIREKE LNEADFEKEA LELQALCKKY KVPFIVNDNV ELAKKIDADG VHVGQEDMNA CKVRELLGPD KILGVSAQTV EEAILAEKQG ADYLGVGAVF PTGSKSDAID VPHETLKAIC KAVKIPVVAI GGITKNNLCQ LKGSGIAGIS VISAIFAQKD IKAAAEELKK RTLEIL // ID I0XFV0_STAAU Unreviewed; 213 AA. AC I0XFV0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CO23_1543; OS Staphylococcus aureus subsp. aureus CO-23. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904795; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CO-23; RA Jones M., Durkin A.S., Huang X.-Z., Kim M., McGann P., Mishra P., RA Nikolich M., Singh I., Peterson S.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJKF01000061; EID87516.1; -; Genomic_DNA. DR ProteinModelPortal; I0XFV0; -. DR SMR; I0XFV0; 4-209. DR PRIDE; I0XFV0; -. DR EnsemblBacteria; EID87516; EID87516; CO23_1543. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID I0XLS3_9LEPT Unreviewed; 222 AA. AC I0XLS3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Putative thiamine-phosphate diphosphorylase; GN ORFNames=LEP1GSC185_2772; OS Leptospira licerasiae serovar Varillal str. VAR 010. OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=1049972; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=VAR 010; RX PubMed=23145189; DOI=10.1371/journal.pntd.0001853; RA Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P., RA Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., RA Webster N.J., Vinetz J.M., Matthias M.A.; RT "Whole Genome Analysis of Leptospira licerasiae Provides Insight into RT Leptospiral Evolution and Pathogenicity."; RL PLoS Negl. Trop. Dis. 6:E1853-E1853(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHOO02000013; EID99830.1; -; Genomic_DNA. DR EnsemblBacteria; EID99830; EID99830; LEP1GSC185_2772. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 222 AA; 25403 MW; DFE4C6105A6453AA CRC64; MEFPLRPRHS IWRAPGIYPI LDLEYCSKFS KDPVRIVELW SYQREWIPFY QIRAKKETTE TLKNVYKSLI KAFPDFPIIL NDFWEEALEW KCFGLHIGKE DYASLSLKDR KKVRSSGLYL GTSCHNSEDI SGLEPEVWDY TGLGPVYITN SKDTEDAPVG LSGLREALQI AKIPVTPIGG IGPEQIRELS ELGPLSYAMI ASASERDSFY DCIHILKEIK NP // ID I0YPD6_9CHLO Unreviewed; 463 AA. AC I0YPD6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-APR-2014, entry version 10. DE SubName: Full=Uncharacterized protein; DE Flags: Fragment; GN ORFNames=COCSUDRAFT_2352; OS Coccomyxa subellipsoidea C-169. OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; OC Coccomyxaceae; Coccomyxa. OX NCBI_TaxID=574566; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C-169; RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39; RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D., RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., RA Proschold T., Salamov A., Schmutz J., Weeks D., Yamada T., RA Claverie J.M., Grigoriev I., Van Etten J., Lomsadze A., Borodovsky M.; RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea RT reveals traits of cold adaptation."; RL Genome Biol. 13:R39-R39(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSI01000016; EIE20255.1; -; Genomic_DNA. DR RefSeq; XP_005644799.1; XM_005644742.1. DR GeneID; 17038326; -. DR KEGG; csl:COCSUDRAFT_2352; -. DR KO; K14153; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; FT NON_TER 1 1 FT NON_TER 463 463 SQ SEQUENCE 463 AA; 47349 MW; AC91089BD7B68457 CRC64; PRVLTIAGSD SGGGAGIQAD LKTFQACGVY GASAITAVTE QNTHGVRGFH TVPLQTLRGQ IDAVLEDIGA DVVKTGMLPT AEVVEAVADR IVEHRVSCLV VDPVLVSTSG HSLGDSDVAR ALVDRLFPLA TMITPNLPEA SAILGDRPIT DLEGMKAAAI DLHALGPQCV LVKGGHLQQD GGQALDVLYD GETVQVIAGP RVDTPNTHGT GCSTASAIAA ELAKGASPVQ AVHAAKAYVS QALQASAALR IGSGSQTPFN HGYATADWTS KDQVSRLDLR LYAVTDPRQN ERMHRSNVEA VSAAIDGGVT VVQLREKDAD GGDFLAEAEA VIKIARPRGV PVIINDRVDV ALAADADGAH IGQSDLPAAV ARRLLGPHKI LGVSCKTVEH ALAAEAAGAD YVGSGAVYAT NTKDSPIMPI DRLADICAAV SIPVVAIGGI TADNAAPTIE AGCAGVAVVS AIF // ID I0YT79_9CHLO Unreviewed; 832 AA. AC I0YT79; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-APR-2014, entry version 11. DE SubName: Full=Uncharacterized protein; GN ORFNames=COCSUDRAFT_30102; OS Coccomyxa subellipsoidea C-169. OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; OC Coccomyxaceae; Coccomyxa. OX NCBI_TaxID=574566; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C-169; RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39; RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D., RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., RA Proschold T., Salamov A., Schmutz J., Weeks D., Yamada T., RA Claverie J.M., Grigoriev I., Van Etten J., Lomsadze A., Borodovsky M.; RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea RT reveals traits of cold adaptation."; RL Genome Biol. 13:R39-R39(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSI01000012; EIE21598.1; -; Genomic_DNA. DR RefSeq; XP_005646142.1; XM_005646085.1. DR GeneID; 17039582; -. DR KEGG; csl:COCSUDRAFT_30102; -. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003661; EnvZ-like_dim/P. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; SQ SEQUENCE 832 AA; 89352 MW; F9FABACF8E5D5407 CRC64; MIFPRSQLRT HTCLLSPGRS TGVHSSISRC PLGAVGGPQQ RPALCSRGCR KRWQASRIAG VAVAASSRVT VFPAGKKQAK VALPACILVL TAADVVERRQ ELTQSIGDAI AAGATGVLLE DDDGTGGAQL YEAAIVLKDV LRGRAVLLIQ DRTDIVAAAE ADGVVLSSRG VPTVVARRSL PDNANLVGRK VATGHEAVRA AADGASLVIL ESGSGRAVAD AAVIQEAKTQ QGGNVPVIAA LSKEEPVSKE AASDLMPQRA YFYGTLCPRL MTDIISLVQE VVPSMEEVGL LRDALKQLDQ PFLMVVVGEF NSGKSTVINA LLGRRFLAEG ILPTTNEISV LKFRSSHCHT PLCAASFGFL RMLACSQVRY LPAALLRDLN IVDTPGTNVI LERQQRLTEE YVPRADMVLF TMSADRPFTD SEVRFLKYIR QWGKKVVFLV NKVDILSGGD EVEEVAQFVS DNARRVLGVD AAKVLPVSAR AALQAKLDAT SSRNGFFGEA SALHRSSPLE TLDEEALARS GQWGESRFGE LERFMVDFLV GGGAAGESLR LKLQTPLFVA DALLEAARQQ LSSELSTAEQ EAEAVASVQG QLRAFRREME ADGTAQRAEC RRLVATAVRR ARELVDDVLQ LSNREALSAY AARRQWREQR EAVAAQAKDA NADGEAGEGD AEESGSDTAV AALMRFEPKA AALVLEEEIR EAVLSSVSSA VGAGLVGVVL TWILPTTLED VLAIVLTGLA GYVALLNLPL RRAEAKAKLE RVANNFIQEV EDRLKAELES SLDACTAEVN AFIKPLEEAT LAVVERVRDS EIRRAVLADE LEQLKQRAAS VE // ID I0ZC67_HELPX Unreviewed; 219 AA. AC I0ZC67; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HP79_02834; OS Helicobacter pylori P79. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1111674; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P79; RX PubMed=22493206; DOI=10.1128/JB.00230-12; RA Clancy C.D., Forde B.M., Moore S.A., O'Toole P.W.; RT "Draft Genome Sequences of Helicobacter pylori Strains 17874 and RT P79."; RL J. Bacteriol. 194:2402-2402(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHW01000193; EIE28236.1; -; Genomic_DNA. DR ProteinModelPortal; I0ZC67; -. DR EnsemblBacteria; EIE28236; EIE28236; HP79_02834. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23897 MW; 033E0191999238BD CRC64; MFDADCLKLM FVAGSQDFYH IKGGKNDRIN ALLDTLELAL QSKITAFQFR QKGDLALQDP TQIKQLAMKC QKLCQKYGAP FIVNDEVQLA LELKADGVHV GQEDMAIEEV ITLCKKRQFI GLSVNTLEQA LKARHLDAVA YLGVGPIFPT PSKKDKQVVG VELLKKIKDS GIKKPLIAIG GITMHNAPKL REYGGIAVIS AIAQAKDKAL AVGKLLNNA // ID I0ZJ51_HELPX Unreviewed; 219 AA. AC I0ZJ51; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=HP17_05985; OS Helicobacter pylori NCTC 11637 = CCUG 17874. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=102618; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 17874; RX PubMed=22493206; DOI=10.1128/JB.00230-12; RA Clancy C.D., Forde B.M., Moore S.A., O'Toole P.W.; RT "Draft Genome Sequences of Helicobacter pylori Strains 17874 and RT P79."; RL J. Bacteriol. 194:2402-2402(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIHX01000004; EIE30670.1; -; Genomic_DNA. DR EnsemblBacteria; EIE30670; EIE30670; HP17_05985. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23908 MW; 27C6A572D2333735 CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDTLELAL QSKITAFQFR QKGDLALQDP TQIKQLALEC QKLCQKYGTP FIVNDEAKLA LELKADGVHV GQEDMVIEEV ITLCQKCLFI GLSVNTLEQA LKACHLDAVA YFGVGPIFPT PSKKDKQVVG VELLKKIRDS GVKKPLIAIG GITMHNAPKL REYGGIAVIS AITQAKDKAL VIGKLLNNA // ID I0ZL73_ECOLX Unreviewed; 193 AA. AC I0ZL73; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=OQE_42770; OS Escherichia coli J53. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1144303; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J53; RX PubMed=22740669; DOI=10.1128/JB.00641-12; RA Yi H., Cho Y.J., Yong D., Chun J.; RT "Genome Sequence of Escherichia coli J53, a Reference Strain for RT Genetic Studies."; RL J. Bacteriol. 194:3742-3743(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=J53; RA Cho Y.-J., Yong D., Chun J.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICK01000039; EIE34994.1; -; Genomic_DNA. DR EnsemblBacteria; EIE34994; EIE34994; OQE_42770. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 19 23 HMP-PP binding (By similarity). FT REGION 116 118 THZ-P binding (By similarity). FT REGION 168 169 THZ-P binding (By similarity). FT METAL 52 52 Magnesium (By similarity). FT METAL 71 71 Magnesium (By similarity). FT BINDING 51 51 HMP-PP (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 193 AA; 20955 MW; 221F8D93D776B08B CRC64; MDSVQWIERL LDAGVRTLQL RIKDRRDEEV EADVVAAIAL GRRYNARLFI NDYWRLAIKH QAYGVHLGQE DLQATDLNAI RAAGLRLGVS THDDMEIDVA LAARPSYIAL GHVFPTQTKQ MPSAPQGLEQ LARHVERLAD YPTVAIGGIS LARAPAVIAT GVGSIAVVSA ITQAADWRLA TAQLLEIAGV GDE // ID I1A9D0_PSEAI Unreviewed; 209 AA. AC I1A9D0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 12. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CF510_28425; OS Pseudomonas aeruginosa PADK2_CF510. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1134459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PADK2_CF510; RX PubMed=22672046; DOI=10.1111/j.1462-2920.2012.02795.x; RA Rau M.H., Marvig R.L., Ehrlich G.D., Molin S., Jelsbak L.; RT "Deletion and acquisition of genomic content during early stage RT adaptation of Pseudomonas aeruginosa to a human host environment."; RL Environ. Microbiol. 14:2200-2211(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJHI01000068; EIE43101.1; -; Genomic_DNA. DR ProteinModelPortal; I1A9D0; -. DR SMR; I1A9D0; 24-200. DR EnsemblBacteria; EIE43101; EIE43101; CF510_28425. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22146 MW; 898DA261D0AFA265 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER HGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAQ LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID I1AN06_PSEAI Unreviewed; 315 AA. AC I1AN06; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 13-NOV-2013, entry version 11. DE SubName: Full=Uncharacterized protein; GN ORFNames=CF510_02945; OS Pseudomonas aeruginosa PADK2_CF510. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1134459; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PADK2_CF510; RX PubMed=22672046; DOI=10.1111/j.1462-2920.2012.02795.x; RA Rau M.H., Marvig R.L., Ehrlich G.D., Molin S., Jelsbak L.; RT "Deletion and acquisition of genomic content during early stage RT adaptation of Pseudomonas aeruginosa to a human host environment."; RL Environ. Microbiol. 14:2200-2211(2012). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJHI01000004; EIE47877.1; -; Genomic_DNA. DR ProteinModelPortal; I1AN06; -. DR EnsemblBacteria; EIE47877; EIE47877; CF510_02945. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 315 AA; 34029 MW; C96E92F337377371 CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EDGEPVRAAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEAHGAEGQ PLAWVEPREL ADYEFPAANA PIVQAARLPA HYLITPDGSE PGELISGVRK AVEAGIRLIQ LRAPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDAEELAL AASMGVEFVT LSPVQPTESH PGEPALGWDK AAELIAGFNQ PVYLLGGLGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID I1AXV0_9RHOB Unreviewed; 200 AA. AC I1AXV0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=C357_09513; OS Citreicella sp. 357. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Citreicella. OX NCBI_TaxID=766499; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=357; RX PubMed=22965089; DOI=10.1128/JB.01261-12; RA Suarez-Suarez L.Y., Brunet-Galmes I., Pina-Villalonga J.M., RA Christie-Oleza J.A., Pena A., Bennasar A., Armengaud J., Nogales B., RA Bosch R.; RT "Draft Genome Sequence of Citreicella aestuarii Strain 357, a Member RT of the Roseobacter Clade Isolated without Xenobiotic Pressure from a RT Petroleum-Polluted Beach."; RL J. Bacteriol. 194:5464-5465(2012). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJKJ01000071; EIE51321.1; -; Genomic_DNA. DR EnsemblBacteria; EIE51321; EIE51321; C357_09513. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 200 AA; 21351 MW; 45286A1B2C953DD9 CRC64; MRLDPFYLIV SDADALERLV PLGVRLVQLR LKDAGATLPA QIIRARECCA AHGAQLVVND HWQLALDLGC DAVHLGQEDM DTADVDALRA GGVAFGLSTH DDSELARALA LRPAYVALGP VWPTRLKKMK WGPQGLDRVT AWKRASGTVP LVGIGGVTPD RLPALFGAGA DCAAVVTDIQ TAADPAARCR DWLAATRKWA // ID I1AZV7_9RHOB Unreviewed; 206 AA. AC I1AZV7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=C357_05528; OS Citreicella sp. 357. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Citreicella. OX NCBI_TaxID=766499; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=357; RX PubMed=22965089; DOI=10.1128/JB.01261-12; RA Suarez-Suarez L.Y., Brunet-Galmes I., Pina-Villalonga J.M., RA Christie-Oleza J.A., Pena A., Bennasar A., Armengaud J., Nogales B., RA Bosch R.; RT "Draft Genome Sequence of Citreicella aestuarii Strain 357, a Member RT of the Roseobacter Clade Isolated without Xenobiotic Pressure from a RT Petroleum-Polluted Beach."; RL J. Bacteriol. 194:5464-5465(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJKJ01000053; EIE52028.1; -; Genomic_DNA. DR EnsemblBacteria; EIE52028; EIE52028; C357_05528. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 21799 MW; 6131B5705F2ED3F8 CRC64; MADADHPQLY LITPPEFDLS EFPAGLHKVL DAVDIACIRL SLATRDEDRI LRAADAVREV AHARDIALVI DTHIVLAQRL GLDGVHLTDG SRNVRAARKE LGPDAIVGAS CGGSRHDGMS AGEAGADYVS FGPIAGETLG DGTLAEFDLF EWWSQVIEVP VVAEGGLTPD LIARFAPVTD FFGIGEEIWS TDDPAAALAR LAAAMG // ID I1B519_ECOLX Unreviewed; 193 AA. AC I1B519; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=ECAI27_39970; OS Escherichia coli AI27. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1089445; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AI27; RX PubMed=23144394; DOI=10.1128/JB.01749-12; RA Lee K., Yi H., Cho Y.J., Jang J., Hur H.G., Chun J.; RT "Draft Genome Sequence of Escherichia coli AI27, a Porcine Isolate RT Belonging to Phylogenetic Group B1."; RL J. Bacteriol. 194:6640-6641(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJPQ01000108; EIE53840.1; -; Genomic_DNA. DR EnsemblBacteria; EIE53840; EIE53840; ECAI27_39970. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 19 23 HMP-PP binding (By similarity). FT REGION 116 118 THZ-P binding (By similarity). FT REGION 168 169 THZ-P binding (By similarity). FT METAL 52 52 Magnesium (By similarity). FT METAL 71 71 Magnesium (By similarity). FT BINDING 51 51 HMP-PP (By similarity). FT BINDING 90 90 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 193 AA; 20983 MW; A098F4E91C98A095 CRC64; MDSVQWIERL LDAGVRTLQL RIKDRRDEEV EVDVVAAIAL GRRYNARLFI NDYWRLAIKH QAYGVHLGQE DLQATDLNAI RAAGLRLGVS THDDMEIDVA LAARPSYIAL GHVFPTQTKQ MPSAPQGLEQ LARHVERLAD YPTVAIGGIS LARAPAVIAT GVGSIAVVSA ITQAADWRLA TAQLLEIAGV GDE // ID I1CVN3_RHIO9 Unreviewed; 506 AA. AC I1CVN3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-APR-2014, entry version 10. DE SubName: Full=Uncharacterized protein; GN ORFNames=RO3G_17111; OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar). OC Eukaryota; Fungi; Fungi incertae sedis; OC Early diverging fungal lineages; Mucoromycotina; Mucorales; OC Mucorineae; Rhizopodaceae; Rhizopus. OX NCBI_TaxID=246409; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880; RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549; RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M., RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E., RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., RA Kodira C.D., Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S., RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., RA Ruiz-Herrera J., Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., RA Cuomo C.A., Wickes B.L.; RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals RT a whole-genome duplication."; RL PLoS Genet. 5:E1000549-E1000549(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG669512; EIE92513.1; -; Genomic_DNA. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 506 AA; 54212 MW; 27BC745A9D545F0A CRC64; MSIKKVDYSL YLVTDSSLVP DGKTFLGQIE KALEGGVTLV QLREKDSDTG PFVKLALQVK ELTRRFGVPL IINDRIDVAL AVDAEGVHIG QDDMPLAQAR AMLGSKKIIG VSCNNEEEAK AAILGGADYL GIGAVWFTST KKLTKQPLGV EGVKRIMKSM EANRIPAVAI GGISAKNAAE LLEGSQTTHD CLEGLAIVSA IMAAEDPKKT CEELKELIQK SFKKTGIVHD CTVEETLDFA VKKAKSVRSL NPMVHHITNY VVINDNANAT LAVGASPIMS TNRAEIDDLA KVNGAMLLNM GTLNDIDTMI FAAQANHKYG HPVVLDPVGC GATKFRKEIL TRFLDECKLS VIKGNTGEIL SMAGIEGKSR GVDSIGNCEE SLMVDTVKYL ARKNGCIIGM TGPIDYVSDG NRVFAIENGS PFLPLITGSG CLVSSVVACF VAACPKTDHL LATVTAILVV TIASEIASKR EYVNGPGTFR SALIDELYNV TNEPEVIKQF AKIRIL // ID I1D6W4_9PSEU Unreviewed; 225 AA. AC I1D6W4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 11. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SacglDRAFT_03843; OS Saccharomonospora glauca K62. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=928724; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K62; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Brambilla E., Klenk H.-P., RA Woyke T.J.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K62; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Brambilla E.-M., Klenk H.-P., Woyke T.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001484; EIF00689.1; -; Genomic_DNA. DR EnsemblBacteria; EIF00689; EIF00689; SacglDRAFT_03843. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 225 AA; 23843 MW; 3946CEF7A71F9ABD CRC64; MPGLDGDQIR KRLDEARLYL CTDARAHRGD LAEFVDAALS GGVDIVQLRD KTGGAPLEAA REIEALEVLA EACARHGALL AVNDRADVAL AVEADVLHLG QEDLPVAVAR RIVGETPVIG RSTHSPEQAR AAATEPGVDY FCVGPCWPTP TKPGRPAAGL DLVRTVSSEF ETTRPWFAIG GIDETRLDEV VAAGARRIVV VRAITEADDP AAAARALRES LTRAA // ID I1DH49_9VIBR Unreviewed; 458 AA. AC I1DH49; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; ORFNames=VT1337_09517; OS Vibrio tubiashii NCIMB 1337 = ATCC 19106. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=866909; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCIMB 1337; RX PubMed=21677855; RA Temperton B., Thomas S., Tait K., Parry H., Emery M., Allen M., RA Quinn J., Macgrath J., Gilbert J.; RT "Permanent draft genome sequence of Vibrio tubiashii strain NCIMB 1337 RT (ATCC19106)."; RL Stand. Genomic Sci. 4:183-190(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCIMB 1337; RA Temperton B., Thomas S., Tait K., Parry H., Emery M., Allen M., RA Quinn J., McGrath J., Gilbert J.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHHF01000052; EIF04274.1; -; Genomic_DNA. DR EnsemblBacteria; EIF04274; EIF04274; VT1337_09517. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 458 AA; 51094 MW; 4F3C186A0233534E CRC64; MSKILIPSSL IELTGLVQQC LLLAKERGFC VEEVELGVSP TQSVQLVRDQ QITHVATDLI DGYDYDSDYP FTLYYRSGLS VEACAEQPSN AIYIGIADGL ACDKKDEVLQ IDIWRHPIND EVRALSVKSK LNSVFESEYH FAWIVVLTVL DFPIEDALTL ARGMTTQQAN VSRETVLNEK SLTHWAEHFN EFPTPVLEDS RLGIQVGWSA QGESVRFANL TKQSLGLYPV VDDVAWIERL LPLGINTIQL RIKNPQQADL EQQIIRAIEL GRQYKAQVFI NDYWQLAIKH GAYGVHLGQE DIEESNLAQL TKAGIHLGLS THGYYELLRI VQIHPSYIAL GHIFPTTTKQ MPSKPQGLVR LALYQKLIDS IPYGCAHEGA SGLALGYPTV AIGGIDQSNA DQVWQTGVSS LAVVRAITLA QSPKPVIEFF NQLMKERQST FTDSISIATN EEREQHAH // ID I1DPQ2_9PROT Unreviewed; 202 AA. AC I1DPQ2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 10. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; GN ORFNames=UNSWCD_545; OS Campylobacter concisus UNSWCD. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=929793; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UNSWCD; RX PubMed=21829448; DOI=10.1371/journal.pone.0022170; RA Deshpande N.P., Kaakoush N.O., Mitchell H., Janitz K., Raftery M.J., RA Li S.S., Wilkins M.R.; RT "Sequencing and validation of the genome of a Campylobacter concisus RT reveals intra-species diversity."; RL PLoS ONE 6:E22170-E22170(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UNSWCD; RA Deshpande N.P., Kaakoush N.O., Mitchell H., Wilkins M.R.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENQ01000020; EIF06927.1; -; Genomic_DNA. DR EnsemblBacteria; EIF06927; EIF06927; UNSWCD_545. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 202 AA; 22438 MW; 7292A41CDC5EE8F0 CRC64; MFKILCVADF ESYGGDDFLK RIQLLCKAGV DEILLRAKGL SEAHFYDLAR VVAQICENYR KKFVINQFFD VACKLKSDFW LTSAQLDFFK NHGVFLDEFR KTAKIYAPAH DLEQAKISAS IADVLVASHI FATSCKADLE PKGLNFISEL KSLDKEIYAL GGLDSGNYKE AIKAGANGVC FMSLAMSGDI ELIKKIVKSK NG // ID I1DR05_9PROT Unreviewed; 203 AA. AC I1DR05; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 19-FEB-2014, entry version 10. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=UNSWCD_81; OS Campylobacter concisus UNSWCD. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=929793; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UNSWCD; RX PubMed=21829448; DOI=10.1371/journal.pone.0022170; RA Deshpande N.P., Kaakoush N.O., Mitchell H., Janitz K., Raftery M.J., RA Li S.S., Wilkins M.R.; RT "Sequencing and validation of the genome of a Campylobacter concisus RT reveals intra-species diversity."; RL PLoS ONE 6:E22170-E22170(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UNSWCD; RA Deshpande N.P., Kaakoush N.O., Mitchell H., Wilkins M.R.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENQ01000012; EIF07380.1; -; Genomic_DNA. DR EnsemblBacteria; EIF07380; EIF07380; UNSWCD_81. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 22156 MW; ECC9BECA1686CA9B CRC64; MAEIYAISDD ILMPENLALD YTREILECGV KFFQFRSKKA VKNEKLASEI LNLCEKFGAK FIVNDDVKFA KKIGAKAVHL GKDDENIKEA FEILGKGAYV GVSCYNDINL AINAAKNGAS YVAFGSVFVS PTKPNAPKCG LEVVKEAKQI LNLPVCVIGG INETNIGSLS HAKPDLIAVI SAIYKDGNIK ENIKNLQKII KNF // ID I1E0K2_9GAMM Unreviewed; 505 AA. AC I1E0K2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-OCT-2013, entry version 11. DE SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; GN Name=thiD; ORFNames=RNAN_2843; OS Rheinheimera nanhaiensis E407-8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Rheinheimera. OX NCBI_TaxID=562729; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E407-8; RX PubMed=23209246; DOI=10.1128/JB.01922-12; RA Zhang X.-Y., Zhang Y.-J., Qin Q.-L., Xie B.-B., Chen X.-L., RA Zhou B.-C., Zhang Y.-Z.; RT "Genome Sequence of the Protease-Producing Bacterium Rheinheimera RT nanhaiensis E407-8T, Isolated from Deep-Sea Sediment of the South RT China Sea."; RL J. Bacteriol. 194:7001-7002(2012). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E407-8; RA Tserendorj M., Badgar B., Tserendorj N., Thillaiampalam S., RA AbouLaila M., Banzragch B., Byambaa P., Yokoyama N., Igarashi I.; RT "A field study on the prevalence of equine piroplasmosis in Mongolian RT horses."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFK01000017; GAB59830.1; -; Genomic_DNA. DR EnsemblBacteria; GAB59830; GAB59830; RNAN_2843. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 4: Predicted; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 505 AA; 54435 MW; 0B6B4CC164AE6510 CRC64; MPEHTSEAKP IVWTIASSDC GGGAGIQADL HTFAALGCHG CSVIAAVTAQ NSIEVVGYES VSPALFVTQL NCLLQDMPPK AIKIGLIPDV TLLEQLAAWL TQHKAQHQFV VIADPVLSSS SGYQFARQSQ LCIWRQQLLP LVDLLTPNLP ELALLSTMPT PNDEMQAAQL RQFGCAAVLI KGGHATDQAD SCDHYLGVDQ QFSLSLPRLC NTHNHGTGCV LSSAIAAACA QGYALADSVI IARAYLQQAL ANGYATGNGA GSLQHHSWPV TPSYWPLLTC DNEQFAGATQ PDNLSFAGMT TPIGLYPVVD SVAWLKRLLP LEPDVVQLRI KQGSAADIER QIAEAVLLSR DYKLRLFIND YWQLAIKYGA YGVHLGQQDL ASANLAAIAA AGLRLGISTH NYTELTRARQ IRPSYIALGH IFTTQTKQMP SKPQGLVRLK YYAALCRDIP TVAIGGIDAT RLDEVLACGV TGVAVVSAIT AQQQPEQAFL TLKQRVEQHY AHQIK // ID I1ITR8_BRADI Unreviewed; 540 AA. AC I1ITR8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-APR-2014, entry version 10. DE SubName: Full=Uncharacterized protein; GN Name=BRADI4G40670; OS Brachypodium distachyon (Purple false brome) (Trachynia distachya). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Pooideae; Brachypodieae; Brachypodium. OX NCBI_TaxID=15368; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Bd21; RX PubMed=20148030; DOI=10.1038/nature08747; RG International Brachypodium Initiative; RT "Genome sequencing and analysis of the model grass Brachypodium RT distachyon."; RL Nature 463:763-768(2010). RN [2] RP IDENTIFICATION. RC STRAIN=cv. Bd21; RG EnsemblPlants; RL Submitted (NOV-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_003576978.1; XM_003576930.1. DR EnsemblPlants; BRADI4G40670.1; BRADI4G40670.1; BRADI4G40670. DR GeneID; 100833618; -. DR KEGG; bdi:100833618; -. DR KO; K14153; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 540 AA; 57411 MW; B6EE19944821445D CRC64; MPSAPAPPPV LHPRFPASSF SCPRRTHPSP RTRPRRLSAA REMPWPHVLT VAGSDSGGGA GIQADIKACA ALGAYCSSVI TAVTAQNTAG VQGVHLVPEE FIRQQLNSVL SDMSVDVVKT GMLPSAGIVQ ILCESLRKFP VKALVVDPVM VSTSGDALSD PSTLTNYRDE LFSMADIVTP NVKEASKLLG GIPLLTVSDM RDAAASIHKF GPRYVLVKGG DMPDSSEAID IFFDGKEFVE LHGHRIKTRN THGTGCTLAS SIAAELAKGS TMLHAVRVAK NFVESALHHS KDLVIGNGPQ GPFDHLFRLK CPPYNIGSQQ MFNPDSLFLY AVTDSRMNKR WDRSIEDAVK AAIEGGATIV QLREKDAESR EFLEAANACV EICKSRGVPL LINDRVDIAL ACNADGVHVG QSDISAREVR ELLGPGKIIG VSCKTPAQAE QAWNDGADYI GCGGVFPTTT KANNPTLGFE GLKAVCLASK LPVVAIGGIN ATNAGSVMEL GLLNLKGVAV VSALFDRECV MTETRGLRSI LTDAFACFRS // ID I1KUN6_SOYBN Unreviewed; 541 AA. AC I1KUN6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 14-MAY-2014, entry version 11. DE SubName: Full=Uncharacterized protein; OS Glycine max (Soybean) (Glycine hispida). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Glycine; Soja. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82; RX PubMed=20075913; DOI=10.1038/nature08670; RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W., RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., RA May G.D., Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., RA Sandhu D., Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., RA Goodstein D., Barry K., Futrell-Griggs M., Abernathy B., Du J., RA Tian Z., Zhu L., Gill N., Joshi T., Libault M., Sethuraman A., RA Zhang X.-C., Shinozaki K., Nguyen H.T., Wing R.A., Cregan P., RA Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.C., RA Jackson S.A.; RT "Genome sequence of the palaeopolyploid soybean."; RL Nature 463:178-183(2010). RN [2] RP IDENTIFICATION. RC STRAIN=Williams 82; RG EnsemblPlants; RL Submitted (MAY-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_006585496.1; XM_006585433.1. DR EnsemblPlants; GLYMA08G20080.1; GLYMA08G20080.1; GLYMA08G20080. DR GeneID; 100811722; -. DR OMA; NTKANNP; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 541 AA; 57473 MW; 6CDB466A0B2E876D CRC64; MATQLLCMCC GAQPQPQPQA APFMRFPFWN SVHPKNPTSV VRVQAEAADM NMNSIPHVLS VAGSDSGGGA GIQADLKTCA ARRVYCSTVI TAVTAQNTAG VQGLNILPED FVADQLHSVL SDMHVHVVKT GMLPSLNIVK VLCQTLRKFP IKALVVDPVM ISTSGDVLVG PSVLAGFLEE LLPMTDIVTP NIKEASVLLG GVPLKSVSDM RTAAKLIHDL GPRNVLVKGG DLPNSLDAID VFFDGEEFYE LCSPRVNTRN SHGTGCTLAS CIAAELAKGS SMLSAVKTAK HFIEAALDYS RDMTIGNGAQ GPFDHFLALN INQSSCRLNR FNPNDLLLYA VTDSAMNRKW GRSIAEAVKA AVEGGATIVQ LREKDAETRD FLEAAKVCLE ICHSYGVPLL INDRIDVALA CDADGVHVGQ SDMPARLART LLGPEKIIGV SCKTPEQAHQ AWIDGADYIG CGGVYPTNTK ANNRTIGLEG LKEVCLASTL PVVAIGGIGL SNAREVMKLG APNLNGVAVV SALFDRECIL TETRNLHALV S // ID I1L837_SOYBN Unreviewed; 915 AA. AC I1L837; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 14-MAY-2014, entry version 13. DE SubName: Full=Uncharacterized protein; OS Glycine max (Soybean) (Glycine hispida). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Glycine; Soja. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82; RX PubMed=20075913; DOI=10.1038/nature08670; RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W., RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., RA May G.D., Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., RA Sandhu D., Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., RA Goodstein D., Barry K., Futrell-Griggs M., Abernathy B., Du J., RA Tian Z., Zhu L., Gill N., Joshi T., Libault M., Sethuraman A., RA Zhang X.-C., Shinozaki K., Nguyen H.T., Wing R.A., Cregan P., RA Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.C., RA Jackson S.A.; RT "Genome sequence of the palaeopolyploid soybean."; RL Nature 463:178-183(2010). RN [2] RP IDENTIFICATION. RC STRAIN=Williams 82; RG EnsemblPlants; RL Submitted (MAY-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_003536908.1; XM_003536860.2. DR EnsemblPlants; GLYMA10G03190.1; GLYMA10G03190.1; GLYMA10G03190. DR GeneID; 100808213; -. DR KEGG; gmx:100808213; -. DR OMA; ESAERCE; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 915 AA; 101271 MW; 2030042B9EF49963 CRC64; MVPCSVTSPS SPFTAIIPRH THSRSPSLPL RVARAFPINS LSNNAESSAQ FNQQLFRPSY PPQQPRTLFP GGYKRPELNV PTLVLQLDPD EFLSADTDAL ALIDKAVSKW VGIVVLASNQ ASGGKLYEAA CSLKSLLQDR AYLLVAERVD IAAAAAASGV LLSDQGLPTV VARNMMLDSK SELVVLPLVA RIVRTVDAAV NASKSEGADF LIYGGGDLNR VGQEVGSVYE SVKIPIFVSC GKNMSYTDAS GLFASGASGF VTSLENFGLF GDEFLHKLFG TVYASDDGGN MSENKLNVDN GFQSETEVVA GFVKLEDREK LLIETERLVL NEAIEAIKRA APLMEEVSLL NDAVSQIDEP FLLVIVGEFN SGKSTVINAL LGERYLKEGV VPTTNEITFL RYTDLDIEQQ RCERHPDGQY ICYIPAPILK EMTIVDTPGT NVILQRQQRL TEEFVPRADL LLFVISADRP LTGSEIAFLR YSQQWKKKAV FVLNKADIYQ NNHELEEAMS FIKDNIQRLL NTEDVMLYPV SARSALEAKL MATSNAGRLN EELSTSYSHY GASSFSELEN FLYSFLDGST IPGMDRMRLK LETPVAIADR LISACETLVT QDYRYAKQDL AAVEDIVNNV NDFALNMVTE SLSWRRPTLS LIETTKSRVV ELVEANLQLS NFDIIASYAF KGEKNALPTT SRIQNDIIGP AVSAVQKILE EYENWLYSKY TQQGRLYKES FEKRWPSLSH ESSQINFGTD QLLKKVDQAG SQVIDNFSSI AVSKSFEQEV REMILGTFGQ LGVAGLSASL LTSVLQTTLE DLLALGICSA GGYLAISTFP ARRQKVIDKV KTKAETLAYE LEEAMKKDLT EAIENLDTFV KVLSKPYQDE AQNRLNRLVE IQEELSNVEK KLRTLQIDIQ NLHVS // ID I1LTF7_SOYBN Unreviewed; 514 AA. AC I1LTF7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 14-MAY-2014, entry version 10. DE SubName: Full=Uncharacterized protein; OS Glycine max (Soybean) (Glycine hispida). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Glycine; Soja. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82; RX PubMed=20075913; DOI=10.1038/nature08670; RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W., RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., RA May G.D., Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., RA Sandhu D., Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., RA Goodstein D., Barry K., Futrell-Griggs M., Abernathy B., Du J., RA Tian Z., Zhu L., Gill N., Joshi T., Libault M., Sethuraman A., RA Zhang X.-C., Shinozaki K., Nguyen H.T., Wing R.A., Cregan P., RA Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.C., RA Jackson S.A.; RT "Genome sequence of the palaeopolyploid soybean."; RL Nature 463:178-183(2010). RN [2] RP IDENTIFICATION. RC STRAIN=Williams 82; RG EnsemblPlants; RL Submitted (MAY-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblPlants; GLYMA12G29140.1; GLYMA12G29140.1; GLYMA12G29140. DR OMA; WINAIRS; -. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 514 AA; 54838 MW; 49C091E0D2A34100 CRC64; MRFPFWNSVH PKNLMSVRVL QAEADMKIPH VLSVAGSDSG GGAGIQADLK TCGARRVYCS TVITAVTAQN TAGVQGLNIL PEDFVADQLH SVLSDMHVHV VKTGMLPSLN IVKVLSQTLR KFPIKALVVD PVMISTSGDV LVGPSVLAGF LEELLPMTDI VTPNIKEASV LLGGVPLKSV SDMRTAAKLI HDLGPRNVLV KGGDLPNSLD AIDVFFDGED FYELCSPRVN TRNSHGTGCT LASCIAAELA KGSSMLSAVK TAKHFIQAAL DYSRDMTIGN GAQGPFDHFL ALKINQSSYR QNRFNPNDLL LYAVTDSAMN RKWDRSIAEA VKAAVEGGAT IVQIREKDAE TRDFLEAAKE CLKICHSYGV PLLINDRIDV ALACDADGVH VGQSDVPARL ARTLLGPEKI IGVSCKTPEQ AHQAWIDGAD YIGCGGVYPT NTKANNRTIG LEGLKEICLA SKLPVVAIGG IGLSNAREVM ELGVPNLNGV AVVSALFGRE CILTETRNLH ALVS // ID I1R4Q4_ORYGL Unreviewed; 548 AA. AC I1R4Q4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 16-APR-2014, entry version 9. DE SubName: Full=Uncharacterized protein; OS Oryza glaberrima (African rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4538; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L., RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K., RA Zuccolo A.; RT "The complete genome of Oryza glaberrima."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (APR-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblPlants; ORGLA12G0051000.1; ORGLA12G0051000.1; ORGLA12G0051000. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 548 AA; 57858 MW; 9F1669B2C5163899 CRC64; MAAAPQQSVH PSLPSSTSTL RLLISSSPRR PPPPPPRARR YNRFAASASA AREMPWPHVL TVAGSDSGGG AGIQADIKAC AALGAYCSSV VTAVTAQNTA GVQGIHVVPE EFIREQLNSV LSDMSVDVVK TGMLPSIGVV RVLCESLKKF PVKALVVDPV MVSTSGDTLS ESSTLSVYRD ELFAMADIVT PNVKEASRLL GGVSLRTVSD MRNAAESIYK FGPKHVLVKG GDMLESSDAT DVFFDGKEFI ELHAHRIKTH NTHGTGCTLA SCIASELAKG ATMLHAVQVA KNFVESALHH SKDLVIGNGP QGPFDHLFKL KCLPYNVGSQ PSFKPDQLFL YAVTDSGMNK KWGRSIKEAV QAAIEGGATI VQLREKDSET REFLEAAKAC MEICKSSGVP LLINDRVDIA LACNADGVHV GQSDMSAHEV RELLGLGKII GVSCKTPAQA QQAWNDGADY IGCGGVFPTS TKANNPTLGF DGLKTVCLAS KLPVVAIGGI NASNAGSVME LGLPNLKGVA VVSALFDRPS VVAETRNMKS ILTNTSRT // ID I1RSX7_GIBZE Unreviewed; 511 AA. AC I1RSX7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 14-MAY-2014, entry version 11. DE SubName: Full=Uncharacterized protein; GN Name=FG07264.1; ORFNames=FGSG_07264; OS Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) OS (Wheat head blight fungus) (Fusarium graminearum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae; OC Fusarium. OX NCBI_TaxID=229533; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084; RX PubMed=17823352; DOI=10.1126/science.1143708; RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., RA Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., RA Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., RA Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J., RA Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., RA Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., RA Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., RA Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.; RT "The Fusarium graminearum genome reveals a link between localized RT polymorphism and pathogen specialization."; RL Science 317:1400-1402(2007). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PH-1; RG The Broad Institute Genome Sequencing Platform; RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., RA Mauceli E., Brockman W., MacCallum I.A., Young S., LaButti K., RA DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., RA Pearson M., Howarth C., Larson L., White J., O'Leary S., Kodira C., RA Zeng Q., Yandava C., Alvarado L., Kistler C., Xu J.-R., Trail F.; RT "Genome Sequence of Fusarium graminearum (Gibberella zeae)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [3] RP GENOME REANNOTATION. RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084; RX PubMed=20237561; DOI=10.1038/nature08850; RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., RA Daboussi M.J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., RA Henrissat B., Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., RA Xu J.R., Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., RA Brown D.W., Butchko R.A., Chapman S., Coulson R., Coutinho P.M., RA Danchin E.G., Diener A., Gale L.R., Gardiner D.M., Goff S., RA Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., RA Kodira C.D., Koehrsen M., Kumar L., Lee Y.H., Li L., Manners J.M., RA Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.Y., RA Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., RA Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., RA Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., RA Rep M.; RT "Comparative genomics reveals mobile pathogenicity chromosomes in RT Fusarium."; RL Nature 464:367-373(2010). RN [4] RP IDENTIFICATION. RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084; RG EnsemblFungi; RL Submitted (OCT-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS231666; ESU13495.1; -; Genomic_DNA. DR RefSeq; XP_387440.1; XM_387440.1. DR ProteinModelPortal; I1RSX7; -. DR EnsemblFungi; FGSG_07264T0; FGSG_07264P0; FGSG_07264. DR GeneID; 2788453; -. DR KEGG; fgr:FG07264.1; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 511 AA; 53198 MW; D5820A18DA206F9A CRC64; MTMTAKPSVN YGLYLVTDST PEILGDRNLE HVVEESLRGG VTILQYRDKH SERSIAVYTA KKLHAIARRY NVPLLINDRV DVAVEVGCEG VHIGQDDMAY EEARKLLGPG KIIGVTASSK EEALKACKAG ADYLGIGTVY STQTKKDTKS IIGPSGVRDI LSALHDAGYG SVPTVCIGGI NASNTAPVLA SAGSPSKALD GVAVVSALIA APDPAAAARD LLSKVVTTKI PEVIRAVVDK TPLSHNMTNL VVQNFAANVA LCVGASPIMA NYAEEAADLA KLGGALVVNM GTVTPDGLKN YLQAIKAYNE AGRPIVLDPV GAGATVVRRN AVKTLLDAGH FTIIKGNEGE IQTIAGATIT QRGVDSTSSL SFAQKASLVR SVALYRRNVV ILTGAVDLIS DGTRTLAISN GHPYLGEVTG TGCTLGTTVS AMVAAYDTDP LLAAVAGTVM FGLAAELAAK RPEVRGPGTF VPAFLDELYA IRKSTASGDL MWLSMAQVKA VEVNVDDTAA E // ID TPS1L_ARATH Reviewed; 522 AA. AC Q5M731; O23128; Q8L7M9; DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 14-MAY-2014, entry version 68. DE RecName: Full=Thiamine biosynthetic bifunctional enzyme TH1, chloroplastic; DE Includes: DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; DE Includes: DE RecName: Full=Hydroxymethylpyrimidine kinase; DE Short=HMP kinase; DE EC=2.7.1.49; DE Flags: Precursor; GN Name=TH1; OrderedLocusNames=At1g22940; ORFNames=F19G10.10; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.; RT "Arabidopsis ORF clones."; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=cv. Columbia; RX PubMed=16666289; RA Komeda Y., Tanaka M., Nishimune T.; RT "A th-1 mutant of Arabidopsis thaliana is defective for a thiamin- RT phosphate-synthesizing enzyme: thiamin phosphate pyrophosphorylase."; RL Plant Physiol. 88:248-250(1988). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS RP OF SER-63. RX PubMed=17174261; DOI=10.1016/j.abb.2006.11.011; RA Ajjawi I., Tsegaye Y., Shintani D.; RT "Determination of the genetic, molecular, and biochemical basis of the RT Arabidopsis thaliana thiamin auxotroph th1."; RL Arch. Biochem. Biophys. 459:107-114(2007). CC -!- FUNCTION: Essential for thiamine biosynthesis. Bifunctional enzyme CC that catalyzes the phosphorylation of hydroxymethylpyrimidine CC phosphate (HMP-P) to HMP-PP and condenses 4-methyl-5-(beta- CC hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino- CC 5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine CC monophosphate (TMP). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-5-hydroxymethyl-2- CC methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2- CC methylpyrimidine. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.8 uM for 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate; CC KM=2.7 uM for thiamine phosphate; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole: step 2/3. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- DISRUPTION PHENOTYPE: Seedling lethality. Mutant plants can grow CC on synthetic medium supplied with thiamine. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAB72162.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF000657; AAB72162.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002684; AEE30313.1; -; Genomic_DNA. DR EMBL; AY128364; AAM91567.1; -; mRNA. DR EMBL; BT020417; AAV97808.1; -; mRNA. DR PIR; E86363; E86363. DR RefSeq; NP_173707.2; NM_102141.3. DR UniGene; At.43074; -. DR UniGene; At.49905; -. DR ProteinModelPortal; Q5M731; -. DR SMR; Q5M731; 29-496. DR STRING; 3702.AT1G22940.1-P; -. DR PRIDE; Q5M731; -. DR EnsemblPlants; AT1G22940.1; AT1G22940.1; AT1G22940. DR GeneID; 838901; -. DR KEGG; ath:AT1G22940; -. DR TAIR; AT1G22940; -. DR InParanoid; Q5M731; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR PhylomeDB; Q5M731; -. DR BioCyc; ARA:AT1G22940-MONOMER; -. DR BioCyc; MetaCyc:AT1G22940-MONOMER; -. DR UniPathway; UPA00060; UER00137. DR UniPathway; UPA00060; UER00141. DR Genevestigator; Q5M731; -. DR GO; GO:0009507; C:chloroplast; IDA:TAIR. DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IGI:TAIR. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IGI:TAIR. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IDA:TAIR. DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:TAIR. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 1: Evidence at protein level; KW ATP-binding; Chloroplast; Complete proteome; Kinase; Magnesium; KW Metal-binding; Multifunctional enzyme; Nucleotide-binding; Plastid; KW Reference proteome; Thiamine biosynthesis; Transferase; KW Transit peptide. FT TRANSIT 1 36 Chloroplast (Potential). FT CHAIN 37 522 Thiamine biosynthetic bifunctional enzyme FT TH1, chloroplastic. FT /FTId=PRO_0000420252. FT REGION 345 349 HMP-PP binding (By similarity). FT REGION 442 444 THZ-P binding (By similarity). FT REGION 495 496 THZ-P binding (By similarity). FT METAL 378 378 Magnesium (By similarity). FT METAL 397 397 Magnesium (By similarity). FT BINDING 377 377 HMP-PP (By similarity). FT BINDING 416 416 HMP-PP (By similarity). FT BINDING 445 445 HMP-PP (By similarity). FT BINDING 472 472 THZ-P; via amide nitrogen (By FT similarity). FT MUTAGEN 63 63 S->F: In th1-201; loss of activity and FT seedling lethality. FT CONFLICT 301 301 S -> P (in Ref. 3; AAM91567). SQ SEQUENCE 522 AA; 55813 MW; D10B8D6C34641B4A CRC64; MNSLGGIRSW PANWRSTTAS MTTTESVRKV PQVLTVAGSD SGAGAGIQAD LKVCAARGVY CASVITAVTA QNTRGVQSVH LLPPEFISEQ LKSVLSDFEF DVVKTGMLPS TEIVEVLLQN LSDFPVRALV VDPVMVSTSG HVLAGSSILS IFRERLLPIA DIITPNVKEA SALLDGFRIE TVAEMRSAAK SLHEMGPRFV LVKGGDLPDS SDSVDVYFDG KEFHELRSPR IATRNTHGTG CTLASCIAAE LAKGSSMLSA VKVAKRFVDN ALDYSKDIVI GSGMQGPFDH FFGLKKDPQS SRCSIFNPDD LFLYAVTDSR MNKKWNRSIV DALKAAIEGG ATIIQLREKE AETREFLEEA KACIDICRSH GVSLLINDRI DIALACDADG VHVGQSDMPV DLVRSLLGPD KIIGVSCKTP EQAHQAWKDG ADYIGSGGVF PTNTKANNRT IGLDGLKEVC EASKLPVVAI GGIGISNAGS VMQIDAPNLK GVAVVSALFD QDCVLTQAKK LHKTLKESKR GI // ID TPS1_BRANA Reviewed; 523 AA. AC O48881; DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 19-FEB-2014, entry version 60. DE RecName: Full=Thiamine biosynthetic bifunctional enzyme BTH1, chloroplastic; DE Includes: DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; DE Includes: DE RecName: Full=Hydroxymethylpyrimidine kinase; DE Short=HMP kinase; DE EC=2.7.1.49; DE Flags: Precursor; GN Name=BTH1; OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC Brassica. OX NCBI_TaxID=3708; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE RP SPECIFICITY, AND INDUCTION. RX PubMed=9700068; DOI=10.1023/A:1006030617502; RA Kim Y.S., Nosaka K., Downs D.M., Kwak J.M., Park D., Chung I.K., RA Nam H.G.; RT "A Brassica cDNA clone encoding a bifunctional hydroxymethylpyrimidine RT kinase/thiamin-phosphate pyrophosphorylase involved in thiamin RT biosynthesis."; RL Plant Mol. Biol. 37:955-966(1998). CC -!- FUNCTION: Essential for thiamine biosynthesis. Bifunctional enzyme CC that catalyzes the phosphorylation of hydroxymethylpyrimidine CC phosphate (HMP-P) to HMP-PP and condenses 4-methyl-5-(beta- CC hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino- CC 5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine CC monophosphate (TMP). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-5-hydroxymethyl-2- CC methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2- CC methylpyrimidine. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole: step 2/3. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and stems. CC -!- INDUCTION: Down-regulated by treatment with exogenous thiamine. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF015310; AAC31298.1; -; mRNA. DR PIR; T07834; T07834. DR ProteinModelPortal; O48881; -. DR BRENDA; 2.7.1.49; 393. DR BRENDA; 2.7.4.7; 393. DR UniPathway; UPA00060; UER00137. DR UniPathway; UPA00060; UER00141. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IGI:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IGI:UniProtKB. DR GO; GO:0009228; P:thiamine biosynthetic process; IGI:UniProtKB. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 1: Evidence at protein level; KW ATP-binding; Chloroplast; Kinase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Plastid; KW Thiamine biosynthesis; Transferase; Transit peptide. FT TRANSIT 1 38 Chloroplast (Potential). FT CHAIN 39 523 Thiamine biosynthetic bifunctional enzyme FT BTH1, chloroplastic. FT /FTId=PRO_0000420253. FT REGION 346 350 HMP-PP binding (By similarity). FT REGION 443 445 THZ-P binding (By similarity). FT REGION 496 497 THZ-P binding (By similarity). FT METAL 379 379 Magnesium (By similarity). FT METAL 398 398 Magnesium (By similarity). FT BINDING 378 378 HMP-PP (By similarity). FT BINDING 417 417 HMP-PP (By similarity). FT BINDING 446 446 HMP-PP (By similarity). FT BINDING 473 473 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 523 AA; 56045 MW; A9EFA395207EE4EB CRC64; MQSLGGIRSW PATWRTTTAS MTTTTTESVR KVAQVLTVAG SDSGAGAGIQ ADIKVCAARG VYCASVKTAV KAKNTRAVQS VHLLPPDSVS EQLKSVLSDF EVDVVKTGML PSPEIVEVLL QNLSEYPVRA LVVDPVMVST SGHVLAGSSI LSIFRERLLP LADIITPNVK EASALLGGVR IQTVAEMRSA AKSLHQMGPR FVLVKGGDLP DSSDSVDVYF DGNEFHELHS PRIATRNTHG TGCTLASCIA AELAKGSNML SAVKVAKRFV DSALNYSKDI VIGSGMQGPF DHFLSLKDPQ SYRQSTFKPD DLFLYAVTDS RMNKKWNRSI VDAVKAAIEG GATIIQLREK EAETREFLEE AKSCVDICRS NGVCLLINDR FDIAIALDAD GVHVGQSDMP VDLVRSLLGP DKIIGVSCKT QEQAHQAWKD GADYIGSGGV FPTNTKANNR TIGLDGLREV CKASKLPVVA IGGIGISNAE SVMRIGEPNL KGVAVVSALF DQECVLTQAK KLHKTLTESK REH // ID O54234_STRLI Unreviewed; 176 AA. AC O54234; DT 01-JUN-1998, integrated into UniProtKB/TrEMBL. DT 01-JUN-1998, sequence version 1. DT 16-OCT-2013, entry version 73. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN Name=thiC; OS Streptomyces lividans. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1916; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1326; RX PubMed=9515933; RA Blanco J., Coque J.R., Martin J.; RT "The folate branch of the methionine biosynthesis pathway in RT Streptomyces lividans: disruption of the 5,10- RT methylenetetrahydrofolate reductase gene leads to methionine RT auxotrophy."; RL J. Bacteriol. 180:1586-1591(1998). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ001630; CAA04884.1; -; Genomic_DNA. DR ProteinModelPortal; O54234; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT NON_TER 1 1 SQ SEQUENCE 176 AA; 18359 MW; 48E5FE862E7BF4EF CRC64; QLRDKGMEAA EELEHLAVFA DACARHGKLL AVNDADVAHA ARADVLHLGQ GDLPVPAARA ILGDDVLIGR STHAESEAAA AAAQEGVDYF CTGPCWPTPT KPGRHAPGLD LVRRTAALGT DRPWFAIGGI DLGNLDEVLE AAARRVVVVR AITAAEDPGA AAAEFARRLR QAPAHG // ID Q00Y64_OSTTA Unreviewed; 669 AA. AC Q00Y64; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 19-FEB-2014, entry version 44. DE SubName: Full=Hydroxymethylpyrimidine kinase (ISS); GN OrderedLocusNames=Ot12g00960; OS Ostreococcus tauri. OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales; OC Ostreococcus. OX NCBI_TaxID=70448; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OTTH0595; RX PubMed=16868079; DOI=10.1073/pnas.0604795103; RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S., RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J., RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P., RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., RA Demaille J., Van de Peer Y., Moreau H.; RT "Genome analysis of the smallest free-living eukaryote Ostreococcus RT tauri unveils many unique features."; RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAID01000012; CAL57187.1; -; Genomic_DNA. DR RefSeq; XP_003082241.1; XM_003082193.1. DR ProteinModelPortal; Q00Y64; -. DR STRING; 70448.Q00Y64; -. DR GeneID; 9836099; -. DR KEGG; ota:Ot12g00960; -. DR eggNOG; COG0351; -. DR KO; K14153; -. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.30.70.330; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF00076; RRM_1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SMART; SM00360; RRM; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50102; RRM; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Transferase. SQ SEQUENCE 669 AA; 70704 MW; 18DD2BBED9C9E234 CRC64; MKTRIARVPS HHRRTIGPSR TRRWTNERTR AIERPPPRPS ARAPPSIDRF ERPSHAEHRL AQCTMSTSKG VKATLGSIDP GASISPFTSA SSTSSLSTDN CACFNARVDD DAPVKSVKTA SRGMSGTASA SAKASTSVAI PPRTASPLTA VDDGRPTAVY VASLTWWTTD AELEGILAEF GRVKSLTFFA DKATGKSKGC CAVEFTTSDA AAACKEKLHG RQINGKACVV TFAEIPKTPA ATIGPNDPLP PPPDTAWKGP IPQDKPGYGG VLYAPPKQMD IKRHQLKNVV VDTVMRAKGG ASLMDADAID DLRDELCPLA TIVTPNVPEA AALLGMDEEA FGRVDMATRA KELGTRLQSE WVLLKGGHCA EKDKGGVAID YLYERATGET TTFEGVRFST PHTHGTGCTL ASSIAASLAQ GYDVPTAVRR AKVYISEAIR TNPGYGTGHG PLNHLPYYAA TASMGKVFRP SALRLYLVSC EALTLEKLEQ ALQSGVTIVQ MRDKNPSTRA LVERARAMKA VCDRYSVPFI VNDRCDVAIA VDADGVHLGQ SDMTCVEARN ILGPNKWIGV SCRTEDLARA AKVDGADYIG CGACFGTDSK GDAQVIGVDG VAKVAAVARE ILLPIVAIGG ISCETASDVR ARTGADGVAV ISCVANAPDV ADAVCRLLA // ID Q00ZF0_OSTTA Unreviewed; 849 AA. AC Q00ZF0; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 44. DE SubName: Full=Mitofusin 1 GTPase, involved in mitochondrila biogenesis (ISS); GN OrderedLocusNames=Ot11g00040; OS Ostreococcus tauri. OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales; OC Ostreococcus. OX NCBI_TaxID=70448; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OTTH0595; RX PubMed=16868079; DOI=10.1073/pnas.0604795103; RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S., RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J., RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P., RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., RA Demaille J., Van de Peer Y., Moreau H.; RT "Genome analysis of the smallest free-living eukaryote Ostreococcus RT tauri unveils many unique features."; RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAID01000011; CAL55609.1; -; Genomic_DNA. DR RefSeq; XP_003081806.1; XM_003081758.1. DR ProteinModelPortal; Q00ZF0; -. DR STRING; 70448.Q00ZF0; -. DR PRIDE; Q00ZF0; -. DR GeneID; 9835775; -. DR KEGG; ota:Ot11g00040; -. DR eggNOG; COG0699; -. DR HOGENOM; HOG000241410; -. DR OMA; PTTHRIN; -. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. PE 4: Predicted; KW Complete proteome; GTP-binding; Nucleotide-binding. SQ SEQUENCE 849 AA; 92117 MW; 9384701EA88FAF6E CRC64; MSRACAGGHR SIPTSSASTP ALSRSRRLGR WEHIRRQRRA TTTTRAFLKK RTGVERDDET SEKRSLFASG SKRSEIRIPG FVAYVDVREA STERGTRAID NALHAGATMI VLQERGMNGG VGESASGRAL YESATALKDL VRGRAKVLIQ DRTDIAVQAE LDGVVLTDDG VPTVVARKTL SPKAVVAHVS DDAVEAEKAS KEGADVLLVS SLRTLSELRE KVSVPIFVDV QGGVSTLLGE DSSTLNGLTI NGANGVTICD IVSDEMCADE ARVKLAVSAV VDALTQNAVN VDRARARALG GDFDIKLLVE ARKSIEDLFL LVIVGEFNAG KSSVINAFLG DKFVAEGILP TTNEITVLRY GERKAREQSE DGFFTYKIPA EILRQVRIVD TPGTNVILQR QQKLTEEFVP RADLILFVLS ADRPMTESEV KFLTYIRKWG KKVVFVVNKT DLLEEANDVR DVSQFVKDNA ERLLGVNDPA VLPVSARKAL KAKKANANYV GTREFVDSGF GQFEDYVMSY LGGSGERAGE ALRLKLLTPL NVCTLLLDAA EQILETEDDE AKSEVAIAIG VKTQMDDYTK EMVADSKAQQ EATRSIVQAA IKRAERIVDD TLRLSNALSL FNTYILGTGS SGVASQYEKL VLGDSEERLG AACEEFSAWL DRNNEAQLQA YIDAVKGRGF DASLSSVDNE KEERAKSLSV VSNFDHTAAA QLLDKSIGKA VETTIGSAGG AFVASFFLSG FFNSFSEDVL VYALGLAGAY IAVLSLPLKR SEIKSKIRRS AAAFLTELEE TMENECTTQV GSTTQKISTI CAPWAAAARA EAARVAECLE ARRELKKSLE KMMIDVANL // ID Q01SR9_SOLUE Unreviewed; 200 AA. AC Q01SR9; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Acid_6375; OS Solibacter usitatus (strain Ellin6076). OC Bacteria; Acidobacteria; Solibacteres; Solibacterales; OC Solibacteraceae; Candidatus Solibacter. OX NCBI_TaxID=234267; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin6076; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., RA Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., RA Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., RA Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C., RA Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., RA Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., RA Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., RA Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., RA Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000473; ABJ87301.1; -; Genomic_DNA. DR RefSeq; YP_827586.1; NC_008536.1. DR ProteinModelPortal; Q01SR9; -. DR STRING; 234267.Acid_6375; -. DR EnsemblBacteria; ABJ87301; ABJ87301; Acid_6375. DR GeneID; 4425474; -. DR KEGG; sus:Acid_6375; -. DR PATRIC; 32015442; VBICanSol30224_6672. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SUSI234267:GHSK-6424-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 200 AA; 20973 MW; 9B4974080DD7ACDF CRC64; MLRYYITDRR AAGGVEPLLL HVERAARDGV ERIQVREKDL CARDLCALVR RILGLARPHG TQVLVNSRVD VALAAGADGV HLAGSSIAPK ILRRILPSGF QIGVSTHCFA DLRAAEAEGA DFVVYGPVFP VVSKPGYAAH VGIDGLRRAV RAVTIPVIAL GGVTQSNAAA CIEAGVAGVA GISMFQNPLD PPAVGQERAL // ID Q01WR4_SOLUE Unreviewed; 212 AA. AC Q01WR4; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 60. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Acid_4942; OS Solibacter usitatus (strain Ellin6076). OC Bacteria; Acidobacteria; Solibacteres; Solibacterales; OC Solibacteraceae; Candidatus Solibacter. OX NCBI_TaxID=234267; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin6076; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., RA Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., RA Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., RA Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C., RA Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., RA Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., RA Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., RA Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., RA Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000473; ABJ85901.1; -; Genomic_DNA. DR RefSeq; YP_826186.1; NC_008536.1. DR ProteinModelPortal; Q01WR4; -. DR STRING; 234267.Acid_4942; -. DR EnsemblBacteria; ABJ85901; ABJ85901; Acid_4942. DR GeneID; 4426841; -. DR KEGG; sus:Acid_4942; -. DR PATRIC; 32012412; VBICanSol30224_5169. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SUSI234267:GHSK-4981-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22889 MW; 3833F67624F37D33 CRC64; MKLPRVYPIL DTESLDRRGI LLETAAASFL DGGAAILQIR HKSHWSRTFF ESARTVARLC REAGTPLIVN DRADFAMLLE AGLHIGQADL SPRDARRLIG PDAALGFSSH NVNQLCAAGG EPVDYVALGP IFITASKQNP DPVTGIGELR RCRPLIEKPL VAIGGITQEN ALQVLEAGAD SLAVIAGLLP ENATAHSLRE RMEQWQRLVK AA // ID Q02H40_PSEAB Unreviewed; 315 AA. AC Q02H40; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Putative pyrophosphohydrolase; GN Name=mutT; OrderedLocusNames=PA14_57190; OS Pseudomonas aeruginosa (strain UCBPP-PA14). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCBPP-PA14; RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90; RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., RA Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.; RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is RT combinatorial."; RL Genome Biol. 7:R90.1-R90.14(2006). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000438; ABJ13671.1; -; Genomic_DNA. DR RefSeq; YP_792746.1; NC_008463.1. DR ProteinModelPortal; Q02H40; -. DR STRING; 208963.PA14_57190; -. DR EnsemblBacteria; ABJ13671; ABJ13671; PA14_57190. DR GeneID; 4382505; -. DR KEGG; pau:PA14_57190; -. DR PATRIC; 19855538; VBIPseAer79785_4698. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PAER208963:GI5K-4648-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34069 MW; 1EBE0F34D4D4D503 CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EDGEPVRAAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEAHGVEGQ PLAWVEPREL ADYEFPAANA PIVQAARLPA HYLITPDGLE PGELISGVRK AVEAGIRLIQ LRAPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDAEELAL AASMGVEFVT LSPVQPTESH PGEPALGWDK AAELIAGFNQ PVYLLGGVGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID Q03X15_LEUMM Unreviewed; 212 AA. AC Q03X15; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 63. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LEUM_1159; OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / OS NCDO 523). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=203120; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8293 / NCDO 523; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., RA Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., RA Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., RA Broadbent J., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M., RA Klaenhammer T., Richardson P., Kozyavkin S., Weimer B., Mills D.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000414; ABJ62257.1; -; Genomic_DNA. DR RefSeq; YP_818630.1; NC_008531.1. DR ProteinModelPortal; Q03X15; -. DR STRING; 203120.LEUM_1159; -. DR EnsemblBacteria; ABJ62257; ABJ62257; LEUM_1159. DR GeneID; 4422921; -. DR KEGG; lme:LEUM_1159; -. DR PATRIC; 22410307; VBILeuMes50664_1156. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LMES203120:GJ8T-1159-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23485 MW; DAE52EFC08B03862 CRC64; MDVNITKVLK LYLVTNRYDY SDEEFLGRIE KACQNGVTLA QLREKEVTTH KYFELATKVK EITDRFRIPL IIDDRIDICQ AVDAAGVHIG DNDLPISVAR RLIGPEKILG VSAKSAMRAT QAELEGADYL GVGAIYPTKT KVITKPTSIE TLKEITRTVS IPVIAIGGIK EHTIHNFKNT EINGVAMVSE IMCAENIADK VSDTIKELDQ VL // ID Q03YW9_LEUMM Unreviewed; 212 AA. AC Q03YW9; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 63. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LEUM_0487; OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / OS NCDO 523). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=203120; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8293 / NCDO 523; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., RA Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., RA Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., RA Broadbent J., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M., RA Klaenhammer T., Richardson P., Kozyavkin S., Weimer B., Mills D.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000414; ABJ61603.1; -; Genomic_DNA. DR RefSeq; YP_817976.1; NC_008531.1. DR ProteinModelPortal; Q03YW9; -. DR STRING; 203120.LEUM_0487; -. DR EnsemblBacteria; ABJ61603; ABJ61603; LEUM_0487. DR GeneID; 4422354; -. DR KEGG; lme:LEUM_0487; -. DR PATRIC; 22408961; VBILeuMes50664_0487. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MLARYFI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LMES203120:GJ8T-487-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23078 MW; 79FB8426440A9921 CRC64; MFDPSILVNY FVLGTQDTNG ERHFFEVLEE ALQSKISVFQ YREKGQLALS GSEKLRVAKK VRQLTADYHV PLIIDDDIQL AHEIDAEGVH FGQKDGDIIN NIQLAGNLAV GVSVSNDSQY KRIENIKGID YIGIGPVFAT VSKADANPEI GVEGLKYLTS KSKWPSVAIG GISEINLSSV LSTGVNGAAV ISMISQSANI SATLKYWRSL HL // ID Q04LH1_STRP2 Unreviewed; 210 AA. AC Q04LH1; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE-2; Synonyms=thiE; OrderedLocusNames=SPD_0631; OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=373153; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D39 / NCTC 7466; RX PubMed=17041037; DOI=10.1128/JB.01148-06; RA Lanie J.A., Ng W.L., Kazmierczak K.M., Andrzejewski T.M., RA Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.; RT "Genome sequence of Avery's virulent serotype 2 strain D39 of RT Streptococcus pneumoniae and comparison with that of unencapsulated RT laboratory strain R6."; RL J. Bacteriol. 189:38-51(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000410; ABJ53945.1; -; Genomic_DNA. DR RefSeq; YP_816127.1; NC_008533.1. DR ProteinModelPortal; Q04LH1; -. DR STRING; 373153.SPD_0631; -. DR PRIDE; Q04LH1; -. DR EnsemblBacteria; ABJ53945; ABJ53945; SPD_0631. DR GeneID; 4441329; -. DR KEGG; spd:SPD_0631; -. DR PATRIC; 19682352; VBIStrPne27904_0716. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE373153:GIX6-631-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; 60239DF9671A7380 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID Q04LH8_STRP2 Unreviewed; 209 AA. AC Q04LH8; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE-1; Synonyms=thiE; OrderedLocusNames=SPD_0624; OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=373153; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D39 / NCTC 7466; RX PubMed=17041037; DOI=10.1128/JB.01148-06; RA Lanie J.A., Ng W.L., Kazmierczak K.M., Andrzejewski T.M., RA Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.; RT "Genome sequence of Avery's virulent serotype 2 strain D39 of RT Streptococcus pneumoniae and comparison with that of unencapsulated RT laboratory strain R6."; RL J. Bacteriol. 189:38-51(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000410; ABJ54832.1; -; Genomic_DNA. DR RefSeq; YP_816120.1; NC_008533.1. DR ProteinModelPortal; Q04LH8; -. DR STRING; 373153.SPD_0624; -. DR EnsemblBacteria; ABJ54832; ABJ54832; SPD_0624. DR GeneID; 4441039; -. DR KEGG; spd:SPD_0624; -. DR PATRIC; 19682338; VBIStrPne27904_0709. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE373153:GIX6-624-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23334 MW; 09552FA5007A2FA0 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGESALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID Q04SM1_LEPBJ Unreviewed; 216 AA. AC Q04SM1; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 48. DE SubName: Full=Thiamine monophosphate synthase; GN Name=thiE; OrderedLocusNames=LBJ_1526; OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=355277; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JB197; RX PubMed=16973745; DOI=10.1073/pnas.0603979103; RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., RA Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., RA Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.; RT "Genome reduction in Leptospira borgpetersenii reflects limited RT transmission potential."; RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000350; ABJ76099.1; -; Genomic_DNA. DR RefSeq; YP_800857.1; NC_008510.1. DR ProteinModelPortal; Q04SM1; -. DR STRING; 355277.LBJ_1526; -. DR EnsemblBacteria; ABJ76099; ABJ76099; LBJ_1526. DR GeneID; 4411740; -. DR KEGG; lbj:LBJ_1526; -. DR PATRIC; 22358447; VBILepBor13265_1936. DR eggNOG; COG0352; -. DR HOGENOM; HOG000117684; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6WX4T9; -. DR BioCyc; LBOR355277:GHYM-1509-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 216 AA; 24537 MW; 507807B59825A613 CRC64; MSLQIQTPVW PLPGIYPILD WDFCKRKNLD LLTLPRIWLE YPDLVPFVQI RAKSASILEL EFLVKSLQDR YPRLLLILND FWEQAIEWNC FGAHVGKEDY EALNSEEKKV LFDSKLYLGT SSHTLEEVNG LDSSLWNYTG LGPIFPTDNK EDAKPAIGTE ILGKVTRESR LPVTLIGGIQ VGNLDLILKK GAFLLSSISM ACLEREFRAA ATKIRK // ID Q050P8_LEPBL Unreviewed; 216 AA. AC Q050P8; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 48. DE SubName: Full=Thiamine monophosphate synthase; GN Name=thiE; OrderedLocusNames=LBL_1750; OS Leptospira borgpetersenii serovar Hardjo-bovis (strain L550). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=355276; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L550; RX PubMed=16973745; DOI=10.1073/pnas.0603979103; RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., RA Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., RA Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.; RT "Genome reduction in Leptospira borgpetersenii reflects limited RT transmission potential."; RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000348; ABJ79197.1; -; Genomic_DNA. DR RefSeq; YP_798130.1; NC_008508.1. DR ProteinModelPortal; Q050P8; -. DR STRING; 355276.LBL_1750; -. DR EnsemblBacteria; ABJ79197; ABJ79197; LBL_1750. DR GeneID; 4407701; -. DR KEGG; lbl:LBL_1750; -. DR PATRIC; 22367510; VBILepBor75619_2211. DR eggNOG; COG0352; -. DR HOGENOM; HOG000117684; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6WX4T9; -. DR BioCyc; LBOR355276:GHUQ-1732-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 216 AA; 24537 MW; 507807B59825A613 CRC64; MSLQIQTPVW PLPGIYPILD WDFCKRKNLD LLTLPRIWLE YPDLVPFVQI RAKSASILEL EFLVKSLQDR YPRLLLILND FWEQAIEWNC FGAHVGKEDY EALNSEEKKV LFDSKLYLGT SSHTLEEVNG LDSSLWNYTG LGPIFPTDNK EDAKPAIGTE ILGKVTRESR LPVTLIGGIQ VGNLDLILKK GAFLLSSISM ACLEREFRAA ATKIRK // ID Q05WX1_9SYNE Unreviewed; 348 AA. AC Q05WX1; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 19-FEB-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RS9916_33117; OS Synechococcus sp. RS9916. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=221359; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RS9916; RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAUA01000001; EAU74449.1; -; Genomic_DNA. DR ProteinModelPortal; Q05WX1; -. DR EnsemblBacteria; EAU74449; EAU74449; RS9916_33117. DR PATRIC; 29885194; VBISynSp14719_1408. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 128 Unknown (By similarity). FT REGION 129 348 Thiamine-phosphate synthase (By FT similarity). FT REGION 180 184 HMP-PP binding (By similarity). FT REGION 277 279 THZ-P binding (By similarity). FT METAL 213 213 Magnesium (By similarity). FT METAL 232 232 Magnesium (By similarity). FT BINDING 212 212 HMP-PP (By similarity). FT BINDING 251 251 HMP-PP (By similarity). FT BINDING 280 280 HMP-PP (By similarity). FT BINDING 307 307 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 348 AA; 37513 MW; 3D1445B6656A1334 CRC64; MKVMVVAPHS EPCVARLIDA NLDRAREGLR VIEDWCRFGL DRLDLVKPLK DWRQQLGQCH REHYKQARST ATDIAAGLAH PAQQQRPQPS QIVAANCARV QEALRVLEEF GRDQDPRLAS TAASIRYGLY DLEVTILQAG HRAVRRQRLA QSRLCLITSP TADLIPRVEA ALKAGVSLVQ YRAKEGNDRE RLAAAGALAE LCRSHGALFI VNDRIDLALL VDADGVHLGQ DDLPTDAARQ LIGGGLLLGR STHNLEQLQA AQQEDCDYLG VGPIYATGTK PDKVPQGLLW ARQASEHATL PWFAIGGINA DRLPELGEAG VSRVAVVGAI MAAADPGAAS GSLLAALG // ID Q060B5_9SYNE Unreviewed; 354 AA. AC Q060B5; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 19-FEB-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BL107_11236; OS Synechococcus sp. BL107. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=313625; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BL107; RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATZ01000003; EAU70638.1; -; Genomic_DNA. DR ProteinModelPortal; Q060B5; -. DR EnsemblBacteria; EAU70638; EAU70638; BL107_11236. DR PATRIC; 29868454; VBISynSp76518_1308. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 130 Unknown (By similarity). FT REGION 131 354 Thiamine-phosphate synthase (By FT similarity). FT REGION 182 186 HMP-PP binding (By similarity). FT METAL 215 215 Magnesium (By similarity). FT METAL 234 234 Magnesium (By similarity). FT BINDING 214 214 HMP-PP (By similarity). FT BINDING 253 253 HMP-PP (By similarity). FT BINDING 282 282 HMP-PP (By similarity). FT BINDING 309 309 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 354 AA; 39037 MW; 1A72AA52AD39574E CRC64; MEPMGEGPLG LVDPRVARLI DANLDRAREG LRVVEDWCRF GLERDDLVVR LKDWRQRLGR LHRNIYKQAR STATDPGAGL SHPAQLERHN PQAVVAANCG RVQEALRVLE EYGRSLDPSL ASESAAIRYG LYDLEVTCLN ASEVNARRRT LHNCQLCLIT TPCPDLIERV TQALTAGVTM VQYRCKSGND RERLDEAKAL RMLCQHHGAL FVINDRIDLA LAVDADGVHL GQNDLPTDVA RELIGEARLL GRSTHTLDDV RRADADACDY LGLGPVYTTA VKPDKPAIGP MRLQEAQALT RRPVFAIGGI ELNNITALLD MGCRRVAVIS AIMAAENPER ASQQLLQALL PPVD // ID Q07HE4_RHOP5 Unreviewed; 229 AA. AC Q07HE4; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 46. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN OrderedLocusNames=RPE_4721; OS Rhodopseudomonas palustris (strain BisA53). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316055; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisA53; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., Kim E., RA Harwood C.S., Oda Y., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisA53."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000463; ABJ08640.1; -; Genomic_DNA. DR RefSeq; YP_783620.1; NC_008435.1. DR ProteinModelPortal; Q07HE4; -. DR STRING; 316055.RPE_4721; -. DR EnsemblBacteria; ABJ08640; ABJ08640; RPE_4721. DR GeneID; 4362424; -. DR KEGG; rpe:RPE_4721; -. DR PATRIC; 23264148; VBIRhoPal93214_4791. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RPAL316055:GHR9-4771-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 229 AA; 23841 MW; 680D494ACE90BE62 CRC64; MSAKPPPLPP APRLYLATPP IDDPATLVAA LPALLNAQPI AAVLLRLKPA DPRSLVTRAK AVAPVVQQAG AALLLDGEPE PVARSGADGA HLNDIAALQD HIGALQPDRI AGVGGLRTRH DAMLAGELGA DYVLFGEPDA QGQRPAPDAI AERLNWWAEL FEPPCVGYAL SFEEAFDFAA AGADFVLVGE LIWDDARGPA AALADATDAI QRGFRARLQA LAPAEAAPR // ID Q07PX0_RHOP5 Unreviewed; 202 AA. AC Q07PX0; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=RPE_2070; OS Rhodopseudomonas palustris (strain BisA53). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316055; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisA53; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., Kim E., RA Harwood C.S., Oda Y., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisA53."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000463; ABJ06014.1; -; Genomic_DNA. DR RefSeq; YP_780994.1; NC_008435.1. DR ProteinModelPortal; Q07PX0; -. DR STRING; 316055.RPE_2070; -. DR EnsemblBacteria; ABJ06014; ABJ06014; RPE_2070. DR GeneID; 4359440; -. DR KEGG; rpe:RPE_2070; -. DR PATRIC; 23258718; VBIRhoPal93214_2111. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; RPAL316055:GHR9-2087-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 202 AA; 21615 MW; 2FE1593CF5010397 CRC64; MPYPDRFYAI VDSLAWVQRL AALGVGTVQL RAKNLDDGGA LQLVTDALNA VKGTRTKLVI NDYWRAAIVA GAQHLHLGQE DLAEADVHEI RKAGLTLGLS THDDAELEAA LSAQPDYIAL GPIFPTTLKS MRFAPQGVPK ITTWKQRVGS IPLVAIGGIK LEQAAEIFAA GADSIAVVSD VTQNPDPDAR VRAWLDFVAE PA // ID Q081L9_SHEFN Unreviewed; 559 AA. AC Q081L9; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Sfri_2200; OS Shewanella frigidimarina (strain NCIMB 400). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=318167; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIMB 400; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., RA Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F., RA Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Richardson P.; RT "Complete sequence of Shewanella frigidimarina NCIMB 400."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000447; ABI72046.1; -; Genomic_DNA. DR RefSeq; YP_750884.1; NC_008345.1. DR ProteinModelPortal; Q081L9; -. DR STRING; 318167.Sfri_2200; -. DR EnsemblBacteria; ABI72046; ABI72046; Sfri_2200. DR GeneID; 4279112; -. DR KEGG; sfr:Sfri_2200; -. DR PATRIC; 23498425; VBISheFri14343_2285. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SFRI318167:GIXS-2280-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 559 AA; 59930 MW; 29D5220C91191BC9 CRC64; MNSSTFVSES ITQTPPIVWT IAGSDSGGGA GIQADLLTMQ DLSCHGCSVI TTVTAQNSVS VSLVETVSES MLLAQFSSLL VDLPPVAIKI GLLASQAQVD ILADCLTQMR ATQKIVPFVV LDPVMVASSG ANFNSIDLDF SPLIGLIDLL TPNQHELKRL CSQYALAQYC DVDNKVAQQQ QMICDAKLLS DTFKCNVLAK GGDAQWQQQY AIDVYVSKNV KGASITHSNA VFMLSSQRIA TTNNHGSGCT LSSAIACFIA HEFVIHDAIV LAKAYVNKGL TLGVSLGQGP GVLARTGWPA DLGMMPSINL VSSDYRAQDR FKPAPLNSFK AVHQSLGIYP VLDDLGILKN VLKAGCKTVQ YRAKLATNTD ADTDTDNRQR LTLEANIIEA IKLGREYHAQ LFINDHWQLA IKHGAFGVHL GQEDLLIADL TAIAATGMAL GLSSHSYFEA LLAHQCSPSY IALGHIFATT TKQMPSAPQG LSKLKRYASL FARHYPTVAI GGINLNNLEQ IAETGVGDAA VVRAVTMADD PAKAYRALHH KWLQLTRPLA KACSPQEGV // ID Q092N6_STIAD Unreviewed; 221 AA. AC Q092N6; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 19-FEB-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=STIAU_4279; OS Stigmatella aurantiaca (strain DW4/3-1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Cystobacteraceae; Stigmatella. OX NCBI_TaxID=378806; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DW4/3-1; RA Nierman W.C.; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMD01000049; EAU66703.1; -; Genomic_DNA. DR ProteinModelPortal; Q092N6; -. DR EnsemblBacteria; EAU66703; EAU66703; STIAU_4279. DR PATRIC; 38554711; VBIStiAur43712_3448. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 22542 MW; C562E3605FF86C32 CRC64; MDVRERLSVY VIVSGSTPET VVEALLGAGV GALQFREKAL PMAEQLVQAR RLRAQCRRAG ALFFVNDRLD LAMAAGADGV HLGQSDLPPA EARRLWGPQA LIGASCATLE ELSIADGADY VGVGPIYATA SKVDAGTPVG TAAVEQICRA FPGPVVGIGG IGPGLAAPLI RAGACGVSVI SAILDAPDPA FAARELLREV RQALAERGPT GSGPPRRAGG A // ID Q0A6W1_ALKEH Unreviewed; 319 AA. AC Q0A6W1; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 63. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=Mlg_2084; OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Alkalilimnicola. OX NCBI_TaxID=187272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., RA King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., RA Xie G., Stolz J.F., Richardson P.; RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000453; ABI57426.1; -; Genomic_DNA. DR RefSeq; YP_742916.1; NC_008340.1. DR ProteinModelPortal; Q0A6W1; -. DR STRING; 187272.Mlg_2084; -. DR EnsemblBacteria; ABI57426; ABI57426; Mlg_2084. DR GeneID; 4269403; -. DR KEGG; aeh:Mlg_2084; -. DR PATRIC; 20863421; VBIAlkEhr114327_2079. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AEHR187272:GHAX-2131-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 319 AA; 34953 MW; B572EF3B2ED2ECA6 CRC64; MARLHVAVGV ILDDRQRVLV ARRAAHRHQG GRWEFPGGKV EPGETVVQAL CRELEEELAI SPTRTSPMMR IEHDYPDRRV SLDVHRVSAW RGEPRGLEGQ PLAWLRATEL ARRPFPQANL PIIRRLALPP FLIITEPLAP GDLAGLARRL QSLAVPARGA WLQLRLPDWD DRAYGRALAL AIRTLGPRGV DVTANRSPAV ARRAGGHALH LNARALMACE ARPEGFVRVG ASCHSPEELA RAEALGLDYA LLSPVAATAS HPRQVPLGWE RFRDWLGRVD LPVYALGGLG PEALELAWAH GAHGVAGIRG FWPPRGSPP // ID Q0A6X8_ALKEH Unreviewed; 213 AA. AC Q0A6X8; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 63. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mlg_2067; OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Alkalilimnicola. OX NCBI_TaxID=187272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., RA King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., RA Xie G., Stolz J.F., Richardson P.; RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000453; ABI57409.1; -; Genomic_DNA. DR RefSeq; YP_742899.1; NC_008340.1. DR ProteinModelPortal; Q0A6X8; -. DR STRING; 187272.Mlg_2067; -. DR EnsemblBacteria; ABI57409; ABI57409; Mlg_2067. DR GeneID; 4270453; -. DR KEGG; aeh:Mlg_2067; -. DR PATRIC; 20863387; VBIAlkEhr114327_2062. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; AEHR187272:GHAX-2114-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22379 MW; D635765FC1F76483 CRC64; MPQREERRRR VRGLYVITDP GLQPPGALPG RVLQAIRGGA AMVQYRDKGA DAARRREEAG ALAELCRRHG VLFIVNDDAA LAAAVGADGV HVGRGDSAVA DARAVVGPER LVGASSYNDP ERARHLQAEG ADYVAFGAFF PSPTKPGAVR ATPEMLRRIR PRLRVPVVAI GGITARNAAP VVAAGADALA VITDVFSAPD VEAAARAYAS LFD // ID Q0AIA7_NITEC Unreviewed; 312 AA. AC Q0AIA7; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Neut_0653; OS Nitrosomonas eutropha (strain C91). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=335283; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C91; RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x; RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J., Shin M., RA Wei X.; RT "Whole-genome analysis of the ammonia-oxidizing bacterium, RT Nitrosomonas eutropha C91: implications for niche adaptation."; RL Environ. Microbiol. 9:2993-3007(2007). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000450; ABI58925.1; -; Genomic_DNA. DR RefSeq; YP_746890.1; NC_008344.1. DR ProteinModelPortal; Q0AIA7; -. DR STRING; 335283.Neut_0653; -. DR EnsemblBacteria; ABI58925; ABI58925; Neut_0653. DR GeneID; 4272209; -. DR KEGG; net:Neut_0653; -. DR PATRIC; 22718375; VBINitEut7577_0859. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NEUT335283:GHT6-668-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 312 AA; 34192 MW; B609706868FE759C CRC64; MPDLPLVEVV VAILIRPDSS FLLTCRPTGK PYSGYWEFPG GKIETGESPV QALARELNEE LGITPDQATP WLTRLFSYPH ATVQLRFYRV TSWQGEPAPR EQQQLAWQTA DNVTVSPLLP ANIPILRSLM LPSIYAITCA AETGVEASLL SIRQAFQSGI KLLQIREKAM PPDQLECYVQ TVLQLARNNH QVTVLLNGNI ALAQTVQADG IHLTSTQLLS LTARPTVNWC GASCHNAEEL KRAEQLGVDF VTLSPVYPTL SHPGAPSLGW DKFSVLLRDY PLPVYALGGL QPTDLAIAQE HGAHGIAMMR GI // ID Q0AKF9_MARMM Unreviewed; 194 AA. AC Q0AKF9; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 13-NOV-2013, entry version 46. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Mmar10_2953; OS Maricaulis maris (strain MCS10). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Maricaulis. OX NCBI_TaxID=394221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCS10; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Viollier P., Stephens C., Richardson P.; RT "Complete sequence of Maricaulis maris MCS10."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000449; ABI67234.1; -; Genomic_DNA. DR RefSeq; YP_758172.1; NC_008347.1. DR ProteinModelPortal; Q0AKF9; -. DR STRING; 394221.Mmar10_2953; -. DR EnsemblBacteria; ABI67234; ABI67234; Mmar10_2953. DR GeneID; 4286260; -. DR KEGG; mmr:Mmar10_2953; -. DR PATRIC; 22454136; VBIMarMar77530_3033. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ACHSERA; -. DR OrthoDB; EOG699751; -. DR BioCyc; MMAR394221:GHNB-3007-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 19956 MW; C6F37874786DCC61 CRC64; MGGSRACALP PLLALTDPQR QPDPVKLVEM LPPGSAIIYR HFGHPDRLAI ARATVAVASE LGIPVLVSSD LDLAYGSAAT GVHWPERMLP AAARARARGC RLLFSGSAHA PMTLLRAKQA GLDAVLVSTA FASASPSAGT AMGPQALAAW ARRTPVPVYA LGGINQKTVN RLTGLGISGV AAVGAIRNAE PTRT // ID Q0ALG6_MARMM Unreviewed; 214 AA. AC Q0ALG6; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Mmar10_2591; OS Maricaulis maris (strain MCS10). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Maricaulis. OX NCBI_TaxID=394221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCS10; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Viollier P., Stephens C., Richardson P.; RT "Complete sequence of Maricaulis maris MCS10."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000449; ABI66877.1; -; Genomic_DNA. DR RefSeq; YP_757815.1; NC_008347.1. DR ProteinModelPortal; Q0ALG6; -. DR STRING; 394221.Mmar10_2591; -. DR EnsemblBacteria; ABI66877; ABI66877; Mmar10_2591. DR GeneID; 4285922; -. DR KEGG; mmr:Mmar10_2591; -. DR PATRIC; 22453382; VBIMarMar77530_2658. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MMAR394221:GHNB-2643-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22472 MW; F250A193F36CFAE6 CRC64; MASPAKRRRM SQLYLITPPR ITADFVTTLE SALEAGPVSA LQIRLKDHSE TELLELAPSL IKVAQSRGVA AILNDSPELA DRLGCDGVHI GQSDGRVKDA RAIMGKDRTI GVTCHASRHL AMVAGEAGAD YVAFGAFYPT QTKPTDHVAT TDLLTWWVEL FELPCVAIGG ITPDNGAPLV EAGADFLAVC GGVWLHADGP AAAVQAFAAL TGDA // ID Q0B403_BURCM Unreviewed; 194 AA. AC Q0B403; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 50. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bamb_5573; OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia OS cepacia (strain AMMD)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=339670; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-244 / AMMD; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., RA Konstantinidis K., Ramette A., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000441; ABI91120.1; -; Genomic_DNA. DR RefSeq; YP_777454.1; NC_008391.1. DR ProteinModelPortal; Q0B403; -. DR STRING; 339670.Bamb_5573; -. DR EnsemblBacteria; ABI91120; ABI91120; Bamb_5573. DR GeneID; 4314462; -. DR KEGG; bam:Bamb_5573; -. DR PATRIC; 19027143; VBIBurAmb61564_5821. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BAMB339670:GH48-5651-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 20120 MW; 2D032CCD16479ECA CRC64; MSATLPRCCV ITPEPASASA ADCQAFLERL SAVLARGETL VQLRVKSFDA PAFARLAAEA LARCTAAGAQ LMLNGPIDAA GVMQLDGAGW HLDSAALRAV AQRPLPPARR VSAACHAADD LVLAARAGVD FVTLSPVLPT LSHPGAPTLG WTRFAALAAQ AVMPVYALGG MTRAHLDDAR RHGAYGVAGI RSFW // ID Q0BIY2_BURCM Unreviewed; 374 AA. AC Q0BIY2; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Bamb_0331; OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia OS cepacia (strain AMMD)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=339670; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-244 / AMMD; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., RA Konstantinidis K., Ramette A., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000440; ABI85891.1; -; Genomic_DNA. DR RefSeq; YP_772225.1; NC_008390.1. DR ProteinModelPortal; Q0BIY2; -. DR STRING; 339670.Bamb_0331; -. DR EnsemblBacteria; ABI85891; ABI85891; Bamb_0331. DR GeneID; 4309991; -. DR KEGG; bam:Bamb_0331; -. DR PATRIC; 19016138; VBIBurAmb61564_0386. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BAMB339670:GH48-344-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 374 AA; 39256 MW; 1792CFB9CE475BC4 CRC64; MSERFADAFW PPADELAEAA ERIRARLGDW PAGTTPWRLC VAAPDVPVDG DVLIVSAGDR AAQARASAAS RPAAPDAVAI EFDEHGATLH AAGVRHALEA AHPLGDDWIA ALAAFLDCGF APIDALVLAL AWRDGDETRG ADAWPVDAAR FPRVAGLAAA PEPAFPPCPA QLGLYPVVPD AEWVERVLDC GARTVQLRVK GAHPAALRGE IARAVAAGRR YPDARVFIND HWQIAVEEGA YGVHLGQEDL ETADLAAIAH AGLRLGLSSH GYYEMLRALH ERPSYLALGP VYATATKAVA APPQGLARIA RYARFAGARA PLVAIGGVGL DALPDVLATG VGSVAVVSAI TGAIDYRAAV VALQQCFARQ FDNH // ID Q0BPL0_GRABC Unreviewed; 221 AA. AC Q0BPL0; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 48. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=GbCGDNIH1_2344; OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Granulibacter. OX NCBI_TaxID=391165; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1260 / CGDNIH1; RX PubMed=17827295; DOI=10.1128/JB.00793-07; RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., RA Sturdevant D.E., Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., RA Holland S.M.; RT "Genome sequence analysis of the emerging human pathogenic acetic acid RT bacterium Granulibacter bethesdensis."; RL J. Bacteriol. 189:8727-8736(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000394; ABI63242.1; -; Genomic_DNA. DR RefSeq; YP_746165.1; NC_008343.1. DR STRING; 391165.GbCGDNIH1_2344; -. DR EnsemblBacteria; ABI63242; ABI63242; GbCGDNIH1_2344. DR GeneID; 4276320; -. DR KEGG; gbe:GbCGDNIH1_2344; -. DR PATRIC; 22080963; VBIGraBet83793_2430. DR eggNOG; NOG121918; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FLPTESH; -. DR OrthoDB; EOG679THR; -. DR BioCyc; GBET391165:GHON-2394-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23978 MW; 5B87829A3D48EEF7 CRC64; MDQKLIAWAR AVKAKAPRNA PPPLWLFTDH RRVPDPRPDI ARLPRGLCGV VFRHDALPDT VRATLLRQVI RLCRARRLIL SVSGCIPGGL PMWTQPHRRG GRLLANRADK ASTCLPAGLP AGLQGRPIIT ASAHTIPEIR RAHRLGAGLI FFSPFLPTES HPGTAALGAG HWNRLVRMAG RSLHNPPYIA ALGGIEGRHT ALLRMSGILN VGAIGALHAR H // ID Q0BT65_GRABC Unreviewed; 214 AA. AC Q0BT65; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=GbCGDNIH1_1089; OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Granulibacter. OX NCBI_TaxID=391165; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1260 / CGDNIH1; RX PubMed=17827295; DOI=10.1128/JB.00793-07; RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., RA Sturdevant D.E., Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., RA Holland S.M.; RT "Genome sequence analysis of the emerging human pathogenic acetic acid RT bacterium Granulibacter bethesdensis."; RL J. Bacteriol. 189:8727-8736(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000394; ABI61987.1; -; Genomic_DNA. DR RefSeq; YP_744910.1; NC_008343.1. DR ProteinModelPortal; Q0BT65; -. DR STRING; 391165.GbCGDNIH1_1089; -. DR EnsemblBacteria; ABI61987; ABI61987; GbCGDNIH1_1089. DR GeneID; 4275168; -. DR KEGG; gbe:GbCGDNIH1_1089; -. DR PATRIC; 22078331; VBIGraBet83793_1139. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GBET391165:GHON-1119-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22366 MW; A51CA60132816F38 CRC64; MMDERCRLYL ITPPALNSDS FADTLARALD AGDVGALQIR LKNLDDDALR HAIDRLRPVA HDRGVAVILN DRPDLVAATG CDGAHIGQED GDVIAARALL GDLTLGVSCH GSRDLAMSAG EAGADYVAFG AFYPSTSKEV VPEATPDLLT WWSEMMELPS VAIGGIDPTN AAPLVKAGAD FLAVIGAVWN HPDGPDAGVK ALNTAIQAAL TDDL // ID Q0BWB9_HYPNA Unreviewed; 198 AA. AC Q0BWB9; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 52. DE SubName: Full=Thiamine monophosphate synthase family protein; GN OrderedLocusNames=HNE_3553; OS Hyphomonas neptunium (strain ATCC 15444). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hyphomonas. OX NCBI_TaxID=228405; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15444; RX PubMed=16980487; DOI=10.1128/JB.00111-06; RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., RA Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., RA Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A., RA Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C., RA Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D., RA Davidsen T.M., Yang Q., Zafar N., Ward N.L.; RT "Comparative genomic evidence for a close relationship between the RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter RT crescentus."; RL J. Bacteriol. 188:6841-6850(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000158; ABI78554.1; -; Genomic_DNA. DR RefSeq; YP_762224.1; NC_008358.1. DR ProteinModelPortal; Q0BWB9; -. DR STRING; 228405.HNE_3553; -. DR EnsemblBacteria; ABI78554; ABI78554; HNE_3553. DR GeneID; 4287490; -. DR KEGG; hne:HNE_3553; -. DR PATRIC; 32219993; VBIHypNep17450_3559. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NRRDSIM; -. DR OrthoDB; EOG699751; -. DR BioCyc; HNEP228405:GI69-3554-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 198 AA; 21283 MW; 5AEF6431CA8D80A6 CRC64; MAARVAARHL PAGLPPAFFL TDPERTAQPE RIVAGLPAGW GVIYRHFGAE DREAVARRLL KLCRKRRLLL LIGADAVLAA KIGAHGVHWP GRLAGGARKW HGRLQIQTMS GHFRDNPGHF RTLPVSAVLY SAVFPSRSAS AGAAMGALRF RQIAKSLPCP VYALGGVNPD NGLLVADSAG LAAIDGWRCF EVREQDPS // ID Q0C8V5_ASPTN Unreviewed; 518 AA. AC Q0C8V5; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 16-APR-2014, entry version 38. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=ATEG_09879; OS Aspergillus terreus (strain NIH 2624 / FGSC A1156). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=341663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIH 2624 / FGSC A1156; RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., RA White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., RA Denning D.W., Nierman W.C., Milne T., Madden K.; RT "Annotation of the Aspergillus terreus NIH2624 genome."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH476608; EAU30070.1; -; Genomic_DNA. DR RefSeq; XP_001218501.1; XM_001218500.1. DR ProteinModelPortal; Q0C8V5; -. DR STRING; 33178.CADATEAP00004313; -. DR EnsemblFungi; CADATEAT00004313; CADATEAP00004313; CADATEAG00004313. DR GeneID; 4354094; -. DR HOGENOM; HOG000214306; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 518 AA; 54309 MW; 6C38CCD7A9AF71C8 CRC64; MKLNLSCYLV TDSTPPILKG RDLCAVVEEA LKGGVTVVQY RDKKSDTGDQ IHTAKKLHQI TTKYGVPLLI NDRVDVALAV GAEGVHLGQD DMTIEEAKRL LPKDAIIGIS ASSIDEAQKA IAAGADYLGI GTMFATPTKT NTKSIIGTAG TQAILDAISE TGRDVGTVSI GGINLSNVQR VLYQSKAPRK GLDGVAIVSA IMAADDPRAA AAEFVRRIAT PPPFVAGPAA PINGLSEMLD TVPAIVQKMV QTHPLVHNMI NFVVANFVAN VALSMGASPI MSPYGEEAVD LCQFDGALLI NMGTLTSESV SNYLKAIKAY NERGNPVVYD PVGAAATHIR RGAVAQLMAG GYFTLIKGNE GEIRQVSGSS GVTQRGVDSG PSSLDSASKA KLARDLARRE HNLVLLTGST DYLSDGERVL AIENGHELLG QVTGTGCAVG TVAGCFLTTH PSDKLLAVLS GLLMYEIAAE NAAARENVRG PGSFVPAFLD ELYVIRQAAL AGDSSWFAGR AKVQEISV // ID Q0EWI9_9PROT Unreviewed; 204 AA. AC Q0EWI9; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 19-FEB-2014, entry version 32. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=SPV1_12565; OS Mariprofundus ferrooxydans PV-1. OC Bacteria; Proteobacteria; Zetaproteobacteria; Mariprofundales; OC Mariprofundaceae; Mariprofundus. OX NCBI_TaxID=314345; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PV-1; RA Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATS01000019; EAU53688.1; -; Genomic_DNA. DR ProteinModelPortal; Q0EWI9; -. DR EnsemblBacteria; EAU53688; EAU53688; SPV1_12565. DR PATRIC; 28825038; VBIMarFer59489_0620. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 204 AA; 21346 MW; DFB97673CCB99362 CRC64; MTVTPPALTL ITDTSRYSGD AFFDAVEQSL TGGLDAVLLR EKTLSSAKLL AMASRLRELT RVHGAQLIIH SQADIAEAVD ADGVHLAARD IGTIPLVRGW LNDPAKMIAA SCHNAQELAL AAQAGADYAT LSPVFPTASH PGSACLGVDD FRRLAEQAAL PVVALGGITT HNCNELDWPY MAVISAIAGA ASPCDATRLL RSCD // ID Q0F2C0_9PROT Unreviewed; 211 AA. AC Q0F2C0; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 19-FEB-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SPV1_01742; OS Mariprofundus ferrooxydans PV-1. OC Bacteria; Proteobacteria; Zetaproteobacteria; Mariprofundales; OC Mariprofundaceae; Mariprofundus. OX NCBI_TaxID=314345; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PV-1; RA Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATS01000002; EAU55630.1; -; Genomic_DNA. DR ProteinModelPortal; Q0F2C0; -. DR EnsemblBacteria; EAU55630; EAU55630; SPV1_01742. DR PATRIC; 28826291; VBIMarFer59489_1630. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22493 MW; 578AC3917D695472 CRC64; MTDRRVSGIY GILPADLDTD DLMGRAEAAL KGGLRILQFR DKKQGYNRAL KRAKALRALT ADYDACFIVN DSVQMALDAR ADGVHLGRDD MPNLTQLRVD AGHDLIVGVT CRGDAGLARH VLREGADYIS IGAVWATQSK PEVPAIGLPR LIKARELFPD ADICAIGGIN LSNIVQIKAA GADCAAVISG LFAADDIELT AARLVALWDA A // ID Q0FF00_9RHOB Unreviewed; 207 AA. AC Q0FF00; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 19-FEB-2014, entry version 31. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=OM2255_06655; OS Rhodobacterales bacterium HTCC2255. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales. OX NCBI_TaxID=367336; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2255; RA Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATR01000001; EAU53189.1; -; Genomic_DNA. DR ProteinModelPortal; Q0FF00; -. DR EnsemblBacteria; EAU53189; EAU53189; OM2255_06655. DR PATRIC; 28469778; VBIRhoBac69559_1027. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 207 AA; 22873 MW; 076D2649E08D195A CRC64; MSDKEIPQIY LITPANTDIT FYTETLAPLL DICPVACIRL GLSSDDESLI SRHADQLREV AHARDISAVM TTHYRLVNSL GLDGVHRLDA AKTIREIREE LGTEAIVGSY CGTSRHVGMN AGEIGADYIS FGPVDHSALT DENIAEFATF EWWSEMVEIP VVAEGNVTLE LAAQLAPVID FLALGQEIWK TDTPLNELQE YLLRISK // ID Q0FHB6_PELBH Unreviewed; 202 AA. AC Q0FHB6; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 22-JAN-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=R2601_23540; OS Pelagibaca bermudensis (strain JCM 13377 / KCTC 12554 / HTCC2601). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pelagibaca. OX NCBI_TaxID=314265; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2601; RX PubMed=20729358; DOI=10.1128/JB.00873-10; RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L., RA Giovannoni S.J.; RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and RT Maritimibacter alkaliphilus HTCC2654T, the type strains of two marine RT Roseobacter genera."; RL J. Bacteriol. 192:5552-5553(2010). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATQ01000077; EAU43593.1; -; Genomic_DNA. DR ProteinModelPortal; Q0FHB6; -. DR EnsemblBacteria; EAU43593; EAU43593; R2601_23540. DR PATRIC; 28148587; VBIRosSp73948_3055. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 202 AA; 22399 MW; 0764557B3A6D2B83 CRC64; MGWLDRFYLI TGHVGRLELL VPQGVRLVQL RLKDLPEAEL RRQIARARDI CAVHGAQLVV NDHWRLALDL NCTFVHLGQE DMDGADFDAL RRAGVRIGVS THDEAELDRA LACAPDYVAL GPVYPTRLKK MKWAPQGLEK VRRWKRLVGD KPLVGIGGLT PERLPGLFEA GADSAAVVTD IQQAASPEAR CREWIAATRV PA // ID Q0FK79_PELBH Unreviewed; 208 AA. AC Q0FK79; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 22-JAN-2014, entry version 31. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=R2601_22477; OS Pelagibaca bermudensis (strain JCM 13377 / KCTC 12554 / HTCC2601). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pelagibaca. OX NCBI_TaxID=314265; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2601; RX PubMed=20729358; DOI=10.1128/JB.00873-10; RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L., RA Giovannoni S.J.; RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and RT Maritimibacter alkaliphilus HTCC2654T, the type strains of two marine RT Roseobacter genera."; RL J. Bacteriol. 192:5552-5553(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATQ01000042; EAU44602.1; -; Genomic_DNA. DR ProteinModelPortal; Q0FK79; -. DR EnsemblBacteria; EAU44602; EAU44602; R2601_22477. DR PATRIC; 28148201; VBIRosSp73948_2822. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 208 AA; 22042 MW; A9DEBD63319EB8CF CRC64; MAETDTDLPQ LYLITPPEFD LSAFPAQLDA VLQAAPIACI RLALTTRDED RIMRAADAVR EVAHAHDVAL VIDTHVVLAQ RLGLDGVHLT DGARSVRHAR KELGPDAIVG AFCSASRHDG MTAGETGADY VSFGPVGGAS LGDGTLAEPE LFEWWSQMIE LPVVAEGGLT PELVATLTPL TDFFGIGEEI WSQDDPAAAL KDLIAAMG // ID Q0G1F2_9RHIZ Unreviewed; 226 AA. AC Q0G1F2; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 19-FEB-2014, entry version 33. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=FP2506_12719; OS Fulvimarina pelagi HTCC2506. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Fulvimarina. OX NCBI_TaxID=314231; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2506; RX PubMed=20639329; DOI=10.1128/JB.00761-10; RA Kang I., Oh H.M., Lim S.I., Ferriera S., Giovannoni S.J., Cho J.C.; RT "Genome sequence of Fulvimarina pelagi HTCC2506T, a Mn(II)-oxidizing RT alphaproteobacterium possessing an aerobic anoxygenic photosynthetic RT gene cluster and Xanthorhodopsin."; RL J. Bacteriol. 192:4798-4799(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATP01000004; EAU41129.1; -; Genomic_DNA. DR ProteinModelPortal; Q0G1F2; -. DR EnsemblBacteria; EAU41129; EAU41129; FP2506_12719. DR PATRIC; 27665615; VBIFulPel16688_0373. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 226 AA; 24051 MW; 424AA0D09395C7FF CRC64; MTSDDPYRQR IVLLTTPLSD GDAEAALGRA LSGGDVASVL IDPAGREHGE FQAFAERLVP LVQNAGAAAI VIDDTRVAGR ARADGLHLTA GDVEALRDAI EAHAPKMIVG GSGFETRHAA LEAGEAMPDY LLFGRLGQDV SDTPHPKTLT MAEWWAAMVE LPCIALGART PESIDTVAET GAEFIGLASF VFDRSGEEAE RVAEANRLLN ERYAREKALA EERADA // ID Q0G7V9_9RHIZ Unreviewed; 201 AA. AC Q0G7V9; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 19-FEB-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FP2506_05436; OS Fulvimarina pelagi HTCC2506. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Fulvimarina. OX NCBI_TaxID=314231; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2506; RX PubMed=20639329; DOI=10.1128/JB.00761-10; RA Kang I., Oh H.M., Lim S.I., Ferriera S., Giovannoni S.J., Cho J.C.; RT "Genome sequence of Fulvimarina pelagi HTCC2506T, a Mn(II)-oxidizing RT alphaproteobacterium possessing an aerobic anoxygenic photosynthetic RT gene cluster and Xanthorhodopsin."; RL J. Bacteriol. 192:4798-4799(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATP01000001; EAU42255.1; -; Genomic_DNA. DR ProteinModelPortal; Q0G7V9; -. DR EnsemblBacteria; EAU42255; EAU42255; FP2506_05436. DR PATRIC; 27662663; VBIFulPel16688_2323. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 177 178 THZ-P binding (By similarity). FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 201 AA; 22274 MW; B20A3F2F364FF77B CRC64; MRLDPFYLIV DSADWIERLV PLGVRLVQLR VKDASREALL EHIRRSREVC NAHGCQLVVN DYWKLAIEEG CDFVHLGQED LLRADVPAIR KAGLKLGVST HDEAELAAAL AADPDYVALG PIWPTILKAM KWAPQTPEKL NTWRRAVGDI PLVAIGGITV ERLPQVFASG ADIAAVVTDI TRNEDPEART AEWIAATRRT P // ID Q0HJ11_SHESM Unreviewed; 565 AA. AC Q0HJ11; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Shewmr4_1882; OS Shewanella sp. (strain MR-4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=60480; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-4; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., RA Tiedje J., Richardson P.; RT "Complete sequence of Shewanella sp. MR-4."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000446; ABI38956.1; -; Genomic_DNA. DR RefSeq; YP_734013.1; NC_008321.1. DR ProteinModelPortal; Q0HJ11; -. DR STRING; 60480.Shewmr4_1882; -. DR EnsemblBacteria; ABI38956; ABI38956; Shewmr4_1882. DR GeneID; 4252456; -. DR KEGG; she:Shewmr4_1882; -. DR PATRIC; 23580432; VBISheSp133532_1958. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SSP60480:GI2N-1968-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 565 AA; 59458 MW; 1E075405FA666423 CRC64; MTPAKDISQV APKPIVWTIA GSDSGGGAGI QADLATIKDL GGHGCSVITT LTAQSSVAVE LVEPVSEAML LTQLSTLLAD LPPQAIKIGL LANQQQLHLV ADWLAGFKTQ FPLVPVILDP VMVASCGDEL GDKSTASKPL DFTPFKGLIS LITPNVQELA RLTAATDKQA SAIHTKAEFA AAAMQLSAQL ACSVLAKGGD IDFAAQASDG INTSDLLSDH KSDITSHHIA TDNQRLAEDL LICHQVTGCS PLDANGGFWL SSVRINTRHN HGSGCTLSSA IASVLASGFV LQDAVVVAKA YVNQGLTYAE GIGQGPGPLA RTAWPHNLTA YPHVTAYSQN SLSESSDLQC GAFNRLDPDL GIYPVVDNLL LLDQLLAAGV KTVQLRIKSN ALKSNVLASD ELEAQIQTAI ALGKHYDAQL FINDHWQLAI KHGAFGIHLG QEDLAVTDLN AIHAAGLALG ISSHGYFELL RAHQHAPSYI ALGHIFPTTT KQMPSAPQGL CKLTHYVELL NAHYPLVAIG GIGPSNLDQV KATGVSNIAV VRAITEANDP VMAYAELTRA WESSL // ID Q0HUX1_SHESR Unreviewed; 565 AA. AC Q0HUX1; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Shewmr7_2096; OS Shewanella sp. (strain MR-7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=60481; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-7; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., RA Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000444; ABI43084.1; -; Genomic_DNA. DR RefSeq; YP_738141.1; NC_008322.1. DR ProteinModelPortal; Q0HUX1; -. DR STRING; 60481.Shewmr7_2096; -. DR EnsemblBacteria; ABI43084; ABI43084; Shewmr7_2096. DR GeneID; 4258363; -. DR KEGG; shm:Shewmr7_2096; -. DR PATRIC; 23589309; VBISheSp85603_2163. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SSP60481:GHW6-2196-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 565 AA; 59339 MW; E0ECCB55D0C97D7D CRC64; MTPAKHISLV APKPIVWTIA GSDSGGGAGI QADLATIKDL GGHGCSVITT LTAQSSVAVA LVEPVSEAIL LTQLSTLLAD LPPQAIKIGL LANQQQVHLV ADWLAGFKTQ FPLVPVILDP VMVASCGDEL GDKSTASKPL DFTPFKGLIS LITPNVQELA RLTAATDKQA SAIHTKAEFA AAAMQLSAQL ACSVLAKGGD IDFAAQASDG INTSDLLSDH KSDITSHPIV TDNQRLAEDL LICHQVTGCS PLDANGGFWL SSARINTRHN HGSGCTLSSA IASVLAFGFV LQDAVVVAKA YVNQGLTHAV GVGQGPGPLA RTAWPHNLTA YPHVTAYSQN SLSESSDLQC GAFNRLDPDL GIYPVVDNLL LLEQLLAAGV KTVQLRIKSN ALKSNVLASD ELEAQIQTAI ALGKHYDAQL FINDHWQLAI KHGAFGIHLG QEDLAVTDLN AIHAAGLALG ISSHGYFELL RAHQHAPSYI ALGHIFPTTT KQMPSAPQGL CKLTHYVELL NAHYPLVAIG GIGPSNLDQV KATGVSNIAV VRAITEANDP VMAYAELTRA WESSL // ID Q0KF30_CUPNH Unreviewed; 378 AA. AC Q0KF30; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 48. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=H16_A0239; OS Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) OS (Ralstonia eutropha). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=381666; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337; RX PubMed=16964242; DOI=10.1038/nbt1244; RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., RA Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., RA Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., RA Friedrich B., Bowien B.; RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium RT Ralstonia eutropha H16."; RL Nat. Biotechnol. 24:1257-1262(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM260479; CAJ91391.1; -; Genomic_DNA. DR RefSeq; YP_724759.1; NC_008313.1. DR ProteinModelPortal; Q0KF30; -. DR STRING; 381666.H16_A0239; -. DR EnsemblBacteria; CAJ91391; CAJ91391; H16_A0239. DR GeneID; 4246945; -. DR KEGG; reh:H16_A0239; -. DR PATRIC; 35229855; VBIRalEut6770_0599. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CNEC381666:GJUJ-239-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 378 AA; 39978 MW; 6FDB77E190F4A50B CRC64; MTRRAVHAAS DGPLRQAVLE HYGETFGVDD KPWQAWRLAD APAQPGAHDV LLFDGEADAG TIARVAAAGA TLIESDREGG QWIDTVRSPM GTWVFSVAAD TDQPHSPAFV AVLLASLALH FPAHDALCLA RAWEPGSADW PSDFARFPHV RHAALVAPEQ AAAPFAPCPA LGLYVVVPSA EWIERLAPLN VPTVQLRFKS EDPAAVRAEI ARAAKATQGS SSRLFVNDHW QAAIDYRAAN GGDQSGIYGI HLGQEDLDDA DLDAIRASGL RLGVSTHGYA EMLRVAAIRP SYLALGAIFP TTTKVMPTQP QGMGRFRAYV KLMQPVIPSL VGIGGVNAAN MREVLAVGVG SAAVVRAVTE ADDVPAAVAQ LISLFPAA // ID Q0P9K9_CAMJE Unreviewed; 201 AA. AC Q0P9K9; DT 19-SEP-2006, integrated into UniProtKB/TrEMBL. DT 19-SEP-2006, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Cj1043c; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., RA Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., RA Whitehead S., Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL111168; CAL35161.1; -; Genomic_DNA. DR PIR; H81306; H81306. DR RefSeq; YP_002344438.1; NC_002163.1. DR ProteinModelPortal; Q0P9K9; -. DR IntAct; Q0P9K9; 14. DR STRING; 192222.Cj1043c; -. DR EnsemblBacteria; CAL35161; CAL35161; Cj1043c. DR GeneID; 905335; -. DR KEGG; cje:Cj1043c; -. DR PATRIC; 20059044; VBICamJej33762_1025. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CJEJ192222:GJTS-1017-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome; Transferase. SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID Q0RFM7_FRAAA Unreviewed; 221 AA. AC Q0RFM7; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 14-MAY-2014, entry version 60. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=FRAAL5075; OS Frankia alni (strain ACN14a). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=326424; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACN14a; RX PubMed=17151343; DOI=10.1101/gr.5798407; RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., RA Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N., RA Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L., RA Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E., RA Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z., RA Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D., RA Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.; RT "Genome characteristics of facultatively symbiotic Frankia sp. strains RT reflect host range and host plant biogeography."; RL Genome Res. 17:7-15(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT573213; CAJ63715.1; -; Genomic_DNA. DR RefSeq; YP_715254.1; NC_008278.1. DR ProteinModelPortal; Q0RFM7; -. DR STRING; 326424.FRAAL5075; -. DR GeneID; 4231801; -. DR KEGG; fal:FRAAL5075; -. DR PATRIC; 21919394; VBIFraAln347_4651. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CVGPVHA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; FALN326424:GJ82-5002-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23294 MW; C3AA1A61F3F6CCFE CRC64; MRVDRLRRLA DARLYLCTPR RAEFGPFLDA VIGPAGRGGV DLVQLREKNL EWADEVRGLR EIQAAGAGGD TLVSANDRAD LAAFTGVDIL HVGQDDVPPA FARRLVGPDV LIGQSTHSPE QFLAALADPD VDYVCVGPVH ATPTKQGRPP VGLGLPRLAA RHAPPFEPGA KPWFVTGGVG PDTLDDILAT GARRVVVVRA LTAAEDPAAG AAALARRLRS A // ID Q0SEN8_RHOSR Unreviewed; 244 AA. AC Q0SEN8; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 14-MAY-2014, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=RHA1_ro02191; OS Rhodococcus sp. (strain RHA1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=101510; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RHA1; RX PubMed=17030794; DOI=10.1073/pnas.0607048103; RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., RA Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., RA Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., RA Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A., RA Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., RA Davies J.E., Mohn W.W., Eltis L.D.; RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a RT catabolic powerhouse."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000431; ABG93998.1; -; Genomic_DNA. DR RefSeq; YP_702156.1; NC_008268.1. DR ProteinModelPortal; Q0SEN8; -. DR STRING; 101510.RHA1_ro02191; -. DR PRIDE; Q0SEN8; -. DR EnsemblBacteria; ABG93998; ABG93998; RHA1_ro02191. DR GeneID; 4218407; -. DR KEGG; rha:RHA1_ro02191; -. DR PATRIC; 23203231; VBIRhoJos26306_2217. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RJOS101510:GJJ1-2189-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 62 66 HMP-PP binding (By similarity). FT REGION 169 171 THZ-P binding (By similarity). FT METAL 104 104 Magnesium (By similarity). FT METAL 123 123 Magnesium (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 172 172 HMP-PP (By similarity). FT BINDING 200 200 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 244 AA; 25993 MW; 8A9963F0B002394E CRC64; MLHFHRRGYR HAVTTSHHSN LTDRRRRLGT ARLYLCTDAR REKGDLAQFA EAALSGGVDI IQLRDKGSAG EKKFGTMDAR DELAALSVLA AAARRHGALL AVNDRADMAL AAGADVLHLG QGDLPVPYAR TVVGSDVLIG RSTHSRAQAS LAAIEDGVDY FCTGPVWATP TKPGRTASGI DLVRSTADSE PNRPWFAIGG IDESRVPEIL AAGASRIVVV RAITEARDPQ AAARSLSALL QQNA // ID Q0SSM2_CLOPS Unreviewed; 193 AA. AC Q0SSM2; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE SubName: Full=Thiamine monophosphate synthase family protein; GN OrderedLocusNames=CPR_1569; OS Clostridium perfringens (strain SM101 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=289380; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM101 / Type A; RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., RA Deboy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., RA Melville S.B., Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial RT pathogen, Clostridium perfringens."; RL Genome Res. 16:1031-1040(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000312; ABG85647.1; -; Genomic_DNA. DR RefSeq; YP_698885.1; NC_008262.1. DR ProteinModelPortal; Q0SSM2; -. DR STRING; 289380.CPR_1569; -. DR EnsemblBacteria; ABG85647; ABG85647; CPR_1569. DR GeneID; 4206447; -. DR KEGG; cpr:CPR_1569; -. DR PATRIC; 19491430; VBICloPer122123_1544. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPER289380:GI76-1581-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 193 AA; 21907 MW; 129630B5D1431AC5 CRC64; MFLITNRKLV NREKYFNTIE EAGKYGVKNI ILREKDLSTE KLIEVYIKIK ELVPEETNII INSNIEAAKI LKEKFIHLSF KDFKKNLEEV KSLEVGVSVH SILEAIEADR LGASYILVSP IFETQCKKDV TPKGINFIKE IKEKVNCKVI ALGGINELNF KEVLGAGADD FACMSLLFMS NNIKECLDTF KSL // ID Q0TQ04_CLOP1 Unreviewed; 193 AA. AC Q0TQ04; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE SubName: Full=Thiamine monophosphate synthase family protein; GN OrderedLocusNames=CPF_1852; OS Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13124 / NCTC 8237 / Type A; RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., RA Deboy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., RA Melville S.B., Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial RT pathogen, Clostridium perfringens."; RL Genome Res. 16:1031-1040(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000246; ABG83719.1; -; Genomic_DNA. DR RefSeq; YP_696286.1; NC_008261.1. DR ProteinModelPortal; Q0TQ04; -. DR STRING; 195103.CPF_1852; -. DR DNASU; 4202449; -. DR EnsemblBacteria; ABG83719; ABG83719; CPF_1852. DR GeneID; 4202449; -. DR KEGG; cpf:CPF_1852; -. DR PATRIC; 19485958; VBICloPer106549_1798. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPER195103:GHAW-1868-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 193 AA; 21967 MW; 53DFE4BE63147552 CRC64; MFLITNRKLV NREKYFNTIE EAGKYGVKNI ILREKDLSTK ELIKIYIKIK ELVTEETNII INSNIEATMI LKEKFIHLSF KDFKRNLEEV KSLQVGVSVH SILEAIEADR LGASYILVSP IFETQCKKGV TPKGINFIKE IKEKVNCNVI ALGGINEHNF KEVLGAGADD FACMSLLFMS NNIKKSLYTF KSL // ID Q0U3E9_PHANO Unreviewed; 522 AA. AC Q0U3E9; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 2. DT 16-APR-2014, entry version 51. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=SNOG_13715; OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OS (Glume blotch fungus) (Septoria nodorum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae; OC Phaeosphaeriaceae; Parastagonospora. OX NCBI_TaxID=321614; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173; RX PubMed=18024570; DOI=10.1105/tpc.107.052829; RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., RA Torriani S.F.F., McDonald B.A., Oliver R.P.; RT "Dothideomycete-plant interactions illuminated by genome sequencing RT and EST analysis of the wheat pathogen Stagonospora nodorum."; RL Plant Cell 19:3347-3368(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH445352; EAT78739.2; -; Genomic_DNA. DR RefSeq; XP_001803922.1; XM_001803870.1. DR ProteinModelPortal; Q0U3E9; -. DR EnsemblFungi; SNOT_13715; SNOT_13715; SNOG_13715. DR GeneID; 5980844; -. DR KEGG; pno:SNOG_13715; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 522 AA; 54973 MW; 90BA6C533E372709 CRC64; MKEQVDYSLY LVTDSTEAIL GSRDLVDVVE QALLGAHNIP LLINDRVDVA LAVGCEGVHL GQDDMNISSA RHILGPDAII GATVSSIDEA RIAVERGADY LGIGTLYATN TKKNAKDIIG INGIRKILRH LEQGNDAEKK VKTVCIGGVN ASNLQRIRYQ LHAPSSPSTP PKAIDGVAIV SAIIGAPDPK AASAHLSILS TSLPPFKSHS TEPHFWLEKE SDEIAHILTS ALTATSNVKK TAPLSHNMTN LVVQNFAANT ALSIGASPIM ANYGAEADDL SALNGALVVN MGTVTPDGLR NYAQAIRAYN LSGGPIVLDP VGAGATSVRR AAVAELMSAA YFDLIKGNER EILAVARASG FSVDDSTQQR GVDSGDALYT LEQRAYIVAR LALRERNVVL MTGATDVISD GIRTYAISNG HEYLGKITGS GCTLGTTLSA YLAANRGDKL LAAVAGVLHY EIAAEQAAGR QAVKGPGTFV PAFIDELYNC SVEIAEGTKT WEGVAKIKCL KDVPDAGLLK EV // ID Q0VRZ1_ALCBS Unreviewed; 312 AA. AC Q0VRZ1; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 14-MAY-2014, entry version 64. DE SubName: Full=MutT/nudix family protein/thiamine-phosphatepyrophosphorylase, putative; GN OrderedLocusNames=ABO_0609; OS Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK2 / ATCC 700651 / DSM 11573; RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., RA Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., RA Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., RA Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A., RA Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., RA Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine RT bacterium Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(2006). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM286690; CAL16057.1; -; Genomic_DNA. DR RefSeq; YP_692329.1; NC_008260.1. DR ProteinModelPortal; Q0VRZ1; -. DR STRING; 393595.ABO_0609; -. DR EnsemblBacteria; CAL16057; CAL16057; ABO_0609. DR GeneID; 4212996; -. DR KEGG; abo:ABO_0609; -. DR PATRIC; 20838871; VBIAlcBor124741_0636. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ABOR393595:GHRI-626-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 312 AA; 33486 MW; 7B0CC6F38C7C638F CRC64; MPTSPTPSII VVAGIIRGSG HICLSKRADH QHQGGCWEFP GGKVEPGETL GAALARELEE ELGMVDAIST PFMTIAHQYD DLHVTLHFRD VHAWQGEPEG KEGQSVQWFV PQALADLRFP AANQPVVNAI RLPEQLVIAP EDISLHELLA GIDRLDAGRQ GLYLRQWSDH AEVSTIVGLC NKKGLKVWLR ASGPQSEVIA KALGVFALHF PGRVLAQLDE RPAFDGITSA AVHDLASRDK AVSLGLDMAL VSPVLPTPTH PGKPVLGWPQ AEVLMKGTPL ACYALGGVMP GDLVSARDYG AVGVAGIRAF WR // ID Q0YT11_9CHLB Unreviewed; 215 AA. AC Q0YT11; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 19-FEB-2014, entry version 39. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=CferDRAFT_1380; OS Chlorobium ferrooxidans DSM 13031. OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=377431; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13031; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M., Hauser L.; RT "Annotation of the draft genome assembly of Chlorobium ferroxidans DSM RT 13031."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13031; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Bruce D., Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of Chlorobium ferroxidans RT DSM 13031."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AASE01000004; EAT59453.1; -; Genomic_DNA. DR ProteinModelPortal; Q0YT11; -. DR EnsemblBacteria; EAT59453; EAT59453; CferDRAFT_1380. DR PATRIC; 27057129; VBIChlFer75923_0783. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 215 AA; 23257 MW; C1CBEBEC01D148EE CRC64; MVHITPHNAP LPRLLLISSG KEAPLIGTPL LIQLQLLPRF MPCMIQIREK HLDAKQLFQL SLMAAEIACE KEVRILINER ADIALAAALH GVHLPENSCP PDKLRAIAPE LIIGCSVHSP LSACIAEERG ADYLLFGPVF DTPSKRKYGP PQGVEKLGAL CRSTSLPVFA VGGITPQNIP CCMKQGAYGA AGISIFEPGS GFVATFEQFH NTLYQ // ID Q0YT12_9CHLB Unreviewed; 209 AA. AC Q0YT12; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 19-FEB-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CferDRAFT_1379; OS Chlorobium ferrooxidans DSM 13031. OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=377431; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13031; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M., Hauser L.; RT "Annotation of the draft genome assembly of Chlorobium ferroxidans DSM RT 13031."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13031; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Bruce D., Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of Chlorobium ferroxidans RT DSM 13031."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AASE01000004; EAT59452.1; -; Genomic_DNA. DR ProteinModelPortal; Q0YT12; -. DR EnsemblBacteria; EAT59452; EAT59452; CferDRAFT_1379. DR PATRIC; 27057127; VBIChlFer75923_0782. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21789 MW; 1DD558ED70BC48E8 CRC64; MMPSSPFLCV ITDEAVCPLS LAEKALQGGA AMIQLRHKTA SGSQLFSWGV EITRRCREYG ALCIINDRID IALACRADGV HLGQQDLPAS AARKLLGNSR IIGVSASSPE EAIQAERDGA DYIGFGHIYP TPSKEKGFDP VGPESLRRVA ALISLPIIAI GGITKSNASL VIGHGAAGIA VISAVSRADD PVSAVQELVC SLQQGDIDG // ID Q111P4_TRIEI Unreviewed; 360 AA. AC Q111P4; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Tery_2583; OS Trichodesmium erythraeum (strain IMS101). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Trichodesmium. OX NCBI_TaxID=203124; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMS101; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Richardson P.; RT "Complete sequence of Trichodesmium erythraeum IMS101."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000393; ABG51780.1; -; Genomic_DNA. DR RefSeq; YP_722253.1; NC_008312.1. DR ProteinModelPortal; Q111P4; -. DR STRING; 203124.Tery_2583; -. DR EnsemblBacteria; ABG51780; ABG51780; Tery_2583. DR GeneID; 4244651; -. DR KEGG; ter:Tery_2583; -. DR PATRIC; 23989680; VBITriEry99848_3267. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TERY203124:GJDR-2606-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 129 Unknown (By similarity). FT REGION 130 360 Thiamine-phosphate synthase (By FT similarity). FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 360 AA; 40954 MW; 6FC009C7F9D018A4 CRC64; MGDQYNLEKN VQPAIRRILD ANLDRAREGL RIIEEWCRFG LNSIDLAHEC KKLRQEIGGW HATELRMSRN TPNDPGTQLT HPQEEHRSDI EQLLQVNFCR LEEALRVLEE YGKIYNSQMA LACKQIRYRV YTIESGILAY KRNQQLQDSY LYLVTSPEEK LVDIVEAALQ GGLTLVQYRN KTADDITRLT EAKKLCEVCR RYGALFIVND RVDLAIAVDA DGVHLGQNDI PLNIARQLLG PQKLVGRSTT NQEEMERAIQ EEADYIGVGP IYETPTKVGK KAVGLEYISY VVKNCPIPWF AIGGIDMQNC DEVLSAGALR VSVVRAIMQS EQPTLVTQYF LSQLSRYQTL RSHSILPEKV // ID Q11DH1_MESSB Unreviewed; 219 AA. AC Q11DH1; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN OrderedLocusNames=Meso_3182; OS Mesorhizobium sp. (strain BNC1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Chelativorans. OX NCBI_TaxID=266779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BNC1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P.; RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000390; ABG64554.1; -; Genomic_DNA. DR RefSeq; YP_675719.1; NC_008254.1. DR ProteinModelPortal; Q11DH1; -. DR STRING; 266779.Meso_3182; -. DR EnsemblBacteria; ABG64554; ABG64554; Meso_3182. DR GeneID; 4182272; -. DR KEGG; mes:Meso_3182; -. DR PATRIC; 21346654; VBICheSp72577_3931. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; CSP266779:GI09-3239-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 219 AA; 23056 MW; 26FA6C2441F7779C CRC64; MSEAPIPSRC RIVLIAPPPD SGDAERIEAA LSGGDVASLL IPGYGADENE LQARAERLTP LAQARGVAVI IAGEPRIAAR VQADGVHVDG SKAELGDIIQ KHQKRMMVGC GGAKSRDDAL ELGETQPDYI FFGRFGYDNK PEPHPRNLSL GRWWAQMIQI PCIVLAGSEI SSIVDVARTG AEFVALGSAV FAEGRDPAAM VAEANALLDA HAPALGENA // ID Q11F76_MESSB Unreviewed; 206 AA. AC Q11F76; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 14-MAY-2014, entry version 70. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Meso_2565; OS Mesorhizobium sp. (strain BNC1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Chelativorans. OX NCBI_TaxID=266779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BNC1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P.; RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000390; ABG63949.1; -; Genomic_DNA. DR RefSeq; YP_675114.1; NC_008254.1. DR ProteinModelPortal; Q11F76; -. DR STRING; 266779.Meso_2565; -. DR EnsemblBacteria; ABG63949; ABG63949; Meso_2565. DR GeneID; 4182980; -. DR KEGG; mes:Meso_2565; -. DR PATRIC; 21345346; VBICheSp72577_3287. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CSP266779:GI09-2610-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 177 178 THZ-P binding (By similarity). FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 23145 MW; 44E109BC1A321F4E CRC64; MRLDPFYLIV DSAAWIERLV PLGVKLLQLR IKEIDEAELR AEIRRARKIC AGHDCQLIVN DYWQLAIEEG CDFVHLGQED LATADLAAIK RAGLKFGIST HDHTELATAL KAEPDYIALG PIYPTILKKM KWEPQGLDRI AEWKERVAPV PLVAIGGLTP ERIPGVFERG ADSAAVVTDI LRNSNPEART REWLEATASW REKSRA // ID Q11YH8_CYTH3 Unreviewed; 197 AA. AC Q11YH8; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 13-NOV-2013, entry version 53. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=CHU_0246; OS Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Cytophaga. OX NCBI_TaxID=269798; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33406 / NCIMB 9469; RX PubMed=17400776; DOI=10.1128/AEM.00225-07; RA Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., RA Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., RA Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B., RA Wilson D.B., McBride M.J.; RT "Genome sequence of the cellulolytic gliding bacterium Cytophaga RT hutchinsonii."; RL Appl. Environ. Microbiol. 73:3536-3546(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000383; ABG57538.1; -; Genomic_DNA. DR RefSeq; YP_676878.1; NC_008255.1. DR ProteinModelPortal; Q11YH8; -. DR STRING; 269798.CHU_0246; -. DR EnsemblBacteria; ABG57538; ABG57538; CHU_0246. DR GeneID; 4184997; -. DR KEGG; chu:CHU_0246; -. DR PATRIC; 21591327; VBICytHut34013_0241. DR eggNOG; NOG86118; -. DR KO; K00788; -. DR OMA; ANAVENF; -. DR OrthoDB; EOG6RC3V1; -. DR BioCyc; CHUT269798:GJ83-258-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 197 AA; 21914 MW; 199025E4E351C476 CRC64; MFMIKVITPE TNHPKEGGIL SALVSIYNCT IHIRKPRFTA DQYKKYLHDH NQLLSHFVLH EHHSLAKEFP VMGVHLKELD RINPAQVHPD IKIISTSIHS IADAGNLSHP FEYIFYSPLF QSISKENYGT NNSLADLKKT VSELKEQTGI PIIGLGGIYE ANIDLVKKSG FDGAALLGAV WVQSDPLAAF GRIASMI // ID Q11YI2_CYTH3 Unreviewed; 203 AA. AC Q11YI2; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CHU_0242; OS Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Cytophaga. OX NCBI_TaxID=269798; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33406 / NCIMB 9469; RX PubMed=17400776; DOI=10.1128/AEM.00225-07; RA Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., RA Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., RA Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B., RA Wilson D.B., McBride M.J.; RT "Genome sequence of the cellulolytic gliding bacterium Cytophaga RT hutchinsonii."; RL Appl. Environ. Microbiol. 73:3536-3546(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000383; ABG57534.1; -; Genomic_DNA. DR RefSeq; YP_676874.1; NC_008255.1. DR ProteinModelPortal; Q11YI2; -. DR STRING; 269798.CHU_0242; -. DR EnsemblBacteria; ABG57534; ABG57534; CHU_0242. DR GeneID; 4184993; -. DR KEGG; chu:CHU_0242; -. DR PATRIC; 21591319; VBICytHut34013_0237. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RTCATIC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CHUT269798:GJ83-254-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 125 127 THZ-P binding (By similarity). FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21945 MW; D3BB29582C05D087 CRC64; MNISNLHYIT DTTQGLEPLL KAGLNWVQLR VKNRNEKEMY NLADSFVALC EKYKAYSIIN DYPKLARRVG ADGVHLGKED MSPAEARALL GKDFIIGGTA NTFEDVEGLY EAGVDYVGLG PLRFTETKKN LSPVLGLEGY NEIMQSCQAN SIRTPIIAIG GIAVEDLAAL YDMGLHGVAV SAAIRKAQNP AAAVKAFLAV NAL // ID Q12HI4_POLSJ Unreviewed; 215 AA. AC Q12HI4; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Bpro_0041; OS Polaromonas sp. (strain JS666 / ATCC BAA-500). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=296591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS666 / ATCC BAA-500; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Anderson I., Richardson P.; RT "Complete sequence of chromosome of Polaromonas sp. JS666."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000316; ABE42008.1; -; Genomic_DNA. DR RefSeq; YP_546906.1; NC_007948.1. DR ProteinModelPortal; Q12HI4; -. DR STRING; 296591.Bpro_0041; -. DR EnsemblBacteria; ABE42008; ABE42008; Bpro_0041. DR GeneID; 4011760; -. DR KEGG; pol:Bpro_0041; -. DR PATRIC; 22953106; VBIPolSp102244_0042. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PSP296591:GHI4-762-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 22694 MW; C4F19F83DF5F239A CRC64; MNTDAFAPLT GPIGFYPVVP DAAWVQRLLG WGVRTIQLRI KAADHTPAEI EREVRAAVEA GRAVPGAQVF INDHWQLALA AGAYGVHLGQ EDLSMAEADL NALRKAGVRL GLSTHTPAEL ARAHAVQPSY LAIGPVYPTL LKVMPYEPVG LERLKEWALR AVPYSVVAIG GISLARLPGV IACGVDGVAV VSAVTQAADP EQATRQALAL FDAPA // ID Q12NC1_SHEDO Unreviewed; 613 AA. AC Q12NC1; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 14-MAY-2014, entry version 69. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN OrderedLocusNames=Sden_1771; OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=318161; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., RA Richardson P.; RT "Complete sequence of Shewanella denitrificans OS217."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000302; ABE55055.1; -; Genomic_DNA. DR RefSeq; YP_562778.1; NC_007954.1. DR ProteinModelPortal; Q12NC1; -. DR STRING; 318161.Sden_1771; -. DR EnsemblBacteria; ABE55055; ABE55055; Sden_1771. DR GeneID; 4018250; -. DR KEGG; sdn:Sden_1771; -. DR PATRIC; 23489419; VBISheDen79529_1882. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SDEN318161:GHKQ-1834-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 2. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 613 AA; 65609 MW; 4542CC221D061DC2 CRC64; MNTPPTIVWT IAGSDSGGGA GIQADLATAQ DLGCHCATVI TTVTAQNSVC VSLVEGVSAA MLLAQLNSLA RDLPPAAIKI GLLASQQQVD VVANWLKRLT QQRRSKGQLA VILDPVMVAS SGDRLNLNPS ISPSISSGMS SSMSSGTGSG FNSGSGLDFS AFIGVVSLIT PNQQELQYLV SGLQLSKTDN SHNRHSQGIG TSIESQADFI AKTEMLANAF GCHVLAKGGD GKHWQGDAAI DCYVCHHVEG ASLHHDNATY LLSSCRVNTG NNHGTGCTLS MAIASFMAQD FVLHDAIVLA KAYVTQGLIE SYQPGSGPGT LARTGWPDDL ALFPQIWPVN DADINGSMKA NSDSIEPPLP NLGQCISLHS KGFKPIEKDL GIYPVVDSLA LLKTLLKAGC RTIQLRLKID SKEAFGLKKQ QLEQKIIDAI ELGRTFNAQV FINDHWQLAL RHKAFGLHLG QEDLFEVDLK AIKAAGMALG LSSHSYFEIL LSHQLRPSYI ALGHIFPTPT KTMASKPQGL KKLKHYAKLL NKHYPTVAIG GIDETRLKEI KATGVANVAV VRALTNATDP TLAFDNLTRL WNGNKAEQYN AKLELEHKKG HMQASVTEVS YAP // ID Q130F4_RHOPS Unreviewed; 223 AA. AC Q130F4; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 14-MAY-2014, entry version 51. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=RPD_4318; OS Rhodopseudomonas palustris (strain BisB5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisB5; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., RA Lykidis A., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisB5."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000283; ABE41535.1; -; Genomic_DNA. DR RefSeq; YP_571436.1; NC_007958.1. DR ProteinModelPortal; Q130F4; -. DR STRING; 316057.RPD_4318; -. DR EnsemblBacteria; ABE41535; ABE41535; RPD_4318. DR GeneID; 4024842; -. DR KEGG; rpd:RPD_4318; -. DR PATRIC; 23283870; VBIRhoPal120395_4480. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RPAL316057:GHDC-4388-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 223 AA; 22756 MW; 9C2477CC031026F7 CRC64; MAKPAPPRPA PRLYLATPAV DDLSTLLAAL PQLLAGADVA AVLLRLAPSD PRTLITRIKA LTGVVQAAGA ALLLDGHAEL VARGGADGAH LSGLAALQEW LPQLQPARIA GVGMLETRHD SMIAGEAGAD YVLFGEPAGD GTRPSAEAIA DRLNWWAELF EPPCVGYATS RDEVEEFAAA GADFVLVGEH IWADASGAAA ALAEAEAALK LGFAGTASTP ARG // ID Q133T4_RHOPS Unreviewed; 202 AA. AC Q133T4; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 62. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=RPD_3431; OS Rhodopseudomonas palustris (strain BisB5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisB5; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., RA Lykidis A., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisB5."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000283; ABE40655.1; -; Genomic_DNA. DR RefSeq; YP_570556.1; NC_007958.1. DR ProteinModelPortal; Q133T4; -. DR STRING; 316057.RPD_3431; -. DR EnsemblBacteria; ABE40655; ABE40655; RPD_3431. DR GeneID; 4023945; -. DR KEGG; rpd:RPD_3431; -. DR PATRIC; 23281987; VBIRhoPal120395_3549. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; RPAL316057:GHDC-3491-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 202 AA; 21700 MW; 80C71B52E69AA276 CRC64; MPYPDRFYPV VDSIAWVKRL AALGVGTVQL RAKDLDDGAA LQLVTDALEA LQGTDTKLVV NDYWRAAIVA GAQHLHLGQE DLAEADLHEI RSAGLTLGLS THDDAELETA LAARPDYIAL GPIFPTTLKS MRFAPQGIPK ITEWKKRAGR IPLVAIGGIK LEQAEEIFAA GADSIAVVSD VTQNPDPDAR VRAWLDAVAE TA // ID Q13TP2_BURXL Unreviewed; 367 AA. AC Q13TP2; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 14-MAY-2014, entry version 59. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=Bxe_A0386; OS Burkholderia xenovorans (strain LB400). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=266265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LB400; RX PubMed=17030797; DOI=10.1073/pnas.0606924103; RA Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., RA Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., RA Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M., RA Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., RA Tiedje J.M.; RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp RT genome shaped for versatility."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000270; ABE32547.1; -; Genomic_DNA. DR RefSeq; YP_560599.1; NC_007951.1. DR ProteinModelPortal; Q13TP2; -. DR STRING; 266265.Bxe_A0386; -. DR EnsemblBacteria; ABE32547; ABE32547; Bxe_A0386. DR GeneID; 4006032; -. DR KEGG; bxe:Bxe_A0386; -. DR PATRIC; 19333896; VBIBurXen52548_4234. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BXEN266265:GJII-4171-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 367 AA; 39757 MW; 8F5C07055B5FE15D CRC64; MTQTLTLKDR DLFWPPADEL TEAAERIRAR LGDWPPTHAP WRICLTAPDE LNGSDLIVIA DAQQHGEQMA HWLVRGAGVI EAAEEKATLH LGGEKYRLEG HLAEDWIAAL AAFLDCGFDP HDALVLALAW RDGDETSADD AFPTDLSRFP RLAGLPDAPA QAFARCPERL GLYPVLPTAE WVERVVGFGV KTVQLRRKSA EPADELKREI ARCVAVGRQY DAQVFINDHW QAALEAGAYG VHLGQEDVHT ADLAALASAG VRLGLSTHGF YEILKALHFR PSYIALGAVF PTTTKIMPTE PQGLRRLARY VRLLDGVVPL VAIGGIDLQV LPDVLATGVG SAAVVRAVTE AADPASAVSA LQHAFTQ // ID Q15UI5_PSEA6 Unreviewed; 612 AA. AC Q15UI5; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 13-NOV-2013, entry version 63. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Patl_1935; OS Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=342610; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T6c / ATCC BAA-1087; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.; RT "Complete sequence of Pseudoalteromonas atlantica T6c."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000388; ABG40453.1; -; Genomic_DNA. DR RefSeq; YP_661507.1; NC_008228.1. DR ProteinModelPortal; Q15UI5; -. DR STRING; 342610.Patl_1935; -. DR EnsemblBacteria; ABG40453; ABG40453; Patl_1935. DR GeneID; 4172782; -. DR KEGG; pat:Patl_1935; -. DR PATRIC; 23048970; VBIPseAtl25434_2073. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; RYQDTHD; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PATL342610:GHGT-1970-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 612 AA; 67219 MW; 3CA752F388C9C936 CRC64; MISHDAIVSD PESLNNGIKP SVLTFSGSDS AGLAGMQMDV KVQHALAVHC TSVLTAVTAQ NNQQVFAVNA VDSAMFRAQI EAVSVFRPKA IKTGFVASEA QAQQIIAVRQ RLKIPLICDP VGAATSGAEL HGKRNTDSHR NINRLLLAHC SLLTPNIPEA QSLVGFDIET AKDLRRAARA LVEIGAQAVL IKGGHWQYAD HMGLDFFYSP EEQFWLQNEP VDTPHTRGTG CALASAIASA IALGYCLKDA IVIGKMAITQ GLHNAKGLLA KSVRYQDVRY QDTHDKQRYQ DTHDKQIKEL ASFDTPELTS EQSLRQQQSQ LNYQDTHDKQ IKELASFDTP ELTSEQSLRQ QQSQLNYQDT HNKGGVEILC FPATQRSLPG LYIESLMATS ELSSLVLQKQ ENPFPGIGDE SLGLYPVVDR AHWLDTLLPL GVTTIQLRIK DLTGQSLEEE IKRAVEIATR FQCRLFINDY WQLAIKHGAY GVHLGQEDLV AAAQNESNPI KQLLEAGMRL GISTHCHYEV ARAHALKPSY IAYGPVFATQ SKDMPWVPQG LAGLAYWQKL LDYPVVAIGG IDHERANAIH GLGVSGIAMI SYITQAENPI KVTKSLLRAL AL // ID Q162K4_ROSDO Unreviewed; 214 AA. AC Q162K4; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiDE; Synonyms=thiE; OrderedLocusNames=RD1_3611; OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter OS sp. (strain OCh 114)) (Roseobacter denitrificans). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=375451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33942 / OCh 114; RX PubMed=17098896; DOI=10.1128/JB.01390-06; RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., RA Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., RA Shah M.K., O'huallachain M.E., Lince M.T., Blankenship R.E., RA Beatty J.T., Touchman J.W.; RT "The complete genome sequence of Roseobacter denitrificans reveals a RT mixotrophic rather than photosynthetic metabolism."; RL J. Bacteriol. 189:683-690(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000362; ABG33089.1; -; Genomic_DNA. DR RefSeq; YP_683775.1; NC_008209.1. DR ProteinModelPortal; Q162K4; -. DR STRING; 375451.RD1_3611; -. DR EnsemblBacteria; ABG33089; ABG33089; RD1_3611. DR GeneID; 4195088; -. DR KEGG; rde:RD1_3611; -. DR PATRIC; 23365177; VBIRosDen86677_3454. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RDEN375451:GJIZ-3405-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 21910 MW; AD3608B78F80AEF4 CRC64; MTGLLKDRLR LYLVTDPQLC AEAGVMNTVQ RAVAGGVTMV QLRDKHAKTP ERIELAIALK NALQSSGVPL VINDDVVAAV ATDVDGAHIG QGDITPAEAR AMLGPGRILG LSCETAQTVR DADPTLVDYL GLGPVFGTAT KDDHAQPIGF DGLAGLVALS PLPTVAIGGL KHDHTNAVAA SGADGMAVVS AICGQPDPQA AAGAFHSFKP EHKA // ID Q165S8_ROSDO Unreviewed; 206 AA. AC Q165S8; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 55. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=RD1_2730; OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter OS sp. (strain OCh 114)) (Roseobacter denitrificans). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=375451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33942 / OCh 114; RX PubMed=17098896; DOI=10.1128/JB.01390-06; RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., RA Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., RA Shah M.K., O'huallachain M.E., Lince M.T., Blankenship R.E., RA Beatty J.T., Touchman J.W.; RT "The complete genome sequence of Roseobacter denitrificans reveals a RT mixotrophic rather than photosynthetic metabolism."; RL J. Bacteriol. 189:683-690(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000362; ABG32265.1; -; Genomic_DNA. DR RefSeq; YP_682951.1; NC_008209.1. DR ProteinModelPortal; Q165S8; -. DR STRING; 375451.RD1_2730; -. DR EnsemblBacteria; ABG32265; ABG32265; RD1_2730. DR GeneID; 4196085; -. DR KEGG; rde:RD1_2730; -. DR PATRIC; 23363459; VBIRosDen86677_2605. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RDEN375451:GJIZ-2568-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 206 AA; 22341 MW; 493A87A37F0D0829 CRC64; MELPEKPQLY LITPPEFELS SFPDVLARVL DTHKVACVRL ELAARDEDTV SRAADALREV THARDIALVL SDHSVLADRL GLDGVHLSDA ARSVRETRKL LGEDAIIGSF CGTSRHDGMS AGEAGADYIC FGPVAASSLG DGSYVAQEVF EWWSEFIEVP VVAEGGLDAA RIAQLTPFTD FFAFGQEVWS AEYPAQRLGE LLEAMG // ID Q16C59_ROSDO Unreviewed; 198 AA. AC Q16C59; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 69. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=RD1_0750; OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter OS sp. (strain OCh 114)) (Roseobacter denitrificans). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=375451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33942 / OCh 114; RX PubMed=17098896; DOI=10.1128/JB.01390-06; RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., RA Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., RA Shah M.K., O'huallachain M.E., Lince M.T., Blankenship R.E., RA Beatty J.T., Touchman J.W.; RT "The complete genome sequence of Roseobacter denitrificans reveals a RT mixotrophic rather than photosynthetic metabolism."; RL J. Bacteriol. 189:683-690(2007). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000362; ABG30434.1; -; Genomic_DNA. DR RefSeq; YP_681120.1; NC_008209.1. DR ProteinModelPortal; Q16C59; -. DR STRING; 375451.RD1_0750; -. DR EnsemblBacteria; ABG30434; ABG30434; RD1_0750. DR GeneID; 4197895; -. DR KEGG; rde:RD1_0750; -. DR PATRIC; 23359659; VBIRosDen86677_0727. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; RDEN375451:GJIZ-702-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 198 AA; 21953 MW; C7CB76FA413F8D4A CRC64; MTLPRFYPIF DDVAWLRRML PLGVKFVQLR IKDQPQDVLR AQLTEGRDLC RAHGALLVVN DHWQLAIDLG CDWVHLGQED LDAADVAAIR SAGLKLGIST HDKAELVRAL ALKPDYVALG PIYPTILKKM KWHQQGVEKL SEWKDRVGDI PLVAIGGMST DRAAAAFDAG ADVVSAVTDI ALHDDPESRV REWLEVCG // ID Q186R4_CLOD6 Unreviewed; 229 AA. AC Q186R4; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 55. DE SubName: Full=Thiamine-phosphate pyrophosphorylase ThiE2; DE EC=2.5.1.3; GN Name=thiE2; OrderedLocusNames=CD630_17060; OS Clostridium difficile (strain 630). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=272563; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=630; RX PubMed=16804543; DOI=10.1038/ng1830; RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A., RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., RA Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.; RT "The multidrug-resistant human pathogen Clostridium difficile has a RT highly mobile, mosaic genome."; RL Nat. Genet. 38:779-786(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM180355; CAJ68574.1; -; Genomic_DNA. DR RefSeq; YP_001088210.1; NC_009089.1. DR ProteinModelPortal; Q186R4; -. DR STRING; 272563.CD1706; -. DR DNASU; 4916034; -. DR EnsemblBacteria; CAJ68574; CAJ68574; CD630_17060. DR GeneID; 4916034; -. DR KEGG; cdf:CD630_17060; -. DR PATRIC; 19441797; VBICloDif38397_1785. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CDIF272563:GJFE-1891-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 229 AA; 27014 MW; F6F6025B5FFE2E92 CRC64; MYLITNRKLC SEERYLEVIK ESILSGVENI IIREKDLEYQ ELRKLYMKIK TKINCIDFQE QISDESLKTN INQKECRNKF KVNFIINSNI EFFEKVDCQG IHLPFKLFLN LIENKYNFNE NKILGLSLHK VEEVDYLEKL IRNQNIKIDY ITLSHIYETK CKEGLNPKGI ELLKEAKKIT DIKIIALGGI LPSNVKETLK YCDDFAIMST IMRSKDIKKT ISNYNEKLN // ID Q1ASC6_RUBXD Unreviewed; 208 AA. AC Q1ASC6; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rxyl_2788; OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129). OC Bacteria; Actinobacteria; Rubrobacteridae; Rubrobacterales; OC Rubrobacterineae; Rubrobacteraceae; Rubrobacter. OX NCBI_TaxID=266117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9941 / NBRC 16129; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E., RA Battista J.R., Richardson P.; RT "Complete sequence of Rubrobacter xylanophilus DSM 9941."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000386; ABG05702.1; -; Genomic_DNA. DR RefSeq; YP_645514.1; NC_008148.1. DR ProteinModelPortal; Q1ASC6; -. DR STRING; 266117.Rxyl_2788; -. DR EnsemblBacteria; ABG05702; ABG05702; Rxyl_2788. DR GeneID; 4117621; -. DR KEGG; rxy:Rxyl_2788; -. DR PATRIC; 23372374; VBIRubXyl52678_2759. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RXYL266117:GH8O-2847-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22297 MW; DB34E60D0B57277E CRC64; MEARERLRRA RLLLVTDPRD DLEERVEAAL RGGVDIVQLR EKRASREEVL PLARRLREVC LRHGALFTVN DDIELARLSG AHGVHLGQED EPVARAREVL GPGAVVGRSA GGVEEARRAV REGADYLGVG SVYPTPTKPD AEVRGLGLIR EMARAALPVP WFAIGGVTLE TAGEVAAAGA PGFAVVRAVL DAEDPEEAAR SLRALLPA // ID Q1ATF5_RUBXD Unreviewed; 252 AA. AC Q1ATF5; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rxyl_2395; OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129). OC Bacteria; Actinobacteria; Rubrobacteridae; Rubrobacterales; OC Rubrobacterineae; Rubrobacteraceae; Rubrobacter. OX NCBI_TaxID=266117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9941 / NBRC 16129; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E., RA Battista J.R., Richardson P.; RT "Complete sequence of Rubrobacter xylanophilus DSM 9941."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000386; ABG05323.1; -; Genomic_DNA. DR RefSeq; YP_645135.1; NC_008148.1. DR ProteinModelPortal; Q1ATF5; -. DR STRING; 266117.Rxyl_2395; -. DR EnsemblBacteria; ABG05323; ABG05323; Rxyl_2395. DR GeneID; 4115641; -. DR KEGG; rxy:Rxyl_2395; -. DR PATRIC; 23371602; VBIRubXyl52678_2378. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RXYL266117:GH8O-2446-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 252 AA; 26539 MW; 8E25FA375C182B39 CRC64; MEDRFQIHLI TDRRRARIGL EEAVLAALRG GVDWVQLREK GGPAAGLYET ALRIAPEARR RGVGVLVNDR VDVALAAGAD GVHLAARSLP PAVARSLISG GMLLGVSVHS LQEARRAVEG GADYVTFGHV YPTASKPGLP PRGVRELARI VESVEVPVLA VGGIDASNVR EVLSTGASGI AVISAILAAA DPEGAARRLR RAVDDLPHRP RRPMPEPRRG GGDADKAQPG ERGARRRPAH RAAAARGEED PG // ID Q1BLV9_BURCA Unreviewed; 194 AA. AC Q1BLV9; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 57. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Bcen_4514; OS Burkholderia cenocepacia (strain AU 1054). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=331271; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AU 1054; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., RA Konstantinidis K., Tiedje J.M., Richardson P.; RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia AU RT 1054."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000379; ABF79396.1; -; Genomic_DNA. DR RefSeq; YP_624369.1; NC_008061.1. DR ProteinModelPortal; Q1BLV9; -. DR STRING; 331271.Bcen_4514; -. DR EnsemblBacteria; ABF79396; ABF79396; Bcen_4514. DR GeneID; 4094485; -. DR KEGG; bcn:Bcen_4514; -. DR PATRIC; 19053004; VBIBurCen11237_4709. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCEN331271:GHKX-4589-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 19918 MW; C6EB413E18D31159 CRC64; MNAPLPRCCV ITPEPASASA ADRAAFLDRL SAVLARGETL VQLRVKSLDA AAFASLAAAA LARCAAAGAH LMLNGPIDAA GVMRLDGAGW HLDGTALRAA AQRPLPAARW VSAACHTQDD LLLAARAGAD FVTLSPVLPT LSHPGAPALG WARFDALAAQ AAMPVFALGG MTRAHLDDAR RHGAYGIAGI RGFW // ID Q1BS13_BURCA Unreviewed; 375 AA. AC Q1BS13; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Bcen_2694; OS Burkholderia cenocepacia (strain AU 1054). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=331271; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AU 1054; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., RA Konstantinidis K., Tiedje J.M., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia AU RT 1054."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000378; ABF77592.1; -; Genomic_DNA. DR RefSeq; YP_622565.1; NC_008060.1. DR ProteinModelPortal; Q1BS13; -. DR STRING; 331271.Bcen_2694; -. DR EnsemblBacteria; ABF77592; ABF77592; Bcen_2694. DR GeneID; 4091600; -. DR KEGG; bcn:Bcen_2694; -. DR PATRIC; 19049174; VBIBurCen11237_2821. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BCEN331271:GHKX-2749-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 375 AA; 39196 MW; 4EC4FA8333C5D3FC CRC64; MSAARFADAF WPPADELAEA AERIRARLGD WPEGAAPWRL CVAAPDVPAD GDVLIVSAGD RAAQARASAV SRPASPDAVA IEFDEQGAVL HAAGGRYALD AAHPLADDWI AALAAFLDCG FAPVDALVLA LAWRDGDETR AADAWPVDAA RFPRVAGLPP APEPAFAPCP ARLGLYPVVP SAEWVERVLD GGARTVQLRV KEATPDALRR EIARAVAAGR RYPDARVFIN DHWEIAAEAG AYGVHLGQED LETADLAAIA GAGLRLGLSS HGYYEMLRAL HERPSYLALG PVYATATKAV AAPPQGLARI ARYARFAGAR APLVAIGGVG LDTLPAVLAT GVGSVAVVSA VTGAADYRTV LIALQQCFTG QFDNH // ID Q1D7A7_MYXXD Unreviewed; 212 AA. AC Q1D7A7; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 16-APR-2014, entry version 53. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=MXAN_3267; OS Myxococcus xanthus (strain DK 1622). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Myxococcus. OX NCBI_TaxID=246197; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DK 1622; RX PubMed=17015832; DOI=10.1073/pnas.0607335103; RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C., RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R., RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R., RA Kaplan H.B.; RT "Evolution of sensory complexity recorded in a myxobacterial genome."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000113; ABF89773.1; -; Genomic_DNA. DR RefSeq; YP_631466.1; NC_008095.1. DR ProteinModelPortal; Q1D7A7; -. DR STRING; 246197.MXAN_3267; -. DR EnsemblBacteria; ABF89773; ABF89773; MXAN_3267. DR GeneID; 4102357; -. DR KEGG; mxa:MXAN_3267; -. DR PATRIC; 22649079; VBIMyxXan43560_3212. DR eggNOG; NOG287972; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VITDWRL; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MXAN246197:GIWU-3239-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 212 AA; 22146 MW; 2B9F58341D88A6D9 CRC64; MVPSTVPRLV VITDWRLPSE RLRWALTRAL DAGPEVAVQH RHPEATGRRF LDEARELAAL CHPRGNPLFI NGRVDVALLV GAHIHLPAHG PSPMDVRPHL PAGRWISAAV HDVAEAHAAR GANLALVSPV FAPGSKPGDT RPPLGPEGFS ALAAALPCPA LALGGITPAR AMTLPDAAGF AVISSVLEAD DPTAAARSLL AARAGRAMLR TP // ID Q1GGZ6_RUEST Unreviewed; 210 AA. AC Q1GGZ6; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=TM1040_1337; OS Ruegeria sp. (strain TM1040) (Silicibacter sp.). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=292414; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TM1040; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Goodwin L., RA Thompson L.S., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Belas R., Moran M.A., Buchan A., Gonzalez J.M., RA Schell M.A., Sun F., Richardson P.; RT "Complete sequence of chromosome of Silicibacter sp. TM1040."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000377; ABF64070.1; -; Genomic_DNA. DR RefSeq; YP_613332.1; NC_008044.1. DR ProteinModelPortal; Q1GGZ6; -. DR STRING; 292414.TM1040_1337; -. DR EnsemblBacteria; ABF64070; ABF64070; TM1040_1337. DR GeneID; 4075908; -. DR KEGG; sit:TM1040_1337; -. DR PATRIC; 23386830; VBIRueSp69653_2234. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RSP292414:GHCT-1361-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 210 AA; 22486 MW; 67F13F74E87491BF CRC64; MDSAEQTPEQ PQIYLVTPPS FELGQFPGQL ARVLDEIEVA CVRLDLVSRD EDTLSRAADA LREVTHARDI ALVISDHQIL AERLGLDGVH LTDSSKSIRS ARKALGTEAI VGCFCGASRH EGLTAGEAGA DYVCFGPVGA SGLGDGAMAE ADLFQWWSEM IEVPVVAEGG LTDDVVRKIA PFTDFFAVGE EIWREEDPVA ALKSLQAAMG // ID Q1GL46_RUEST Unreviewed; 198 AA. AC Q1GL46; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 14-MAY-2014, entry version 70. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=TM1040_3653; OS Ruegeria sp. (strain TM1040) (Silicibacter sp.). OG Plasmid megaplasmid TM1040. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=292414; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TM1040; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Goodwin L., RA Thompson L.S., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Belas R., Moran M.A., Buchan A., Gonzalez J.M., RA Schell M.A., Sun F., Richardson P.; RT "Complete sequence of megaplasmid of Silicibacter sp. TM1040."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000376; ABF62620.1; -; Genomic_DNA. DR RefSeq; YP_611882.1; NC_008043.1. DR ProteinModelPortal; Q1GL46; -. DR STRING; 292414.TM1040_3653; -. DR EnsemblBacteria; ABF62620; ABF62620; TM1040_3653. DR GeneID; 4075622; -. DR KEGG; sit:TM1040_3653; -. DR PATRIC; 23383798; VBIRueSp69653_0743. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; RSP292414:GHCT-3726-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Plasmid; Thiamine biosynthesis; Transferase. SQ SEQUENCE 198 AA; 22298 MW; 6B1C55DF868CB352 CRC64; MTLDRFYPIF DDANWLQRML PLGVKLVQLR IKDQPIDVVQ QQITRSRGLC RQHGAVLVVN DYWQLAIELG CDWVHLGQED LDDADLKAIR AAGLKLGVST HDEDELDRVL ALSPEYVALG PVYPTILKHM KWHEQGLPRV REWKTRIGSI PLVGIGGMSV ERAPGVFEAG ADIVSVVTDI TLNSDPEARV RQWVEATR // ID Q1GNP4_SPHAL Unreviewed; 208 AA. AC Q1GNP4; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 13-NOV-2013, entry version 51. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Sala_3023; OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) OS (Sphingomonas alaskensis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=317655; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13593 / LMG 18877 / RB2256; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., RA Chertkov O., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Cavicchioli R., Robb F., Ertan H., Schut F., RA Ting L.M., Richardson P.; RT "Complete sequence of chromosome of Sphingopyxis alaskensis RB2256."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000356; ABF54728.1; -; Genomic_DNA. DR RefSeq; YP_618061.1; NC_008048.1. DR ProteinModelPortal; Q1GNP4; -. DR STRING; 317655.Sala_3023; -. DR EnsemblBacteria; ABF54728; ABF54728; Sala_3023. DR GeneID; 4082855; -. DR KEGG; sal:Sala_3023; -. DR PATRIC; 23695426; VBISphAla23391_3118. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NRRDSIM; -. DR OrthoDB; EOG679THR; -. DR BioCyc; SALA317655:GHHY-3067-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 208 AA; 22993 MW; B9CF2EE8723061B0 CRC64; MRARHPPPSK VPGVWLFSDE RARTGLRKLA ARLPPGSGIV LRHDSRPPGA RWRLLRRLMR LGRARRLTVL LAGTPAIARR WGADGVYLRQ RDLHQARRAQ ALGLILTLPV HDAREARRAR RVGAHAAFVS PLHPTRSHPG APALGQAAWL RLARLAGGQP IALGGMTRAR ARRLNRASGI AAGWAAIDAW DEKPAKRRLR QKRNAVPT // ID Q1GTJ3_SPHAL Unreviewed; 216 AA. AC Q1GTJ3; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 14-MAY-2014, entry version 68. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Sala_1315; OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) OS (Sphingomonas alaskensis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=317655; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13593 / LMG 18877 / RB2256; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., RA Chertkov O., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Cavicchioli R., Robb F., Ertan H., Schut F., RA Ting L.M., Richardson P.; RT "Complete sequence of chromosome of Sphingopyxis alaskensis RB2256."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000356; ABF53029.1; -; Genomic_DNA. DR RefSeq; YP_616362.1; NC_008048.1. DR ProteinModelPortal; Q1GTJ3; -. DR STRING; 317655.Sala_1315; -. DR EnsemblBacteria; ABF53029; ABF53029; Sala_1315. DR GeneID; 4082239; -. DR KEGG; sal:Sala_1315; -. DR PATRIC; 23691844; VBISphAla23391_1358. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FQFRVKG; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SALA317655:GHHY-1325-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22704 MW; 129DBB1B4BD01901 CRC64; MTTAPTAPTC QLYLISPLDV GGDFPARLEE ALAAGPVAAF QFRVKGLDQH DAARLAEPLR AICAEHDVAF IVNDDVALAK RLKADGVHLG QGDGDPKEAR RQLGPDAQIG VTCHDSRHLA MDAGEAGADY VAFGAFFPTT TKTVEHRADP EILTWWQGLF ELPCVAIGGI TIDNAKTLAD AGADFVAVSG GVWNYRDGPG AAVRAFAEIL GNQPAG // ID Q1GZ40_METFK Unreviewed; 310 AA. AC Q1GZ40; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 14-MAY-2014, entry version 68. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=Mfla_2230; OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylobacillus. OX NCBI_TaxID=265072; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT / ATCC 51484 / DSM 6875; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., RA Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N., Anderson I., RA Richardson P.; RT "Complete sequence of Methylobacillus flagellatus KT."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000284; ABE50497.1; -; Genomic_DNA. DR RefSeq; YP_546338.1; NC_007947.1. DR ProteinModelPortal; Q1GZ40; -. DR STRING; 265072.Mfla_2230; -. DR EnsemblBacteria; ABE50497; ABE50497; Mfla_2230. DR GeneID; 3999786; -. DR KEGG; mfa:Mfla_2230; -. DR PATRIC; 32270269; VBIMetFla97085_2345. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MFLA265072:GHWJ-2287-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 310 AA; 34444 MW; 0C6011D52E72FF92 CRC64; MSVVRVAAAV LQRADGQVLL AERPVGKPWE GWWEFPGGKI ESGETPYHAL VRELREELGI EVEKAYPWLL RRFEYPDRSV ELHFFIVRGW RHDPHGCEGQ QLSWQHPAAL TVGPMLPANA PILAALGLPS MYAVSNAVEL GEQRFLERLQ RALDQGLRLL QLREKHLSLE SLERLAEQVL TLAQPYQARV LLNGEPETAR ALGMAGVHLS SERLMALPER PHDMLCAASC HDAQQLARAQ SLALDFAVLS PVLPTLSHPQ ARVLGWEGFS TLVQGSSLPV YALGGLQKAH MEQAWQHGAH GIAMMRGAWD // ID Q1I5C9_PSEE4 Unreviewed; 314 AA. AC Q1I5C9; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 14-MAY-2014, entry version 62. DE SubName: Full=Putative hydrolase MutT/nudix family/Thiamine monophosphate synthase; GN OrderedLocusNames=PSEEN4474; OS Pseudomonas entomophila (strain L48). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=384676; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L48; RX PubMed=16699499; DOI=10.1038/nbt1212; RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C., RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., RA Wincker P., Weissenbach J., Lemaitre B., Medigue C., Boccard F.; RT "Complete genome sequence of the entomopathogenic and metabolically RT versatile soil bacterium Pseudomonas entomophila."; RL Nat. Biotechnol. 24:673-679(2006). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT573326; CAK17156.1; -; Genomic_DNA. DR RefSeq; YP_609940.1; NC_008027.1. DR ProteinModelPortal; Q1I5C9; -. DR STRING; 384676.PSEEN4474; -. DR EnsemblBacteria; CAK17156; CAK17156; PSEEN4474. DR GeneID; 4089669; -. DR KEGG; pen:PSEEN4474; -. DR PATRIC; 19867012; VBIPseEnt83862_4311. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PENT384676:GJB8-4251-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 34265 MW; AEF06B68B13023E5 CRC64; MKRIHVVAAV IRGTDGRILI ARRADTQHQG GLWEFPGGKV EDGEGVEVAL ARELREELGI EVARSRPLIK VSHDYPDKQV LLDVREVDAF TGEPHGAEGQ PLAWVAPRDL GQYEFPEANK PIVAAARLPD QYLITPDGLE VPELLKGIQR AVASGIRLIQ LRAPDMYDPK YRDVAVDAVG LCAGKAQLML KGPLEWLGDF PSAGWHLTAA QLRKYAAKGR PFPKERWLAA SCHNAEELAL AEQMGVDFVT LSPVQATQTH PDATPLGWDE AQRLITGISH PVFLLGGVGP GERERAWEAG AQGVAGIRAF WPDV // ID Q1II90_KORVE Unreviewed; 210 AA. AC Q1II90; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 13-NOV-2013, entry version 52. DE SubName: Full=Thiamine-phosphate diphosphorylase; GN OrderedLocusNames=Acid345_4410; OS Koribacter versatilis (strain Ellin345). OC Bacteria; Acidobacteria; Candidatus Koribacter. OX NCBI_TaxID=204669; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin345; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., RA Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., RA Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., RA Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C., RA Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., RA Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., RA Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., RA Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., RA Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000360; ABF43410.1; -; Genomic_DNA. DR RefSeq; YP_593484.1; NC_008009.1. DR ProteinModelPortal; Q1II90; -. DR STRING; 204669.Acid345_4410; -. DR EnsemblBacteria; ABF43410; ABF43410; Acid345_4410. DR GeneID; 4073316; -. DR KEGG; aba:Acid345_4410; -. DR PATRIC; 31986189; VBICanKor57425_4713. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; KVER204669:GHL8-4449-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 210 AA; 22201 MW; D90D720EC09C75F4 CRC64; MILYYITDRR ALKGDLIAKI SEAAHAGVDY VQLREKDLSP RELERLARGA MDAISGTNTK LLVNSRSDVA ISVGAHGVHL TSNDISAGDA RALWRERRPV IGVSCHSTAD VRMAEAQGAD FAVLAPVFGK GEQPGIGLQV LAEATGIVPP PEHTESAPRA VRFPALALGG VTVENARMCL AYGAAGVAGI RLFQENDVSA VVRALRAHTS // ID Q1JX79_DESAC Unreviewed; 497 AA. AC Q1JX79; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 19-FEB-2014, entry version 44. DE SubName: Full=Phosphomethylpyrimidine kinase; GN ORFNames=Dace_0922; OS Desulfuromonas acetoxidans DSM 684. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Desulfuromonadaceae; Desulfuromonas. OX NCBI_TaxID=281689; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 684; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M., Hauser L.; RT "Annotation of the draft genome assembly of Desulfuromonas acetoxidans RT DSM 684."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 684; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Bruce D., RA Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of Desulfuromonas RT acetoxidans DSM 684."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEW02000016; EAT14913.1; -; Genomic_DNA. DR ProteinModelPortal; Q1JX79; -. DR EnsemblBacteria; EAT14913; EAT14913; Dace_0922. DR PATRIC; 26635073; VBIDesAce8486_2796. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 497 AA; 52396 MW; F7530E45419B06F9 CRC64; MVFDRALSGC GFFMISSLQT TPQHIPLRGV YLITDDSPEN VLLENVKLAL RGGTRIVQYR DKIRPLNEQQ QLAKRLRTLC HEFQALFIIN DSARLAAEVC ADGVHLGQSD GHIREARQLL GDKAIIGVST QTLELARQAE QDGADYIGVG SVYPTGTKQD AVHIGLDDLK TIATGVSLPV VAIGGITAAR LPDVLDAGAD SVAVVSAIMS DAQPEVASRE LALQFQRNQP LPHGRVLTVA GSDSGGGAGI QADLKAITLL GSYGSSVLTA LTAQNTLGVT AIHAPPIDFV QQQLDAVLCD IGTDIIKTGM LYSAEIIATV AERFRSYGAL CVIDPVMIAK GGSALLQQEA IDTFIRDLLP QAYLLTPNIP EAETLTGLSI ATVSDMEQAA KALQTMGARN VLIKGGHLEG DPIDLLQYGT TTITLPGKRL DTPHTHGTGC TTASVIATLL AQGVSLPQAV TQAKQFITNA IADAPHIGHG HGPVNHYTAA LTLVGDR // ID Q1JYF7_DESAC Unreviewed; 203 AA. AC Q1JYF7; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 19-FEB-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=Dace_1218; OS Desulfuromonas acetoxidans DSM 684. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Desulfuromonadaceae; Desulfuromonas. OX NCBI_TaxID=281689; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 684; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M., Hauser L.; RT "Annotation of the draft genome assembly of Desulfuromonas acetoxidans RT DSM 684."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 684; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Bruce D., RA Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of Desulfuromonas RT acetoxidans DSM 684."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEW02000012; EAT15249.1; -; Genomic_DNA. DR ProteinModelPortal; Q1JYF7; -. DR EnsemblBacteria; EAT15249; EAT15249; Dace_1218. DR PATRIC; 26634101; VBIDesAce8486_2321. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 21797 MW; C97781715507D043 CRC64; MAVDFSLYLI SDRRQTGGRD LLEVIEAALS GGVQAVQLRE KDLSTRELFT MGCALRKLTQ RYQATLLIND RIDIALAVDA DGVHLTEQSL EVEVARRLLG PDKLIGVSTH HVDRAVAVEQ QGADFITFSP IYATPSKAAY GAPQGLDKLR NLCRQVSLPV IALGGINAQR RQAVLAAGAS GCAVISAILT ANDPCQAAKT LRF // ID Q1KPV0_ARATH Unreviewed; 912 AA. AC Q1KPV0; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 14-MAY-2014, entry version 61. DE SubName: Full=FZL; DE SubName: Full=FZO-like protein; GN Name=FZL; OrderedLocusNames=At1g03160; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [2] RP NUCLEOTIDE SEQUENCE. RX PubMed=16617119; DOI=10.1073/pnas.0507287103; RA Gao H., Sage T.L., Osteryoung K.W.; RT "FZL, an FZO-like protein in plants, is a determinant of thylakoid and RT chloroplast morphology."; RL Proc. Natl. Acad. Sci. U.S.A. 103:6759-6764(2006). RN [3] RP NUCLEOTIDE SEQUENCE. RG TAIR; RA Swarbreck D., Lamesch P., Wilks C., Huala E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ462573; ABE96616.1; -; mRNA. DR EMBL; CP002684; AEE27537.1; -; Genomic_DNA. DR RefSeq; NP_171815.3; NM_100198.4. DR UniGene; At.44048; -. DR EnsemblPlants; AT1G03160.1; AT1G03160.1; AT1G03160. DR GeneID; 839566; -. DR KEGG; ath:AT1G03160; -. DR TAIR; AT1G03160; -. DR eggNOG; COG0699; -. DR HOGENOM; HOG000241410; -. DR InParanoid; Q1KPV0; -. DR OMA; YVCYLPA; -. DR Genevestigator; Q1KPV0; -. DR GO; GO:0009507; C:chloroplast; IDA:TAIR. DR GO; GO:0031969; C:chloroplast membrane; IDA:TAIR. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR. DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 2: Evidence at transcript level; KW Complete proteome; Reference proteome. SQ SEQUENCE 912 AA; 100731 MW; 6904836A55B43456 CRC64; MRTLISHRQC VTSPFLISAA SPPFPGRCFK LSSFTPPRHR RFSSLSIRNI SHESADQTSS SRPRTLYPGG YKRPELAVPG LLLRLDADEV MSGNREETLD LVDRALAKSV QIVVIDGGAT AGKLYEAACL LKSLVKGRAY LLIAERVDIA SAVGASGVAL SDEGLPAIVA RNTLMGSNPD SVLLPLVARI VKDVDSALIA SSSEGADFLI LGSGEEDTQV ADSLLKSVKI PIYVTCRGNE EAKEELQLLK SGVSGFVISL KDLRSSRDVA LRQSLDGAYV VNNHETQNMN ELPEKKNSAG FIKLEDKQKL IVEMEKSVLR ETIEIIHKAA PLMEEVSLLI DAVSRIDEPF LMVIVGEFNS GKSTVINALL GKRYLKEGVV PTTNEITFLC YSDLESEEQQ RCQTHPDGQY VCYLPAPILK DINIVDTPGT NVILQRQQRL TEEFVPRADL LVFVLSADRP LTESEVAFLR YTQQWKKKFV FILNKSDIYR DARELEEAIS FVKENTRKLL NTENVILYPV SARSALEAKL STASLVGRDD LEIADPGSNW RVQSFNELEK FLYSFLDSST ATGMERIRLK LETPMAIAER LLSSVEALVR QDCLAAREDL ASADKIISRT KEYALKMEYE SISWRRQALS LIDNARLQVV DLIGTTLRLS SLDLAISYVF KGEKSASVAA TSKVQGEILA PALTNAKELL GKYAEWLQSN TAREGSLSLK SFENKWPTYV NSKTQLGIDT YDLLQKTDKV SLKTIQNLSA GTTSKRLEQD IREVFFVTVG GLGAAGLSAS LLTSVLPTTL EDLLALGLCS AGGYVAIANF PYRRQAIIGK VNKVADALAQ QLEDAMQKDL SDATSNLVNF VNIVAKPYRE EAQLRLDRLL GIQKELSDIR SKLQLLQVDI DNLHVSRDEM RL // ID Q1LS24_RALME Unreviewed; 376 AA. AC Q1LS24; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 14-MAY-2014, entry version 57. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=Rmet_0166; OS Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=266264; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH34 / ATCC 43123 / DSM 2839; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Mergeay M., Benotmane M.A., RA Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., RA van der Lelie D., Richardson P.; RT "Complete sequence of the chromosome of Ralstonia metallidurans RT CH34."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000352; ABF07052.1; -; Genomic_DNA. DR RefSeq; YP_582321.1; NC_007973.1. DR ProteinModelPortal; Q1LS24; -. DR STRING; 266264.Rmet_0166; -. DR EnsemblBacteria; ABF07052; ABF07052; Rmet_0166. DR GeneID; 4036951; -. DR KEGG; rme:Rmet_0166; -. DR PATRIC; 20284856; VBIRalMet4734_0545. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CMET266264:GJ5G-169-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 376 AA; 39588 MW; EEABAB48D6220266 CRC64; MTRQGVAAAI DAALFDDLMA RYAAMFGRDE TPWRIWSAAN APAALDRHDV VLSDGEATGD LIDRVVAADA VLIESEREGG RWIDTVRSPM GTWVLDVRAD DDTPHSAAFV AVLRAALSLH FPAHDALCIA RAWLPGATAW PNDFARFPQV RHAALVPPGQ TAQPFAPCPP DLGLYAVMPS AAWIETLVPL AVPTVQLRFK SGDADAVKHE VARAAKAAKG SQSRLFINDH WRVAIDHHAA CGGDSGIYGI HLGQEDLDDA DLDAIRASGL RLGVSTHGYA EMLRVAAISP SYLALGAIFP TTTKVMPTQP QGMGRFQSYV ALMQPVIPSL VGIGGVNAGN MGEVLAVGVG SAAVVRAITE ASDVPAAVAG LNALFA // ID Q1LU44_BAUCH Unreviewed; 214 AA. AC Q1LU44; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 14-MAY-2014, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BCI_0042; OS Baumannia cicadellinicola subsp. Homalodisca coagulata. OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia. OX NCBI_TaxID=374463; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188; RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., RA Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., RA Moran N.A., Eisen J.A.; RT "Metabolic complementarity and genomics of the dual bacterial RT symbiosis of sharpshooters."; RL PLoS Biol. 4:1079-1092(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000238; ABF14139.1; -; Genomic_DNA. DR RefSeq; YP_588520.1; NC_007984.1. DR ProteinModelPortal; Q1LU44; -. DR STRING; 374463.BCI_0042; -. DR EnsemblBacteria; ABF14139; ABF14139; BCI_0042. DR GeneID; 4056568; -. DR KEGG; bci:BCI_0042; -. DR PATRIC; 21073573; VBIBauCic75062_0043. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BCIC374463:GI6Q-42-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 24044 MW; CDB16DDA77A3F8BB CRC64; MLTDKYLDLP NRLGLYPIID SLVWLVRMLD LGITTIQLRI KDKSEAEVEP DIEAAIVLGR RYNARVFIND YWRLAIRHSA YGVHLGQEDI NKADIHAINH AGLFWGISTH NEEELMRAIT YGPSYIALGH IFPTTTKIMH SRPQGLKNLR KLVTKSRNLP TVAIGGISAT KIDSVLECGV GSIAVVSAIT RAPDWHKATI NILNKIKHWQ SIYA // ID Q1M5U4_RHIL3 Unreviewed; 211 AA. AC Q1M5U4; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 14-MAY-2014, entry version 62. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=pRL110442; OS Rhizobium leguminosarum bv. viciae (strain 3841). OG Plasmid pRL11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=216596; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3841; PLASMID=pRL11; RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34; RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., RA Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D., RA Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C., RA Arrowsmith C., Cherevach I., Chillingworth T., Clarke K., Cronin A., RA Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S., RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., RA Whitehead S., Parkhill J.; RT "The genome of Rhizobium leguminosarum has recognizable core and RT accessory components."; RL Genome Biol. 7:R34.1-R34.20(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM236085; CAK03395.1; -; Genomic_DNA. DR RefSeq; YP_771476.1; NC_008384.1. DR ProteinModelPortal; Q1M5U4; -. DR STRING; 216596.pRL110442; -. DR EnsemblBacteria; CAK03395; CAK03395; pRL110442. DR GeneID; 4405072; -. DR KEGG; rle:pRL110442; -. DR PATRIC; 23148793; VBIRhiLeg32091_7293. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RLEG216596:GKE5-6065-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Plasmid; KW Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21646 MW; 2D940767E532CEC9 CRC64; MKAFDLSLYL VLDPDLCAGI GMVETARLAV AGGATMVQLR DKHAGTIRMI ETGRALKQAL DGTGALLIVN DDVEAAIAIG VDGLHIGQED MDAMRARAMI GPEMILGLSV ESEALANAVD PGLVDYTGVG PVFATPTKAD HKQPIGFDGL ARLVKASPVP SVAIGGLKAD HVAQVFAAGA SGLAVVSAIC GTPDPEAATR RIAAEIRKVR A // ID Q1MC02_RHIL3 Unreviewed; 217 AA. AC Q1MC02; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 14-MAY-2014, entry version 52. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase like protein; DE EC=2.5.1.3; GN Name=thiE2; OrderedLocusNames=RL4040; OS Rhizobium leguminosarum bv. viciae (strain 3841). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=216596; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3841; RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34; RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., RA Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D., RA Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C., RA Arrowsmith C., Cherevach I., Chillingworth T., Clarke K., Cronin A., RA Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S., RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., RA Whitehead S., Parkhill J.; RT "The genome of Rhizobium leguminosarum has recognizable core and RT accessory components."; RL Genome Biol. 7:R34.1-R34.20(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM236080; CAK09530.1; -; Genomic_DNA. DR RefSeq; YP_769617.1; NC_008380.1. DR ProteinModelPortal; Q1MC02; -. DR STRING; 216596.RL4040; -. DR EnsemblBacteria; CAK09530; CAK09530; RL4040. DR GeneID; 4400561; -. DR KEGG; rle:RL4040; -. DR PATRIC; 23144889; VBIRhiLeg32091_5356. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RLEG216596:GKE5-4107-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 217 AA; 22786 MW; 0204F0423F9A7469 CRC64; MTEPENRCRL VLIVADIADA DEQAKIVADA LKGGDVASVI VPQYGLDDGT FQKHAEKLVP LIQDAGAAAL IAGDSRVAGR AKADGLHLSG NAEALSEAID KHAPKLIVGG GNAADRHHAL EIGEVRPDYI FFGKLDGDIK PEAHPKNLAL GEWWASMIEI PCIVMGGTDP ASALAVAETG AEFVAMRLAV FAEPARAPAI VAEINALLDE KAPRFED // ID Q1MYG4_9GAMM Unreviewed; 492 AA. AC Q1MYG4; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=RED65_02128; OS Bermanella marisrubri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Bermanella. OX NCBI_TaxID=207949; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RED65; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQH01000026; EAT10981.1; -; Genomic_DNA. DR ProteinModelPortal; Q1MYG4; -. DR EnsemblBacteria; EAT10981; EAT10981; RED65_02128. DR PATRIC; 27186008; VBIBerMar44794_2198. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 492 AA; 54049 MW; 9E6E0AB9F79133CF CRC64; MNHETRPMVL CVSGIDAQGL SGYQADLRAL EAMAVHGCLA ATALTAQTQT GVNALNPVDI EVFQSQLDSI ASEYQINVIK VGLVASEEQV DVLLNHPISQ NAKIILDPIL SATSGHFQNL ATQLAIVKKL IERAYVVTPN WDEALLLSNA DQNVIVEELA NQVLALGCHS VYLKGGHTAQ KNRDLFRQCN AELKDIGESF NLVGKRTQSF SARGTGCIIA SSIAAALALG HRLEDAVVIA KMQMESAWDN EFELSSGQVA LQPKSLFSGT SMIQYLPLIH GHRDLLDTHF LPCEPGLGLY PVVDRAEWLT RLLPLGIRII QLRIKDLSGQ ALREEITRAI HISEDYGVQL FINDYWQLAI ELGAYGVHLG QEDLLEADLK AIEQAGLRLG VSSHCYFEVA RALTINPSYL AYGPIYHTDS KQMPWQPQGL QQLSFWKKNI QHIPMVAIGG IKLERISQVA LTGVDSIAMI SAITQAEDPE LVTETMMKEM EL // ID Q1ND52_9SPHN Unreviewed; 187 AA. AC Q1ND52; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 32. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=SKA58_18127; OS Sphingomonas sp. SKA58. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=314266; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SKA58; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQG01000006; EAT09033.1; -; Genomic_DNA. DR ProteinModelPortal; Q1ND52; -. DR EnsemblBacteria; EAT09033; EAT09033; SKA58_18127. DR PATRIC; 29451207; VBISphSp87348_2228. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 187 AA; 20603 MW; 00270B3A390B4A2F CRC64; MAMHRRHRKS LPGLWLMTDE RVADDRLLAA ARALPRGRAG IILRHYRTPP AQRRALFDAL RAIARRRRLI LLLAGPVRAA AAWRADGWHG RDSRRPPRPL LHSAPAHDSR EIRMAQRAGS DLLFLSPLFP TRSHPGARSL GRARFAALAH ATPLPVIALG GVTARHRRSL AALSAAGWAA IDGLTNN // ID Q1NDL0_9SPHN Unreviewed; 260 AA. AC Q1NDL0; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SKA58_09861; OS Sphingomonas sp. SKA58. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=314266; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SKA58; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQG01000005; EAT09259.1; -; Genomic_DNA. DR ProteinModelPortal; Q1NDL0; -. DR EnsemblBacteria; EAT09259; EAT09259; SKA58_09861. DR PATRIC; 29448004; VBISphSp87348_0274. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 82 86 HMP-PP binding (By similarity). FT REGION 180 182 THZ-P binding (By similarity). FT METAL 115 115 Magnesium (By similarity). FT METAL 134 134 Magnesium (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 183 183 HMP-PP (By similarity). FT BINDING 210 210 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 260 AA; 27442 MW; F7650B26A42F7A2D CRC64; MLSAGQGSIH SRPWRGRRSS YKAAMTDFTD VELALDPQFA AQFEQGFRPA CQLYLISPPA IDAAFVDRLA AALDGGRVAA FQLRLKGMDE DEIARAAEPL QKLCAERDVA FIINDSVALA QRLGADGVHL GQGDGDPKDA RKLLGPKVQI GVTCHDSRHL AMEAGEAGAD YVAFGAFYPT TTKDTVHRPE PSILGWWTTL FELPCVAIGG ITADNAAPLV AAGADFLAVS GAVWNHPAGP RAGVAAFADV LASNPPPPRA // ID Q1NIZ2_9DELT Unreviewed; 219 AA. AC Q1NIZ2; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MldDRAFT_2012; OS delta proteobacterium MLMS-1. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=262489; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MLMS-1; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M., Hauser L.; RT "Annotation of the draft genome assembly of delta proteobacterium RT MLMS-1."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MLMS-1; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Bruce D., RA Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of delta proteobacterium RT MLMS-1."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQF01000415; EAT01670.1; -; Genomic_DNA. DR ProteinModelPortal; Q1NIZ2; -. DR EnsemblBacteria; EAT01670; EAT01670; MldDRAFT_2012. DR PATRIC; 38449684; VBIDelPro91573_5087. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23749 MW; 080231D2E8BD9295 CRC64; MDIYQERVRK FQEEVTLYPV SCQKLARGRD DLQWLAAVLA GGARIVQLRD KEASARQLLV KAHAFREQTR AAGALFIVND RLDIALLSGA DGIHLGNDDL PAAEVRRYAP EMLIGVSCNT EEQAKSAAQR GASYYNIGPL FATSTKEGIK EFLGLAAIAR FSRHCELPFT VMGGIKEEHL PSLLAAGARR PAVVTAITQA PDMAAATAAM LATIHRHLG // ID Q1NXG9_9DELT Unreviewed; 219 AA. AC Q1NXG9; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MldDRAFT_1131; OS delta proteobacterium MLMS-1. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=262489; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MLMS-1; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M., Hauser L.; RT "Annotation of the draft genome assembly of delta proteobacterium RT MLMS-1."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MLMS-1; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Bruce D., RA Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of delta proteobacterium RT MLMS-1."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQF01000006; EAT06345.1; -; Genomic_DNA. DR ProteinModelPortal; Q1NXG9; -. DR EnsemblBacteria; EAT06345; EAT06345; MldDRAFT_1131. DR PATRIC; 38439652; VBIDelPro91573_0360. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23752 MW; 52123BC8E8BD8EE9 CRC64; MDIYQERVRK FQEEVTLYPV SCQKLARGRD DLQWLAAVLA GGARIVQLRD KEASARQLLV KAHAFREQTR AAGALFIVND RLDIALLSGA DGIHLGNDDL PAAEVRRYAP EMLIGVSCNT EEQAKSAAQR GASYYNIGPL FATSTKEGIK EFLGLAAIAR FSRRSELPFT VMGGIKEEHL PSLLAAGARR PAVVTAITQA PDMAAATAAM LATIHRHLG // ID Q1PUI8_9BACT Unreviewed; 228 AA. AC Q1PUI8; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=kustb0149; OS Candidatus Kuenenia stuttgartiensis. OC Bacteria; Planctomycetes; Planctomycetia; Candidatus Brocadiales; OC Candidatus Brocadiaceae; Candidatus Kuenenia. OX NCBI_TaxID=174633; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=16598256; DOI=10.1038/nature04647; RA Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., RA Taylor M.W., Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., RA Fonknechten N., Vallenet D., Segurens B., Schenowitz-Truong C., RA Medigue C., Collingro A., Snel B., Dutilh B.E., OpDenCamp H.J.M., RA vanDerDrift C., Cirpus I., vanDePas-Schoonen K.T., Harhangi H.R., RA vanNiftrik L., Schmid M., Keltjens J., vanDeVossenberg J., Kartal B., RA Meier H., Frishman D., Huynen M.A., Mewes H., Weissenbach J., RA Jetten M.S.M., Wagner M., LePaslier D.; RT "Deciphering the evolution and metabolism of an anammox bacterium from RT a community genome."; RL Nature 440:790-794(2006). RN [2] RP NUCLEOTIDE SEQUENCE. RA Genoscope; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT573074; CAJ70894.1; -; Genomic_DNA. DR ProteinModelPortal; Q1PUI8; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 25102 MW; 9EEAD143B1C66837 CRC64; MKNSTIKYKK RFSDVLLYVI ISPTLVRKNG GNILQEVIRG GADAVQLREK TMPDNEFLAI AKDFREITGQ TNTLFIINDR AKIAGKVNAD GLHIGQTDMN INNARKIIGN DKIIGRSTHN IFQARLAEQE GADYISVGPL FYTATKSHEP PVGLRYLQQV RQEISLPFVV IGGITANNAA EIIQAGGNRI AICSAIICSE NITQATRTLK DLLVKNNPFS GQEKKLPL // ID Q1PZK7_9BACT Unreviewed; 219 AA. AC Q1PZK7; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiC; Synonyms=thiE; ORFNames=kustd1766; OS Candidatus Kuenenia stuttgartiensis. OC Bacteria; Planctomycetes; Planctomycetia; Candidatus Brocadiales; OC Candidatus Brocadiaceae; Candidatus Kuenenia. OX NCBI_TaxID=174633; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=16598256; DOI=10.1038/nature04647; RA Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., RA Taylor M.W., Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., RA Fonknechten N., Vallenet D., Segurens B., Schenowitz-Truong C., RA Medigue C., Collingro A., Snel B., Dutilh B.E., OpDenCamp H.J.M., RA vanDerDrift C., Cirpus I., vanDePas-Schoonen K.T., Harhangi H.R., RA vanNiftrik L., Schmid M., Keltjens J., vanDeVossenberg J., Kartal B., RA Meier H., Frishman D., Huynen M.A., Mewes H., Weissenbach J., RA Jetten M.S.M., Wagner M., LePaslier D.; RT "Deciphering the evolution and metabolism of an anammox bacterium from RT a community genome."; RL Nature 440:790-794(2006). RN [2] RP NUCLEOTIDE SEQUENCE. RA Genoscope; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT573072; CAJ72511.1; -; Genomic_DNA. DR ProteinModelPortal; Q1PZK7; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23851 MW; 2BE03F032D6C2E29 CRC64; MPLQRKQSAY SPAFVLITDR KQSRLPLINA VKLALKGGVN TIQLREKDLP TKDIYSLACE LRTITHGLNA SLIINDRVDI VLAANADGVH LGWQSMPVSR VRNLIGFERI IGISAHNMQE ALQARDSGAD YITYGPIFKT PSKEGVVEPT GTESLRKLKE KIRIPVIALG GITVDNAESV MESGANGIAV VSSILKSDNP ENTALRLYSI IQHHSKMSG // ID Q1QA40_PSYCK Unreviewed; 360 AA. AC Q1QA40; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 14-MAY-2014, entry version 59. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=Pcryo_1686; OS Psychrobacter cryohalolentis (strain K5). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=335284; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K5; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.; RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000323; ABE75463.1; -; Genomic_DNA. DR RefSeq; YP_580947.1; NC_007969.1. DR ProteinModelPortal; Q1QA40; -. DR STRING; 335284.Pcryo_1686; -. DR EnsemblBacteria; ABE75463; ABE75463; Pcryo_1686. DR GeneID; 4036040; -. DR KEGG; pcr:Pcryo_1686; -. DR PATRIC; 23062941; VBIPsyCry128170_1792. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; VAVIHYQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PCRY335284:GHE9-1721-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 360 AA; 39629 MW; 3E20D42E38656F8A CRC64; MTVKQSNSLT NTSITTVNVA VAVIHYQNQY LLGFRAASQH QGNRYEFVGG KIDAHETAKQ GLIREVAEET GINIANNTAV KLGRLHHDYG DKQVCLQVYR IEVTAQQYAQ YKNLSYGLEG QKLTWVEEAE LLAGHYDLPA ANKTILAWLQ LPMQITVTYP LSHFDAASNP IAAWLQYHHE HITAGAWVYM RTKAAGTENS IKQLLQLRTD IQAITPDHLD MDKADNVEAN NQIIASHLTQ TQLMQWSSGV AKEPMSYSAL STSLPLIVSC HDVDSINAAN QLASIRLQQQ LPPVIGIFLA PVECTQTHPD TPALGWEAWS NLANLADMPV IGLGGLSPMM YKQAVLHGGV AVAGIRQFLK // ID Q1QCZ1_PSYCK Unreviewed; 226 AA. AC Q1QCZ1; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 14-MAY-2014, entry version 59. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Pcryo_0679; OS Psychrobacter cryohalolentis (strain K5). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=335284; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K5; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.; RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000323; ABE74462.1; -; Genomic_DNA. DR RefSeq; YP_579946.1; NC_007969.1. DR ProteinModelPortal; Q1QCZ1; -. DR STRING; 335284.Pcryo_0679; -. DR EnsemblBacteria; ABE74462; ABE74462; Pcryo_0679. DR GeneID; 4034372; -. DR KEGG; pcr:Pcryo_0679; -. DR PATRIC; 23060837; VBIPsyCry128170_0749. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IGRTCHG; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PCRY335284:GHE9-703-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24368 MW; 9C7C6A20FD86B435 CRC64; MIQSSVSTVS HTIPKLYLLT NDDEFSLLYQ KLEAALATGL IALLQIRRKQ ILALPDGESV LYKEALQIVN LAKTYNVPVL INDNIALAEK LGIGVHLGQQ DGDLSEATQS LAPNQIIGRT CHGDITLVKA AKTEGASYAA MGAIFASTTK PNAATILRQQ LIEGCQQDIK ICVIGGLTAE NISELAGLPI AYIAIVGDIM DLPVHQIATR CQQWQQVLNK WNVPAE // ID Q1QHN3_NITHX Unreviewed; 233 AA. AC Q1QHN3; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 14-MAY-2014, entry version 51. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN OrderedLocusNames=Nham_3535; OS Nitrobacter hamburgensis (strain X14 / DSM 10229). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=323097; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X14 / DSM 10229; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Ward B., RA Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., RA Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.; RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000319; ABE64264.1; -; Genomic_DNA. DR RefSeq; YP_578724.1; NC_007964.1. DR ProteinModelPortal; Q1QHN3; -. DR STRING; 323097.Nham_3535; -. DR EnsemblBacteria; ABE64264; ABE64264; Nham_3535. DR GeneID; 4030518; -. DR KEGG; nha:Nham_3535; -. DR PATRIC; 22695121; VBINitHam61822_4555. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; NHAM323097:GHP7-3591-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 233 AA; 24015 MW; 8B9DB1A782E5B13D CRC64; MLAKPVSPRP APRLYLATPS VDDPSQLAAR LPALLAAADV AAVMVRLSAA DPRTLISRIK ALAPAIQGDG AALLLDGHAD LVARSGADGA HLTGIEAMQE AMPSLKPDRI AGVGGLSTRH DSMIAGEAGA DYVLFGEPDE AGERPSADAI AERLAWWAEL FEPPCVGYAT SIDEARTFAA SGADFILAGD FIWNDPRGAA AAAMDTIDAI RQGHGSQGDR AMPATKPDRG DAG // ID Q1QJD5_NITHX Unreviewed; 208 AA. AC Q1QJD5; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Nham_2894; OS Nitrobacter hamburgensis (strain X14 / DSM 10229). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=323097; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X14 / DSM 10229; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Ward B., RA Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., RA Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.; RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000319; ABE63662.1; -; Genomic_DNA. DR RefSeq; YP_578122.1; NC_007964.1. DR ProteinModelPortal; Q1QJD5; -. DR STRING; 323097.Nham_2894; -. DR EnsemblBacteria; ABE63662; ABE63662; Nham_2894. DR GeneID; 4033200; -. DR KEGG; nha:Nham_2894; -. DR PATRIC; 22693717; VBINitHam61822_3858. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NHAM323097:GHP7-2947-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 208 AA; 22683 MW; FB4138D6B53AE5D1 CRC64; MPYPDRSAYP DRFYPVVDTL DWVRRLTGLG VGTVQLRAKD LNDGESLQLV SDALQIVKDT PTRLVVNDYW RAAIVAGAKH VHLGQEDLTT ADVHEIRKAG LTLGLSTHDD AELDTALAAE PDYVALGPIF FTTLKSMRFA PQGIPKIAEW KKRVGNIPLV AIGGIKLEQA AEIFDAGADS IAVVSDVTQN PDPDARVKAW LEQVIETA // ID Q1QSB1_CHRSD Unreviewed; 220 AA. AC Q1QSB1; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Csal_3303; OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB OS 13768). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., RA O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., RA Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., RA Canovas D., Richardson P.; RT "Complete sequence of Chromohalobacter salexigens DSM 3043."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000285; ABE60647.1; -; Genomic_DNA. DR RefSeq; YP_575346.1; NC_007963.1. DR ProteinModelPortal; Q1QSB1; -. DR STRING; 290398.Csal_3303; -. DR EnsemblBacteria; ABE60647; ABE60647; Csal_3303. DR GeneID; 4028848; -. DR KEGG; csa:Csal_3303; -. DR PATRIC; 21450486; VBIChrSal113723_3320. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23101 MW; F4D8CD24A7553467 CRC64; MNRTPDWTRG IYAITDATLL PDDAHLFAAC ERALEAGLAL LQYRDKSADA GKRWRQASGL AARCHAAGVP LIVNDDIALA ARLRSRVGSH VGLHLGQRDG SLRDARQALG DEAIIGATCH ARLDLAERAA AEGASYLAFG RFFASRTKPE APPASLDLLG EAARFGLPRV AIGGLDVHTM RLAREAGADL LATVHAVFGA GDPAAAVRAL QASLGDTAQH // ID Q1QVH8_CHRSD Unreviewed; 314 AA. AC Q1QVH8; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 14-MAY-2014, entry version 66. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=Csal_2179; OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB OS 13768). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., RA O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., RA Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., RA Canovas D., Richardson P.; RT "Complete sequence of Chromohalobacter salexigens DSM 3043."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000285; ABE59530.1; -; Genomic_DNA. DR RefSeq; YP_574229.1; NC_007963.1. DR ProteinModelPortal; Q1QVH8; -. DR STRING; 290398.Csal_2179; -. DR EnsemblBacteria; ABE59530; ABE59530; Csal_2179. DR GeneID; 4026673; -. DR KEGG; csa:Csal_2179; -. DR PATRIC; 21448210; VBIChrSal113723_2199. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 35170 MW; C36028A7AAA5218C CRC64; MVKRRVHVAA AAIIREDGHV LLARRPSIVD QGGLWEFPGG KLAPYETGFE ALRRELREEL GIEIQRAQPL IRVHHEYEDK RILLDVWQVH AFEGEPFGRE GQAVRWVPQE ELNNYPFPEA NHAILRAVCL PHDYLISDEE DDDAVFLGKL ERALRDDGVR LVQLRAKSLD EDAYLKRAEQ ALALCRRYQA RLILNGDPAL LEHVDADGVH LPSRTLMALE HRPIATGKWL AASTHNPEQL AQAATIGCDF VTFSPLRITP SHPDAAPVGW HDFQQLVETA AMPVFALGGV TRGDIDQARA VGAQGIASIR DLWK // ID Q1V1B8_PELUQ Unreviewed; 180 AA. AC Q1V1B8; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 16-OCT-2013, entry version 34. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=PU1002_04546; OS Candidatus Pelagibacter ubique HTCC1002. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=314261; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC1002; RA Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPV01000001; EAS84960.1; -; Genomic_DNA. DR ProteinModelPortal; Q1V1B8; -. DR EnsemblBacteria; EAS84960; EAS84960; PU1002_04546. DR PATRIC; 30361432; VBICanPel113578_0898. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 180 AA; 20983 MW; E75A12350E5F6208 CRC64; MHNKILKKYY FINKFNQSHI DKQDQETTII YRNYDQDIDE KLILRIKSYC KKRGHKFLLS NNIKLAIKLN LNGAYIPSFN NDKKHLSYSF KKNFIILGSA HNVFEIRNKE SQNVKAIFLS SIFKKNKNFL GINRFKLLSR LSKKPFIALG GISKTSLKKL NLVNCIGFAG ISFFEQKKGP // ID Q1V1Z4_PELUQ Unreviewed; 207 AA. AC Q1V1Z4; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=PU1002_03416; OS Candidatus Pelagibacter ubique HTCC1002. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=314261; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC1002; RA Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPV01000001; EAS84734.1; -; Genomic_DNA. DR ProteinModelPortal; Q1V1Z4; -. DR EnsemblBacteria; EAS84734; EAS84734; PU1002_03416. DR PATRIC; 30360956; VBICanPel113578_0672. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 23584 MW; 5684365B7BA57471 CRC64; MKQNKINKKF VYLISPNKIS DKNFYNYLAL VLSSKKISFF QLRLKKETNL NKLIIGKKIK KICNKYKVKF LINDDPLLAK KLNADGCHLG QKDMDLIKAR KILKNKIIGV TCHNSINLAK KAINDGADYL AFGAFYATKT KTVKYRASLT VLKSIKKITS LPIVAIGGIK LSNYKKLLLN KANFLAISGY IWNNKKYKPL EAIRKLK // ID Q1V5A5_VIBAL Unreviewed; 471 AA. AC Q1V5A5; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 46. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=V12G01_09973; OS Vibrio alginolyticus 12G01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=314288; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=12G01; RA Polz M., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPS01000037; EAS74572.1; -; Genomic_DNA. DR ProteinModelPortal; Q1V5A5; -. DR EnsemblBacteria; EAS74572; EAS74572; V12G01_09973. DR PATRIC; 29684818; VBIVibAlg125131_3071. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Transferase. SQ SEQUENCE 471 AA; 52596 MW; 9D7260D05E842F4D CRC64; MSKILIPSSL IELTGLVQQC LLLAKEQGFS IEDIELGVSP TQSIQLVRDQ QITHITTDLI GGHNFEPECS FTLYYRSALS VEACAKQPSK AIYIGIADTQ VSDEKEKVLQ LDIWRHPIND EVRALSVKSK FNAMLDPEHH LAWIVTLTVL DFPIEDALTL ARGMLTQQAN VSRETLLNDN LDEGRTAQWA DQFDNFPTPV LEDNRLGIQV GWSAQGESVS FPTLTKQSLG LYPVVDDVAW IEHLLPLGIN TIQLRIKNPQ QADLEQQIIR AIELGRQYQA QVFINDYWQL AIKHGAYGVH LGQEDIEESN LAQLTKAGIR LGLSTHGYYE LLRIVQIHPS YIALGHIFPT TTKQMPSKPQ GLVRLALYQK LIDSIPYTNT EATFRPSKYK AVSDHVLGFP TVAIGGIDQS NAAQVWQTGV SSLAVVRAIT LAESPQSVIE FFAQLMKERQ RTFTDQNSEL ADIKRGEHAH G // ID Q1V7G8_VIBAL Unreviewed; 204 AA. AC Q1V7G8; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=V12G01_03621; OS Vibrio alginolyticus 12G01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=314288; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=12G01; RA Polz M., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPS01000021; EAS75257.1; -; Genomic_DNA. DR ProteinModelPortal; Q1V7G8; -. DR EnsemblBacteria; EAS75257; EAS75257; V12G01_03621. DR PATRIC; 29680107; VBIVibAlg125131_1112. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21914 MW; 804712EF031E6A12 CRC64; MNAYRLYLVT DDQQDLATLK RVVRKAVEGG VTMVQVREKH GDVRAFIERA QAVKDILKDT NVPLIINDRV DVALAVDADG VHLGQSDMPA TIARELIGPN KILGLSIENE EQLAEADSLP IDYIGLSAIF ATPTKTNTKK FWGIDGLKMA LETTSLPIVA IGGINESNIP QLSATGVHGL ALVSAICHAE DPKAASEYLL GLMS // ID Q1YFH7_MOBAS Unreviewed; 218 AA. AC Q1YFH7; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=SI859A1_03204; OS Manganese-oxidizing bacterium (strain SI85-9A1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Aurantimonas. OX NCBI_TaxID=287752; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SI85-9A1; RX PubMed=18344346; DOI=10.1128/AEM.01656-07; RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., RA Bernier-Latmani R., McCarthy J.K., Torpey J.W., Clement B.G., RA Gaasterland T., Tebo B.M.; RT "Genomic insights into Mn(II) oxidation by the marine RT alphaproteobacterium Aurantimonas sp. strain SI85-9A1."; RL Appl. Environ. Microbiol. 74:2646-2658(2008). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPJ01000006; EAS48996.1; -; Genomic_DNA. DR ProteinModelPortal; Q1YFH7; -. DR EnsemblBacteria; EAS48996; EAS48996; SI859A1_03204. DR PATRIC; 24564119; VBIAurMan112117_0226. DR BioCyc; AURANTIMONAS:SI859A1_03204-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 218 AA; 23866 MW; B86979FCAD9C33A6 CRC64; MSQAGERGVA ERPGKELRLD PFYLIVDDAE MAERLVPVGV KLLQLRAKDM DAARLRREIR RTRDVCAAHG CLLVINDFWR LAIEEGCDVV HLGQEDLAEA DCAAIRAAGL KLGVSTHDSA ELAVALAADP DYVALGPVWQ TKLKVMKWAP QTPERLGVWR QRIGDLPLVA IGGITVERLP QVFAQGADSA AVVTDVTRAA DPEARAREWL AATAPYRR // ID Q1YK22_MOBAS Unreviewed; 217 AA. AC Q1YK22; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 37. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; GN ORFNames=SI859A1_00824; OS Manganese-oxidizing bacterium (strain SI85-9A1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Aurantimonas. OX NCBI_TaxID=287752; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SI85-9A1; RX PubMed=18344346; DOI=10.1128/AEM.01656-07; RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., RA Bernier-Latmani R., McCarthy J.K., Torpey J.W., Clement B.G., RA Gaasterland T., Tebo B.M.; RT "Genomic insights into Mn(II) oxidation by the marine RT alphaproteobacterium Aurantimonas sp. strain SI85-9A1."; RL Appl. Environ. Microbiol. 74:2646-2658(2008). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPJ01000002; EAS50701.1; -; Genomic_DNA. DR ProteinModelPortal; Q1YK22; -. DR EnsemblBacteria; EAS50701; EAS50701; SI859A1_00824. DR PATRIC; 24558766; VBIAurMan112117_1555. DR BioCyc; AURANTIMONAS:SI859A1_00824-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 217 AA; 22539 MW; DE477192F00448CF CRC64; MDTEYIRPRL VLLTTPLGDA DAVTAMQAAL AGGDVASVIL DPAGRDAVSF QNLAEKLVPI IQAAGAAAIV ADDTQCAGRV QADGIHLTSG DPGELGEAME RFAPKLIVGA SGFETRHDAL EAGELRPDYL LFGRFGGDVD PNPHPKSIAM GEWWAEIVEL PCIVLAGSDI ESVVEAAATR AEFIALSAAV FAQPDAAGEM VARANALIDA WFESAAA // ID Q1YXG2_PHOPR Unreviewed; 204 AA. AC Q1YXG2; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=P3TCK_00960; OS Photobacterium profundum 3TCK. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=314280; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3TCK; RA Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E., RA Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., RA Kravitz S., Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPH01000043; EAS40982.1; -; Genomic_DNA. DR ProteinModelPortal; Q1YXG2; -. DR EnsemblBacteria; EAS40982; EAS40982; P3TCK_00960. DR PATRIC; 30922379; VBIPhoPro77067_5079. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22136 MW; D3EC4CB11D4F924D CRC64; MNKYRLYLVT DEHQDIEALT FVIKEAIAGG VTMVQIREKH GDIRAFIQRA MVIKALLLNT GIPLIINDRI DVALAVDADG VHLGQSDMPA DIARRLIGPN KILGLSVENE TQLEHAQSLP IDYLGISAIF PTPTKTDTVY TWRIDGLSKA VKSSKLPLVA IGGINKENIQ TVAQTHVAGI ALVSAICHAQ SPKIACEELN QLIG // ID Q1Z2C2_PHOPR Unreviewed; 423 AA. AC Q1Z2C2; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=P3TCK_22750; OS Photobacterium profundum 3TCK. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=314280; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3TCK; RA Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E., RA Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., RA Kravitz S., Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPH01000017; EAS42770.1; -; Genomic_DNA. DR ProteinModelPortal; Q1Z2C2; -. DR EnsemblBacteria; EAS42770; EAS42770; P3TCK_22750. DR PATRIC; 30921552; VBIPhoPro77067_4682. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 423 AA; 46581 MW; 9B1F4A239DC65D5E CRC64; MSSLCLPDHL TPLLMHVEPL LANADQYQLG NAVSVSVSES GVVDIKIEER QLSLVFNQAE AGFAGLKVLD QWYAPYPCVR EMQLKVEQDS RLVVCGLPTE NGCVDIWHHN GEARAVYCHH AGAGEPQRAM LLCALALDYP LEDAVTLARA HARGYQSSHQ DGHGEVSWPV SRELFPCPLT ANHPEVDVLG WQSKEVAVKP FSATDALQLA LYPVVDTAEW VERLLDLGVK TTQLRIKNPQ DPQLETQVQQ IIAAGNQYKA QVFVNDYWQL AIKHQAYGVH LGQEDLETAD LVAIQQAGLR IGLSTHGYYE ILRAAEFSPS YIALGHIFPT TTKEMPSKPQ GLNRLALYQK LIGDTFPTVA IGGIDLPRAE KVWRTGVSSV AVVRAITEAS DPAVAVNAFN QLLVRPEFPE VINETITDRI DAD // ID Q1ZLD3_PHOAS Unreviewed; 405 AA. AC Q1ZLD3; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 19-FEB-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=VAS14_22709; OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain OS S14 / CCUG 15956)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=314292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S14; RX PubMed=19805210; DOI=10.1073/pnas.0903507106; RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S., RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A., RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V., RA Robb F.T., Kjelleberg S., Cavicchioli R.; RT "The genomic basis of trophic strategy in marine bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOJ01000012; EAS62904.1; -; Genomic_DNA. DR ProteinModelPortal; Q1ZLD3; -. DR EnsemblBacteria; EAS62904; EAS62904; VAS14_22709. DR PATRIC; 31353107; VBIPhoAng36222_4134. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 405 AA; 44711 MW; 6B11C510CCAC3EBB CRC64; MSTLSLPKVL SSLVMHIEPL LASAAEYQLG EQVTLMPSSQ EWIEVSTPSC VKRVGFEQAC STQQIDYVFQ DQWVSSEVDL SLIKAQILKR SNVVVCGLPV NGGYLDLWHH DGDVRGCFSV ELGNATQQRA MLLVALALDY PLEDALVLAR AYAKSTQMGI WPTERDAFPD IVCANFSKLS DIGWQFECQP VEAFAPVDSE KLTLYPVVDS VQWVKQLLKL DVKTTQLRIK DPNAQGLEQD VAHAIALGQQ ANAQVFINDY WQLAIEHGAF GVHLGQEDLA VADLNAIQQA NLRLGISTHG YYEILRAMAF NPSYIALGHI YPTTTKQMPS LPQGVHRLKL YQQLIGNTFP TVAIGGIDLS RVPVVWKTGV SSVAVVRAIT QSSEPAIAVE QLNQCLSERE VMYDN // ID Q20X40_RHOPB Unreviewed; 230 AA. AC Q20X40; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 14-MAY-2014, entry version 50. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=RPC_4774; OS Rhodopseudomonas palustris (strain BisB18). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisB18; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., RA Anderson I., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisB18."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000301; ABD90296.1; -; Genomic_DNA. DR RefSeq; YP_534615.1; NC_007925.1. DR ProteinModelPortal; Q20X40; -. DR STRING; 316056.RPC_4774; -. DR EnsemblBacteria; ABD90296; ABD90296; RPC_4774. DR GeneID; 3972977; -. DR KEGG; rpc:RPC_4774; -. DR PATRIC; 23274444; VBIRhoPal29154_4885. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RPAL316056:GH3E-4845-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 230 AA; 23792 MW; 19364AD9BFE2B1EF CRC64; MAAKPAPPPP APRLYLATAM LDDVAALAAT LPGLIATHQV AALLLRLKLT DQRGMISRAK TLAPAVQNAG AALLLDGHPE LVARSGADGA HLTGVEAMQE HLPELQPDRI AGVGGLRTRH DSMLAGEAGA DYVLFGEPDA DGQRPAQDAI AERLQWWAEL FEPPCVGYAA TLAEAQDFAA AGADFVLVGD MIWDDPRGAD AALGDARAAI AQGYQSLLAS LAGPAKVGQQ // ID Q216G9_RHOPB Unreviewed; 202 AA. AC Q216G9; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=RPC_2163; OS Rhodopseudomonas palustris (strain BisB18). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisB18; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., RA Anderson I., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisB18."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000301; ABD87717.1; -; Genomic_DNA. DR RefSeq; YP_532036.1; NC_007925.1. DR ProteinModelPortal; Q216G9; -. DR STRING; 316056.RPC_2163; -. DR EnsemblBacteria; ABD87717; ABD87717; RPC_2163. DR GeneID; 3971984; -. DR KEGG; rpc:RPC_2163; -. DR PATRIC; 23269036; VBIRhoPal29154_2217. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; RPAL316056:GH3E-2188-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 202 AA; 21852 MW; 8CA08234A42E1E50 CRC64; MPYPDRFYPV VDSLAWVARL TAQGVGTLQL RVKELDDAQS LQLVTDALAL VKNTTTRLVI NDYWRAAIVA GAQHLHLGQE DLADADLGEI RKAGLTLGLS THDDAELETA LKAEPDYIAL GPIFPTTLKS MRFAPQGVPK LRDWKKRVGN IPLVAIGGIK LEQADEIFAA GADSIAVVSD VTQNPDPDAR VRAWLDYVAA AG // ID Q21MF9_SACD2 Unreviewed; 317 AA. AC Q21MF9; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 14-MAY-2014, entry version 66. DE SubName: Full=Mutator mutT protein; GN OrderedLocusNames=Sde_0858; OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Saccharophagus. OX NCBI_TaxID=203122; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2-40 / ATCC 43961 / DSM 17024; RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087; RA Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M., RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., RA Lamed R., Richardson P.M., Borovok I., Hutcheson S.; RT "Complete genome sequence of the complex carbohydrate-degrading marine RT bacterium, Saccharophagus degradans strain 2-40 T."; RL PLoS Genet. 4:E1000087-E1000087(2008). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000282; ABD80120.1; -; Genomic_DNA. DR RefSeq; YP_526332.1; NC_007912.1. DR ProteinModelPortal; Q21MF9; -. DR STRING; 203122.Sde_0858; -. DR EnsemblBacteria; ABD80120; ABD80120; Sde_0858. DR GeneID; 3965207; -. DR KEGG; sde:Sde_0858; -. DR PATRIC; 23400483; VBISacDeg56404_0945. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SDEG203122:GI2M-864-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 317 AA; 34005 MW; C94DD52F722F8CFA CRC64; MGVIKDASDN ILIAKRPEHV HMGGRWEFPG GKVERNESVA AALARELHEE LGIDITGDSR ITPLITIRHQ YADKTVLLDV RIVEQFGGEP TGKEGQPLRW VPVASLQDYT FPDANYPIIS ALQLPRILPI SPAFLSLADC DALSEFYVQQ RYTLWHMRSP NCEREVFIKA INRAVESVGV EVGITVNASV AEYERVNALH LHLNSAQLLS LKARPQLRSG GLLSASCHNL EELNAAHKLG VEYVLFSPVN ATASHPSANA AGWSALQAFC AAARVPVYAL GGVGECDVGK AIACGAQGVA GISAFSPLAN IGIGQGV // ID Q21VL9_RHOFD Unreviewed; 312 AA. AC Q21VL9; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Rfer_2467; OS Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Albidiferax. OX NCBI_TaxID=338969; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15236 / ATCC BAA-621 / T118; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM RT 15236."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000267; ABD70184.1; -; Genomic_DNA. DR RefSeq; YP_523715.1; NC_007908.1. DR ProteinModelPortal; Q21VL9; -. DR STRING; 338969.Rfer_2467; -. DR EnsemblBacteria; ABD70184; ABD70184; Rfer_2467. DR GeneID; 3960282; -. DR KEGG; rfr:Rfer_2467; -. DR PATRIC; 23237631; VBIRhoFer131161_2818. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RFKSEDR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; AFER338969:GHU9-2495-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 312 AA; 33313 MW; 5E2712EF0A40B445 CRC64; MSQHDSMVQT IVTAHADLAL APGAGTSQRA ATATFTCDAA AYRAAKSACL ALGFIEADAE CVALAWQNQT DRTGHFDVTV WPDQPEDFSM QAWPRPTAFA ACPRQLGLYA VLPDAVWVGR MARAGVSTVQ LRFKSDDTVV IAREVRAAVM AVKGTNARLF INDHWQAAID AGAYGVHLGQ EDMVEADLEK IRAAGLRLGL SSHGYAEMLR ADHYSPSYIA MGAVFATTLK RMLTPPQGLA RLGAYARLMR DYPKVAIGGI DASKLLDVLN CGVGSIAVVR ALVAAENPEV MANSLQAKIN DRLSAMAPEP AL // ID Q253G2_CHLFF Unreviewed; 242 AA. AC Q253G2; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CF0804; OS Chlamydophila felis (strain Fe/C-56). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydophila. OX NCBI_TaxID=264202; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fe/C-56; RX PubMed=16766509; DOI=10.1093/dnares/dsi027; RA Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H., RA Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., RA Fukushi H., Hattori M., Kuhara S., Shirai M.; RT "Genome sequence of the cat pathogen, Chlamydophila felis."; RL DNA Res. 13:15-23(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006861; BAE81576.1; -; Genomic_DNA. DR RefSeq; YP_515721.1; NC_007899.1. DR ProteinModelPortal; Q253G2; -. DR STRING; 264202.CF0804; -. DR GeneID; 3959098; -. DR KEGG; cfe:CF0804; -. DR PATRIC; 20205283; VBIChlFel51660_0845. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CFEL264202:GJCG-831-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 68 72 HMP-PP binding (By similarity). FT METAL 101 101 Magnesium (By similarity). FT METAL 120 120 Magnesium (By similarity). FT BINDING 168 168 HMP-PP (By similarity). FT BINDING 196 196 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 242 AA; 26229 MW; D760C966A78A6956 CRC64; MAVVFILKGF FKSILISLLL RKRVICRGTP LEEDFFKLIL ITDRKNIPVD EYVDFVVACV HSGVTAVQLR EKELSHREIL GFGEALKSVL DPLEIPLIIS DSVAVCMDLD ASGVHLGQTD GDVIEARELI GPDKIIGWNV NTLEQLLTAN TLPIDYLGLS AMFETQNKPE AAHLWGFSGL EQAVSLCEHP IVAVGGIDES NASDVIEAGA AGIAAIGVFH TANNPSLVTK SLREIVDRGL RC // ID Q26DP7_FLABB Unreviewed; 211 AA. AC Q26DP7; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 19-FEB-2014, entry version 37. DE SubName: Full=Uncharacterized protein; GN ORFNames=BBFL7_00277; OS Flavobacteria bacterium (strain BBFL7). OC Bacteria; Bacteroidetes; Flavobacteriia. OX NCBI_TaxID=156586; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BBFL7; RA Azam F., Beardsley C., Gaasterland T., Malfatti F., Mayali X., RA Podell S., Samo T., Smriga S., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPD01000003; EAS19731.1; -; Genomic_DNA. DR ProteinModelPortal; Q26DP7; -. DR EnsemblBacteria; EAS19731; EAS19731; BBFL7_00277. DR PATRIC; 27385534; VBIFlaBac90662_0306. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 211 AA; 23597 MW; 3EF615DAABF2028E CRC64; MIPKLHYISQ GATASIHLEN VQKACSSGVE LIQLDLQHIP ENKRLTLATE VLKITTHFQT RLIIRSFYKI AYDLKIDGVY LLPIDSNPSH VRKQLYSWQS IGAMAHHITD CEKLLHNDVD YIVLGPFKST TDPVTSPLDL TAYSVIRDSL KTETPLLAYG DIHTADVKAI LETGISGLVV SQAINDNFNH IKTFNQLLGA SSTDEMRHSF K // ID Q28PL1_JANSC Unreviewed; 209 AA. AC Q28PL1; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 14-MAY-2014, entry version 52. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Jann_2434; OS Jannaschia sp. (strain CCS1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Jannaschia. OX NCBI_TaxID=290400; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCS1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E., RA Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., RA Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.; RT "Complete sequence of chromosome of Jannaschia sp. CCS1."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000264; ABD55351.1; -; Genomic_DNA. DR RefSeq; YP_510376.1; NC_007802.1. DR ProteinModelPortal; Q28PL1; -. DR STRING; 290400.Jann_2434; -. DR EnsemblBacteria; ABD55351; ABD55351; Jann_2434. DR GeneID; 3934891; -. DR KEGG; jan:Jann_2434; -. DR PATRIC; 22148646; VBIJanSp43325_2586. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; JSP290400:GI1R-2455-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 209 AA; 22239 MW; C0FCC6011F5FF1E1 CRC64; MDDATAPETP QLYLITPTAF EPEVFAPHLA TVLDAVDIAC IRLALVTEDE AALSRAADQC RDVAHARDVP LVIDRHIQLV ERLGLDGVHL TDGARSVRDT RKALGADAII GAYCGNSRHD GMSAGEAGAD YVSFGPVGEN ALGDGTRAEH DLFAWWSQMI EVPVVAEGAL DAALVETFAP VTDFFAIGPE IWRHDDPLAA LQGVTASIL // ID Q2B0F4_9BACI Unreviewed; 221 AA. AC Q2B0F4; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 16-OCT-2013, entry version 34. DE SubName: Full=Transcriptional regulator TenI; GN ORFNames=B14911_17885; OS Bacillus sp. NRRL B-14911. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=313627; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL B-14911; RA Siefert J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOX01000061; EAR63309.1; -; Genomic_DNA. DR ProteinModelPortal; Q2B0F4; -. DR EnsemblBacteria; EAR63309; EAR63309; B14911_17885. DR PATRIC; 36906456; VBIBacSp102338_0417. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 221 AA; 23869 MW; BA8EFE8421A7E6CD CRC64; MVFLRRLQGW PSRDKLQLHA ISAGQPAEEF IRIASSISRN VDYIHIREHH LIAADIYEMG RILLEKGVPG EQIIINNRVD AAAALGVKGV QLGYHSLPVR EVRITFPGLL IGKSVHSIEE AVQAEEDGAD YVMYGHCFPT SSKPGMEPRG LSSLEEMTGR LSIPVIALGG ISPDNMEQVI RAGASGAAVL SGIFKAVSPE EAAGAYRVAL NRGGGRYEES L // ID Q2BDM6_9BACI Unreviewed; 209 AA. AC Q2BDM6; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 19-FEB-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=B14911_27225; OS Bacillus sp. NRRL B-14911. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=313627; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL B-14911; RA Siefert J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOX01000002; EAR68422.1; -; Genomic_DNA. DR ProteinModelPortal; Q2BDM6; -. DR EnsemblBacteria; EAR68422; EAR68422; B14911_27225. DR PATRIC; 36909105; VBIBacSp102338_1737. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22124 MW; 3FDC617B393D8E37 CRC64; MKELLKVYFI MGSTNCTKNP DMVMKEAIKG GISLFQYREK GAGCLGRQEK YVLAEQLQRM CRTGGIPFII NDDIELACEI GADGVHIGQE DEPAEAVREK IGDKILGVSA HTLVEANEAV RAGADYLGLG PIYPTSTKAD AKAIQGMALI QELRESAITI PVVGIGGITP HNARAVILAG ADGVSVITSI SQAADIKEAA ASLKRSVTI // ID Q2BGF1_NEPCE Unreviewed; 320 AA. AC Q2BGF1; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 19-FEB-2014, entry version 50. DE SubName: Full=Probable pyrophosphohydrolase; GN ORFNames=MED92_15770; OS Neptuniibacter caesariensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Neptuniibacter. OX NCBI_TaxID=207954; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED92; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOW01000046; EAR59533.1; -; Genomic_DNA. DR ProteinModelPortal; Q2BGF1; -. DR EnsemblBacteria; EAR59533; EAR59533; MED92_15770. DR PATRIC; 25471516; VBINepCae91145_0944. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 320 AA; 34676 MW; E7C83F5B15F70585 CRC64; MTRKLIHVAA AVIRNDAGEI FIAKRSDDKH QGGLWEFPGG KVEAGEPVKQ ALARELDEEL GIQVLDCRPL IQIPHHYSDK SVLLDVFEVG TFSGEPYGRE GQPVKWVSNT ELVSYEFPEA NRPIIDACLL PSTLAITPFN TKPDELLSFA ESAVAKGAGG IVLRFSGLSD QSETLSAEVE VACRSLIGYC HEKSIFLSLN TSVSIANHLA ADAIHLSSER LKSLSQRSDF AGRWLSVSCH NAAELKIAEE KGSNFVFLSP VTETTSHPDE ESLGWESFSA LLTEVKQPVY ALGGVGPDDV NQAQIFGAQG IAAISAWLEE // ID Q2BHE1_NEPCE Unreviewed; 211 AA. AC Q2BHE1; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 19-FEB-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=MED92_17460; OS Neptuniibacter caesariensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Neptuniibacter. OX NCBI_TaxID=207954; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED92; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOW01000030; EAR59853.1; -; Genomic_DNA. DR ProteinModelPortal; Q2BHE1; -. DR EnsemblBacteria; EAR59853; EAR59853; MED92_17460. DR PATRIC; 25472210; VBINepCae91145_1282. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22443 MW; 51CCB392D89D28CC CRC64; MQYQLQGLYG ITDAELMPST EVMLKKVEQS IKGGAKIIQY RDKSSDLQKR VEQASAVNHL CQNHKIPLLI NDDAGLAAGI GAAGVHLGQS DGAIPEAREM LGEQAIIGVT CHDSLAFALQ AAAEGADYIA FGAFFPSKTK PNATPAPLEL LMQAKHEVNL PIVAIGGISV DNAAQIIDAG ADMVAVIHAL YAQNNIKATA QQFHQQFSNR I // ID Q2C2T2_9GAMM Unreviewed; 405 AA. AC Q2C2T2; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 19-FEB-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=SKA34_00375; OS Photobacterium sp. SKA34. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=121723; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SKA34; RA Hagstrom A.J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOU01000019; EAR55258.1; -; Genomic_DNA. DR EnsemblBacteria; EAR55258; EAR55258; SKA34_00375. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 405 AA; 44861 MW; 8075E6C5DCBABDB3 CRC64; MSTLSLPKVL SSLVMHIEPL LASAAEYQLG EQVTLIPSSQ AWIEVSTPSC VKRVGFENAC STQLIDYVLQ DQWVSSDVDL SLIKAQILKR TNVVVCGLPV NGGYLDLWYH DGEVRGCFSV ERGNATQQRA MLLVALALDY PLEDALVLAR AYAQSTQMGI WPTERDAFPE IVCANFSKLS DIGWQFEYQP VEAFAPVDSE KLKLYPVVDS IQWVKQLLEL DVKTTQLRIK DPNAQSLEQD IAHAIVLGLQ ANAQVFINDY WQLAIEHGAF GVHLGQEDLA VADLNAIQQA NLRLGISTHG YYEILRAMTF SPSYIALGHI YPTTTKQMPS LPQGVHRLKL YQRLVGNTFP TVAIGGIDLS RVPVVWKTGV SSVAVVRAIT QSSELAIAVE QLNQCLSERE VMYDN // ID Q2CAR0_9RHOB Unreviewed; 208 AA. AC Q2CAR0; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 19-FEB-2014, entry version 33. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=OG2516_04753; OS Oceanicola granulosus HTCC2516. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Oceanicola. OX NCBI_TaxID=314256; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2516; RX PubMed=20418400; DOI=10.1128/JB.00412-10; RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.; RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola RT batsensis HTCC2597(TDelta)."; RL J. Bacteriol. 192:3549-3550(2010). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOT01000048; EAR49778.1; -; Genomic_DNA. DR ProteinModelPortal; Q2CAR0; -. DR EnsemblBacteria; EAR49778; EAR49778; OG2516_04753. DR PATRIC; 28498528; VBIOceGra115923_0415. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 208 AA; 22265 MW; 9F364CCD4D062D70 CRC64; MTDASGDIPQ IYLISPPDFD LSGFPDRLAA CLDRVPVGCV RLALASHDED RICRAADALR EVTHARDVAL VIDNHALLVE RLGLDGVHLT DGARSVRTMR KSLDADAIVG AFCATSRHDG MSAAEAGADY VSFGPVGGMT LGDGRRAELD TFQWWSEMIE VPVVAEGALD AELVRSLAPH TDFLGLGEEI WRTDDPAETL AGLVAALR // ID Q2G6X1_NOVAD Unreviewed; 213 AA. AC Q2G6X1; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Saro_1962; OS Novosphingobium aromaticivorans (strain DSM 12444 / F199). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=279238; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12444; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.; RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000248; ABD26402.1; -; Genomic_DNA. DR RefSeq; YP_497236.1; NC_007794.1. DR ProteinModelPortal; Q2G6X1; -. DR STRING; 279238.Saro_1962; -. DR EnsemblBacteria; ABD26402; ABD26402; Saro_1962. DR GeneID; 3917278; -. DR KEGG; nar:Saro_1962; -. DR PATRIC; 22786638; VBINovAro50627_2010. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NARO279238:GHBU-1994-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22953 MW; 565D4F7B59C88958 CRC64; MAKLSSELYL ISPLDVEGTF PERLERALDA GPVAAFQFRV KDVDEHSAAR MAEPLQRICA DRDVAFIVND SISLAKRLGA DGVHLGQKDG DVKDARERLG RNAQIGVTCH DSRHLAMDAG EAGADYVAFG AFFPSSTKET KHVAGLDLLE WWQSIFELPC VAIGGITPAN CAPLIRAGAD FLAVSNAVWD GDEAANVAAF FDAIRANPRI TEQ // ID Q2GB91_NOVAD Unreviewed; 178 AA. AC Q2GB91; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 53. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Saro_0434; OS Novosphingobium aromaticivorans (strain DSM 12444 / F199). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=279238; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12444; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.; RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000248; ABD24882.1; -; Genomic_DNA. DR RefSeq; YP_495716.1; NC_007794.1. DR ProteinModelPortal; Q2GB91; -. DR STRING; 279238.Saro_0434; -. DR EnsemblBacteria; ABD24882; ABD24882; Saro_0434. DR GeneID; 3917580; -. DR KEGG; nar:Saro_0434; -. DR PATRIC; 22783472; VBINovAro50627_0449. DR eggNOG; NOG121918; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NRRDSIM; -. DR OrthoDB; EOG679THR; -. DR BioCyc; NARO279238:GHBU-439-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 178 AA; 19065 MW; 0E7496090BE6D6FB CRC64; MAKRQTIQRA RAPHLILLSD ARNDAALARA IARLPRGSAL VFRHYHLPAH ERRRRFAELR RLARARGISM IGARVPTAWG GEGVYGTARE VAGRRGIRLA TAHSLGEVAA AARAGADAVL LSPVHPTRSH PGAPVLGPVR FLLLARRSPL PVIALGGMTA RRAARLPVHG WAAIDGLA // ID Q2GE59_NEOSM Unreviewed; 193 AA. AC Q2GE59; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=NSE_0348; OS Neorickettsia sennetsu (strain Miyayama). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Neorickettsia. OX NCBI_TaxID=222891; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Miyayama; RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., RA Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., RA Nelson W., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., RA Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M., Haft D.H., RA Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., RA Forberger H., Halpin R., Mulligan S., Robinson J., White O., RA Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000237; ABD46051.1; -; Genomic_DNA. DR RefSeq; YP_506237.1; NC_007798.1. DR ProteinModelPortal; Q2GE59; -. DR STRING; 222891.NSE_0348; -. DR EnsemblBacteria; ABD46051; ABD46051; NSE_0348. DR GeneID; 3932196; -. DR KEGG; nse:NSE_0348; -. DR PATRIC; 22680783; VBINeoSen119815_0323. DR eggNOG; NOG323178; -. DR HOGENOM; HOG000127309; -. DR OMA; TTRANIW; -. DR OrthoDB; EOG679THR; -. DR BioCyc; NSEN222891:GHFU-349-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 193 AA; 22502 MW; FBA9E3682470DA56 CRC64; MMFFKRRAHL FRWLFVIDVV PSLSEIVFVL KQLPLGSLVV LRCYEHLQRK NLAHWLSRMC RKLRLIFLVA GDPFIALVTR ASGLHVREST FSKMRKWRYF KKRWFISCAS HSVKQNLKIQ AAGFDAALFS PVFRSKKTNF KAMGATKFLK YQAFTRKIGV FALGGTTRAN IWKLREARQK VGIAGINLYN DRL // ID Q2GEI1_NEOSM Unreviewed; 214 AA. AC Q2GEI1; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 57. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=NSE_0220; OS Neorickettsia sennetsu (strain Miyayama). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Neorickettsia. OX NCBI_TaxID=222891; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Miyayama; RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., RA Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., RA Nelson W., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., RA Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M., Haft D.H., RA Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., RA Forberger H., Halpin R., Mulligan S., Robinson J., White O., RA Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000237; ABD46427.1; -; Genomic_DNA. DR RefSeq; YP_506115.1; NC_007798.1. DR ProteinModelPortal; Q2GEI1; -. DR STRING; 222891.NSE_0220; -. DR EnsemblBacteria; ABD46427; ABD46427; NSE_0220. DR GeneID; 3931586; -. DR KEGG; nse:NSE_0220; -. DR PATRIC; 22680539; VBINeoSen119815_0207. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CIGGINE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NSEN222891:GHFU-221-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 24444 MW; 8A8033300246AB92 CRC64; MQLSKAFYIL SPNRQITTAE YADLARLFRN FSTYVYAFQL RIKDRNLLER EIPRLSDLCH EYKIPLIVND FIDLALRFEA DGVHVGVADN TLEQCRHLLP SGKIVGVSCY NDIDRAKKNL FADYVSFGCF FESQTKPNPA AKASLATLNN WKNIAPRVPC VCIGGINEKN FVQLLRNGAD IVAFSSYLWR GESPYGKFAA LIETSRHYET YRNK // ID Q2GFU5_EHRCR Unreviewed; 244 AA. AC Q2GFU5; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 68. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ECH_0893; OS Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=205920; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC CRL-10679 / Arkansas; RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., RA Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., RA Nelson W., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., RA Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M., Haft D.H., RA Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., RA Forberger H., Halpin R., Mulligan S., Robinson J., White O., RA Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(2006). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000236; ABD44828.1; -; Genomic_DNA. DR RefSeq; YP_507688.1; NC_007799.1. DR ProteinModelPortal; Q2GFU5; -. DR STRING; 205920.ECH_0893; -. DR EnsemblBacteria; ABD44828; ABD44828; ECH_0893. DR GeneID; 3927772; -. DR KEGG; ech:ECH_0893; -. DR PATRIC; 20577186; VBIEhrCha103583_0775. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; YKAYGVH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECHA205920:GJNR-896-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 244 AA; 27850 MW; 5FB7D3638F72F830 CRC64; MQKDALIIAR ASANQSVEDA SFLDERYFPI ITLNKDYYFD KNFHPMLDPV GFYQIVPDLF WLKYVINLGV KVVQLRIKNE PIEEVEYKIK EGVHIANQNG VKLFVNDYWQ FAVKYKAYGV HLGQEDLRSA NFNEIYNAGL RLGISTHCYH ELAIAKYIRP SYIAFGPIFP TTLKNMNFMP QGTDLLNYWV KNLPYKIVAI GGINLSNVDS VIGTGVDGIA VISAVLNSEY PDKVVHEFIQ KCQI // ID Q2GJC3_ANAPZ Unreviewed; 200 AA. AC Q2GJC3; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=APH_0960; OS Anaplasma phagocytophilum (strain HZ). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Anaplasma; phagocytophilum group. OX NCBI_TaxID=212042; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HZ; RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., RA Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., RA Nelson W., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., RA Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M., Haft D.H., RA Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., RA Forberger H., Halpin R., Mulligan S., Robinson J., White O., RA Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000235; ABD44213.1; -; Genomic_DNA. DR RefSeq; YP_505528.1; NC_007797.1. DR ProteinModelPortal; Q2GJC3; -. DR STRING; 212042.APH_0960; -. DR EnsemblBacteria; ABD44213; ABD44213; APH_0960. DR GeneID; 3930631; -. DR KEGG; aph:APH_0960; -. DR PATRIC; 20950638; VBIAnaPha602_1025. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; APHA212042:GHPM-960-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 125 127 THZ-P binding (By similarity). FT REGION 176 177 THZ-P binding (By similarity). FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 156 156 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 200 AA; 22164 MW; 9EC762079384E769 CRC64; MDDIGFYLIV PDAHWFEFAA SCGVRTIQLR AKDKPVSEVE NMVKRCSEIA VRYGVRFIVN DYWELALKYN AYGIHLGQED IKTADLYRIS SSGIRLGIST HCYHEFARAS FYKPSYIALG PIYDTTSKSM QFHAQGLELL KQWVKSSSCP VVAIGGITLA NIDDVVRCNA GGVAVISAVT EAADPKDAIR RFLDKCSVGV // ID Q2HA73_CHAGB Unreviewed; 484 AA. AC Q2HA73; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 16-APR-2014, entry version 39. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=CHGG_02881; OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC OS 6347 / NRRL 1970) (Soil fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae; OC Chaetomium. OX NCBI_TaxID=306901; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970; RG The Broad Institute Genome Sequencing Platform; RA Birren B.W., Lander E.S., Galagan J.E., Devon K., Nusbaum C., RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., RA Engels R., Montgomery P., Pearson M., Howarth C., Kodira C.D., RA Yandava C., Zeng Q., Alvarado L., Oleary S., Untereiner W.; RT "Annotation of the Chaetomium globosum CBS 148.51 genome."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH408030; EAQ90946.1; -; Genomic_DNA. DR RefSeq; XP_001229397.1; XM_001229396.1. DR ProteinModelPortal; Q2HA73; -. DR PRIDE; Q2HA73; -. DR GeneID; 4389218; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 2. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 484 AA; 51167 MW; 7D7E4259CCC33378 CRC64; MGKPEVDYGL YLVTDSTPAI LGDRNLNEVV EASLKGGVTI VQLREKKGDT AELIAKAKAL HEITKRYNVP LLINDRVDVA LAVDCEGIHI GQDDMDLSTA RKLLGPDKII GVTASTVDEA LKACEGGADY LGIGTVYATP TKTNTKEIIG AAGVREILGK IADAGHKTQT VCIGGVNESN LQRIVFQCAA AYKRLDGVAI VSAIMAAQDP ESAAKKLLAL VRSPPAFQAD TRGKDSDVAD VKTVVDLAPS VLQRVHETTP LSHNMTNIVV QNIAANVALA IGASPIMAGY GEEAPDLCKL GGALVINMGS VDPNGLTNYL KALKAYNLEG RPVVFDPVGQ EQQRGVDSSS TLDASQKAQL VRELAAREKN VVVMTGKTDF VSDGVRTFAI DNGHEYLGMV TGTGCTLGTT ISAAIASRTT NRLVAVIAAI LHFEIAAEIA ASRPEVRGPG SFVPAFLDEL YLIRQATASK ELSWLERAKV RSVV // ID Q2IKV3_ANADE Unreviewed; 203 AA. AC Q2IKV3; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Adeh_2516; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=290397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-C; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000251; ABC82286.1; -; Genomic_DNA. DR RefSeq; YP_465723.1; NC_007760.1. DR ProteinModelPortal; Q2IKV3; -. DR STRING; 290397.Adeh_2516; -. DR EnsemblBacteria; ABC82286; ABC82286; Adeh_2516. DR GeneID; 3889904; -. DR KEGG; ade:Adeh_2516; -. DR PATRIC; 20921207; VBIAnaDeh31384_2581. DR eggNOG; NOG270906; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ADEH290397:GI2Z-2547-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 134 136 THZ-P binding (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 20539 MW; 1989B8FCBE45AF1A CRC64; MEVPVVHLIT DRRLASSLPA RAAAALRGLP PGIAAIHLRE KDLCGLDLLR LARALAAVCR DAGQRLIVND RLDVALAAGA DGAHLPSAGV SPADARRLLG PAALLGVSCH SEADVLRARE GGAGFATFGP VYDTPSKRPY GAPVGVGALR AAARLGLPLV ALGGVDPSRV PELRAAGAHG VAAIRAWLIG DDPAGAVRAL LGP // ID Q2IRK5_RHOP2 Unreviewed; 223 AA. AC Q2IRK5; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=RPB_4472; OS Rhodopseudomonas palustris (strain HaA2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316058; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HaA2; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A., RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris HaA2."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000250; ABD09155.1; -; Genomic_DNA. DR RefSeq; YP_488066.1; NC_007778.1. DR ProteinModelPortal; Q2IRK5; -. DR STRING; 316058.RPB_4472; -. DR EnsemblBacteria; ABD09155; ABD09155; RPB_4472. DR GeneID; 3912288; -. DR KEGG; rpb:RPB_4472; -. DR PATRIC; 23303825; VBIRhoPal125544_4672. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RPAL316058:GHF1-4530-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 223 AA; 22712 MW; AFB81F10F9B0E2A5 CRC64; MAKPAPPRPA PRLYLATPVV DDPAQLLAAL PHLLAAADVA AVLLRLAPSD PRTLITRIKA VTAVAQAGGA ALLLDGHADL VARGGADGAH LSGLAAMQEW LPQLQPQRIA GVGALETRHD SMVAGEAGAD YVLFGEPAAD GTRPSTEAIA DRLNWWAELF EPPCVGYAIS RDEVGEFAAA GADFVLVGDH IWAEADGAAA ALADAEAALK QGFAGTAPAP AQG // ID Q2IYP7_RHOP2 Unreviewed; 202 AA. AC Q2IYP7; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 69. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=RPB_1955; OS Rhodopseudomonas palustris (strain HaA2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316058; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HaA2; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A., RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris HaA2."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000250; ABD06663.1; -; Genomic_DNA. DR RefSeq; YP_485574.1; NC_007778.1. DR ProteinModelPortal; Q2IYP7; -. DR STRING; 316058.RPB_1955; -. DR EnsemblBacteria; ABD06663; ABD06663; RPB_1955. DR GeneID; 3908034; -. DR KEGG; rpb:RPB_1955; -. DR PATRIC; 23298515; VBIRhoPal125544_2051. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; RPAL316058:GHF1-1975-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 202 AA; 21675 MW; D28B34BDEF1F7FA9 CRC64; MPYPDRFYPV VDSIAWVKRL AALGVGTVQL RAKDLDDGAA LQLVTDALDA VKGTSVRLII NDYWRAAIVA GAQHLHLGQE DLATADLHEI RAAGLTLGLS THDDAELETA LAARPDYIAL GPIFPTTLKS MRFAPQGIPK ITDWKQRVGS IPLVAIGGIK LEQAEEIFAA GADSIAVVSD VTQNPDPDAR VRAWLDFVAE TA // ID Q2J8G5_FRASC Unreviewed; 237 AA. AC Q2J8G5; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Francci3_3070; OS Frankia sp. (strain CcI3). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=106370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CcI3; RX PubMed=17151343; DOI=10.1101/gr.5798407; RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., RA Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N., RA Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L., RA Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E., RA Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z., RA Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D., RA Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.; RT "Genome characteristics of facultatively symbiotic Frankia sp. strains RT reflect host range and host plant biogeography."; RL Genome Res. 17:7-15(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000249; ABD12427.1; -; Genomic_DNA. DR RefSeq; YP_482156.1; NC_007777.1. DR ProteinModelPortal; Q2J8G5; -. DR STRING; 106370.Francci3_3070; -. DR EnsemblBacteria; ABD12427; ABD12427; Francci3_3070. DR GeneID; 3904271; -. DR KEGG; fra:Francci3_3070; -. DR PATRIC; 21929434; VBIFraSp10456_3332. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CVGPVHA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; FSP106370:GI1F-3106-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 158 160 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 161 161 HMP-PP (By similarity). FT BINDING 194 194 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 237 AA; 24852 MW; C8148E00BB266963 CRC64; MLSPEVEGSS PRAGGPARAD RLRRLADARL YLCTPRRAEF DAFLSAVVGT PEAPGVDLIQ LREKGLEWDE ELGGLRRVQA AAGARGVLVS ANDRADLAAF AGVDILHVGQ GDIPPRFARR LVGPDVLIGQ STHDPDQFLA ALADPDVDYV CVGPVHATPT KEGRPPVGLG LPRLAARHAP PFAPGVKPWF VTGGVGPDTL DQILATGARR VVVVRGLTGV EDPAASAVAL AQRLRAV // ID Q2JKL8_SYNJB Unreviewed; 348 AA. AC Q2JKL8; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CYB_1815; OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium OS Yellowstone B-Prime). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=321332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JA-2-3B'a(2-13); RX PubMed=18059494; DOI=10.1038/ismej.2007.46; RA Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., RA Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.; RT "Population level functional diversity in a microbial community RT revealed by comparative genomic and metagenomic analyses."; RL ISME J. 1:703-713(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000240; ABD02771.1; -; Genomic_DNA. DR RefSeq; YP_478034.1; NC_007776.1. DR ProteinModelPortal; Q2JKL8; -. DR STRING; 321332.CYB_1815; -. DR EnsemblBacteria; ABD02771; ABD02771; CYB_1815. DR GeneID; 3901198; -. DR KEGG; cyb:CYB_1815; -. DR PATRIC; 23805968; VBISynSp29577_1824. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSP321332:GH1B-1815-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 126 Unknown (By similarity). FT REGION 127 348 Thiamine-phosphate synthase (By FT similarity). FT REGION 174 178 HMP-PP binding (By similarity). FT REGION 271 273 THZ-P binding (By similarity). FT METAL 207 207 Magnesium (By similarity). FT METAL 226 226 Magnesium (By similarity). FT BINDING 206 206 HMP-PP (By similarity). FT BINDING 245 245 HMP-PP (By similarity). FT BINDING 274 274 HMP-PP (By similarity). FT BINDING 301 301 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 348 AA; 38837 MW; 29D21EEE82807B22 CRC64; MKPQAVARIL DANLDRAREG LRVLEEWFRF GLEEGKLSAE CKAMRQALAR WHSDPLRLAR DTSADPGTQI SHPQEEQRRD LRHLLQANCS RVQEALRVLE EYGKLAESHH WVAPGLAKLA KDMRYRLYVL ESELLGGSLR QRLLAAHLYL VTSPVPHWLE VVEKSLRGGV TLVQYRRKNL PDGEMLRDLK QLRQLCDRYQ ALMIVNDRVD LALVSQADGV HLGQTDLPVA QARHLLGSQR LIGLSTTNAE ELAQALNSDV DYIGVGPVYP TPTKAEKPPA GLEYVRLAAE KAHLPWFAIG GIDPHNLPEV RRAGATRVAV VRALMEAADP TQTARTMLAE LQGIPALS // ID Q2JU87_SYNJA Unreviewed; 348 AA. AC Q2JU87; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 59. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CYA_1569; OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium OS Yellowstone A-Prime). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=321327; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JA-3-3Ab; RX PubMed=18059494; DOI=10.1038/ismej.2007.46; RA Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., RA Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.; RT "Population level functional diversity in a microbial community RT revealed by comparative genomic and metagenomic analyses."; RL ISME J. 1:703-713(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000239; ABC99733.1; -; Genomic_DNA. DR RefSeq; YP_474996.1; NC_007775.1. DR ProteinModelPortal; Q2JU87; -. DR STRING; 321327.CYA_1569; -. DR EnsemblBacteria; ABC99733; ABC99733; CYA_1569. DR GeneID; 3899870; -. DR KEGG; cya:CYA_1569; -. DR PATRIC; 23811426; VBISynSp90045_1557. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSP321327:GHFX-1561-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 126 Unknown (By similarity). FT REGION 127 348 Thiamine-phosphate synthase (By FT similarity). FT REGION 174 178 HMP-PP binding (By similarity). FT REGION 271 273 THZ-P binding (By similarity). FT METAL 207 207 Magnesium (By similarity). FT METAL 226 226 Magnesium (By similarity). FT BINDING 206 206 HMP-PP (By similarity). FT BINDING 245 245 HMP-PP (By similarity). FT BINDING 274 274 HMP-PP (By similarity). FT BINDING 301 301 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 348 AA; 38719 MW; 90DD02FD0FBE437B CRC64; MKPQAVARIL DANLDRAREG LRVLEEWFRF GLENGELASE CKAMRQALAR WHSDPLRLAR DTPADPGTQI SHPQEEQRRD LGHLLQANCS RVQEALRVLE EYGKLAESSH WVAPGLAKLA KDMRYRLYVL ESELLGGSLR QRLLAAHLYL VTSPVPHWLE VVEKALRGGV TLVQYRRKNL TDREMLWDLK QLRQVCDRYQ ALMIVNDRVD LALVSQADGV HLGQTDLPVA QARHLLGSQR LIGLSTTNAE ELAQALNSGV DYIGVGPVYA TPTKAEKPPA GLEYVRLAAE KAHLPWFAIG GIDLHNLAEV RQAGASRVAV VRALMEAADP TQTARAMLAE LQRIPALS // ID Q2K0X6_RHIEC Unreviewed; 211 AA. AC Q2K0X6; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiEe; Synonyms=thiE; OrderedLocusNames=RHE_PE00336; OS Rhizobium etli (strain CFN 42 / ATCC 51251). OG Plasmid p42e. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=347834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFN 42 / ATCC 51251; PLASMID=p42e; RX PubMed=16505379; DOI=10.1073/pnas.0508502103; RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., RA Jimenez-Jacinto V., Collado-Vides J., Davila G.; RT "The partitioned Rhizobium etli genome: genetic and metabolic RT redundancy in seven interacting replicons."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000137; ABC93771.1; -; Genomic_DNA. DR RefSeq; YP_472498.1; NC_007765.1. DR ProteinModelPortal; Q2K0X6; -. DR STRING; 347834.RHE_PE00336; -. DR EnsemblBacteria; ABC93771; ABC93771; RHE_PE00336. DR GeneID; 3895734; -. DR KEGG; ret:RHE_PE00336; -. DR PATRIC; 23091946; VBIRhiEtl108884_5602. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RETL347834:GJJ0-5053-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Plasmid; KW Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21746 MW; 6C4281369F36DAFB CRC64; MKAFDLSLYL VLDPNLCAQI GMVETARLAV TGGATMVQLR DKRAGTSEMI QTGRALKQAL GGTGARLIVN DDVEAAIAIG ADGLHIGQED MDARTARELI GPEMILGLSV ETEALAAAVD PDLVDYTGVG PVFATPTKAD HKQPIGFDGL ARLVQLSPVP SVAIGGLKAE HVAEVFAAGA KGLAVVSAIC GTPDPEAATR RIAAEIRKVP A // ID Q2K4F3_RHIEC Unreviewed; 247 AA. AC Q2K4F3; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 47. DE SubName: Full=Thiamine-phosphate pyrophosphorylase protein; DE EC=2.5.1.3; GN Name=thiEch; OrderedLocusNames=RHE_CH03527; OS Rhizobium etli (strain CFN 42 / ATCC 51251). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=347834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFN 42 / ATCC 51251; RX PubMed=16505379; DOI=10.1073/pnas.0508502103; RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., RA Jimenez-Jacinto V., Collado-Vides J., Davila G.; RT "The partitioned Rhizobium etli genome: genetic and metabolic RT redundancy in seven interacting replicons."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000133; ABC92283.1; -; Genomic_DNA. DR RefSeq; YP_471010.1; NC_007761.1. DR ProteinModelPortal; Q2K4F3; -. DR STRING; 347834.RHE_CH03527; -. DR EnsemblBacteria; ABC92283; ABC92283; RHE_CH03527. DR GeneID; 3894313; -. DR KEGG; ret:RHE_CH03527; -. DR PATRIC; 23088731; VBIRhiEtl108884_4008. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RETL347834:GJJ0-3542-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 247 AA; 26408 MW; E7F945885E682A66 CRC64; MQASSNGTTH TKRVRIRPFQ KGIRRKRKDL MTEAENRCRL VLIVPDIADA DEQARIVADA LKGGDVASVI VPQYGLDDGA FQKHAEKLVP VIQDAGAAAL IAGDSRVAGR AKADGLHITG NAQALSEAID KHAPKLIVGG GNASDRHNAL EIGEVRPDYI FFGKLDGDIK PEAHPKNLAL GEWWASMIEI PCIVMAGTDP ASALAVAETR AEFVALRLAV FGEPGRAPSI VAEINALLDE KAPRFED // ID Q2KUN9_BORA1 Unreviewed; 321 AA. AC Q2KUN9; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 63. DE SubName: Full=Putative NUDIX hydrolase; GN OrderedLocusNames=BAV3038; OS Bordetella avium (strain 197N). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=360910; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=197N; RX PubMed=16885469; DOI=10.1128/JB.01927-05; RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., RA King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., RA Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., RA Squares S., Woodward J., Parkhill J., Temple L.M.; RT "Comparison of the genome sequence of the poultry pathogen Bordetella RT avium with those of B. bronchiseptica, B. pertussis, and B. RT parapertussis reveals extensive diversity in surface structures RT associated with host interaction."; RL J. Bacteriol. 188:6002-6015(2006). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM167904; CAJ50648.1; -; Genomic_DNA. DR RefSeq; YP_787533.1; NC_010645.1. DR ProteinModelPortal; Q2KUN9; -. DR STRING; 360910.BAV3038; -. DR GeneID; 6266343; -. DR KEGG; bav:BAV3038; -. DR PATRIC; 21132387; VBIBorAvi43433_3072. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BAVI360910:GCKI-3112-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 321 AA; 34464 MW; 66290D8B480FEDA2 CRC64; MSDKIIDVAA GLILRPDGQL LLGQRPEGKP WSGWWELPGG KLEPGETVLQ ALARELQEEI GITVTESRRW VSYVHVYPHT TVRLAFCFVT GWTGEPRGLE NQQLAWVDPQ QAAKVGELLP ATLPPLRWLR LPTAYGISSA GSPAALPAFL TRLEQALAQG LKLVQWREPG WPGGPAAPDL HAAFQETLKR CRQAGARLLV NSVHPETWWR QADGVHLRAR DAATRQTRPA LAEGHLVGVS AHTAAEIAQA RLLEADFAVI GPVAATATHP GQIPLGWDGF EAANRDAGLP VYALGGQSPA TLAQAQQHGA HGIAAIRGLL G // ID Q2LUV3_SYNAS Unreviewed; 229 AA. AC Q2LUV3; DT 21-FEB-2006, integrated into UniProtKB/TrEMBL. DT 21-FEB-2006, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SYN_00442; OS Syntrophus aciditrophicus (strain SB). OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophaceae; Syntrophus. OX NCBI_TaxID=56780; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB; RA Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., RA Campbell J., McInerney M., Moutakki H., Rio-Hernandez L.; RT "The genome of the syntrophic bacterium Syntrophus aciditrophicus: RT Life dependent on negative change in electrical potential."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000252; ABC77860.1; -; Genomic_DNA. DR RefSeq; YP_462028.1; NC_007759.1. DR ProteinModelPortal; Q2LUV3; -. DR STRING; 56780.SYN_00442; -. DR EnsemblBacteria; ABC77860; ABC77860; SYN_00442. DR GeneID; 3883801; -. DR KEGG; sat:SYN_00442; -. DR PATRIC; 23864712; VBISynAci70500_2141. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SACI56780:GHXT-2027-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 53 57 HMP-PP binding (By similarity). FT REGION 153 155 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 127 127 HMP-PP (By similarity). FT BINDING 156 156 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 25302 MW; 3671181D6FCE2035 CRC64; MRAFCLRYEM RVHNKKIIGE PSLYLVLSEE YGAGRSVMSI AEEAVAGGID ILQMREKHKS REDLLRLGSA LGELCRKNKV TFIVNDDPLL AAELDADGVH MGQKDLQRCP LDEVRRIIGI DRIIGLSTHS LEQFQRANTL DVDYLAFGPI FPTQTKDYSI GTADIRETLR VALKPVVFIG GVNTANLGIL LKEGAASMAL IRDIMQADDV ASRTAWYKSQ LAKGGINAK // ID Q2LWX8_SYNAS Unreviewed; 232 AA. AC Q2LWX8; DT 21-FEB-2006, integrated into UniProtKB/TrEMBL. DT 21-FEB-2006, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SYN_00302; OS Syntrophus aciditrophicus (strain SB). OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophaceae; Syntrophus. OX NCBI_TaxID=56780; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB; RA Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., RA Campbell J., McInerney M., Moutakki H., Rio-Hernandez L.; RT "The genome of the syntrophic bacterium Syntrophus aciditrophicus: RT Life dependent on negative change in electrical potential."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000252; ABC78587.1; -; Genomic_DNA. DR RefSeq; YP_462755.1; NC_007759.1. DR ProteinModelPortal; Q2LWX8; -. DR STRING; 56780.SYN_00302; -. DR EnsemblBacteria; ABC78587; ABC78587; SYN_00302. DR GeneID; 3882700; -. DR KEGG; sat:SYN_00302; -. DR PATRIC; 23866300; VBISynAci70500_2930. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SACI56780:GHXT-2759-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 232 AA; 24927 MW; 94B8A4089A93C21F CRC64; MTMIQPRAHS RKKIAGLYLV TDRALCGNRG LEEVVSLAVQ GGAACVQLRE KDLPTRPFVE EAKRLKALLS PLRVPLIIND RLDVALAAEA DGVHIGQEDM PCDIARRLLG PNAVIGLSVE TWEDVEAAEL MDVDYLGVSP VFATPTKTDT KAPWGLEGLT RIRAYSSHPL VAIGGISRDN AADVILAGAD CAAVVSAICA ASDPRMAAAD IQAEISWALK KKQRNKQHLI HP // ID Q2N781_ERYLH Unreviewed; 194 AA. AC Q2N781; DT 07-FEB-2006, integrated into UniProtKB/TrEMBL. DT 07-FEB-2006, sequence version 1. DT 14-MAY-2014, entry version 52. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=ELI_11840; OS Erythrobacter litoralis (strain HTCC2594). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=314225; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2594; RX PubMed=19168610; DOI=10.1128/JB.00026-09; RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.; RT "Complete genome sequence of Erythrobacter litoralis HTCC2594."; RL J. Bacteriol. 191:2419-2420(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000157; ABC64460.1; -; Genomic_DNA. DR RefSeq; YP_459257.1; NC_007722.1. DR ProteinModelPortal; Q2N781; -. DR STRING; 314225.ELI_11840; -. DR EnsemblBacteria; ABC64460; ABC64460; ELI_11840. DR GeneID; 3871508; -. DR KEGG; eli:ELI_11840; -. DR PATRIC; 21861875; VBIEryLit102657_2352. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NRRDSIM; -. DR OrthoDB; EOG679THR; -. DR BioCyc; ELIT314225:GHLE-2410-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 194 AA; 21650 MW; 7960586FCC7429B0 CRC64; MGLRYSGRVA HFQTCLERSR KDLPDLWLLS DERNDGVLEH RLRTLPPGSG FVYRHYHLPP AERVARFFAL KRIAEARGHL VILADSALTA REWGADGIYG APRSLYPTRR DLVTIATAHD LAEIGQANRA RSDAVMLSPA FPTRSHPGAA TLGPQRFRRL ARHAQMPVIA LGGMTQATAR RLDWPRWAAI DGLS // ID Q2NGH2_METST Unreviewed; 521 AA. AC Q2NGH2; DT 07-FEB-2006, integrated into UniProtKB/TrEMBL. DT 07-FEB-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Msp_0683; OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / OS MCB-3). OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanosphaera. OX NCBI_TaxID=339860; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3; RX PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006; RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., RA Hedderich R., Gottschalk G., Thauer R.K.; RT "The genome sequence of Methanosphaera stadtmanae reveals why this RT human intestinal archaeon is restricted to methanol and H2 for methane RT formation and ATP synthesis."; RL J. Bacteriol. 188:642-658(2006). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000102; ABC57081.1; -; Genomic_DNA. DR RefSeq; YP_447724.1; NC_007681.1. DR ProteinModelPortal; Q2NGH2; -. DR STRING; 339860.Msp_0683; -. DR EnsemblBacteria; ABC57081; ABC57081; Msp_0683. DR GeneID; 3855871; -. DR KEGG; mst:Msp_0683; -. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; WIDVIIN; -. DR BioCyc; MSTA339860:GJEZ-683-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005502; Ribosyl_crysJ1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF03747; ADP_ribosyl_GH; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF101478; SSF101478; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 521 AA; 58057 MW; D6AADFE3F4979763 CRC64; MDIDYSVYLV TDQFDFTESE FLNIIEEALK GNTTIVQIRE KNSSTRDFLN LAQKVKKLTD KYNVPLIIND RIDIALAVDS AGVHLGQDDM PCKIARKIIG PDKIIGISAE NYGDALQAQE DGADYLGIGA IEKTPTKTDC SVISEEDLNK IKKTIKIPHV AIGGVKEHNT REIIDKYGFD GVAIVSAIMK SDLPKEAATN FYNLVNSKLT LDDVYAAIYG VIVGDALGVP YEFKPRSTLQ KTPVTGMRGH GTYDKPEGTW SDDSSLTLAL ADSLVYGIDY DDIMSRFSKW LYQNMYTPEN EVFDVGQTTE EAIYNYTMGV NPLDCGGVEE YENGNGSLMR IMPLLLYINR KSIDEKSAIE LINNVSSLTH AHKTSKACCN IYNFLVQAII ENREANNLKT LIKKAIERAK KQYPLKEYPE FKSLYDDLFF DSGENLDSTG YVVNALQIAF YACYHSSDYS DAVLCAVNFG EDTDTNAAIT GGIAALYYGY KSIPPKWIDV IINKELINEV LDAFSEGLKH Y // ID Q2NZC9_XANOM Unreviewed; 315 AA. AC Q2NZC9; DT 07-FEB-2006, integrated into UniProtKB/TrEMBL. DT 07-FEB-2006, sequence version 1. DT 14-MAY-2014, entry version 65. DE SubName: Full=DGTP-pyrophosphohydrolase; GN OrderedLocusNames=XOO3593; OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=342109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF 311018; RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.; RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests RT contribution of large numbers of effector genes and insertion RT sequences to its race diversity."; RL Jpn. Agric. Res. Q. 39:275-287(2005). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008229; BAE70348.1; -; Genomic_DNA. DR RefSeq; YP_452622.1; NC_007705.1. DR ProteinModelPortal; Q2NZC9; -. DR STRING; 342109.XOO_3593; -. DR EnsemblBacteria; BAE70348; BAE70348; BAE70348. DR GeneID; 3859382; -. DR KEGG; xom:XOO_3593; -. DR PATRIC; 24117407; VBIXanOry49434_4102. DR eggNOG; COG0494; -. DR HOGENOM; HOG000004851; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XORY342109:GIX9-3650-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34826 MW; 851AEAEA9B66C6A6 CRC64; MPDSLRSIHV VAGVITDPRG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIEAQVGD WLMDVPQLYP DKRLRLEVRH ITAWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGAL RQPDHYLITP EPEDDARWLE GLERALQNGI TRIQLRARQT APAQWQALLQ QVMRLRGRTR AQLLLNRDIA LAAELGVGVH LGSEQLAGLQ ERPLPAEQLV AASCHGLDDL RHAQRIGCDF AVLGPVQATA SHPGATPLGW GGFETLREQV SLPIYALGGM QIEDVREARS HGAQGIAAIR SLWPQ // ID Q2P6Q3_XANOM Unreviewed; 207 AA. AC Q2P6Q3; DT 07-FEB-2006, integrated into UniProtKB/TrEMBL. DT 07-FEB-2006, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=XOO1019; OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=342109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF 311018; RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.; RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests RT contribution of large numbers of effector genes and insertion RT sequences to its race diversity."; RL Jpn. Agric. Res. Q. 39:275-287(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008229; BAE67774.1; -; Genomic_DNA. DR RefSeq; YP_450048.1; NC_007705.1. DR ProteinModelPortal; Q2P6Q3; -. DR STRING; 342109.XOO_1019; -. DR EnsemblBacteria; BAE67774; BAE67774; BAE67774. DR GeneID; 3858283; -. DR KEGG; xom:XOO_1019; -. DR PATRIC; 24111461; VBIXanOry49434_1160. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XORY342109:GIX9-1043-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21465 MW; 34275AD1F494C2DA CRC64; MPNRLNVRGV YLITPDEPNT QRLLLRTTPL LASIAWLQYR NKQADAALRL RQASALREAC VAHGVPLIIN DDAQLAAQVG AQGVHLGEDD GEVTAARALL GEHAIIGVSC YDAIGRARAA AAAGASYVAF GAFFPTITKQ TTRRATPALL QQAAELHLAR VAIGGIAPAQ VPALVTAGAD LIAVVSGVYA APDPVAAVQA YRAGFAA // ID TPS1_ORYSJ Reviewed; 548 AA. AC Q2QWK9; Q0IPK3; DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 2. DT 16-APR-2014, entry version 60. DE RecName: Full=Probable thiamine biosynthetic bifunctional enzyme, chloroplastic; DE Includes: DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; DE Includes: DE RecName: Full=Hydroxymethylpyrimidine kinase; DE Short=HMP kinase; DE EC=2.7.1.49; DE Flags: Precursor; GN OrderedLocusNames=Os12g0192500, LOC_Os12g09000; ORFNames=OsJ_35490; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16188032; DOI=10.1186/1741-7007-3-20; RG The rice chromosomes 11 and 12 sequencing consortia; RT "The sequence of rice chromosomes 11 and 12, rich in disease RT resistance genes and recent gene duplications."; RL BMC Biol. 3:20-20(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., RA Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., RA Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., RA Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). CC -!- FUNCTION: Essential for thiamine biosynthesis. Bifunctional enzyme CC that catalyzes the phosphorylation of hydroxymethylpyrimidine CC phosphate (HMP-P) to HMP-PP and condenses 4-methyl-5-(beta- CC hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino- CC 5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine CC monophosphate (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-5-hydroxymethyl-2- CC methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2- CC methylpyrimidine. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole: step 2/3. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity). CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DP000011; ABA96049.2; -; Genomic_DNA. DR EMBL; AP008218; BAF29362.2; -; Genomic_DNA. DR EMBL; CM000149; EEE52897.1; -; Genomic_DNA. DR EMBL; AK066087; BAG89812.1; -; mRNA. DR RefSeq; NP_001066343.2; NM_001072875.2. DR UniGene; Os.12097; -. DR ProteinModelPortal; Q2QWK9; -. DR EnsemblPlants; OS12T0192500-02; OS12T0192500-02; OS12G0192500. DR GeneID; 4351707; -. DR KEGG; osa:4351707; -. DR Gramene; Q2QWK9; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR UniPathway; UPA00060; UER00137. DR UniPathway; UPA00060; UER00141. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 2: Evidence at transcript level; KW ATP-binding; Chloroplast; Complete proteome; Kinase; Magnesium; KW Metal-binding; Multifunctional enzyme; Nucleotide-binding; Plastid; KW Reference proteome; Thiamine biosynthesis; Transferase; KW Transit peptide. FT TRANSIT 1 47 Chloroplast (Potential). FT CHAIN 48 548 Probable thiamine biosynthetic FT bifunctional enzyme, chloroplastic. FT /FTId=PRO_0000420254. FT REGION 372 376 HMP-PP binding (By similarity). FT REGION 469 471 THZ-P binding (By similarity). FT REGION 522 523 THZ-P binding (By similarity). FT METAL 405 405 Magnesium (By similarity). FT METAL 424 424 Magnesium (By similarity). FT BINDING 404 404 HMP-PP (By similarity). FT BINDING 443 443 HMP-PP (By similarity). FT BINDING 472 472 HMP-PP (By similarity). FT BINDING 499 499 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 548 AA; 57804 MW; 9B5204B75835A72E CRC64; MAAAPQQSVH PSLPSSTSTL RLLISSSPRR PPPPPPRARR YNRLAASASA AREMPWPHVL TVAGSDSGGG AGIQADIKAC AALGAYCSSV VTAVTAQNTA GVQGIHVVPE EFIREQLNSV LSDMSVDVVK TGMLPSIGVV RVLCESLKKF PVKALVVDPV MVSTSGDTLS ESSTLSVYRD ELFAMADIVT PNVKEASRLL GGVSLRTVSD MRNAAESIYK FGPKHVLVKG GDMLESSDAT DVFFDGKEFI ELHAHRIKTH NTHGTGCTLA SCIASELAKG ATMLHAVQVA KNFVESALHH SKDLVVGNGP QGPFDHLFKL KCPPYNVGSQ PSFKPDQLFL YAVTDSGMNK KWGRSIKEAV QAAIEGGATI VQLREKDSET REFLEAAKAC MEICKSSGVP LLINDRVDIA LACNADGVHV GQLDMSAHEV RELLGPGKII GVSCKTPAQA QQAWNDGADY IGCGGVFPTS TKANNPTLGF DGLKTVCLAS KLPVVAIGGI NASNAGSVME LGLPNLKGVA VVSALFDRPS VVAETRNMKS ILTNTSRT // ID Q2RL12_MOOTA Unreviewed; 178 AA. AC Q2RL12; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 14-MAY-2014, entry version 70. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Moth_0547; OS Moorella thermoacetica (strain ATCC 39073). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Moorella group; Moorella. OX NCBI_TaxID=264732; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39073; RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x; RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.; RT "The complete genome sequence of Moorella thermoacetica (f. RT Clostridium thermoaceticum)."; RL Environ. Microbiol. 10:2550-2573(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000232; ABC18877.1; -; Genomic_DNA. DR RefSeq; YP_429420.1; NC_007644.1. DR ProteinModelPortal; Q2RL12; -. DR STRING; 264732.Moth_0547; -. DR EnsemblBacteria; ABC18877; ABC18877; Moth_0547. DR GeneID; 3831447; -. DR KEGG; mta:Moth_0547; -. DR PATRIC; 22638197; VBIMooThe6753_0589. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MTHE264732:GH0A-579-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Thiamine biosynthesis; KW Transferase. FT REGION 8 12 HMP-PP binding (By similarity). FT REGION 104 106 THZ-P binding (By similarity). FT BINDING 39 39 HMP-PP (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 134 134 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 178 AA; 18141 MW; 874BF91DB0F17BE2 CRC64; MAGADYFQLR EKDLPAGELY NLAREIKRVL PSRVRLIIND RLDVAMAAGA DGVHLGEASL PTDVARRLLG PGKILGVSVH SVAAARQAAA AGADYLLFGH IFPTASKESL PPRGLVSLRE VAASVGIPIF ALGGITVDRV ASCLAAGAGG VAVMSGVMAA ADPAGAVAAY RKALDMVG // ID Q2RN68_RHORT Unreviewed; 272 AA. AC Q2RN68; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 14-MAY-2014, entry version 53. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Rru_A3633; OS Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S.1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., RA Reslewic S., Zhou S., Schwartz D.C.; RT "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC RT 11170."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000230; ABC24427.1; -; Genomic_DNA. DR RefSeq; YP_428714.1; NC_007643.1. DR ProteinModelPortal; Q2RN68; -. DR STRING; 269796.Rru_A3633; -. DR EnsemblBacteria; ABC24427; ABC24427; Rru_A3633. DR GeneID; 3837089; -. DR KEGG; rru:Rru_A3633; -. DR PATRIC; 23331074; VBIRhoRub82919_3754. DR eggNOG; bactNOG43146; -. DR HOGENOM; HOG000155781; -. DR OMA; ENSITEM; -. DR BioCyc; RRUB269796:GCN1-3697-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 272 AA; 28497 MW; 15822A9FC91704CC CRC64; MRPGARGGKL ARIMPRTLVH FIAKGSPLSR LGSRRSAAAP PRLLLMTDDQ RLADPLGAAD RLPPKAGVIV RHYACAGAVR HGLARALIAR LRARRIAVIL AAPSPAHALP AGLAGLHLPD KLAAHGLLAR LLLWRRAARG RWLCAAAHDA PAMIRARRLG CALIVLSPLF PTASHPGARG LGARRAALLI HRLAARRAPA GSRAGKAPAV IALGGISTLS FRRLAGCGFG GIAGISALPG MKWRRSGREK PKPRTGDGKS RRPPVCLSPL SA // ID Q2RVG4_RHORT Unreviewed; 216 AA. AC Q2RVG4; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 14-MAY-2014, entry version 70. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Rru_A1080; OS Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S.1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., RA Reslewic S., Zhou S., Schwartz D.C.; RT "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC RT 11170."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000230; ABC21881.1; -; Genomic_DNA. DR RefSeq; YP_426168.1; NC_007643.1. DR ProteinModelPortal; Q2RVG4; -. DR STRING; 269796.Rru_A1080; -. DR EnsemblBacteria; ABC21881; ABC21881; Rru_A1080. DR GeneID; 3833541; -. DR KEGG; rru:Rru_A1080; -. DR PATRIC; 23325760; VBIRhoRub82919_1138. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IGRTCHG; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RRUB269796:GCN1-1103-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22991 MW; 6778BD683175801C CRC64; MSDPACRLYL ITPPRLDDWA AFAETLKRTL AAGDVACLQL RMKDESDDAI RRAVAAIRPV CHGADVALLL NDRPDLAKET GCDGVHVGQT DASYAQARAI VGADAIVGVT CHDSRHLAMI AGEAGADYVA FGAFFPSTTK EPPTQADPEI LRWWSEMMIV PSVAIGGITV ENCAPLVETG TDFLAVCNGV WGHAEGPEAA VRAFVRVIAE VYAQPD // ID Q2S370_SALRD Unreviewed; 210 AA. AC Q2S370; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=SRU_1236; OS Salinibacter ruber (strain DSM 13855 / M31). OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Salinibacter. OX NCBI_TaxID=309807; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13855 / M31; RX PubMed=16330755; DOI=10.1073/pnas.0509073102; RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., RA Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., RA Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., RA Charlebois R.L., Legault B., Rodriguez-Valera F.; RT "The genome of Salinibacter ruber: convergence and gene exchange among RT hyperhalophilic bacteria and archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000159; ABC46233.1; -; Genomic_DNA. DR RefSeq; YP_445361.1; NC_007677.1. DR ProteinModelPortal; Q2S370; -. DR STRING; 309807.SRU_1236; -. DR EnsemblBacteria; ABC46233; ABC46233; SRU_1236. DR GeneID; 3850843; -. DR KEGG; sru:SRU_1236; -. DR PATRIC; 23424887; VBISalRub86502_1284. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VITDWRL; -. DR OrthoDB; EOG6W19NW; -. DR PhylomeDB; Q2S370; -. DR BioCyc; SRUB309807:GJJD-1233-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 210 AA; 22219 MW; 947DFF7554C6BC3A CRC64; MAALPYPRLA LIADGFTNDA RADRAVEAVR AGVRWVHLRD HEASPEAFAT AAHALADRLQ TAADDVTITV NTRVDVADAL GSGAHIGWRG PSVGETRERL GPEALIGYSA HEHVEAEGDR TQGVDYYFFS PVFPTTSKPD RPPTGIGPLR AFCRVAAPVP VLALGGITPE RVSVCREAGA HGVAVLSGIM NVDTPRAAAR AYLRALAEHA // ID Q2SQL4_HAHCH Unreviewed; 487 AA. AC Q2SQL4; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 16-APR-2014, entry version 66. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=HCH_00141; OS Hahella chejuensis (strain KCTC 2396). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Hahellaceae; Hahella. OX NCBI_TaxID=349521; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 2396; RX PubMed=16352867; DOI=10.1093/nar/gki1016; RA Jeong H., Yim J.H., Lee C., Choi S.H., Park Y.K., Yoon S.H., Hur C.G., RA Kang H.Y., Kim D., Lee H.H., Park K.H., Park S.H., Park H.S., RA Lee H.K., Oh T.K., Kim J.F.; RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing RT an algicidal agent."; RL Nucleic Acids Res. 33:7066-7073(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000155; ABC27060.1; -; Genomic_DNA. DR RefSeq; YP_431485.1; NC_007645.1. DR ProteinModelPortal; Q2SQL4; -. DR STRING; 349521.HCH_00141; -. DR GeneID; 3841167; -. DR KEGG; hch:HCH_00141; -. DR PATRIC; 22081450; VBIHahChe29232_0133. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; HCHE349521:GHAL-138-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 487 AA; 52108 MW; AEEA1CE4B858F00C CRC64; MTNHTPKVWI IAASDSAGAS GIQADLATLR GLEVHGGVAL TAVTAQNSQE VLSINPVATA VLRDQLRALR ADGDAVAIKI GLLTDAEQVD VLREFLCAYS GLVVLDPVLG SSTGAGFGMS VAALKSLLPY VDVVTPNIPE AEQLADRRIS SPADMLSAAV RLRELGAKGV WLKGGHLGLG EQCLDLVWLS EQPYWFAQPR LSVRHHRGTG CTLASALAAF VARGESLLDA AALANAYVKQ GLRQGYAIGP GPGPIARQGW PSLMTDFPRI TDRLDWLDYA AFPDCGASSL GLYPVVDSVE WLRKLLPLGI DTCQLRIKSN DLTLLEGAIS EAAKLGRQYG CRLFINDHWR LAIKHGAYGV HLGQEDIADA DLNAIRDAGL RLGVSTHGDF EWARAATIQP SYIAIGAIFP TQTKEVRIVG LEKLARWVAL LQDHYPLTAI GGINLSNMDV ILKTGVDSVA VVSAITQAPD LRDAVTNLSR KLLKGWE // ID Q2SU90_BURTA Unreviewed; 364 AA. AC Q2SU90; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BTH_I3005; OS Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / OS CIP 106301). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=271848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E264 / ATCC 700388 / DSM 13276 / CIP 106301; RX PubMed=16336651; DOI=10.1186/1471-2164-6-174; RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., RA DeShazer D.; RT "Bacterial genome adaptation to niches: divergence of the potential RT virulence genes in three Burkholderia species of different survival RT strategies."; RL BMC Genomics 6:174-174(2005). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000086; ABC36700.1; -; Genomic_DNA. DR RefSeq; YP_443509.1; NC_007651.1. DR ProteinModelPortal; Q2SU90; -. DR STRING; 271848.BTH_I3005; -. DR EnsemblBacteria; ABC36700; ABC36700; BTH_I3005. DR GeneID; 3847348; -. DR KEGG; bte:BTH_I3005; -. DR PATRIC; 19309242; VBIBurTha36512_5893. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BTHA271848:GJMY-3005-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 364 AA; 38243 MW; FCD898A1062C157D CRC64; MSAALPDAFW PPADELSEAA ERIRAALGVW PRPDARTRIC LAPPEHPRAG DLWVAAAGDA DVHIARLTAA GAQAIVIDDV SATLHTGAAR HALASRAPLA DDWIAALAAF LDCGFAAPDA LVLALAWRDG DEARGDDPWP VDPARFPRVL GVPAAPEPAF PPCPQRLGLY PVLPSAEWVE RVLDCGVRTV QLRVKDASPD ALRAEVERAV AAGRRHPDAR VFINDHWRLA LDAGAYGIHL GQEDLETAEL RAIAQAGVRL GLSSHGYYEM LVALQLKPSY LALGPVFATA TKAVAAPPQG LARLARYARF AGPQAPLVAI GGITVDTLGA VLAAGVGSAA VVSAITAAAD YREAIVAMQK NFGR // ID Q2T7R6_BURTA Unreviewed; 196 AA. AC Q2T7R6; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE SubName: Full=Thiamine-phosphate pyrophosphorylase ThiE, putative; GN OrderedLocusNames=BTH_II0583; OS Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / OS CIP 106301). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=271848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E264 / ATCC 700388 / DSM 13276 / CIP 106301; RX PubMed=16336651; DOI=10.1186/1471-2164-6-174; RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., RA DeShazer D.; RT "Bacterial genome adaptation to niches: divergence of the potential RT virulence genes in three Burkholderia species of different survival RT strategies."; RL BMC Genomics 6:174-174(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000085; ABC34696.1; -; Genomic_DNA. DR RefSeq; YP_438783.1; NC_007650.1. DR ProteinModelPortal; Q2T7R6; -. DR STRING; 271848.BTH_II0583; -. DR EnsemblBacteria; ABC34696; ABC34696; BTH_II0583. DR GeneID; 3845254; -. DR KEGG; bte:BTH_II0583; -. DR PATRIC; 19298666; VBIBurTha36512_0664. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BTHA271848:GJMY-3927-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 196 AA; 20166 MW; 70D187519719CF0D CRC64; MNDALALPPH YLITPEPDSG SDADLAAFLD RLSAALATGL KLVQLRVKTL DAPAYAALAA DALARCRAQC ARMIVNGPIG AEAALALGAS GVHLGSIALR AATARPIASD GLLSAACHSL DELLHAQRIG ADLATLSPVL PTLTHPGAPT LGWARFAEYA AQTRVPVYAL GGMTRAHLAT ARAHHAHGIA SIRGLW // ID Q2TZM1_ASPOR Unreviewed; 519 AA. AC Q2TZM1; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 16-APR-2014, entry version 48. DE SubName: Full=Thiamine monophosphate synthase; GN ORFNames=AO090011000799; OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=510516; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 42149 / RIB 40; RX PubMed=16372010; DOI=10.1038/nature04300; RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., RA Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., RA Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., RA Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W., RA Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., RA Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., RA Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., RA Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., RA Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., RA Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., RA Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., RA Kuhara S., Ogasawara N., Kikuchi H.; RT "Genome sequencing and analysis of Aspergillus oryzae."; RL Nature 438:1157-1161(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP007171; BAE65244.1; -; Genomic_DNA. DR RefSeq; XP_001826377.1; XM_001826325.2. DR ProteinModelPortal; Q2TZM1; -. DR STRING; 5062.CADAORAP00005402; -. DR EnsemblFungi; CADAORAT00005503; CADAORAP00005402; CADAORAG00005503. DR GeneID; 5998480; -. DR KEGG; aor:AOR_1_1340054; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 519 AA; 54957 MW; 3858C5DE999ABFDC CRC64; MPLNLSLYLV TDSTPAILKG RDLCTVVEEA LKGGVTIVQY RDKKSDTGEQ IQTAKKLHQI TQKYGVPLLI NDRVDVALAA GVEGVHLGQD DMAIEQAKQL LPKDAIIGIT AASIEEAQKA IDAGADYLGI GTMFATPTKT NTKHIIGTAG TQAILDAISD TGRSVGTVSI GGINLSNVQR VLYQSRAPRK ELDGVAIVSA IIAADDPKAA AAEFVKRIAT PPPFVRAPAA PQIREVAALQ EEVPKIVQKV VQAHPLVHNM INFVVANFVA NVALSMGASP IMAPHGDEAV DLAQFDGGLV VNMGTLTSES VPNYVKAIKA YNERGNPVVY DPVGAPATHI RRGAVKQLMA GGYFDLIKGN EGEIRQVFGS SGVIQRGVDS GPSRLDGQAK AILVRDLARR EHNLVLLTGA VDYLSDGERV IAVENGHELL GQVTGTGCAV GTVSGCFLTG HPSDRLLAVL SGILMYEIAA ENAASKEYVR GPGSFVPAFL DELYAIRQAA LKGDHSWFTG RAKIQMIDL // ID Q2UVH9_MAIZE Unreviewed; 551 AA. AC Q2UVH9; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 19-MAR-2014, entry version 45. DE SubName: Full=Phosphomethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase; GN Name=bth1; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaf; RA Rapala-Kozik M., Olczak M., Kozik A.; RT "Molecular characterization of THI6-like gene involved in thiamine RT biosynthesis in Zea mays."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM167973; CAJ45026.1; -; mRNA. DR RefSeq; NP_001105900.1; NM_001112430.1. DR UniGene; Zm.19349; -. DR ProteinModelPortal; Q2UVH9; -. DR PRIDE; Q2UVH9; -. DR GeneID; 732816; -. DR KEGG; zma:732816; -. DR Gramene; Q2UVH9; -. DR KO; K14153; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 2: Evidence at transcript level; KW Kinase; Transferase. SQ SEQUENCE 551 AA; 57756 MW; 97B03880A701FC7E CRC64; MTSVPLPPLP AALAQYRPSA AATLGFRTPS SAPGVSASSS TRARRFSVIA SAREMPWPHV LTVAGSDSSA GAGIQADIKA CAALGAYCSS AITAVTAQNT VGVQGIHAVP EKFVGEQLRS VLSDMSVDVV KTGMLPSAGV VKVLCESLRK FPVKALVVDP VMVSTSGDTL SGPSTLATYR DELFSMADIV TPNVKEASKL LGDVSLHTIS DMRNAAESIY KLGPKYVLVK GGDMPDSSDA IDVLFDGKEF TELRGLRIKT RNTHGTGCTL ASCIAAELAK GATMLHAVQA AKKFVESALY HSKDLVIGNG PQGPFDHLFE LKSPSYKMGS LQKFNPDDLF LYAVTDSGMN KKWGRSIKDA VKAAIEGGAT IVQLREKDAE TREFLEAAKA CVEICKSLGV PLLINDRVDV ALACDAGGVH VGQSDIPAWE VRGLLGPGKI IGVSCKTLAQ AEQAWKDGAD YIGCGGVFPT TTKANNPTLG FEGLRTVCLA SKLPVVAIGG INAGNAGSVM ELGLPNLKGV AVVSALFDRE RVAAETRNLR SILMKNAHSR S // ID Q2W3B3_MAGSA Unreviewed; 147 AA. AC Q2W3B3; DT 10-JAN-2006, integrated into UniProtKB/TrEMBL. DT 10-JAN-2006, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=amb2858; OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Magnetospirillum. OX NCBI_TaxID=342108; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AMB-1 / ATCC 700264; RX PubMed=16303747; DOI=10.1093/dnares/dsi002; RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., RA Takeyama H.; RT "Complete genome sequence of the facultative anaerobic magnetotactic RT bacterium Magnetospirillum sp. strain AMB-1."; RL DNA Res. 12:157-166(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP007255; BAE51662.1; -; Genomic_DNA. DR RefSeq; YP_422221.1; NC_007626.1. DR ProteinModelPortal; Q2W3B3; -. DR STRING; 342108.amb2858; -. DR EnsemblBacteria; BAE51662; BAE51662; amb2858. DR GeneID; 3802722; -. DR KEGG; mag:amb2858; -. DR PATRIC; 22439980; VBIMagMag129836_2826. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MMAG342108:GJNU-2890-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 147 AA; 15383 MW; 488D13CAC4C2B425 CRC64; MAVLLNDRPD LAFETGCDGV HVGQTDASYK AARQAVGPEG IVGITCHDSR HLAMEAGEAG ADYVAFGAFF PTETKEAPTR AEIELLEWWH GLFTVPCVAI GGITVENCRP LVTAGADFLA VSGGVWNHPE GPEAAVRAFA KICADGG // ID Q2WBE8_MAGSA Unreviewed; 199 AA. AC Q2WBE8; DT 10-JAN-2006, integrated into UniProtKB/TrEMBL. DT 10-JAN-2006, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=amb0023; OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Magnetospirillum. OX NCBI_TaxID=342108; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AMB-1 / ATCC 700264; RX PubMed=16303747; DOI=10.1093/dnares/dsi002; RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., RA Takeyama H.; RT "Complete genome sequence of the facultative anaerobic magnetotactic RT bacterium Magnetospirillum sp. strain AMB-1."; RL DNA Res. 12:157-166(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP007255; BAE48827.1; -; Genomic_DNA. DR RefSeq; YP_419386.1; NC_007626.1. DR ProteinModelPortal; Q2WBE8; -. DR STRING; 342108.amb0023; -. DR EnsemblBacteria; BAE48827; BAE48827; amb0023. DR GeneID; 3806645; -. DR KEGG; mag:amb0023; -. DR PATRIC; 22434306; VBIMagMag129836_0024. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NRRDSIM; -. DR OrthoDB; EOG699751; -. DR BioCyc; MMAG342108:GJNU-24-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 199 AA; 21452 MW; D4CDC075F671C880 CRC64; MTLANRRTRL NTPPHDPFPW LVLVTDEARL PDPRAAMERL PPGAGVILRH YGAEKRRPMA KAVAALARRR RLVLLVAGDW RLAAELGADG LHLPEGMARH GLLAGALGWV WRRRRLLLVA CHGSLALGRA RDLGAHGALL SPVFPTASHP GAATIGPVRF GLWARRTRIP VIALGGMTRQ RLRHLPGAAG MAAIGSLLA // ID Q2YAB1_NITMU Unreviewed; 325 AA. AC Q2YAB1; DT 20-DEC-2005, integrated into UniProtKB/TrEMBL. DT 20-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 61. DE SubName: Full=NUDIX hydrolase; GN OrderedLocusNames=Nmul_A1007; OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosospira. OX NCBI_TaxID=323848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25196 / NCIMB 11849; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC RT 25196."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000103; ABB74310.1; -; Genomic_DNA. DR RefSeq; YP_411702.1; NC_007614.1. DR ProteinModelPortal; Q2YAB1; -. DR STRING; 323848.Nmul_A1007; -. DR EnsemblBacteria; ABB74310; ABB74310; Nmul_A1007. DR GeneID; 3785838; -. DR KEGG; nmu:Nmul_A1007; -. DR PATRIC; 22725202; VBINitMul110821_1170. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NMUL323848:GKEC-1030-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 325 AA; 36021 MW; 80C08E1ED9AD1A00 CRC64; MRPAPSIVEV VAAIIIGSDG SFLLARRPEG KPYAGYWEFP GGKVNPEESL LRALKRELLE ELGIHVKHAY PWITRTFTYP HARVRLHFYR VVEWHGEPHP HEDQELSWQF ADNVSVEPLL PANAPVLRAL ALPPVYGITN AAEWGPQIAA ARIGHALQKG LRLVQLREKG MRSKALDAFA REVTALAHHY GARILVNSGT GNESLCQELD MDGIHFTSAD LMNLSKRPDV EWCAASCHNA EELFRAEQLE MDFAVLAPVL PTLSHPDSPV LGWRKLARII HGSAIPVYAL GGLQSEDLAI AWEHGAHGIA LMRRIEQVRG TGQKA // ID Q2YP59_BRUA2 Unreviewed; 203 AA. AC Q2YP59; DT 07-FEB-2006, integrated into UniProtKB/TrEMBL. DT 07-FEB-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BAB1_0215; OS Brucella abortus (strain 2308). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308; RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005; RG Microbial Genomics Group; RG Lawrence Livermore National Laboratory; RG and the Genome Analysis Group; RG Oak Ridge National Laboratory; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM040264; CAJ10171.1; -; Genomic_DNA. DR RefSeq; YP_413697.1; NC_007618.1. DR ProteinModelPortal; Q2YP59; -. DR STRING; 359391.BAB1_0215; -. DR EnsemblBacteria; CAJ10171; CAJ10171; BAB1_0215. DR GeneID; 3787003; -. DR KEGG; bmf:BAB1_0215; -. DR PATRIC; 17843271; VBIBruMel86222_0225. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BABO359391:GKDV-218-MONOMER; -. DR BioCyc; BMEL359391:GJOQ-218-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID Q2YRC7_BRUA2 Unreviewed; 221 AA. AC Q2YRC7; DT 07-FEB-2006, integrated into UniProtKB/TrEMBL. DT 07-FEB-2006, sequence version 1. DT 14-MAY-2014, entry version 52. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; DE EC=2.5.1.3; GN OrderedLocusNames=BAB1_1719; OS Brucella abortus (strain 2308). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308; RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005; RG Microbial Genomics Group; RG Lawrence Livermore National Laboratory; RG and the Genome Analysis Group; RG Oak Ridge National Laboratory; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM040264; CAJ11675.1; -; Genomic_DNA. DR RefSeq; YP_415069.1; NC_007618.1. DR ProteinModelPortal; Q2YRC7; -. DR STRING; 359391.BAB1_1719; -. DR EnsemblBacteria; CAJ11675; CAJ11675; BAB1_1719. DR GeneID; 3788236; -. DR KEGG; bmf:BAB1_1719; -. DR PATRIC; 17846465; VBIBruMel86222_1782. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BABO359391:GKDV-1762-MONOMER; -. DR BioCyc; BMEL359391:GJOQ-1762-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID Q30R65_SULDN Unreviewed; 183 AA. AC Q30R65; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 55. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Suden_1238; OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) OS (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251)). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Sulfurimonas. OX NCBI_TaxID=326298; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33889 / DSM 1251; RX PubMed=18065616; DOI=10.1128/AEM.01844-07; RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S., Hauser L.J., RA Hemp J., Hugler M., Land M., Lapidus A., Larimer F.W., Lucas S., RA Malfatti S.A., Meyer F., Paulsen I.T., Ren Q., Simon J., RA USF Genomics Class; RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas RT denitrificans."; RL Appl. Environ. Microbiol. 74:1145-1156(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000153; ABB44516.1; -; Genomic_DNA. DR RefSeq; YP_393751.1; NC_007575.1. DR ProteinModelPortal; Q30R65; -. DR STRING; 326298.Suden_1238; -. DR EnsemblBacteria; ABB44516; ABB44516; Suden_1238. DR GeneID; 3763698; -. DR KEGG; tdn:Suden_1238; -. DR PATRIC; 23771100; VBISulDen68967_1285. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; STHSHEE; -. DR OrthoDB; EOG6FJNJD; -. DR BioCyc; SDEN326298:GH9P-1286-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 183 AA; 20632 MW; 28F2A74EF19286D5 CRC64; MQKYLITSAQ FYTQNSDIFY QTLYKQLKKQ KPEYVLFRDK TATNYEELAS VFTLTCKEIG GVKSFVHQDI YLAKALGADG VHLTSKQFCE IELAKSKNLE VIISTHSHEE VLQAQKLGAD AVTYSPIFAS PDKGEPKGVN DLEELLSKCK IKVFALGGIV TNEHVEMISK TKVYGFASIR YFI // ID Q30RD0_SULDN Unreviewed; 186 AA. AC Q30RD0; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=Suden_1173; OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) OS (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251)). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Sulfurimonas. OX NCBI_TaxID=326298; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33889 / DSM 1251; RX PubMed=18065616; DOI=10.1128/AEM.01844-07; RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S., Hauser L.J., RA Hemp J., Hugler M., Land M., Lapidus A., Larimer F.W., Lucas S., RA Malfatti S.A., Meyer F., Paulsen I.T., Ren Q., Simon J., RA USF Genomics Class; RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas RT denitrificans."; RL Appl. Environ. Microbiol. 74:1145-1156(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000153; ABB44451.1; -; Genomic_DNA. DR RefSeq; YP_393686.1; NC_007575.1. DR ProteinModelPortal; Q30RD0; -. DR STRING; 326298.Suden_1173; -. DR EnsemblBacteria; ABB44451; ABB44451; Suden_1173. DR GeneID; 3763722; -. DR KEGG; tdn:Suden_1173; -. DR PATRIC; 23770960; VBISulDen68967_1219. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NADIAFI; -. DR OrthoDB; EOG6WX4T9; -. DR BioCyc; SDEN326298:GH9P-1217-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 186 AA; 20914 MW; 9AA2577205F43943 CRC64; MRLYALCDQD LLDKKGLSLE DFISTAKEKN AEIIQYRNKN ADIAFIKQQL IKIRKMYDGF LIVNDAYELI EFCDGVHVGQ EDLMAIDKDI FAAVKIIREV IKKDKILGIS THNEKEILEA NQMDLNYIGL GAYRNTDTKN NVTTVLGEKL DSLASLSKHY VAAIGGVKES DKFSHVTYHV VGSGLL // ID Q311P1_DESDG Unreviewed; 214 AA. AC Q311P1; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 69. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dde_1558; OS Desulfovibrio desulfuricans (strain G20). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=207559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G20; RX PubMed=21685289; DOI=10.1128/JB.05400-11; RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., RA Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., RA Lucas S., Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.; RT "Complete genome sequence and updated annotation of Desulfovibrio RT alaskensis G20."; RL J. Bacteriol. 193:4268-4269(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000112; ABB38355.1; -; Genomic_DNA. DR RefSeq; YP_388050.1; NC_007519.1. DR ProteinModelPortal; Q311P1; -. DR STRING; 207559.Dde_1558; -. DR EnsemblBacteria; ABB38355; ABB38355; Dde_1558. DR GeneID; 3755997; -. DR KEGG; dde:Dde_1558; -. DR PATRIC; 21742063; VBIDesDes50040_1553. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HRFYFIT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DALA207559:GH1L-1359-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23052 MW; 64FCD38D3F30F464 CRC64; MKNNMADWDI YCLTDAGLSR GRDTVEVVRA MLQGGARVIQ YREKDKKAGE MLRECMEIRK LTRDAGCCFI VNDHIDVAML CDADGVHVGQ EDIPVPEVRR LVGDGKIIGL STHSPEQCCD AVAQGADYIG VGPVFFTRTK KDVCAPVGFE YLDYVAANHT VPFVAIGGIK EHNIEEVAAH GARCCALVSA ITGADDIAAT VAGLRGRLRS ASGR // ID Q312G8_DESDG Unreviewed; 218 AA. AC Q312G8; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 2. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Dde_1379; OS Desulfovibrio desulfuricans (strain G20). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=207559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G20; RX PubMed=21685289; DOI=10.1128/JB.05400-11; RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., RA Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., RA Lucas S., Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.; RT "Complete genome sequence and updated annotation of Desulfovibrio RT alaskensis G20."; RL J. Bacteriol. 193:4268-4269(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000112; ABB38178.2; -; Genomic_DNA. DR RefSeq; YP_387873.2; NC_007519.1. DR STRING; 207559.Dde_1379; -. DR EnsemblBacteria; ABB38178; ABB38178; Dde_1379. DR GeneID; 3756166; -. DR KEGG; dde:Dde_1379; -. DR PATRIC; 21741693; VBIDesDes50040_1369. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; DALA207559:GH1L-1192-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 22847 MW; E6462FB15142EBC5 CRC64; MTRMQPDYSV YLVTDRTLCV SGTLEDVVAR AVQGGVTMVQ LREKQLCTRE FVELGRALRA LLAPRGVPLL VNDRVDVALA CGADGVHIGQ SDIRYADARR LMGAGAVIGV SVESVEQAAE AERCGADYMG VSPVFATPTK TDTSAPWGLE GLRGLRRRFS LPLVAIGGIG PDNAAEVFEA GADGIAVVSA ICASPDPQQA AATLRAVARG KRRAAAVL // ID Q319L7_PROM9 Unreviewed; 365 AA. AC Q319L7; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 60. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PMT9312_1368; OS Prochlorococcus marinus (strain MIT 9312). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=74546; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9312; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., RA Land M., Kyrpides N., Lykidis A., Richardson P.; RT "Complete sequence of Prochlorococcus marinus str. MIT 9312."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000111; ABB50428.1; -; Genomic_DNA. DR RefSeq; YP_397864.1; NC_007577.1. DR ProteinModelPortal; Q319L7; -. DR STRING; 74546.PMT9312_1368; -. DR EnsemblBacteria; ABB50428; ABB50428; PMT9312_1368. DR GeneID; 3766180; -. DR KEGG; pmi:PMT9312_1368; -. DR PATRIC; 23006668; VBIProMar70153_1501. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR74546:GHRG-1400-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 142 Unknown (By similarity). FT REGION 143 365 Thiamine-phosphate synthase (By FT similarity). FT REGION 194 198 HMP-PP binding (By similarity). FT REGION 291 293 THZ-P binding (By similarity). FT METAL 227 227 Magnesium (By similarity). FT METAL 246 246 Magnesium (By similarity). FT BINDING 226 226 HMP-PP (By similarity). FT BINDING 265 265 HMP-PP (By similarity). FT BINDING 294 294 HMP-PP (By similarity). FT BINDING 321 321 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 365 AA; 41901 MW; 4E08BBD99324981F CRC64; MPLRFLKTIK NKFLMQNSSP KEPEDLRIFQ IIDANLDRAR EGLRVLEDWS RFGLGENNFV TKIKNFRQIL GKNHLEIYKQ SRNYNEDKCK GLTHQEQLKR KAPKQIISSN AGRVQEALRV IEEFSRLHNH ELSKIASEIR YEIYNLEIDL LNLSKRKKSD EILYKTHLYV ITDQKKNLLR IIEDILIAGV KIIQYRFKTG TDKDNLEEAI QIKNLCEKYN SLFIINDRVD IAIASNADGV HLGQEDLDLK TARKLLGYSK IIGISANNEN DISNALKEGC DYIGIGPVFE TSTKKNKKPL GIEKIKTLTK DLNIPWFAIG GVTTNNISFL KSHGFKKVAL VSQIMNSEDP KEDAIMILKD LSNEN // ID Q31I35_THICR Unreviewed; 316 AA. AC Q31I35; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 66. DE SubName: Full=MutT/NUDIX family protein; GN OrderedLocusNames=Tcr_0592; OS Thiomicrospira crunogena (strain XCL-2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Thiomicrospira. OX NCBI_TaxID=317025; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XCL-2; RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383; RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., RA Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., RA Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A., RA Freyermuth S.K., Harmer T.L., Hauser L.J., Huegler M., Kerfeld C.A., RA Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L., RA Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z., RA Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T., RA Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E., RA Zeruth G.T.; RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira RT crunogena XCL-2."; RL PLoS Biol. 4:1-17(2006). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000109; ABB41188.1; -; Genomic_DNA. DR RefSeq; YP_390862.1; NC_007520.2. DR ProteinModelPortal; Q31I35; -. DR STRING; 317025.Tcr_0592; -. DR EnsemblBacteria; ABB41188; ABB41188; Tcr_0592. DR GeneID; 3762456; -. DR KEGG; tcx:Tcr_0592; -. DR PATRIC; 23973088; VBIThiCru83387_0608. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TCRU317025:GHE8-602-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 316 AA; 35208 MW; CD7BE019E7BF55F7 CRC64; MSQRIDIAIG VLRQGNRVLL AQRQAKQSHA LKWEFPGGKV EKEEPIEVAL VREFQEEVGV ETTHWRSLIQ IPWDYETVSV HLHVYESDQF QGEPHGKEGQ PVQWVAISEL NEYDFPEANQ GILTALQLPE TLMISGSFHD EQDALTRLEA ALDEGIRLVQ LRAKQMEEVA FKTLAKKAIT LTHRYEGGKI LINGKPDWLE VLPEADGLQL ASSMIMDLTK RPVSENKILS ISTHSKAEVA KALELNADLL LLSPVKETRS HPDMSGMGWK TFADMVADIP VPVYALGGMK LSDVKESRKH GAQGIAAISG LWPDPI // ID Q31JD3_THICR Unreviewed; 218 AA. AC Q31JD3; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 57. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Tcr_0144; OS Thiomicrospira crunogena (strain XCL-2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Thiomicrospira. OX NCBI_TaxID=317025; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XCL-2; RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383; RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., RA Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., RA Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A., RA Freyermuth S.K., Harmer T.L., Hauser L.J., Huegler M., Kerfeld C.A., RA Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L., RA Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z., RA Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T., RA Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E., RA Zeruth G.T.; RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira RT crunogena XCL-2."; RL PLoS Biol. 4:1-17(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000109; ABB40740.1; -; Genomic_DNA. DR RefSeq; YP_390414.1; NC_007520.2. DR ProteinModelPortal; Q31JD3; -. DR STRING; 317025.Tcr_0144; -. DR EnsemblBacteria; ABB40740; ABB40740; Tcr_0144. DR GeneID; 3762436; -. DR KEGG; tcx:Tcr_0144; -. DR PATRIC; 23972158; VBIThiCru83387_0151. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HIANIQK; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; TCRU317025:GHE8-144-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 218 AA; 24002 MW; F75E8840F5D47DFF CRC64; MQFLSCHSPE KPLGIYPLVD RADKLLPFFD AGITTAQIRI KDLDGQPLEQ EMAQADTLAK SYQARLFIND YWEMALQLNS YGVHLGQEDV LKADLPAMHR AGLRLGVSTH TPEEIASALT IQPSYIAIGP VFETQSKQLP YPTTGLNNLH HWVKTLNVPV VAIGGIQRHN LTDVILAGAN GVAMINGLNL PGCTTMESIH KLIHTFDQAY QTRALSYG // ID Q31PD2_SYNE7 Unreviewed; 343 AA. AC Q31PD2; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 59. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Synpcc7942_1057; OS Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=1140; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7942; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC RT 7942."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000100; ABB57087.1; -; Genomic_DNA. DR RefSeq; YP_400074.1; NC_007604.1. DR ProteinModelPortal; Q31PD2; -. DR STRING; 1140.Synpcc7942_1057; -. DR EnsemblBacteria; ABB57087; ABB57087; Synpcc7942_1057. DR GeneID; 3773987; -. DR KEGG; syf:Synpcc7942_1057; -. DR PATRIC; 23787381; VBISynElo51371_1221. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SYNEL:SYNPCC7942_1057-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 128 Unknown (By similarity). FT REGION 129 343 Thiamine-phosphate synthase (By FT similarity). FT REGION 176 180 HMP-PP binding (By similarity). FT REGION 273 275 THZ-P binding (By similarity). FT METAL 209 209 Magnesium (By similarity). FT METAL 228 228 Magnesium (By similarity). FT BINDING 208 208 HMP-PP (By similarity). FT BINDING 247 247 HMP-PP (By similarity). FT BINDING 276 276 HMP-PP (By similarity). FT BINDING 303 303 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 343 AA; 37967 MW; ABC2792D80C7722B CRC64; MSSESSMDWV ETRCHRILDA NLDRAREGLR ILEEWCRFGL ERADLSATCK ALRQEVGSWH RPEFRQARDT THDPGTSLSH PQERQRTDLN AVLLANCARV QEALRVIEEY GKLIEGDLSD RAKAMRYQIY VLESQLQSRD RLSRLRQARL YLVTSPHPRL LEVVEAALSA GLKLVQYRDK QQEDATRLET ACRLAELCQR YGALFLVNDR VDLALACGAD GVHLGQQDVP MDVARRILGP DRIVGRSTTS PEELARANAE GADYVGVGPI FATPTKPGKA AAGFDYLGYA RQQAQQPFYA IGGIDVSNAA AVVAAGADRL AVVRAIMEAP DPKAATAELL QML // ID Q393K9_BURS3 Unreviewed; 194 AA. AC Q393K9; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 59. DE SubName: Full=Thiamine monophosphate synthase; DE EC=2.5.1.3; GN OrderedLocusNames=Bcep18194_B2246; OS Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 OS / NCIB 9086 / R18194)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=482957; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=383; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., RA Richardson P.; RT "Complete sequence of chromosome 2 of Burkholderia sp. 383."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000152; ABB12357.1; -; Genomic_DNA. DR RefSeq; YP_373001.1; NC_007511.1. DR ProteinModelPortal; Q393K9; -. DR STRING; 269483.Bcep18194_B2246; -. DR EnsemblBacteria; ABB12357; ABB12357; Bcep18194_B2246. DR GeneID; 3754012; -. DR KEGG; bur:Bcep18194_B2246; -. DR PATRIC; 19295395; VBIBurSp120713_7058. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BSP269483:GHLS-5666-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 194 AA; 20005 MW; 7683FD28BF229A3C CRC64; MNATLPRCYV ITPEPASASA ADGAAFLDRL SAVLARGETL VQLRVKSLDA AAFARLAAEA LARCNAAGAH LMLNGPIDAA GVIRLDGAGW HLDGTALRAA AQRPLPAGRW VSAACHTRDD LLLAARAGAD FVTLSPVLPT LSHPGAPTLG WAQFGALAAE AAMPVFALGG MTRTHLDDAR HHGAYGIAGI RGFW // ID Q39KA3_BURS3 Unreviewed; 374 AA. AC Q39KA3; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 71. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Bcep18194_A3511; OS Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 OS / NCIB 9086 / R18194)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=482957; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=383; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., RA Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia sp. 383."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000151; ABB07113.1; -; Genomic_DNA. DR RefSeq; YP_367757.1; NC_007510.1. DR ProteinModelPortal; Q39KA3; -. DR STRING; 269483.Bcep18194_A3511; -. DR EnsemblBacteria; ABB07113; ABB07113; Bcep18194_A3511. DR GeneID; 3748688; -. DR KEGG; bur:Bcep18194_A3511; -. DR PATRIC; 19284290; VBIBurSp120713_1586. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BSP269483:GHLS-345-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 374 AA; 39041 MW; 3C302452FEF2E97D CRC64; MSARFADAFW PPADELAEAA ERIRARLGDW PDGAAPWRLC VAVPDVPADG DVLIVSSGDR AAQARASAAS RPAAPGAVAI EFDEQGAVLH TAGARYALAA AHPLGDDWIA ALAAFLDCGF APVDALVLAL AWRDGDETRG ADAWPVDATR FPRIAGLPAA PEPAFAPCPE QLGLYPVVPD AEWVERVLDC GVLTVQLRVK GATPDTLRRE IARAVAAGRR HPDARVFIND HWQIAADEGA YGVHLGQEDL ETADLAAIAR AGLRLGLSSH GYYEMLRALH ERPSYLALGP VYATATKAVA APPQGLARIA RYAHFAGAQA PLVAIGGVGL DALPAVLATG VGSVAVVSAV TGATDYRAAV AALQQCFPGQ FDNH // ID Q39RH1_GEOMG Unreviewed; 213 AA. AC Q39RH1; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 72. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; Synonyms=tenI; OrderedLocusNames=Gmet_2935; OS Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=269799; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GS-15 / ATCC 53774 / DSM 7210; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Geobacter metallireducens GS-15."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000148; ABB33153.1; -; Genomic_DNA. DR RefSeq; YP_006721893.1; NC_007517.1. DR ProteinModelPortal; Q39RH1; -. DR STRING; 269799.Gmet_2935; -. DR EnsemblBacteria; ABB33153; ABB33153; Gmet_2935. DR GeneID; 3740829; -. DR KEGG; gme:Gmet_2935; -. DR PATRIC; 22005126; VBIGeoMet55070_2969. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GMET269799:GHNY-2981-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22401 MW; E17325CD5B0F037E CRC64; MSKVDFSLYL ITDRRQTTGR DLPAVVEEAL AGGVRAVQLR EKDLSSRELL ELARVMRELT GRYGAKLIIN DRVDIALATD ADGVHLGEAS IPADAARRIL GAHRLIGVSC HNREGALAAE KSGADFITFG PVYPTPSKAA YGAPVGVERL AEAAALLTIP VFALGGIKGD NIPEVLATGA AGVALISAVI AAVNPNEEAR AILTLLEQGR RTE // ID Q39RJ7_GEOMG Unreviewed; 497 AA. AC Q39RJ7; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 65. DE SubName: Full=4-amino-5-hydroxymethyl-2-methylpyrimidine-phosphate kinase and thiamin monophosphate synthase; GN Name=thiD; Synonyms=thiE; OrderedLocusNames=Gmet_2909; OS Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=269799; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GS-15 / ATCC 53774 / DSM 7210; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Geobacter metallireducens GS-15."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000148; ABB33127.1; -; Genomic_DNA. DR RefSeq; YP_006721866.1; NC_007517.1. DR ProteinModelPortal; Q39RJ7; -. DR STRING; 269799.Gmet_2909; -. DR EnsemblBacteria; ABB33127; ABB33127; Gmet_2909. DR GeneID; 3740859; -. DR KEGG; gme:Gmet_2909; -. DR PATRIC; 22005072; VBIGeoMet55070_2943. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OMA; YLAQGEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; GMET269799:GHNY-2953-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 497 AA; 52391 MW; D89049C6DDF85AD1 CRC64; MGSNGHNLRL VVNRDKQDSP IRGVYLVTDH GDRLAERVEA AIDGGVRIVQ YRNKGKDRAQ RYAVGEELRD LCSRRGVIFI VNDDLDLALQ LKADGIHLGQ EDGDPRIARR ELGPGRIIGV STHTMEEALA AQAAGADYIG FGAMFPTNSK EIGHLAGPEG LAAIRSRIMI PIVAIGGISR DNGPRVVDAG ADALAVISAV LAHPDPFLAA TELGLLFNRR APHPRGAVLT IAGSDSGGGA GIQADLKTAT LLGSYGSSVI TALTAQNTRG VSGIHGVPPS FVAEQLDAVL SDIPVDTVKT GMLFSAEIIA TVADKLAEYR KRIVVVDPVM VAKGGAPLID RGAVNVLKDR LMPRTYLLTP NIPEAERLTG LTIVDEEGMQ EAARRLFRLG ARNVLVKGGH LVAGDAVDIL FDGSAFHRFT APRILSKNTH GTGCTYAAAI ATYLAQGEPL REAVGRAKEF VTAAIRLGQP LGRGHGPVNH LLAALEVGDQ GPGTGDR // ID Q3A2D3_PELCD Unreviewed; 490 AA. AC Q3A2D3; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 2. DT 14-MAY-2014, entry version 64. DE SubName: Full=4-amino-5-hydroxymethyl-2-methylpyrimidine-phosphate kinase and thiamin monophosphate synthase; GN Name=thiD; Synonyms=thiE; OrderedLocusNames=Pcar_2235; OS Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Pelobacteraceae; Pelobacter. OX NCBI_TaxID=338963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2380 / Gra Bd 1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Pelobacter carbinolicus DSM 2380."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000142; ABA89474.2; -; Genomic_DNA. DR RefSeq; YP_006717987.1; NC_007498.2. DR STRING; 338963.Pcar_2235; -. DR EnsemblBacteria; ABA89474; ABA89474; Pcar_2235. DR GeneID; 3724908; -. DR KEGG; pca:Pcar_2235; -. DR PATRIC; 22890736; VBIPelCar86875_2418. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PCAR338963:GKDU-2458-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 490 AA; 51635 MW; 15FAD97C2D28A8A5 CRC64; MAIFLFEPGT AMKNRHFRGL YLITDDSRGD QLQAKLVAAL KGGTRIVQYR GKHLPEDVRH REARMVHSLC KQAGALFIVN DDPHLALACQ ADGVHLGQQD MHIAEARALL GPDKIIGTSN RTVEQAVNSQ KAGADYVAAG SVYPTGSKQD AVHIGLDVLH DIRQAVDIPL VAIGGINRDN TSEVIHAGAD AIALISAVMA DPSPALAARE ISLQFNRRAP VPHGRVLTVA GSDSGGGAGI QADLKTITLL GGYGMSVITA LTAQNTCGVQ NIYPVPASFV GEQLAAVLGD LQPEVVKTGM LLDAAIVRLV AQALKDHGLL AVVDPVMIAK GGASLLRDEA TKVCREHLLP HTYLLTPNLP EAEQLTGLPV HTEADMEKAA RRLQQLGARH VLLKGGHLEG EAVDLLLDGN TLHRLPAKRI DSRNTHGTGC TSSAAIAALL AGGHPLPQAV ALAKEFITEA IRTAPDLGAG HGPVNHFAAA KYLMNTIEGL // ID Q3A6Z1_PELCD Unreviewed; 208 AA. AC Q3A6Z1; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 69. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=tenI-2; Synonyms=thiE; OrderedLocusNames=Pcar_0607; OS Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Pelobacteraceae; Pelobacter. OX NCBI_TaxID=338963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2380 / Gra Bd 1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Pelobacter carbinolicus DSM 2380."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000142; ABA87866.1; -; Genomic_DNA. DR RefSeq; YP_006716301.1; NC_007498.2. DR ProteinModelPortal; Q3A6Z1; -. DR STRING; 338963.Pcar_0607; -. DR EnsemblBacteria; ABA87866; ABA87866; Pcar_0607. DR GeneID; 3724061; -. DR KEGG; pca:Pcar_0607; -. DR PATRIC; 22887190; VBIPelCar86875_0670. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PCAR338963:GKDU-692-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22320 MW; 0D8E5D93F7093A0F CRC64; MNTDDFRLYL ITDRNNLPAG RDLLTAVEQA LDGGVRAVQL REKDLPADEL YRCAMELKSL MDRYGARLLI NDRIDVALAA GADGVHLGEH SLPTHAARKI LGKQAIIGRS THHAGDIERE YRQGADFVTF SPVYFTPSKA PYGAPQGLEA LRRACASASL PVLALGGIRR DRIPEVRAAG AAGVALISAI LAASDPEAAT RALLAEIQ // ID Q3A7P2_PELCD Unreviewed; 206 AA. AC Q3A7P2; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=tenI-1; Synonyms=thiE; OrderedLocusNames=Pcar_0342; OS Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Pelobacteraceae; Pelobacter. OX NCBI_TaxID=338963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2380 / Gra Bd 1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Pelobacter carbinolicus DSM 2380."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000142; ABA87602.1; -; Genomic_DNA. DR RefSeq; YP_006716013.1; NC_007498.2. DR ProteinModelPortal; Q3A7P2; -. DR STRING; 338963.Pcar_0342; -. DR EnsemblBacteria; ABA87602; ABA87602; Pcar_0342. DR GeneID; 3723475; -. DR KEGG; pca:Pcar_0342; -. DR PATRIC; 22886606; VBIPelCar86875_0380. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MTREDIC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PCAR338963:GKDU-389-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21886 MW; 5245A83847E9E983 CRC64; MTREDICGVY LITESVPDML ERVRIALANG VKVVQYRGKN DPEAKRLPMA NRLRCLCGEY GAFFIVNDDP GLALACRADG VHLGQGDGSV MQARQMLGEA ALIGVSTHSL SEAEQAQRQG ADYIGFGCLF ATASKRDTVS ASLDELRLVR HVVSLPIVAI GGIHIGNAAL AVQAGADAVA VISAVMQADD CKSTVCELDR QCRALI // ID Q3ACN5_CARHZ Unreviewed; 215 AA. AC Q3ACN5; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CHY_1265; OS Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Carboxydothermus. OX NCBI_TaxID=246194; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Z-2901 / DSM 6008; RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065; RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., RA Madupu R., Sullivan S.A., Kolonay J.F., Haft D.H., Nelson W.C., RA Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., RA Robb F.T., Eisen J.A.; RT "Life in hot carbon monoxide: the complete genome sequence of RT Carboxydothermus hydrogenoformans Z-2901."; RL PLoS Genet. 1:563-574(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000141; ABB15033.1; -; Genomic_DNA. DR RefSeq; YP_360099.1; NC_007503.1. DR ProteinModelPortal; Q3ACN5; -. DR STRING; 246194.CHY_1265; -. DR EnsemblBacteria; ABB15033; ABB15033; CHY_1265. DR GeneID; 3727134; -. DR KEGG; chy:CHY_1265; -. DR PATRIC; 21275671; VBICarHyd26463_1211. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CHYD246194:GJCN-1264-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 24296 MW; ECF0A9C352BD22FB CRC64; MEDYNIYCIT AEKFSRGREN LKVVSEMLKA GIRIIQYREK YKSLKEKYYE CLKIRELTRQ YGAILIVNDH VDLCQMVDAD GVHLGQDDYP VKEARRILGD EYIIGVSTHS PEQLKKAAKE GADYAGVGPL FATNTKDNAI PPVGLEYLKW AVANSSIPFV AIGGIKEYNI QEVLDLGSKC IALVTEIVGA EDIKDKIDRL NKILERYRVS NKAFD // ID Q3AE34_CARHZ Unreviewed; 364 AA. AC Q3AE34; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 62. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=CHY_0746; OS Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Carboxydothermus. OX NCBI_TaxID=246194; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Z-2901 / DSM 6008; RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065; RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., RA Madupu R., Sullivan S.A., Kolonay J.F., Haft D.H., Nelson W.C., RA Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., RA Robb F.T., Eisen J.A.; RT "Life in hot carbon monoxide: the complete genome sequence of RT Carboxydothermus hydrogenoformans Z-2901."; RL PLoS Genet. 1:563-574(2005). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000141; ABB15834.1; -; Genomic_DNA. DR RefSeq; YP_359600.1; NC_007503.1. DR ProteinModelPortal; Q3AE34; -. DR STRING; 246194.CHY_0746; -. DR EnsemblBacteria; ABB15834; ABB15834; CHY_0746. DR GeneID; 3727945; -. DR KEGG; chy:CHY_0746; -. DR PATRIC; 21274626; VBICarHyd26463_0700. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CHYD246194:GJCN-746-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 364 AA; 40908 MW; 1F35550A7E3C4443 CRC64; MIRYNQPLPS SGRGLFFSGR YLMEIYRIID VNLNRAREGI RVLEEVARFG LANRKLFEEF KHLRHFIKEI EKSLAGNPLW YRDAQNDPGQ ELSSEEMARN NLREVVLANA KRAQESLRVL EEFGKLLDAA IVLNAKKARF LLYELEKEVL TLIKPSVDLT LYVLTDDAYL NEEKFWRVVE DCLKNGVTAF QYRAKGKKGA EMYREGLRLK ELCAKYGVSF FVNDRLDLGL ALNADGVHLG QEDLLLEVAR KHFPGKIIGL SATNYEEGVL GIKAGADYLG LGPIFPTSTK EDAAPPCGVE VIQKLKEEFP NSPVIAIGGI DREKVFEVIR AGADGIAVIS AVFGAESPAR AVYELRETII RARE // ID Q3ASE3_CHLCH Unreviewed; 217 AA. AC Q3ASE3; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 68. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Cag_0816; OS Chlorobium chlorochromatii (strain CaD3). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=340177; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CaD3; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Chlorobium chlorochromatii CaD3."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000108; ABB28082.1; -; Genomic_DNA. DR RefSeq; YP_379125.1; NC_007514.1. DR ProteinModelPortal; Q3ASE3; -. DR STRING; 340177.Cag_0816; -. DR EnsemblBacteria; ABB28082; ABB28082; Cag_0816. DR GeneID; 3746815; -. DR KEGG; cch:Cag_0816; -. DR PATRIC; 21369257; VBIChlChl46571_0846. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CCHL340177:GHBW-826-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22254 MW; 0971DF5930847310 CRC64; MINPILPPLR HIPTSPFLCA LTDATLPPLP FVKAVLAGGA TMIQLRVKEA TTRELIAWGV EIRTLCHAAG ACFIVNDRVD VALACGADGV HLGQQDMPCS LARKLFGKDM LIGVSASTVA EALQAEQDGA DYIGFGHIYP TNSKEKPHSP VGLSTLQQVA KAISLPIVAI GGISGENASA VIAAGASGIA VIAALSKVEN PTVAATKLCA AMQGVAL // ID Q3ASE4_CHLCH Unreviewed; 224 AA. AC Q3ASE4; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 56. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; DE EC=2.5.1.3; GN OrderedLocusNames=Cag_0815; OS Chlorobium chlorochromatii (strain CaD3). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=340177; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CaD3; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Chlorobium chlorochromatii CaD3."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000108; ABB28081.1; -; Genomic_DNA. DR RefSeq; YP_379124.1; NC_007514.1. DR ProteinModelPortal; Q3ASE4; -. DR STRING; 340177.Cag_0815; -. DR EnsemblBacteria; ABB28081; ABB28081; Cag_0815. DR GeneID; 3747469; -. DR KEGG; cch:Cag_0815; -. DR PATRIC; 21369255; VBIChlChl46571_0845. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FGPPQGL; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CCHL340177:GHBW-825-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 224 AA; 24126 MW; 07BC3761AC5EA092 CRC64; MTSAPSMSSP LPRLFIISSG TERVHSTTFQ IATPPPTLLL QQLALIPPHL RCMVQLREKA LNHAQLLHLA KLAKGANSAG NVRFVVNGSL EIARLAELDG VHLPEGSALL TTMRQAAPTM LLGCSVHSLE AAQYAAENGA DYLYFSPIFD TPSKRQYGAP QGLQALETVC KRLSLPVYAL GGITVERIAQ CRNCGAYGIA ALSLFQALDK LPHLLEQCNN LLES // ID Q3AX16_SYNS9 Unreviewed; 346 AA. AC Q3AX16; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Syncc9902_1502; OS Synechococcus sp. (strain CC9902). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=316279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC9902; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Synechococcus sp. CC9902."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000097; ABB26460.1; -; Genomic_DNA. DR RefSeq; YP_377504.1; NC_007513.1. DR ProteinModelPortal; Q3AX16; -. DR STRING; 316279.Syncc9902_1502; -. DR EnsemblBacteria; ABB26460; ABB26460; Syncc9902_1502. DR GeneID; 3741854; -. DR KEGG; sye:Syncc9902_1502; -. DR PATRIC; 23800433; VBISynSp76179_1672. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSP316279:GJCI-1514-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 122 Unknown (By similarity). FT REGION 123 346 Thiamine-phosphate synthase (By FT similarity). FT REGION 174 178 HMP-PP binding (By similarity). FT METAL 207 207 Magnesium (By similarity). FT METAL 226 226 Magnesium (By similarity). FT BINDING 206 206 HMP-PP (By similarity). FT BINDING 245 245 HMP-PP (By similarity). FT BINDING 274 274 HMP-PP (By similarity). FT BINDING 301 301 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 346 AA; 37964 MW; F2F6C8EC2F495596 CRC64; MRLVDPRVAR LIDANLDRSR EGLRVVEDWC RFGLERDDLV VQLKDWRQRL GRLHRSTYKQ ARSTATDPGA GLSHPAQLER DNPQAVVAAN CGRVQEALRV LEEYGRSIDP SLASESAAIR YGLYDLEVTC LNASLGNARR QTLNNCQLCL ITTPCPDLIE RVRQSLTAGV TMVQYRCKSG NDRERLDEAK ALRMLCQTHG ALFVINDRID LALAVDADGV HLGQDDLPTD VARDLIGEAR LLGRSTHTLD DVRRADTEAC DYLGLGPVHT TAVKPEKAAI GPVRLQDAQA LTRLPVFAIG GIELKNITAL LDVGCRRVAV IGAIMAAENP ESASQQLLQA LLPPVD // ID Q3B4B0_PELLD Unreviewed; 214 AA. AC Q3B4B0; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 53. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=Plut_0959; OS Pelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM OS 273)). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Pelodictyon. OX NCBI_TaxID=319225; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 273; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Pelodictyon luteolum DSM 273."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000096; ABB23821.1; -; Genomic_DNA. DR RefSeq; YP_374864.1; NC_007512.1. DR ProteinModelPortal; Q3B4B0; -. DR STRING; 319225.Plut_0959; -. DR EnsemblBacteria; ABB23821; ABB23821; Plut_0959. DR GeneID; 3745371; -. DR KEGG; plt:Plut_0959; -. DR PATRIC; 21379486; VBIChlLut1287_1008. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INERSDI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PLUT319225:GHDM-965-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 214 AA; 22771 MW; FEBB59A33768905B CRC64; MKARTPSSAP LPRITVISSP ATSTQVGSGT ESLLLRLAGA PPCMILIREK HLSGRQLFAL ARDARKLPLT AGSRLLVSER IDIALTVGLD GVHLPEEACP LHLLRKAAPS LIFGRSVHSL RDAVAAEEAG AGYLFFSPVY STPSKLAFGP PQGTEKLREV CRAVSIPVYA LGGITLERTK ECMECGAWGI AAISLFSGSE HLPSTIENLY RITG // ID Q3BPQ0_XANC5 Unreviewed; 240 AA. AC Q3BPQ0; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 69. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=XCV3532; OS Xanthomonas campestris pv. vesicatoria (strain 85-10). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=316273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=85-10; RX PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005; RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., RA Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., RA Bonas U., Bartels D., Kaiser O.; RT "Insights into genome plasticity and pathogenicity of the plant RT pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed RT by the complete genome sequence."; RL J. Bacteriol. 187:7254-7266(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM039952; CAJ25263.1; -; Genomic_DNA. DR RefSeq; YP_365263.1; NC_007508.1. DR ProteinModelPortal; Q3BPQ0; -. DR STRING; 316273.XCV3532; -. DR EnsemblBacteria; CAJ25263; CAJ25263; XCV3532. DR GeneID; 3730429; -. DR KEGG; xcv:XCV3532; -. DR PATRIC; 24096670; VBIXanCam71633_3804. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XCAM316273:GJF8-3635-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 66 70 HMP-PP binding (By similarity). FT REGION 164 166 THZ-P binding (By similarity). FT REGION 213 214 THZ-P binding (By similarity). FT METAL 99 99 Magnesium (By similarity). FT METAL 118 118 Magnesium (By similarity). FT BINDING 98 98 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 167 167 HMP-PP (By similarity). FT BINDING 193 193 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 240 AA; 24999 MW; B5A52E6FD8B13FAA CRC64; MSRSSDNRGH ATVGLHCPIP STAFGSVAMP NRLDVRGVYL ITPDEPNTQR LLLRTAPLLG SITWLQYRNK QADAALRLRQ AGALREACAA HGVPLIINDD AQLAAQVGAQ GVHLGEDDGD VAAARALLGE QAIIGVSSYD DIERARAAAE AGANYVAFGA FFPTTTKQTT RRATPALLQQ AAELNLPRVA IGGIAPAQVT ALVTAGADLI AVVSGVYAAP DPVAAVQEYR AGFAAQRGKL // ID Q3BXE2_XANC5 Unreviewed; 315 AA. AC Q3BXE2; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 66. DE SubName: Full=Putative NUDIX hydrolase family / thiamine monophosphate synthase fusionprotein; GN OrderedLocusNames=XCV0840; OS Xanthomonas campestris pv. vesicatoria (strain 85-10). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=316273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=85-10; RX PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005; RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., RA Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., RA Bonas U., Bartels D., Kaiser O.; RT "Insights into genome plasticity and pathogenicity of the plant RT pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed RT by the complete genome sequence."; RL J. Bacteriol. 187:7254-7266(2005). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM039952; CAJ22471.1; -; Genomic_DNA. DR RefSeq; YP_362571.1; NC_007508.1. DR ProteinModelPortal; Q3BXE2; -. DR STRING; 316273.XCV0840; -. DR EnsemblBacteria; CAJ22471; CAJ22471; XCV0840. DR GeneID; 3731810; -. DR KEGG; xcv:XCV0840; -. DR PATRIC; 24091068; VBIXanCam71633_1046. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XCAM316273:GJF8-855-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34949 MW; 1F053438483BAD82 CRC64; MPDSLRSIHV VAGVITDPRG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIEAQVGD WVMEVPQLYP DKRLRLEVRH ITSWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGAL RQPDRYLITP EPEDEARWLE GLELALHNGI TRIQLRARQL APARWQALLQ QVMRLRGRAR AQLLLNRDIA LAADLGIGVH LGSEQLAGLQ ERPLPADRLV AASCHGLDDL RHAQRIGCDF AVLGPVQATA SHPGATPIGW DGFETLREQV WLPIYALGGM QGEDVRQARS HGAQGIAAIR ALWPQ // ID Q3D320_STRAG Unreviewed; 223 AA. AC Q3D320; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 16-APR-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAI_0921; OS Streptococcus agalactiae H36B. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=342615; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=H36B; RX PubMed=16172379; DOI=10.1073/pnas.0506758102; RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D., RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., RA Deboy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., RA Peterson J.D., Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A., RA Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N., RA Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J., RA Smith S., Utterback T.R., White O., Rubens C.E., Grandi G., RA Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R., RA Fraser C.M.; RT "Genome analysis of multiple pathogenic isolates of Streptococcus RT agalactiae: implications for the microbial 'pan-genome'."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJS01000011; EAO78635.1; -; Genomic_DNA. DR ProteinModelPortal; Q3D320; -. DR EnsemblBacteria; EAO78635; EAO78635; SAI_0921. DR PATRIC; 25720626; VBIStrAga45836_0579. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24635 MW; C8592610981AB9B1 CRC64; MKDTLKLYFV CGTVDCSRKN ILTVVEEALQ AGITLFQFRE KGFTALQGKE KIAMAKQLQI LCKQYQVPFI IDDDIDLVEL IDADGLHIGQ NDLPVDEARR RLPDKIIGLS VSTMDEYQKS QLSVVDYIGI GPFNPTQSKA DAKPAVGNRT TKAVREINQD IPIVAIGGIT SDFVHDIIES GADGIAVISA ISKANHIVDA TRQLRYEVEK ALVNRQKHSD VIK // ID Q3D6X7_STRAG Unreviewed; 223 AA. AC Q3D6X7; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 16-APR-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAN_0943; OS Streptococcus agalactiae COH1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=342616; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=COH1; RX PubMed=16172379; DOI=10.1073/pnas.0506758102; RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D., RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., RA Deboy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., RA Peterson J.D., Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A., RA Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N., RA Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J., RA Smith S., Utterback T.R., White O., Rubens C.E., Grandi G., RA Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R., RA Fraser C.M.; RT "Genome analysis of multiple pathogenic isolates of Streptococcus RT agalactiae: implications for the microbial 'pan-genome'."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJR01000052; EAO75239.1; -; Genomic_DNA. DR ProteinModelPortal; Q3D6X7; -. DR EnsemblBacteria; EAO75239; EAO75239; SAN_0943. DR PATRIC; 25717555; VBIStrAga70477_1584. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24591 MW; BE824D7D2C0AFCA5 CRC64; MKDTLKLYFV CGTVDCSRKN ILTVVEEALQ AGITLFQFRE KGFTALQGKE KIAMAKQLQI LCKQYQVPFI IDDDIDLVEL IDADGLHIGQ NDLPVDEARR RLPDKIIGLS VSTMAEYQKS QLSVVDYIGI GPFNPTQSKA DAKPAVGNRT TKAVREINQD IPIVAIGGIT SDFVHDIIES GADGIAVISA ISKANHIVDA TRQLRYEVEK ALVNRQKHSD VIK // ID Q3DGZ7_STRAG Unreviewed; 223 AA. AC Q3DGZ7; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 16-APR-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAM_0868; OS Streptococcus agalactiae CJB111. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=342617; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CJB111; RX PubMed=16172379; DOI=10.1073/pnas.0506758102; RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D., RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., RA Deboy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., RA Peterson J.D., Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A., RA Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N., RA Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J., RA Smith S., Utterback T.R., White O., Rubens C.E., Grandi G., RA Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R., RA Fraser C.M.; RT "Genome analysis of multiple pathogenic isolates of Streptococcus RT agalactiae: implications for the microbial 'pan-genome'."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJQ01000003; EAO74208.1; -; Genomic_DNA. DR ProteinModelPortal; Q3DGZ7; -. DR EnsemblBacteria; EAO74208; EAO74208; SAM_0868. DR PATRIC; 25710169; VBIStrAga57283_0268. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24635 MW; C8592610981AB9B1 CRC64; MKDTLKLYFV CGTVDCSRKN ILTVVEEALQ AGITLFQFRE KGFTALQGKE KIAMAKQLQI LCKQYQVPFI IDDDIDLVEL IDADGLHIGQ NDLPVDEARR RLPDKIIGLS VSTMDEYQKS QLSVVDYIGI GPFNPTQSKA DAKPAVGNRT TKAVREINQD IPIVAIGGIT SDFVHDIIES GADGIAVISA ISKANHIVDA TRQLRYEVEK ALVNRQKHSD VIK // ID Q3DND4_STRAG Unreviewed; 223 AA. AC Q3DND4; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 16-APR-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAL_0899; OS Streptococcus agalactiae 515. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=342614; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=515; RX PubMed=16172379; DOI=10.1073/pnas.0506758102; RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D., RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., RA Deboy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., RA Peterson J.D., Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A., RA Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N., RA Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J., RA Smith S., Utterback T.R., White O., Rubens C.E., Grandi G., RA Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R., RA Fraser C.M.; RT "Genome analysis of multiple pathogenic isolates of Streptococcus RT agalactiae: implications for the microbial 'pan-genome'."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJP01000006; EAO71921.1; -; Genomic_DNA. DR ProteinModelPortal; Q3DND4; -. DR EnsemblBacteria; EAO71921; EAO71921; SAL_0899. DR PATRIC; 25705448; VBIStrAga41311_0308. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24610 MW; BE824D7D2C1F1CA5 CRC64; MKDTLKLYFV CGTVDCSRKN ILTVVEEALQ AGITLFQFRE KGFTALQGKE KIAMAKQLQI LCKQYQVPFI IDDDIDLVEL IDADGLHIGQ NDLPVDEARR RLPDKIIGLS VSTMAEYQKS QLSVVDYIGI GPFNPTQSKA DAKPAVGNRT TKAVREINQD IPIVAIGGIT SDFVHDIIES GADGIAVISA ISKANHIVDA TRQLRYEVEK ALVNRQKRSD VIK // ID Q3DQF7_STRAG Unreviewed; 177 AA. AC Q3DQF7; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 16-APR-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=SAJ_0895; OS Streptococcus agalactiae 18RS21. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=342613; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=18RS21; RX PubMed=16172379; DOI=10.1073/pnas.0506758102; RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D., RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., RA Deboy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., RA Peterson J.D., Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A., RA Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N., RA Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J., RA Smith S., Utterback T.R., White O., Rubens C.E., Grandi G., RA Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R., RA Fraser C.M.; RT "Genome analysis of multiple pathogenic isolates of Streptococcus RT agalactiae: implications for the microbial 'pan-genome'."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJO01000134; EAO61771.1; -; Genomic_DNA. DR ProteinModelPortal; Q3DQF7; -. DR EnsemblBacteria; EAO61771; EAO61771; SAJ_0895. DR PATRIC; 38568616; VBIStrAga107603_1755. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 177 AA; 19774 MW; 21FF4D5850EF994F CRC64; MKDTLKLYFV CGTVDCSRKN ILTVVEEALQ AGITLFQFRE KGFTALQGKE KIAMAKQLQI LCKQYQVPFI IDDDIDLVEL IDADGLHIGQ NDLPVDEARR RLPDKIIGLS VSTMDEYQKS QLSVVDYIGI GPFNPTQSKA DAKPAVGNRT TKAVRENYQI FPSVHRGGIT SDFVHDI // ID Q3DTW1_STRAG Unreviewed; 223 AA. AC Q3DTW1; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 16-APR-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SAJ_0899, SAJ_2416; OS Streptococcus agalactiae 18RS21. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=342613; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=18RS21; RX PubMed=16172379; DOI=10.1073/pnas.0506758102; RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D., RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., RA Deboy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., RA Peterson J.D., Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A., RA Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N., RA Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J., RA Smith S., Utterback T.R., White O., Rubens C.E., Grandi G., RA Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R., RA Fraser C.M.; RT "Genome analysis of multiple pathogenic isolates of Streptococcus RT agalactiae: implications for the microbial 'pan-genome'."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJO01000188; EAO61563.1; -; Genomic_DNA. DR EMBL; AAJO01000019; EAO62990.1; -; Genomic_DNA. DR EnsemblBacteria; EAO61563; EAO61563; SAJ_2416. DR EnsemblBacteria; EAO62990; EAO62990; SAJ_0899. DR PATRIC; 38566001; VBIStrAga107603_0543. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24635 MW; C8592610981AB9B1 CRC64; MKDTLKLYFV CGTVDCSRKN ILTVVEEALQ AGITLFQFRE KGFTALQGKE KIAMAKQLQI LCKQYQVPFI IDDDIDLVEL IDADGLHIGQ NDLPVDEARR RLPDKIIGLS VSTMDEYQKS QLSVVDYIGI GPFNPTQSKA DAKPAVGNRT TKAVREINQD IPIVAIGGIT SDFVHDIIES GADGIAVISA ISKANHIVDA TRQLRYEVEK ALVNRQKHSD VIK // ID Q3EQX5_BACTI Unreviewed; 173 AA. AC Q3EQX5; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 16-OCT-2013, entry version 32. DE SubName: Full=Regulatory protein TENI; GN ORFNames=RBTH_03631; OS Bacillus thuringiensis serovar israelensis ATCC 35646. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=339854; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35646; RA Anderson I., Sorokin A., Kapatral V., Reznik G., Bhattacharya A., RA Mikhailova N., Burd H., Joukov V., Kaznadzey D., Walunas T., RA D'Souza M., Larsen N., Pusch G., Liolios K., Grechkin Y., Lapidus A., RA Goltsman E., Chu L., Fonstein M., Ehrlich D., Overbeek R., RA Kyrpides N., Ivanova N.; RT "Comparative genome analysis of Bacillus cereus group genomes with RT Bacillus subtilis."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJM01000223; EAO53705.1; -; Genomic_DNA. DR EnsemblBacteria; EAO53705; EAO53705; RBTH_03631. DR PATRIC; 38351779; VBIBacThu7829_4092. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 173 AA; 19756 MW; 7EA15CF5C0AB88A1 CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLMEGFPA SKIVINDRID IAILLNIPRV QLGYRSTDVK SVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEISDIARC LSIPITLLEE LLLRIQRIFW QVK // ID Q3EYR6_BACTI Unreviewed; 222 AA. AC Q3EYR6; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 19-FEB-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RBTH_06998; OS Bacillus thuringiensis serovar israelensis ATCC 35646. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=339854; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35646; RA Anderson I., Sorokin A., Kapatral V., Reznik G., Bhattacharya A., RA Mikhailova N., Burd H., Joukov V., Kaznadzey D., Walunas T., RA D'Souza M., Larsen N., Pusch G., Liolios K., Grechkin Y., Lapidus A., RA Goltsman E., Chu L., Fonstein M., Ehrlich D., Overbeek R., RA Kyrpides N., Ivanova N.; RT "Comparative genome analysis of Bacillus cereus group genomes with RT Bacillus subtilis."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAJM01000023; EAO56445.1; -; Genomic_DNA. DR ProteinModelPortal; Q3EYR6; -. DR EnsemblBacteria; EAO56445; EAO56445; RBTH_06998. DR PATRIC; 38345528; VBIBacThu7829_1089. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23955 MW; 180CFC6889BF439A CRC64; MKHTMRIETK KMSKLLQVYF IMGSNNCTRD PLAVLKEALD GGVTLFQFRE KGEGSLIGGD RVRFAKELQT LCKEYSVPFI VNDDVELAIE LDADGVHVGQ NDEGITSVRE KMGDKIIGVS AHTIEEARFA IENGADYLGV GPIFPTSTKK DTKAVQGTKG LAYFREQGIT VPIVGIGGIT IENTAAVIEA GADGVSVISA ISLAESAYES TRKLAEEVKR SL // ID Q3IFN5_PSEHT Unreviewed; 508 AA. AC Q3IFN5; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 66. DE SubName: Full=Putative phosphomethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE EC=2.7.4.7; GN Name=thiDE; OrderedLocusNames=PSHAa0484; OS Pseudoalteromonas haloplanktis (strain TAC 125). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=326442; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TAC 125; RX PubMed=16169927; DOI=10.1101/gr.4126905; RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., RA Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., RA Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., RA Danchin A.; RT "Coping with cold: the genome of the versatile marine Antarctica RT bacterium Pseudoalteromonas haloplanktis TAC125."; RL Genome Res. 15:1325-1335(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR954246; CAI85580.1; -; Genomic_DNA. DR RefSeq; YP_339023.1; NC_007481.1. DR ProteinModelPortal; Q3IFN5; -. DR STRING; 326442.PSHAa0484; -. DR EnsemblBacteria; CAI85580; CAI85580; PSHAa0484. DR GeneID; 3710277; -. DR KEGG; pha:PSHAa0484; -. DR PATRIC; 32294487; VBIPseHal105694_0460. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PHAL326442:GJIU-488-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 508 AA; 54755 MW; D57957A6FB489019 CRC64; MNNVVWTIAG SDSGGGAGIQ ADIKAMQSFG VHGCTAITAL TAQNSLGVEA INAVSTDIIE SQLLALEKDM KAKVIKIGML ANVQQIQLIS EHISHYKAKW PVPPVIVYDP VAIASSGDLL TEEDTVSAIK ECLLPLVDVI TPNTHETQLL TGVYLIGPAA IKEAANKLLS WGAKAVVIKG GHWDYPSGYC IDYCINNFTQ KGEEYWLGNE KIQTPHNHGT GCSMASVIAA CLAKDYPLKD AFILAKAYIN QGLKVAVRYG EGIGPVAQTS FPTNLADYPQ VIEAGSWLGD ELDFDVPLDF NMAADFAPCE SKSLGLYAVV DSVDWLEKCL QQGVKTVQLR VKNKDDAQLD ELVAKAVALG EQYNAQVFIN DYWQLAIKHG AYGVHLGQQD LENTNLAAIK NAGLRLGLST HGFYEMLRAH NYRPSYLAFG AIYPTTTKDM TGQIQGLEKL FKFVPLMQSY PTVAIGGIDL KRASQVAKTG VGSVAVVRAI SEADDYVQAI SALQAAIN // ID Q3IXX2_RHOS4 Unreviewed; 206 AA. AC Q3IXX2; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 48. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN ORFNames=RSP_3828; OS Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM OS 158). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=272943; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., RA Kaplan S.; RT "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000144; ABA80612.1; -; Genomic_DNA. DR RefSeq; YP_354513.1; NC_007494.2. DR ProteinModelPortal; Q3IXX2; -. DR STRING; 272943.RSP_3828; -. DR EnsemblBacteria; ABA80612; ABA80612; RSP_3828. DR GeneID; 3721410; -. DR KEGG; rsp:RSP_3828; -. DR PATRIC; 23156120; VBIRhoSph57909_3415. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; RSPH272943:GJAS-3122-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome; Transferase. SQ SEQUENCE 206 AA; 22171 MW; 11DDB967817BEAEA CRC64; MAEVERPQLY LVTPPEIDLE IFPDRLAAVL DSTEVACLRL ALAGKDEDRI ARTGDALREV AHARDVALVI ENHVLMVERL GLDGVHLTDG ARLVRKLRKD LGPDAILGAF CGRTRHEGIN AAEAGADYVA FGPVGTTALG DGSLAEAELF GWWSEMIEVP VVAEGALTPE KVAELAPLTD FFAVGEEIWR EEDAAAALRR LLAPLG // ID Q3J062_RHOS4 Unreviewed; 203 AA. AC Q3J062; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=RSP_0648; OS Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM OS 158). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=272943; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., RA Kaplan S.; RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000143; ABA79822.1; -; Genomic_DNA. DR RefSeq; YP_353723.1; NC_007493.2. DR ProteinModelPortal; Q3J062; -. DR STRING; 272943.RSP_0648; -. DR EnsemblBacteria; ABA79822; ABA79822; RSP_0648. DR GeneID; 3718297; -. DR KEGG; rsp:RSP_0648; -. DR PATRIC; 23154455; VBIRhoSph57909_2598. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RSPH272943:GJAS-2312-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 203 AA; 20386 MW; 7E48C40474FAF26D CRC64; MNLSLYFVTP DGAEGLEQLV AAAVRGGATL VQLRDKHRSD AELIPLARRL VAALDAQGVP LIVNDRIEVV LASGAAGLHV GQGDLGVAEA RRRIGPDRLL GLSVEAPEHL EALPLGIVDY VGAGPVRATA SKPDHAPPIG FEGLARLVAA APVPAVAIGG LGAGDAHAVK AAGAAGMAIV SAIGAAADPE AAARALALEW ERA // ID Q3JEB2_NITOC Unreviewed; 321 AA. AC Q3JEB2; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 63. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=Noc_0306; OS Nitrosococcus oceani (strain ATCC 19707 / NCIMB 11848). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=323261; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19707 / NCIMB 11848; RX PubMed=16957257; DOI=10.1128/AEM.00463-06; RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., RA Poret-Peterson A.T., Vergez L.M., Ward B.B.; RT "Complete genome sequence of the marine, chemolithoautotrophic, RT ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707."; RL Appl. Environ. Microbiol. 72:6299-6315(2006). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000127; ABA56834.1; -; Genomic_DNA. DR RefSeq; YP_342364.1; NC_007484.1. DR ProteinModelPortal; Q3JEB2; -. DR STRING; 323261.Noc_0306; -. DR EnsemblBacteria; ABA56834; ABA56834; Noc_0306. DR GeneID; 3706477; -. DR KEGG; noc:Noc_0306; -. DR PATRIC; 22704316; VBINitOce57959_0402. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NOCE323261:GCI3-310-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 321 AA; 35262 MW; F731BA7BB7EC631E CRC64; MVLQVAAGAI FNRQGQVLLS KRPLHVHQGN LWEFPGGKLK PGEEVRQALS RELWEELGIQ VLQARPLLQV HHDYPDRSVL LHVWRVDRFS GTPKGQEGQP VVWVSPENLN AYPLPAANHA VVTAVCLPPT YLITKEPAGN QMAFLSSLRQ SLQAGVQLVQ LRAKKLSPEH YQNLTWKVQR LCFEYKAILL VNTVPAQAAE WGADGVHLTG NHLMHLSHRP LPANKWVAAS CHNAAQLAHA ANIGVDFAVL GPVFHTSTHP QALPLGWERF QTLIAQIPFP VYALGGVGPE HLKEAWSRGA QGIAAIRALW GDRAGSFGVS P // ID Q3JK67_BURP1 Unreviewed; 196 AA. AC Q3JK67; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 56. DE SubName: Full=DGTP-pyrophosphohydrolase thiamine phosphate synthase; DE EC=2.5.1.3; GN Name=thiE2; OrderedLocusNames=BURPS1710b_A0878; OS Burkholderia pseudomallei (strain 1710b). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320372; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1710b; RA Woods D.E., Nierman W.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000125; ABA51630.1; -; Genomic_DNA. DR RefSeq; YP_336036.1; NC_007435.1. DR ProteinModelPortal; Q3JK67; -. DR STRING; 320372.BURPS1710b_A0878; -. DR EnsemblBacteria; ABA51630; ABA51630; BURPS1710b_A0878. DR GeneID; 3694312; -. DR KEGG; bpm:BURPS1710b_A0878; -. DR PATRIC; 19242173; VBIBurPse115837_4924. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPSE320372:GBYB-4676-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Transferase. SQ SEQUENCE 196 AA; 20321 MW; 6128620A8545801F CRC64; MHDDLALPPY YLITPEPASG SDADLAAFLD RLSDALATGL TLVQLRVKTL DAPAYAALAA GALARCRAQR ARMIVNGPIA VEAALALGAA GVHLGSAALR AATARPLGSE GLLSAACHSL DELRHAQRIG ADLATLSPVL PTLTHPGAPT LGWTRFAECA AHTRVPVYAL GGMTRTHLET ARAHHAHGIA SIRGLW // ID Q3JM34_BURP1 Unreviewed; 212 AA. AC Q3JM34; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 55. DE SubName: Full=DGTP-pyrophosphohydrolase thiamine phosphate synthase; DE EC=2.5.1.3; GN Name=thiE2; OrderedLocusNames=BURPS1710b_A0210; OS Burkholderia pseudomallei (strain 1710b). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320372; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1710b; RA Woods D.E., Nierman W.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000125; ABA52874.1; -; Genomic_DNA. DR RefSeq; YP_335369.1; NC_007435.1. DR ProteinModelPortal; Q3JM34; -. DR STRING; 320372.BURPS1710b_A0210; -. DR EnsemblBacteria; ABA52874; ABA52874; BURPS1710b_A0210. DR GeneID; 3692783; -. DR KEGG; bpm:BURPS1710b_A0210; -. DR PATRIC; 19240673; VBIBurPse115837_4175. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VTDRTLC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPSE320372:GBYB-4008-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Transferase. SQ SEQUENCE 212 AA; 22904 MW; 57980D4D05E67B05 CRC64; MIESIIHRHL KIIVNKSANL PSEYLITPEP PGDEALSDYL ATLERTLKAG ISLVQLRAKA VTAPYYARLT EYALACCRRY NARLLVNAAP EVARGLHTDG VHLTSTRLMT CSTRPLPAGL LVSAACHDED QVRHADSIGV DLITISPVMP TATHTTAEPL GWPRFRELAT LTSVPVYALG GMSVDSLAEA RNAGAYGIAA IRAFWGSNVD RS // ID Q3JMY4_BURP1 Unreviewed; 367 AA. AC Q3JMY4; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 67. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=BURPS1710b_3705; OS Burkholderia pseudomallei (strain 1710b). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320372; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1710b; RA Woods D.E., Nierman W.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000124; ABA47735.1; -; Genomic_DNA. DR RefSeq; YP_335069.1; NC_007434.1. DR ProteinModelPortal; Q3JMY4; -. DR STRING; 320372.BURPS1710b_3705; -. DR EnsemblBacteria; ABA47735; ABA47735; BURPS1710b_3705. DR GeneID; 3691886; -. DR KEGG; bpm:BURPS1710b_3705; -. DR PATRIC; 19240026; VBIBurPse115837_3856. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BPSE320372:GBYB-3704-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Transferase. SQ SEQUENCE 367 AA; 38315 MW; 3E9B351CCB7F5C2B CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW PRPAVRTRIC LAPPEQPRAA DLWVAIAGDA GAHAAHIARL NAAGARAIVI DDASATLHTG AARHALASRA PLADDWIAAL AAFLDCGFAA SDALVLALAW RDGDEARGGD PWPVDPARFP RVLGLPAAPE PAFAPCPQRL GLYPVLPSAE WVERVLDCGV RTVQLRVKDA SPDALRAEIE RAVAAGRRHP DARVFINDHW RLALDAGAYG VHLGQEDLET ADLGAIARAG ARLGLSSHGY YEMLVALQFK PSYLALGPVF ATATKAVAAP PQGLARLARY VRFAGPQAPL VAIGGIAPDT LGAVLAAGVG SAAVVSAITA AADYREAIVA LQQNFGR // ID Q3K7U2_PSEPF Unreviewed; 314 AA. AC Q3K7U2; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 77. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=Pfl01_4425; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pf0-1; RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51; RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R., RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M., RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J., RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L., RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K., RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M., RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.; RT "Genomic and genetic analyses of diversity and plant interactions of RT Pseudomonas fluorescens."; RL Genome Biol. 10:R51.1-R51.16(2009). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000094; ABA76162.1; -; Genomic_DNA. DR RefSeq; YP_350153.1; NC_007492.2. DR ProteinModelPortal; Q3K7U2; -. DR STRING; 205922.Pfl01_4425; -. DR EnsemblBacteria; ABA76162; ABA76162; Pfl01_4425. DR GeneID; 3713464; -. DR KEGG; pfo:Pfl01_4425; -. DR PATRIC; 19891004; VBIPseFlu44242_4429. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PFLU205922:GJBD-4491-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 33845 MW; 303EB9C45B6983E2 CRC64; MKRVHVAAAV IRDGSGKILI ARRADTQHQG GLWEFPGGKV EADESVQTAL ARELHEELGI VVGAARPLIK VRHDYPDKQV LLDVWEVSSF TGEPHGAEGQ PLAWVSAREL TDYEFPAANQ PIVAAARLPA EYLITPEDLE TPALLRGIQK AIAGGIKLIQ LRAPNGYDPK YRDLAVDAVG LCAGKAQLMI KGPFEWLGDF PAAGWHITSA QLRKYAAAGR PLPAERWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWEQ ASTLIEGFSK PVFLLGGVGP AEREKAWNAG AQGVAGIRAF WPEA // ID Q3M2Z2_ANAVT Unreviewed; 379 AA. AC Q3M2Z2; DT 25-OCT-2005, integrated into UniProtKB/TrEMBL. DT 25-OCT-2005, sequence version 1. DT 14-MAY-2014, entry version 62. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Ava_5047; OS Anabaena variabilis (strain ATCC 29413 / PCC 7937). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena. OX NCBI_TaxID=240292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29413 / PCC 7937; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.; RT "Complete sequence of Anabaena variabilis ATCC 29413."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000117; ABA24644.1; -; Genomic_DNA. DR RefSeq; YP_325539.1; NC_007413.1. DR ProteinModelPortal; Q3M2Z2; -. DR STRING; 240292.Ava_5047; -. DR EnsemblBacteria; ABA24644; ABA24644; Ava_5047. DR GeneID; 3683528; -. DR KEGG; ava:Ava_5047; -. DR PATRIC; 35431665; VBIAnaVar43351_6349. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AVAR240292:GCY3-5112-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 157 Unknown (By similarity). FT REGION 158 379 Thiamine-phosphate synthase (By FT similarity). FT REGION 205 209 HMP-PP binding (By similarity). FT REGION 302 304 THZ-P binding (By similarity). FT METAL 238 238 Magnesium (By similarity). FT METAL 257 257 Magnesium (By similarity). FT BINDING 237 237 HMP-PP (By similarity). FT BINDING 276 276 HMP-PP (By similarity). FT BINDING 305 305 HMP-PP (By similarity). FT BINDING 332 332 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 379 AA; 42304 MW; CDE885B2005CB9B7 CRC64; MQILDARNIA NMKEAGYYDE SITNGVVVMV EPYSQQKQIQ QVVYRILDAN LDRAREGLRI IEEWCRFGLN SGQLAGECKY LRQEVAVWHT EELRAARDTA GDPGTDLSHP HEEQRSSIKA LLQANFCRVE EALRVLEEYG KLYHPKMGQA CKQMRYRVYS LETNLMGHQR HQLLRRSRLY LVTSPSESLL PTVEAALKGG LTLLQYRDKD ADDSVRLELA TKLRQLCHSY GALFIINDRV DLALAVDADG VHLGQQDMPI ATARQLLGPQ RLIGRSTTNA DEMQRAIAEG ADYIGVGPVY ETPTKVGKAA AGLGYVSYAA QHSSVPWFAI GGIDANNIND VIDAGAERVA VVRSLMQAEQ PTLVTQYLIS QLHRIQPES // ID Q3MSL9_PLAFA Unreviewed; 538 AA. AC Q3MSL9; DT 25-OCT-2005, integrated into UniProtKB/TrEMBL. DT 25-OCT-2005, sequence version 1. DT 19-FEB-2014, entry version 32. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OS Plasmodium falciparum. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=5833; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3D7; RX PubMed=16497163; DOI=10.1515/BC.2006.007; RA Wrenger C., Eschbach M.L., Muller I.B., Laun N.P., Begley T.P., RA Walter R.D.; RT "Vitamin B1 de novo synthesis in the human malaria parasite Plasmodium RT falciparum depends on external provision of 4-amino-5-hydroxymethyl-2- RT methylpyrimidine."; RL Biol. Chem. 387:41-51(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ938174; CAI79613.1; -; mRNA. DR ProteinModelPortal; Q3MSL9; -. DR SMR; Q3MSL9; 11-256. DR eggNOG; COG0352; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 2. PE 2: Evidence at transcript level; KW Transferase. SQ SEQUENCE 538 AA; 62651 MW; 54FF307A7EC6F3EE CRC64; MNIGKSGKSL KKCVDYSLYL VTDDKFLKDK ENVCGTFVNK IIQGVLGGVG LIQLRLKKSD DIYFYNTAVK MKNLLLPFNV PLIINNRLDI CLSVNADGVH LGKSDLPLYH ARNILGENKI IGATINFSDE KDIEMCINNK IDYIAHDHTL YESTTKKTIV SNEQGLKEQI QILENKIKYL YHKGKIIKSH NNTDDNFKNI IPPIILIGGI NTNNIQNTMI SFSNTCEGLA VVSCILDENS PSFVNTLKLK YIIDKYKKSD HVAFINMYSN CLNYLYYQHI EIEEQLNLPI IFHSTKKKNI NTFLVTNMIL DKNKSYFIPF KNNDYFDIIS LNEFFKNNEK ANLFLFHSSY DLFLNNNNKI DNNINGILNK EKHDDHIYEN IKEQIIKRII QLKHIKKEHM GHNIFILIGE EIWDLFNKHC YPQFFNSNFF FVIKKHSTIQ STMSEQWLYY DTQNACIQYN HNIINIFLKN AHFFSEENIK KFTLLMSYFL IVQDKEITPQ FLQQIATQGG TNFHEQTLWK FIATVDISLK LVEKSMGI // ID Q3RCE6_XYLFS Unreviewed; 204 AA. AC Q3RCE6; DT 25-OCT-2005, integrated into UniProtKB/TrEMBL. DT 25-OCT-2005, sequence version 1. DT 19-FEB-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=XfasaDRAFT_0269; OS Xylella fastidiosa Dixon. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=155919; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Dixon; RA DOE Joint Genome Institute; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Dixon; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M.; RT "Annotation of the draft genome assembly of Xylella fastidiosa RT Dixon."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Dixon; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T., RA Hammon N., Israni S., Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of Xylella fastidiosa RT Dixon."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAAL02000015; EAO12349.1; -; Genomic_DNA. DR ProteinModelPortal; Q3RCE6; -. DR EnsemblBacteria; EAO12349; EAO12349; XfasaDRAFT_0269. DR PATRIC; 26341647; VBIXylFas50652_2675. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21961 MW; 3D83B679BAFD11BD CRC64; MSQPRGIYLI TPDETDTARL IARTAPLLNG IVWLQYRNKL ANTALRTEQA QALLALCRPT GIPLLINDDL ELAQTIGADG VHLGMHDSNP SIARAQLGPH AIIGVSCYNQ IERAKQAIKA GASYVGFGAF YPSHTKTTPY RATPELLHQT THLGVPRVAI GGLTPKNIAP IIEAGAELLA VISGIYSAKN PITALKAYQY QFNI // ID Q3RDV2_XYLFS Unreviewed; 320 AA. AC Q3RDV2; DT 25-OCT-2005, integrated into UniProtKB/TrEMBL. DT 25-OCT-2005, sequence version 1. DT 19-FEB-2014, entry version 51. DE SubName: Full=Mutator MutT; GN ORFNames=XfasaDRAFT_0784; OS Xylella fastidiosa Dixon. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=155919; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Dixon; RA DOE Joint Genome Institute; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Dixon; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M.; RT "Annotation of the draft genome assembly of Xylella fastidiosa RT Dixon."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Dixon; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T., RA Hammon N., Israni S., Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of Xylella fastidiosa RT Dixon."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAAL02000008; EAO12848.1; -; Genomic_DNA. DR ProteinModelPortal; Q3RDV2; -. DR EnsemblBacteria; EAO12848; EAO12848; XfasaDRAFT_0784. DR PATRIC; 26340355; VBIXylFas50652_2045. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 320 AA; 35355 MW; D455D4A933B399C9 CRC64; MTDSLRSIHV VAAVIVDVRG RLLLSRRTEN SDMPGLWEFP GGKRESGETS EQALARELYE ELGISADVGE WLMEVPQLYP GKRLRLEVRR VRAWKGGLRG REGQALTWVE PDKLLRYSMP PADQPVVGML RQPAHYLVTP EPGEKDAEWL DAVEHAYRLG IERIQLRMRQ HDPARWSGLV REAVQRRGRA HVEVLLNRDI ALAEALGIGV HLGAEQLAVL YARPLPVGLP VGASCHCLAD LCHAQRIGCD FAVLGPVLPT ESHPGAVTLG WEGFEQLREQ VALPIYAIGG MCADQVKEAR RHGAQGIAAM RGLWPGGAKQ // ID Q3SA80_9EURY Unreviewed; 208 AA. AC Q3SA80; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 19-FEB-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thieE; Synonyms=thiE; OS uncultured euryarchaeote Alv-FOS4. OC Archaea; Euryarchaeota; environmental samples. OX NCBI_TaxID=337893; RN [1] RP NUCLEOTIDE SEQUENCE. RA Moussard H., Hennecke G., Moreira D., Jouffe V., Lopez-Garcia P., RA Jeanthon C.; RT "A hyperthermophilic lifestyle for uncultured Archaea of the DHVE2 RT lineage: evidence from environmental genomics."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ118404; AAZ32502.1; -; Genomic_DNA. DR ProteinModelPortal; Q3SA80; -. DR SMR; Q3SA80; 2-203. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 179 180 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 159 159 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21973 MW; 59411A7E221CF2B7 CRC64; MLTEKLRLYV ILPDSKNAPA LAEKALQGGA TAVQLRMKGT GDRECLQIAR KVRRITREYD ALFIVDDRVD VALLSDADGV HLGAEDLPVK DVRELAPNLI IGATVRSVES AKSAEKEGAD YLGVGSIYPS PSKDAPVIGV QTLKELASSV NIPVVAIGGI TEKNVAEVIA AGAAGVAVLS AIFSSENVRE KTTLLRRSVD SALARRGT // ID Q3SAA0_9EURY Unreviewed; 207 AA. AC Q3SAA0; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 19-FEB-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OS uncultured euryarchaeote Alv-FOS1. OC Archaea; Euryarchaeota; environmental samples. OX NCBI_TaxID=337892; RN [1] RP NUCLEOTIDE SEQUENCE. RA Moussard H., Hennecke G., Moreira D., Jouffe V., Lopez-Garcia P., RA Jeanthon C.; RT "A hyperthermophilic lifestyle for uncultured Archaea of the DHVE2 RT lineage: evidence from environmental genomics."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ118403; AAZ32473.1; -; Genomic_DNA. DR ProteinModelPortal; Q3SAA0; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21934 MW; 705B4622525D2FCF CRC64; MVQIRDKLRL YAVLPENGEH VKLADQALKG GATAIQLRMK AVPDREFLRV ARELRKVTEE YDALFVVDDR VDIAILADAD GVHLGADDVS VADAKALDPG LIVGATVRDV EMAKSAVREG ADYLGAGSVF PSRTKHAPVI GVEGIRDIVS AVKVPVVAIG GIDETNVVDV MRAGVAGVAV VCALFCRGDV ENRAIVLRGL VDSALSR // ID Q3SMR1_THIDA Unreviewed; 312 AA. AC Q3SMR1; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 14-MAY-2014, entry version 70. DE SubName: Full=NUDIX hydrolase; DE Flags: Precursor; GN OrderedLocusNames=Tbd_0027; OS Thiobacillus denitrificans (strain ATCC 25259). OC Bacteria; Proteobacteria; Betaproteobacteria; Hydrogenophilales; OC Hydrogenophilaceae; Thiobacillus. OX NCBI_TaxID=292415; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25259; RX PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006; RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.; RT "The genome sequence of the obligately chemolithoautotrophic, RT facultatively anaerobic bacterium Thiobacillus denitrificans."; RL J. Bacteriol. 188:1473-1488(2006). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000116; AAZ95980.1; -; Genomic_DNA. DR RefSeq; YP_313785.1; NC_007404.1. DR ProteinModelPortal; Q3SMR1; -. DR STRING; 292415.Tbd_0027; -. DR EnsemblBacteria; AAZ95980; AAZ95980; Tbd_0027. DR GeneID; 3671988; -. DR KEGG; tbd:Tbd_0027; -. DR PATRIC; 23966183; VBIThiDen82923_0025. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TDEN292415:GHWG-27-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 312 AA; 33368 MW; 042D09219D3C14BA CRC64; MNAAVVEVVA AVLTQPDGRV LLAQRPAGKV YAGHWEFPGG KVEAGETLED ALVRELREEL GITVSADCRW ITRVFEYPHA TVRLNFFRVF AWQGTPHPHE GQVFSWQRPE AVEVTPLLPA NFPIVKALSL PPVLGISQAE TLGADSFLAR LDVALAEGLR LIQVRDKSLP EDERLHLARE TVRRARRHGA RVLVNGSADL AQAADADGVH LDAAAAARCS VRPDCEWVGV SCHDADELAQ AAAIGADFAL LSPVLPTLTH PGAPTLGWAR FSALAAASPI PVYGLGGLAR DDVALARTRG AHGVALLRGA WT // ID Q3SP00_NITWN Unreviewed; 233 AA. AC Q3SP00; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 14-MAY-2014, entry version 52. DE SubName: Full=Thiamine monophosphate synthase; DE Flags: Precursor; GN OrderedLocusNames=Nwi_2738; OS Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=323098; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nb-255 / ATCC 25391; RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006; RA Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., RA Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., RA Arp D.J., Hickey W.J.; RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing RT bacterium Nitrobacter winogradskyi Nb-255."; RL Appl. Environ. Microbiol. 72:2050-2063(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000115; ABA05991.1; -; Genomic_DNA. DR RefSeq; YP_319343.1; NC_007406.1. DR ProteinModelPortal; Q3SP00; -. DR STRING; 323098.Nwi_2738; -. DR EnsemblBacteria; ABA05991; ABA05991; Nwi_2738. DR GeneID; 3676332; -. DR KEGG; nwi:Nwi_2738; -. DR PATRIC; 22702546; VBINitWin102302_3080. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; NWIN323098:GJEG-2788-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 233 AA; 24182 MW; 20B6C3397482752D CRC64; MPPKAAPPRP APRLYLATPV IDDPSHVAAQ LPALLASADV AAVLVRLSPS DPRTMISRIK ALAPLIQSTG VALLLEAHAD LVARAGADGA HLTGIEALQE TLPVLKPDRI AGVGGLSTRH DSMVAGEAGA DYVLFGEPDE TGDRPSAEAI AERLTWWAEL FEPPCVAHAM NIDEARLFAA SGADFILVDD IVWTDTRGAA LALADIATAI ARGHESQGGA ERTDPPHGVR GAG // ID Q3SPS1_NITWN Unreviewed; 214 AA. AC Q3SPS1; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Nwi_2467; OS Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=323098; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nb-255 / ATCC 25391; RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006; RA Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., RA Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., RA Arp D.J., Hickey W.J.; RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing RT bacterium Nitrobacter winogradskyi Nb-255."; RL Appl. Environ. Microbiol. 72:2050-2063(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000115; ABA05720.1; -; Genomic_DNA. DR RefSeq; YP_319072.1; NC_007406.1. DR ProteinModelPortal; Q3SPS1; -. DR STRING; 323098.Nwi_2467; -. DR EnsemblBacteria; ABA05720; ABA05720; Nwi_2467. DR GeneID; 3674684; -. DR KEGG; nwi:Nwi_2467; -. DR PATRIC; 22701932; VBINitWin102302_2774. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NWIN323098:GJEG-2516-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23416 MW; A473339969F1A853 CRC64; MQYPDRSAYP DRNAYPDRFY PVVDTLDWVR RLTGLGVGTV QLRAKDLNDG EALQLVSDAL EIVKDTPVRL VVNDYWRAAI VAGAKHLHLG QEDLATADVH EIRKAGLTLG LSTHDDAELE TALAAEPDYI ALGPIFPTTL KAMRFAPQGI PKITEWKQRV GNIPLVAIGG IKLEQAPEIY AAGADSIAVV SDITQNPDPD ARVKAWLDQM IEPA // ID Q3YSP7_EHRCJ Unreviewed; 349 AA. AC Q3YSP7; DT 27-SEP-2005, integrated into UniProtKB/TrEMBL. DT 27-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 69. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=Ecaj_0208; OS Ehrlichia canis (strain Jake). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=269484; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Jake; RX PubMed=16707693; DOI=10.1128/JB.01837-05; RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., RA Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., RA Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., RA Kyrpides N.C.; RT "The genome of the obligately intracellular bacterium Ehrlichia canis RT reveals themes of complex membrane structure and immune evasion RT strategies."; RL J. Bacteriol. 188:4015-4023(2006). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000107; AAZ68258.1; -; Genomic_DNA. DR RefSeq; YP_302856.1; NC_007354.1. DR ProteinModelPortal; Q3YSP7; -. DR STRING; 269484.Ecaj_0208; -. DR EnsemblBacteria; AAZ68258; AAZ68258; Ecaj_0208. DR GeneID; 3617687; -. DR KEGG; ecn:Ecaj_0208; -. DR PATRIC; 20573922; VBIEhrCan118076_0226. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; YKAYGVH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECAN269484:GI02-225-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 349 AA; 39935 MW; 992355263C9BC647 CRC64; MFECNEIYII GKDDLVQYSH TSQLKNLDDI IKSVSLLYSI KKKSIYAIDV TDRSNNKCLD YYFNGQEGLW ISYKSEPYND NAKFLLEYKK ACTLESKCLN PLDFQKDTLV IARACTNQSV ESTSFLDEKC FPNIMIDKDT RFEKNFPAII DPIRFYQIVP DLYWLRYVIN LGVKVVQLRI KDKPIENIEN QIKEGVCLAN QSNIKLFIND YWQLAIKYKA YGVHLGQKDL KDANFNEIFN AGLRLGISTH CYHELAIARY LRPSYIAFGP IFTTTLKNMD FMPQGVDLLS YWVKNLRSSI IAIGGINLLN VDSVIKTGVN GVAVVSAVLS NNNPAEATYE FIQKCGSIY // ID Q3Z8D5_DEHM1 Unreviewed; 352 AA. AC Q3Z8D5; DT 27-SEP-2005, integrated into UniProtKB/TrEMBL. DT 27-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=DET0782; OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195) OS (Dehalococcoides ethenogenes (strain 195)). OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales; OC Dehalococcoidaceae; Dehalococcoides. OX NCBI_TaxID=243164; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=195; RX PubMed=15637277; DOI=10.1126/science.1102226; RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., RA Methe B.A., Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., RA Kolonay J.F., Dodson R.J., Daugherty S.C., Brinkac L.M., RA Sullivan S.A., Madupu R., Nelson K.E., Kang K.H., Impraim M., Tran K., RA Robinson J.M., Forberger H.A., Fraser C.M., Zinder S.H., RA Heidelberg J.F.; RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides RT ethenogenes."; RL Science 307:105-108(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000027; AAW39920.1; -; Genomic_DNA. DR RefSeq; YP_181514.1; NC_002936.3. DR ProteinModelPortal; Q3Z8D5; -. DR STRING; 243164.DET0782; -. DR EnsemblBacteria; AAW39920; AAW39920; DET0782. DR GeneID; 3229882; -. DR KEGG; det:DET0782; -. DR PATRIC; 21608625; VBIDehEth89364_0746. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DETH243164:GJNF-783-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 179 183 HMP-PP binding (By similarity). FT REGION 276 278 THZ-P binding (By similarity). FT REGION 326 327 THZ-P binding (By similarity). FT METAL 212 212 Magnesium (By similarity). FT METAL 231 231 Magnesium (By similarity). FT BINDING 211 211 HMP-PP (By similarity). FT BINDING 250 250 HMP-PP (By similarity). FT BINDING 279 279 HMP-PP (By similarity). FT BINDING 306 306 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 352 AA; 38434 MW; 308453A02C3D6DC6 CRC64; MDNLDKLWRI VDVNQNRLSE GLRILEEIAR LYLEDETLTS RLKNLRHSLT LQDITSNSRL LFSRQADTDI GAQLETADQS KPETLFSVVS ANAKRAEQSL RVLEEFAGLS ETGLDAALYS RGRFELYTLE KDLAARLLRK HRRDMITGLY VAIDADYLAG RDIPAVTREA LEGGCRLIQL RAKTASTRKF LALAVNLKEI CLEYGALFIV NDRLDIALAC GADGLHLGQT DMPLSQARRF LPPDSIIGIS ADTPEQAVSA QNEGADYVAA GAVFPTQTKP DVLFGGLSGL KAIHQVVKIP LVAIGGINKS NFYEAMQAGA DSLCLISAVL GAPDIKKATS EFITLMEAAK ID // ID Q3ZXD4_DEHMC Unreviewed; 352 AA. AC Q3ZXD4; DT 27-SEP-2005, integrated into UniProtKB/TrEMBL. DT 27-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=cbdbA758; OS Dehalococcoides mccartyi (strain CBDB1). OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales; OC Dehalococcoidaceae; Dehalococcoides. OX NCBI_TaxID=255470; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBDB1; RX PubMed=16116419; DOI=10.1038/nbt1131; RA Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.; RT "Genome sequence of the chlorinated compound-respiring bacterium RT Dehalococcoides species strain CBDB1."; RL Nat. Biotechnol. 23:1269-1273(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ965256; CAI82915.1; -; Genomic_DNA. DR RefSeq; YP_307831.1; NC_007356.1. DR ProteinModelPortal; Q3ZXD4; -. DR STRING; 255470.cbdb_A758; -. DR EnsemblBacteria; CAI82915; CAI82915; cbdbA758. DR GeneID; 3623335; -. DR KEGG; deh:cbdb_A758; -. DR PATRIC; 21611613; VBIDehSp125902_0642. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; EISTWAY; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DSP255470:GJXW-654-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 179 183 HMP-PP binding (By similarity). FT REGION 276 278 THZ-P binding (By similarity). FT REGION 326 327 THZ-P binding (By similarity). FT METAL 212 212 Magnesium (By similarity). FT METAL 231 231 Magnesium (By similarity). FT BINDING 211 211 HMP-PP (By similarity). FT BINDING 250 250 HMP-PP (By similarity). FT BINDING 279 279 HMP-PP (By similarity). FT BINDING 306 306 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 352 AA; 38380 MW; DB76FB22E5595F25 CRC64; MDNLEKLWRI VDVNQNRLSE GLRILEEIAR LYLENETLTL RLKNLRHALT LQDTASNCHL LFSRQADTDI GAHLKTVDQS KPETLFSLIS ANAKRAEQSL RVLEEFAGLL ELGLDTSIYS RGRFELYTLE KDLAAILLRK NRRDMIKGLY VAIDVDYLAG RDIPRVTKEV LEGGCRLVQL RAKTASARQF LSLALSLKEL CIEYGAVFIV NDRLDIALAC GADGLHLGQT DLPLSQARRL MPAGSIIGIS ADSPEDAASA QAGDADYVAA GAVFPTQTKL DVLYGGLSGL KAIRQVVNIP LVAIGGINKS NYNEALQAGA DSLCLISAVL GAPDIKKATS EFMTLVEAEK ND // ID Q40JL9_EHRCH Unreviewed; 348 AA. AC Q40JL9; DT 27-SEP-2005, integrated into UniProtKB/TrEMBL. DT 27-SEP-2005, sequence version 1. DT 19-FEB-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN ORFNames=EchaDRAFT_0301; OS Ehrlichia chaffeensis str. Sapulpa. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=332415; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sapulpa; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M.; RT "Annotation of the draft genome assembly of Ehrlichia chaffeensis str. RT Sapulpa."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sapulpa; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T., RA Hammon N., Israni S., Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of Ehrlichia chaffeensis RT str. Sapulpa."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAIF01000021; EAM85801.1; -; Genomic_DNA. DR ProteinModelPortal; Q40JL9; -. DR EnsemblBacteria; EAM85801; EAM85801; EchaDRAFT_0301. DR PATRIC; 26677034; VBIEhrCha122199_0348. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 348 AA; 39742 MW; 51622051C49DFF80 CRC64; MSENDFSEVC IVDKRDLIQY CCTTQLEDLD DIVRSVNSLY SIKKKSIYVI NVASQKYGRC WDYYFNGIEG LWFLYNGVSY NGKENFLSAY KASVLVSKCL NAADLQKDAL IIARASANQS AEDASFLDER YFPIITLNKD YYFDKNFHPM LDPVGFYQIV PDLFWLKYVI NLGVKVVQLR IKNEPIEEVE YKIKEGVHIA NQNGVKLFVN DYWQFAVKYK AYGVHLGQED LRSANFNEIY NAGLRLGIST HCYHELAIAK YIRPSYIAFG PIFPTTLKNM NFMPQGTDLL NYWVKNLPYK IVAIGGINLS NVDSVIGTGV DGIAVISAVL NSEYPDKVVH EFIQKCQI // ID Q46JJ7_PROMT Unreviewed; 350 AA. AC Q46JJ7; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PMN2A_0840; OS Prochlorococcus marinus (strain NATL2A). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=59920; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NATL2A; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., RA Steglich C., Church G.M., Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000095; AAZ58331.1; -; Genomic_DNA. DR RefSeq; YP_292034.1; NC_007335.2. DR ProteinModelPortal; Q46JJ7; -. DR STRING; 59920.PMN2A_0840; -. DR EnsemblBacteria; AAZ58331; AAZ58331; PMN2A_0840. DR GeneID; 3606221; -. DR KEGG; pmn:PMN2A_0840; -. DR PATRIC; 23025465; VBIProMar14922_1664. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR59920:GI1O-1687-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 128 Unknown (By similarity). FT REGION 129 350 Thiamine-phosphate synthase (By FT similarity). FT REGION 180 184 HMP-PP binding (By similarity). FT METAL 213 213 Magnesium (By similarity). FT METAL 232 232 Magnesium (By similarity). FT BINDING 212 212 HMP-PP (By similarity). FT BINDING 251 251 HMP-PP (By similarity). FT BINDING 280 280 HMP-PP (By similarity). FT BINDING 307 307 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 350 AA; 39481 MW; DE371921CBD631C7 CRC64; MKSIPVTPPS DNRIAQLIDA NLDRAREGLR VMEDWCRFGL KRSDFSIQIK DWRQQLGVHH HNIYRKERLT SIDPAMGISH PLQTVRSTPE DVFIANSSRV QEALRVIEEF TRTTDPHLCE IASKIRYETY DIEIKVLNST EGVNKREILK DCSLYLITSN SRDLEEVVLY ALKAGVKIVQ YREKFLNDNE KISQAKCLAS LCKKFNSLFI VNDRIDIALA VDADGIHLGQ EDMPTKIARQ LLGAEKIIGR STHCLEDIKN AEAEGCDYIG IGPIFPSETK KQLNPIGIDY LKKGLSETLL PAFAIGGMNK SNITKLNQIN NLRIAVCNAI INSNNPFSTT DELIKLLKCN // ID Q476U2_CUPPJ Unreviewed; 378 AA. AC Q476U2; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 50. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=Reut_A0209; OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia OS eutropha (strain JMP 134)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=264198; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JMP134 / LMG 1197; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., RA Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000090; AAZ59591.1; -; Genomic_DNA. DR RefSeq; YP_294435.1; NC_007347.1. DR ProteinModelPortal; Q476U2; -. DR STRING; 264198.Reut_A0209; -. DR EnsemblBacteria; AAZ59591; AAZ59591; Reut_A0209. DR GeneID; 3610541; -. DR KEGG; reu:Reut_A0209; -. DR PATRIC; 20225853; VBIRalEut24049_0805. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CPIN264198:GIW3-209-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 378 AA; 39925 MW; A500874A00A9C2A3 CRC64; MTRHAVHAPS DGPLRQAVLE HYGETFGVSD HPWQAWRLAD APASPGVHDV LLSDGEADAD LIARVGAAGA TLIETDREGG QWIDTVRSPM GTWVLSSHAD DDHAHSPAFV AVLLACLSLH FPAHDALCLA RAWRPGSAEW PSEFERFPRV RHAALVAPEA ATQAFAPCPP ALGLYAVVPS AEWIERLVPL GVPTVQLRFK SDDPAAVRAE IARAAQAAKG SQSRLFINDH WQVAVELHAA AGGDSGIYGI HLGQEDLDNA DLDALRASGL RLGVSTHGYA EMLRVAAIRP SYLALGAIFP TTTKVMPTAP QGMGRFRAYA KVMQPVIPSL VGIGGVNASN MGQVLAVGVR SAAVVRAITE ADDVPAAVAH LISLFPAA // ID Q479P6_DECAR Unreviewed; 314 AA. AC Q479P6; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 68. DE SubName: Full=NUDIX hydrolase:Thiamine monophosphate synthase; GN OrderedLocusNames=Daro_3706; OS Dechloromonas aromatica (strain RCB). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Dechloromonas. OX NCBI_TaxID=159087; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCB; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K., RA Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.; RT "Complete sequence of Dechloromonas aromatica RCB."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000089; AAZ48435.1; -; Genomic_DNA. DR RefSeq; YP_286905.1; NC_007298.1. DR ProteinModelPortal; Q479P6; -. DR STRING; 159087.Daro_3706; -. DR EnsemblBacteria; AAZ48435; AAZ48435; Daro_3706. DR GeneID; 3567918; -. DR KEGG; dar:Daro_3706; -. DR PATRIC; 21606090; VBIDecAro89105_3687. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DARO159087:GI5B-3782-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 34028 MW; F96B2EE6F9A72559 CRC64; MTKIVEVAAA VMLRADGREF LLAQRPEGKV YAGYWEFPGG KVEPGETVRQ ALIRELQEEL GITVTACSQW LTRQFTYPHA TVRLNFWRVT AWDGEIGITA PLEHSAVEWQ KTGGAASVAP ILPANDPILK ALSLPTTMAI TMAESEGTER QLERLEEALN AGLRLIQIRD KSLPPAQRLW FAETVLQLAR SHGATVVIND DEALARRIGA DGVHLSAARL AACQQRPDFT WVGASCHSAE EIVRAGELGL DYALLGPVMP TPTHPESTGL GWTEFEGRLA GNTLPVFALG GMKPGMLAEA QGHGAHGLAL MRGW // ID Q48A92_COLP3 Unreviewed; 529 AA. AC Q48A92; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 19-FEB-2014, entry version 74. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiDE; OrderedLocusNames=CPS_0254; OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio OS psychroerythus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=167879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=34H / ATCC BAA-681; RX PubMed=16043709; DOI=10.1073/pnas.0504766102; RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B., RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.; RT "The psychrophilic lifestyle as revealed by the genome sequence of RT Colwellia psychrerythraea 34H through genomic and proteomic RT analyses."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000083; AAZ25695.1; -; Genomic_DNA. DR RefSeq; YP_267021.1; NC_003910.7. DR ProteinModelPortal; Q48A92; -. DR STRING; 167879.CPS_0254; -. DR EnsemblBacteria; AAZ25695; AAZ25695; CPS_0254. DR GeneID; 3519941; -. DR KEGG; cps:CPS_0254; -. DR PATRIC; 21463903; VBIColPsy94388_0222. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CPSY167879:GI48-254-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 529 AA; 57726 MW; 64075802CBE21C74 CRC64; MKTEQQVAIK PIIWTISGSD CSGGAGIAAD IKTGHGLGVE VCHLITANTV QNSHQLLSVN AISVELLQQQ AAVLMDDKPP SVIKIGLVAN AEQVQWLAQL IEQIKQVIPT LISVYDPVGQ ASVGGSFNNL TLEQLSPLLL KIDVITPNLM EAKSLAKLDG LPDKNSAEKL ANKIHQNFAI NSIIVKGGHI HSDDRYSIDF CLHQLNQLNG KQDNQDKAQT AISYQLGALR IDSHYSHGGG CSFASALASF LAQGYLIRDA FTLAKAFISQ GLSTSKQVSE LHGHQYYGAF EQQGWPRNAE CFPQVIDELS QQYQNLPAFN SLDLAEKKLG LYPVIDSLYW LKRLLSLGLE IIQLRVKNLA ESELEQVIIT AIALAKKYDT RLFINDYWQL AIKHGAYGVH IGQEDLQDAD LTAIQQSGIR LGISTHGCYE FLSAQRLQPS YLAIGAIFPT KTKDMTGQIQ GIDNLRQVLS LRPENKHKIP VVAIGGINLE RAAEVIATGV ESIAVVTAIT EAECSHGISP EQAVTRLQF // ID Q48EG9_PSE14 Unreviewed; 316 AA. AC Q48EG9; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 67. DE SubName: Full=MutT/nudix family protein; GN OrderedLocusNames=PSPPH_4097; OS Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=264730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1448A / Race 6; RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005; RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., RA Brinkac L.M., Daugherty S.C., Deboy R., Durkin A.S., Giglio M.G., RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S., Crabtree J., RA Creasy T., Davidsen T., Haft D.H., Zafar N., Zhou L., Halpin R., RA Holley T., Khouri H., Feldblyum T., White O., Fraser C.M., RA Chatterjee A.K., Cartinhour S., Schneider D.J., Mansfield J., RA Collmer A., Buell C.R.; RT "Whole-genome sequence analysis of Pseudomonas syringae pv. RT phaseolicola 1448A reveals divergence among pathovars in genes RT involved in virulence and transposition."; RL J. Bacteriol. 187:6488-6498(2005). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000058; AAZ34380.1; -; Genomic_DNA. DR RefSeq; YP_276219.1; NC_005773.3. DR ProteinModelPortal; Q48EG9; -. DR STRING; 264730.PSPPH_4097; -. DR EnsemblBacteria; AAZ34380; AAZ34380; PSPPH_4097. DR GeneID; 3556933; -. DR KEGG; psp:PSPPH_4097; -. DR PATRIC; 19977659; VBIPseSyr78478_4287. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PSAV264730:GKDE-4101-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 316 AA; 34071 MW; 8C3092083F8F7236 CRC64; MKRVHVAAAV IRGADGSVLI ARRADTQHQG GLWEFPGGKV EEGETVQAAL ARELQEELGI HVTAARPLIK VGHDYADKQV LLDVWEVSAF TGEPHGAEGQ PLVWAAPREL PDYDFPAANQ PIVAAARLPG EYLITPDGLD NIELLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPENRWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWQQ AAQLIAGFNK PVFLLGGVGP SERQQAWESG AQGVAGIRAF WPDEIV // ID Q49UE9_STAS1 Unreviewed; 218 AA. AC Q49UE9; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 51. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=SSPP136; OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / OS DSM 20229). OG Plasmid pSSP1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=342451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15305 / DSM 20229; PLASMID=pSSP1; RX PubMed=16135568; DOI=10.1073/pnas.0502950102; RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., RA Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., RA Hattori M., Ohta T.; RT "Whole genome sequence of Staphylococcus saprophyticus reveals the RT pathogenesis of uncomplicated urinary tract infection."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008935; BAE19627.1; -; Genomic_DNA. DR RefSeq; YP_302572.1; NC_007351.1. DR ProteinModelPortal; Q49UE9; -. DR STRING; 342451.SSPP136; -. DR EnsemblBacteria; BAE19627; BAE19627; SSPP136. DR GeneID; 3617403; -. DR KEGG; ssp:SSPP136; -. DR PATRIC; 19626566; VBIStaSap90642_2466. DR eggNOG; NOG327032; -. DR HOGENOM; HOG000090085; -. DR OMA; FAGICAI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSAP342451:GKFA-2566-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Plasmid. SQ SEQUENCE 218 AA; 24801 MW; 799DEC9C0ECEDCC7 CRC64; MINVIIQRYF STRKSNVFLF GVKILFIAIT PYQDLSKSHI KHYCEIEGVI DYLLIRVPMN TEEVIQWVHG LLKNEFPKDK IIVHSDINVI IQCDLSAIHF RESDPYIEEV QASYPDMQIS MSTHHKDAIA NAKYLGLDFV LFGHVFETSS KPQQTPRAKS EVEEALQIDI PIIAIGGINQ HTLSSLPNGF SGIAGISVFN QYSKEKLINM KEVWDGHV // ID Q4C3Q4_CROWT Unreviewed; 338 AA. AC Q4C3Q4; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 19-FEB-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CwatDRAFT_3783; OS Crocosphaera watsonii WH 8501. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Crocosphaera. OX NCBI_TaxID=165597; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 8501; RG DOE Joint Genome Institute; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 8501; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M.; RT "Annotation of the draft genome assembly of Crocosphaera watsonii WH RT 8501."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 8501; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T., RA Hammon N., Israni S., Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of Crocosphaera watsonii RT WH 8501."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AADV02000015; EAM50788.1; -; Genomic_DNA. DR ProteinModelPortal; Q4C3Q4; -. DR EnsemblBacteria; EAM50788; EAM50788; CwatDRAFT_3783. DR PATRIC; 27702100; VBICroWat128338_3108. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 1 121 Unknown (By similarity). FT REGION 122 338 Thiamine-phosphate synthase (By FT similarity). FT REGION 169 173 HMP-PP binding (By similarity). FT REGION 266 268 THZ-P binding (By similarity). FT METAL 202 202 Magnesium (By similarity). FT METAL 221 221 Magnesium (By similarity). FT BINDING 201 201 HMP-PP (By similarity). FT BINDING 240 240 HMP-PP (By similarity). FT BINDING 269 269 HMP-PP (By similarity). FT BINDING 296 296 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 338 AA; 37951 MW; 2C3ADB39EA0BD386 CRC64; MDKNLAIARI LDANLDRARE GLRVVEEWCR LGLENSDCTD KCKQMRQEIA HWHTSDLRKA RDTINDPGTD LSHPQEAIRE NIEQLLQANL CRVQEALRVL EEYGKLYDPN MGNAFKKIRY QVYILESELL QSYRYKKLIN ASLYLVTSST KNLLKTVESA LQGGLTLVQY RKKDVDDIIR LEMAQKLSEL CHKYDALFIV NDRADIALEV NADGVHLGQQ DIPISLARRI LGPNKIIGRS TTNPQEMAKA IAEKADYIGV GPVYATPTKP DKQAAGLDYV KYAAQHSPIP WFAIGGIDEH NVTELIASGA TQVALVRAIM EADNPQKTTA KLLKKLKG // ID Q4EM56_LISMN Unreviewed; 214 AA. AC Q4EM56; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 19-FEB-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMOh7858_0354; OS Listeria monocytogenes serotype 4b str. H7858. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=267410; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4b H7858; RX PubMed=15115801; DOI=10.1093/nar/gkh562; RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., RA Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., RA Peterson J., White O., Nelson W.C., Nierman W., Beanan M.J., RA Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., RA Haft D.H., Selengut J., Van Aken S., Khouri H., Fedorova N., RA Forberger H., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., RA Bayles D.O., Luchansky J.B., Fraser C.M.; RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food- RT borne pathogen Listeria monocytogenes reveal new insights into the RT core genome components of this species."; RL Nucleic Acids Res. 32:2386-2395(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AADR01000001; EAL10868.1; -; Genomic_DNA. DR ProteinModelPortal; Q4EM56; -. DR EnsemblBacteria; EAL10868; EAL10868; LMOh7858_0354. DR PATRIC; 30237328; VBILisMon13611_0104. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22624 MW; 10F8C1830CF46A06 CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAE EAERLGAVDY IGVGPIFPTI SKADAEPVSG TTILKEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GYPS // ID Q4ER25_LISMN Unreviewed; 214 AA. AC Q4ER25; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 19-FEB-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=LMOf6854_0326; OS Listeria monocytogenes serotype 1/2a str. F6854. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=267409; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1/2a F6854; RX PubMed=15115801; DOI=10.1093/nar/gkh562; RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., RA Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., RA Peterson J., White O., Nelson W.C., Nierman W., Beanan M.J., RA Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., RA Haft D.H., Selengut J., Van Aken S., Khouri H., Fedorova N., RA Forberger H., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., RA Bayles D.O., Luchansky J.B., Fraser C.M.; RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food- RT borne pathogen Listeria monocytogenes reveal new insights into the RT core genome components of this species."; RL Nucleic Acids Res. 32:2386-2395(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AADQ01000022; EAL06135.1; -; Genomic_DNA. DR ProteinModelPortal; Q4ER25; -. DR EnsemblBacteria; EAL06135; EAL06135; LMOf6854_0326. DR PATRIC; 30234350; VBILisMon99803_1731. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22392 MW; 67844F688FC140A4 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALKCQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAA EAELLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GITIPIVGIG GINETNLAEV LTAGADGVSV ISAITQSDDC HSVIKQLKNP GSPS // ID Q4FNQ7_PELUB Unreviewed; 180 AA. AC Q4FNQ7; DT 30-AUG-2005, integrated into UniProtKB/TrEMBL. DT 30-AUG-2005, sequence version 1. DT 14-MAY-2014, entry version 52. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=SAR11_0360; OS Pelagibacter ubique (strain HTCC1062). OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=335992; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC1062; RX PubMed=16109880; DOI=10.1126/science.1114057; RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., RA Baptista D., Bibbs L., Eads J., Richardson T.H., Noordewier M., RA Rappe M.S., Short J.M., Carrington J.C., Mathur E.J.; RT "Genome streamlining in a cosmopolitan oceanic bacterium."; RL Science 309:1242-1245(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000084; AAZ21182.1; -; Genomic_DNA. DR RefSeq; YP_265785.1; NC_007205.1. DR ProteinModelPortal; Q4FNQ7; -. DR EnsemblBacteria; AAZ21182; AAZ21182; SAR11_0360. DR GeneID; 3517690; -. DR KEGG; pub:SAR11_0360; -. DR PATRIC; 31990179; VBICanPel5618_0359. DR OMA; SARIHIQ; -. DR OrthoDB; EOG679THR; -. DR BioCyc; CPEL335992:GH3Z-361-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 180 AA; 21017 MW; E75A123D26FDE008 CRC64; MHNKILKKYY FINKFNQSHI DKQDQETTII YRNYDQDIDE KLILRIKSYC KKRGHKFLLS NNIKLAIKLN LNGAYIPSFN NDKKHLSYSF KKNFIILGSA HNVFEIRNKE SQNVKAIFLS SIFKKNKNFL GINRFKFLSR LSKKPFIALG GISKTSLKKL NLVNCIGFAG ISFFEQKKGP // ID Q4FRK3_PSYA2 Unreviewed; 360 AA. AC Q4FRK3; DT 30-AUG-2005, integrated into UniProtKB/TrEMBL. DT 30-AUG-2005, sequence version 1. DT 14-MAY-2014, entry version 67. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=Psyc_1507; OS Psychrobacter arcticus (strain DSM 17307 / 273-4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=259536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17307 / 273-4; RX PubMed=20154119; DOI=10.1128/AEM.02101-09; RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., RA Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., RA Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., RA Richardson P., Murray A., Thomashow M., Tiedje J.M.; RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive RT Siberian permafrost bacterium, reveals mechanisms for adaptation to RT low-temperature growth."; RL Appl. Environ. Microbiol. 76:2304-2312(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000082; AAZ19355.1; -; Genomic_DNA. DR RefSeq; YP_264789.1; NC_007204.1. DR ProteinModelPortal; Q4FRK3; -. DR STRING; 259536.Psyc_1507; -. DR DNASU; 3515468; -. DR EnsemblBacteria; AAZ19355; AAZ19355; Psyc_1507. DR GeneID; 3515468; -. DR KEGG; par:Psyc_1507; -. DR PATRIC; 23057717; VBIPsyArc98534_1772. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; VAVIHYQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PARC259536:GI3A-1543-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 360 AA; 39721 MW; A721F3875F64B5EB CRC64; MAVEKSTSIK NNSIKTVNVA VAVIHYQNQY LLGFRAASQH QGNRYEFVGG KIDAHETAKQ ALIREVAEET GINIANNTAV KLGRLHHDYG DKQVCLQVYR IEVTAQQYAQ YKNLSCGLEG QKLTWVDKAK LLAGHYDLPA ANKTILVWLQ LPVQITITYP LAHFNGFPNP RAAWSQYHHE HIAADALVYM RIKVAGAEDS IERLLQLRSD IKAIAPDHLH TDKADNAVIN RQIIAGHLTQ TQLMQWSSSV AKESMSYSAL STNLPLIVSC HDADSINAAN QLAFFRLQQQ LPPVIGIFLA PVECTQTHPD TPPLGWEAWS KLAELADMPV IGLGGLSPVM SEQAMLHGGI AVAGIRQFLK // ID Q4FTU4_PSYA2 Unreviewed; 236 AA. AC Q4FTU4; DT 30-AUG-2005, integrated into UniProtKB/TrEMBL. DT 30-AUG-2005, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Thiamine-phosphate diphosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=Psyc_0705; OS Psychrobacter arcticus (strain DSM 17307 / 273-4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=259536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17307 / 273-4; RX PubMed=20154119; DOI=10.1128/AEM.02101-09; RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., RA Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., RA Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., RA Richardson P., Murray A., Thomashow M., Tiedje J.M.; RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive RT Siberian permafrost bacterium, reveals mechanisms for adaptation to RT low-temperature growth."; RL Appl. Environ. Microbiol. 76:2304-2312(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000082; AAZ18564.1; -; Genomic_DNA. DR RefSeq; YP_263998.1; NC_007204.1. DR ProteinModelPortal; Q4FTU4; -. DR STRING; 259536.Psyc_0705; -. DR EnsemblBacteria; AAZ18564; AAZ18564; Psyc_0705. DR GeneID; 3516165; -. DR KEGG; par:Psyc_0705; -. DR PATRIC; 23055827; VBIPsyArc98534_0837. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IGRTCHG; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PARC259536:GI3A-729-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 236 AA; 25512 MW; 02B7D23C3C40CC1F CRC64; MIQPSFSTAS HAIPKLYLLT NDDEFSLLYH KLEAALATGL IALLQIRRKH ILALPDGESL LYKEALQIVN LAKTYNVPVL INDNIALAAK LGIGVHLGQQ DGDISEATQC LAPNKIIGRT CHGDVALVKA AKNEGARYAA MGAVFASTTK PNAATISRQQ LIDGCQQDIK VCVIGGLTAE NILELAGLPI TYIAIVGDIM DLPVHQIAAR CQQWQQVLNK WNVPAEYISR PLIINS // ID Q4HEZ8_CAMCO Unreviewed; 201 AA. AC Q4HEZ8; DT 16-AUG-2005, integrated into UniProtKB/TrEMBL. DT 16-AUG-2005, sequence version 1. DT 19-FEB-2014, entry version 36. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=CCO1110; OS Campylobacter coli RM2228. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=306254; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RM2228; RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015; RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., RA Nelson K.E.; RT "Major structural differences and novel potential virulence mechanisms RT from the genomes of multiple Campylobacter species."; RL PLoS Biol. 3:72-85(2005). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAFL01000007; EAL56435.1; -; Genomic_DNA. DR ProteinModelPortal; Q4HEZ8; -. DR EnsemblBacteria; EAL56435; EAL56435; CCO1110. DR PATRIC; 30463376; VBICamCol113778_1293. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 201 AA; 23386 MW; 3EB32B7F410860B3 CRC64; MWDKKIIAIS DRKCVEIDFL KQVEKLAKSG IDAFVLREKD LSEFEYYDLA KEVLAICAKH KTTCFLHFFD RECLKLGHRY FHMPLALLRQ EPKMSKYFHM IGTSVHSKEE LLEAMNYGVN YTFVGHIFES SCKKDLEPRG LEFLNSLLSF SQIPLYAIGG INVQNIASFK DINVAGVCMR EVLMREKDVK KYLVECKRNL L // ID Q4HGM1_CAMCO Unreviewed; 210 AA. AC Q4HGM1; DT 16-AUG-2005, integrated into UniProtKB/TrEMBL. DT 16-AUG-2005, sequence version 1. DT 19-FEB-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CCO1155; OS Campylobacter coli RM2228. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=306254; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RM2228; RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015; RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., RA Nelson K.E.; RT "Major structural differences and novel potential virulence mechanisms RT from the genomes of multiple Campylobacter species."; RL PLoS Biol. 3:72-85(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAFL01000002; EAL57007.1; -; Genomic_DNA. DR ProteinModelPortal; Q4HGM1; -. DR EnsemblBacteria; EAL57007; EAL57007; CCO1155. DR PATRIC; 30462204; VBICamCol113778_0719. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23256 MW; F7221F023DA3BA7E CRC64; MKNDLDLSLY LVASRGKKSD ELFLNTLEEA IKGGVSIIQL REKELSSREF YKLGLKVQKL CKEYEIPFLI NDRIDIALAL DADGVHLGQE DLEVRFARKI LGKEKIIGLS LKNLEQLKDI DGADYLGCGA IKATPTKESS VISFETLSQI CEKSPIGVVA IGGIDKELIK ELKGIKISGI AVVRAIMDAQ NAYLAAKELR QEMNENLSFK // ID Q4HRG7_CAMUP Unreviewed; 187 AA. AC Q4HRG7; DT 16-AUG-2005, integrated into UniProtKB/TrEMBL. DT 16-AUG-2005, sequence version 1. DT 19-FEB-2014, entry version 37. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=CUP0540; OS Campylobacter upsaliensis RM3195. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=306264; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RM3195; RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015; RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., RA Nelson K.E.; RT "Major structural differences and novel potential virulence mechanisms RT from the genomes of multiple Campylobacter species."; RL PLoS Biol. 3:72-85(2005). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAFJ01000004; EAL53396.1; -; Genomic_DNA. DR ProteinModelPortal; Q4HRG7; -. DR EnsemblBacteria; EAL53396; EAL53396; CUP0540. DR PATRIC; 27775962; VBICamUps61687_0798. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 187 AA; 21661 MW; 048411D26412DD3A CRC64; MQDDFLRQVE KLAKAKIDAF VLREKDLSEY EYYDLAKEVL KICTKYKITC FLHGYLTPTL KLEHKYFQAP LALLRKESNI AKYFHILGTS VHSKEELLEA INYKVNHAFV GHIFKSSCKP NLKPYGIELL KDLLSFSSIP LYAIGGINAE NIKFFKNINI AGVCMREALM REKNPKKYLA LCKKEFV // ID Q4HTB6_CAMUP Unreviewed; 207 AA. AC Q4HTB6; DT 16-AUG-2005, integrated into UniProtKB/TrEMBL. DT 16-AUG-2005, sequence version 1. DT 19-FEB-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=CUP0765; OS Campylobacter upsaliensis RM3195. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=306264; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RM3195; RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015; RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., RA Nelson K.E.; RT "Major structural differences and novel potential virulence mechanisms RT from the genomes of multiple Campylobacter species."; RL PLoS Biol. 3:72-85(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAFJ01000001; EAL54004.1; -; Genomic_DNA. DR ProteinModelPortal; Q4HTB6; -. DR EnsemblBacteria; EAL54004; EAL54004; CUP0765. DR PATRIC; 27774629; VBICamUps61687_0154. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22391 MW; 4610F0573927948F CRC64; MLDLSLYLVA SRGNLNNEKF LNVLESAIKG GVSLIQLREK NLNARDFFTL GLKAQKLCQK HQIPLIINDR IDLALALNAD GVHLGQDDLP LQIARKILGK DKIIGLSLKS LKQLEGIEGA DYLGCGAIKK TPTKESSVLS LELLSQICQN SSLPVVAIGG IDEAVIKDLR DIKLGGVAVV RAIMNAKNPY QAAKTLKKAV CENLSLK // ID Q4K7C3_PSEF5 Unreviewed; 314 AA. AC Q4K7C3; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 2. DT 14-MAY-2014, entry version 62. DE SubName: Full=Mutator mutT protein/thiamine monophosphate synthase (TenI); DE EC=3.6.1.-; GN OrderedLocusNames=PFL_4779; OS Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=220664; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pf-5 / ATCC BAA-477; RX PubMed=15980861; DOI=10.1038/nbt1110; RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S., RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J., RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., RA Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., RA Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., RA Pierson L.S.III., Thomashow L.S., Loper J.E.; RT "Complete genome sequence of the plant commensal Pseudomonas RT fluorescens Pf-5."; RL Nat. Biotechnol. 23:873-878(2005). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000076; AAY94009.2; -; Genomic_DNA. DR RefSeq; YP_261860.2; NC_004129.6. DR ProteinModelPortal; Q4K7C3; -. DR STRING; 220664.PFL_4779; -. DR EnsemblBacteria; AAY94009; AAY94009; PFL_4779. DR GeneID; 3479190; -. DR KEGG; pfl:PFL_4779; -. DR PATRIC; 19879014; VBIPseFlu72549_4890. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR BioCyc; PFLU220664:GIX8-4820-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 33850 MW; 764AC3DB200902D9 CRC64; MKRVHVAAAV IRDASGKILI ARRADTQHQG GLWEFPGGKV EPGEAVEAAL ARELQEELGI AVTAARPLIK VQHDYPDKQV LLDVWEVSAF SGEPHGAEGQ PLAWVTAREL ADYEFPAANQ PIVAAARLPA QYLITPEGLE TPTLLRGMQK AVAQGCKLIQ LRAPGGYDPQ YRDLAVDAVG LCAGKAQLML KGPFEWLGDF PSAGWHITAA QLRKYASAGR PFGKDRWLAA SCHNAEELSL AQQMDVDFVT LSPVQPTQTH PDAQPLGWQQ AEQLISGFNK PVYLLGGVGP AECQQAWAAG AQGVAGIRAF WPQD // ID Q4L901_STAHJ Unreviewed; 197 AA. AC Q4L901; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 14-MAY-2014, entry version 55. DE SubName: Full=Staphylococcus haemolyticus JCSC1435 DNA, complete genome; GN OrderedLocusNames=SH0565; OS Staphylococcus haemolyticus (strain JCSC1435). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=279808; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC1435; RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005; RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., RA Lee J.C., Hiramatsu K.; RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the RT extreme plasticity of its genome and the evolution of human-colonizing RT staphylococcal species."; RL J. Bacteriol. 187:7292-7308(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006716; BAE03874.1; -; Genomic_DNA. DR RefSeq; YP_252480.1; NC_007168.1. DR ProteinModelPortal; Q4L901; -. DR STRING; 279808.SH0565; -. DR EnsemblBacteria; BAE03874; BAE03874; SH0565. DR GeneID; 3484190; -. DR KEGG; sha:SH0565; -. DR PATRIC; 19617157; VBIStaHae67511_0555. DR eggNOG; COG0352; -. DR HOGENOM; HOG000090085; -. DR OMA; FAGICAI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SHAE279808:GJX7-567-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 197 AA; 22389 MW; EAADBF672C385951 CRC64; MIDIFIAITT YKHLTEADLQ HFIEISKGID GLLFRTPMSS DDLFSFLEKL IAAGFPKDKI IIHSDVDLLE SLTLKRLHCR EMDTLAFDYK AQHPDVEVSM STHTINSVKQ AYQHQLDYVF YGHIFTTASK PNQQPRSMSE IKAVLQVPIP VYAIGGITED TIQRLPNGFA GICAISYFMS ASLQQIQHLR KEWLKDA // ID Q4MQD1_BACCE Unreviewed; 219 AA. AC Q4MQD1; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 19-FEB-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=BCE_G9241_0383; OS Bacillus cereus G9241. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=269801; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=G9241; RX PubMed=15155910; DOI=10.1073/pnas.0402414101; RA Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D., RA Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W., RA Maiden M.C., Priest F.G., Barker M., Jiang L., Cer R.Z., Rilstone J., RA Peterson S.N., Weyant R.S., Galloway D.R., Read T.D., Popovic T., RA Fraser C.M.; RT "Identification of anthrax toxin genes in a Bacillus cereus associated RT with an illness resembling inhalation anthrax."; RL Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEK01000015; EAL14378.1; -; Genomic_DNA. DR ProteinModelPortal; Q4MQD1; -. DR SMR; Q4MQD1; 1-215. DR EnsemblBacteria; EAL14378; EAL14378; BCE_G9241_0383. DR PATRIC; 24957823; VBIBacCer116370_2843. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23599 MW; F6BBDDA6D3E3D325 CRC64; MSRISKAEMS RLLSVYFIMG SNNCTKDPLQ VLRDALEGGI TIFQFREKGE GALTGEKRIY FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITFVREKMG DKIIGVSTHI IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSNSL // ID Q4MWY1_BACCE Unreviewed; 206 AA. AC Q4MWY1; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 16-OCT-2013, entry version 35. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN ORFNames=BCE_G9241_0715; OS Bacillus cereus G9241. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=269801; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=G9241; RX PubMed=15155910; DOI=10.1073/pnas.0402414101; RA Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D., RA Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W., RA Maiden M.C., Priest F.G., Barker M., Jiang L., Cer R.Z., Rilstone J., RA Peterson S.N., Weyant R.S., Galloway D.R., Read T.D., Popovic T., RA Fraser C.M.; RT "Identification of anthrax toxin genes in a Bacillus cereus associated RT with an illness resembling inhalation anthrax."; RL Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEK01000002; EAL16358.1; -; Genomic_DNA. DR ProteinModelPortal; Q4MWY1; -. DR EnsemblBacteria; EAL16358; EAL16358; BCE_G9241_0715. DR PATRIC; 24952978; VBIBacCer116370_0452. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 22752 MW; E7537382E2B61E79 CRC64; MKNELHVISN GHMSFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK IVINDRIDIA ILLNIPRVQL GYRSADVRSV KEKFSYLHVG YSVHSLEEAI NAFKNGADSL VYGHVFPTDC KKGVPARGLE EISDIAKCLS IPITAIGGIT TENTGDVLTN GVSGIAVMSG IISSSNPYSK AKSYKESIRK WAEKHV // ID Q4PB99_USTMA Unreviewed; 568 AA. AC Q4PB99; DT 19-JUL-2005, integrated into UniProtKB/TrEMBL. DT 19-JUL-2005, sequence version 1. DT 16-APR-2014, entry version 48. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=UM02614.1; OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina; OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago. OX NCBI_TaxID=237631; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=521 / FGSC 9021; RX PubMed=17080091; DOI=10.1038/nature05248; RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., RA Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., RA Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., RA Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J., RA Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., RA Guzman P., Farman M.L., Stajich J.E., Sentandreu R., RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., RA Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., RA Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., RA Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., RA Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., RA Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.; RT "Insights from the genome of the biotrophic fungal plant pathogen RT Ustilago maydis."; RL Nature 444:97-101(2006). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACP01000086; EAK83784.1; -; Genomic_DNA. DR RefSeq; XP_758761.1; XM_753668.1. DR ProteinModelPortal; Q4PB99; -. DR STRING; 5270.UM02614.1; -. DR EnsemblFungi; UM02614T0; UM02614P0; UM02614. DR GeneID; 3630672; -. DR KEGG; uma:UM02614.1; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 568 AA; 58808 MW; 179188A6BCC27FBA CRC64; MSAPSFIDKA RVDYSVYLVT GRELLPAGVD YYESLELSLS QNNVTVVQIR EKHAETDKFL EIARRSLAIC DKYDVPMLIN DNLSVCLSLP ERVGLHIGQE DIPVSEARRI LGEKRLLGVS VKTVEQAKVA MKQGKVDYVG VGPCYGTLSK AGITEDKVIG CAGAQKIVAE LKKQEKRLPC VLIGGLNQKT AARTLFGATS AVNAPDGIAV ISAIVGRTDS DVAAKELADV VGKFKAGVIA STGSSSNGVA SSFALPPSTA QAKKDVEWYK SAIANLLSFH REASQGPPLI QTITSHVSST MSANLALAFS SSPIMSHEAA EAADLSLAIG ALVLNIGTIS PASLEGMHVA GTCANRNLKP VVLDPVGGGA TQFRKDVVRG LLNATQVTLL KGNAAELASI AGKSDQVKSR GVDSGAGALK DAVGLVKSLA QKERCLVLLS GKKDYLTDGQ TVITSDNGHP LLGAITGSGC ALGVTVGAGL AAACNLAKSQ SGDTDVRSLG NTIVAHGHVD LLVGALTGLL AMTIASEKAA ARDDVKGPGT FIPALQDELA AISAADIHRY AKIDIVTS // ID Q4UQY1_XANC8 Unreviewed; 315 AA. AC Q4UQY1; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 14-MAY-2014, entry version 67. DE SubName: Full=DGTP-pyrophosphohydrolase; GN OrderedLocusNames=XC_3499; OS Xanthomonas campestris pv. campestris (strain 8004). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=314565; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8004; RX PubMed=15899963; DOI=10.1101/gr.3378705; RA Qian W., Jia Y., Ren S.X., He Y.Q., Feng J.X., Lu L.F., Sun Q., RA Ying G., Tang D.J., Tang H., Wu W., Hao P., Wang L., Jiang B.L., RA Zeng S., Gu W.Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., RA Fang R., Qiang B., Chen Z., Zhao G.P., Tang J.L., He C.; RT "Comparative and functional genomic analyses of the pathogenicity of RT phytopathogen Xanthomonas campestris pv. campestris."; RL Genome Res. 15:757-767(2005). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000050; AAY50542.1; -; Genomic_DNA. DR RefSeq; YP_244562.1; NC_007086.1. DR ProteinModelPortal; Q4UQY1; -. DR STRING; 314565.XC_3499; -. DR EnsemblBacteria; AAY50542; AAY50542; XC_3499. DR GeneID; 3379114; -. DR KEGG; xcb:XC_3499; -. DR PATRIC; 24068689; VBIXanCam24967_3706. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XCAM314565:GCQG-3526-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34550 MW; 9C6B29D3BC9C10E2 CRC64; MPDSLRSIHV VAGVITDARG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIDAHVGA WVMDVPQLYP DKRLRLEVRE ITGWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGVL RQPDRYLITP EPQNDAAWLD GVEQALQQEI ARIQLRAPAV DPARWRALVH QVMGLRGRQR AQWLLNRDIG LASELGIGVH LGSEQLATLT ERPLPADQPV AASCHGLEDL RHAQRLGCDF AVLGPVQATA SHPGATPLGW EGFETLREQV SLPIYALGGM QPGDVREARA HGAQGIAAIR GLWPA // ID Q4X1S3_ASPFU Unreviewed; 519 AA. AC Q4X1S3; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-APR-2014, entry version 49. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative; GN ORFNames=AFUA_2G08970; OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC OS A1100) (Aspergillus fumigatus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=330879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., RA Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., RA Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., RA Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., RA Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., RA Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., RA Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., RA Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., RA Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., RA Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., RA Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., RA Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., RA Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., RA Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., RA White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., RA Machida M., Hall N., Barrell B.G., Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(2005). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAHF01000001; EAL93192.1; -; Genomic_DNA. DR RefSeq; XP_755230.1; XM_750137.1. DR ProteinModelPortal; Q4X1S3; -. DR STRING; 5085.CADAFUAP00004078; -. DR EnsemblFungi; CADAFUAT00004078; CADAFUAP00004078; CADAFUAG00004078. DR GeneID; 3513112; -. DR KEGG; afm:AFUA_2G08970; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 519 AA; 55133 MW; A3795EDB88BDF14B CRC64; MALDLSVYLV TDSTPAILKG RDLCTVVEEA LKGGVTIVQY RDKTSDTGAL IQTAKELHKI TKAYGVPLLI NDRVDVALAV GAEGVHLGQD DMYIEEAKKL LPKDAIIGIS ASSVEEAQRA IEAGADYLGI GTMFATPTKT NTKHILGTAG TQAILDAISD SSRNVGTVAI GGIKLSNVQR VIYQSKAPRK GLDGVAIVSA IMAADDPRAA AEEFVKRINN PPSFAWEPKA PRANEAAALA EEVAQIVQKM VKAQPLVHNM INYVVANFVA NVALAIGASP IMSPYGEEAV DLAKFDGALV INMGTLSRES IPNYLQAIKS YNERGNPVVY DPVGAAATHI RRGAVKELMS GGYFDLIKGN EGEIKQVSGS RNAVQRGVDS GPSTLDGQEK ARLARDLARR ERNVVLLTGA VDYLSDGERV IAVENGHEFL GQVTGTGCAV GMVSGCFLAV HPSDKLLAVL SGLLMYEIAA ENAASKDYVR GPGSFVPAFL DELYAIRQAA LKGDDSWFSG RAKIQEIKL // ID Q4ZP01_PSEU2 Unreviewed; 316 AA. AC Q4ZP01; DT 07-JUN-2005, integrated into UniProtKB/TrEMBL. DT 07-JUN-2005, sequence version 1. DT 14-MAY-2014, entry version 67. DE SubName: Full=8-oxo-dGTPase; DE EC=3.6.1.-; GN OrderedLocusNames=Psyr_4091; OS Pseudomonas syringae pv. syringae (strain B728a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=205918; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B728a; RX PubMed=16043691; DOI=10.1073/pnas.0504930102; RA Feil H., Feil W.S., Chain P., Larimer F., DiBartolo G., Copeland A., RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S., RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M., RA Kyrpides N.C., Ivanova N., Lindow S.E.; RT "Comparison of the complete genome sequences of Pseudomonas syringae RT pv. syringae B728a and pv. tomato DC3000."; RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000075; AAY39121.1; -; Genomic_DNA. DR RefSeq; YP_237159.1; NC_007005.1. DR ProteinModelPortal; Q4ZP01; -. DR STRING; 205918.Psyr_4091; -. DR EnsemblBacteria; AAY39121; AAY39121; Psyr_4091. DR GeneID; 3369627; -. DR KEGG; psb:Psyr_4091; -. DR PATRIC; 19988922; VBIPseSyr42314_4209. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PSYR205918:GJ94-4152-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 316 AA; 34126 MW; 1D4C4737F77497DE CRC64; MKRVHVAAAV IRGADGSVLI ARRADTQHQG GLWEFPGGKV EEGETVQAAL ARELQEELGI LVTAARPLIK VCHDYPDKQV LLDVWEVSAF TGQAHGAEGQ PLVWATPREL ANYDFPAANQ PIVAAARLPG EYLITPDGLD TIELLRGMQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAE QLRKYASRGR PFPENRWLAA SCHNAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWQQ AMQLIAGFNK PVFLLGGVGP AERQQAWESG AQGVAGIRAF WPDEIV // ID Q564C3_BIFAN Unreviewed; 516 AA. AC Q564C3; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 19-FEB-2014, entry version 45. DE SubName: Full=ThiE-ThiD fusion protein; DE EC=2.5.1.3; DE EC=2.7.1.49; DE EC=2.7.4.7; GN Name=thiE-thiD; OS Bifidobacterium animalis subsp. lactis (Bifidobacterium lactis). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=302911; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=15214632; DOI=10.1078/0723-2020-00274; RA Janer C., Rohr L.M., Pelaez C., Laloi M., Cleusix V., Requena T., RA Meile L.; RT "Hydrolysis of oligofructoses by the recombinant beta- RT fructofuranosidase from Bifidobacterium lactis."; RL Syst. Appl. Microbiol. 27:279-285(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY509036; AAS87045.1; -; Genomic_DNA. DR ProteinModelPortal; Q564C3; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. SQ SEQUENCE 516 AA; 54334 MW; BA2BECA74309264A CRC64; MNSFPYPSMR DRFDLRFYFV VGPDDCGNRP ILDVVAKALD GGASFIQLRA KTQDVAEIVS LANDIAEEIA GHHVEHSVAF VVDDRVDAAL EARAKGIKVD GVHIGQDDLD PVVARKLLGP DAIIGLSAKT VDEVREANHL PEGTIDYIGA GPLHMTATKP ESMIVDENGD ITTLNVSSID EMRTMSKYPL IVGGGVKADD IPMLAKTKAD GWFVVSAIAG ATDPEQATRR LVDDWTAIRG DEKPRYTGRK PAATKLPAVL TIATTDSSGG AGIPADLKTM LANDVFGECV VAGITAQNTT GVQAIAAVDP SIVGAQIDSV FDDIRPTAVK IGVIVGVESV KTVARKLRDH QATNIVVDPV MVATSGSSLA ADDTIAEEIS SLFPIATVIT PNIPEAQVLA QMPIGNQADM ETAAVQLAKD YGTCVLVKGG HGVKDADDVL AFPTGAVTWF EGERIANDNT HGTGCTLSSA IASYLAQGED LEDAVRDAKA YLSGALRANL NLGKGHGPMD HAWAMH // ID Q57BH3_BRUAB Unreviewed; 221 AA. AC Q57BH3; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 14-MAY-2014, entry version 57. DE SubName: Full=Hypothetical thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BruAb1_1692; OS Brucella abortus biovar 1 (strain 9-941). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=262698; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9-941; RX PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005; RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., RA Qing Z., Li L.L., Kapur V., Alt D.P., Olsen S.C.; RT "Completion of the genome sequence of Brucella abortus and comparison RT to the highly similar genomes of Brucella melitensis and Brucella RT suis."; RL J. Bacteriol. 187:2715-2726(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017223; AAX75011.1; -; Genomic_DNA. DR RefSeq; YP_222372.1; NC_006932.1. DR ProteinModelPortal; Q57BH3; -. DR STRING; 262698.BruAb1_1692; -. DR EnsemblBacteria; AAX75011; AAX75011; BruAb1_1692. DR GeneID; 3339652; -. DR KEGG; bmb:BruAb1_1692; -. DR PATRIC; 17825168; VBIBruAbo15061_1786. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BABO262698:GJC2-1732-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID Q57FG6_BRUAB Unreviewed; 203 AA. AC Q57FG6; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BruAb1_0209; OS Brucella abortus biovar 1 (strain 9-941). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=262698; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9-941; RX PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005; RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., RA Qing Z., Li L.L., Kapur V., Alt D.P., Olsen S.C.; RT "Completion of the genome sequence of Brucella abortus and comparison RT to the highly similar genomes of Brucella melitensis and Brucella RT suis."; RL J. Bacteriol. 187:2715-2726(2005). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017223; AAX73618.1; -; Genomic_DNA. DR RefSeq; YP_220979.1; NC_006932.1. DR ProteinModelPortal; Q57FG6; -. DR STRING; 262698.BruAb1_0209; -. DR EnsemblBacteria; AAX73618; AAX73618; BruAb1_0209. DR GeneID; 3339159; -. DR KEGG; bmb:BruAb1_0209; -. DR PATRIC; 17821975; VBIBruAbo15061_0229. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BABO262698:GJC2-212-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22348 MW; CD395C956EBFF4FA CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAF GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID Q5AEJ1_CANAL Unreviewed; 514 AA. AC Q5AEJ1; DT 26-APR-2005, integrated into UniProtKB/TrEMBL. DT 26-APR-2005, sequence version 1. DT 16-APR-2014, entry version 57. DE SubName: Full=Putative uncharacterized protein THI6; GN Name=THI6; ORFNames=CaO19.277, CaO19.7909; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; OC Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., RA Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., RA Davis R.W., Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACQ01000027; EAL01116.1; -; Genomic_DNA. DR EMBL; AACQ01000026; EAL01252.1; -; Genomic_DNA. DR RefSeq; XP_719975.1; XM_714882.1. DR RefSeq; XP_720107.1; XM_715014.1. DR STRING; 5476.CAL0004069; -. DR GeneID; 3638271; -. DR GeneID; 3638333; -. DR KEGG; cal:CaO19.277; -. DR KEGG; cal:CaO19.7909; -. DR CGD; CAL0004069; THI6. DR eggNOG; COG0352; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 514 AA; 55448 MW; 04FE09B0ACA0424B CRC64; MTLSKMKVDY TLYLVTDSGM VPESSSFLKQ VEDSINSGAT IVQLREKSLS TLEFIKRAEQ VHKLTQKQGI PLIINDRVDV ALAVNAEGVH VGQDDMPAAI ARKLIGDDKI LGVTCSNVTE VQEVVEQGIA DYVGLGTVYK TNTKKDVTDP EGTGPSGIRR MLRVLQKHNS KSGAKKIQSV AIGGINHSNV RNVMFQCAVP GEKINGVAVV SCIMANENAA EATLSLSQLI SSAPYGYEPY EESQYLDDYQ HSLKQLSSSS PMIHHITNNV VKNFSANVTL AIGASPIMSE FDEEFNELAS TPNTALVLNL GTPSKEMMKI FKNSIIAHQS RNPIVFDPVG CGASKGRLEC CRQLLDTGYF AVIKGNVGEI SALRKLTSSY RESQSKSYMR GVDSISNLTE EEIIEIGKDV SIEFKAVVVI TGPTNYIIEG EDKVVKVEGG NKLMGSITGS GCALGSTIAA FVSSQARSPQ GPNNFYAAVH AVKLYNKAGA AVSEKTPGKF MASFIDELYK LTHS // ID Q5B6F2_EMENI Unreviewed; 1490 AA. AC Q5B6F2; DT 26-APR-2005, integrated into UniProtKB/TrEMBL. DT 26-APR-2005, sequence version 1. DT 14-MAY-2014, entry version 66. DE SubName: Full=Putative uncharacterized protein; GN ORFNames=AN3878.2; OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL OS 194 / M139) (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=227321; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=16372000; DOI=10.1038/nature04341; RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., RA Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., RA Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., RA Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., RA Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., RA Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., RA Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., RA Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., RA Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.; RT "Sequencing of Aspergillus nidulans and comparative analysis with A. RT fumigatus and A. oryzae."; RL Nature 438:1105-1115(2005). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACD01000062; EAA59143.1; -; Genomic_DNA. DR RefSeq; XP_661482.1; XM_656390.1. DR ProteinModelPortal; Q5B6F2; -. DR SMR; Q5B6F2; 1098-1482. DR STRING; 162425.CADANIAP00004823; -. DR GeneID; 2873301; -. DR KEGG; ani:AN3878.2; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR004046; GST_C. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR002306; Trp-tRNA-ligase. DR Pfam; PF14497; GST_C_3; 1. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR Pfam; PF01588; tRNA_bind; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF47616; SSF47616; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. DR TIGRFAMs; TIGR00233; trpS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; SQ SEQUENCE 1490 AA; 161749 MW; EBF1F4E5AEB1E555 CRC64; MKLDLSVYLV TDSTPPILKG RDLCAVVEEA VKGGVTVVQY RDKKSDTGAQ IETARKLHRI TQAHGVPLII NDRVDVALAV GAEGVHLGQD DMVISEAKKL LPENAIIGIS ASSIEEAQAA VAAGADYLGI GTLFATPTKT NTKHIIGTAG TQAILDSIAE SGRDVGTVCI GGINLSNVQR VLYQSASPRK SLNGAAIVSA IMAADDPRAA AAELARAIAT PPPFVRKADG PLVRNVAGLL EKVPHIVQKM VEIHPLVHNM INFVVANFVA NVTLAIGASP IMSPYGDEAT DLCQFDGALL INMGTLTSQS PSEYLKAIRA YNQRGNPVVY DPVGAGATQI RRGVVKELMA GGYFDLIKGN EGEIRQVAGS TSVQQRGVDS GPSTLDHQGK ARLARDLARR EKNIVLLTGA VDYLSDGERI VAVENGHELL GQVTGTGCAV GTVAGCFIAA NPTDKFLAVL SALLMYEIAA ENAAARDSVR GPGSFATTFI DELYAIRQAS LQGDHSWYAG RARFSRTSSF LKPHILGRDN VVPTGGESGM WLVRHDSAHF LWDDSSRPPE RSLLLGIPHL AKLSLFNPFS TLIRVSRVFP RTAYPLANTL RVNHVTPLLR PPAKYPAYTF ANMAINSAPE SSLLSLLYRS YPAAISPDET EPDLLAVNPK VFPGVTYNAS DEADIKQWLA TTSSLQSALS KDDKSAVSDI LAQINTHLAT RTTLLGNKAS VADVAAYALL APVVEKWSPE ERTGEKGYHN IVRHVDFVQN SRVFSLQIPD EEKVKIDVND VRFVPKPVDP KAEKERKKKE KAAAQGAGAE QTVVVGQTKP EKAAPDAAAA GKAEGKPKKE KKEKKEKQPK PAPAPAAPPS PSLIDLRVGH ILRAVNHPNA DSLYVSTIDC GDAPGSDNTS VDEETGKTVR TVCSGLNGLV PLEEMQGRKI VAVCNLKPVT MRGIKSAAMV LAASPRVAEG EDSHAGPVEL VTPPADAPAG DRIYFEGWND GEPEKVLNPK KKVWETFQPG FTTTDSLEVA FDSSAVPVAQ SQQGKPALGK LVAKSGGVCT VKTLKGATSI GLNILTMAET PATANKVVSE LDINPWSVAG GTDASGNAIQ IDYEALSKKW NTSLIDQALL DRFEKVTGHK PHRWLRRGLF FSHRDFEKIL TKKEKGEPFF LYTGRGPSSG SLHLGHTIPL TFTKWLQDVF DVPLVFMLTD DEKALFKDSL TFEETLHYAM ENAKDIIALG FDLKKTFIYS DLKYVSNHIL MNTWEFSKLV TFNQVRGAFG FNESTNIGRI FFPSVQCVAA FATSYPEIWT DEPLKERKKE IAEIQCLIPM GIDQDPYFRL LRDNAHKMRF PSPKPALIHS KFLTALQGAG GKMSSSDPNS AIFMTDTAKQ IKTKINKYAF SGGQVSIEDH RRLGGNPDVD VSYIYLTYFE DDDAKLEEIY KSYKSGELLT GELKALAIKK LQEYVAEFQD RRKEVTDELL EKYMTPRRLE WSGTAHPKIK // ID Q5E0Q4_VIBF1 Unreviewed; 212 AA. AC Q5E0Q4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 14-MAY-2014, entry version 72. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=VF_A0322; OS Vibrio fischeri (strain ATCC 700601 / ES114). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=312309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700601 / ES114; RX PubMed=15703294; DOI=10.1073/pnas.0409900102; RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., RA Stevens A., Visick K., Whistler C., Greenberg E.P.; RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium RT with pathogenic congeners."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000021; AAW87392.1; -; Genomic_DNA. DR RefSeq; YP_206280.1; NC_006841.2. DR ProteinModelPortal; Q5E0Q4; -. DR STRING; 312309.VF_A0322; -. DR EnsemblBacteria; AAW87392; AAW87392; VF_A0322. DR GeneID; 3280572; -. DR KEGG; vfi:VF_A0322; -. DR PATRIC; 20116626; VBIVibFis127983_2926. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AFIS312309:GIWP-3065-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22766 MW; 088364E4242AB1C7 CRC64; MNNPYTLYLV TDEKQDIDTL CHVVAEAVKG GVTMVQVREK HGDVRAFIQR SLAIKEILKD SGVPLIINDR VDVALAVQAD GVHLGQSDMP AQIARQLIGP DMILGLSVEN ETQLCNAQEL PVDYLGISAI FSTPTKTNII KEWGIQGLAF AVKESQLPLV AIGGINDSNI REVVDTGVDG IALVSAICHA SSPKQASQAL LGLMNDDVEL KK // ID Q5E8W8_VIBF1 Unreviewed; 219 AA. AC Q5E8W8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 14-MAY-2014, entry version 74. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=VF_0033; OS Vibrio fischeri (strain ATCC 700601 / ES114). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=312309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700601 / ES114; RX PubMed=15703294; DOI=10.1073/pnas.0409900102; RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., RA Stevens A., Visick K., Whistler C., Greenberg E.P.; RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium RT with pathogenic congeners."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000020; AAW84528.1; -; Genomic_DNA. DR RefSeq; YP_203416.1; NC_006840.2. DR ProteinModelPortal; Q5E8W8; -. DR STRING; 312309.VF_0033; -. DR EnsemblBacteria; AAW84528; AAW84528; VF_0033. DR GeneID; 3279828; -. DR KEGG; vfi:VF_0033; -. DR PATRIC; 20110555; VBIVibFis127983_0035. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KWRERTN; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; AFIS312309:GIWP-34-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24221 MW; DF94786684C96456 CRC64; MFAFPNIDKS KFGLYPVVDD VSWIEKLLKL DVKTIQLRIK NPEQADLEQQ IIKAIRLGRE YDAQVFINDY WQLAIKHNAF GIHLGQEDIE VADLQAIAEA NICLGLSTHD DSELLKVKAL NPSYLALGHI FPTPTKEMPS QPQGLTNLAK NQQLAGDTPT VAIGGIDLSV ANDVWQTGVD SIAVVRAITE AEDTEQAVAK FNAIISEPRR GNLQEVAYE // ID Q5FFG1_EHRRG Unreviewed; 350 AA. AC Q5FFG1; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 14-MAY-2014, entry version 71. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ERGA_CDS_02030; OS Ehrlichia ruminantium (strain Gardel). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=302409; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Gardel; RX PubMed=16547041; DOI=10.1128/JB.188.7.2533-2542.2006; RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., RA Martinez D.; RT "Comparative genomic analysis of three strains of Ehrlichia RT ruminantium reveals an active process of genome size plasticity."; RL J. Bacteriol. 188:2533-2542(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR925677; CAI27655.1; -; Genomic_DNA. DR RefSeq; YP_196129.1; NC_006831.1. DR ProteinModelPortal; Q5FFG1; -. DR STRING; 302409.ERGA_CDS_02030; -. DR EnsemblBacteria; CAI27655; CAI27655; ERGA_CDS_02030. DR GeneID; 3268781; -. DR KEGG; erg:ERGA_CDS_02030; -. DR PATRIC; 20578095; VBIEhrRum72196_0214. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; YKAYGVH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ERUM302409:GHVW-218-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 181 185 HMP-PP binding (By similarity). FT REGION 329 330 THZ-P binding (By similarity). FT METAL 214 214 Magnesium (By similarity). FT METAL 233 233 Magnesium (By similarity). FT BINDING 213 213 HMP-PP (By similarity). FT BINDING 252 252 HMP-PP (By similarity). FT BINDING 281 281 HMP-PP (By similarity). FT BINDING 309 309 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 350 AA; 40114 MW; A3E630ED61DE888C CRC64; MHQCNCDEIY IVDQADLIEF CSIQLKEPAD VINSVNLLYD IKKKNIYVVD VINTDSNLCR DYYFDGEKGF WLFYNRIESN TKTEFISIYK KTNTLASKCL NCCDIQKDSL VLARAFMNQI AKQCTSFLDE ECFPTVVYDN HSNNFAKIKF SSILEPIGFY QIVPNLSWLK YVVNCGVKVI QLRIKDESMD KVIQEVEEGI YIANKYGIKL FINDYWELAI KYKAYGVHLG QEDLQNANFQ EIFNAGLRLG ISTHCYYELA IARYLSPSYI AFGPIFPTML KNMNFMSQGV SLLASWVKHL HYRIVAIGGI NLSNLDSIIK TGVDGIAVIS AVINSKYPDK DIREFLDKCS // ID Q5FNT4_GLUOX Unreviewed; 203 AA. AC Q5FNT4; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 14-MAY-2014, entry version 75. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=GOX2228; OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=290633; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=621H; RX PubMed=15665824; DOI=10.1038/nbt1062; RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., RA Ehrenreich A., Gottschalk G., Deppenmeier U.; RT "Complete genome sequence of the acetic acid bacterium Gluconobacter RT oxydans."; RL Nat. Biotechnol. 23:195-200(2005). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000009; AAW61963.1; -; Genomic_DNA. DR RefSeq; YP_192619.1; NC_006677.1. DR ProteinModelPortal; Q5FNT4; -. DR STRING; 290633.GOX2228; -. DR EnsemblBacteria; AAW61963; AAW61963; GOX2228. DR GeneID; 3249847; -. DR KEGG; gox:GOX2228; -. DR PATRIC; 32612418; VBIGluOxy81109_2544. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; GOXY290633:GHB3-2226-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22603 MW; D5D3A8991B40AF04 CRC64; MMTLDPFYLL VGEVGLLETL LPCGVRLVQL RLKDKPEAEI RCQIRHARDL CERHGAQLVI NDYWRLALEL GCDFVHLGQE DMETADFAAL RDAGIRFGLS THDPAELERA LSYEPAYVAL GPVYPTLLKK MKWGPQGLER VADWKKRAGQ TPLVAIGGLT PERLPGVFFA GADSAAVVTD IQMADDPVAR CREWVAATRA YVR // ID Q5FUD4_GLUOX Unreviewed; 192 AA. AC Q5FUD4; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 14-MAY-2014, entry version 49. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=GOX0229; OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=290633; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=621H; RX PubMed=15665824; DOI=10.1038/nbt1062; RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., RA Ehrenreich A., Gottschalk G., Deppenmeier U.; RT "Complete genome sequence of the acetic acid bacterium Gluconobacter RT oxydans."; RL Nat. Biotechnol. 23:195-200(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000009; AAW60012.1; -; Genomic_DNA. DR RefSeq; YP_190668.1; NC_006677.1. DR ProteinModelPortal; Q5FUD4; -. DR STRING; 290633.GOX0229; -. DR EnsemblBacteria; AAW60012; AAW60012; GOX0229. DR GeneID; 3248607; -. DR KEGG; gox:GOX0229; -. DR PATRIC; 32608138; VBIGluOxy81109_0450. DR KO; K00788; -. DR OMA; NIRNTED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GOXY290633:GHB3-229-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 192 AA; 20184 MW; A50812225C8A8880 CRC64; MTACDLYPVL PAGFKTDAAL EVLRDILVLP EITALRIPAG WTPEATQLSQ LVDLLHANGV AMILEVAGSL ADTPKSLLGI CDGLHVANVE DLVSLRKTVG SDMPVGCLCT NRDDAMKSGE SGADYVAFPP GDLELVKWWS SVMELPGVAE NIRNTEDASS AITAGADFLA IPLQFDGKDA ERFSAMAVLA AG // ID Q5FUY3_GLUOX Unreviewed; 206 AA. AC Q5FUY3; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=GOX0009; OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=290633; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=621H; RX PubMed=15665824; DOI=10.1038/nbt1062; RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., RA Ehrenreich A., Gottschalk G., Deppenmeier U.; RT "Complete genome sequence of the acetic acid bacterium Gluconobacter RT oxydans."; RL Nat. Biotechnol. 23:195-200(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000009; AAW59808.1; -; Genomic_DNA. DR RefSeq; YP_190464.1; NC_006677.1. DR ProteinModelPortal; Q5FUY3; -. DR STRING; 290633.GOX0009; -. DR EnsemblBacteria; AAW59808; AAW59808; GOX0009. DR GeneID; 3249144; -. DR KEGG; gox:GOX0009; -. DR PATRIC; 32607678; VBIGluOxy81109_0235. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HTHEELQ; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; GOXY290633:GHB3-9-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 206 AA; 22800 MW; B9F0403417633485 CRC64; MSSLPSRIYA VVDHPRWVER LGGAGLRFIE LYLRDLPEEE IRAQALLAQE LAARFNVSLA LNRYWQTAIE LGYEWLHLGP EDLETADLNA IRTAGIRFGI STHTHEELQT ALACKPDYVS FGPVWSTQLR GVPLTGRGLE KLAEWRGLCG NVPLVAIGGI TVPRLAECLE AGADTVAVMS DFIGHQDPEG QVRRWLDAVS RETAPT // ID Q5GW51_XANOR Unreviewed; 315 AA. AC Q5GW51; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 14-MAY-2014, entry version 69. DE SubName: Full=Thiamine monophosphate synthase; GN Name=ThiE; OrderedLocusNames=XOO3816; OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=291331; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC10331 / KXO85; RX PubMed=15673718; DOI=10.1093/nar/gki206; RA Lee B.M., Park Y.J., Park D.S., Kang H.W., Kim J.G., Song E.S., RA Park I.C., Yoon U.H., Hahn J.H., Koo B.S., Lee G.B., Kim H., RA Park H.S., Yoon K.O., Kim J.H., Jung C.H., Koh N.H., Seo J.S., RA Go S.J.; RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, RT the bacterial blight pathogen of rice."; RL Nucleic Acids Res. 33:577-586(2005). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE013598; AAW77070.1; -; Genomic_DNA. DR RefSeq; YP_202455.1; NC_006834.1. DR ProteinModelPortal; Q5GW51; -. DR STRING; 291331.XOO3816; -. DR EnsemblBacteria; AAW77070; AAW77070; XOO3816. DR GeneID; 3263870; -. DR KEGG; xoo:XOO3816; -. DR PATRIC; 24107219; VBIXanOry111333_4220. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XORY291331:GJBV-3540-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34826 MW; 851AEAEA9B66C6A6 CRC64; MPDSLRSIHV VAGVITDPRG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIEAQVGD WLMDVPQLYP DKRLRLEVRH ITAWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGAL RQPDHYLITP EPEDDARWLE GLERALQNGI TRIQLRARQT APAQWQALLQ QVMRLRGRTR AQLLLNRDIA LAAELGVGVH LGSEQLAGLQ ERPLPAEQLV AASCHGLDDL RHAQRIGCDF AVLGPVQATA SHPGATPLGW GGFETLREQV SLPIYALGGM QIEDVREARS HGAQGIAAIR SLWPQ // ID Q5H3U4_XANOR Unreviewed; 223 AA. AC Q5H3U4; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 14-MAY-2014, entry version 78. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=XOO1123; OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=291331; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC10331 / KXO85; RX PubMed=15673718; DOI=10.1093/nar/gki206; RA Lee B.M., Park Y.J., Park D.S., Kang H.W., Kim J.G., Song E.S., RA Park I.C., Yoon U.H., Hahn J.H., Koo B.S., Lee G.B., Kim H., RA Park H.S., Yoon K.O., Kim J.H., Jung C.H., Koh N.H., Seo J.S., RA Go S.J.; RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, RT the bacterial blight pathogen of rice."; RL Nucleic Acids Res. 33:577-586(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE013598; AAW74377.1; -; Genomic_DNA. DR RefSeq; YP_199762.1; NC_006834.1. DR ProteinModelPortal; Q5H3U4; -. DR STRING; 291331.XOO1123; -. DR EnsemblBacteria; AAW74377; AAW74377; XOO1123. DR GeneID; 3265048; -. DR KEGG; xoo:XOO1123; -. DR PATRIC; 24101231; VBIXanOry111333_1250. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XORY291331:GJBV-1039-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 54 58 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 87 87 Magnesium (By similarity). FT METAL 106 106 Magnesium (By similarity). FT BINDING 86 86 HMP-PP (By similarity). FT BINDING 125 125 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23007 MW; E5888F6BB6D90C55 CRC64; MGLHCPIPST AFGSAAMPNR LNVRGVYLIT PDEPNTQRLL LRTTPLLASI AWLQYRNKQA DAALRLRQAS ALREACVAHG VPLIINDDAQ LAAQVGAQGV HLGEDDGEVT AARALLGEHA IIGVSCYDAI GRARAAAAAG ASYVAFGAFF PTITKQTTRR ATPALLEQAA ELHLARVAIG GIAPAQVPAL VTAGADLIAV VSGVYAAPDP VAAVQAYRAG FAA // ID Q5HBW9_EHRRW Unreviewed; 350 AA. AC Q5HBW9; Q5FCZ7; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 14-MAY-2014, entry version 79. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=probable thiE; Synonyms=thiE; GN OrderedLocusNames=Erum2060, ERWE_CDS_02080; OS Ehrlichia ruminantium (strain Welgevonden). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=254945; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Welgevonden, and Welgevonden [ARC-OVI]; RX PubMed=15637156; DOI=10.1073/pnas.0406633102; RA Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., RA Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., RA Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., RA Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., RA Allsopp M.T., Allsopp B.A.; RT "The genome of the heartwater agent Ehrlichia ruminantium contains RT multiple tandem repeats of actively variable copy number."; RL Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Welgevonden [CIRAD]; RX PubMed=16547041; DOI=10.1128/JB.188.7.2533-2542.2006; RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., RA Martinez D.; RT "Comparative genomic analysis of three strains of Ehrlichia RT ruminantium reveals an active process of genome size plasticity."; RL J. Bacteriol. 188:2533-2542(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR767821; CAH57924.1; -; Genomic_DNA. DR EMBL; CR925678; CAI26702.1; -; Genomic_DNA. DR RefSeq; YP_180075.1; NC_005295.2. DR RefSeq; YP_197084.1; NC_006832.1. DR ProteinModelPortal; Q5HBW9; -. DR STRING; 254945.Erum2060; -. DR EnsemblBacteria; CAH57924; CAH57924; Erum2060. DR EnsemblBacteria; CAI26702; CAI26702; ERWE_CDS_02080. DR GeneID; 3232610; -. DR GeneID; 3260722; -. DR KEGG; eru:Erum2060; -. DR KEGG; erw:ERWE_CDS_02080; -. DR PATRIC; 20580195; VBIEhrRum92411_0222. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; YKAYGVH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ERUM254945:GJ2L-223-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 181 185 HMP-PP binding (By similarity). FT REGION 329 330 THZ-P binding (By similarity). FT METAL 214 214 Magnesium (By similarity). FT METAL 233 233 Magnesium (By similarity). FT BINDING 213 213 HMP-PP (By similarity). FT BINDING 252 252 HMP-PP (By similarity). FT BINDING 281 281 HMP-PP (By similarity). FT BINDING 309 309 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 350 AA; 40026 MW; DE4BEE65E1D57314 CRC64; MHQCNCDEIY IVDQADLIEF CAIQLKEPAD VINSVNLLYN VKKKNIYVVD VINTDSNLCR DYYFDGEKGF WLFYNRIESN TKTEFISIYK KTNTLASKCL SCCDIQKDSL VLARAFMNQI VKQCTSFLDE ECFPTVVYDN HSNNFAKIKF SSILEPIGFY QIVPNLSWLK YVINCGVKVI QLRIKDESMD KVIQEVEEGV YIANKYGIKL FINDYWELAI KYKAYGVHLG QEDLQNANFQ EIFNAGLRLG ISTHCYYELA IARYLSPSYI AFGPIFPTML KNMNFMSQGV SLLASWVKHL HYRIVAIGGI NLSNLDSIIK TGVDGIAVVS AVINSKYPDK AIREFLDKCS // ID Q5HLB7_STAEQ Unreviewed; 152 AA. AC Q5HLB7; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 14-MAY-2014, entry version 59. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=SERP2070; OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=176279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35984 / RP62A; RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., Deboy R.T., RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L., Beanan M., RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., RA Haft D.H., Vamathevan J., Khouri H., Utterback T., Lee C., RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K., RA Hance I.R., Nelson K.E., Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete RT genome analysis of an early methicillin-resistant Staphylococcus RT aureus strain and a biofilm-producing methicillin-resistant RT Staphylococcus epidermidis strain."; RL J. Bacteriol. 187:2426-2438(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000029; AAW52932.1; -; Genomic_DNA. DR RefSeq; YP_189626.1; NC_002976.3. DR ProteinModelPortal; Q5HLB7; -. DR STRING; 176279.SERP2070; -. DR EnsemblBacteria; AAW52932; AAW52932; SERP2070. DR GeneID; 3240573; -. DR KEGG; ser:SERP2070; -. DR PATRIC; 19615054; VBIStaEpi130894_2016. DR eggNOG; COG0352; -. DR HOGENOM; HOG000090085; -. DR OMA; FAGICAI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SEPI176279:GJJB-2147-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 152 AA; 17203 MW; 5BB8AF5DBECD383B CRC64; MIQSLLQLGF SKDKIIIHSD VTLLEDLHLK RIHFKENDTT AFTYKEAHPD ICVSMSTHDV ETVKRCYENG LDSVFFGHIF PTSSHPNVPP RSKEAIQQAL NVPIPIYAIG GINEHSLQKM PPGFKGICAI SYFNNASLEE IKQLRKEWST HA // ID Q5HU58_CAMJR Unreviewed; 201 AA. AC Q5HU58; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 14-MAY-2014, entry version 58. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=CJE1187; OS Campylobacter jejuni (strain RM1221). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=195099; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM1221; RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015; RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., RA Nelson K.E.; RT "Major structural differences and novel potential virulence mechanisms RT from the genomes of multiple Campylobacter species."; RL PLoS Biol. 3:72-85(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000025; AAW35512.1; -; Genomic_DNA. DR PIR; H81306; H81306. DR RefSeq; YP_179177.1; NC_003912.7. DR ProteinModelPortal; Q5HU58; -. DR STRING; 195099.CJE1187; -. DR EnsemblBacteria; AAW35512; AAW35512; CJE1187. DR GeneID; 3231696; -. DR KEGG; cjr:CJE1187; -. DR PATRIC; 20044170; VBICamJej134361_1203. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CJEJ195099:GJC0-1214-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 23462 MW; 5215A3BA4607D5F1 CRC64; MWDKKIIAIS DRKCVEIDFL KQIEKLAKAK VDAIVLREKD LSEFEYYDLA KEVLSICAKQ KVTCFLHFFD RECLKLGHRY FHAPLSLLRK EPKLTKYFHI LGTSVHSKEE LLEAMSYKVN YAFVGHIFES SCKMGLEPKG IDFLKSLLEF SQIPLYAIGG INAQNIENFK DINVVGVCMR EILMKEKDLK KYLLECRQNL R // ID Q5KB56_CRYNJ Unreviewed; 555 AA. AC Q5KB56; Q55MT0; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 16-APR-2014, entry version 68. DE SubName: Full=Thiamine biosynthetic bifunctional enzyme, putative; GN OrderedLocusNames=CNI03710; OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / OS ATCC MYA-565) (Filobasidiella neoformans). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Tremellomycetes; Tremellales; Tremellaceae; Filobasidiella; OC Filobasidiella/Cryptococcus neoformans species complex. OX NCBI_TaxID=214684; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JEC21 / ATCC MYA-565; RX PubMed=15653466; DOI=10.1126/science.1103773; RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., RA D'Souza C.A., Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., RA Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., RA Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., RA Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., RA Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., RA Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., RA Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., RA Fraser C.M., Hyman R.W.; RT "The genome of the basidiomycetous yeast and human pathogen RT Cryptococcus neoformans."; RL Science 307:1321-1324(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017349; AAW45288.1; -; Genomic_DNA. DR RefSeq; XP_572595.1; XM_572595.1. DR UniGene; Fne.663; -. DR ProteinModelPortal; Q5KB56; -. DR STRING; 214684.CNI03710; -. DR EnsemblFungi; AAW45288; AAW45288; CNI03710. DR GeneID; 3259752; -. DR KEGG; cne:CNI03710; -. DR KO; K14154; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 555 AA; 59219 MW; 012F5FD0ECE906DF CRC64; MPKPTLDYSL YLVTGRELLP PGKDYYESLE ESLQGGVTLV QVREKYADTG EFIEVARRTK AICDKYNVPV LINDRIDVHL AVGTAGIHVG QTDCPIGLAR SLVGPDAIIG LSVSNVNEAK RAIQQGADYV GIGAVWPTNS KDVANKKMLG PDGVGEILDL LHGTGVQSVA IGGIHLPNVA QLLHASIAPQ SRNALDGIAI ISDIVASLTP REAATNLREV VQSFKRARSQ LSNLEAVYGT NLFSGPRGVD GFIKEAVHLM DVIKRETPLI NQMTNNVVIN DSANVTLAIG ASPIMATHPR DVHDLSPAIG ALLINFGYDS YQCSFKSLML MLESSTITDK AGMLVAGRQA NINRKPIIFD PVAIGATPYR QETSVELLSH WQPTIIKGNA GEIGFMARST EVASRGVDSV GSGFSRPGAV VKALARKQAA IIVLTGEHDY ISDGSTTLKI SNGHHYLERI TGSGCQLGSV IASFAATARL EHLAKHGEWE NASQLVQGDM LAAAVTGVLV YTIAAEVAAA REDVKGPGTF RAALIDELYN LTPEVLQQRA KVEIL // ID Q5L2C3_GEOKA Unreviewed; 201 AA. AC Q5L2C3; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=GK0622; OS Geobacillus kaustophilus (strain HTA426). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=235909; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTA426; RX PubMed=15576355; DOI=10.1093/nar/gkh970; RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., RA Matsui S., Uchiyama I.; RT "Thermoadaptation trait revealed by the genome sequence of RT thermophilic Geobacillus kaustophilus."; RL Nucleic Acids Res. 32:6292-6303(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000043; BAD74907.1; -; Genomic_DNA. DR RefSeq; YP_146475.1; NC_006510.1. DR ProteinModelPortal; Q5L2C3; -. DR STRING; 235909.GK0622; -. DR EnsemblBacteria; BAD74907; BAD74907; GK0622. DR GeneID; 3184753; -. DR KEGG; gka:GK0622; -. DR PATRIC; 21962451; VBIGeoKau81518_0697. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GKAU235909:GJO7-697-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 201 AA; 21085 MW; 88EB5141BF610405 CRC64; MGVLHFVSTG RQTVDEFAAI CAHTHPYADL IHIREKGKTA REVAAFVAAL LRVGVPLQKI IVNDRVDVAA VYGVKGVQLA YHSLPVRAVR RSFPDLTVGC SVHGSEEAKQ AEQDGAHFCL YGHIFPTDSK PGLPPRGLDS LAEIAAAVSI PVIAIGGIHA GNARRVLEAG AAGVAVLSAV FFAADPVAEA KRLADIVKGR G // ID Q5LCA1_BACFN Unreviewed; 202 AA. AC Q5LCA1; DT 21-JUN-2005, integrated into UniProtKB/TrEMBL. DT 21-JUN-2005, sequence version 1. DT 14-MAY-2014, entry version 51. DE SubName: Full=Putative thiamine phosphate pyrophosphorylase; GN ORFNames=BF9343_2483; OS Bacteroides fragilis (strain ATCC 25285 / NCTC 9343). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=272559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25285 / NCTC 9343; RX PubMed=15746427; DOI=10.1126/science.1107008; RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., RA Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., RA Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., RA Line A., Lord A., Norbertczak H., Ormond D., Price C., RA Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J.; RT "Extensive DNA inversions in the B. fragilis genome control variable RT gene expression."; RL Science 307:1463-1465(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR626927; CAH08264.1; -; Genomic_DNA. DR RefSeq; YP_212188.1; NC_003228.3. DR ProteinModelPortal; Q5LCA1; -. DR SMR; Q5LCA1; 1-202. DR STRING; 272559.BF2564; -. DR EnsemblBacteria; CAH08264; CAH08264; BF9343_2483. DR GeneID; 3287407; -. DR KEGG; bfs:BF2564; -. DR PATRIC; 21041694; VBIBacFra29119_2574. DR eggNOG; NOG86118; -. DR HOGENOM; HOG000228370; -. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR OrthoDB; EOG6RC3V1; -. DR BioCyc; BFRA272559:GKF0-2519-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 23245 MW; A6533F52928C16DB CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHKRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYSGH ISCSCHSVEE VKNKKHFYDY VFMSPVYDSI SKEGYNSPYT AEELRLAAKD KIIDNKVMAL GGITPDNILE VKDFGFGGAV VLGDLWGKFD ACSDQDYLAV IEHFKKLKRM AD // ID Q5LRR9_RUEPO Unreviewed; 206 AA. AC Q5LRR9; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=SPO2056; OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) OS (Silicibacter pomeroyi). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=246200; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3; RX PubMed=15602564; DOI=10.1038/nature03170; RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L., RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., RA Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A., RA Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J., RA Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., RA Haft D.H., Selengut J., Ward N.; RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the RT marine environment."; RL Nature 432:910-913(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000031; AAV95327.1; -; Genomic_DNA. DR RefSeq; YP_167286.1; NC_003911.12. DR ProteinModelPortal; Q5LRR9; -. DR STRING; 246200.SPO2056; -. DR EnsemblBacteria; AAV95327; AAV95327; SPO2056. DR GeneID; 3194714; -. DR KEGG; sil:SPO2056; -. DR PATRIC; 23377453; VBIRuePom114501_2083. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 21763 MW; D8863E2A5108DA02 CRC64; METPEQPQLY LITPPSIDLD LFPDQLARVL DGAEIACIRL ALASRDEDLL SRAADACREV AHARDVALVI ADHVLLAQRL GLDGVHLSDA ARSVRAARKE LGADAIVGSF CGTSRHDGMS AGEAGADYVA FGPIGAHGLD DGSVAERDLF EWWSAVIEVP VVAEGALTAD LVRSFAPITD FFGVGDEIWS AEDPLAALKG LISAMT // ID Q5LWJ0_RUEPO Unreviewed; 198 AA. AC Q5LWJ0; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 14-MAY-2014, entry version 74. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=SPO0048; OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) OS (Silicibacter pomeroyi). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=246200; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3; RX PubMed=15602564; DOI=10.1038/nature03170; RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L., RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., RA Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A., RA Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J., RA Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., RA Haft D.H., Selengut J., Ward N.; RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the RT marine environment."; RL Nature 432:910-913(2004). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000031; AAV93379.1; -; Genomic_DNA. DR RefSeq; YP_165322.1; NC_003911.12. DR ProteinModelPortal; Q5LWJ0; -. DR STRING; 246200.SPO0048; -. DR EnsemblBacteria; AAV93379; AAV93379; SPO0048. DR GeneID; 3194380; -. DR KEGG; sil:SPO0048; -. DR PATRIC; 23373331; VBIRuePom114501_0051. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 198 AA; 22089 MW; 7EB8780A172D928F CRC64; MTLDRFYPIF DHTDWLRRML PLGVKLVQLR IKDQSDPVIR AEIDTARDLC RAHGAVLVIN DYWQAAIDAG CDWLHLGQED LDQADLPAIR KAGLRLGVST HDDDELERVL GMDPDYVALG PVYPTILKQM KWHQQGLPRV TEWKARVGSI PLVGIGGMSV ERAPGVLGAG ADIVSVVTDI TLNADPEARV HQWIEVTR // ID Q5N4T8_SYNP6 Unreviewed; 343 AA. AC Q5N4T8; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 14-MAY-2014, entry version 71. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=syc0491_c; OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) OS (Anacystis nidulans). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=269084; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1; RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4; RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., RA Kanehisa M., Omata T., Sugiura M., Sugita M.; RT "Complete nucleotide sequence of the freshwater unicellular RT cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene RT content and organization."; RL Photosyn. Res. 93:55-67(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008231; BAD78681.1; -; Genomic_DNA. DR RefSeq; YP_171201.1; NC_006576.1. DR ProteinModelPortal; Q5N4T8; -. DR STRING; 269084.syc0491_c; -. DR EnsemblBacteria; BAD78681; BAD78681; syc0491_c. DR GeneID; 3199792; -. DR KEGG; syc:syc0491_c; -. DR PATRIC; 32486582; VBISynElo117686_0565. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SELO269084:GCDQ-500-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 1 128 Unknown (By similarity). FT REGION 129 343 Thiamine-phosphate synthase (By FT similarity). FT REGION 176 180 HMP-PP binding (By similarity). FT REGION 273 275 THZ-P binding (By similarity). FT METAL 209 209 Magnesium (By similarity). FT METAL 228 228 Magnesium (By similarity). FT BINDING 208 208 HMP-PP (By similarity). FT BINDING 247 247 HMP-PP (By similarity). FT BINDING 276 276 HMP-PP (By similarity). FT BINDING 303 303 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 343 AA; 37966 MW; A84F21FB8685160B CRC64; MSSESSMDWV ETRCHRILDA NLDRAREGLR ILEEWCRFGL ERADLSATCK ALRQEVGSWH RPKFRQARDT THDPGTSLSH PQERQRTDLN AVLLANCARV QEALRVIEEY GKLIEGDLSD RAKAMRYQIY VLESQLQSRD RLSRLRQARL YLVTSPHPRL LEVVEAALSA GLKLVQYRDK QQEDATRLET ACRLAELCQR YGALFLVNDR VDLALACGAD GVHLGQQDVP MDVARRILGP DRIVGRSTTS PEELARANAE GADYVGVGPI FATPTKPGKA AAGFDYLGYA RQQAQQPFYA IGGIDVSNAA AVVAAGADRL AVVRAIMEAP DPKAATAELL QML // ID Q5NML1_ZYMMO Unreviewed; 196 AA. AC Q5NML1; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 14-MAY-2014, entry version 54. DE SubName: Full=Thiamine monophosphate synthase; GN OrderedLocusNames=ZMO1425; OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=264203; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31821 / ZM4 / CP4; RX PubMed=15592456; DOI=10.1038/nbt1045; RA Seo J.S., Chong H., Park H.S., Yoon K.O., Jung C., Kim J.J., RA Hong J.H., Kim H., Kim J.H., Kil J.I., Park C.J., Oh H.M., Lee J.S., RA Jin S.J., Um H.W., Lee H.J., Oh S.J., Kim J.Y., Kang H.L., Lee S.Y., RA Lee K.J., Kang H.S.; RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis RT ZM4."; RL Nat. Biotechnol. 23:63-68(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008692; AAV90049.1; -; Genomic_DNA. DR RefSeq; YP_163160.1; NC_006526.2. DR ProteinModelPortal; Q5NML1; -. DR STRING; 264203.ZMO1425; -. DR EnsemblBacteria; AAV90049; AAV90049; ZMO1425. DR GeneID; 3188400; -. DR KEGG; zmo:ZMO1425; -. DR PATRIC; 32568124; VBIZymMob102260_1347. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; NRRDSIM; -. DR OrthoDB; EOG679THR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 196 AA; 22971 MW; E9F7A99D946DC6CA CRC64; MNDKLKNTWP RLWLMTDERF GDGLLEAVKK LPQGSGIVFR HYRLPFKIRK NLFQKIQRIA KKRKLVLFLA DSARLAAAWK ADGVHGRFSS QRTARPLLRS QAVHNRRDSI MCRKVDFVFL SPLFSTRSHP GKPFLGRVKF LQLKRSIRQK VFALGGINAK TIRALPACDG FSGIDIWQDD EFRHHRLWFF WANQQR // ID Q5P2L6_AROAE Unreviewed; 313 AA. AC Q5P2L6; DT 04-JAN-2005, integrated into UniProtKB/TrEMBL. DT 04-JAN-2005, sequence version 1. DT 14-MAY-2014, entry version 75. DE SubName: Full=NUDIX hydrolase; GN ORFNames=ebA4102; OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Aromatoleum. OX NCBI_TaxID=76114; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EbN1; RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9; RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., RA Reinhardt R.; RT "The genome sequence of an anaerobic aromatic-degrading denitrifying RT bacterium, strain EbN1."; RL Arch. Microbiol. 183:27-36(2005). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR555306; CAI08448.1; -; Genomic_DNA. DR RefSeq; YP_159349.1; NC_006513.1. DR ProteinModelPortal; Q5P2L6; -. DR STRING; 76114.ebA4102; -. DR EnsemblBacteria; CAI08448; CAI08448; ebA4102. DR GeneID; 3180043; -. DR KEGG; eba:ebA4102; -. DR PATRIC; 20970816; VBIAroAro98752_2352. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AARO76114:GJTA-2348-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 313 AA; 34305 MW; DA89FC3E417A9479 CRC64; MKKRVEVAAG VITRPDGSFL LGQRAPDTFY PGYWEFPGGK VEAGETAEQA LVRELDEELG IRVTCIRPWI TREHRYEHAH VRLHFFEVTA WDGEINDHVH SALSWEHAGW LGVGPMLPAN GPILKALHLP RWMGITHAVD IGTKVQLARL DAALERGLRL VQVREPGMPR DELASFAGAV IRRAREYRAL VVINQDSGLA HELGADGVHL PAAELGRTTA RPAFEWVGAS CHCRAELERA AGLGLDYALL GAVRPTLTHP HRETLGWHAF AELVRDLPIP VLALGGLVEA DMEPARSAGA HGIAGIRGVW LQS // ID Q5PBC4_ANAMM Unreviewed; 340 AA. AC Q5PBC4; DT 04-JAN-2005, integrated into UniProtKB/TrEMBL. DT 04-JAN-2005, sequence version 1. DT 14-MAY-2014, entry version 70. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=AM318; OS Anaplasma marginale (strain St. Maries). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Anaplasma. OX NCBI_TaxID=234826; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=St. Maries; RX PubMed=15618402; DOI=10.1073/pnas.0406656102; RA Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., RA Palmer G.H., McGuire T.C., Knowles D.P.Jr.; RT "Complete genome sequencing of Anaplasma marginale reveals that the RT surface is skewed to two superfamilies of outer membrane proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000030; AAV86405.1; -; Genomic_DNA. DR RefSeq; YP_153660.1; NC_004842.2. DR ProteinModelPortal; Q5PBC4; -. DR STRING; 234826.AM318; -. DR EnsemblBacteria; AAV86405; AAV86405; AM318. DR GeneID; 3171800; -. DR KEGG; ama:AM318; -. DR PATRIC; 20946687; VBIAnaMar46146_0272. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HELARAC; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 170 174 HMP-PP binding (By similarity). FT REGION 267 269 THZ-P binding (By similarity). FT REGION 318 319 THZ-P binding (By similarity). FT METAL 203 203 Magnesium (By similarity). FT METAL 222 222 Magnesium (By similarity). FT BINDING 202 202 HMP-PP (By similarity). FT BINDING 241 241 HMP-PP (By similarity). FT BINDING 270 270 HMP-PP (By similarity). FT BINDING 298 298 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 340 AA; 37446 MW; D2E71601B10F3D69 CRC64; MHLMRGDNMA SCAVAEAVRD AHLQGEGDVY AVNAECADGT YADYYFDGNE EIKLLYKCPG PTDCDTFARS YRHVAYHVLN TTKCKDMKDA RLDCIVLARM LASAVVSGGS VADWNPYNIN GEYFPRIASG FDCRDTMYGF DKLENIGLYL IVPDDTWFER AVRCGVKTIQ LRAKEAPIGE VDRMVRRCAQ LSKDKGVCLI VNDHWNIAIE HGAHGVHLGQ EDVQTADLES ILKSKMKLGL STHCYHELAR ACFIRPSYVA LGPVFHTTSK DMRFKPQGLQ LLKQWVQCAK LPVVGIGGID ASNIGSVVNC GVSGVAVISA VTRAEDPEAA MLNLQRAFDV // ID Q5QUC9_IDILO Unreviewed; 504 AA. AC Q5QUC9; DT 04-JAN-2005, integrated into UniProtKB/TrEMBL. DT 04-JAN-2005, sequence version 1. DT 19-FEB-2014, entry version 68. DE SubName: Full=Thiamine monophosphate synthase; GN Name=thiE; OrderedLocusNames=IL0766; OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=283942; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR; RX PubMed=15596722; DOI=10.1073/pnas.0407638102; RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., RA Campbell S., Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.; RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina RT loihiensis reveals amino acid fermentation as a source of carbon and RT energy."; RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017340; AAV81607.1; -; Genomic_DNA. DR RefSeq; YP_155156.1; NC_006512.1. DR ProteinModelPortal; Q5QUC9; -. DR STRING; 283942.IL0766; -. DR EnsemblBacteria; AAV81607; AAV81607; IL0766. DR GeneID; 3173350; -. DR KEGG; ilo:IL0766; -. DR PATRIC; 22139563; VBIIdiLoi21852_0768. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ILOI283942:GI0U-765-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 504 AA; 55069 MW; A145476799D1124D CRC64; MSIPVVWTIA GSDSGGGAGI QADLHTFRSL NVHGCSVIST ITAQNSVATT GLFPLAADAV RQQLECLQQD MPPAAIKIGL LSNVQQLQCV ADFLKQWSDP LPQPFVVWDP VVVSTQQDRL SELKPQHCAE LFPLVDIMTP NLDELSWLSG LEVTDEDSMY RAAEQLFQAG LSRILVTGTD FGRADEISDY YLSSDGHTQY IQQKLRTKHS HGTGCTLSSA IAAALAHDYP LEDAITVANA YVHQGLIEAK GIGRGPGPVA HTHWPQQIDH FPKINTPELP CVDLQFPSLD QEPGLYPVVD SYEWIEKLLK LGIKTLQLRI KDPDAPQLET AIKKSIQLAE KYSAQLFIND HWQLAIKHNA YGVHLGQEDL TEANLHAIQQ AGLRLGISTH SYTELLIAQA YKPSYIALGH IFPTQTKTMP SKPQGLQRLR RYAALLAPKN IPTVAIGGIS LERVAPVTAT GVNGIAVVSA ITAARNVEQA VHQLLTEMEA ELEVKEKNEV AHAE // ID Q5UF47_9PROT Unreviewed; 208 AA. AC Q5UF47; DT 07-DEC-2004, integrated into UniProtKB/TrEMBL. DT 07-DEC-2004, sequence version 1. DT 16-OCT-2013, entry version 37. DE SubName: Full=Predicted thiamin-phosphate pyrophosphorylase; GN ORFNames=Red7D11_39; OS uncultured proteobacterium RedeBAC7D11. OC Bacteria; Proteobacteria; environmental samples. OX NCBI_TaxID=295350; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=15305915; DOI=10.1111/j.1462-2920.2004.00676.x; RA Sabehi G., Beja O., Suzuki M.T., Preston C.M., DeLong E.F.; RT "Different SAR86 subgroups harbour divergent proteorhodopsins."; RL Environ. Microbiol. 6:903-910(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY744396; AAV34480.1; -; Genomic_DNA. DR ProteinModelPortal; Q5UF47; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 208 AA; 23602 MW; 649DD3C391E52B05 CRC64; MIQGLYAITP SGLEENDLLT KTEVLLKEGI KLIQYRDKIL DKKTLQEKAH ALLKLTKKYG AKLLINDHVE ICLEISADGF HLGLEDYLSE GNVELLKKNK EFISKKLICG LSCKWNKELV VNPPENEIKW TYLAVGSFYP SNTKSTIPET NEKVKRKFLS YTDKPLVAIG GINKKNIGEV RSLGYSCFAL SEALFINPQH VLNEYKRL // ID Q5WWJ6_LEGPL Unreviewed; 488 AA. AC Q5WWJ6; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 14-MAY-2014, entry version 75. DE SubName: Full=Uncharacterized protein; GN Name=thiDE; OrderedLocusNames=lpl1457; OS Legionella pneumophila (strain Lens). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=297245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lens; RX PubMed=15467720; DOI=10.1038/ng1447; RA Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L., RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., RA Etienne J., Glaser P., Buchrieser C.; RT "Evidence in the Legionella pneumophila genome for exploitation of RT host cell functions and high genome plasticity."; RL Nat. Genet. 36:1165-1173(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR628337; CAH15697.1; -; Genomic_DNA. DR RefSeq; YP_126803.1; NC_006369.1. DR ProteinModelPortal; Q5WWJ6; -. DR STRING; 297245.lpl1457; -. DR EnsemblBacteria; CAH15697; CAH15697; lpl1457. DR GeneID; 3116000; -. DR KEGG; lpf:lpl1457; -. DR PATRIC; 22316597; VBILegPne33733_1625. DR LegioList; lpl1457; -. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; LPNE297245:GJD4-1574-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 488 AA; 54228 MW; 848982B2403F4E29 CRC64; MKKPIVWTIA GVDSSGLAGV HADMETFSRL NVRACSVITA VTAQNAHSIT AVEAISRDQV AAQCRVLELN LKPDAIKIGM LCSTPICEEI AYFLKGYEGF VVLDPIITSS SGTNLFFPDL QQHKKNLIQL FPYITIITPN RIEAEIILNR SISSYQDIIN AASDLLSLGA KQVLLKGGHV KDNSFSQDYW TDGKESFWIA NHRFPERNYR GTGCALSSAL TACLALGYSM KDAIVIAKMY VSRGIRQSIE IDKEASQLYH DGWPEDEADL PYLSPTPFIK PVPSFKKYSM GFYPIVDSSH WLEMLLPSGI KCIQLRIKET SQERLEEEIK RSVHLANQYN AALFINDHWE LAIHYGAAGV HLGQEDLEKA DVDRINRAGL FLGISTHCYY EVARAHALNP SYVACGPIYE TTSKIMPFQA QGIARLERWR KTLRYPLVAI GGITLKNLSD VLKTKIDGVS VISAITKASA PLVAAKQFLT QMNESHNE // ID Q5X4Z4_LEGPA Unreviewed; 488 AA. AC Q5X4Z4; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 14-MAY-2014, entry version 75. DE SubName: Full=Uncharacterized protein; GN Name=thiDE; OrderedLocusNames=lpp1526; OS Legionella pneumophila (strain Paris). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=297246; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Paris; RX PubMed=15467720; DOI=10.1038/ng1447; RA Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L., RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., RA Etienne J., Glaser P., Buchrieser C.; RT "Evidence in the Legionella pneumophila genome for exploitation of RT host cell functions and high genome plasticity."; RL Nat. Genet. 36:1165-1173(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR628336; CAH12677.1; -; Genomic_DNA. DR RefSeq; YP_123850.1; NC_006368.1. DR ProteinModelPortal; Q5X4Z4; -. DR STRING; 297246.lpp1526; -. DR EnsemblBacteria; CAH12677; CAH12677; lpp1526. DR GeneID; 3116835; -. DR KEGG; lpp:lpp1526; -. DR PATRIC; 22323443; VBILegPne27771_1780. DR LegioList; lpp1526; -. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 488 AA; 54258 MW; 83FEA453779F20B8 CRC64; MKKPIVWTIA GIDSSGLAGV HADMETFSRL NVRACSVITA VTAQNAHSIT AVEEISRDQV AAQCRALELN LKPDAIKIGM LCSTPICEEI AYFLKGYEGF VVLDPIITSS SGTNLFFPDL QQHKKNLIQL FRYVTVITPN RIEAEAILNR SISSYQDIIN AASDLLSLGA KQVLLKGGHL KDNLFSQDYW TDGKESFWIA NHRFPETNYR GTGCVLSSAL TACLALGYSI KDAIVIAKMY VNRGIRQSIE IDKDASQLYH DSWPEDEADL PYLSPTPFIK PVPSFKKCSM GFYPIVDSSH WLEMLLPLGI KCIQLRIKEA SQERLEEEIK RSVHLANQYN AALFINDYWE LAIHYGAAGV HLGQEDLEKA DVDRINRSGL FLGISTHCYY EVARAHALNP SYVACGPIYE TTSKIMPFQA QGIARLERWR KTLHYPLVAI GGITLKNLSD VLKTKIDGVS VISAITKASA PLVAAKQFLT QMNESHNE // ID Q5ZV72_LEGPH Unreviewed; 495 AA. AC Q5ZV72; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 14-MAY-2014, entry version 72. DE SubName: Full=Phosphomethylpyrimidine kinase ThiD/thiamin-phosphate pyrophosphorylase fused protein ThiE; GN Name=thiDE; OrderedLocusNames=lpg1568; OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / OS ATCC 33152 / DSM 7513). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=272624; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513; RX PubMed=15448271; DOI=10.1126/science.1099776; RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., RA Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., RA Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R., RA Pampou S., Georghiou A., Chou I.C., Iannuccilli W., Ulz M.E., RA Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G., RA Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J., RA Ju J., Kalachikov S., Shuman H.A., Russo J.J.; RT "The genomic sequence of the accidental pathogen Legionella RT pneumophila."; RL Science 305:1966-1968(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017354; AAU27650.1; -; Genomic_DNA. DR RefSeq; YP_095597.1; NC_002942.5. DR ProteinModelPortal; Q5ZV72; -. DR STRING; 272624.lpg1568; -. DR DNASU; 3077941; -. DR EnsemblBacteria; AAU27650; AAU27650; lpg1568. DR GeneID; 3077941; -. DR KEGG; lpn:lpg1568; -. DR PATRIC; 22330240; VBILegPne29832_1643. DR eggNOG; COG0351; -. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; LPNE272624:GHDI-1567-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. SQ SEQUENCE 495 AA; 55081 MW; 69C8A29273F3E689 CRC64; MASGKQFMKK PIVWTIAGVD SSGLAGVHAD METFSRLNVR ACSVITAVTA QNAHSIIAVE EISRDQVAAQ CRALELNLKP DAIKIGMLCS TPICEEIAYF LKGYEGFVVL DPIITSSSGT NLFFPDLQQH KNNLIQLFPY ITIITPNRIE AEIILNRSIY SYQDIINAAS DLLSLGAKQV LLKGGHVKDN SFSQDYWTDG KESFWIANRR FPETNYRGTG CVLSSALTAC LALGYSIKDA IVIAKMYVNR GIRQSIEIDK DASQLYHDGW PEDEADLPYL SPTPFIKPVP SFKKYSMGFY PIVDSSHWLE MLLPLGIKCI QLRIKEASQE RLEEEIKRSV HLANQYNAAL FINDHWELAI HYGAAGVHLG QEDLEKADVD RINRSGLFLG ISTHCYYEVA RAHALNPSYV ACGPIYETTS KIMPFQAQGI ARLERWRKTL RYPLVAIGGI TLKNLSDVLK TKIDGVSVIS AITKASAPLV AAKQFLTQMN ESHNE // ID Q607S7_METCA Unreviewed; 306 AA. AC Q607S7; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 14-MAY-2014, entry version 71. DE SubName: Full=Putative nucleotide pyrophosphorylase; GN OrderedLocusNames=MCA1678; OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath). OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylococcus. OX NCBI_TaxID=243233; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath; RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303; RA Ward N., Larsen O., Sakwa J., Bruseth L., Khouri H., Durkin A.S., RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M., Nelson K.E., RA Methe B., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D., Ravel J., RA Tettelin H., Ren Q., Read T., DeBoy R.T., Seshadri R., Salzberg S.L., RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H., RA Holt I., Eidhammer I., Jonasen I., Vanaken S., Utterback T., RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.; RT "Genomic insights into methanotrophy: the complete genome sequence of RT Methylococcus capsulatus (Bath)."; RL PLoS Biol. 2:1616-1628(2004). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017282; AAU92103.1; -; Genomic_DNA. DR RefSeq; YP_114121.1; NC_002977.6. DR ProteinModelPortal; Q607S7; -. DR STRING; 243233.MCA1678; -. DR EnsemblBacteria; AAU92103; AAU92103; MCA1678. DR GeneID; 3103017; -. DR KEGG; mca:MCA1678; -. DR PATRIC; 22607196; VBIMetCap22254_1707. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 306 AA; 33719 MW; ED199E4EDE315661 CRC64; MAVGVVEDAG GRILIARRPA EVDQGGLWEF PGGKIEPGET PFDALRRELM EETGIAVDGA EPMLVVRHDY PLRRVVLDVW RVRRFSGIAR GRLGQPVRWV RPDELVDFRF PAANRSIVTA ARLPFHYPIV EDAAGDLGAM RRQFRRLVAE GHSLIQLRAK ALSRTDFRAF ARECLYHCAD NHTRLILNAE PELAVELGAA GVHLTSARLN SLDSRPLDDR FWVAASCHDV SELEKAESLQ LDFAVFGPVL PTRSHPESAP LGWEHVSQCL QSVNLPVYAL GGMAAEHLAS ARSAGAWGIA GIRGFL // ID Q62DX9_BURMA Unreviewed; 196 AA. AC Q62DX9; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 59. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase ThiE; GN OrderedLocusNames=BMAA0287; OS Burkholderia mallei (strain ATCC 23344). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=243160; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23344; RX PubMed=15377793; DOI=10.1073/pnas.0403306101; RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E., RA Feldblyum T., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C., RA Davidsen T.D., Deboy R.T., Dimitrov G., Dodson R.J., Durkin A.S., RA Gwinn M.L., Haft D.H., Khouri H., Kolonay J.F., Madupu R., RA Mohammoud Y., Nelson W.C., Radune D., Romero C.M., Sarria S., RA Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y., Zafar N., RA Zhou L., Fraser C.M.; RT "Structural flexibility in the Burkholderia mallei genome."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000011; AAU46206.1; -; Genomic_DNA. DR RefSeq; YP_105099.1; NC_006349.2. DR ProteinModelPortal; Q62DX9; -. DR STRING; 243160.BMAA0287; -. DR EnsemblBacteria; AAU46206; AAU46206; BMAA0287. DR GeneID; 3087117; -. DR KEGG; bma:BMAA0287; -. DR PATRIC; 19122598; VBIBurMal55007_3788. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QLMLNGP; -. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 196 AA; 20321 MW; 6128620A8545801F CRC64; MHDDLALPPY YLITPEPASG SDADLAAFLD RLSDALATGL TLVQLRVKTL DAPAYAALAA GALARCRAQR ARMIVNGPIA VEAALALGAA GVHLGSAALR AATARPLGSE GLLSAACHSL DELRHAQRIG ADLATLSPVL PTLTHPGAPT LGWTRFAECA AHTRVPVYAL GGMTRTHLET ARAHHAHGIA SIRGLW // ID Q62GC7_BURMA Unreviewed; 216 AA. AC Q62GC7; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 76. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BMA2727; OS Burkholderia mallei (strain ATCC 23344). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=243160; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23344; RX PubMed=15377793; DOI=10.1073/pnas.0403306101; RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E., RA Feldblyum T., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C., RA Davidsen T.D., Deboy R.T., Dimitrov G., Dodson R.J., Durkin A.S., RA Gwinn M.L., Haft D.H., Khouri H., Kolonay J.F., Madupu R., RA Mohammoud Y., Nelson W.C., Radune D., Romero C.M., Sarria S., RA Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y., Zafar N., RA Zhou L., Fraser C.M.; RT "Structural flexibility in the Burkholderia mallei genome."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000010; AAU48293.1; -; Genomic_DNA. DR RefSeq; YP_104247.1; NC_006348.1. DR ProteinModelPortal; Q62GC7; -. DR STRING; 243160.BMA2727; -. DR EnsemblBacteria; AAU48293; AAU48293; BMA2727. DR GeneID; 3091379; -. DR KEGG; bma:BMA2727; -. DR PATRIC; 19120605; VBIBurMal55007_2796. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22582 MW; F27E8C9961E0AF7B CRC64; MLGLPAAPEP AFAPCPQRLG LYPVLPSAEW VERVLDCGVR TVQLRVKDAS PDALRAEIER AVAAGRRHPD ARVFINDHWR LALDAGAYGV HLGQEDLETA DLGAIARAGA RLGLSSHGYY EMLVALQFKP SYLALGPVFA TATKAVAAPP QGLARLARYV RFAGPQAPLV AIGGIAPDTL GAVLAAGVGS AAVVSAITAA ADYREAIVAL QQNFGR // ID Q63FR8_BACCZ Unreviewed; 206 AA. AC Q63FR8; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 63. DE SubName: Full=Thiamine-phosphate diphosphorylase (Thiamine monophosphate synthase) (TMP-PPase); DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=BCE33L0639; OS Bacillus cereus (strain ZK / E33L). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=288681; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZK / E33L; RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000001; AAU19603.1; -; Genomic_DNA. DR RefSeq; YP_082244.1; NC_006274.1. DR ProteinModelPortal; Q63FR8; -. DR STRING; 288681.BCZK0639; -. DR EnsemblBacteria; AAU19603; AAU19603; BCE33L0639. DR GeneID; 3022967; -. DR KEGG; bcz:BCZK0639; -. DR PATRIC; 18884668; VBIBacCer95304_0674. DR eggNOG; COG0352; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER288681:GHG7-725-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID Q63JC2_BURPS Unreviewed; 196 AA. AC Q63JC2; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=BPSS1796; OS Burkholderia pseudomallei (strain K96243). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=272560; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., RA Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., RA Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I., RA Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., RA Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., RA Keith K.E., Maddison M., Moule S., Price C., Quail M.A., RA Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, RT Burkholderia pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571966; CAH39272.1; -; Genomic_DNA. DR RefSeq; YP_111800.1; NC_006351.1. DR ProteinModelPortal; Q63JC2; -. DR STRING; 272560.BPSS1796; -. DR EnsemblBacteria; CAH39272; CAH39272; BPSS1796. DR GeneID; 3097206; -. DR KEGG; bps:BPSS1796; -. DR PATRIC; 19271894; VBIBurPse99623_6117. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPSE272560:GJNI-5370-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 196 AA; 20351 MW; 7B9869A0244E300E CRC64; MHDDLALPPY YLITPEPASG SDADLTAFLD RLSDALATGL TLVQLRVKTL DAPAYAALAA GALARCRAQR ARMIVNGPIA VEAALALGAA GVHLGSAALR AATARPLGSE GLLSAACHSL DELRHAQRIG ADLATLSPVL PTLTHPGAPT LGWTRFAECA AHTRVPVYAL GGMTRTHLET ARAHHAHGIA SIRGLW // ID Q63KZ7_BURPS Unreviewed; 199 AA. AC Q63KZ7; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 59. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN OrderedLocusNames=BPSS1216; OS Burkholderia pseudomallei (strain K96243). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=272560; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., RA Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., RA Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I., RA Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., RA Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., RA Keith K.E., Maddison M., Moule S., Price C., Quail M.A., RA Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, RT Burkholderia pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571966; CAH38683.1; -; Genomic_DNA. DR RefSeq; YP_111224.1; NC_006351.1. DR ProteinModelPortal; Q63KZ7; -. DR STRING; 272560.BPSS1216; -. DR EnsemblBacteria; CAH38683; CAH38683; BPSS1216. DR GeneID; 3097261; -. DR KEGG; bps:BPSS1216; -. DR PATRIC; 19270432; VBIBurPse99623_5386. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AYLHISH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPSE272560:GJNI-4778-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome; Transferase. SQ SEQUENCE 199 AA; 21410 MW; 4AC4457A90171166 CRC64; MNKSANLPSE YLITPEPPGD EALSDYLATL ERTLKAGISL VQLRAKAVTA PYYARLTEYA LACCRRYNAR LLVNAAPEVA LSLHTDGVHL TSTRLMTCST RPLPAGLLVS AACHDEDQVR HADSIGVDLI TISPVMPTAT HTTAEPLGWP RFRELATLTS VPVYALGGMS VDSLAEARNA GAYGIAAIRA FWESNVDRS // ID Q63Q74_BURPS Unreviewed; 364 AA. AC Q63Q74; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 74. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=BPSL3151; OS Burkholderia pseudomallei (strain K96243). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=272560; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., RA Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., RA Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I., RA Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., RA Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., RA Keith K.E., Maddison M., Moule S., Price C., Quail M.A., RA Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, RT Burkholderia pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571965; CAH37161.1; -; Genomic_DNA. DR RefSeq; YP_109744.1; NC_006350.1. DR ProteinModelPortal; Q63Q74; -. DR STRING; 272560.BPSL3151; -. DR EnsemblBacteria; CAH37161; CAH37161; BPSL3151. DR GeneID; 3092618; -. DR KEGG; bps:BPSL3151; -. DR PATRIC; 19266823; VBIBurPse99623_3600. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BPSE272560:GJNI-3235-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Transferase. SQ SEQUENCE 364 AA; 38046 MW; 5D5059F3DAC03A2B CRC64; MSAALPDAFW PPADELTEAA ERIRATLGAW QRPAVRTRIC LAPPEQPRAA DLWVAIAGAH AAHIARLNAA GAQAIVIDDA SATLHTGAAR HALASRAPLA DDWIAALAAF LDCGFAASDA LVLALAWRDG DEARGGDPWP VDPARFPRVL GLPAAPEPAF APCPQRLGLY PVLPSAEWVE RVLDCGVRTV QLRVKDASPD ALRAEIERAV AAGRRHPDAR VFINDHWRLA LDAGAYGVHL GQEDLETADL GAIARAGARL GLSSHGYYEM LVALQFKPSY LALGPVFATA TKAVAAPPQG LARLARYVRF AGPQAPLVAI GGIAPDTLGA VLAAGVGSAA VVSAITAAAD YQEAIVALQQ NFGR // ID Q64T95_BACFR Unreviewed; 202 AA. AC Q64T95; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 51. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN OrderedLocusNames=BF2535; OS Bacteroides fragilis (strain YCH46). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=295405; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YCH46; RX PubMed=15466707; DOI=10.1073/pnas.0404172101; RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.; RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA RT inversions regulating cell surface adaptation."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006841; BAD49284.1; -; Genomic_DNA. DR RefSeq; YP_099818.1; NC_006347.1. DR ProteinModelPortal; Q64T95; -. DR SMR; Q64T95; 1-202. DR STRING; 295405.BF2535; -. DR EnsemblBacteria; BAD49284; BAD49284; BF2535. DR GeneID; 3083793; -. DR KEGG; bfr:BF2535; -. DR PATRIC; 21050693; VBIBacFra17906_2443. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR OrthoDB; EOG6RC3V1; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 202 AA; 23245 MW; A6533F52928C16DB CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHKRIVTH EHFYLKEEFN LMGIHLNARN PKEPHDYSGH ISCSCHSVEE VKNKKHFYDY VFMSPVYDSI SKEGYNSPYT AEELRLAAKD KIIDNKVMAL GGITPDNILE VKDFGFGGAV VLGDLWGKFD ACSDQDYLAV IEHFKKLKRM AD // ID Q65L97_BACLD Unreviewed; 203 AA. AC Q65L97; Q62WN6; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 69. DE SubName: Full=Regulatory protein TenI; DE SubName: Full=Transcriptional regulator; GN Name=tenI; OrderedLocusNames=BL01591, BLi01260; OS Bacillus licheniformis (strain DSM 13 / ATCC 14580). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580, and DSM 13 / ATCC 14580 [Novozymes]; RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., RA Olsen P.B., Rasmussen M.D., Andersen J.T., Jorgensen P.L., RA Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., RA Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:R77.1-R77.12(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13, and DSM 13 / ATCC 14580 [Goettingen]; RX PubMed=15383718; DOI=10.1159/000079829; RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., RA Ehrenreich P., Baumer S., Henne A., Liesegang H., Merkl R., RA Ehrenreich A., Gottschalk G.; RT "The complete genome sequence of Bacillus licheniformis DSM13, an RT organism with great industrial potential."; RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14580; RA Berka R.M., Rey M.W., Ramaiya P.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13; RA Wiegand S., Hertel R., Dietrich S., Volland S., Liesegang H.; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000002; AAU22822.1; -; Genomic_DNA. DR EMBL; AE017333; AAU40167.1; -; Genomic_DNA. DR RefSeq; YP_006712641.1; NC_006322.1. DR RefSeq; YP_078460.1; NC_006270.3. DR SMR; Q65L97; 1-191. DR STRING; 279010.BL01591; -. DR EnsemblBacteria; AAU22822; AAU22822; BL01591. DR EnsemblBacteria; AAU40167; AAU40167; BLi01260. DR GeneID; 3030266; -. DR GeneID; 3098563; -. DR KEGG; bld:BLi01260; -. DR KEGG; bli:BL01591; -. DR PATRIC; 18948093; VBIBacLic203714_1251. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BLIC279010:GJ2P-1252-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 203 AA; 22376 MW; 3BE3AB481BF14203 CRC64; MHLHAITDDK HSVEELSAKI ISIHDAVDFI HIRERSKKVS EISSLIDRLA EEGVDKRKLI INDRVDIALF HHIHRVQLPS HGFSVKSVRS RFPHLKIGKS VHSPEEAVQA ETEGADYVLF GHIFETDCKK GRKGRGALSL AEVKAAVRIP VIAIGGITEQ RLAEVKMADG IAVMSGIFSH DRPNEAAARL ASLAKGDSYE KAL // ID Q67Z21_ARATH Unreviewed; 740 AA. AC Q67Z21; DT 11-OCT-2004, integrated into UniProtKB/TrEMBL. DT 11-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 74. DE SubName: Full=FZO-like protein; DE SubName: Full=Putative uncharacterized protein At1g03160; GN Name=FZL; OrderedLocusNames=At1g03160; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [2] RP NUCLEOTIDE SEQUENCE. RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., RA Hayashizaki Y., Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T., RA Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., RA Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., RA Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., RA Hayashizaki Y., Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE. RG TAIR; RA Swarbreck D., Lamesch P., Wilks C., Huala E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [5] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002684; AEE27538.1; -; Genomic_DNA. DR EMBL; AK176297; BAD44060.1; -; mRNA. DR EMBL; AK227660; BAE99647.1; -; mRNA. DR RefSeq; NP_001077452.1; NM_001083983.1. DR UniGene; At.44048; -. DR STRING; 3702.AT1G03160.1-P; -. DR EnsemblPlants; AT1G03160.2; AT1G03160.2; AT1G03160. DR GeneID; 839566; -. DR KEGG; ath:AT1G03160; -. DR TAIR; AT1G03160; -. DR HOGENOM; HOG000241410; -. DR Genevestigator; Q67Z21; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 2: Evidence at transcript level; KW Complete proteome; Reference proteome. SQ SEQUENCE 740 AA; 81738 MW; 7720EAC9DE6EBA50 CRC64; MRTLISHRQC VTSPFLISAA SPPFPGRCFK LSSFTPPRHR RFSSLSIRNI SHESADQTSS SRPRTLYPGG YKRPELAVPG LLLRLDADEV MSGNREETLD LVDRALAKSV QIVVIDGGAT AGKLYEAACL LKSLVKGRAY LLIAERVDIA SAVGASGVAL SDEGLPAIVA RNTLMGSNPD SVLLPLVARI VKDVDSALIA SSSEGADFLI LGSGEEDTQV ADSLLKSVKI PIYVTCRGNE EAKEELQLLK SGVSGFVISL KDLRSSRDVA LRQSLDGAYV VNNHETQNMN ELPEKKNSAG FIKLEDKQKL IVEMEKSVLR ETIEIIHKAA PLMEEVSLLI DAVSRIDEPF LMVIVGEFNS GKSTVINALL GKRYLKEGVV PTTNEITFLC YSDLESEEQQ RCQTHPDGQY VCYLPAPILK DINIVDTPGT NVILQRQQRL TEEFVPRADL LVFVLSADRP LTESEVAFLR YTQQWKKKFV FILNKSDIYR DARELEEAIS FVKENTRKLL NTENVILYPV SARSALEAKL STASLVGRDD LEIADPGSNW RVQSFNELEK FLYSFLDSST ATGMERIRLK LETPMAIAER LLSSVEALVR QDCLAAREDL ASADKIISRT KEYALKMEYE SISWRRQALS LIDNARLQVV DLIGTTLRLS SLDLAISYVF KGEKSASVAA TSKVQGEILA PALTNAKVSV MLYSLSIGLT GDMLVIYMRN CLENMLNGYN QILPVKGVCL // ID Q6A9C4_PROAC Unreviewed; 270 AA. AC Q6A9C4; DT 13-SEP-2004, integrated into UniProtKB/TrEMBL. DT 13-SEP-2004, sequence version 1. DT 14-MAY-2014, entry version 78. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PPA0886; OS Propionibacterium acnes (strain KPA171202 / DSM 16379). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=267747; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KPA171202 / DSM 16379; RX PubMed=15286373; DOI=10.1126/science.1100330; RA Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., RA Strittmatter A., Hujer S., Durre P., Gottschalk G.; RT "The complete genome sequence of Propionibacterium acnes, a commensal RT of human skin."; RL Science 305:671-673(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017283; AAT82642.1; -; Genomic_DNA. DR RefSeq; YP_055600.1; NC_006085.1. DR ProteinModelPortal; Q6A9C4; -. DR STRING; 267747.PPA0886; -. DR EnsemblBacteria; AAT82642; AAT82642; PPA0886. DR GeneID; 2931882; -. DR KEGG; pac:PPA0886; -. DR PATRIC; 23036489; VBIProAcn64440_0919. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IGISCHT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PACN267747:GHO9-897-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 195 197 THZ-P binding (By similarity). FT REGION 245 246 THZ-P binding (By similarity). FT METAL 128 128 Magnesium (By similarity). FT METAL 147 147 Magnesium (By similarity). FT BINDING 127 127 HMP-PP (By similarity). FT BINDING 166 166 HMP-PP (By similarity). FT BINDING 198 198 HMP-PP (By similarity). FT BINDING 225 225 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 270 AA; 28245 MW; C497F4A1DC860701 CRC64; MTISSRPCPR PPCCVSSPNG QLSAVLVRGL SRKLSLTNYS WCHPTRLVSG EGSAMSRPEF DLSVYLVTDT AQCGGPDEVV ETVRHAIAGG VTLVQFRDHD LSDDEFVALG RRVREICVSG GVPLIIDDRV HLVAEIGADG VHVGQSDMPV DQARAILGDD LLIGLSAQTP AHVEAALSQG RDIVDYLGVG ALHGTGTKPE AGELGLAGMR DVVNASPWPV CVIGGVSASD AQDVARVGCD GLSVVSAICR STAPKSSARE LAEAWRTAKE // ID Q6ABQ7_PROAC Unreviewed; 217 AA. AC Q6ABQ7; DT 13-SEP-2004, integrated into UniProtKB/TrEMBL. DT 13-SEP-2004, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=PPA0112; OS Propionibacterium acnes (strain KPA171202 / DSM 16379). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=267747; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KPA171202 / DSM 16379; RX PubMed=15286373; DOI=10.1126/science.1100330; RA Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., RA Strittmatter A., Hujer S., Durre P., Gottschalk G.; RT "The complete genome sequence of Propionibacterium acnes, a commensal RT of human skin."; RL Science 305:671-673(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017283; AAT81872.1; -; Genomic_DNA. DR RefSeq; YP_054830.1; NC_006085.1. DR ProteinModelPortal; Q6ABQ7; -. DR STRING; 267747.PPA0112; -. DR EnsemblBacteria; AAT81872; AAT81872; PPA0112. DR GeneID; 2932263; -. DR KEGG; pac:PPA0112; -. DR PATRIC; 23034855; VBIProAcn64440_0115. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6PZXB0; -. DR BioCyc; PACN267747:GHO9-111-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 217 AA; 22418 MW; 6F9581023BCB011C CRC64; MTLDLRCYLV TSGIDRHTIE TAAAAAGAGA GMVQVRAKEL STRDLLSLVL QVGEAVRRAN PATRVVVDDR ADVAWAAIRA RGNVHGVHVG LTDLPVRDAR AMLGPDAIVG YTTGTLDLVR SAEPFADALD YVGAGPFRPT PTKESGRSPL GVQGYPALVG ASSLPVVAIG DVQVADVPVL AATGVAGVAM VRAIMASDDP AAVVRQVVQS FDEVRVS // ID Q6APA6_DESPS Unreviewed; 240 AA. AC Q6APA6; DT 13-SEP-2004, integrated into UniProtKB/TrEMBL. DT 13-SEP-2004, sequence version 1. DT 14-MAY-2014, entry version 75. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=DP1089; OS Desulfotalea psychrophila (strain LSv54 / DSM 12343). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfotalea. OX NCBI_TaxID=177439; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LSv54 / DSM 12343; RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x; RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., RA Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K., RA Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., RA Klenk H.-P.; RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium RT from permanently cold Arctic sediments."; RL Environ. Microbiol. 6:887-902(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR522870; CAG35818.1; -; Genomic_DNA. DR RefSeq; YP_064825.1; NC_006138.1. DR ProteinModelPortal; Q6APA6; -. DR STRING; 177439.DP1089; -. DR EnsemblBacteria; CAG35818; CAG35818; DP1089. DR GeneID; 2947278; -. DR KEGG; dps:DP1089; -. DR PATRIC; 21711891; VBIDesPsy67261_1170. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HRFYFIT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DPSY177439:GJW5-1122-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 56 60 HMP-PP binding (By similarity). FT REGION 158 160 THZ-P binding (By similarity). FT REGION 209 210 THZ-P binding (By similarity). FT METAL 89 89 Magnesium (By similarity). FT METAL 108 108 Magnesium (By similarity). FT BINDING 88 88 HMP-PP (By similarity). FT BINDING 126 126 HMP-PP (By similarity). FT BINDING 161 161 HMP-PP (By similarity). FT BINDING 189 189 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 240 AA; 26590 MW; 50C2542ABF744663 CRC64; MVKDGKSRQA DLYGWRRKVL MDEVTVYPVC CEQLSAGRSD KEWLDNVLAG GAKIVQLRDK KSDDRLLLEK AKYFREKTRE AGALFLINDR FDIGLLADSD GIHVGQGDLP PEEIRRLTPD WIIGQSCNDL AEVEALGAQV QAGSSAVDYY NIGPIYRTDT KEGLHTFLGA GDIQQISAAC PLPFTVMGGI KWDHIPELAA AGVRRMAVVT AISMAADMQA ETRRWIDEIR RVTTLPVNSL // ID Q6CBT9_YARLI Unreviewed; 511 AA. AC Q6CBT9; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 16-APR-2014, entry version 60. DE SubName: Full=YALI0C15554p; GN ORFNames=YALI0_C15554g; OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida OS lipolytica). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia. OX NCBI_TaxID=284591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIB 122 / E 150; RX PubMed=15229592; DOI=10.1038/nature02579; RG Genolevures; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR382129; CAG82186.1; -; Genomic_DNA. DR RefSeq; XP_501873.1; XM_501873.1. DR ProteinModelPortal; Q6CBT9; -. DR STRING; 4952.Q6CBT9; -. DR EnsemblFungi; CAG82186; CAG82186; YALI0_C15554g. DR GeneID; 2909412; -. DR KEGG; yli:YALI0C15554g; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 511 AA; 54351 MW; 31B8B5E031F82484 CRC64; MPFNKSKTDY SIYLVTDSGL VPDNFTLEHQ VEQSILGGAT LIQLREKTAD TGKFLETAKR IHAITKKHGV PLLINDRLDI ALAIDCEGVH VGQDDMPVVE CRRMLGEDKI IGLSITNREE YDAALEADAA GANLDYFGVG AIYGTFTKKL RAEPLGLSGA RNLFAYITEK EKSLSRQHKF VTIGGIKPDN TPSVRYMCGA TCNGVAVVSC IIAAQDAKLV TEVLSKQWHD AITEPVLQVT TETLSKINSY FGTPTFVHHI TNNVVKNCSA NITIAIGSSP AMSETRAEFH EFAGIPNASL LLNMGTATSD GVETFLAAGQ AYNAARRPVV FDPVGGGASE ARKSAVKTLL KGIRMSVIKG NDGEIFSAAG LAGKMRGVDS IGESLLDERL KAAFKLSRDA NTVVVMTGKK DVVIGPSGQY VLVDNGDELL TQITGSGCML GSVITSIVAG HVGDVFDAAL AGLLLYTIAS EKAGPLSDGP GTFVPRLIDE ISKLAKTGVQ VEDIKVQFGK I // ID Q6CWR3_KLULA Unreviewed; 516 AA. AC Q6CWR3; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 16-APR-2014, entry version 60. DE SubName: Full=KLLA0B02134p; GN OrderedLocusNames=KLLA0B02134g; ORFNames=KLLA0_B02134g; OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC OS 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=284590; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / RC WM37; RX PubMed=15229592; DOI=10.1038/nature02579; RG Genolevures; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR382122; CAH02019.1; -; Genomic_DNA. DR RefSeq; XP_451626.1; XM_451626.1. DR ProteinModelPortal; Q6CWR3; -. DR STRING; 28985.Q6CWR3; -. DR GeneID; 2897424; -. DR KEGG; kla:KLLA0B02134g; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW Complete proteome. SQ SEQUENCE 516 AA; 55246 MW; 9AD3500066A3FF84 CRC64; MVNKESVDYT LYLVTDSTML PEGKTLLFQV EQGLKNGVTM VQLREKDTDA KTFVAEALAV KKICDSFNVP LIINDRVDVA LAIDASGIHV GQEDIPIPMV RKLVGPDKIV GWSVGKVEEV DRLAEWGPDM IDYIGVGTVF ETQTKKDIKK IPMGPEGVSR ILTRLEEKKC DWIRTVAIGG LHPDNIGRVL FQAQALNGKR SVDGISIVSD IMASHDAGQS TRILRQILDK GSFHFFEGSE EAKDASTIKE NVKKLAPLIH HITNRVHQNF GANVALAIGC SPIMSEVAEE FEDLSKIPHS VLLLNSGTVA DISVLQHAVK TYNAQKRPIV FDPVGFSASS ARLVLNKKVL SAGQFACIKG NTGEIMGVSG LGGNMKGVDS CGEDTLETRI KATQLVAFKY RTVAVCTGEI DVVADGSVSS TAPLKRGLGA SPAELPYELI KGEDVPLFGR ITASGCSLGT VIAGFIGAAA EESIYSAVLQ AVSLYKLAGT KANVTAKGSG SFLVGLVDNL YNVMEE // ID Q6FA83_ACIAD Unreviewed; 304 AA. AC Q6FA83; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 72. DE SubName: Full=Putative bifunctional protein; GN OrderedLocusNames=ACIAD2236; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33305 / BD413 / ADP1; RX PubMed=15514110; DOI=10.1093/nar/gkh910; RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., RA Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., RA Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.; RT "Unique features revealed by the genome sequence of Acinetobacter sp. RT ADP1, a versatile and naturally transformation competent bacterium."; RL Nucleic Acids Res. 32:5766-5779(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR543861; CAG69030.1; -; Genomic_DNA. DR RefSeq; YP_046852.1; NC_005966.1. DR ProteinModelPortal; Q6FA83; -. DR STRING; 62977.ACIAD2236; -. DR EnsemblBacteria; CAG69030; CAG69030; ACIAD2236. DR GeneID; 2879036; -. DR KEGG; aci:ACIAD2236; -. DR PATRIC; 20742128; VBIAciSp98416_2007. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ASP62977:GJVV-2103-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 304 AA; 35045 MW; 4035D6223BC25F77 CRC64; MRKFEELQKY MPKPVIDVSI GILLHKNKVL IGWREASQHQ GNKHEFPGGK VEHNESPVDA CRREIYEEVG VGIKEWHVFD QITHEYDDVI VKLHLFHAFV PDELLALIHQ PWSWFGRDQL KNLNFPKAND AILQRLSWPH YIKISELPPN FSSDRLQYWR SQDSVQQNIE HMSEAQLSVL IINQDQWQRL DHYLQEQIKT IHLKQHQLMQ LKQGDLVVSK RYIAACHDLV AINHAHKLGC DAVFISPVQP TPTHPEAVTL GWDGLAQMAQ HSHIPVFALG GLHPDDLEQA VKHGAYGVAG IRNF // ID Q6FCY2_ACIAD Unreviewed; 211 AA. AC Q6FCY2; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 69. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=ACIAD1200; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33305 / BD413 / ADP1; RX PubMed=15514110; DOI=10.1093/nar/gkh910; RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., RA Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., RA Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.; RT "Unique features revealed by the genome sequence of Acinetobacter sp. RT ADP1, a versatile and naturally transformation competent bacterium."; RL Nucleic Acids Res. 32:5766-5779(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR543861; CAG68077.1; -; Genomic_DNA. DR RefSeq; YP_045899.1; NC_005966.1. DR ProteinModelPortal; Q6FCY2; -. DR STRING; 62977.ACIAD1200; -. DR EnsemblBacteria; CAG68077; CAG68077; ACIAD1200. DR GeneID; 2880058; -. DR KEGG; aci:ACIAD1200; -. DR PATRIC; 20740239; VBIAciSp98416_1078. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ASP62977:GJVV-1134-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22558 MW; 47C3E928481D68F6 CRC64; MRGLYLITND DPLELLLDKL EIALSTGHIA ILQYRRKKVP KTDQAFEVEQ IKVLCEAYQV PFVINDDLVL AAQFDLGVHL GQSDGEISDA VNRLTSGAVI GRTCLNSLVL AEKAIADGAT YIAFGAVYAT ATKPEAGNVG IEVIKQARQK FNTPICAIGG LTVENSKVVI ESGADLCAVI SDILGRSVQD IPTRINAWAA LFAETSSAVN V // ID Q6FV03_CANGA Unreviewed; 540 AA. AC Q6FV03; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 16-APR-2014, entry version 67. DE SubName: Full=Strain CBS138 chromosome E complete sequence; GN OrderedLocusNames=CAGL0E05808g; OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / OS NRRL Y-65) (Yeast) (Torulopsis glabrata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces; OC mitosporic Nakaseomyces. OX NCBI_TaxID=284593; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65; RX PubMed=15229592; DOI=10.1038/nature02579; RG Genolevures; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) IN COMPLEX WITH MAGNESIUM. RX PubMed=20968298; DOI=10.1021/bi101008u; RA Paul D., Chatterjee A., Begley T.P., Ealick S.E.; RT "Domain organization in Candida glabrata THI6, a bifunctional enzyme RT required for thiamin biosynthesis in eukaryotes."; RL Biochemistry 49:9922-9934(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR380951; CAG58860.1; -; Genomic_DNA. DR RefSeq; XP_445941.1; XM_445941.1. DR PDB; 3NL2; X-ray; 3.08 A; A/B/C/D/E/F=1-540. DR PDB; 3NL3; X-ray; 3.01 A; A/B/C/D/E/F=1-540. DR PDB; 3NL5; X-ray; 3.30 A; A/B/C=1-540. DR PDB; 3NL6; X-ray; 2.61 A; A/B/C=1-540. DR PDB; 3NM1; X-ray; 3.21 A; A/B/C/D/E/F=1-540. DR PDB; 3NM3; X-ray; 3.10 A; A/B/C/D/E/F=1-540. DR PDBsum; 3NL2; -. DR PDBsum; 3NL3; -. DR PDBsum; 3NL5; -. DR PDBsum; 3NL6; -. DR PDBsum; 3NM1; -. DR PDBsum; 3NM3; -. DR ProteinModelPortal; Q6FV03; -. DR GeneID; 2887447; -. DR KEGG; cgr:CAGL0E05808g; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR EvolutionaryTrace; Q6FV03; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IDA:CGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IDA:CGD. DR GO; GO:0016310; P:phosphorylation; IDA:GOC. DR GO; GO:0009228; P:thiamine biosynthetic process; ISO:CGD. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Magnesium; Metal-binding. FT METAL 49 49 Magnesium 1. FT METAL 50 50 Magnesium 1; via amide nitrogen. FT METAL 51 51 Magnesium 1. FT METAL 51 51 Magnesium 2. FT METAL 51 51 Magnesium 3. FT METAL 76 76 Magnesium 2. FT METAL 76 76 Magnesium 4. FT METAL 95 95 Magnesium 2. FT METAL 95 95 Magnesium 4. FT METAL 340 340 Magnesium 5. FT METAL 340 340 Magnesium 6. FT METAL 341 341 Magnesium 3; via carbonyl oxygen. FT METAL 341 341 Magnesium 5; via carbonyl oxygen. FT METAL 341 341 Magnesium 6; via carbonyl oxygen. FT METAL 372 372 Magnesium 3. FT METAL 372 372 Magnesium 5. FT METAL 372 372 Magnesium 6. SQ SEQUENCE 540 AA; 58066 MW; EC0C7FB7BFC66324 CRC64; MKFSKEQFDY SLYLVTDSGM IPEGKTLYGQ VEAGLQNGVT LVQIREKDAD TKFFIEEALQ IKELCHAHNV PLIINDRIDV AMAIGADGIH VGQDDMPIPM IRKLVGPDMV IGWSVGFPEE VDELSKMGPD MVDYIGVGTL FPTLTKKNPK KAPMGTAGAI RVLDALERNN AHWCRTVGIG GLHPDNIERV LYQCVSSNGK RSLDGICVVS DIIASLDAAK STKILRGLID KTDYKFVNIG LSTKNSLTTT DEIQSIISNT LKARPLVQHI TNKVHQNFGA NVTLALGSSP IMSEIQSEVN DLAAIPHATL LLNTGSVAPP EMLKAAIRAY NDVKRPIVFD PVGYSATETR LLLNNKLLTF GQFSCIKGNS SEILGLAELN KERMKGVDAS SGISNELLIQ ATKIVAFKYK TVAVCTGEFD FIADGTIEGK YSLSKGTNGT SVEDIPCVAV EAGPIEIMGD ITASGCSLGS TIACMIGGQP SEGNLFHAVV AGVMLYKAAG KIASEKCNGS GSFQVELIDA LYRLTRENTP VTWAPKLTHT // ID Q6FYP1_BARQU Unreviewed; 220 AA. AC Q6FYP1; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 58. DE SubName: Full=Thiamine-phosphate pyrosphorylase; GN Name=thiE2; OrderedLocusNames=BQ11920; OS Bartonella quintana (strain Toulouse) (Rochalimaea quintana). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=283165; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Toulouse; RX PubMed=15210978; DOI=10.1073/pnas.0305659101; RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., RA La Scola B., Holmberg M., Andersson S.G.E.; RT "The louse-borne human pathogen Bartonella quintana is a genomic RT derivative of the zoonotic agent Bartonella henselae."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX897700; CAF26651.1; -; Genomic_DNA. DR RefSeq; YP_032723.1; NC_005955.1. DR ProteinModelPortal; Q6FYP1; -. DR STRING; 283165.BQ11920; -. DR PRIDE; Q6FYP1; -. DR EnsemblBacteria; CAF26651; CAF26651; BQ11920. DR GeneID; 2866596; -. DR KEGG; bqu:BQ11920; -. DR PATRIC; 31953807; VBIBarQui58630_1301. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FACVILY; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BQUI283165:GHZA-1190-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 220 AA; 25035 MW; C63A071AA7ECB94B CRC64; MTKQKSKSIE SPSYPQLVLT LDVQRILEPT FLRQILQTKS FACVILYDSQ GFKDDAFFLQ KQAQIYVEDI QQNGAALLIA DERRIAERVK ADGLHVEGDL NALERFENQK KEQKIIGFGN LRNRHCAMVA GEAGVDYLFF GKLGADKKPH AHPRNLQLGR WWAEIMEIPA IIQAGNDFAS FDEVIKTACE FIAVEEIIFA HDTPLLMLKM IKEKCENSHL // ID Q6G0A3_BARQU Unreviewed; 201 AA. AC Q6G0A3; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; OrderedLocusNames=BQ04070; OS Bartonella quintana (strain Toulouse) (Rochalimaea quintana). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=283165; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Toulouse; RX PubMed=15210978; DOI=10.1073/pnas.0305659101; RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., RA La Scola B., Holmberg M., Andersson S.G.E.; RT "The louse-borne human pathogen Bartonella quintana is a genomic RT derivative of the zoonotic agent Bartonella henselae."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX897700; CAF25906.1; -; Genomic_DNA. DR RefSeq; YP_032087.1; NC_005955.1. DR ProteinModelPortal; Q6G0A3; -. DR STRING; 283165.BQ04070; -. DR EnsemblBacteria; CAF25906; CAF25906; BQ04070. DR GeneID; 2867299; -. DR KEGG; bqu:BQ04070; -. DR PATRIC; 31952065; VBIBarQui58630_0468. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BQUI283165:GHZA-406-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 22910 MW; 9F7A36982F4846C5 CRC64; MKLDPFYLIV DNADWVERLV PLGVKLIQLR MKNENPKIIS QHIKRAKNIC DKLGTQLIIN DHWTIAIDEK CNFIHLGQED LSNADLPAIR KNGIRFGLST HDEHELDIAL SVHPNYIALG PIYPTILKEM KWMPQGLEKI KKWKKRIGAL PLIGIGGLTP ERATDVLKAG ANSAAVVTDI ILHKKPRERV QQWIKVTKAW R // ID Q6G481_BARHE Unreviewed; 201 AA. AC Q6G481; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE1; OrderedLocusNames=BH04870; OS Bartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea OS henselae). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=283166; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49882 / Houston 1; RX PubMed=15210978; DOI=10.1073/pnas.0305659101; RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., RA La Scola B., Holmberg M., Andersson S.G.E.; RT "The louse-borne human pathogen Bartonella quintana is a genomic RT derivative of the zoonotic agent Bartonella henselae."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX897699; CAF27295.1; -; Genomic_DNA. DR RefSeq; YP_033323.1; NC_005956.1. DR ProteinModelPortal; Q6G481; -. DR STRING; 283166.BH04870; -. DR EnsemblBacteria; CAF27295; CAF27295; BH04870. DR GeneID; 2865214; -. DR KEGG; bhe:BH04870; -. DR PATRIC; 20544751; VBIBarHen29080_0528. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BHEN283166:GIVZ-486-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 201 AA; 23034 MW; C765090272BBC409 CRC64; MKLDPFYPIV DNADWVERLV PLGIKLIQLR MKNENLKTIR EHIKRAKNIC DKLGAQLIIN DHWTIAIDEK CHFIHLGQED LRNADLPAIR KNAIRFGLST HDEHELDIAR SVDPDYIALG PIYPTILKEM KWMPQGLEKI KQWRKQIGAL PLIGIGGLTP ERAIGVLKAG ANSAAVVTDI LLHKKPEKRV RQWIKVTQAW R // ID Q6G5Q6_BARHE Unreviewed; 220 AA. AC Q6G5Q6; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 56. DE SubName: Full=Thiamine-phosphate pyrosphorylase; GN Name=thiE2; OrderedLocusNames=BH14940; OS Bartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea OS henselae). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=283166; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49882 / Houston 1; RX PubMed=15210978; DOI=10.1073/pnas.0305659101; RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., RA La Scola B., Holmberg M., Andersson S.G.E.; RT "The louse-borne human pathogen Bartonella quintana is a genomic RT derivative of the zoonotic agent Bartonella henselae."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX897699; CAF28257.1; -; Genomic_DNA. DR RefSeq; YP_034192.1; NC_005956.1. DR ProteinModelPortal; Q6G5Q6; -. DR STRING; 283166.BH14940; -. DR EnsemblBacteria; CAF28257; CAF28257; BH14940. DR GeneID; 2865215; -. DR KEGG; bhe:BH14940; -. DR PATRIC; 20547216; VBIBarHen29080_1716. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FACVILY; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BHEN283166:GIVZ-1489-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 220 AA; 24977 MW; C80D2B158E1C8663 CRC64; MTKQKSKPVE YHPFPQLVLT LDVRRSFTPT FLRQILQTRS FACVILYDSQ GVQDDAVFLQ KQAQIYAEDI QSNGAAFLIS GERRVSERIK ADGLHIEGDL KALEYCDYQK KEQKIIGFGN IRNRHCAMVA GEAGVDYLLF GKLGADKKPH AHPRNLQLAR WWAEIMETPA IVQAGSDFAT FDEVIKTACE FIAIEEVIFA HDNPLMLLKM MQEKCKNSPL // ID Q6HN87_BACHK Unreviewed; 206 AA. AC Q6HN87; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 63. DE SubName: Full=Thiamine-phosphate diphosphorylase (Thiamine monophosphate synthase) (TMP-PPase); DE EC=2.5.1.3; GN Name=thiE; OrderedLocusNames=BT9727_0639; OS Bacillus thuringiensis subsp. konkukian (strain 97-27). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=281309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27; RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017355; AAT59087.1; -; Genomic_DNA. DR RefSeq; YP_034984.1; NC_005957.1. DR ProteinModelPortal; Q6HN87; -. DR STRING; 281309.BT9727_0639; -. DR EnsemblBacteria; AAT59087; AAT59087; BT9727_0639. DR GeneID; 2855094; -. DR KEGG; btk:BT9727_0639; -. DR PATRIC; 18981881; VBIBacThu119411_0672. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BTHU281309:GJID-736-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID Q6LVX9_PHOPR Unreviewed; 423 AA. AC Q6LVX9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 72. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=VC0062; OrderedLocusNames=PBPRA0107; OS Photobacterium profundum (Photobacterium sp. (strain SS9)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=74109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SS9; RX PubMed=15746425; DOI=10.1126/science.1103341; RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., RA Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., RA Romualdi C., Bartlett D.H., Valle G.; RT "Life at depth: Photobacterium profundum genome sequence and RT expression analysis."; RL Science 307:1459-1461(2005). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR378663; CAG18546.1; -; Genomic_DNA. DR RefSeq; YP_128348.1; NC_006370.1. DR ProteinModelPortal; Q6LVX9; -. DR STRING; 298386.PBPRA0107; -. DR EnsemblBacteria; CAG18546; CAG18546; PBPRA0107. DR GeneID; 3123087; -. DR KEGG; ppr:PBPRA0107; -. DR PATRIC; 22930850; VBIPhoPro109272_0172. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 423 AA; 46852 MW; 63D650EB3BD8C7F6 CRC64; MSSLCLPDHL TPLLMHVEPL LANADQYQLG NTVSVSVSES GVVDIKIEER QLSLIFNQAE ADFSGFKILD QWYAPYPSVR EMQVKVEQDS RVIVCGLPTE KGCVDIWHHN GEARAVYCHH AGAGEPQRAM LLCALALDYP LEDAVTLARA HARGYQSSHQ DGHGEVSWPV SRELFPRPLT ANHPEVDVLG WQSKEVAVEP FCATDAQQLA LYPVVDTAEW VDRLLELGVK TTQLRIKNSQ DPQLETQVQQ IIAAGNQYQA QVFVNDYWQL AIKHQAYGVH LGQEDLETAD LVAIQQAGLR IGLSTHGYYE ILRAVEFSPS YIALGHIFPT TTKEMPSKPQ GLNRLALYQK LIGDTFPTVA IGGIDLPRAE KVWRTGVSSV AVVRAITEAS DPAMAVDAFN QLLVRPEFPD AINEKITDRI DAD // ID Q6N3W6_RHOPA Unreviewed; 202 AA. AC Q6N3W6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 62. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=RPA3576; OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=258594; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-98 / CGA009; RX PubMed=14704707; DOI=10.1038/nbt923; RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., RA Harrison F.H., Gibson J., Harwood C.S.; RT "Complete genome sequence of the metabolically versatile RT photosynthetic bacterium Rhodopseudomonas palustris."; RL Nat. Biotechnol. 22:55-61(2004). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX572604; CAE29017.1; -; Genomic_DNA. DR RefSeq; NP_948914.1; NC_005296.1. DR ProteinModelPortal; Q6N3W6; -. DR STRING; 258594.RPA3576; -. DR EnsemblBacteria; CAE29017; CAE29017; RPA3576. DR GeneID; 2690186; -. DR KEGG; rpa:RPA3576; -. DR PATRIC; 23291679; VBIRhoPal84835_3755. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 202 AA; 21730 MW; 682ECD8D698ED10E CRC64; MPYPDRFYPV VDSIAWVKRL AALGVGTVQL RAKDLDDGAA LQLVTDALAA VKDTPTKLII NDYWRAAIVA GAQHLHLGQE DLAEADLHEI KSAGLTLGLS THDDAELETA LAAEPDYIAL GPIFPTTLKS MRFAPQGIPK ITEWKKRVGN IPLVAIGGIK LEQAEEIFAA GADSIAVVSD VTQNPDPDAR VRAWLDFVAE KA // ID Q6NB89_RHOPA Unreviewed; 219 AA. AC Q6NB89; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 56. DE SubName: Full=Possible thiamine-phosphate pyrophosphorylase; DE Flags: Precursor; GN OrderedLocusNames=RPA0939; OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=258594; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-98 / CGA009; RX PubMed=14704707; DOI=10.1038/nbt923; RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., RA Harrison F.H., Gibson J., Harwood C.S.; RT "Complete genome sequence of the metabolically versatile RT photosynthetic bacterium Rhodopseudomonas palustris."; RL Nat. Biotechnol. 22:55-61(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX572595; CAE26383.1; -; Genomic_DNA. DR RefSeq; NP_946292.1; NC_005296.1. DR ProteinModelPortal; Q6NB89; -. DR STRING; 258594.RPA0939; -. DR EnsemblBacteria; CAE26383; CAE26383; RPA0939. DR GeneID; 2690427; -. DR KEGG; rpa:RPA0939; -. DR PATRIC; 23286091; VBIRhoPal84835_0988. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Signal. FT SIGNAL 1 29 Potential. FT CHAIN 30 219 Potential. FT /FTId=PRO_5000097076. SQ SEQUENCE 219 AA; 22551 MW; 13A0D56913997BE1 CRC64; MNAKPAPSRP APRLYLATPV TADPAALAAA LPKLLAAADI AAVLLRLESS DPRTLTSRIK AVAPVVQAGG AALLVDGHAD LVARGGADGA HLSGIKAMQE WLPQLQPSRI AGVGGLETRH DSMIAGEAGA DYVLFGEPGA DGTRPSPEAI AERLDWWAEL FEPPCVGYAT SCEEVHQFAT AGADFVLVGD FIWGADDPTA ALADAGEALR QGFAAAPRQ // ID Q6NKI9_CORDI Unreviewed; 222 AA. AC Q6NKI9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=DIP0030; OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype OS gravis). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=257309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis; RX PubMed=14602910; DOI=10.1093/nar/gkg874; RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., RA Hamlin N., Holroyd S., Jagels K., Moule S., Quail M.A., RA Rabbinowitsch E., Rutherford K.M., Thomson N.R., Unwin L., RA Whitehead S., Barrell B.G., Parkhill J.; RT "The complete genome sequence and analysis of Corynebacterium RT diphtheriae NCTC13129."; RL Nucleic Acids Res. 31:6516-6523(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX248354; CAE48541.1; -; Genomic_DNA. DR RefSeq; NP_938439.1; NC_002935.2. DR ProteinModelPortal; Q6NKI9; -. DR STRING; 257309.DIP0030; -. DR EnsemblBacteria; CAE48541; CAE48541; DIP0030. DR GeneID; 2650614; -. DR KEGG; cdi:DIP0030; -. DR PATRIC; 21481233; VBICorDip47633_0031. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6PZXB0; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). SQ SEQUENCE 222 AA; 23441 MW; E139E5E250F11341 CRC64; MLPTPRWGRD FDPRCYFVTG TGSVDHIVDV ARQAARAGAG LIQVRSKPIA ARDLYILGRE VARAVAEVNP RTRVLIDDRV DVALALMNNG EHIHGVHVGQ DDLPVRHVRA LLGDNAIIGL TTGTLELVRA SRQVAEVIDY IGAGPFRPTP TKDSGRAPVG LAGYPPLVAE SLVPVVAIGD VRPEDAADLA ATGVAGVAIV RALMNSQGVA TDVKLVLKGF AQ // ID Q6NQ84_ARATH Unreviewed; 642 AA. AC Q6NQ84; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-APR-2014, entry version 50. DE SubName: Full=At1g03160; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RA Cheuk R., Chen H., Kim C.J., Shinn P., Bowser L., Carninci P., RA Dale J.M., Hayashizaki Y., Ishida J., Jones T., Kamiya A., RA Karlin-Neumann G., Kawai J., Lam B., Lin J., Miranda M., Narusaka M., RA Nguyen M., Onodera C.S., Palm C.J., Quach H.L., Sakurai T., Satou M., RA Seki M., Southwick A., Toriumi M., Wong C., Wu H.C., Yamada K., Yu G., RA Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Arabidopsis ORF clones."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BT010575; AAQ65198.1; -; mRNA. DR ProteinModelPortal; Q6NQ84; -. DR Genevestigator; Q6NQ84; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 642 AA; 71235 MW; 64570D52E15C044E CRC64; MRTLISHRQC VTSPFLISAA SPPFPGRCFK LSSFTPPRHR RFSSLSIRNI SHESADQTSS SRPRTLYPGG YKRPELAVPG LLLRLDADEV MSGNREETLD LVDRALAKSV QIVVIDGGAT AGKLYEAACL LKSLVKGRAY LLIAERVDIA SAVGASGVAL SDEGLPAIVA RNTLMGSNPD SVLLPLVARI VKDVDSALIA SSSEGADFLI LGSGEEDTQV ADSLLKSVKI PIYVTCRGNE EAKEELQLLK SGVSGFVISL KDLRSSRDVA LRQSLDGAYV VNNHETQNMN ELPEKKNSAG FIKLEDKQKL IVEMEKSVLR ETIEIIHKAA PLMEEVSLLI DAVSRIDEPF LMVIVGEFNS GKSTVINALL GKRYLKEGVV PTTNEITFLC YSDLESEEQQ RCQTHPDGQY VCYLPAPILK DINIVDTPGT NVILQRQQRL TEEFVPRADL LVFVLSADRP LTESEVAFLR YTQQWKKKFV FILNKSDIYR DARELEEAIS FVKENTRKLL NTENVILYPV SARSALEAKL STASLVGRDD LEIADPGSNW RVQSFNELEK FLYSFLDSST ATGMERIRLK LETPMAIAER LLSSVEALVR QDCLAAREDL ASADKIISRT KEYALKMEYE SISWRRQALS LV // ID Q6SFQ9_9BACT Unreviewed; 309 AA. AC Q6SFQ9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-OCT-2013, entry version 58. DE SubName: Full=Mutator mutT protein, putative; GN ORFNames=MBMO_EBAC080-L31E09.71; OS uncultured marine bacterium 578. OC Bacteria; environmental samples. OX NCBI_TaxID=257399; RN [1] RP NUCLEOTIDE SEQUENCE. RA Heidelberg J.F., Eisen J.A., Nelson W.C., DeLong E.F.; RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RA DeLong E.F.; RT "Monterey Bay Coastal Ocean Microbial Observatory environmental clone RT sequencing."; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY458646; AAR38153.1; -; Genomic_DNA. DR ProteinModelPortal; Q6SFQ9; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01401; MUTATORMUTT. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Hydrolase. SQ SEQUENCE 309 AA; 35028 MW; 5F0E22819E4C1D26 CRC64; MQTKNKIIEV VVGIIRNENK EILIAKRQKD QFMPSYWELP GGKIEVGEDS FSALSRELYE EVGITVKDCS LIHKIFHHYP DKSVNLSIYN IKDFLGDPLG KEGQEIAWSS IEQFNNYKLL PTMWKIIHKI SLPKSYWITP DEHQTKSTID ACRKHLISGT KLIQLRSKTI LDSTYIENMY KLCKEYKARL ILNTPIKTYT EICDGWHLTS SELLSLKERP CDDNKLLGAS THNKLETAHA EKISADYISL SPVEATLSHP NAKTLGWDRS SNIIDQCNLP LFLLGGMNKE LIGKALSIGA QGVAGIREI // ID Q729I8_DESVH Unreviewed; 219 AA. AC Q729I8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 84. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE-2; Synonyms=thiE; OrderedLocusNames=DVU_2362; OS Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB OS 8303). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hildenborough / ATCC 29579 / NCIMB 8303; RX PubMed=15077118; DOI=10.1038/nbt959; RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J., RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., RA Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., RA Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M.; RT "The genome sequence of the anaerobic, sulfate-reducing bacterium RT Desulfovibrio vulgaris Hildenborough."; RL Nat. Biotechnol. 22:554-559(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017285; AAS96835.1; -; Genomic_DNA. DR RefSeq; YP_011575.1; NC_002937.3. DR ProteinModelPortal; Q729I8; -. DR STRING; 882.DVU2362; -. DR EnsemblBacteria; AAS96835; AAS96835; DVU_2362. DR GeneID; 2796521; -. DR KEGG; dvu:DVU2362; -. DR PATRIC; 32064346; VBIDesVul119526_2138. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DVUL882:GJIL-2416-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22455 MW; 1B76358C9963C708 CRC64; MTRVRKAAVD YGLYLVTDAG LTDARLHEVV TAAISGGVGI VQLREKATPT RAFVDRARAL VALLRPRGIP LLINDRVDVA LAAGADGVHV GQSDMHVGDV RALMGPDAIV GLSVETPAQA KAAEHAPVDY LGVSPVFATA TKPDAAPPWG VAGLCGLRRM TRHVLVGIGG IGPVNAAEVL HAGAEGIAVV SAICGAADPL AATRALRAVV DEVRVPVRI // ID Q72AA6_DESVH Unreviewed; 226 AA. AC Q72AA6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 83. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE-1; Synonyms=thiE; OrderedLocusNames=DVU_2091; OS Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB OS 8303). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hildenborough / ATCC 29579 / NCIMB 8303; RX PubMed=15077118; DOI=10.1038/nbt959; RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J., RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., RA Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., RA Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M.; RT "The genome sequence of the anaerobic, sulfate-reducing bacterium RT Desulfovibrio vulgaris Hildenborough."; RL Nat. Biotechnol. 22:554-559(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017285; AAS96564.1; -; Genomic_DNA. DR RefSeq; YP_011304.1; NC_002937.3. DR ProteinModelPortal; Q72AA6; -. DR STRING; 882.DVU2091; -. DR EnsemblBacteria; AAS96564; AAS96564; DVU_2091. DR GeneID; 2793545; -. DR KEGG; dvu:DVU2091; -. DR PATRIC; 32063866; VBIDesVul119526_1903. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DVUL882:GJIL-2137-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23899 MW; 56DCC90A1670FDA7 CRC64; MPVILPGTTP DADIYCLTDS GLCLGRPTVD VVDAMLQAGA RIIQYREKEK KAGEMLRECL ELRRMTREAG ACFIVNDHVD IAILCDADGV HIGQDDLPVG EVRRLIGPDR AIGLSTHSPE QAMAAVAAGV DYIGVGPIFA TKTKKDVCDP VGYAYLDWVV THLDIPFVAI GGIKLHNIGE VAAHGARCCA LVSEIVGAVD IVAQVQTVRR AMRGVAAAGT DSPQAG // ID Q72R36_LEPIC Unreviewed; 214 AA. AC Q72R36; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LIC_11915; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar OS copenhageni (strain Fiocruz L1-130). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=267671; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fiocruz L1-130; RX PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004; RA Nascimento A.L., Ko A.I., Martins E.A., Monteiro-Vitorello C.B., RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., RA Marques M.V., Oliveira M.C., Menck C.F., Leite L.C., Carrer H., RA Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., RA Ferro E.S., Ferro M.I., Furlan L.R., Gamberini M., Giglioti E.A., RA Goes-Neto A., Goldman G.H., Goldman M.H., Harakava R., Jeronimo S.M., RA Junqueira-De-Azevedo I.L., Kimura E.T., Kuramae E.E., Lemos E.G., RA Lemos M.V., Marino C.L., Nunes L.R., De Oliveira R.C., Pereira G.G., RA Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., RA Simpson A.J., Ferro J.A., Camargo L.E., Kitajima J.P., Setubal J.C., RA Van Sluys M.A.; RT "Comparative genomics of two Leptospira interrogans serovars reveals RT novel insights into physiology and pathogenesis."; RL J. Bacteriol. 186:2164-2172(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016823; AAS70498.1; -; Genomic_DNA. DR RefSeq; YP_001861.1; NC_005823.1. DR ProteinModelPortal; Q72R36; -. DR STRING; 267671.LIC11915; -. DR EnsemblBacteria; AAS70498; AAS70498; LIC_11915. DR GeneID; 2771551; -. DR KEGG; lic:LIC11915; -. DR PATRIC; 22376255; VBILepInt6257_2289. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6WX4T9; -. DR BioCyc; LINT267671:GHQI-1911-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 214 AA; 24557 MW; 5C226CDA2E43FB12 CRC64; MRANSFPWRV PGIYPILDLD FCKSRNLDYF SLPKFWIEYP DLIPFIQIRA KSASINELEF IVKSLQDLYP DLFWIVNDFW KQAIEWNCFG AHVGKEDYEA LNLEEKNTLF KSKLYLGTSS HTLEEVSELD SSLWNYTGLG PIFPTENKED AKSPIGTKTL NKIKNGNYLP VTVIGGLKVE NLDLILKEGS FLISSISMAC LENEFRTAAT KLRK // ID Q73DB4_BACC1 Unreviewed; 206 AA. AC Q73DB4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 65. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=BCE_0799; OS Bacillus cereus (strain ATCC 10987). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=222523; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10987; RX PubMed=14960714; DOI=10.1093/nar/gkh258; RA Rasko D.A., Ravel J., Okstad O.A., Helgason E., Cer R.Z., Jiang L., RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J., RA Nelson W.C., Kolsto A.-B., Fraser C.M., Read T.D.; RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic RT adaptations and a large plasmid related to Bacillus anthracis pXO1."; RL Nucleic Acids Res. 32:977-988(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017194; AAS39731.1; -; Genomic_DNA. DR RefSeq; NP_977123.1; NC_003909.8. DR ProteinModelPortal; Q73DB4; -. DR STRING; 222523.BCE_0799; -. DR EnsemblBacteria; AAS39731; AAS39731; BCE_0799. DR GeneID; 2751610; -. DR KEGG; bca:BCE_0799; -. DR PATRIC; 18850514; VBIBacCer118379_0762. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 206 AA; 22745 MW; 2ACBBBB968FF5CF9 CRC64; MKNELHVISN GHMSFEELVN VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK IVINDRIDIA ILLNIPRVQL GYRSADVRSV KEKFSYLYVG YSVHSLEEAI DAFKNGADSL VYGHVFPTDC KKGVPARGLE EISDIAKCLS IPITAIGGIT PENTGDVLAN GVSGIAVMSG IISSSNPYSK AKSYKESIRK WAEKHV // ID Q755D3_ASHGO Unreviewed; 547 AA. AC Q755D3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-APR-2014, entry version 63. DE SubName: Full=AFL110Cp; GN OrderedLocusNames=AFL110C; ORFNames=AGOS_AFL110C; OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL OS Y-1056) (Yeast) (Eremothecium gossypii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=284811; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient RT Saccharomyces cerevisiae genome."; RL Science 304:304-307(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=23749448; DOI=10.1534/g3.112.002881; RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.; RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type RT loci, numerous translocations, lack of transposons, and distinct gene RT duplications."; RL G3 (Bethesda) 3:1225-1239(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016819; AAS53264.1; -; Genomic_DNA. DR RefSeq; NP_985440.1; NM_210794.1. DR ProteinModelPortal; Q755D3; -. DR STRING; 33169.AGOS_AFL110C; -. DR EnsemblFungi; AAS53264; AAS53264; AGOS_AFL110C. DR GeneID; 4621667; -. DR KEGG; ago:AGOS_AFL110C; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR PhylomeDB; Q755D3; -. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. SQ SEQUENCE 547 AA; 58695 MW; 594C659F1DC2FAF4 CRC64; MKEVDYSLYL VTDSSMLPQG TTLDSQVTAA LQNGATLVQL REKDADGCDF VEAALRVKRI CAEFNVPLLI NDRVDVALAV DADGVHVGQQ DIPPPLVRKL VGPSKIVGWS VGRPEEVQQL AEWGQGCVDY IGVGMIFPTE TKKNPRKVPM GISGAIEIMD ALEECRATWC RTVLIGGLHA DNIGRVLLQC ASSNGKRAAD GVAVVSEIMA ASDARGATQR LRRLLDDGAY RFVVGKFTED VDYRAPDDME TYVPMLLEAS PLVHHVTNKV HQNFAANVTL AAGSSPIMSE VSSEFEDLST AAHSALVLNT GSLVDLEVAT AAVRAYNKAR RPVVFDPVGF AASRTRLDYN GHLLNMGQYT CIKGNASEIL ALSSSEHRAM RGVDSEHDVD IDTLCNAARQ VAYRYRTVVV LTGQNDIVVN GALDCSFNLG FGSAPPQDHL PAYIVSCDSI PLFSKVTATG CSLGSVIACF LGALPPDGSP FHAVLSAVLI YKSAGYFAAG RATGGASFQT ELLDELDTLF EKGSHGQMAK IYPFGSWPVK VERVDIP // ID Q7CT79_AGRT5 Unreviewed; 217 AA. AC Q7CT79; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 2. DT 14-MAY-2014, entry version 60. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=Atu3750; OS Agrobacterium tumefaciens (strain C58 / ATCC 33970). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=176299; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11743193; DOI=10.1126/science.1066804; RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., RA Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., RA Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., RA Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C., RA Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., RA Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., RA Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., RA Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., RA Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., RA Nester E.W.; RT "The genome of the natural genetic engineer Agrobacterium tumefaciens RT C58."; RL Science 294:2317-2323(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970; RX PubMed=11743194; DOI=10.1126/science.1066803; RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., RA Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., RA Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., RA Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B., RA Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., RA Cielo C., Slater S.; RT "Genome sequence of the plant pathogen and biotechnology agent RT Agrobacterium tumefaciens C58."; RL Science 294:2323-2328(2001). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE007870; AAK89656.2; -; Genomic_DNA. DR RefSeq; NP_356871.2; NC_003063.2. DR ProteinModelPortal; Q7CT79; -. DR STRING; 176299.Atu3750; -. DR EnsemblBacteria; AAK89656; AAK89656; Atu3750. DR GeneID; 1135624; -. DR KEGG; atu:Atu3750; -. DR PATRIC; 20816950; VBIAgrTum91616_3584. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 217 AA; 22812 MW; 8C7EC64B3E05E6A3 CRC64; MSIVEDRCRL VLIVPQRDDA QKQVTEVEDA LRGGDVASVI IPQYGLDDAA FQKWAELIVP IVQAAGAAAL IAGDSRTASR VKADGLHVGG NAEALAEAVE NFTPKLIVGG GNADDRHKAL EMGESNPDYV FFGKLEGDIK PEAHPKNLAL GEWWASMIEI PAIVMGGTDL SSVVAVSETG VEFVAMRSGV FDNASGAAQA VSEINALLDE KAPRFGG // ID Q7MGM4_VIBVY Unreviewed; 444 AA. AC Q7MGM4; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 14-MAY-2014, entry version 82. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=VV3206; OS Vibrio vulnificus (strain YJ016). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=196600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJ016; RX PubMed=14656965; DOI=10.1101/gr.1295503; RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., RA Liao T.-L., Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., RA Shao C.-P., Lee C.-T., Hor L.-I., Tsai S.-F.; RT "Comparative genome analysis of Vibrio vulnificus, a marine RT pathogen."; RL Genome Res. 13:2577-2587(2003). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000037; BAC95970.1; -; Genomic_DNA. DR RefSeq; NP_935999.1; NC_005139.1. DR ProteinModelPortal; Q7MGM4; -. DR STRING; 196600.VV3206; -. DR EnsemblBacteria; BAC95970; BAC95970; BAC95970. DR GeneID; 2626077; -. DR KEGG; vvy:VV3206; -. DR PATRIC; 20173304; VBIVibVul40472_3173. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RIKDSTH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; VVUL196600:GJ9W-3326-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 444 AA; 49291 MW; 1FD0616862377568 CRC64; MRLLIPSAII ELTGEIQQCL LLAKQQGFAI DHIELGVSPT RTLQLISSAK TVVFETDLIH NDSRHLGAHD FALHYHHSLA LTEVSSYLGS ECKAKTLLIN LQGEQGEAFD VWQHPLADET RALRFLSRQN HSQNESVESI YRHLAWVVTL SALDFPIEDC LTLARAMLNV SRETWVSDFA LFPTPVLHLD EFGILPSHNL EGLTKAFPRV IAQQLGLYPV VDDVSWIEKL LPLGIKTVQL RIKDPNQVDL EQQIVRAIQL GRDYGAKVYI NDYWQLAIQY QAYGVHLGQE DLQVADLAAL TNAGIALGLS THGYYELLRI VQLQPSYIAL GHIFPTTTKQ MPSLPQGLVR LKLYQQLIDT IPYDESITGV PTVAIGGIDQ SNAATVWQCG VSSLAVVRAI TLAKDVKAVI EYFKQVMAPN TTLLRLDSVS THSLEPTSEA NHVG // ID Q7MSL8_WOLSU Unreviewed; 189 AA. AC Q7MSL8; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 14-MAY-2014, entry version 57. DE SubName: Full=Putative uncharacterized protein thiB; GN Name=thiB; OrderedLocusNames=WS0320; OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC OS 11488 / FDC 602W) (Vibrio succinogenes). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Wolinella. OX NCBI_TaxID=273121; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W; RX PubMed=14500908; DOI=10.1073/pnas.1932838100; RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., RA Meyer F., Lederer H., Schuster S.C.; RT "Complete genome sequence and analysis of Wolinella succinogenes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571657; CAE09471.1; -; Genomic_DNA. DR RefSeq; NP_906571.1; NC_005090.1. DR ProteinModelPortal; Q7MSL8; -. DR STRING; 273121.WS0320; -. DR EnsemblBacteria; CAE09471; CAE09471; WS0320. DR GeneID; 2554702; -. DR KEGG; wsu:WS0320; -. DR PATRIC; 24037732; VBIWolSuc63014_0307. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FATPNKG; -. DR OrthoDB; EOG6FJNJD; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 189 AA; 20923 MW; B74C9D210B006DA6 CRC64; MKSYLITDPA LYPSAPPLFQ NYLREIFHLH HPHCACLRDS KESRRELLAP LFVKACQECG VIPLLNSDIK MALAHGFEGV HLKGNQLGEI PKLQAYGLKS FYSAHSLQDL QRASKEGVGV ATISPIFATP NKGEPLGIEF LEILEEYAFA CEIFALGGIV SQKEIDFLKG FSSINGFASI RFFLPLPSN // ID Q7MT72_PORGI Unreviewed; 647 AA. AC Q7MT72; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 14-MAY-2014, entry version 86. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=PG_2109; OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=242619; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-308 / W83; RX PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003; RA Nelson K., Fleishmann R., DeBoy R., Paulsen I., Fouts D., Eisen J., RA Daugherty S., Dodson R., Durkin A., Gwinn M., Haft D., Kolonay J., RA Nelson W., White O., Mason T., Tallon L., Gray J., Granger D., RA Tettelin H., Dong H., Galvin J., Duncan M., Dewhirst F., Fraser C.; RT "Complete genome sequence of the oral pathogenic bacterium RT Porphyromonas gingivalis strain W83."; RL J. Bacteriol. 185:5591-5601(2003). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015924; AAQ67068.1; -; Genomic_DNA. DR RefSeq; NP_906169.1; NC_002950.2. DR ProteinModelPortal; Q7MT72; -. DR STRING; 242619.PG2109; -. DR DNASU; 2551490; -. DR EnsemblBacteria; AAQ67068; AAQ67068; PG_2109. DR GeneID; 2551490; -. DR KEGG; pgi:PG2109; -. DR PATRIC; 22981202; VBIPorGin134034_1964. DR KO; K00788; -. DR OMA; WINAIRS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PGIN242619:GHX8-1907-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 2. DR SUPFAM; SSF51391; SSF51391; 2. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 647 AA; 70947 MW; 2E91C3303B24ECCB CRC64; MKPWLITPER LTSEQIGLLD HFFDRGLERL HLRLPSAGEE DYSQVIEAVA ACYRRRIVVH DHPRLVGRYG LCGLHLPERV WKGMTDRPQL PDGCTVSASC HAIEDIESFP FRLDYCFLSP VFDSLCKVGY AGRFSPDSLG DRLQRLHLPV VALGGITPDR LPQLRRAGFA SAAALGYVWL VEGRELMRWQ ELCTPAVICV GGVDPSAGAG ITADVRTAEN MGVRAYTVAT AITFQGSGSY RGERWVDSAD IIRQIESLSA EMEPAVAKIG LIRDSDTLSL VVDCLKKVFP SIRIVWDPVL RASADSSAGQ ADRFNLEDIT ALSRIDFITP NLPEARHLLG CEPDDETLLD FYRRSGVGLV LKGGHAGESV VTDRIVYDGR CEALRLLRGG TGKHGTGCAH STAFAAALAL EQEPFTAAGM AQLYVSRLRE RASGLLAMHK DLPVDPVVRL MSEIDLQFIT HRQPDLSELE EAEAVCRIGV RWVQLRMKEA SDEEMLHTAC AVKAVCRHHG ALFVVNDRVE IARQVDADGV HLGKEDMAIV EARRILGSNK IIGRTCNTME DVRRAYAEGA DYVGIGPYRY TETKQRLAPV LGLEGYKAIA ACMQAEGIRL PAFAIGGIED ADIPLIRDCG IGGIAVSGSL IRKIKKN // ID Q7NS16_CHRVO Unreviewed; 290 AA. AC Q7NS16; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 14-MAY-2014, entry version 82. DE SubName: Full=Probable bifunctional dGTP-pyrophosphohydrolase/thiamine phosphate synthase; DE EC=3.6.1.-; GN OrderedLocusNames=CV_3611; OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / OS NBRC 12614 / NCIMB 9131 / NCTC 9757). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Chromobacterium. OX NCBI_TaxID=243365; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / RC NCTC 9757; RX PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., RA Batista J.S., Belo A., van den Berg C., Bogo M., Bonatto S., RA Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., RA Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., RA Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., RA Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., RA Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., RA Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., RA Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., RA di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., RA Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., RA Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., RA Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., RA Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., RA Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., RA Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., RA Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., RA Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., RA Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016825; AAQ61273.1; -; Genomic_DNA. DR RefSeq; NP_903281.1; NC_005085.1. DR ProteinModelPortal; Q7NS16; -. DR STRING; 243365.CV_3611; -. DR EnsemblBacteria; AAQ61273; AAQ61273; CV_3611. DR GeneID; 2548365; -. DR KEGG; cvi:CV_3611; -. DR PATRIC; 21442045; VBIChrVio67196_3538. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CVIO243365:GHUD-3706-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 290 AA; 31284 MW; 6618316DB4DBD836 CRC64; MLGSRPEGKP YAGYWEFPGG KVEAGETPLA ALKREFNEEM GITVTAATPW LTKIHHYEHA SVHLRFFRIW DWLGDPHPRE GQSFAWQRPG RLTVAPMLPA NGPILKSLAL PSCYAITCAA EIGVEAQLAR LAERDWGMVQ VREREMGREA LADFVARAAA IVRPRGGKLV VNADPAWLEG WPVDGVHLNG ARLAALESRP AFDWVGASIH GADELARAGE LGLDYALLSP VAPTATHPGA SLLGWDGFSA CLAGGVPLPV YALGGMRAEN LDLARLHGAH GVALMRGAWR // ID Q7P415_FUSNV Unreviewed; 206 AA. AC Q7P415; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 19-MAR-2014, entry version 45. DE SubName: Full=Regulatory protein TENI; GN ORFNames=FNV0366; OS Fusobacterium nucleatum subsp. vincentii ATCC 49256. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=209882; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49256; RX PubMed=12799352; DOI=10.1101/gr.566003; RA Kapatral V., Ivanova N., Anderson I., Reznik G., Bhattacharyya A., RA Gardner W.L., Mikhailova N., Lapidus A., Larsen N., D'Souza M., RA Walunas T., Haselkorn R., Overbeek R., Kyrpides N.; RT "Genome analysis of F. nucleatum sub spp vincentii and its comparison RT with the genome of F. nucleatum ATCC 25586."; RL Genome Res. 13:1180-1189(2003). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49256; RA Karpatral V., Ivanova N., Anderson I., Reznik G., Bhattacharyya A., RA Gardner W.L., Mikhailova N., Larsen N., D'Souza M., Walunas T., RA Haselkorn R., Overbeek R., Kyrpides N.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AABF01000148; EAA23347.1; -; Genomic_DNA. DR ProteinModelPortal; Q7P415; -. DR EnsemblBacteria; EAA23347; EAA23347; EAA23347. DR PATRIC; 30272114; VBIFusNuc72376_2003. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; SQ SEQUENCE 206 AA; 23935 MW; 04B7AF8D602400CF CRC64; MIENKIKLNI ISNRKLCENE NLEKQIEKIF SAYQRKIILE NFEIVALTLR EKDLYKNEYL KLVEKIYPIC QKYRIDLILH QNYDLVLEDK YNIEGIHLSY NTFKSLNKNI RKELIKKYKK IGVSIHSIDE AKEAENLGAT YIVAGHIFKT DCKKDLEPRG LEFIQELSSA LIIPIFAIGG INQENSHLVI NNGAFGVCMM SSLMKH // ID Q7P5E1_FUSNV Unreviewed; 206 AA. AC Q7P5E1; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 19-MAR-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=FNV0947; OS Fusobacterium nucleatum subsp. vincentii ATCC 49256. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=209882; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49256; RX PubMed=12799352; DOI=10.1101/gr.566003; RA Kapatral V., Ivanova N., Anderson I., Reznik G., Bhattacharyya A., RA Gardner W.L., Mikhailova N., Lapidus A., Larsen N., D'Souza M., RA Walunas T., Haselkorn R., Overbeek R., Kyrpides N.; RT "Genome analysis of F. nucleatum sub spp vincentii and its comparison RT with the genome of F. nucleatum ATCC 25586."; RL Genome Res. 13:1180-1189(2003). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49256; RA Karpatral V., Ivanova N., Anderson I., Reznik G., Bhattacharyya A., RA Gardner W.L., Mikhailova N., Larsen N., D'Souza M., Walunas T., RA Haselkorn R., Overbeek R., Kyrpides N.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AABF01000072; EAA23916.1; -; Genomic_DNA. DR ProteinModelPortal; Q7P5E1; -. DR EnsemblBacteria; EAA23916; EAA23916; EAA23916. DR PATRIC; 30270859; VBIFusNuc72376_1424. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22765 MW; DD440E5E3CE4346B CRC64; MDLKDCKIYL VTDEKSCNGK DFYKCIEEAI KGGVKIIQLR EKTLSTKDFF IKALKVKEIC KSYGVLFIIN DRLDITQAVE ADGVHLGQSD MPIEKAREIL KDKFLIGATA KNIEEAKKAE LLGADYIGSG AIFGTSTKDN AKKLDMKDLK KIVNSVKIPV FAIGGININN VWMLKNIGLQ GICSVSGILS EIDCKKAVEN ILKNFN // ID Q7VF49_HELHP Unreviewed; 214 AA. AC Q7VF49; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 14-MAY-2014, entry version 83. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=HH_1828; OS Helicobacter hepaticus (strain ATCC 51449 / 3B1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=235279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51449 / 3B1; RX PubMed=12810954; DOI=10.1073/pnas.1332093100; RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., RA Bell M., Droge M., Fartmann B., Fischer H.P., Ge Z., Horster A., RA Holland R., Klein K., Konig J., Macko L., Mendz G.L., Nyakatura G., RA Schauer D.B., Shen Z., Weber J., Frosch M., Fox J.G.; RT "The complete genome sequence of the carcinogenic bacterium RT Helicobacter hepaticus."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017125; AAP78425.1; -; Genomic_DNA. DR RefSeq; NP_861359.1; NC_004917.1. DR ProteinModelPortal; Q7VF49; -. DR STRING; 235279.HH1828; -. DR EnsemblBacteria; AAP78425; AAP78425; HH_1828. DR GeneID; 1492375; -. DR KEGG; hhe:HH1828; -. DR PATRIC; 20591090; VBIHelHep90276_1802. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HHEP235279:GHUA-1869-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23661 MW; 8543EBBFBF8907C9 CRC64; MKPKLQGIYA ISDEILTPYE ILPQCLESAL KAGVKIFQLR DKSHSDSWLY PQAKKLMALC EKYNALFVMN DRLNLALKLN APALHLGKDD GVIAQARERF KGILGASSYA DLQRAKDLES LGVNYVAFGA FFASPTKPNA PLTPLEILES AKAILNIPIC AIGGISTQNI YLLKNADMFA VISALWQYKI QDSPLEIQCQ NIHRNALALI QSLE // ID Q7VG26_HELHP Unreviewed; 199 AA. AC Q7VG26; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 16-APR-2014, entry version 56. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=HH_1498; OS Helicobacter hepaticus (strain ATCC 51449 / 3B1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=235279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51449 / 3B1; RX PubMed=12810954; DOI=10.1073/pnas.1332093100; RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., RA Bell M., Droge M., Fartmann B., Fischer H.P., Ge Z., Horster A., RA Holland R., Klein K., Konig J., Macko L., Mendz G.L., Nyakatura G., RA Schauer D.B., Shen Z., Weber J., Frosch M., Fox J.G.; RT "The complete genome sequence of the carcinogenic bacterium RT Helicobacter hepaticus."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017125; AAP78095.1; -; Genomic_DNA. DR RefSeq; NP_861029.1; NC_004917.1. DR ProteinModelPortal; Q7VG26; -. DR STRING; 235279.HH1498; -. DR EnsemblBacteria; AAP78095; AAP78095; HH_1498. DR GeneID; 1492045; -. DR KEGG; hhe:HH1498; -. DR PATRIC; 20590452; VBIHelHep90276_1485. DR KO; K00788; -. DR OMA; IIGYSAH; -. DR OrthoDB; EOG6FJNJD; -. DR BioCyc; HHEP235279:GHUA-1537-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 199 AA; 22532 MW; ADECD23F29BA5C06 CRC64; MKNTDFITLL ITPHINGAYL ENLQLKIQSL SVDWIMYRHQ NSEWIESFTQ SLSFLHKPLL LNIPFKNTEE ILQLSKDFAG VHLKSIYLSW ITPLRESYLA LGEKKIIGYS AHSIDEVTYA LACGADYCTL SPIFSTPNKG TPLGMEVFYQ IPKSLRSRII ALGGINNYHI PLLKELGLLG FAGIRCFEET NENHRGVAD // ID Q7VSW1_BORPE Unreviewed; 320 AA. AC Q7VSW1; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 14-MAY-2014, entry version 79. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=BP3809; OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257313; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX640422; CAE44064.1; -; Genomic_DNA. DR RefSeq; NP_882307.1; NC_002929.2. DR ProteinModelPortal; Q7VSW1; -. DR STRING; 257313.BP3809; -. DR EnsemblBacteria; CAE44064; CAE44064; BP3809. DR GeneID; 2665081; -. DR KEGG; bpe:BP3809; -. DR PATRIC; 21161304; VBIBorPer7866_4115. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPER257313:BP3809-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Reference proteome. SQ SEQUENCE 320 AA; 34128 MW; 760C8F90EDF29237 CRC64; MSEKIVDVAA GLILRPDGQL LLGQRPEGKP WAGWWELPGG KLEPGETVLQ ALARELHEEL GIRVTEAHPW VTYVHVYPHT TVRLAFCHVT GWEGEPRGLE NQRLEWVDPA RAHEVGDLLP AALPPLRWLQ LPTAYAISAI GAPAALADFT ARLRQALDGG LKLVLLREPD WPGGADAASL RDAMQAILAQ CRAAGARLLV SSRHPQAWWR EADGVHLTAR DAQALKQRPA LPEGALVGVS AHGHAEIVHA RDLGADFAVL GPVLATASHP EQAPLGWPGF AAGIRDAGMP VYALGGQSPA TLAEARLHGA HGIAGIRGLL // ID Q7W3S4_BORPA Unreviewed; 320 AA. AC Q7W3S4; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 14-MAY-2014, entry version 82. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=BPP3955; OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257311; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX640435; CAE39238.1; -; Genomic_DNA. DR RefSeq; NP_886103.1; NC_002928.3. DR ProteinModelPortal; Q7W3S4; -. DR STRING; 257311.BPP3955; -. DR EnsemblBacteria; CAE39238; CAE39238; BPP3955. DR GeneID; 1664835; -. DR KEGG; bpa:BPP3955; -. DR PATRIC; 21151988; VBIBorPar43418_4152. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPAR257311:BPP3955-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 320 AA; 34128 MW; 760C8F90EDF29237 CRC64; MSEKIVDVAA GLILRPDGQL LLGQRPEGKP WAGWWELPGG KLEPGETVLQ ALARELHEEL GIRVTEAHPW VTYVHVYPHT TVRLAFCHVT GWEGEPRGLE NQRLEWVDPA RAHEVGDLLP AALPPLRWLQ LPTAYAISAI GAPAALADFT ARLRQALDGG LKLVLLREPD WPGGADAASL RDAMQAILAQ CRAAGARLLV SSRHPQAWWR EADGVHLTAR DAQALKQRPA LPEGALVGVS AHGHAEIVHA RDLGADFAVL GPVLATASHP EQAPLGWPGF AAGIRDAGMP VYALGGQSPA TLAEARLHGA HGIAGIRGLL // ID Q7WF52_BORBR Unreviewed; 320 AA. AC Q7WF52; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 14-MAY-2014, entry version 82. DE SubName: Full=Putative uncharacterized protein; GN OrderedLocusNames=BB4428; OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) OS (Alcaligenes bronchisepticus). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX640450; CAE34791.1; -; Genomic_DNA. DR RefSeq; NP_890962.1; NC_002927.3. DR ProteinModelPortal; Q7WF52; -. DR STRING; 257310.BB4428; -. DR EnsemblBacteria; CAE34791; CAE34791; BB4428. DR GeneID; 2659778; -. DR KEGG; bbr:BB4428; -. DR PATRIC; 21142319; VBIBorBro124907_4505. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BBRO257310:BB4428-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 320 AA; 34128 MW; 760C8F90EDF29237 CRC64; MSEKIVDVAA GLILRPDGQL LLGQRPEGKP WAGWWELPGG KLEPGETVLQ ALARELHEEL GIRVTEAHPW VTYVHVYPHT TVRLAFCHVT GWEGEPRGLE NQRLEWVDPA RAHEVGDLLP AALPPLRWLQ LPTAYAISAI GAPAALADFT ARLRQALDGG LKLVLLREPD WPGGADAASL RDAMQAILAQ CRAAGARLLV SSRHPQAWWR EADGVHLTAR DAQALKQRPA LPEGALVGVS AHGHAEIVHA RDLGADFAVL GPVLATASHP EQAPLGWPGF AAGIRDAGMP VYALGGQSPA TLAEARLHGA HGIAGIRGLL // ID Q81HQ8_BACCR Unreviewed; 208 AA. AC Q81HQ8; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 68. DE SubName: Full=Regulatory protein TENI; GN OrderedLocusNames=BC_0746; OS Bacillus cereus (strain ATCC 14579 / DSM 31). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., RA Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., RA Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., RA Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D., RA Overbeek R., Kyrpides N.C.; RT "Genome sequence of Bacillus cereus and comparative analysis with RT Bacillus anthracis."; RL Nature 423:87-91(2003). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016877; AAP07737.1; -; Genomic_DNA. DR RefSeq; NP_830536.1; NC_004722.1. DR ProteinModelPortal; Q81HQ8; -. DR STRING; 226900.BC0746; -. DR PRIDE; Q81HQ8; -. DR EnsemblBacteria; AAP07737; AAP07737; BC_0746. DR GeneID; 1203097; -. DR KEGG; bce:BC0746; -. DR PATRIC; 32597144; VBIBacCer54481_0685. DR eggNOG; COG0352; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER226900:GJEU-748-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 208 AA; 23036 MW; 316214A22E470F4E CRC64; MNMKNELHVI SNGHMPFEEL VNVAMQIESE IDYLHIRERE KSTKELYEGV ESLLMEGFPA SKIVINDRID IAILLNIPRV QLGYRSTDVK SVKEKFSYLH VGYSVHSLDE AIVAFKNGAD SLVYGHVFPT DCKKGVPARG LEEISDIARC LSIPITAIGG ITPENTVDVL TNGVSGIAVM SGIVSSSNPY SKAKSYKESI RKWAEKHV // ID Q81UX7_BACAN Unreviewed; 206 AA. AC Q81UX7; E9QZM1; E9QZM2; Q6I359; Q6KWX8; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 86. DE SubName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=BA_0729, BAS0695, GBAA_0729; OS Bacillus anthracis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames, and Ames / isolate Porton; RX PubMed=12721629; DOI=10.1038/nature01586; RA Read T.D., Peterson S.N., Tourasse N., Baillie L.W., Paulsen I.T., RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M., RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., RA Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., RA Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., RA Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., RA Hazen A., Cline R., Redmond C., Thwaite J.E., White O., Salzberg S.L., RA Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolsto A.B., RA Fraser C.M.; RT "The genome sequence of Bacillus anthracis Ames and comparison to RT closely related bacteria."; RL Nature 423:81-86(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sterne; RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., RA Richardson P., Rubin E., Tice H.; RT "Complete genome sequence of Bacillus anthracis Sterne."; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames ancestor, and Ames Ancestor; RX PubMed=18952800; DOI=10.1128/JB.01347-08; RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.; RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."; RL J. Bacteriol. 191:445-446(2009). RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ames; RA Joardar V., Shrivastava S., Brinkac L.M., Harkins D.M., Durkin A.S., RA Sutton G.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016879; AAP24740.1; -; Genomic_DNA. DR EMBL; AE017334; AAT29837.1; -; Genomic_DNA. DR EMBL; AE017225; AAT53022.1; -; Genomic_DNA. DR RefSeq; NP_843254.1; NC_003997.3. DR RefSeq; YP_017362.1; NC_007530.2. DR RefSeq; YP_026971.1; NC_005945.1. DR STRING; 198094.BA_0729; -. DR DNASU; 1088663; -. DR EnsemblBacteria; AAP24740; AAP24740; BA_0729. DR EnsemblBacteria; AAT29837; AAT29837; GBAA_0729. DR EnsemblBacteria; AAT53022; AAT53022; BAS0695. DR GeneID; 1088663; -. DR GeneID; 2814395; -. DR GeneID; 2849549; -. DR KEGG; ban:BA_0729; -. DR KEGG; bar:GBAA_0729; -. DR KEGG; bat:BAS0695; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ANTHRA:TENI-MONOMER; -. DR BioCyc; BANT260799:GJAJ-775-MONOMER; -. DR BioCyc; BANT261594:GJ7F-803-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 206 AA; 22890 MW; 1704B425B019B985 CRC64; MKNELHVISN GHMSFEELVS VAMQIESEID YLHIREREKS TKELYEGVES LLKKGFPASK LVINDRIDIA ILLNIPRVQL GYRSTDVRSV KEKFSYLHVG YSVHSLEEAI EAFKNGADSL VYGHVFPTEC KKGVPARGLE EISDIARSLS IPIIAIGGIT PENTKDILAS EVSGIAVMSG IVSSSNPYSK AKSYKESIRK WAEKHV // ID Q82ST9_NITEU Unreviewed; 311 AA. AC Q82ST9; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 77. DE SubName: Full=NUDIX hydrolase; GN OrderedLocusNames=NE2215; OS Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=228410; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19718 / NBRC 14298; RX PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003; RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.; RT "Complete genome sequence of the ammonia-oxidizing bacterium and RT obligate chemolithoautotroph Nitrosomonas europaea."; RL J. Bacteriol. 185:2759-2773(2003). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL954747; CAD86127.1; -; Genomic_DNA. DR RefSeq; NP_842217.1; NC_004757.1. DR ProteinModelPortal; Q82ST9; -. DR STRING; 228410.NE2215; -. DR EnsemblBacteria; CAD86127; CAD86127; NE2215. DR GeneID; 1083180; -. DR KEGG; neu:NE2215; -. DR PATRIC; 22715815; VBINitEur56163_2486. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; CGASCHN; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NEUR228410:GJNO-2259-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 311 AA; 34263 MW; 2FCE8FD0690D0165 CRC64; MAGPSLVEVA AAVLIRPDDS FLLACRPDGK PYAGYWEFPG GKIETGESPL QALARELDEE LGITVRQATP WLTRTFSYPH ATVRLRFYRV TDWHGELTPR ERQQFAWQTA ENITVSPLLP ANTPILRSLA LPSIYAVTRT VETDIEASLL SIGQTLGNGV KLLQIRQKAM SHDQLEHFSR TALQLARSYQ ATVLINENIP LAQTLQADGV HLTAAQLRSL HSRPAVNWCG ASCHNEQELQ RAERLGVDFV TLSPVQPTLS HPGAAALGWK EFAALIRDYP LPVYALGGLL PADLETAREY GAHGIAMMRS I // ID Q83EI6_COXBU Unreviewed; 479 AA. AC Q83EI6; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 82. DE SubName: Full=Phosphomethylpyrimidine kinase; DE EC=2.5.1.3; DE EC=2.7.1.49; DE EC=2.7.4.7; GN Name=thiDE; OrderedLocusNames=CBU_0334; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Coxiella. OX NCBI_TaxID=227377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I; RX PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., RA Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., RA DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., RA Khouri H.M., Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., RA Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella RT burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493; RX PubMed=19047403; DOI=10.1128/IAI.01141-08; RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., RA Samuel J.E., Heinzen R.A.; RT "Comparative genomics reveal extensive transposon-mediated genomic RT plasticity and diversity among potential effector proteins within the RT genus Coxiella."; RL Infect. Immun. 77:642-656(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016828; AAO89890.1; -; Genomic_DNA. DR RefSeq; NP_819376.1; NC_002971.3. DR ProteinModelPortal; Q83EI6; -. DR STRING; 227377.CBU_0334; -. DR PRIDE; Q83EI6; -. DR EnsemblBacteria; AAO89890; AAO89890; CBU_0334. DR GeneID; 1208216; -. DR KEGG; cbu:CBU_0334; -. DR PATRIC; 17929361; VBICoxBur82552_0328. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CBUR227377:GJ7S-339-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. SQ SEQUENCE 479 AA; 52752 MW; 3D5E25FB3133E295 CRC64; MNQKSIVWSI GGSDCSGGAG CQADILTCRD FNVHAASIIT TITAQNAEQV LKINYCDSDL IQKQIQALKE TLPPTVIKLG LLGTKEIVTA VASYLKNYSG KVVCDPVLNS TSGVLLHASD YLDLLKKLLF PHVDLLTPNI PEAEILIQNK IHTFSDIISA AHQLLKCGVS AVLLKGGHLI GSKARDFFTD GKCEFWLAHT KIPKTRVRGT GCALSSAISS AIALGYSLKD AIVVAKMYVQ QGIRQNFKVN TQELMGRQGF PRRSIDLPWV TKNANFKRKS FPLCNSFGFY PIVDSVEWVE RLLSYGVRTI QLRIKNASPQ KIKKAVIESV ALARHYQAKL FINDYWKLAI EAGAYGVHLG QEDLETADLS AIRAVNLRLG ISTHTLYELS RAHAIQPSYV AFGPIYETYS KPMPYSARGL EWLRYWCEIS PYPVVAIGGI NLNRLESVLN AGAVNVAVIS AVTKSKTPQK TVRAFLNRI // ID Q87EA6_XYLFT Unreviewed; 320 AA. AC Q87EA6; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 80. DE SubName: Full=DGTP-pyrophosphohydrolase; GN Name=mutT; OrderedLocusNames=PD_0412; OS Xylella fastidiosa (strain Temecula1 / ATCC 700964). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=183190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Temecula1 / ATCC 700964; RX PubMed=12533478; DOI=10.1128/JB.185.3.1018-1026.2003; RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., RA Miyaki C.Y., Furlan L.R., Camargo L.E., da Silva A.C., Moon D.H., RA Takita M.A., Lemos E.G., Machado M.A., Ferro M.I., da Silva F.R., RA Goldman M.H., Goldman G.H., Lemos M.V., El-Dorry H., Tsai S.M., RA Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., RA Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., RA Marino C.L., Giglioti E., Abreu I.L., Alves L.M., do Amaral A.M., RA Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., RA da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., RA Leoni S.G., Oliveira A.R., Rosa V.E.Jr., Sassaki F.T., Sena J.A., RA de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., RA Civerolo E.L., Simpson A.J., Almeida N.F.Jr., Setubal J.C., RA Kitajima J.P.; RT "Comparative analyses of the complete genome sequences of Pierce's RT disease and citrus variegated chlorosis strains of Xylella RT fastidiosa."; RL J. Bacteriol. 185:1018-1026(2003). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE009442; AAO28291.1; -; Genomic_DNA. DR RefSeq; NP_778642.1; NC_004556.1. DR ProteinModelPortal; Q87EA6; -. DR STRING; 183190.PD0412; -. DR EnsemblBacteria; AAO28291; AAO28291; PD_0412. DR GeneID; 1144615; -. DR KEGG; xft:PD0412; -. DR PATRIC; 24148433; VBIXylFas71109_0537. DR eggNOG; COG0494; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XFAS183190:GIX4-412-MONOMER; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 320 AA; 35468 MW; E7754B57E973CFA1 CRC64; MTDSLRSIHV VAAVIADVRG RLLLSRRTEN SDMPGLWEFP GGKRESGETS EQALARELYE ELGISADVGE WLMEVPQLYP GKRLRLEVRR VRAWKGGLRG REGQALTWVE PDKLLRYSMP PADQPVVGML RQPDRYLVTP EPGEQDAEWL DAVEHAYRLG IERIQLRMRQ HDPVRWSGLV RQAVQRRGRA HVEVLLNRDI ALAEALGIGV HLGAEQLAVL DARPLPVGLP VGASCHCLAD LCHAQRIGCD FAVLGPVLPT ESHPGAVTLG WERFEQLREQ VALPIYAIGG MCADQVKEAR RHGAQGIAAM RGLWPGGAKQ // ID Q87KF1_VIBPA Unreviewed; 444 AA. AC Q87KF1; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 81. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; GN OrderedLocusNames=VP3026; OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=223926; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIMD 2210633; RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1; RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.; RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism RT distinct from that of V. cholerae."; RL Lancet 361:743-749(2003). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000031; BAC61289.1; -; Genomic_DNA. DR RefSeq; NP_799405.1; NC_004603.1. DR ProteinModelPortal; Q87KF1; -. DR STRING; 223926.VP3026; -. DR DNASU; 1190618; -. DR EnsemblBacteria; BAC61289; BAC61289; BAC61289. DR GeneID; 1190618; -. DR KEGG; vpa:VP3026; -. DR PATRIC; 20144318; VBIVibPar50997_2909. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RIKDSTH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; VPAR223926:GHK4-3162-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 444 AA; 49173 MW; BFD241E09C3971C7 CRC64; MAKILIPSSL IPLTGAVLQC LLLAKEQGFS IDEIELGVSP TQFIQLVLGQ NTFRVGTDLI DVCEEAETAD FVLYYQSGLS VSECRQQPSS AIFIGIQDVE SKLDDSVKTT SADVLDIWRH PVNDEIRALS VASTSRTTTL QTDQHLAWTV TLLALDFPIE DALTLARPMT NVSRETLING ETMVKQEWAS QFADFPTPVL EDCRLGIKVG WSSHGQSVNF PHLSKQSLGL YPVVDDVSWI ERLLPLGINT IQLRIKDPYQ PDLEQQIARA IELGRQYDAQ VFINDYWQLA IKHGAFGVHL GQEDIEDSNL SQLSTAGICL GLSTHGYYEL LRIVQINPSY IALGHIFSTT TKQMPSKPQG LVRLALYQKL NDSIPYGESV GYPTVAIGGI DQSNAEQVWQ CGVSSLAVVR AITLSESPKQ VIEFFDQLMN TTSTSLVMED YRAY // ID Q87WZ6_PSESM Unreviewed; 316 AA. AC Q87WZ6; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 83. DE SubName: Full=MutT/nudix family protein; GN OrderedLocusNames=PSPTO_4397; OS Pseudomonas syringae pv. tomato (strain DC3000). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=223283; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DC3000; RX PubMed=12928499; DOI=10.1073/pnas.1731982100; RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T., RA Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., RA Madupu R., Daugherty S., Brinkac L., Beanan M.J., Haft D.H., RA Nelson W.C., Davidsen T., Zafar N., Zhou L., Liu J., Yuan Q., RA Khouri H., Fedorova N., Tran B., Russell D., Berry K., Utterback T., RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.L., Ramos A.R., RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., RA Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X., Bender C.L., RA White O., Fraser C.M., Collmer A.; RT "The complete genome sequence of the Arabidopsis and tomato pathogen RT Pseudomonas syringae pv. tomato DC3000."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016853; AAO57846.1; -; Genomic_DNA. DR RefSeq; NP_794151.1; NC_004578.1. DR ProteinModelPortal; Q87WZ6; -. DR STRING; 223283.PSPTO_4397; -. DR EnsemblBacteria; AAO57846; AAO57846; PSPTO_4397. DR GeneID; 1186078; -. DR KEGG; pst:PSPTO_4397; -. DR PATRIC; 20000304; VBIPseSyr93040_4512. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PSYR223283:GJIX-4462-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 316 AA; 34146 MW; 1DCEE6E09B2CF250 CRC64; MKRVHVAAAV IRGTDGRVLI ARRADSQHQG GLWEFPGGKV EAGETVEIAL ARELQEELGI VVTAARPLIK VCHDYPDKQV LLDVWEVSAF TGEPHGAEGQ PLVWASPREL ANYDFPAANQ PIVAAARLPG EYLITPEGLD NIELLRGLQK AIAGGIKLVQ LRAPGGYDPK YRDLAVDAAG LCAGKAQLML KGPLEWLGDF PSAGWHLTAQ QLRKYASNGR PFPENRWLAA SCHSAEELAL AEQMGVDFVT LSPVQPTLTH PDAQPLGWEQ ATRLIAGFNK PVFLLGGVGP AQRQQAWESG AQGVAGIRAF WPDEII // ID Q88N67_PSEPK Unreviewed; 314 AA. AC Q88N67; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 81. DE SubName: Full=MutT/nudix family protein/thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=PP_1348; OS Pseudomonas putida (strain KT2440). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=160488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT2440; RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x; RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., RA Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M., RA Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., RA Madupu R., Nelson W., White O., Peterson J., Khouri H., Hance I., RA Chris Lee P., Holtzapple E., Scanlan D., Tran K., Moazzez A., RA Utterback T., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., RA Kiewitz C., Eisen J.A., Timmis K.N., Dusterhoft A., Tummler B., RA Fraser C.M.; RT "Complete genome sequence and comparative analysis of the RT metabolically versatile Pseudomonas putida KT2440."; RL Environ. Microbiol. 4:799-808(2002). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015451; AAN66971.1; -; Genomic_DNA. DR RefSeq; NP_743507.1; NC_002947.3. DR ProteinModelPortal; Q88N67; -. DR STRING; 160488.PP_1348; -. DR EnsemblBacteria; AAN66971; AAN66971; PP_1348. DR GeneID; 1047011; -. DR KEGG; ppu:PP_1348; -. DR PATRIC; 19940897; VBIPsePut30601_1427. DR eggNOG; COG0494; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPUT160488:GIXO-1388-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 314 AA; 34390 MW; 98E1884B3EDE7ED0 CRC64; MKRIHVVAAV IRGADGRILI ARRADTQHQG GLWEFPGGKV EEGESVEAAL ARELREELGI EVSRSRALIK VSHDYPDKQV LLDVREVEAF TGEPHGAEGQ PLEWVAPRDL PQYEFPEANK PIVAAARLPD QYLITPDGLE VPQLLKGIQK AVANGIRLIQ LRAPDMYDPK YRDVAVDAVG LCAGKAQLML KGPLEWLGDF PAAGWHLTAA QLRKYAARGR PFPKERWLAA SCHSAEELAL AEQMGVDFVT LSPVQATQTH PEAVPLGWDE AQRLTAGFNK PVYLLGGVGP SEREQAWEAG AQGVAGIRAF WPEV // ID Q893R4_CLOTE Unreviewed; 204 AA. AC Q893R4; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 68. DE SubName: Full=Regulatory protein tenI; GN Name=tenI; OrderedLocusNames=CTC_01746; OS Clostridium tetani (strain Massachusetts / E88). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=212717; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Massachusetts / E88; RX PubMed=12552129; DOI=10.1073/pnas.0335853100; RA Bruggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., RA Gottschalk G.; RT "The genome sequence of Clostridium tetani, the causative agent of RT tetanus disease."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015927; AAO36278.1; -; Genomic_DNA. DR RefSeq; NP_782341.1; NC_004557.1. DR ProteinModelPortal; Q893R4; -. DR STRING; 212717.CTC01746; -. DR EnsemblBacteria; AAO36278; AAO36278; CTC_01746. DR GeneID; 1060941; -. DR KEGG; ctc:CTC01746; -. DR PATRIC; 19511545; VBICloTet101274_1820. DR KO; K00788; -. DR OMA; YILAGHI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CTET212717:GJAM-1608-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 204 AA; 22928 MW; 08028F094D600F65 CRC64; MAKRFDIMIF VVTNRKICGE ENFIKTIEEC AKYKPFSIIL REKDLDYKNL YKLAVDIKKV TDKYNIPLII NGDLKISKEL NTWGYHCSIS AFRKINVKVD RKLGISVHSL NEAVEAEKLG ADYILAGHIY ETKCKEGLKG RGQNFIKSIS QKVSIPIIAI GGITEENTAN VIKSGAKGIA IMSSAMKKPS TILTLKKEFR TILI // ID Q89FP1_BRADU Unreviewed; 208 AA. AC Q89FP1; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 86. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=blr6658; OS Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC OS 14792 / USDA 110). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=224911; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110; RX PubMed=12597275; DOI=10.1093/dnares/9.6.189; RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., RA Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., RA Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., RA Tabata S.; RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium RT Bradyrhizobium japonicum USDA110."; RL DNA Res. 9:189-197(2002). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000040; BAC51923.1; -; Genomic_DNA. DR RefSeq; NP_773298.1; NC_004463.1. DR ProteinModelPortal; Q89FP1; -. DR STRING; 224911.blr6658; -. DR EnsemblBacteria; BAC51923; BAC51923; BAC51923. DR GeneID; 1054201; -. DR KEGG; bja:blr6658; -. DR PATRIC; 21197168; VBIBraJap65052_6818. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BJAP224911:GJEJ-6709-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 208 AA; 22498 MW; 3D75696BAD2D37E3 CRC64; MPYPDRNAYP DRFYPVVDSL AWVERLTKLG VGTIQLRAKD LNDAEALQIV TDALAITEGT QAKLVVNDYW RAAIVAGAKY LHLGQEDLAD ADLKAIREAG LSLGVSTHDD AELATALAAK PDYVALGPIF FTTLKSMRFE PQGIPKITEW KKRIGTIPLV AIGGIKFEHA AEIFAAGADS IAVVSDVTQN TDPDARVRQW LGLPAEAA // ID Q89U98_BRADU Unreviewed; 186 AA. AC Q89U98; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 60. DE SubName: Full=Bll1519 protein; GN OrderedLocusNames=bll1519; OS Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC OS 14792 / USDA 110). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=224911; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110; RX PubMed=12597275; DOI=10.1093/dnares/9.6.189; RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., RA Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., RA Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., RA Tabata S.; RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium RT Bradyrhizobium japonicum USDA110."; RL DNA Res. 9:189-197(2002). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000040; BAC46784.1; -; Genomic_DNA. DR RefSeq; NP_768159.1; NC_004463.1. DR ProteinModelPortal; Q89U98; -. DR STRING; 224911.bll1519; -. DR EnsemblBacteria; BAC46784; BAC46784; BAC46784. DR GeneID; 1055269; -. DR KEGG; bja:bll1519; -. DR PATRIC; 21186632; VBIBraJap65052_1578. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BJAP224911:GJEJ-1537-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 186 AA; 19456 MW; 9793714026E10852 CRC64; MLVRLKETDQ RTMISRIKAL APPVQKAGAA LLIDGHAELV ARGGADGAHL PGIAALKEAL PSLKPDRIAG VGGLTTRHHS MDAGEIGADY LLFGEPDAKG QRPSSEAIAE RLDWWAELFE PPCVGFATSL EEAYDFAASG ADFVLVGEFV WADPRGAKAA LIEADATIKK AHAAALASQN PAGEHG // ID Q8AA18_BACTN Unreviewed; 202 AA. AC Q8AA18; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 69. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN OrderedLocusNames=BT_0647; OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC OS 10582 / E50 / VPI-5482). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=226186; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482; RX PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., RA Chiang H.C., Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(2003). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS). RA Forouhar F., Chen Y., Seetharaman J., Janjua H., Mao L., Xiao R., RA Foote E.L., Maglaqui M., Ciccosanti C., Zhao L., Baran M.C., RA Acton T.B., Montelione G.T., Hunt J.F., Tong L.; RT "Crystal structure of thiamine phosphate pyrophosphorylase (BT_0647) RT from Bacteroides thetaiotaomicron. Northeast Structural Genomics RT Consortium target BtR268."; RL Submitted (FEB-2008) to the PDB data bank. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VPI-5482; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of RT its two dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015928; AAO75754.1; -; Genomic_DNA. DR RefSeq; NP_809560.1; NC_004663.1. DR PDB; 3CEU; X-ray; 2.30 A; A/B=1-202. DR PDBsum; 3CEU; -. DR ProteinModelPortal; Q8AA18; -. DR STRING; 226186.BT_0647; -. DR DNASU; 1072401; -. DR EnsemblBacteria; AAO75754; AAO75754; BT_0647. DR GeneID; 1072401; -. DR KEGG; bth:BT_0647; -. DR PATRIC; 21056063; VBIBacThe70966_0658. DR KO; K00788; -. DR OMA; PVFNSIS; -. DR OrthoDB; EOG6RC3V1; -. DR BioCyc; BTHE226186:GJXV-649-MONOMER; -. DR EvolutionaryTrace; Q8AA18; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. SQ SEQUENCE 202 AA; 23421 MW; 5449323C0AB043AC CRC64; MKLIVVTTPT FFVEEDKIIT ALFEEGLDIL HLRKPETPAM YSERLLTLIP EKYHRRIVTH EHFYLKEEFN LMGIHLNARN PSEPHDYAGH VSCSCHSVEE VKNRKHFYDY VFMSPIYDSI SKVNYYSTYT AEELREAQKA KIIDSKVMAL GGINEDNLLE IKDFGFGGAV VLGDLWNKFD ACLDQNYLAV IEHFKKLKKL AD // ID Q8CN32_STAES Unreviewed; 160 AA. AC Q8CN32; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 66. DE SubName: Full=Thiamine phosphate synthase; GN OrderedLocusNames=SE_2057; OS Staphylococcus epidermidis (strain ATCC 12228). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=176280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12228; RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x; RA Zhang Y.Q., Ren S.X., Li H.L., Wang Y.X., Fu G., Yang J., Qin Z.Q., RA Miao Y.G., Wang W.Y., Chen R.S., Shen Y., Chen Z., Yuan Z.H., RA Zhao G.P., Qu D., Danchin A., Wen Y.M.; RT "Genome-based analysis of virulence genes in a non-biofilm-forming RT Staphylococcus epidermidis strain (ATCC 12228)."; RL Mol. Microbiol. 49:1577-1593(2003). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015929; AAO05698.1; -; Genomic_DNA. DR RefSeq; NP_765612.1; NC_004461.1. DR ProteinModelPortal; Q8CN32; -. DR STRING; 176280.SE2057; -. DR EnsemblBacteria; AAO05698; AAO05698; SE_2057. DR GeneID; 1056015; -. DR KEGG; sep:SE2057; -. DR PATRIC; 19609980; VBIStaEpi113981_2010. DR eggNOG; COG0352; -. DR OMA; IVYKENT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SEPI176280:GCDG-2116-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 160 AA; 18192 MW; 1CF9C4416E954C53 CRC64; MNNEENKEMI QSLLQLGFSK DKIIIHSDVT LLEDLHLKRI HFKENDTTAF TYKEAHPDIC VSMSTHDVET VKRCYENGLD SVFFGHIFPT SSHPNVPPRS KEAIQQALNV PIPIYAIGGI NEHSLQKMPP GFKGICAISY FNNASLEEIK QLRKEWSTHA // ID Q8D248_WIGBR Unreviewed; 215 AA. AC Q8D248; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 79. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OS Wigglesworthia glossinidia brevipalpis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Wigglesworthia. OX NCBI_TaxID=36870; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12219091; DOI=10.1038/ng986; RA Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M., RA Aksoy S.; RT "Genome sequence of the endocellular obligate symbiont of tsetse RT flies, Wigglesworthia glossinidia."; RL Nat. Genet. 32:402-407(2002). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000021; BAC24652.1; -; Genomic_DNA. DR RefSeq; NP_871509.1; NC_004344.2. DR ProteinModelPortal; Q8D248; -. DR STRING; 36870.WGLp506; -. DR EnsemblBacteria; BAC24652; BAC24652; BAC24652. DR GeneID; 1257317; -. DR KEGG; wbr:WGLp506; -. DR PATRIC; 24025240; VBIWigGlo15804_0546. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 215 AA; 24727 MW; 86C817BC655DBC56 CRC64; MCNKIKFPII PKNIGLYPII DSLSWLVRIL SVGIKTVQIR IKEKDKINLD REIESAIILG KKYKANLFIN DYWELAVKHK AYGVHLGQKD MNNADIKYIY KSGLRLGLST RNDQEVERAL KWNPSYISFG HVFHTNTKIM KSSPQGINKL KELCNKINNC PKVAIGGIGL CQIDEVLKCK INGISMISAI TKSKDWKKTI YKIQKKIKIK LYEKY // ID Q8DDL5_VIBVU Unreviewed; 444 AA. AC Q8DDL5; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 87. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=VV1_0963; OS Vibrio vulnificus (strain CMCP6). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=216895; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CMCP6; RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., RA Choy H.E.; RT "Complete genome sequence of Vibrio vulnificus CMCP6."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016795; AAO09457.1; -; Genomic_DNA. DR RefSeq; NP_759930.1; NC_004459.3. DR ProteinModelPortal; Q8DDL5; -. DR STRING; 216895.VV1_0963; -. DR EnsemblBacteria; AAO09457; AAO09457; VV1_0963. DR GeneID; 1177900; -. DR KEGG; vvu:VV1_0963; -. DR PATRIC; 20158745; VBIVibVul94426_0929. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RIKDSTH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; VVUL216895:GIYM-889-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 444 AA; 49291 MW; 1FD0616862377568 CRC64; MRLLIPSAII ELTGEIQQCL LLAKQQGFAI DHIELGVSPT RTLQLISSAK TVVFETDLIH NDSRHLGAHD FALHYHHSLA LTEVSSYLGS ECKAKTLLIN LQGEQGEAFD VWQHPLADET RALRFLSRQN HSQNESVESI YRHLAWVVTL SALDFPIEDC LTLARAMLNV SRETWVSDFA LFPTPVLHLD EFGILPSHNL EGLTKAFPRV IAQQLGLYPV VDDVSWIEKL LPLGIKTVQL RIKDPNQVDL EQQIVRAIQL GRDYGAKVYI NDYWQLAIQY QAYGVHLGQE DLQVADLAAL TNAGIALGLS THGYYELLRI VQLQPSYIAL GHIFPTTTKQ MPSLPQGLVR LKLYQQLIDT IPYDESITGV PTVAIGGIDQ SNAATVWQCG VSSLAVVRAI TLAKDVKAVI EYFKQVMAPN TTLLRLDSVS THSLEPTSEA NHVG // ID Q8EED8_SHEON Unreviewed; 525 AA. AC Q8EED8; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 14-MAY-2014, entry version 89. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiDE; OrderedLocusNames=SO_2444; OS Shewanella oneidensis (strain MR-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-1; RX PubMed=12368813; DOI=10.1038/nbt749; RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., RA Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., RA Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., RA White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., RA Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., RA Venter J.C., Nealson K.H., Fraser C.M.; RT "Genome sequence of the dissimilatory metal ion-reducing bacterium RT Shewanella oneidensis."; RL Nat. Biotechnol. 20:1118-1123(2002). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014299; AAN55478.2; -; Genomic_DNA. DR RefSeq; NP_718034.2; NC_004347.2. DR STRING; 211586.SO_2444; -. DR EnsemblBacteria; AAN55478; AAN55478; SO_2444. DR GeneID; 1170159; -. DR KEGG; son:SO_2444; -. DR PATRIC; 23524505; VBISheOne101494_2352. DR HOGENOM; HOG000155781; -. DR KO; K14153; -. DR OMA; PIVWTIA; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; ISS:TIGR. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; ISS:TIGR. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 525 AA; 56017 MW; A2E3D7B82ABA606A CRC64; MTPTKHFNHL VPKPIVWTIA GSDSGGGAGI QADLATINDL GGHGCSVITT LTAQSSVAVD LVEPVSEAML LTQLSTLLAD LPPQAIKIGL LADQQQLQLL ADWLANFKTH YPHVPVILDP VMVASCGDEL GNRSTPLDFS RFKGLISLIT PNVKELARLT SFTDAQTIPS KMTKADFAAA AIQLAEQLGC SVLAKGGDNR FDPHLAEDLL VCHDVAGCSE LDSHGHFWLV SDRIDTVHNH GSGCTLSSAI ASVLAFGFVL HDAIVVAKAY VNQGLTHARG LGHGPGPLAR TTWPHSLLQY PKIVAVCADK QPQPYAFKRL TTDLGVYPVV NNLLLLEQLL AAGVKTIQLR VKSDAGITAA ELEAQIQTAI ALGKHYDAQL FINDHWQLAI KHGAFGVHLG QEDLAMADLN AIHGAGLALG ISSHSYFELL RAHQHAPSYI ALGHIFPTTT KQMPSAPQGL FKLAHYVELL KAYYPLVAIG GIGPSNLDQV NATGVRNIAV VRAITEADDP IAALAELTRA WEQGR // ID Q8F4P9_LEPIN Unreviewed; 214 AA. AC Q8F4P9; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 70. DE SubName: Full=Thiamine phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=LA_1991; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai OS (strain 56601). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=189518; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=56601; RX PubMed=12712204; DOI=10.1038/nature01597; RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., RA Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., RA Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., RA Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., RA Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., RA Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., RA Xu J.-G., Zhao G.-P.; RT "Unique physiological and pathogenic features of Leptospira RT interrogans revealed by whole-genome sequencing."; RL Nature 422:888-893(2003). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE010300; AAN49190.1; -; Genomic_DNA. DR RefSeq; NP_712172.1; NC_004342.2. DR ProteinModelPortal; Q8F4P9; -. DR STRING; 189518.LA1991; -. DR EnsemblBacteria; AAN49190; AAN49190; LA_1991. DR GeneID; 1151334; -. DR KEGG; lil:LA_1991; -. DR PATRIC; 22384827; VBILepInt91350_1986. DR HOGENOM; HOG000117684; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6WX4T9; -. DR BioCyc; LINT189518:GJBB-1603-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 214 AA; 24559 MW; 214912E2D1840FBC CRC64; MRANSFPWRV PGIYPILDLD FCKSRNLDYF SLPKFWIEYP DLIPFIQIRA KSASINELEF IVKSLQDLYP DLFWIVNDFW KQAIEWNCFG AHVGKEDYEA LNLEERNTLF KSKLYLGTSS HTLEEVSELD SSLWNYTGLG PIFPTENKED AKSAIGTKTL NKIKNGNYLP VTVIGGIKVE NLDLILKEGS FLISSISMAC LENEFRTAAT KLRK // ID Q8FYZ8_BRUSU Unreviewed; 221 AA. AC Q8FYZ8; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 66. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=BR1707, BS1330_I1701; OS Brucella suis biovar 1 (strain 1330). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=204722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=12271122; DOI=10.1073/pnas.192319099; RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., RA Read T.D., Dodson R.J., Umayam L., Brinkac L.M., Beanan M.J., RA Daugherty S.C., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J., Van Aken S.E., RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.; RT "The Brucella suis genome reveals fundamental similarities between RT animal and plant pathogens and symbionts."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1330; RA Paulsen I., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., RA Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., RA Salzberg S.L., Hoover D.L., Lindler L., Halling S.M., Boyle S.M., RA Fraser C.M.; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=22038969; DOI=10.1128/JB.06181-11; RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.; RT "Revised genome sequence of Brucella suis 1330."; RL J. Bacteriol. 193:6410-6410(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014291; AAN30607.1; -; Genomic_DNA. DR EMBL; CP002997; AEM19024.1; -; Genomic_DNA. DR PIR; AC3293; AC3293. DR RefSeq; NP_698692.1; NC_004310.3. DR RefSeq; YP_005616516.1; NC_017251.1. DR STRING; 204722.BR1707; -. DR EnsemblBacteria; AAN30607; AAN30607; BR1707. DR EnsemblBacteria; AEM19024; AEM19024; BS1330_I1701. DR GeneID; 1167400; -. DR GeneID; 12137471; -. DR KEGG; bms:BR1707; -. DR KEGG; bsi:BS1330_I1701; -. DR PATRIC; 17791802; VBIBruSui107850_1734. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID Q8G2V0_BRUSU Unreviewed; 203 AA. AC Q8G2V0; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 72. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=BR0214, BS1330_I0214; OS Brucella suis biovar 1 (strain 1330). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=204722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=12271122; DOI=10.1073/pnas.192319099; RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., RA Read T.D., Dodson R.J., Umayam L., Brinkac L.M., Beanan M.J., RA Daugherty S.C., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J., Van Aken S.E., RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.; RT "The Brucella suis genome reveals fundamental similarities between RT animal and plant pathogens and symbionts."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1330; RA Paulsen I., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., RA Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., RA Salzberg S.L., Hoover D.L., Lindler L., Halling S.M., Boyle S.M., RA Fraser C.M.; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=22038969; DOI=10.1128/JB.06181-11; RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.; RT "Revised genome sequence of Brucella suis 1330."; RL J. Bacteriol. 193:6410-6410(2011). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014291; AAN29163.1; -; Genomic_DNA. DR EMBL; CP002997; AEM17575.1; -; Genomic_DNA. DR PIR; AB3469; AB3469. DR RefSeq; NP_697248.1; NC_004310.3. DR RefSeq; YP_005615067.1; NC_017251.1. DR STRING; 204722.BR0214; -. DR EnsemblBacteria; AAN29163; AAN29163; BR0214. DR EnsemblBacteria; AEM17575; AEM17575; BS1330_I0214. DR GeneID; 1165872; -. DR GeneID; 12138756; -. DR KEGG; bms:BR0214; -. DR KEGG; bsi:BS1330_I0214; -. DR PATRIC; 17788697; VBIBruSui107850_0220. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID Q8KD80_CHLTE Unreviewed; 218 AA. AC Q8KD80; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 14-MAY-2014, entry version 64. DE SubName: Full=Thiamine-phosphate pyrophosphorylase, putative; GN OrderedLocusNames=CT1174; OS Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=194439; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49652 / DSM 12025 / TLS; RX PubMed=12093901; DOI=10.1073/pnas.132181499; RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., RA Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., RA Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., RA Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P., RA Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., RA Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., RA Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.; RT "The complete genome sequence of Chlorobium tepidum TLS, a RT photosynthetic, anaerobic, green-sulfur bacterium."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE006470; AAM72407.1; -; Genomic_DNA. DR RefSeq; NP_662065.1; NC_002932.3. DR ProteinModelPortal; Q8KD80; -. DR STRING; 194439.CT1174; -. DR EnsemblBacteria; AAM72407; AAM72407; CT1174. DR GeneID; 1006538; -. DR KEGG; cte:CT1174; -. DR PATRIC; 21400315; VBIChlTep116050_1069. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FGPPQGL; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CTEP194439:GHN0-1206-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 218 AA; 23437 MW; F8F069EBF48E92BA CRC64; MPEIAFMTEK HPSLPRLMIV SSGGEHFSQK GLVLAQAQTL ARSAPVIFQV REKMLDSASM WRLCSQIAPL VDNSGSILTI NERFDIALAS KAGGVHLPES SCPADVVRKT ARKLLVGQSV HSETTALKAA STGLDYLLFG PVFHTPSKAS FGPPQGLDRL REICEKVRIP VFAVGGITPE KVPACIECGA WGVAALTPFL DAGSLPETVN RFYSFMQS // ID Q8KJ34_RHILI Unreviewed; 201 AA. AC Q8KJ34; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 16-OCT-2013, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OS Rhizobium loti (Mesorhizobium loti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=381; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R7A; RX PubMed=12003951; DOI=10.1128/JB.184.11.3086-3095.2002; RA Sullivan J.T., Trzebiatowski J.R., Cruickshank R.W., Gouzy J., RA Brown S.D., Elliot R.M., Fleetwood D.J., McCallum N.G., Rossbach U., RA Stuart G.S., Weaver J.E., Webby R.J., de Bruijn F.J., Ronson C.W.; RT "Comparative sequence analysis of the symbiosis island of RT Mesorhizobium loti strain R7A."; RL J. Bacteriol. 184:3086-3095(2002). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL672115; CAD31249.1; -; Genomic_DNA. DR ProteinModelPortal; Q8KJ34; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22547 MW; E4CE6585BB36508D CRC64; MKLDPFYLIV DSAAWIERLV PLGVKLVQLR IKTMDEAGLR AEIRKAKALC AQNRCQLIVN DHWRLAIEEG CDFVHLGQED LQTADRSRIR VAGVRLGLST HDDIELETAM AAGPDYIALG PIYPTILKTM KWAPQGLERI SEWKRRVAPI PLVAIGGLNP DRLNGVFAAD ADSAAVVTDI TLNADPEART REWIEKTERW R // ID Q8NNY9_CORGL Unreviewed; 221 AA. AC Q8NNY9; Q6M418; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 14-MAY-2014, entry version 85. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=cg2236, Cgl2038; OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / OS LMG 3730 / NCIMB 10025). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196627; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Nakagawa S.; RT "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1; RA Ikeda M., Nakagawa S.; RT "The Corynebacterium glutamicum genome: features and impacts on RT biotechnological processes."; RL Appl. Microbiol. Biotechnol. 62:99-109(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., RA Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence RT and its impact on the production of L-aspartate-derived amino acids RT and vitamins."; RL J. Biotechnol. 104:5-25(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000036; BAB99431.1; -; Genomic_DNA. DR EMBL; BX927154; CAF20377.1; -; Genomic_DNA. DR RefSeq; NP_601242.1; NC_003450.3. DR RefSeq; YP_226278.1; NC_006958.1. DR ProteinModelPortal; Q8NNY9; -. DR STRING; 196627.cg2236; -. DR DNASU; 1019993; -. DR EnsemblBacteria; BAB99431; BAB99431; BAB99431. DR EnsemblBacteria; CAF20377; CAF20377; cg2236. DR GeneID; 1019993; -. DR GeneID; 3344856; -. DR KEGG; cgb:cg2236; -. DR KEGG; cgl:NCgl1961; -. DR PATRIC; 21496078; VBICorGlu203724_1975. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6PZXB0; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). SQ SEQUENCE 221 AA; 23130 MW; 4CFA0D0666F50FFC CRC64; MFENRFDLRC YVVTGAGSVD EVVHTASAAA RGGAGVVQVR SKPISPEAMR ELASKVALEV ARCSPTTRVL IDDHLHVASS LMREGLPIHG VHLGQDDMSV LEARELLGPE AIIGLTTGTL ELVAAANELS DVLDYIGAGP FRKTPTKDSG RPPIGLAGYP PLVELSKVPI VAIGDVTPAD VRALSATGVA GVAMVRAFSE SDDPQQVAEN VVANFELGRL S // ID Q8PCJ0_XANCP Unreviewed; 315 AA. AC Q8PCJ0; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 14-MAY-2014, entry version 83. DE SubName: Full=Bifunctional DGTP-pyrophosphohydrolase/thiamine phosphate synthase; GN OrderedLocusNames=XCC0736; OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / OS LMG 568). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190485; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / NCPPB 528 / LMG 568; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008922; AAM40051.1; -; Genomic_DNA. DR RefSeq; NP_636127.1; NC_003902.1. DR ProteinModelPortal; Q8PCJ0; -. DR STRING; 190485.XCC0736; -. DR EnsemblBacteria; AAM40051; AAM40051; XCC0736. DR GeneID; 998171; -. DR KEGG; xcc:XCC0736; -. DR PATRIC; 24072132; VBIXanCam115730_0801. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XCAM190485:GIXZ-735-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Reference proteome. SQ SEQUENCE 315 AA; 34550 MW; 9C6B29D3BC9C10E2 CRC64; MPDSLRSIHV VAGVITDARG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIDAHVGA WVMDVPQLYP DKRLRLEVRE ITGWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGVL RQPDRYLITP EPQNDAAWLD GVEQALQQEI ARIQLRAPAV DPARWRALVH QVMGLRGRQR AQWLLNRDIG LASELGIGVH LGSEQLATLT ERPLPADQPV AASCHGLEDL RHAQRLGCDF AVLGPVQATA SHPGATPLGW EGFETLREQV SLPIYALGGM QPGDVREARA HGAQGIAAIR GLWPA // ID Q8PP99_XANAC Unreviewed; 315 AA. AC Q8PP99; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 14-MAY-2014, entry version 81. DE SubName: Full=DGTP-pyrophosphohydrolase; GN OrderedLocusNames=XAC0789; OS Xanthomonas axonopodis pv. citri (strain 306). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190486; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008923; AAM35677.1; -; Genomic_DNA. DR RefSeq; NP_641141.1; NC_003919.1. DR ProteinModelPortal; Q8PP99; -. DR STRING; 190486.XAC0789; -. DR EnsemblBacteria; AAM35677; AAM35677; XAC0789. DR GeneID; 1154860; -. DR KEGG; xac:XAC0789; -. DR PATRIC; 24053500; VBIXanAxo33670_0849. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XAXO190486:GH55-789-MONOMER; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 315 AA; 34843 MW; 57641CE349DDD9A9 CRC64; MPDSLRSIHV VAGVVTDPRG RILLTRRTET RDMPGLWEFP GGKREPGETS EQALVRELNE ELGIEAQVGD WVMDVPQLYP DKRLRLEVRH ITSWKGSPRG REGQAMTWVA ADKLARYSMP PADVPVVGAL RQPDRYLITP DPEDDARWLE SLELALQNGI TRIQLRARQL APARWQALLQ QVMRLRGRAR AQLLLNRDIA LAADLGIGVH LGSEQLAGLQ ERPLPAEQLV AASCHGLDDL RHAQRIGCDF AVLGPVQATA SHPGATPIGW DGFETLREQV SLPIYALGGM QVEDVRQARS HGAQGIAAIR ALWPQ // ID Q8RI65_FUSNN Unreviewed; 206 AA. AC Q8RI65; DT 01-JUN-2002, integrated into UniProtKB/TrEMBL. DT 01-JUN-2002, sequence version 1. DT 13-NOV-2013, entry version 68. DE SubName: Full=Regulatory protein TENI; GN OrderedLocusNames=FN1752; OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP OS 101130 / JCM 8532 / LMG 13131). OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=190304; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131; RX PubMed=11889109; DOI=10.1128/JB.184.7.2005-2018.2002; RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A., RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., RA Vasieva O., Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., RA Larsen N., D'Souza M., Walunas T., Pusch G., Haselkorn R., RA Fonstein M., Kyrpides N.C., Overbeek R.; RT "Genome sequence and analysis of the oral bacterium Fusobacterium RT nucleatum strain ATCC 25586."; RL J. Bacteriol. 184:2005-2018(2002). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE009951; AAL93867.1; -; Genomic_DNA. DR RefSeq; NP_602568.1; NC_003454.1. DR ProteinModelPortal; Q8RI65; -. DR STRING; 190304.FN1752; -. DR EnsemblBacteria; AAL93867; AAL93867; FN1752. DR GeneID; 992635; -. DR KEGG; fnu:FN1752; -. DR PATRIC; 21949021; VBIFusNuc122357_0241. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 206 AA; 24009 MW; 9DC3F67648C14DE5 CRC64; MIENKIKLNI ITNRKLCENE NLEKQIEKIF SAYKRKIILE DFEIVALTLR EKDLDKNEYL KLVEKIYPIC QKYRIDLILH QNYDLNLDEK YNIGGIHLSY EIFKSLNKNI REELIKKYKK IGVSIHSIDE AKEVEMLGAT YIVAGHIFET DCKKDLEPRG LKFIQELSST LTIPIFVIGG MNQENSHLVI NSGAFGVCMM SSLMRY // ID Q8XK04_CLOPE Unreviewed; 193 AA. AC Q8XK04; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 14-MAY-2014, entry version 66. DE SubName: Full=Thiamin phosphate pyrophosphorylase; GN Name=thiE; OS Clostridium perfringens (strain 13 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195102; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13 / Type A; RX PubMed=11792842; DOI=10.1073/pnas.022493799; RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., RA Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.; RT "Complete genome sequence of Clostridium perfringens, an anaerobic RT flesh-eater."; RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000016; BAB81305.1; -; Genomic_DNA. DR RefSeq; NP_562515.1; NC_003366.1. DR ProteinModelPortal; Q8XK04; -. DR STRING; 195102.CPE1599; -. DR EnsemblBacteria; BAB81305; BAB81305; BAB81305. DR GeneID; 989909; -. DR KEGG; cpe:CPE1599; -. DR PATRIC; 19497149; VBICloPer59675_1670. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPER195102:GJFM-1645-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 193 AA; 21926 MW; 8CC9E04BA3A0ECB5 CRC64; MFLITNRKLV NRERYFNTIE EAGKYGVKNI ILREKDLSTE ELIEVYIKIK ELVPEETNII INSNIEATRI LKEKFIHLSF KDFKKNLEEV KSLQVGVSVH SILEAIEADR LGASYILVSP IFETQCKKGV TPKGINFIKE IKEKVNCKVI ALGGINEHNF KEVLGAGADD FACMSLLFMS NNIKKSLDTF KAL // ID Q8XR75_RALSO Unreviewed; 198 AA. AC Q8XR75; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 14-MAY-2014, entry version 72. DE SubName: Full=Putative thiamine-phosphate pyrophosphorylase protein; DE EC=2.5.1.3; GN Name=thiE2; OrderedLocusNames=RSp0984; OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum). OG Plasmid megaplasmid Rsp. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=267608; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GMI1000; RX PubMed=11823852; DOI=10.1038/415497a; RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., RA Arlat M., Billault A., Brottier P., Camus J.-C., Cattolico L., RA Chandler M., Choisne N., Claudel-Renard C., Cunnac S., Demange N., RA Gaspin C., Lavie M., Moisan A., Robert C., Saurin W., Schiex T., RA Siguier P., Thebault P., Whalen M., Wincker P., Levy M., RA Weissenbach J., Boucher C.A.; RT "Genome sequence of the plant pathogen Ralstonia solanacearum."; RL Nature 415:497-502(2002). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL646053; CAD18135.1; -; Genomic_DNA. DR RefSeq; NP_522545.1; NC_003296.1. DR ProteinModelPortal; Q8XR75; -. DR STRING; 267608.RSp0984; -. DR EnsemblBacteria; CAD18135; CAD18135; RSp0984. DR GeneID; 1223296; -. DR KEGG; rso:RSp0984; -. DR PATRIC; 20267589; VBIRalSol70888_4462. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RSOL267608:GCVU-4493-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 198 AA; 21566 MW; C623C333B7715BD0 CRC64; MRSVSLPDFY QVTPEPAGSP NFEPFFAELT DTLRSGVRLL QLRAKRLDSR EHLAVAQRTR DLCRQFGTIL MLNGPIDMAR EAGCDGVHLS SDALMSLRSR PVPETMLVSA ACHSAEQLEQ AARMAVDFVT LSPVLPTRTH PEADPLGWER FAALVQGARI PVFALGGMRP DMLDQAKQAG AWGIAAISAT WRRPSAGG // ID Q8Y373_RALSO Unreviewed; 383 AA. AC Q8Y373; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 14-MAY-2014, entry version 66. DE SubName: Full=Probable thiamine-phosphate pyrophosphorylase protein; DE EC=2.5.1.3; GN Name=thiE1; OrderedLocusNames=RSc0108; OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=267608; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GMI1000; RX PubMed=11823852; DOI=10.1038/415497a; RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., RA Arlat M., Billault A., Brottier P., Camus J.-C., Cattolico L., RA Chandler M., Choisne N., Claudel-Renard C., Cunnac S., Demange N., RA Gaspin C., Lavie M., Moisan A., Robert C., Saurin W., Schiex T., RA Siguier P., Thebault P., Whalen M., Wincker P., Levy M., RA Weissenbach J., Boucher C.A.; RT "Genome sequence of the plant pathogen Ralstonia solanacearum."; RL Nature 415:497-502(2002). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL646052; CAD13636.1; -; Genomic_DNA. DR RefSeq; NP_518229.1; NC_003295.1. DR ProteinModelPortal; Q8Y373; -. DR STRING; 267608.RSc0108; -. DR EnsemblBacteria; CAD13636; CAD13636; RSc0108. DR GeneID; 1218911; -. DR KEGG; rso:RSc0108; -. DR PATRIC; 20258753; VBIRalSol70888_0111. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INDHWQI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; RSOL267608:GCVU-109-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 383 AA; 40037 MW; 12978CCB6EEA5E8F CRC64; MSASALRFAS AWPDAAALAD RLIDRHADAF GRAPHAWSVT DRADDAATAA VLLTTDAAQA ERARAAGAAV VLSEARNGER IDTVHDRLGT YRFAAPATGA VFGERFVAMF GAALALAFEP RDALCVARAW IAEAAADALA WPARFDALPR VLEPALPCAA SPDLAFAPCP PRLGVYAVVP DAEWVERLVA LKVPTVQLRV KSDDARAVAG QVRRAAAAAR GSQTRLFIND HWRVALDVHA QTPDSGLYGI HLGQEDIDDA DLAAIRASGL RLGISTHGYA EMLRVAALNP SYLALGAVFA TPTKTMPTLP QGLGRLFAHA AAMRSRVPAP PLVAIGGIDL AAMPRVLESG VGGVAVVRAI TQAEDVPAAV QALQATFAAH ARA // ID Q8YEZ1_BRUME Unreviewed; 203 AA. AC Q8YEZ1; D0B4R5; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 14-MAY-2014, entry version 82. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BMEI1736; ORFNames=BAWG_0497; OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=224914; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=16M; RA Letesson J.-J.; RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16M, and 16M / ATCC 23456 / NCTC 10094; RX PubMed=11756688; DOI=10.1073/pnas.221575398; RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.J., RA Haselkorn R., Kyrpides N., Overbeek R.; RT "The genome sequence of the facultative intracellular pathogen RT Brucella melitensis."; RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=16M; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella melitensis bv. 1 str. 16M."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008917; AAL52917.1; -; Genomic_DNA. DR EMBL; GG703778; EEW88389.1; -; Genomic_DNA. DR PIR; AB3469; AB3469. DR RefSeq; NP_540653.1; NC_003317.1. DR STRING; 224914.BMEI1736; -. DR EnsemblBacteria; AAL52917; AAL52917; BMEI1736. DR EnsemblBacteria; EEW88389; EEW88389; BAWG_0497. DR GeneID; 1197447; -. DR KEGG; bme:BMEI1736; -. DR PATRIC; 17796449; VBIBruMel146950_0048. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HIANIQK; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; BMEL224914:GCJ0-1781-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 203 AA; 22314 MW; C7935C980EB2999A CRC64; MTALDPFYPI FDSADWLERM VPLGIRLVQL RVKDKADAQL RAEIRAARDI CAAHDCQLIV NDYWKLALDE GCDFIHLGQE DLDGADLDAI RAGGLKLGVS SHDEAELDRA LSVRPDYIAL GPIYPTILKK MKWHEQGLPR LGEWKARIGN IPLVGIGGLS VERAPGVFAA GADIVSVVTD ITLHADPAAR VREWIAVTRP FVA // ID Q8YIW0_BRUME Unreviewed; 221 AA. AC Q8YIW0; D0BA84; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 14-MAY-2014, entry version 78. DE SubName: Full=Thiamin-phosphate pyrophosphorylase; DE EC=2.5.1.3; DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=BMEI0329; ORFNames=BAWG_3005; OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=224914; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=16M; RA Letesson J.-J.; RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16M, and 16M / ATCC 23456 / NCTC 10094; RX PubMed=11756688; DOI=10.1073/pnas.221575398; RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.J., RA Haselkorn R., Kyrpides N., Overbeek R.; RT "The genome sequence of the facultative intracellular pathogen RT Brucella melitensis."; RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=16M; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., RA Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Brucella melitensis bv. 1 str. 16M."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008917; AAL51510.1; -; Genomic_DNA. DR EMBL; GG703781; EEW86260.1; -; Genomic_DNA. DR PIR; AC3293; AC3293. DR RefSeq; NP_539246.1; NC_003317.1. DR STRING; 224914.BMEI0329; -. DR EnsemblBacteria; AAL51510; AAL51510; BMEI0329. DR EnsemblBacteria; EEW86260; EEW86260; BAWG_3005. DR GeneID; 1196040; -. DR KEGG; bme:BMEI0329; -. DR PATRIC; 17802309; VBIBruMel146950_3471. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; BMEL224914:GCJ0-339-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 221 AA; 23260 MW; 9E922D59975AD087 CRC64; MNTRAPQTEP ERCRIVLVAP PIADGAALAK LLTAALSGGD VASVILDTGD LDEATFQAVA EKTVPVIQEK GVAALILNDT RIAGRVGADG IHIEGKPADL AEAIEKHAPK MIVGTGNLRD RHGAMEVGEL QPDYLFFGKI GADNKPDAHP RNLSLAGWWA EMVEIPCIAQ AGSALESIVR AAETGADFVA LGRAVFDAQD PAEAVAQANR LLDEKAPRFE N // ID Q92M70_RHIME Unreviewed; 217 AA. AC Q92M70; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 14-MAY-2014, entry version 66. DE SubName: Full=Probable thiamine-phosphate pyrophosphorylase; DE EC=2.5.1.3; GN Name=thiE2; OrderedLocusNames=R02780; ORFNames=SMc03996; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11481430; DOI=10.1073/pnas.161294398; RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., RA Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., RA Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.; RT "Analysis of the chromosome sequence of the legume symbiont RT Sinorhizobium meliloti strain 1021."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11474104; DOI=10.1126/science.1060966; RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., RA Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., RA Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., RA Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., RA Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., RA Ramsperger U., Surzycki R., Thebault P., Vandenbol M., RA Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.; RT "The composite genome of the legume symbiont Sinorhizobium meliloti."; RL Science 293:668-672(2001). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL591688; CAC47359.1; -; Genomic_DNA. DR RefSeq; NP_386886.1; NC_003047.1. DR ProteinModelPortal; Q92M70; -. DR STRING; 266834.SMc03996; -. DR EnsemblBacteria; CAC47359; CAC47359; SMc03996. DR GeneID; 1234456; -. DR KEGG; sme:SMc03996; -. DR PATRIC; 23635123; VBISinMel96828_4292. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; SMEL266834:GJF6-2847-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Transferase. SQ SEQUENCE 217 AA; 22682 MW; 219C4A7B75DEEA83 CRC64; MSNIEDRCRL VLVVPDIADS AERARLVGEA LKGGDVASVI VPQYALSDAD FQKHAEALVP VIQQAGAAAL IEGDTRVAGR AKADGLHIAG GPDALADAIE RHAPKLIVGG GNATDRHHAL EIGELRPDYV FFGRTDGDIK PEAHPKNLAL AEWWASMIEI PCIVMGGTDP QSALAVAETG AEFVALRLAV FGEAGQAPSV VAAVNALLDE KAPRFEG // ID Q92TI7_RHIME Unreviewed; 201 AA. AC Q92TI7; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 14-MAY-2014, entry version 90. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; ORFNames=SM_b20618; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OG Plasmid pSymB. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; PLASMID=pSymB; RX PubMed=11481431; DOI=10.1073/pnas.161294698; RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., RA Vorhoelter F.J., Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., RA Golding B., Puehler A.; RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2- RT fixing endosymbiont Sinorhizobium meliloti."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11474104; DOI=10.1126/science.1060966; RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., RA Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., RA Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., RA Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., RA Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., RA Ramsperger U., Surzycki R., Thebault P., Vandenbol M., RA Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.; RT "The composite genome of the legume symbiont Sinorhizobium meliloti."; RL Science 293:668-672(2001). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL591985; CAC49930.1; -; Genomic_DNA. DR PIR; B96033; B96033. DR RefSeq; NP_438070.1; NC_003078.1. DR ProteinModelPortal; Q92TI7; -. DR STRING; 266834.SM_b20618; -. DR EnsemblBacteria; CAC49930; CAC49930; SM_b20618. DR GeneID; 1237862; -. DR KEGG; sme:SM_b20618; -. DR PATRIC; 23639472; VBISinMel96828_6456. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SMEL266834:GJF6-4963-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Plasmid; Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22633 MW; B34924F53ABED61A CRC64; MKLDPFYLIV DSAQWIERLV PLGVKLVQLR IKDRNEEDIR HQIRVARTVC SAHACQLIVN DYWQLAIEEA CDFIHLGQED LAEADLAAIR AAGLKLGVST HDEAELAKAL AAEPDYVALG PIYPTILKKM KWAPQGLERL SWWRERVHPL PLVAIGGLNT ERIEGVFAHG ADSAAVVTDI TLNADPEGRT REWIRKTEAW R // ID Q93CY7_LACSK Unreviewed; 66 AA. AC Q93CY7; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 16-OCT-2013, entry version 28. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; DE Flags: Fragment; GN Name=thiE; OS Lactobacillus sakei. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1599; RN [1] RP NUCLEOTIDE SEQUENCE. RA Dudez A.-M., Chaillou S., Zagorec M.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RX PubMed=11832506; RA Dudez A.-M., Chaillou S., Hissler L., Stentz R., RA Champomier-Verges M.-C., Alpert C.-A., Zagorec M.; RT "Physical and genetic map of the Lactobacillus sakei 23K chromosome."; RL Microbiology 148:421-431(2002). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF401659; AAL00938.1; -; Genomic_DNA. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; FT NON_TER 66 66 SQ SEQUENCE 66 AA; 7290 MW; 3F48D2F4EA812435 CRC64; MTNIAQEILQ TYLVAGTQDT GRENFLPILD QALQAGITCF QFRDKGPNSL PTDAMRSDYA KKAQAL // ID Q97F34_CLOAB Unreviewed; 195 AA. AC Q97F34; DT 01-OCT-2001, integrated into UniProtKB/TrEMBL. DT 01-OCT-2001, sequence version 1. DT 11-DEC-2013, entry version 72. DE SubName: Full=Thiamine monophosphate synthase; GN Name=tenI; OrderedLocusNames=CA_C2920; OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG OS 5710 / VKM B-1787). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., RA Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., RA Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., RA Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE001437; AAK80862.1; -; Genomic_DNA. DR PIR; C97259; C97259. DR RefSeq; NP_349522.1; NC_003030.1. DR ProteinModelPortal; Q97F34; -. DR STRING; 272562.CA_C2920; -. DR EnsemblBacteria; AAK80862; AAK80862; CA_C2920. DR GeneID; 1119103; -. DR KEGG; cac:CA_C2920; -. DR PATRIC; 32040251; VBICloAce74127_3104. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AGHIFET; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CACE272562:GJIH-3003-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 195 AA; 21204 MW; A665BB197818F6B9 CRC64; MIYVVTNRKL AKNKDLLGCV EKVLKYGACS VILREKDLGY DELYEIAKKI KFITDKHSAK LIVNGSLRVA EEVKAYAYHS SFVNFINNGG SKIIKNGVSI HSLEEAKRAE ENGADYVLAG NIYETACKPG LKGRGLEFVN SISKNITIPE IAIGGISEEN VQELINSGAN GAAVMSSAMK NPAVIKKIIG KLNKK // ID Q98AZ7_RHILO Unreviewed; 201 AA. AC Q98AZ7; DT 01-OCT-2001, integrated into UniProtKB/TrEMBL. DT 01-OCT-2001, sequence version 1. DT 14-MAY-2014, entry version 88. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=mll5789; OS Rhizobium loti (strain MAFF303099) (Mesorhizobium loti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=266835; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF303099; RX PubMed=11214968; DOI=10.1093/dnares/7.6.331; RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium RT Mesorhizobium loti."; RL DNA Res. 7:331-338(2000). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000012; BAB52175.1; -; Genomic_DNA. DR RefSeq; NP_106389.1; NC_002678.2. DR ProteinModelPortal; Q98AZ7; -. DR STRING; 266835.mll5789; -. DR EnsemblBacteria; BAB52175; BAB52175; BAB52175. DR GeneID; 1229048; -. DR KEGG; mlo:mll5789; -. DR PATRIC; 22483452; VBIMesLot2464_4605. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; MLOT266835:GJ9L-4539-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Thiamine biosynthesis; Transferase. SQ SEQUENCE 201 AA; 22656 MW; 82A5E4344242B900 CRC64; MKLDPFYLIV DSAAWIERLL PLGVKLVQLR IKTKDEAGLR AEIRKATALC AEHQSQLIVN DHWRLAIEEG CNFVHLGQED LQTADRARIR AAGVRLGLST HDHVELETAL FAEPDYIALG PIYPTILKKM KWAPQGLKRI REWKRRVAPV PLVAIGGLNP DRLDGVFAAG VDSAAVVTDI TLNADPEART REWIEKTERW R // ID Q98F64_RHILO Unreviewed; 231 AA. AC Q98F64; DT 01-OCT-2001, integrated into UniProtKB/TrEMBL. DT 01-OCT-2001, sequence version 1. DT 14-MAY-2014, entry version 63. DE SubName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=mlr3913; OS Rhizobium loti (strain MAFF303099) (Mesorhizobium loti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=266835; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF303099; RX PubMed=11214968; DOI=10.1093/dnares/7.6.331; RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium RT Mesorhizobium loti."; RL DNA Res. 7:331-338(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000012; BAB50703.1; -; Genomic_DNA. DR RefSeq; NP_104917.1; NC_002678.2. DR ProteinModelPortal; Q98F64; -. DR STRING; 266835.mlr3913; -. DR EnsemblBacteria; BAB50703; BAB50703; BAB50703. DR GeneID; 1227578; -. DR KEGG; mlo:mlr3913; -. DR PATRIC; 22480449; VBIMesLot2464_3113. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PDYIFFG; -. DR OrthoDB; EOG6W19KR; -. DR BioCyc; MLOT266835:GJ9L-3059-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome. SQ SEQUENCE 231 AA; 24475 MW; B30D49A8D28064D9 CRC64; MQPSSPGIGE TRDRRTMNDA TPPNRCRIVL IAPPGVPAAR IATAFDGGDV ASLILPENGM DEASFQAFAE QIVPTAQAAG VAVIIAGDTR IAGRVQADGI HVETSKAELA ETIEHFQAKM MVGAGGAKKR DDALELGEVR PDYIFFGRFG YDNKPEPHPR NLSLGEWWAQ MIQIPCIVMA GSDLASVEEV AATGAEFVAL SSAVFADGVD PKTAVARANA LLDETAPRFE D // ID Q9A220_CAUCR Unreviewed; 182 AA. AC Q9A220; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 14-MAY-2014, entry version 66. DE SubName: Full=Uncharacterized protein; GN OrderedLocusNames=CC_3746; OS Caulobacter crescentus (strain ATCC 19089 / CB15). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=190650; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19089 / CB15; RX PubMed=11259647; DOI=10.1073/pnas.061029298; RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R., RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., RA Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J., RA Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J., RA Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L., RA Fraser C.M.; RT "Complete genome sequence of Caulobacter crescentus."; RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE005673; AAK25708.1; -; Genomic_DNA. DR PIR; H87713; H87713. DR RefSeq; NP_422540.1; NC_002696.2. DR ProteinModelPortal; Q9A220; -. DR SMR; Q9A220; 5-180. DR EnsemblBacteria; AAK25708; AAK25708; CC_3746. DR GeneID; 940596; -. DR KEGG; ccr:CC_3746; -. DR PATRIC; 21304530; VBICauCre124313_3748. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; INERSDI; -. DR OrthoDB; EOG699751; -. DR BioCyc; CAULO:CC3746-MONOMER; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. SQ SEQUENCE 182 AA; 18913 MW; 701042AB09D5118B CRC64; MALPRLLFFT DPARITDPEA VAERLPPGSA IVFRAFGATD AVEQGRRLRA IATARDLMLL VGAHAGLAEG VGADGVHLPE RMAANLPRLR AEHPRYLVTV AAHDLAAVQT AERSGADAVV VSPVFPSNSP SAGEPLGLEG LMRLVEATAL PVYALGGVRA HTVDQLFDSG VAGIAAVEAL AR // ID Q9A3E0_CAUCR Unreviewed; 214 AA. AC Q9A3E0; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 14-MAY-2014, entry version 88. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OrderedLocusNames=CC_3264; OS Caulobacter crescentus (strain ATCC 19089 / CB15). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=190650; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19089 / CB15; RX PubMed=11259647; DOI=10.1073/pnas.061029298; RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R., RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., RA Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J., RA Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J., RA Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L., RA Fraser C.M.; RT "Complete genome sequence of Caulobacter crescentus."; RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE005673; AAK25226.1; -; Genomic_DNA. DR PIR; F87653; F87653. DR RefSeq; NP_422058.1; NC_002696.2. DR ProteinModelPortal; Q9A3E0; -. DR SMR; Q9A3E0; 27-198. DR EnsemblBacteria; AAK25226; AAK25226; CC_3264. DR GeneID; 943818; -. DR KEGG; ccr:CC_3264; -. DR PATRIC; 21303556; VBICauCre124313_3270. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CAULO:CC3264-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22241 MW; 9C085C0B9A8C19DE CRC64; MTLDCRLYLI TPPALTDLAD FGRQLARALE GGDVAALQIR LKDAPDDLVA AAVDVLGPIA QARDVAVILN DRPDLAARLP VDGVHVGQSD MACRDARKLM GDRMVGVTCH DSRHLAMEAA EAGADYVAFG AFFPTSTKDA PTRAEPDILT IWQETMETPC VAIGGITVEN ASGLATAGAD FLAVSAGVWS YAQGPDAAVA ALNAAIAEGL AARK // ID Q9EXE8_LISMN Unreviewed; 208 AA. AC Q9EXE8; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 19-FEB-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OS Listeria monocytogenes. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1639; RN [1] RP NUCLEOTIDE SEQUENCE. RA Perehinec T.M., Hill P.J., Rees C.E.D.; RT "Characterisation of partial cytosine DNA methylation of Listeria RT monocytogenes."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ302030; CAC22273.1; -; Genomic_DNA. DR ProteinModelPortal; Q9EXE8; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21913 MW; 91665D070EBAFD9D CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAE EAERLGAVDY IGVGPIFPTI SKADAEPVSG TTILKEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC QLVIANLI // ID Q9HW06_PSEAE Unreviewed; 315 AA. AC Q9HW06; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 14-MAY-2014, entry version 79. DE SubName: Full=Probable pyrophosphohydrolase; GN OrderedLocusNames=PA4400; OS Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG OS 12228). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004091; AAG07788.1; -; Genomic_DNA. DR PIR; H83096; H83096. DR RefSeq; NP_253090.1; NC_002516.2. DR ProteinModelPortal; Q9HW06; -. DR SMR; Q9HW06; 6-123, 127-313. DR STRING; 208964.PA4400; -. DR GeneID; 881318; -. DR KEGG; pae:PA4400; -. DR PATRIC; 19843523; VBIPseAer58763_4608. DR PseudoCAP; PA4400; -. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IDA:PseudoCAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IDA:PseudoCAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Reference proteome. SQ SEQUENCE 315 AA; 34055 MW; 9165F7469596B47A CRC64; MKRVHVAAAV IRGSDGRVLI ARRPEDKHQG GLWEFPGGKV EDGEPVRAAL ARELEEELGI RVERARPLIQ VRHDYADKHV LLDVWEVDGF SGEAHGAEGQ PLAWVEPREL ADYEFPAANA PIVQAARLPA HYLITPDGLE PGELISGVRK AVEAGIRLIQ LRAPNMFSPE YRDLAIDIQG LCAGKAQLML KGPLEWLGDF PAAGWHLTSA QLRKYASAGR PFPEGRLLAA SCHDAEELAL AASMGVEFVT LSPVQPTESH PGEPALGWDK AAELIAGFNQ PVYLLGGLGP QQAEQAWEHG AQGVAGIRAF WPGGL // ID Q9KVS7_VIBCH Unreviewed; 440 AA. AC Q9KVS7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 14-MAY-2014, entry version 88. DE RecName: Full=Thiamine-phosphate synthase; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN OrderedLocusNames=VC_0062; OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=243277; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39315 / El Tor Inaba N16961; RX PubMed=10952301; DOI=10.1038/35020000; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., RA Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., RA Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I., RA Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., RA Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., RA Mekalanos J.J., Venter J.C., Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE003852; AAF93240.1; -; Genomic_DNA. DR PIR; A82369; A82369. DR RefSeq; NP_229721.1; NC_002505.1. DR ProteinModelPortal; Q9KVS7; -. DR STRING; 243277.VC0062; -. DR DNASU; 2614105; -. DR EnsemblBacteria; AAF93240; AAF93240; VC_0062. DR GeneID; 2614105; -. DR KEGG; vch:VC0062; -. DR PATRIC; 20079182; VBIVibCho83274_0060. DR KO; K00788; -. DR OMA; RIKDSTH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; VCHO:VC0062-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; ISS:TIGR. DR GO; GO:0009228; P:thiamine biosynthetic process; ISS:TIGR. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Thiamine biosynthesis; KW Transferase. SQ SEQUENCE 440 AA; 48903 MW; 0703E84D24BE83C4 CRC64; MVRLVFPRHL SALIGHVQYA LLQAKEQGVA IQHIRLDVGS EAQFILEKSE ESLRIGSSLC SQKEGFEPCD YYLDYVSENR VLPEAMMCNA RCTVTVGLHD EYGFTLDKWQ YGHAAEQLIV YPSENHRLNS KVNQHLAWVL ATLTLDFSIG DGLCIARAAI TQGDSVSRET WPTQFERFPA VQSNIRSLST QVFLTTRAFP TIDKAKFNLY PVVDDVNWIE HLLKLGVRTV QLRIKDPKQG DLEAQIIRAI ALGREFNAQV FINDHWQLAI KHQAYGVHLG QEDLTSANLT ELLDAGIRLG LSTHGYYELL IAAGIQPSYI ALGHIFPTTT KQMPSKPQGL VRLAAYQRLV NQMPYQGQHG IPTVAIGGID CRNIRDVLDC GVTAVAVVRA ITESPDPSLA VQALSSAFAD FVDAEYKLMP ASESCEPLSY LAMEVADAHR // ID Q9PEA8_XYLFA Unreviewed; 320 AA. AC Q9PEA8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 14-MAY-2014, entry version 88. DE SubName: Full=Bifunctional DGTP-pyrophosphohydrolase/thiamine phosphate synthase; GN OrderedLocusNames=XF_1120; OS Xylella fastidiosa (strain 9a5c). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=160492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9a5c; RX PubMed=10910347; DOI=10.1038/35018003; RA Simpson A.J., Reinach F.C., Arruda P., Abreu F.A., Acencio M., RA Alvarenga R., Alves L.M., Araya J.E., Baia G.S., Baptista C.S., RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R., RA Bueno M.R., Camargo A.A., Camargo L.E., Carraro D.M., Carrer H., RA Colauto N.B., Colombo C., Costa F.F., Costa M.C., Costa-Neto C.M., RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., RA Facincani A.P., Ferreira A.J., Ferreira V.C., Ferro J.A., Fraga J.S., RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., RA Goldman G.H., Goldman M.H., Gomes S.L., Gruber A., Ho P.L., RA Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., RA Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C., RA Lemos E.G., Lemos M.V., Lopes S.A., Lopes C.R., Machado J.A., RA Machado M.A., Madeira A.M., Madeira H.M., Marino C.L., Marques M.V., RA Martins E.A., Martins E.M., Matsukuma A.Y., Menck C.F., Miracca E.C., RA Miyaki C.Y., Monteriro-Vitorello C.B., Moon D.H., Nagai M.A., RA Nascimento A.L., Netto L.E., Nhani A.Jr., Nobrega F.G., Nunes L.R., RA Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., RA Paris A., Peixoto B.R., Pereira G.A., Pereira H.A.Jr., Pesquero J.B., RA Quaggio R.B., Roberto P.G., Rodrigues V., de M Rosa A.J., RA de Rosa V.E.Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., RA da Silva A.C., da Silva A.M., da Silva F.R., da Silva W.A.Jr., RA da Silveira J.F., Silvestri M.L., Siqueira W.J., de Souza A.A., RA de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., RA Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., RA Zago M.A., Zatz M., Meidanis J., Setubal J.C.; RT "The genome sequence of the plant pathogen Xylella fastidiosa."; RL Nature 406:151-159(2000). CC -!- SIMILARITY: Contains nudix hydrolase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE003849; AAF83930.1; -; Genomic_DNA. DR PIR; E82720; E82720. DR RefSeq; NP_298410.1; NC_002488.3. DR ProteinModelPortal; Q9PEA8; -. DR STRING; 160492.XF1120; -. DR EnsemblBacteria; AAF83930; AAF83930; XF_1120. DR GeneID; 1126661; -. DR KEGG; xfa:XF1120; -. DR PATRIC; 24132304; VBIXylFas578_1186. DR KO; K03574; -. DR OMA; RWLAASC; -. DR OrthoDB; EOG6W19NW; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome; Hydrolase. SQ SEQUENCE 320 AA; 35438 MW; BC8647DE49F169AB CRC64; MTDSLRSIHV VAAVIADVRG RLLLSRRTEN RDMPGLWEFP GGKREFGETS EQALARELYE ELGISADVGE WLMEVPQLYP GKRLRLEVRR VRAWKGGLRG REGQALTWVE PDKLLRYSMP PADQPVVGML RQPARYLVTP EPGKQDAEWL DAVERAYRLG IERIQLRMRQ HDPARWSGLV REAVQRRGRA HVEVLLNRDI ALAEAVGIGV HLGAEQLAVL DARPLPVGLP VGASCHCLAD LRHAQRIGCD FAVLGPVLPT ESHPGAVTLG WEGFEQLREQ VALPIYAIGG MGADQVKEAR RHGAQGIAAM RGLWPGGAKQ // ID Q9RNK2_ZYMMB Unreviewed; 238 AA. AC Q9RNK2; Q5NQP8; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 14-MAY-2014, entry version 93. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; GN Name=thiE; OS Zymomonas mobilis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=542; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZM4; RA Lee H.J., Kang H.S.; RT "Sequence analysis of 42F4 fosmid clone of Zymomonas mobilis ZM4."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF180145; AAD56925.1; -; Genomic_DNA. DR RefSeq; YP_162067.1; NC_006526.2. DR ProteinModelPortal; Q9RNK2; -. DR STRING; 264203.ZMO0332; -. DR GeneID; 3188243; -. DR KEGG; zmo:ZMO0332; -. DR PATRIC; 32566006; VBIZymMob102260_0317. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Magnesium; Metal-binding; Thiamine biosynthesis; Transferase. FT REGION 60 64 HMP-PP binding (By similarity). FT REGION 158 160 THZ-P binding (By similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 112 112 Magnesium (By similarity). FT BINDING 92 92 HMP-PP (By similarity). FT BINDING 131 131 HMP-PP (By similarity). FT BINDING 161 161 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 238 AA; 25614 MW; B79C390DBF103D9D CRC64; MAENEILTDN DEALDAFTNN YQRPSENPCG LYLISPPEID EHFVERLKKA FDGGDVSAFQ LRLKGLNEHA IARLAEPLQK VCADRDVAFI VNDSVSLAKR LGADGVHLGQ GDGDAAEARV ILGPSAQIGV TCHNSRHLAM IAGEKGADYV AFGAFYPTTS KDVRYYARPE ILSWWATLFE LPSVAIGGIT TENVAPIVKA GADFVAVCAG IWKAKEGEDK AVAHFNTVLD QAVKGEIA // ID Q9SA53_ARATH Unreviewed; 823 AA. AC Q9SA53; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 16-APR-2014, entry version 66. DE SubName: Full=F10O3.1; DE Flags: Fragment; GN Name=F10O3.1; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC006550; AAD25810.1; -; Genomic_DNA. DR PIR; G86162; G86162. DR ProteinModelPortal; Q9SA53; -. DR SMR; Q9SA53; 135-296, 385-458. DR PRIDE; Q9SA53; -. DR Genevestigator; Q9SA53; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; FT NON_TER 1 1 SQ SEQUENCE 823 AA; 91460 MW; 159A0A7A5FFE743F CRC64; MEALEHLVLW DGPIGYLRDK KTNQKHRRRY LTLSLSLSMR TLISHRQCVT SPFLISAASP PFPGRCFKLS SFTPPRHRRF SSLSIRNISH ESADQTSSSR PRTLYPGGYK RPELAVPGLL LRLDADEVMS GNREETLDLV DRALAKSVQI VVIDGGATAG KLYEAACLLK SLVKGRAYLL IAERVDIASA VGASGVALSD EGLPAIVARN TLMGSNPDSV LLPLVARIVK DVDSALIASS SEGADFLILG SGEEDTQVAD SLLKSVKIPI YVTCRGNEEA KEELQLLKSG VSGFVISLKD LRSSRDVALR QSLDGAYVVN NHETQNMNEL PEKKNSAGFI KLEDKQKLIV EMEKSVLRET IEIIHKAAPL MEEVSLLIDA VSRIDEPFLM VIVGEFNSGK STVINALLGK RYLKEGVVPT TNEITFLCYS DLESEEQQRC QTHPDGQYIN IVDTPGTNVI LQRQQRLTEE FVPRADLLVF VLSADRPLTE SEVEVTVLLG MEGKVVTRLN AYIKVAFLRY TQQWKKKFVF ILNKSDIYRD ARELEEAISF VKENTRKLLN TENVILYPVS ARSALEAKLS TASLVGRDDL EIADPGSNWR VQSFNELEKF LYSFLDSSTA TGMERIRLKL ETPMAIAERL LSSVEALVRQ DCLAAREDLA SADKIISRTK EYALKMEYES ISWRRQALSL IDNARLQVVD LIGTTLRLSS LDLAISYVFK GEKSASVAAT SKVQGEILAP ALTNAKELLG KYAEWLQSNT AREGSLSLKS FENKWPTYVN SKTQLGIDTY DLLQKTDKVS LKTIQNLSAG TTSKRLEQDI REV // ID TENI_BACSU Reviewed; 205 AA. AC P25053; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 14-MAY-2014, entry version 98. DE RecName: Full=Regulatory protein TenI; GN Name=tenI; OrderedLocusNames=BSU11660; OS Bacillus subtilis (strain 168). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1898926; RA Pang A.S.-H., Nathoo S., Wong S.-L.; RT "Cloning and characterization of a pair of novel genes that regulate RT production of extracellular enzymes in Bacillus subtilis."; RL J. Bacteriol. 173:46-54(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF APOPROTEIN. RX PubMed=15709744; DOI=10.1021/bi0478648; RA Toms A.V., Haas A.L., Park J.-H., Begley T.P., Ealick S.E.; RT "Structural characterization of the regulatory proteins TenA and TenI RT from Bacillus subtilis and identification of TenA as a thiaminase RT II."; RL Biochemistry 44:2319-2329(2005). CC -!- FUNCTION: Reduces the stimulatory effect of the TenA CC transcriptional activator on production of certain extracellular CC enzymes. Is not an essential protein, but affects the sporulation CC frequency. CC -!- PATHWAY: Cofactor metabolism; thiamine degradation [regulation]. CC -!- SUBUNIT: Dimer of dimers. CC -!- INDUCTION: Repressed by thiamine. CC -!- SIMILARITY: Belongs to the TMP-PPase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M73546; AAA22849.1; -; Genomic_DNA. DR EMBL; AL009126; CAB13023.1; -; Genomic_DNA. DR PIR; B39184; XMBSTI. DR RefSeq; NP_389048.1; NC_000964.3. DR PDB; 1YAD; X-ray; 2.10 A; A/B/C/D=1-205. DR PDB; 3QH2; X-ray; 2.23 A; A/B/C/D=1-205. DR PDBsum; 1YAD; -. DR PDBsum; 3QH2; -. DR ProteinModelPortal; P25053; -. DR SMR; P25053; 1-200. DR STRING; 224308.BSU11660; -. DR PaxDb; P25053; -. DR EnsemblBacteria; CAB13023; CAB13023; BSU11660. DR GeneID; 936411; -. DR KEGG; bsu:BSU11660; -. DR PATRIC; 18974049; VBIBacSub10457_1218. DR GenoList; BSU11660; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K10810; -. DR OMA; ELVNVAM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BSUB:BSU11660-MONOMER; -. DR BioCyc; MetaCyc:BSU11660-MONOMER; -. DR UniPathway; UPA00841; -. DR EvolutionaryTrace; P25053; -. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR GO; GO:0009230; P:thiamine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1 205 Regulatory protein TenI. FT /FTId=PRO_0000157087. FT STRAND 2 6 FT HELIX 13 23 FT HELIX 24 26 FT STRAND 28 32 FT HELIX 39 51 FT HELIX 56 58 FT STRAND 59 63 FT HELIX 65 69 FT TURN 70 72 FT STRAND 75 78 FT HELIX 85 91 FT STRAND 96 101 FT HELIX 104 112 FT STRAND 116 121 FT HELIX 136 146 FT STRAND 151 156 FT HELIX 159 161 FT HELIX 162 167 FT STRAND 171 176 FT HELIX 177 180 FT STRAND 182 184 FT HELIX 185 199 SQ SEQUENCE 205 AA; 22929 MW; B04749ED70F0A088 CRC64; MELHAITDDS KPVEELARII ITIQNEVDFI HIRERSKSAA DILKLLDLIF EGGIDKRKLV MNGRVDIALF STIHRVQLPS GSFSPKQIRA RFPHLHIGRS VHSLEEAVQA EKEDADYVLF GHVFETDCKK GLEGRGVSLL SDIKQRISIP VIAIGGMTPD RLRDVKQAGA DGIAVMSGIF SSAEPLEAAR RYSRKLKEMR YEKAL // ID THI6_SCHPO Reviewed; 518 AA. AC P40386; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 14-MAY-2014, entry version 109. DE RecName: Full=Probable thiamine biosynthetic bifunctional enzyme; DE Includes: DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; DE Includes: DE RecName: Full=Hydroxyethylthiazole kinase; DE EC=2.7.1.50; DE AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase; DE Short=TH kinase; DE Short=THZ kinase; GN Name=thi4; ORFNames=SPAC23H4.10c; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=7961415; RA Zurlinden A., Schweingruber M.E.; RT "Cloning, nucleotide sequence, and regulation of Schizosaccharomyces RT pombe thi4, a thiamine biosynthetic gene."; RL J. Bacteriol. 176:6631-6635(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- INDUCTION: Repressed by thiamine and 5-(2-hydroxyethyl)-4- CC methylthiazole. CC -!- SIMILARITY: In the N-terminal section; belongs to the thiamine- CC phosphate synthase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the Thz kinase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X78824; CAA55402.1; -; Genomic_DNA. DR EMBL; CU329670; CAB11664.1; -; Genomic_DNA. DR PIR; S44183; S44183. DR RefSeq; NP_593396.1; NM_001018828.2. DR ProteinModelPortal; P40386; -. DR BioGrid; 278362; 7. DR MINT; MINT-4689729; -. DR STRING; 4896.SPAC23H4.10c-1; -. DR MaxQB; P40386; -. DR EnsemblFungi; SPAC23H4.10c.1; SPAC23H4.10c.1:pep; SPAC23H4.10c. DR GeneID; 2541872; -. DR KEGG; spo:SPAC23H4.10c; -. DR PomBase; SPAC23H4.10c; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR PhylomeDB; P40386; -. DR UniPathway; UPA00060; UER00139. DR UniPathway; UPA00060; UER00141. DR NextBio; 20802959; -. DR GO; GO:0005737; C:cytoplasm; IDA:PomBase. DR GO; GO:0005829; C:cytosol; IDA:PomBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 2: Evidence at transcript level; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 518 Probable thiamine biosynthetic FT bifunctional enzyme. FT /FTId=PRO_0000157089. FT REGION 1 229 Thiamine-phosphate synthase. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT REGION 230 518 Hydroxyethylthiazole kinase. FT ACT_SITE 433 433 Proton acceptor; for hydroxyethylthiazole FT kinase activity (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). FT BINDING 281 281 4-methyl-5-(2-hydroxyethyl)thiazole; via FT amide nitrogen (By similarity). FT BINDING 355 355 ATP (By similarity). FT BINDING 403 403 ATP (By similarity). FT BINDING 430 430 4-methyl-5-(2-hydroxyethyl)thiazole; via FT amide nitrogen (By similarity). SQ SEQUENCE 518 AA; 55566 MW; B8836D2BD67C79AA CRC64; MKRQIDYSLY LVTSSSLIAP GSTIERQVEE GILGGVTLVQ HREKDISTKC FVERAKRLSE ICKKYDVPFL INDRIDVALA VGADGVHIGQ DDMDCALARK ILGDDAIIGV STNNIEEIEK AAADGADYVG IGSIYETNTK DVKDRLIGIT GLRKILEHVS KMHCQLGTVA IAGLNSSNIQ RVIYLSEANG KRIDGIALVS AIMCSITPRE TAKELRNLIA TPPCFAQARS SLTTPKDLLN QIPAALQKLK DFTPLIHHLT NAVAKNFSAN VTLAAYGSPT MGESYDEVAD FAKAPGALVL NIGILENTKT YIHAAQVNND LARPVILDPV AVGATTARSK VINTLLNYAY YDIIKGNEGE IMNLAGEQGL MRGVDSISQH TLAARITAVH RLAVERRCVV AMSGAVDVIS DGNSTYVIKN GNPLLGQITA SGCSLGSVMG VTASICQNDK LLAAITATLL YNIASELAVE AKNSCGDLLV QGPGTFIPIF VDKLHQLINE TIKGNVDWIE RAKLEKAE // ID THI6_YEAST Reviewed; 540 AA. AC P41835; D6W3F6; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 14-MAY-2014, entry version 123. DE RecName: Full=Thiamine biosynthetic bifunctional enzyme; DE Includes: DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; DE Includes: DE RecName: Full=Hydroxyethylthiazole kinase; DE EC=2.7.1.50; DE AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase; DE Short=TH kinase; DE Short=THZ kinase; GN Name=THI6; OrderedLocusNames=YPL214C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ND5-5A; RX PubMed=7982968; RA Nosaka K., Nishimura H., Kawasaki Y., Tsujihara T., Iwashima A.; RT "Isolation and characterization of the THI6 gene encoding a RT bifunctional thiamin-phosphate pyrophosphorylase/hydroxyethylthiazole RT kinase from Saccharomyces cerevisiae."; RL J. Biol. Chem. 269:30510-30516(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., RA Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., RA Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., RA Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., RA Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., RA Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., RA Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., RA Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., RA Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., RA Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., RA Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., RA Zollner A., Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). CC -!- FUNCTION: Essential for thiamine biosynthesis. The kinase activity CC is involved in the salvage synthesis of TH-P from the thiazole. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SUBUNIT: Homooctamer. CC -!- SIMILARITY: In the N-terminal section; belongs to the thiamine- CC phosphate synthase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the Thz kinase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D31908; BAA06703.1; -; Genomic_DNA. DR EMBL; Z73570; CAA97929.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11222.1; -; Genomic_DNA. DR PIR; A55145; A55145. DR RefSeq; NP_015110.1; NM_001184028.1. DR ProteinModelPortal; P41835; -. DR SMR; P41835; 3-536. DR BioGrid; 35971; 44. DR DIP; DIP-1666N; -. DR IntAct; P41835; 1. DR MINT; MINT-403731; -. DR STRING; 4932.YPL214C; -. DR MaxQB; P41835; -. DR PaxDb; P41835; -. DR EnsemblFungi; YPL214C; YPL214C; YPL214C. DR GeneID; 855887; -. DR KEGG; sce:YPL214C; -. DR CYGD; YPL214c; -. DR SGD; S000006135; THI6. DR eggNOG; COG0352; -. DR HOGENOM; HOG000214306; -. DR KO; K14154; -. DR OMA; NLVVQNF; -. DR OrthoDB; EOG7KDFMZ; -. DR BioCyc; MetaCyc:YPL214C-MONOMER; -. DR BioCyc; YEAST:YPL214C-MONOMER; -. DR UniPathway; UPA00060; UER00139. DR UniPathway; UPA00060; UER00141. DR NextBio; 980553; -. DR Genevestigator; P41835; -. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IMP:SGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IMP:SGD. DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:SGD. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 540 Thiamine biosynthetic bifunctional FT enzyme. FT /FTId=PRO_0000157090. FT REGION 1 238 Thiamine-phosphate synthase. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 209 210 THZ-P binding (By similarity). FT REGION 239 540 Hydroxyethylthiazole kinase. FT ACT_SITE 465 465 Proton acceptor; for hydroxyethylthiazole FT kinase activity (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). FT BINDING 290 290 4-methyl-5-(2-hydroxyethyl)thiazole; via FT amide nitrogen (By similarity). FT BINDING 365 365 ATP (By similarity). FT BINDING 415 415 ATP (By similarity). FT BINDING 462 462 4-methyl-5-(2-hydroxyethyl)thiazole; via FT amide nitrogen (By similarity). FT VARIANT 370 370 E -> K (in THI6-3; possesses TMP-PPASE FT activity only). FT VARIANT 476 476 G -> D (in THI6-2; both enzyme activities FT greatly decreased). FT VARIANT 510 510 G -> D (in THI6-1; both enzyme activities FT greatly decreased). SQ SEQUENCE 540 AA; 58059 MW; F34FA1E0B76E3930 CRC64; MVFTKEEVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDIE TKNFVAEALE VQKICKKYNV PLIINDRIDV AMAIDADGVH VGQDDMPIPM VRKLLGPSKI LGWSVGKPSE VETLAKWGPD MVDYIGVGTL FPTSTKKNPK KSPMGPQGAI AILDALEEFK ATWCRTVGIG GLHPDNIQRV LCQCVASNGK RSLDGISLVS DIMAAPDACA ATKRLRGLLD ATRYQFVECE LNNTFPTTTS IQNVISQVSN NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL ARIPNASLLL NTGSVAPIEM LKAAINAYNE VNRPITFDPV GYSATETRLC LNNTLLTYGQ FACIKGNCSE ILSLAKLNNH KMKGVDSSSG KTNIDTLVRA TQIVAFQYRT VAVCTGEFDC VADGTFGGEY KLSSGTEGIT AEDLPCVIIE DGPIPIMGDI TASGCSLGST IASFIGGLDS TGKLFDAVVG AVLLYKSAGK LASTRCQGSG SFHVELIDAL YQLFHENKPE KWSASLKKFK // ID THIE1_AQUAE Reviewed; 215 AA. AC O66833; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 14-MAY-2014, entry version 95. DE RecName: Full=Thiamine-phosphate synthase 1; DE Short=TP synthase 1; DE Short=TPS 1; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase 1; DE Short=TMP pyrophosphorylase 1; DE Short=TMP-PPase 1; GN Name=thiE1; OrderedLocusNames=aq_558; OS Aquifex aeolicus (strain VF5). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=224324; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex RT aeolicus."; RL Nature 392:353-358(1998). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000657; AAC06786.1; -; Genomic_DNA. DR PIR; E70350; E70350. DR RefSeq; NP_213393.1; NC_000918.1. DR ProteinModelPortal; O66833; -. DR STRING; 224324.aq_558; -. DR EnsemblBacteria; AAC06786; AAC06786; aq_558. DR GeneID; 1193251; -. DR KEGG; aae:aq_558; -. DR PATRIC; 20958648; VBIAquAeo85532_0459. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; WQVELTE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AAEO224324:GJBH-413-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 215 Thiamine-phosphate synthase 1. FT /FTId=PRO_0000156990. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 24245 MW; 96A05E23BDEB20CE CRC64; MNLTIYLITD DKYFKDRDLF NTIEQALQGG VTAVQYRFEN KTTRQMYEEL VKLRELTRKY NADLVVNDRV DLALAVEADG VHIGKDDLPP EVVRKIVGDK MYIGYTANSL EEVKRAQELP VDYIGFGSIY HTSTKENYKL VGVEALKEAV KISQKPIVCI GGIMPYRVPE VVRAGCRNIA VSSGILGFAD VKKAAESIKR AYQETLRMLM LMGKV // ID THIE1_STRPN Reviewed; 209 AA. AC Q97RS5; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 14-MAY-2014, entry version 84. DE RecName: Full=Thiamine-phosphate synthase 1; DE Short=TP synthase 1; DE Short=TPS 1; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase 1; DE Short=TMP pyrophosphorylase 1; DE Short=TMP-PPase 1; GN Name=thiE1; OrderedLocusNames=SP_0718; OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=170187; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-334 / TIGR4; RX PubMed=11463916; DOI=10.1126/science.1061217; RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D., RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., RA Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., RA Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.; RT "Complete genome sequence of a virulent isolate of Streptococcus RT pneumoniae."; RL Science 293:498-506(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE005672; AAK74859.1; -; Genomic_DNA. DR PIR; B95083; B95083. DR RefSeq; NP_345219.1; NC_003028.3. DR ProteinModelPortal; Q97RS5; -. DR STRING; 170187.SP_0718; -. DR EnsemblBacteria; AAK74859; AAK74859; SP_0718. DR GeneID; 930668; -. DR KEGG; spn:SP_0718; -. DR PATRIC; 19705801; VBIStrPne105772_0747. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE170187:GHGN-719-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase 1. FT /FTId=PRO_0000157055. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23276 MW; BE95DD9F842DE374 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGEGALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFGTQS KDDAGGTIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID THIE1_STRR6 Reviewed; 209 AA. AC Q8DQK4; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 76. DE RecName: Full=Thiamine-phosphate synthase 1; DE Short=TP synthase 1; DE Short=TPS 1; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase 1; DE Short=TMP pyrophosphorylase 1; DE Short=TMP-PPase 1; GN Name=thiE1; OrderedLocusNames=spr0630; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-255 / R6; RX PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001; RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., RA LeBlanc D.J., Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., RA McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I., RA Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P., RA Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G., RA Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L., RA Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE007317; AAK99434.1; -; Genomic_DNA. DR PIR; F97950; F97950. DR RefSeq; NP_358224.1; NC_003098.1. DR ProteinModelPortal; Q8DQK4; -. DR STRING; 171101.spr0630; -. DR EnsemblBacteria; AAK99434; AAK99434; spr0630. DR GeneID; 932808; -. DR KEGG; spr:spr0630; -. DR PATRIC; 19701157; VBIStrPne107296_0701. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE171101:GJC8-637-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase 1. FT /FTId=PRO_0000157056. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23334 MW; 09552FA5007A2FA0 CRC64; MFHKELLKLY FICGTTTCQG KNLYTVVEEA LKGGITLFQF REKGESALEG LEKLELAIQI KELCKKYNVP FIVNDDIDLA MEIDADGVHV GQDDIGVDEI RKLMPDKIIG LSIRNEEEFQ QSKVEYVDYV GVGPVFDTQS KDDAGGAIGY EGLELMRKLL PQMPLVAIGG IQTKHIKDII KTNMDGVSII SAISYAKNIE KTVREMSEQ // ID THIE2_AQUAE Reviewed; 186 AA. AC O67378; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 14-MAY-2014, entry version 77. DE RecName: Full=Putative thiamine-phosphate synthase 2; DE Short=TP synthase 2; DE Short=TPS 2; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase 2; DE Short=TMP pyrophosphorylase 2; DE Short=TMP-PPase 2; GN Name=thiE2; OrderedLocusNames=aq_1366; OS Aquifex aeolicus (strain VF5). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=224324; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex RT aeolicus."; RL Nature 392:353-358(1998). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000657; AAC07326.1; -; Genomic_DNA. DR PIR; G70418; G70418. DR RefSeq; NP_213942.1; NC_000918.1. DR ProteinModelPortal; O67378; -. DR STRING; 224324.aq_1366; -. DR EnsemblBacteria; AAC07326; AAC07326; aq_1366. DR GeneID; 1192816; -. DR KEGG; aae:aq_1366; -. DR PATRIC; 20959910; VBIAquAeo85532_1069. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AAEO224324:GJBH-983-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 186 Putative thiamine-phosphate synthase 2. FT /FTId=PRO_0000157088. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 181 182 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 161 161 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 186 AA; 21031 MW; 0C9D78E643EB1452 CRC64; MELPRLYAIT DRKKYGENFL ETLEKILKKG VRMVQLREKD LKDRELYKLA KEVRALTKKY KALLLINERF DIALAVEADG VHLPEQSFPP SVVKRVNPNF IVGFSAHSLE SAKYAEKEGA DFITLSPIFK TSSHPEAQPI GLKTLKEVSE KVNIPVYALG GITWEKIKVC YKNGAYGIAG ISMFLE // ID THIE2_STRPN Reviewed; 210 AA. AC P66920; Q97RR8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase 2; DE Short=TP synthase 2; DE Short=TPS 2; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase 2; DE Short=TMP pyrophosphorylase 2; DE Short=TMP-PPase 2; GN Name=thiE2; OrderedLocusNames=SP_0725; OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=170187; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-334 / TIGR4; RX PubMed=11463916; DOI=10.1126/science.1061217; RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D., RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., RA Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., RA Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.; RT "Complete genome sequence of a virulent isolate of Streptococcus RT pneumoniae."; RL Science 293:498-506(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE005672; AAK74866.1; -; Genomic_DNA. DR PIR; A95084; A95084. DR RefSeq; NP_345226.1; NC_003028.3. DR ProteinModelPortal; P66920; -. DR STRING; 170187.SP_0725; -. DR PRIDE; P66920; -. DR EnsemblBacteria; AAK74866; AAK74866; SP_0725. DR GeneID; 930675; -. DR KEGG; spn:SP_0725; -. DR PATRIC; 19705815; VBIStrPne105772_0754. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE170187:GHGN-726-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase 2. FT /FTId=PRO_0000157057. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; 60239DF9671A7380 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID THIE2_STRR6 Reviewed; 210 AA. AC P66921; Q97RR8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase 2; DE Short=TP synthase 2; DE Short=TPS 2; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase 2; DE Short=TMP pyrophosphorylase 2; DE Short=TMP-PPase 2; GN Name=thiE2; OrderedLocusNames=spr0637; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-255 / R6; RX PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001; RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., RA LeBlanc D.J., Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., RA McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I., RA Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P., RA Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G., RA Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L., RA Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE007317; AAK99441.1; -; Genomic_DNA. DR PIR; E97951; E97951. DR RefSeq; NP_358231.1; NC_003098.1. DR ProteinModelPortal; P66921; -. DR STRING; 171101.spr0637; -. DR PRIDE; P66921; -. DR EnsemblBacteria; AAK99441; AAK99441; spr0637. DR GeneID; 934175; -. DR KEGG; spr:spr0637; -. DR PATRIC; 19701171; VBIStrPne107296_0708. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SPNE171101:GJC8-644-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase 2. FT /FTId=PRO_0000157058. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22770 MW; 60239DF9671A7380 CRC64; MNREALRLYL VTNRYQDSVE SFLAKVETAC RSGVTIVQLR EKNLTTNQYY QLAKQVKEIT DAYQVPLIID DRLDVCLAVD AAGLHIGDDE LPVSVARKVL GPEKILGVTA KTVKRALEAE KSGADYLGTG AIFPTTTKEN APITLISTLK TICQTVAIPV VAIGGLTSEN IDQLMGTGIA GVAVVRDLMQ AEDIEAKTQA FLKKLHNILS // ID THIEC_BIFLO Reviewed; 917 AA. AC Q8G7X1; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-FEB-2014, entry version 72. DE RecName: Full=Thiamine biosynthesis bifunctional protein ThiEC; DE Includes: DE RecName: Full=Thiamine-phosphate synthase; DE Short=TMP-PPase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Includes: DE RecName: Full=Phosphomethylpyrimidine synthase; DE EC=4.1.99.17; DE AltName: Full=Hydroxymethylpyrimidine phosphate synthase; DE Short=HMP-P synthase; DE Short=HMP-phosphate synthase; DE Short=HMPP synthase; DE AltName: Full=Thiamine biosynthesis protein ThiC; GN Name=thiE/thiC; OrderedLocusNames=BL0114; OS Bifidobacterium longum (strain NCC 2705). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=206672; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCC 2705; RX PubMed=12381787; DOI=10.1073/pnas.212527599; RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., RA Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., RA Pridmore R.D., Arigoni F.; RT "The genome sequence of Bifidobacterium longum reflects its adaptation RT to the human gastrointestinal tract."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine + formate + CO. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: In the N-terminal section; belongs to the thiamine- CC phosphate synthase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the ThiC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014295; AAN23979.1; -; Genomic_DNA. DR RefSeq; NP_695343.1; NC_004307.2. DR ProteinModelPortal; Q8G7X1; -. DR STRING; 206672.BL0114; -. DR EnsemblBacteria; AAN23979; AAN23979; BL0114. DR GeneID; 1023237; -. DR KEGG; blo:BL0114; -. DR PATRIC; 21117273; VBIBifLon107831_0122. DR eggNOG; COG0352; -. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR OMA; INTICSA; -. DR OrthoDB; EOG6NWBM5; -. DR BioCyc; BLON206672:GI1E-113-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF01964; ThiC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Magnesium; KW Metal-binding; Multifunctional enzyme; Reference proteome; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Transferase; Zinc. FT CHAIN 1 917 Thiamine biosynthesis bifunctional FT protein ThiEC. FT /FTId=PRO_0000152856. FT REGION 1 243 Thiamine-phosphate synthase. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 157 159 THZ-P binding (By similarity). FT REGION 216 217 THZ-P binding (By similarity). FT REGION 271 917 Phosphomethylpyrimidine synthase. FT REGION 601 603 5-aminoimidazole ribonucleotide binding FT (By similarity). FT REGION 642 645 5-aminoimidazole ribonucleotide binding FT (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 109 109 Magnesium (By similarity). FT METAL 685 685 Zinc (By similarity). FT METAL 749 749 Zinc (By similarity). FT METAL 829 829 Iron-sulfur (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 832 832 Iron-sulfur (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 837 837 Iron-sulfur (4Fe-4S-S-AdoMet) (By FT similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 160 160 HMP-PP (By similarity). FT BINDING 196 196 THZ-P; via amide nitrogen (By FT similarity). FT BINDING 487 487 5-aminoimidazole ribonucleotide (By FT similarity). FT BINDING 516 516 5-aminoimidazole ribonucleotide (By FT similarity). FT BINDING 545 545 5-aminoimidazole ribonucleotide (By FT similarity). FT BINDING 581 581 5-aminoimidazole ribonucleotide (By FT similarity). FT BINDING 681 681 5-aminoimidazole ribonucleotide (By FT similarity). FT BINDING 708 708 5-aminoimidazole ribonucleotide (By FT similarity). SQ SEQUENCE 917 AA; 100355 MW; 00000DA28A98E1F6 CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLADTKA AGWFVVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE // ID THIED_COREF Reviewed; 739 AA. AC Q8FTH8; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 83. DE RecName: Full=Thiamine biosynthesis multifunctional protein ThiED; DE Includes: DE RecName: Full=Thiamine-phosphate synthase; DE Short=TMP-PPase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Includes: DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; DE EC=2.7.1.49; DE EC=2.7.4.7; DE AltName: Full=Hydroxymethylpyrimidine kinase; DE Short=HMP kinase; DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase; DE Short=HMP-P kinase; DE Short=HMP-phosphate kinase; DE Short=HMPP kinase; GN Name=thiED; OrderedLocusNames=CE1591; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM OS 11189 / NBRC 100395). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., RA Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., RA Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-5-hydroxymethyl-2- CC methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2- CC methylpyrimidine. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-2-methyl-5- CC phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5- CC diphosphomethylpyrimidine. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole: step 3/3. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- MISCELLANEOUS: There is also a ThiE protein in this bacteria (AC CC Q8FP55). CC -!- SIMILARITY: In the N-terminal section; belongs to the thiamine- CC phosphate synthase family. CC -!- SIMILARITY: In the central section; belongs to the ThiD family. CC -!- SIMILARITY: In the C-terminal section; belongs to the thiaminase-2 CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000035; BAC18401.1; -; Genomic_DNA. DR RefSeq; NP_738201.1; NC_004369.1. DR ProteinModelPortal; Q8FTH8; -. DR STRING; 196164.CE1591; -. DR EnsemblBacteria; BAC18401; BAC18401; BAC18401. DR GeneID; 1034064; -. DR KEGG; cef:CE1591; -. DR PATRIC; 21489321; VBICorEff9312_1583. DR HOGENOM; HOG000225275; -. DR KO; K14153; -. DR OMA; RHELEFF; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00138. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.910.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF03070; TENA_THI-4; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; SSF48613; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 739 Thiamine biosynthesis multifunctional FT protein ThiED. FT /FTId=PRO_0000192038. FT REGION 1 210 Thiamine-phosphate synthase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT REGION 226 481 Hydroxymethylpyrimidine/ FT phosphomethylpyrimidine kinase. FT REGION 527 739 Thiaminase-2. FT METAL 70 70 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). FT BINDING 263 263 Hydroxymethylpyrimidine (By similarity). SQ SEQUENCE 739 AA; 77744 MW; D6631B0553929077 CRC64; MTDFSLYLVT DPHLGGGPER VAGIVEDAIN GGVTVVQLRD KDADEQTFRE HAMELKRVCD RLGVPLFLND RFAVAAELSC HVHIGQGDLP YVQARRQLPG HLMIGLTIET MDQLETVIAD CTRAGIALPD VVGLGPVQAT DTKPDAPQAV GVDGVAAMAK VARAHGIASV AIGGVGLANA ADLARTGVDG LCVVSAIMAA PSPAEAAREL LDVWEAGRRV AQPRVLTIAG TDPTGGAGVQ ADLKSIAAAG GFGMSVITAL VAQNTHGVTG VHTPPADFLD EQLESVFSDV TVDAVKLGML GRADTVRQVT GWLRTRPHGP VILDPVMVAT SGDSLLDPDA TEALLELATV VDVITPNIPE LAVLCGEQPA PSFDAAIEQA RRFATDVGTT VIVKGGHLTG PRADNAVVYP DGSVHMVANP RVDTTNSHGT GCSLSAALAT RMGAGHPVDK ALDWATRWLN EALRGADALQ VGSGSGPVDH FAVTRRLLRA ADATPWPHLR MGAPSDGIIT PSDTQSPAPA LAPAGPYTRA LWEATGDVLG EILDSGFIRG LGDGTLSREE FLFYIDQDAH YLRQYSRALA TLSSRAPDAP AQVDWATSAA ECITVEAELH RTYLNKGLAE TGVSAPSPVT MAYTDFLIAR SHADDYVVGA AAVLPCYWLY AEIGLILAKQ NHPEHPYTDW LDTYSGEGFL AGTVKAIARV EAAMAGAGPD QQRVAAQTYL SACVHEREFF DQATRQGWN // ID THIED_CORGL Reviewed; 763 AA. AC Q8NQH1; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 2. DT 14-MAY-2014, entry version 85. DE RecName: Full=Thiamine biosynthesis multifunctional protein ThiED; DE Includes: DE RecName: Full=Thiamine-phosphate synthase; DE Short=TMP-PPase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Includes: DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; DE EC=2.7.1.49; DE EC=2.7.4.7; DE AltName: Full=Hydroxymethylpyrimidine kinase; DE Short=HMP kinase; DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase; DE Short=HMP-P kinase; DE Short=HMP-phosphate kinase; DE Short=HMPP kinase; GN Name=theD; Synonyms=thiD1; OrderedLocusNames=Cgl1463, cg1654; OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / OS LMG 3730 / NCIMB 10025). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196627; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1; RA Ikeda M., Nakagawa S.; RT "The Corynebacterium glutamicum genome: features and impacts on RT biotechnological processes."; RL Appl. Microbiol. Biotechnol. 62:99-109(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., RA Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence RT and its impact on the production of L-aspartate-derived amino acids RT and vitamins."; RL J. Biotechnol. 104:5-25(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-5-hydroxymethyl-2- CC methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2- CC methylpyrimidine. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-2-methyl-5- CC phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5- CC diphosphomethylpyrimidine. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole: step 3/3. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: In the N-terminal section; belongs to the thiamine- CC phosphate synthase family. CC -!- SIMILARITY: In the central section; belongs to the ThiD family. CC -!- SIMILARITY: In the C-terminal section; belongs to the thiaminase-2 CC family. CC -!- SEQUENCE CAUTION: CC Sequence=BAB98856.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000036; BAB98856.1; ALT_INIT; Genomic_DNA. DR EMBL; BX927152; CAF21472.1; -; Genomic_DNA. DR RefSeq; NP_600680.3; NC_003450.3. DR RefSeq; YP_225748.1; NC_006958.1. DR ProteinModelPortal; Q8NQH1; -. DR STRING; 196627.cg1654; -. DR DNASU; 3345397; -. DR EnsemblBacteria; BAB98856; BAB98856; BAB98856. DR EnsemblBacteria; CAF21472; CAF21472; cg1654. DR GeneID; 1019437; -. DR GeneID; 3345397; -. DR KEGG; cgb:cg1654; -. DR KEGG; cgl:NCgl1407; -. DR PATRIC; 21494969; VBICorGlu203724_1430. DR eggNOG; COG0351; -. DR HOGENOM; HOG000225275; -. DR KO; K14153; -. DR OMA; GFWEMFP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CGLU196627:GJDM-1450-MONOMER; -. DR UniPathway; UPA00060; UER00138. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.910.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF03070; TENA_THI-4; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; SSF48613; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 763 Thiamine biosynthesis multifunctional FT protein ThiED. FT /FTId=PRO_0000192039. FT REGION 1 210 Thiamine-phosphate synthase. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT REGION 245 500 Hydroxymethylpyrimidine/ FT phosphomethylpyrimidine kinase. FT REGION 550 763 Thiaminase-2. FT METAL 70 70 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). FT BINDING 282 282 Hydroxymethylpyrimidine (By similarity). SQ SEQUENCE 763 AA; 80355 MW; CA992321E884577F CRC64; MTDFSLYLVT DPVLGGGPEK VAGIVDSAIS GGVSVVQLRD KNSGVEDVRA AAKELKELCD ARGVALVVND YLDIAVELGL HLHIGQGDTP YTQARELLPA HLELGLSIEN LDQLHAVIAQ CAETGVALPD VIGIGPVAST ATKPDAAPAL GVEGIAEIAA VAQDHGIASV AIGGVGLRNA AELAATPIDG LCVVSEIMTA ANPAAAATRL RTAFQPTFSP ETQTELSQTE LQGAFVNSPS APRVLSIAGT DPTGGAGIQA DLKSIAAGGG YGMCVVTSLV AQNTHGVNTI HTPPLTFLEE QLEAVFSDVT VDAIKLGMLG SADTVDLVAS WLGSHEHGPV VLDPVMIATS GDRLLDASAE ESLRRLAVHV DVVTPNIPEL AVLCDSAPAI TMDEAIAQAQ GFARTHDTIV IVKGGHLTGA LADNAVVRPD GSVFQVENLR VNTTNSHGTG CSLSASLATK IAAGESVEKA LEWSTRWLNE ALRHADHLAV GTGNGPVDHG HLARRMTHAA ETTPWAHLRA PRLDGATAAS FTTPSTVKSP APRIEPAGPF TRALWEASGD IIAGINSSDF ITMLGDGTLR RPEFDFYIDQ DAQYLAQYSR ALARLSSIAP DSHAQIEWAQ SAAECLVVEA ELHRSYMAGK EVSAPSHITM AYTDFLIART YTEDYVCGVA AVLPCYWLYA EIGLMLAEQN HDEHPYKDWL NTYSGEEFIA GTRAAIARLE KALENAGAEQ RVDAARAFLS ASVHEREFFD QATRHGWTMV GSS // ID THIED_GEOSL Reviewed; 490 AA. AC P61422; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 1. DT 14-MAY-2014, entry version 80. DE RecName: Full=Thiamine biosynthesis bifunctional protein ThiED; DE Includes: DE RecName: Full=Thiamine-phosphate synthase; DE Short=TMP-PPase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Includes: DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; DE EC=2.7.1.49; DE EC=2.7.4.7; DE AltName: Full=Hydroxymethylpyrimidine kinase; DE Short=HMP kinase; DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase; DE Short=HMP-P kinase; DE Short=HMP-phosphate kinase; DE Short=HMPP kinase; GN Name=thiDE; OrderedLocusNames=GSU0605; OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=243231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51573 / DSM 12127 / PCA; RX PubMed=14671304; DOI=10.1126/science.1088727; RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C., RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J., RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A., RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., RA Van Aken S.E., Lovley D.R., Fraser C.M.; RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface RT environments."; RL Science 302:1967-1969(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-5-hydroxymethyl-2- CC methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2- CC methylpyrimidine. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-2-methyl-5- CC phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5- CC diphosphomethylpyrimidine. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole: step 3/3. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: In the N-terminal section; belongs to the thiamine- CC phosphate synthase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the ThiD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017180; AAR33936.1; -; Genomic_DNA. DR RefSeq; NP_951663.1; NC_002939.5. DR ProteinModelPortal; P61422; -. DR STRING; 243231.GSU0605; -. DR EnsemblBacteria; AAR33936; AAR33936; GSU0605. DR GeneID; 2687129; -. DR KEGG; gsu:GSU0605; -. DR PATRIC; 22023961; VBIGeoSul17553_0603. DR eggNOG; COG0351; -. DR HOGENOM; HOG000134175; -. DR KO; K14153; -. DR OMA; YLAQGEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; GSUL243231:GH27-611-MONOMER; -. DR UniPathway; UPA00060; UER00138. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013749; HMP-P_kinase-1. DR InterPro; IPR004399; HMP-P_kinase-2. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 490 Thiamine biosynthesis bifunctional FT protein ThiED. FT /FTId=PRO_0000192040. FT REGION 1 213 Thiamine-phosphate synthase. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT REGION 229 490 Hydroxymethylpyrimidine/ FT phosphomethylpyrimidine kinase. FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). FT BINDING 266 266 Hydroxymethylpyrimidine (By similarity). SQ SEQUENCE 490 AA; 51910 MW; 924B153FCD5E83D4 CRC64; MASNGHTLRL VINRDKHDSV IRGLYLVTDH DDNLIPRVEA AIDGGARVVQ YRNKNQDRES RLALGLELRE LCRRRSIPFI VNDDLEMAVS LKADGLHLGQ GDGDPREARR VLGPGKIIGV STHTLSEALE AQAAGVDYIG LGAMFPSRSK EVEHVAGSEL LAAIRSSISI PIVAIGGITR DNGASVIDAG ADAVAVISAV LSHPDPALAA TEIALLFNRR APFPRGSVLT VAGSDSGGGA GIQADLKTVT LLGSYGSSVL TALTAQNTRG VSGIHGVPPA FVADQLDAVF SDIPVDVVKT GMLFSAETIV AIAAKLTEYR RRMVVVDPVM VAKGGANLID RGAVSVLKER LFPLAYLVTP NIPEAERLTG ANISDEESMR EAARRLHRLG ARNVLLKGGH LLAGDSVDIL FDGAAFHRFV SPRILSKNTH GTGCTFASAI ATYLAQGDPL REAIARAKRY ITAAIRLAQP LGRGHGPVNH ILAAEDVRDR // ID THIE_ACIC1 Reviewed; 212 AA. AC A0LTK3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Acel_0990; OS Acidothermus cellulolyticus (strain ATCC 43068 / 11B). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Acidothermaceae; Acidothermus. OX NCBI_TaxID=351607; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43068 / 11B; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Berry A.M., Adney W.S., Normand P., RA Leu D., Pujic P., Richardson P.; RT "Complete sequence of Acidothermus cellulolyticus 11B."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000481; ABK52763.1; -; Genomic_DNA. DR RefSeq; YP_872749.1; NC_008578.1. DR ProteinModelPortal; A0LTK3; -. DR STRING; 351607.Acel_0990; -. DR EnsemblBacteria; ABK52763; ABK52763; Acel_0990. DR GeneID; 4485933; -. DR KEGG; ace:Acel_0990; -. DR PATRIC; 20672422; VBIAciCel132453_1049. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ACEL351607:GIXW-1014-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_0000336368. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22359 MW; B14BB8196FAB6256 CRC64; MKASLADARL YLCVDSRRRQ GDLPAFLDAV LGAGVDVVQL REKGLEAKEE LRLLDVFAEA CRRHGALLAV NDRADIAYAA RSDVLHLGQD DLPVGIARSI VGDDVVIGLS THSVEQVQAA VSDPAVDYFC VGPCWPTPTK PGRPAAGLDV VRYAAQAAGD RPWFAIGGIN LQNLDEVLEA GARRVVVVRA IADAPDPAEA AAEFAARLAA AA // ID THIE_ACIF2 Reviewed; 217 AA. AC B7JBI2; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=AFE_3304; OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / NCIB OS 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=243159; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23270 / DSM 14882 / NCIB 8455; RX PubMed=19077236; DOI=10.1186/1471-2164-9-597; RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., RA Blake R. II, Eisen J.A., Holmes D.S.; RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to RT industrial applications."; RL BMC Genomics 9:597-597(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001219; ACK79913.1; -; Genomic_DNA. DR RefSeq; YP_002427657.1; NC_011761.1. DR ProteinModelPortal; B7JBI2; -. DR STRING; 243159.AFE_3304; -. DR EnsemblBacteria; ACK79913; ACK79913; AFE_3304. DR GeneID; 7134557; -. DR KEGG; afr:AFE_3304; -. DR PATRIC; 20657537; VBIAciFer29821_3011. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AFER243159:GH3S-3299-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_1000117293. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22628 MW; 01F0013C44881B3F CRC64; MAGDDHLISG LYAITDAHLM PEPVFLARAE AALRGGARIL QYRDKGDVVT DARRRRMQAG ALRELCAQYG ALFVVNDDPR LARVVGAPAL HVGAEDAPPA ALRAQFGRAI LIGVSCYGSV PQAQEAATQG ADYVAFGSFF ASPSKPQAPV VSVDVLTAAR AMIDLPIVAI GGITEANGRA LIAAGADALA VISGVFAAED VEGAARRFTA LFNNRKE // ID THIE_ACIF5 Reviewed; 217 AA. AC B5ERP0; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Lferr_2902; OS Acidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum OS ferrooxidans (ATCC 53993)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=380394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 53993; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Borole A.P.; RT "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001132; ACH85086.1; -; Genomic_DNA. DR RefSeq; YP_002221293.1; NC_011206.1. DR ProteinModelPortal; B5ERP0; -. DR STRING; 380394.Lferr_2902; -. DR EnsemblBacteria; ACH85086; ACH85086; Lferr_2902. DR GeneID; 6878906; -. DR KEGG; afe:Lferr_2902; -. DR PATRIC; 20663390; VBIAciFer6930_2870. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AFER380394:GHE0-2957-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_1000093658. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22628 MW; 01F0013C44881B3F CRC64; MAGDDHLISG LYAITDAHLM PEPVFLARAE AALRGGARIL QYRDKGDVVT DARRRRMQAG ALRELCAQYG ALFVVNDDPR LARVVGAPAL HVGAEDAPPA ALRAQFGRAI LIGVSCYGSV PQAQEAATQG ADYVAFGSFF ASPSKPQAPV VSVDVLTAAR AMIDLPIVAI GGITEANGRA LIAAGADALA VISGVFAAED VEGAARRFTA LFNNRKE // ID THIE_ACTP7 Reviewed; 218 AA. AC B3GX82; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=APP7_0582; OS Actinobacillus pleuropneumoniae serotype 7 (strain AP76). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=537457; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AP76; RA Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N., RA Tegetmeyer H., Singh M., Gerlach G.F.; RT "Genome and proteome analysis of A. pleuropneumoniae serotype 7."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001091; ACE61234.1; -; Genomic_DNA. DR RefSeq; YP_001968376.1; NC_010939.1. DR ProteinModelPortal; B3GX82; -. DR STRING; 537457.APP7_0582; -. DR EnsemblBacteria; ACE61234; ACE61234; APP7_0582. DR GeneID; 6396486; -. DR KEGG; apa:APP7_0582; -. DR PATRIC; 20754774; VBIActPle116979_0599. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; APLE537457:GJI0-595-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 218 Thiamine-phosphate synthase. FT /FTId=PRO_1000093659. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 24090 MW; 491DAAE0E7ED3954 CRC64; MYDIRQMLQL YFIAGTQDCP NPTEDRSQNL LLILEQALQA GITCFQFRDK SKNSLEDQPN AQKALAIQCR DLCRLYNVPF IVDDNVALAI EIDADGVHVG QKDMSPIMIR QMTDKPLIIG LSNNTLEDLW RSEQMIEVDY CGLGPVFPTN SKEKHNPPIG LDFVKKAREA GIRKPIVSIG GVKAEHVATL KQNGADGVAV ITAISLASDV SQAVKRLL // ID THIE_ACTSZ Reviewed; 221 AA. AC A6VPG9; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Asuc_1508; OS Actinobacillus succinogenes (strain ATCC 55618 / 130Z). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=339671; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55618 / 130Z; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., RA Richardson P.; RT "Complete sequence of Actinobacillus succinogenes 130Z."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000746; ABR74866.1; -; Genomic_DNA. DR RefSeq; YP_001344801.1; NC_009655.1. DR ProteinModelPortal; A6VPG9; -. DR STRING; 339671.Asuc_1508; -. DR EnsemblBacteria; ABR74866; ABR74866; Asuc_1508. DR GeneID; 5347914; -. DR KEGG; asu:Asuc_1508; -. DR PATRIC; 20761398; VBIActSuc117883_1573. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ASUC339671:GHDX-1578-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 221 Thiamine-phosphate synthase. FT /FTId=PRO_1000071282. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 24262 MW; 9B6F7DB5438C573F CRC64; MNKIKSMLSV YFIAGSQDCR HLPGSPVENL LNILQQALEA GITCFQFREK GERSLAQNPQ LKHRLALQCQ QLCRQFNVPF IINDDIGLAL AIRADGIHVG QKDTAVERIL SRADYRPIIG LSINTLEQAQ ANKERLGIDY FGIGPIFATQ SKADHAPAVG MEFIRQIHEL GIDKPCVAIG GIHEDNTAEI RRLGANGVAV ISAITRSNDI ARTVQNLACH S // ID THIE_AGRT5 Reviewed; 220 AA. AC Q8UAS8; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2002, sequence version 2. DT 14-MAY-2014, entry version 78. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Atu3289; ORFNames=AGR_L_3059; OS Agrobacterium tumefaciens (strain C58 / ATCC 33970). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=176299; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970; RX PubMed=11743193; DOI=10.1126/science.1066804; RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., RA Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., RA Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., RA Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C., RA Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., RA Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., RA Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., RA Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., RA Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., RA Nester E.W.; RT "The genome of the natural genetic engineer Agrobacterium tumefaciens RT C58."; RL Science 294:2317-2323(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970; RX PubMed=11743194; DOI=10.1126/science.1066803; RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., RA Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., RA Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., RA Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B., RA Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., RA Cielo C., Slater S.; RT "Genome sequence of the plant pathogen and biotechnology agent RT Agrobacterium tumefaciens C58."; RL Science 294:2323-2328(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE007870; AAK90101.2; -; Genomic_DNA. DR PIR; AC2961; AC2961. DR PIR; C98322; C98322. DR RefSeq; NP_357316.2; NC_003063.2. DR ProteinModelPortal; Q8UAS8; -. DR STRING; 176299.Atu3289; -. DR EnsemblBacteria; AAK90101; AAK90101; Atu3289. DR GeneID; 1135163; -. DR KEGG; atu:Atu3289; -. DR PATRIC; 20816036; VBIAgrTum91616_3130. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HGSTREM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AGRO:ATU3289-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 220 Thiamine-phosphate synthase. FT /FTId=PRO_0000156989. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 22880 MW; 6E27E3FEBBC35BC1 CRC64; MNKVDYRLNA LVDASLADVA PLPELALAAA LNGATILQYR DKHGSTREMI ENARAIREAI GGTGVPLVIN DRVDVALASG ADGVHLGADD MDAKTARRIL GEKAIIGLTV KNRADAERAA SMPADYACIG GVFETVSKVN PDKPVGIEGF TTLRALLKEW QPDMPVGAIA GIDLDRVPAV IAAGADGVAV ISAIFRAANI ASATSDFRSA IDAALKARQP // ID THIE_ALCBS Reviewed; 217 AA. AC Q0VSP5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 19-FEB-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=ABO_0355; OS Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK2 / ATCC 700651 / DSM 11573; RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., RA Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., RA Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., RA Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A., RA Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., RA Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine RT bacterium Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=CAL15803.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM286690; CAL15803.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_692075.1; NC_008260.1. DR ProteinModelPortal; Q0VSP5; -. DR STRING; 393595.ABO_0355; -. DR EnsemblBacteria; CAL15803; CAL15803; ABO_0355. DR GeneID; 4211937; -. DR KEGG; abo:ABO_0355; -. DR PATRIC; 20838321; VBIAlcBor124741_0376. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ABOR393595:GHRI-357-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_0000336369. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22906 MW; 948E8089D223AD50 CRC64; MPLHRLHGLY AITDPALTPD EHLLPAAEAA LRGGAKLLQY RDKTASPTQR EYRAAQLRQL CHQYHALFIV NDDPALAAQV NADGVHIGQS DGGIKAARDQ LGGSRIIGVT CHGDLTLAAR AAEAGADYLA MGRFFTSHTK PLAPPASLAL LRQACQQFHQ PVVAIGGVNP DNAPQLINAG AVSVAVIHAL FGQTDTDAIE AAARQLSACF QTNRSAP // ID THIE_ALKMQ Reviewed; 211 AA. AC A6TMN5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Amet_1247; OS Alkaliphilus metalliredigens (strain QYMF). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Alkaliphilus. OX NCBI_TaxID=293826; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QYMF; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Ye Q., RA Zhou J., Fields M., Richardson P.; RT "Complete sequence of Alkaliphilus metalliredigens QYMF."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000724; ABR47453.1; -; Genomic_DNA. DR RefSeq; YP_001319112.1; NC_009633.1. DR ProteinModelPortal; A6TMN5; -. DR STRING; 293826.Amet_1247; -. DR EnsemblBacteria; ABR47453; ABR47453; Amet_1247. DR GeneID; 5311298; -. DR KEGG; amt:Amet_1247; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AMET293826:GI5P-1272-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000336370. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22420 MW; 994224E2299E59F8 CRC64; MSPIVKTDYS LYLVTDRSLL NGKDLMESIE AAIKGGVSIV QLREKQATSA VFYETALALK KLTDQYQIPL IINDRLDIAL AVDAAGLHIG PDDLPIKKAR ELLGPHKTLG YSAATLAEAL EAESLGANYL GVGALFPTKT KKDTESVSLQ LLQKIKSSVS IPIVGIGGIS QGNASQVIQS GADGIAVVSA ILSKQYPEIA AKNLYLKTQN K // ID THIE_ALKOO Reviewed; 209 AA. AC A8MK92; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Clos_2693; OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii OS (strain OhILAs)). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Alkaliphilus. OX NCBI_TaxID=350688; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OhILAs; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., RA Ranganathan M., Basu P., Richardson P.; RT "Complete genome of Alkaliphilus oremlandii OhILAs."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000853; ABW20224.1; -; Genomic_DNA. DR RefSeq; YP_001514220.1; NC_009922.1. DR ProteinModelPortal; A8MK92; -. DR STRING; 350688.Clos_2693; -. DR EnsemblBacteria; ABW20224; ABW20224; Clos_2693. DR GeneID; 5678746; -. DR KEGG; aoe:Clos_2693; -. DR PATRIC; 20870872; VBIAlkOre124042_2813. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AORE350688:GHBG-2806-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_0000336371. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22487 MW; 6D30128117DD3AA9 CRC64; MKYNHTVDYG LYLVSDRDVL KGRDFIKSLE EAILGGATIV QLREKEASSL EFYQLALKAK ALTEKYNVPL IINDRVDIAL AVDADGVHVG QSDLPAHIVR SMIGQNKILG VSTATLEESK KAAEDGADYI GVGALFPTGT KTDANPVTLD QLRYIKENMD IPVVGIGGIC EDNIKTIMEV GIDGVAIVSA ILGKENIKEA AESLKASIK // ID THIE_ANADE Reviewed; 222 AA. AC Q2IM25; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 57. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Adeh_0075; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=290397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-C; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000251; ABC79853.1; -; Genomic_DNA. DR RefSeq; YP_463290.1; NC_007760.1. DR ProteinModelPortal; Q2IM25; -. DR STRING; 290397.Adeh_0075; -. DR EnsemblBacteria; ABC79853; ABC79853; Adeh_0075. DR GeneID; 3886176; -. DR KEGG; ade:Adeh_0075; -. DR PATRIC; 20916153; VBIAnaDeh31384_0081. DR eggNOG; NOG133055; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HRFYFIT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ADEH290397:GI2Z-77-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 222 Thiamine-phosphate synthase. FT /FTId=PRO_0000336372. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 22027 MW; 9A98B4FB8EA252C3 CRC64; MPVSEASVSA GRRARLGGLY VIVGGADPVA QARAAIGGGA RAIQVRMKDA PAGAVLEATR RILALATGRA LVLVNDRADL ALLAGADGVH LGDDDLPVPE ARRLLGPDLL VGRTTRTLEE ARAALAEGAD HVGYGPIFAS RSKALPVPPR GLAALAEVAR ALPAPVVAIG GIGLDDVAAV ARAGAACAAV IEAVLGAADP EAAAARMQAA FEAGRAARGA TP // ID THIE_CALBD Reviewed; 219 AA. AC B9MN52; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Athe_0372; OS Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320) OS (Anaerocellum thermophilum). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=521460; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Kataeva I., Adams M.W.W.; RT "Complete sequence of chromosome of Anaerocellum thermophilum DSM RT 6725."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001393; ACM59508.1; -; Genomic_DNA. DR RefSeq; YP_002572281.1; NC_012034.1. DR ProteinModelPortal; B9MN52; -. DR STRING; 521460.Athe_0372; -. DR EnsemblBacteria; ACM59508; ACM59508; Athe_0372. DR GeneID; 7409302; -. DR KEGG; ate:Athe_0372; -. DR PATRIC; 20897726; VBIAnaThe135187_0393. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CBES521460:GH8H-374-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000198070. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24408 MW; EF3B8880FD66D747 CRC64; MTKEGKLKLF STYTIYGMTA EKFSNGRSNI EVVKVMLDSG IKIIQYREKY KSLKEKYKEC LEIRKLTEDY EALLIVNDHA DLCQMVGADG VHLGQEDLPA DEVRKLLGDK FIIGVTTHTK DQVLKAKEDG ADYVGLGPVF ASFTKDNPHP PIGLEMVKWA AENSPLPFVA IGGIKEHNLK EVLASGARCI CAVTEIVGAD DIRKKIESLF KILKSFERS // ID THIE_ANOFW Reviewed; 217 AA. AC B7GKQ8; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Aflv_1346; OS Anoxybacillus flavithermus (strain DSM 21510 / WK1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus. OX NCBI_TaxID=491915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21510 / WK1; RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161; RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A., RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V., RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., RA Alam M.; RT "Encapsulated in silica: genome, proteome and physiology of the RT thermophilic bacterium Anoxybacillus flavithermus WK1."; RL Genome Biol. 9:R161.1-R161.16(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000922; ACJ33714.1; -; Genomic_DNA. DR RefSeq; YP_002315699.1; NC_011567.1. DR ProteinModelPortal; B7GKQ8; -. DR STRING; 491915.Aflv_1346; -. DR EnsemblBacteria; ACJ33714; ACJ33714; Aflv_1346. DR GeneID; 7037599; -. DR KEGG; afl:Aflv_1346; -. DR PATRIC; 20954549; VBIAnoFla45531_1384. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AFLA491915:GHEO-1417-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_1000117294. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 24037 MW; DEBDDD862D44B772 CRC64; MMKQKLSLYF VMGSIDCTKD PLAVLDEAIK GGITMFQFRE KGKGALTGIE KYRLAEKLLE RCRMYNIPFI VNDDVDLALA LQADGVHVGQ EDEVAERVRD RIGDKYLGVS VHNLNEVKKA LAACADYVGL GPIFPTVSKE DAKQACGLTM IEHIRAHEKR VPLVAIGGIT EQTAKQVIEA GADGIAVISA ICRAEHIYEQ TKRLYEMVMR AKQKGDR // ID THIE_ARCFU Reviewed; 210 AA. AC O28205; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 14-MAY-2014, entry version 95. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=AF_2074; OS Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM OS 9628 / NBRC 100126). OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; OC Archaeoglobaceae; Archaeoglobus. OX NCBI_TaxID=224325; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126; RX PubMed=9389475; DOI=10.1038/37052; RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., RA Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., RA Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., RA Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., RA Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., RA Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., RA Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., RA Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., RA Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., RA Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., RA Woese C.R., Venter J.C.; RT "The complete genome sequence of the hyperthermophilic, sulphate- RT reducing archaeon Archaeoglobus fulgidus."; RL Nature 390:364-370(1997). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000782; AAB89175.1; -; Genomic_DNA. DR PIR; A69509; A69509. DR RefSeq; NP_070898.1; NC_000917.1. DR ProteinModelPortal; O28205; -. DR SMR; O28205; 4-205. DR STRING; 224325.AF2074; -. DR EnsemblBacteria; AAB89175; AAB89175; AF_2074. DR GeneID; 1485301; -. DR KEGG; afu:AF2074; -. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; AFUL224325:GJBC-2116-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_0000157067. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). SQ SEQUENCE 210 AA; 23050 MW; EC6A041F2483337E CRC64; MSRLEDYLSV YFITDSEFGR THEELAEMAL RAGVRAIQFR EKKLSTKRMY EIGKRLRALT RDYDALFFVN DRIDVALAVD ADGVHIGQDD MPAFAAREIF PGYIGVSAGN VEEAKKDERF ADYLGVGPVF PTKTKEDAGE AIGIEGLRRI VESVSVPVVA IGSINKQNAI EVLKTGVAGI AVISAIAAAD DPERAARELV ELVRRFKSGL // ID THIE_AROAE Reviewed; 208 AA. AC Q5P6J5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 14-MAY-2014, entry version 70. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=AZOSEA09410; ORFNames=ebB48; OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Aromatoleum. OX NCBI_TaxID=76114; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EbN1; RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9; RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., RA Reinhardt R.; RT "The genome sequence of an anaerobic aromatic-degrading denitrifying RT bacterium, strain EbN1."; RL Arch. Microbiol. 183:27-36(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR555306; CAI07066.1; -; Genomic_DNA. DR RefSeq; YP_157967.1; NC_006513.1. DR ProteinModelPortal; Q5P6J5; -. DR STRING; 76114.ebB48; -. DR EnsemblBacteria; CAI07066; CAI07066; ebB48. DR GeneID; 3181740; -. DR KEGG; eba:ebB48; -. DR PATRIC; 20967991; VBIAroAro98752_0956. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PRLHVIT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AARO76114:GJTA-960-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 208 Thiamine-phosphate synthase. FT /FTId=PRO_0000336374. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 21834 MW; 1960CE6E518E5731 CRC64; MPDTRLRGLY LITPDSPDTT TLVAQVERAL RGQPALLQYR SKQRDAALRL GQARQIAALC REAGVPFIVN DSLELALATD ADGVHLGRED GDLDAARRAL GPGRILGVTC YNEWPRAVAG CAAGADYVAF GAVFPSATKP AAVRAPLELF VRGRRELDVP LAAIGGITLD NAAQVIAAGA SLLAVVSDVF DAPDPGARAA AYRTLFDA // ID THIE_ARTS2 Reviewed; 237 AA. AC A0JYP1; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Arth_2782; OS Arthrobacter sp. (strain FB24). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=290399; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FB24; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., RA Nakatsu C.H., Richardson P.; RT "Complete sequence of chromosome 1 of Arthrobacter sp. FB24."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000454; ABK04161.1; -; Genomic_DNA. DR RefSeq; YP_832261.1; NC_008541.1. DR ProteinModelPortal; A0JYP1; -. DR STRING; 290399.Arth_2782; -. DR EnsemblBacteria; ABK04161; ABK04161; Arth_2782. DR GeneID; 4444528; -. DR KEGG; art:Arth_2782; -. DR PATRIC; 21000957; VBIArtSp72239_3162. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CVGPVHA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ASP290399:GHIF-2848-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 237 Thiamine-phosphate synthase. FT /FTId=PRO_0000336373. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 192 192 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 237 AA; 24338 MW; 4DFCE07699F306C2 CRC64; MTEQALLTDA RLYLCTDART DRGDFADFVD AAYAGGVDII QLRDKGLEAA EELELLEVLE TAARRHGRLW SVNDRADIAS LSGAPVLHVG QKDLPLASAR KFLGGEAVIG LSTHSHGQID AAIAASRGAG GLDYFCVGPV WATPTKPGRA AVGLELVRYA AEAAGKTTAK TTGGAAGPTV DGPRLPWFAI GGIDLGNVEQ VAAAGAERIV VVRAITEADD PAAAARSLLA ALDAGAS // ID THIE_AZOC5 Reviewed; 212 AA. AC A8IGE6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=AZC_0079; OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / ORS 571). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Azorhizobium. OX NCBI_TaxID=438753; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43989 / DSM 5975 / ORS 571; RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., RA Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., RA Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., RA Oyaizu H.; RT "Complete genome sequence of the nitrogen-fixing bacterium RT Azorhizobium caulinodans ORS571."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAF86077.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009384; BAF86077.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_001522995.1; NC_009937.1. DR ProteinModelPortal; A8IGE6; -. DR STRING; 438753.AZC_0079; -. DR EnsemblBacteria; BAF86077; BAF86077; AZC_0079. DR GeneID; 5690147; -. DR KEGG; azc:AZC_0079; -. DR PATRIC; 21016591; VBIAzoCau17976_0080. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ACAU438753:GJF3-79-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_0000336375. FT REGION 39 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 21630 MW; A2D17FFCFF8F1A91 CRC64; MPHPFDLSLY LVTDRRLTAE RGLLETVEEA VAGGVTLVQL RDPEAKGRAL AEEARALIGL LRPKGIPLII NDRVDVAAAV GAEGVHLGQD DLDPAAARAI LGPDAIIGLS VGSLEELSAS NLGPVDYVGC GPINATGTKG DAGGAIGIEG FAFLRSHIAL PMVGIGGLKA EDAEAVMQAG ANGIAVVSAL CAAPDVTEAA RTLKTIIETS RR // ID THIE_AZOSB Reviewed; 206 AA. AC A1KB60; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=azo3450; OS Azoarcus sp. (strain BH72). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azoarcus. OX NCBI_TaxID=62928; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BH72; RX PubMed=17057704; DOI=10.1038/nbt1243; RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.; RT "Complete genome of the mutualistic, N2-fixing grass endophyte RT Azoarcus sp. strain BH72."; RL Nat. Biotechnol. 24:1385-1391(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM406670; CAL96066.1; -; Genomic_DNA. DR RefSeq; YP_934952.1; NC_008702.1. DR ProteinModelPortal; A1KB60; -. DR STRING; 62928.azo3450; -. DR EnsemblBacteria; CAL96066; CAL96066; azo3450. DR GeneID; 4608987; -. DR KEGG; azo:azo3450; -. DR PATRIC; 21015352; VBIAzoSp26047_3494. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 206 Thiamine-phosphate synthase. FT /FTId=PRO_1000008121. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21204 MW; 6E28D91F7B7C5F5F CRC64; MGERIRGLYL VTPDAADSAT LLASVERVLP ARPALLQYRN KLADPLRQLD EARSLRQLCS SAGVPLIIND DVALARAVAA DGVHLGRDDG SPAAARAVLG ADALIGVSCY DEWVRAEDAA AAGADYVAFG AMFPSSTKPG AVRAPLTLLT RARAALDCPV AAIGGITLDN APALIEAGAD LLAVISDVFA AADPLQRALA YSALFA // ID THIE_AZOVD Reviewed; 209 AA. AC C1DMY6; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Avin_09270; OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=322710; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJ / ATCC BAA-1303; RX PubMed=19429624; DOI=10.1128/JB.00504-09; RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G., RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L., RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., RA Hernandez J.A., Houmiel K., Imperial J., Kennedy C., Larson T.J., RA Latreille P., Ligon L.S., Lu J., Maerk M., Miller N.M., Norton S., RA O'Carroll I.P., Paulsen I., Raulfs E.C., Roemer R., Rosser J., RA Segura D., Slater S., Stricklin S.L., Studholme D.J., Sun J., RA Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H., Dean D.R., RA Dixon R., Wood D.; RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe RT specialized to support diverse anaerobic metabolic processes."; RL J. Bacteriol. 191:4534-4545(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001157; ACO77166.1; -; Genomic_DNA. DR RefSeq; YP_002798141.1; NC_012560.1. DR ProteinModelPortal; C1DMY6; -. DR STRING; 322710.Avin_09270; -. DR EnsemblBacteria; ACO77166; ACO77166; Avin_09270. DR GeneID; 7759875; -. DR KEGG; avn:Avin_09270; -. DR PATRIC; 21028147; VBIAzoVin72790_0866. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AVIN322710:GJ0M-928-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_1000202747. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22295 MW; C12BA0B6B2206BAB CRC64; MKLRGLYAIT DSRLLADGRL LPYVEAALRG GARLLQYRDK SDEDARRLRE AEALRDLCLR YGAQLIVNDD LELAARLGVG LHLGQQDGSL SAARALLGPK AIIGATCHGQ LELAEQAAAD GASYLAFGRF FDSSTKPGAP PASLELLERA RARFPQPLVA IGGVTLDNAP ELIRRGAAMI AVINALFAAA NAAEVEQRAR AFGQLFADT // ID THIE_BACA2 Reviewed; 224 AA. AC A7ZA58; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=RBAM_035550; OS Bacillus amyloliquefaciens subsp. plantarum (strain DSM 23117 / BGSC OS 10A6 / FZB42). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=326423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23117 / BGSC 10A6 / FZB42; RX PubMed=17704766; DOI=10.1038/nbt1325; RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., RA Strittmatter A., Gottschalk G., Borriss R.; RT "Comparative analysis of the complete genome sequence of the plant RT growth-promoting bacterium Bacillus amyloliquefaciens FZB42."; RL Nat. Biotechnol. 25:1007-1014(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000560; ABS75884.1; -; Genomic_DNA. DR RefSeq; YP_001423115.1; NC_009725.1. DR ProteinModelPortal; A7ZA58; -. DR SMR; A7ZA58; 1-221. DR STRING; 326423.RBAM_035550; -. DR EnsemblBacteria; ABS75884; ABS75884; RBAM_035550. DR GeneID; 5462270; -. DR KEGG; bay:RBAM_035550; -. DR PATRIC; 18752320; VBIBacAmy31356_3606. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BAMY326423:GCM4-3552-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 224 Thiamine-phosphate synthase. FT /FTId=PRO_1000008122. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23810 MW; DB690E1E58202F2E CRC64; MTRISREMMK DMLSVYFIMG SNNTSADPVS VVEKAIEGGA TLFQFREKGS GSLTGEERLL FAKRVQDVCR QAGIPFIIND DVELALRLEA DGVHIGQDDA DAEETRAAIG DMILGVSAHN VSEVKRAEAA GADYVGMGPV YPTETKKDAE AVQGVTLIEE VRRQGITIPI VGIGGITADN AAPVIEAGAD GVSMISAISQ AEDPKAAARK FSEEIRRSKA GLSR // ID THIE_BACAA Reviewed; 219 AA. AC C3PBW1; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BAA_0440; OS Bacillus anthracis (strain A0248). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=592021; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A0248; RA Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., RA Sims D., Brettin T.; RT "Genome sequence of Bacillus anthracis A0248."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001598; ACQ50807.1; -; Genomic_DNA. DR RefSeq; YP_002864993.1; NC_012659.1. DR ProteinModelPortal; C3PBW1; -. DR SMR; C3PBW1; 1-215. DR STRING; 592021.BAA_0440; -. DR EnsemblBacteria; ACQ50807; ACQ50807; BAA_0440. DR GeneID; 7853024; -. DR KEGG; bai:BAA_0440; -. DR PATRIC; 18766615; VBIBacAnt132916_0682. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BANT592021:GJAQ-426-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000198071. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23600 MW; 6D85F0FE3EFD3046 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGFI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWVIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID THIE_BACAC Reviewed; 219 AA. AC C3L627; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BAMEG_0443; OS Bacillus anthracis (strain CDC 684 / NRRL 3495). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=568206; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 684 / NRRL 3495; RA Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., RA Han C., Sutton G., Sims D.; RT "Genome sequence of Bacillus anthracis str. CDC 684."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001215; ACP14865.1; -; Genomic_DNA. DR RefSeq; YP_002813055.1; NC_012581.1. DR ProteinModelPortal; C3L627; -. DR SMR; C3L627; 1-215. DR STRING; 568206.BAMEG_0443; -. DR EnsemblBacteria; ACP14865; ACP14865; BAMEG_0443. DR GeneID; 7783918; -. DR KEGG; bah:BAMEG_0443; -. DR PATRIC; 18790593; VBIBacAnt127120_0683. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BANT568206:GHVT-423-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000198072. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23600 MW; 6D85F0FE3EFD3046 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGFI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWVIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID THIE_BACAH Reviewed; 219 AA. AC A0R981; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BALH_0375; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=412694; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Al Hakam; RX PubMed=17337577; DOI=10.1128/JB.00241-07; RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Green L.D., Han C.S., Hill K.K., Hitchcock P., RA Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., RA Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., RA Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., RA Wills P.L., Gilna P., Brettin T.S.; RT "The complete genome sequence of Bacillus thuringiensis Al Hakam."; RL J. Bacteriol. 189:3680-3681(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000485; ABK83774.1; -; Genomic_DNA. DR RefSeq; YP_893281.1; NC_008600.1. DR ProteinModelPortal; A0R981; -. DR SMR; A0R981; 1-215. DR STRING; 412694.BALH_0375; -. DR EnsemblBacteria; ABK83774; ABK83774; BALH_0375. DR GeneID; 4542168; -. DR KEGG; btl:BALH_0375; -. DR PATRIC; 18992863; VBIBacThu63319_0478. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BTHU412694:GH1W-423-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000008123. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23498 MW; 72DA0EEF285CFD8A CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESSYESTKK LVEEVSRSL // ID THIE_BACAN Reviewed; 219 AA. AC Q81Z95; Q6I437; Q6KXU7; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 84. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BA_0377, GBAA_0377, BAS0363; OS Bacillus anthracis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames / isolate Porton; RX PubMed=12721629; DOI=10.1038/nature01586; RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L., RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., RA Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., RA Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., RA Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., RA Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., RA Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., RA Hanna P.C., Kolstoe A.-B., Fraser C.M.; RT "The genome sequence of Bacillus anthracis Ames and comparison to RT closely related bacteria."; RL Nature 423:81-86(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames ancestor; RX PubMed=18952800; DOI=10.1128/JB.01347-08; RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.; RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."; RL J. Bacteriol. 191:445-446(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sterne; RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., RA Richardson P., Rubin E., Tice H.; RT "Complete genome sequence of Bacillus anthracis Sterne."; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016879; AAP24407.1; -; Genomic_DNA. DR EMBL; AE017334; AAT29472.1; -; Genomic_DNA. DR EMBL; AE017225; AAT52694.1; -; Genomic_DNA. DR RefSeq; NP_842921.1; NC_003997.3. DR RefSeq; YP_016997.1; NC_007530.2. DR RefSeq; YP_026643.1; NC_005945.1. DR ProteinModelPortal; Q81Z95; -. DR SMR; Q81Z95; 1-215. DR IntAct; Q81Z95; 1. DR STRING; 198094.BA_0377; -. DR DNASU; 1084546; -. DR EnsemblBacteria; AAP24407; AAP24407; BA_0377. DR EnsemblBacteria; AAT29472; AAT29472; GBAA_0377. DR EnsemblBacteria; AAT52694; AAT52694; BAS0363. DR GeneID; 1084546; -. DR GeneID; 2819882; -. DR GeneID; 2853172; -. DR KEGG; ban:BA_0377; -. DR KEGG; bar:GBAA_0377; -. DR KEGG; bat:BAS0363; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ANTHRA:THIE-MONOMER; -. DR BioCyc; BANT260799:GJAJ-405-MONOMER; -. DR BioCyc; BANT261594:GJ7F-415-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_0000156991. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23600 MW; 6D85F0FE3EFD3046 CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGFI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWVIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID THIE_BACC0 Reviewed; 219 AA. AC B7JN72; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BCAH820_0420; OS Bacillus cereus (strain AH820). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405535; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AH820; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus AH820."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001283; ACK90198.1; -; Genomic_DNA. DR RefSeq; YP_002449412.1; NC_011773.1. DR ProteinModelPortal; B7JN72; -. DR STRING; 405535.BCAH820_0420; -. DR EnsemblBacteria; ACK90198; ACK90198; BCAH820_0420. DR GeneID; 7191953; -. DR KEGG; bcu:BCAH820_0420; -. DR PATRIC; 18837670; VBIBacCer122868_0392. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER405535:GHSL-430-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000117295. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23482 MW; D33A0EEF285CFD9C CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID THIE_BACC1 Reviewed; 224 AA. AC P61410; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 1. DT 14-MAY-2014, entry version 74. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BCE_0487; OS Bacillus cereus (strain ATCC 10987). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=222523; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10987; RX PubMed=14960714; DOI=10.1093/nar/gkh258; RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.; RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic RT adaptations and a large plasmid related to Bacillus anthracis pXO1."; RL Nucleic Acids Res. 32:977-988(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017194; AAS39422.1; -; Genomic_DNA. DR RefSeq; NP_976814.1; NC_003909.8. DR ProteinModelPortal; P61410; -. DR SMR; P61410; 1-220. DR STRING; 222523.BCE_0487; -. DR EnsemblBacteria; AAS39422; AAS39422; BCE_0487. DR GeneID; 2750967; -. DR KEGG; bca:BCE_0487; -. DR PATRIC; 18849826; VBIBacCer118379_0460. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 224 Thiamine-phosphate synthase. FT /FTId=PRO_0000156992. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24083 MW; 94574987749E9231 CRC64; MSRISKAEMS RLLSVYFIMG SNNCTKDPLQ ILKDALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQEDE GITSVREKMG DKIIGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKQ LVEEVSKKGT SHKY // ID THIE_BACC3 Reviewed; 219 AA. AC C1EVE6; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BCA_0455; OS Bacillus cereus (strain 03BB102). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=572264; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=03BB102; RA Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C., RA Tapia R., Han C., Sutton G., Sims D.; RT "Genome sequence of Bacillus cereus 03BB102."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001407; ACO31086.1; -; Genomic_DNA. DR RefSeq; YP_002747794.1; NC_012472.1. DR ProteinModelPortal; C1EVE6; -. DR STRING; 572264.BCA_0455; -. DR EnsemblBacteria; ACO31086; ACO31086; BCA_0455. DR GeneID; 7691057; -. DR KEGG; bcx:BCA_0455; -. DR PATRIC; 18814031; VBIBacCer84800_0375. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER572264:GH22-432-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000198073. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23556 MW; C298A06F6B321763 CRC64; MSRISKEEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESSYESTKK LVEEVSRSL // ID THIE_BACC4 Reviewed; 219 AA. AC B7H7H5; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BCB4264_A0440; OS Bacillus cereus (strain B4264). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405532; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4264; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus B4264."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001176; ACK64106.1; -; Genomic_DNA. DR RefSeq; YP_002365219.1; NC_011725.1. DR ProteinModelPortal; B7H7H5; -. DR STRING; 405532.BCB4264_A0440; -. DR EnsemblBacteria; ACK64106; ACK64106; BCB4264_A0440. DR GeneID; 7100820; -. DR KEGG; bcb:BCB4264_A0440; -. DR PATRIC; 18872843; VBIBacCer117876_0373. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER405532:GI1K-438-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000117296. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23601 MW; C59B2F0170EB9C21 CRC64; MARIEIDKMS KLLQVYFIMG SNNCTRDPLA VLKEALDGGV TIFQFREKGE GSLIGEDRVR FAKELQTLCK EYSVPFIVND DVELAIELDA DGVHVGQDDE GITSVREKMG DKIIGVSAHT IEEARFAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAY FREQGITVPI VGIGGITIEN TAAVIEAGAD GVSVISAISL AESAYESTRK LAEEVKRSL // ID THIE_BACC7 Reviewed; 219 AA. AC B7HT70; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BCAH187_A0487; OS Bacillus cereus (strain AH187). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405534; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AH187; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B., RA Okstad O.A., Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus AH187."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001177; ACJ81765.1; -; Genomic_DNA. DR RefSeq; YP_002336513.1; NC_011658.1. DR ProteinModelPortal; B7HT70; -. DR STRING; 405534.BCAH187_A0487; -. DR EnsemblBacteria; ACJ81765; ACJ81765; BCAH187_A0487. DR GeneID; 7078217; -. DR KEGG; bcr:BCAH187_A0487; -. DR PATRIC; 18826409; VBIBacCer120511_0721. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER405534:GHXM-463-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000117297. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23583 MW; 9EF4BB9B5967DB91 CRC64; MSRISKSEMS RLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTEEKRIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKR LVEEVSNSL // ID THIE_BACCN Reviewed; 217 AA. AC A7GKR4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Bcer98_0364; OS Bacillus cereus subsp. cytotoxis (strain NVH 391-98). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315749; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NVH 391-98; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., RA Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., RA Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., RA Weissenbach J., Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000764; ABS20722.1; -; Genomic_DNA. DR RefSeq; YP_001373717.1; NC_009674.1. DR ProteinModelPortal; A7GKR4; -. DR SMR; A7GKR4; 1-215. DR STRING; 315749.Bcer98_0364; -. DR EnsemblBacteria; ABS20722; ABS20722; Bcer98_0364. DR GeneID; 5344839; -. DR KEGG; bcy:Bcer98_0364; -. DR PATRIC; 18929012; VBIBacCyt128034_0394. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCYT315749:GH2A-434-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_1000075569. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23406 MW; 206A1C90EBF782E3 CRC64; MARIETEKMS QLLQVYFIMG SNNCHKGPLQ VMKEALDGGI TLFQFREKGE GALTGEKRVQ FAKQLQALCR EYRVPFIVND DVDLALKLDA DGVHVGQDDE GIEVVREKMG DKIVGVSAHT IEEAHFAIAN GADYLGIGPI FPTNTKKDTK AVQGLNGLRY FREKGINIPI VGIGGITIEN ASSVIEAGAD GVSVISAISL ASSAFDSAKA FVHQVKK // ID THIE_BACCQ Reviewed; 219 AA. AC B9J2L5; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BCQ_0462; OS Bacillus cereus (strain Q1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=361100; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Q1; RX PubMed=19060151; DOI=10.1128/JB.01629-08; RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., RA Xu X., Xue Y., Zhu Y., Jin Q.; RT "Complete genome sequence of the extremophilic Bacillus cereus strain RT Q1 with industrial applications."; RL J. Bacteriol. 191:1120-1121(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000227; ACM10934.1; -; Genomic_DNA. DR RefSeq; YP_002528226.1; NC_011969.1. DR ProteinModelPortal; B9J2L5; -. DR STRING; 361100.BCQ_0462; -. DR EnsemblBacteria; ACM10934; ACM10934; BCQ_0462. DR GeneID; 7377189; -. DR KEGG; bcq:BCQ_0462; -. DR PATRIC; 18908385; VBIBacCer120424_0407. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER361100:GJ7M-452-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000198074. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23583 MW; 9EF4BB9B5967DB91 CRC64; MSRISKSEMS RLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTEEKRIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GVSVISAISL AESAYESTKR LVEEVSNSL // ID THIE_BACCR Reviewed; 219 AA. AC Q81IG8; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 14-MAY-2014, entry version 78. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BC_0420; OS Bacillus cereus (strain ATCC 14579 / DSM 31). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., RA Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., RA Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., RA Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D., RA Overbeek R., Kyrpides N.C.; RT "Genome sequence of Bacillus cereus and comparative analysis with RT Bacillus anthracis."; RL Nature 423:87-91(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAP07460.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016877; AAP07460.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_830259.1; NC_004722.1. DR ProteinModelPortal; Q81IG8; -. DR SMR; Q81IG8; 2-217. DR STRING; 226900.BC0420; -. DR EnsemblBacteria; AAP07460; AAP07460; BC_0420. DR GeneID; 1202773; -. DR KEGG; bce:BC0420; -. DR PATRIC; 32596464; VBIBacCer54481_0389. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER226900:GJEU-422-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_0000156993. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23587 MW; 35CE2F0420BD7AC2 CRC64; MARIEIDKMS KLLQVYFIMG SNNCTRDPLA VLKEALDGGV TIFQFREKGE GSLIGEDRVR FAKELQTLCN EYSVPFIVND DVELAIELDA DGVHVGQDDE GITSVREKMG DKIIGVSAHT IEEARFAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAY FREQGITVPI VGIGGITIEN TAAVIEAGAD GVSVISAISL AESAYESTRK LAEEVKRSL // ID THIE_BACCZ Reviewed; 219 AA. AC Q63GK3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 68. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BCE33L0349; OS Bacillus cereus (strain ZK / E33L). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=288681; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZK / E33L; RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000001; AAU19890.1; -; Genomic_DNA. DR RefSeq; YP_081958.1; NC_006274.1. DR ProteinModelPortal; Q63GK3; -. DR SMR; Q63GK3; 1-215. DR STRING; 288681.BCZK0349; -. DR EnsemblBacteria; AAU19890; AAU19890; BCE33L0349. DR GeneID; 3025092; -. DR KEGG; bcz:BCZK0349; -. DR PATRIC; 18883980; VBIBacCer95304_0372. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCER288681:GHG7-397-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000008124. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23482 MW; 12F3284BF11177AD CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIIGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TASVIEAGAD GISVISAISL AESAYESTKK LVEEVSKSL // ID THIE_BACFN Reviewed; 204 AA. AC Q5LCA7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BF2558; OS Bacteroides fragilis (strain ATCC 25285 / NCTC 9343). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=272559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25285 / NCTC 9343; RX PubMed=15746427; DOI=10.1126/science.1107008; RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., RA Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., RA Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., RA Line A., Lord A., Norbertczak H., Ormond D., Price C., RA Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J.; RT "Extensive DNA inversions in the B. fragilis genome control variable RT gene expression."; RL Science 307:1463-1465(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR626927; CAH08258.1; -; Genomic_DNA. DR RefSeq; YP_212182.1; NC_003228.3. DR ProteinModelPortal; Q5LCA7; -. DR STRING; 272559.BF2558; -. DR EnsemblBacteria; CAH08258; CAH08258; BF9343_2477. DR GeneID; 3287400; -. DR KEGG; bfs:BF2558; -. DR PATRIC; 21041682; VBIBacFra29119_2568. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BFRA272559:GKF0-2513-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 204 Thiamine-phosphate synthase. FT /FTId=PRO_1000008125. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22047 MW; 234B20E4A19674DF CRC64; MLSLQFITHQ TENYSYLESA RMALEGGCKW IQLRMKEASP EEVEAVALQL KPLCKAKEAI LILDDHVELA KKLEVDGVHL GKKDMPIGEA RQMLGEAFII GGTANTFEDV KLHHAAGADY LGIGPFRFTT TKKNLSPVLG LEGYTSILAQ MNEAGIRIPV VAIGGIVAED IPAIMETGVN GIALSGAILQ APDPVEETKR ILNI // ID THIE_BACFR Reviewed; 204 AA. AC Q64TA1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BF2529; OS Bacteroides fragilis (strain YCH46). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=295405; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YCH46; RX PubMed=15466707; DOI=10.1073/pnas.0404172101; RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.; RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA RT inversions regulating cell surface adaptation."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006841; BAD49278.1; -; Genomic_DNA. DR RefSeq; YP_099812.1; NC_006347.1. DR ProteinModelPortal; Q64TA1; -. DR STRING; 295405.BF2529; -. DR EnsemblBacteria; BAD49278; BAD49278; BF2529. DR GeneID; 3083787; -. DR KEGG; bfr:BF2529; -. DR PATRIC; 21050677; VBIBacFra17906_2435. DR eggNOG; NOG287972; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 204 Thiamine-phosphate synthase. FT /FTId=PRO_1000008126. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22090 MW; 7BC369019F0674DC CRC64; MLSLQFITHQ TENYSYLESA RMALEGGCKW IQLRMKEASP EEVEAVALQL KPLCKAKEAI LILDDHVELA KKLEVDGVHL GKKDMPIGEA RQMLGEAFII GGTANTFEDV KLHHAAGADY LGIGPFRFTT TKINLSPVLG LEGYTSILAQ MNEADIRIPV VAIGGIVAED IPAIMETGVN GIALSGAILQ APDPVEETKR ILNI // ID THIE_BACHD Reviewed; 211 AA. AC Q9KCY8; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 14-MAY-2014, entry version 85. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BH1431; OS Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM OS 9153 / C-125). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=272558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125; RX PubMed=11058132; DOI=10.1093/nar/28.21.4317; RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., RA Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., RA Horikoshi K.; RT "Complete genome sequence of the alkaliphilic bacterium Bacillus RT halodurans and genomic sequence comparison with Bacillus subtilis."; RL Nucleic Acids Res. 28:4317-4331(2000). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000004; BAB05150.1; -; Genomic_DNA. DR PIR; G83828; G83828. DR RefSeq; NP_242297.1; NC_002570.2. DR ProteinModelPortal; Q9KCY8; -. DR STRING; 272558.BH1431; -. DR EnsemblBacteria; BAB05150; BAB05150; BAB05150. DR GeneID; 890782; -. DR KEGG; bha:BH1431; -. DR PATRIC; 18939955; VBIBacHal18977_1491. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BHAL272558:GJC5-1514-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000156994. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23151 MW; 86AAB506608D2D6E CRC64; MRDFRLYAIT GEEFHPDRSL QAVMEEAILG GVDIIQLRDK KSHKREVLEK ARVLQALAKK YDIPLIINDH IDVALAVDAD GIHLGQDDLP LSEARKIMGR DKIIGISTHK IEEAREAEKG GADYIGVGPI FETKSKEDVV DPVTTAYIQQ VAHEISIPFV AIGGIKLHNV EQVLDAGATR ICMISEIVGA EDVKGTCEVF STILEQRGIG S // ID THIE_BACHK Reviewed; 219 AA. AC Q6HP17; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 71. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BT9727_0353; OS Bacillus thuringiensis subsp. konkukian (strain 97-27). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=281309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27; RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017355; AAT61239.1; -; Genomic_DNA. DR RefSeq; YP_034703.1; NC_005957.1. DR ProteinModelPortal; Q6HP17; -. DR SMR; Q6HP17; 1-215. DR STRING; 281309.BT9727_0353; -. DR EnsemblBacteria; AAT61239; AAT61239; BT9727_0353. DR GeneID; 2855110; -. DR KEGG; btk:BT9727_0353; -. DR PATRIC; 18981203; VBIBacThu119411_0375. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BTHU281309:GJID-413-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000008127. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23508 MW; D33A0EEF3BE4C60C CRC64; MSRISKAEMS KLLSVYFIMG SNNCTKDPLQ VLREALEGGI TIFQFREKGE GALTGEERIC FAKELQAICK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIVGVSTHT IEEARWAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITIPI VGIGGISIEN TALVIEAGAD GVSVISAISL AESAYESTKK LVEEVSRSL // ID THIE_BACLD Reviewed; 224 AA. AC Q65DK0; Q62P20; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 75. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BLi04051, BL03866; OS Bacillus licheniformis (strain DSM 13 / ATCC 14580). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13 / ATCC 14580; RX PubMed=15383718; DOI=10.1159/000079829; RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., RA Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., RA Ehrenreich A., Gottschalk G.; RT "The complete genome sequence of Bacillus licheniformis DSM13, an RT organism with great industrial potential."; RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13 / ATCC 14580; RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., RA Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., RA Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., RA Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:R77.1-R77.12(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000002; AAU25491.1; -; Genomic_DNA. DR EMBL; AE017333; AAU42864.1; -; Genomic_DNA. DR RefSeq; YP_006715328.1; NC_006322.1. DR RefSeq; YP_081129.1; NC_006270.3. DR ProteinModelPortal; Q65DK0; -. DR SMR; Q65DK0; 1-219. DR STRING; 279010.BL03866; -. DR EnsemblBacteria; AAU25491; AAU25491; BL03866. DR EnsemblBacteria; AAU42864; AAU42864; BLi04051. DR GeneID; 3030322; -. DR GeneID; 3097679; -. DR KEGG; bld:BLi04051; -. DR KEGG; bli:BL03866; -. DR PATRIC; 18953912; VBIBacLic203714_4131. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BLIC279010:GJ2P-4006-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 224 Thiamine-phosphate synthase. FT /FTId=PRO_1000008128. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23650 MW; 38CCB4D4F480C6E1 CRC64; MTRVSEEAMK DLLSVYFIMG SNNTAGDPLT VIEKALKGGA TLFQFREKGE GALKAGDQTA FARQVQALCK QFNVPFIIND DVELALELDA DGVHIGQDDD KAADVRARIG DKILGVSAHT LEEVLKAEKD GADYIGAGPV YPTETKRDTK AVQGVSLIQE IRRQGIGIPV VGIGGITVEN CVPVIEAGAD GISVISAISK AADPKQAAEA FSEKVQATKQ SAHS // ID THIE_BACP2 Reviewed; 222 AA. AC A8FIR6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BPUM_3483; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=315750; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., RA Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C., RA Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., RA Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., RA Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., RA Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., RA Venkateswaran K., Highlander S.K., Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000813; ABV64133.1; -; Genomic_DNA. DR RefSeq; YP_001488693.1; NC_009848.1. DR ProteinModelPortal; A8FIR6; -. DR SMR; A8FIR6; 1-219. DR STRING; 315750.BPUM_3483; -. DR EnsemblBacteria; ABV64133; ABV64133; BPUM_3483. DR GeneID; 5622778; -. DR KEGG; bpu:BPUM_3483; -. DR PATRIC; 18970936; VBIBacPum16546_3537. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPUM315750:GH6N-3565-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 222 Thiamine-phosphate synthase. FT /FTId=PRO_1000057640. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23959 MW; CF489DA17D854202 CRC64; MTKTDQQQIK QQLSVYFIMG TANTSRQPLD VLKEAIQGGI TMFQFREKGE GALQGEEKKQ LARQLQVLCQ EANVPFVVND DVQLAIDLDA DGVHVGQEDT NAEDVRQKIG DKILGVSTHN LDEVKQAMKD GADYVGMGPV YPTETKKDTR SVQGVSLITE VRHHGLHIPI VGIGGIAYDN AAPVIQAGAD GISIISAISQ SADPKKAAEE LRALVTSEKA LL // ID THIE_BACSK Reviewed; 209 AA. AC Q5WH87; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=ABC1733; OS Bacillus clausii (strain KSM-K16). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=66692; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16; RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., RA Kawai S., Ito S., Horikoshi K.; RT "The complete genome sequence of the alkaliphilic Bacillus clausii RT KSM-K16."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006627; BAD64268.1; -; Genomic_DNA. DR RefSeq; YP_175229.1; NC_006582.1. DR ProteinModelPortal; Q5WH87; -. DR STRING; 66692.ABC1733; -. DR EnsemblBacteria; BAD64268; BAD64268; ABC1733. DR GeneID; 3203412; -. DR KEGG; bcl:ABC1733; -. DR PATRIC; 18922958; VBIBacCla58185_1842. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BCLA66692:GHMP-1801-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_1000008129. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22579 MW; AE476A39A5AE238A CRC64; MKPFRLYAIT GEEFHPGRDV VEVMEEAIQG GVDIIQLRDK TSSKKAVLEK ARRLKKLAAD YGIPFIVNDH IDVALAVDAS GVHVGQDDLP LPEVRKLLGP DKIIGVSTHK LEEALEAEKN GADYIGVGPI FPTNSKADVV DPVTTAYIRE VKEHVTIPFV AIGGIKRHNV REVIEAGAEA ICVITEIVAA RDVKAASQAL LAAMEEASQ // ID THIE_BACSU Reviewed; 222 AA. AC P39594; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 14-MAY-2014, entry version 113. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; Synonyms=thiC, ywbK; OrderedLocusNames=BSU38290; GN ORFNames=ipa-26d; OS Bacillus subtilis (strain 168). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x; RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., RA Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I., RA Presecan E., Santana M., Schneider E., Schweizer J., Vertes A., RA Rapoport G., Danchin A.; RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb RT region from 325 degrees to 333 degrees."; RL Mol. Microbiol. 10:371-384(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, KINETIC PARAMETERS, AND RP INDUCTION. RC STRAIN=168 / CU1065; RX PubMed=9139923; RA Zhang Y., Taylor S.V., Chiu H.-J., Begley T.P.; RT "Characterization of the Bacillus subtilis thiC operon involved in RT thiamine biosynthesis."; RL J. Bacteriol. 179:3030-3035(1997). RN [4] RP FUNCTION, SUBSTRATE SPECIFICITY, MUTAGENESIS OF SER-117, AND REACTION RP MECHANISM. RC STRAIN=168 / CU1065; RX PubMed=11513588; DOI=10.1021/bi010267q; RA Reddick J.J., Nicewonger R., Begley T.P.; RT "Mechanistic studies on thiamin phosphate synthase: evidence for a RT dissociative mechanism."; RL Biochemistry 40:10095-10102(2001). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH THIAMINE RP PHOSPHATE AND MAGNESIUM PYROPHOSPHATE. RC STRAIN=168 / CU1065; RX PubMed=10350464; DOI=10.1021/bi982903z; RA Chiu H.-J., Reddick J.J., Begley T.P., Ealick S.E.; RT "Crystal structure of thiamin phosphate synthase from Bacillus RT subtilis at 1.25 A resolution."; RL Biochemistry 38:6460-6470(1999). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-117 RP IN COMPLEXES WITH SUBSTRATE; PRODUCTS AND INTERMEDIATES. RC STRAIN=168 / CU1065; RX PubMed=11513589; DOI=10.1021/bi0104726; RA Peapus D.H., Chiu H.J., Campobasso N., Reddick J.J., Begley T.P., RA Ealick S.E.; RT "Structural characterization of the enzyme-substrate, enzyme- RT intermediate, and enzyme-product complexes of thiamin phosphate RT synthase."; RL Biochemistry 40:10103-10114(2001). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS). RA McCulloch K.M., Hanes J.W., Abdelwahed S., Mahanta N., Hazra A., RA Ishida K., Begley T.P., Ealick S.E.; RT "Crystal structure and kinetic characterization of Bacillus subtilis RT thiamin phosphate synthase with a carboxylated thiazole phosphate."; RL Submitted (JUL-2011) to the PDB data bank. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP). Is also able to use the 2-methoxy analog MeO-HMP-PP, as CC substrate in vitro, but not the 2-trifluoromethyl analog CF(3)- CC HMP-PP. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.7 uM for HMP-PP; CC KM=1.2 uM for THZ-P; CC Vmax=0.7 umol/min/mg enzyme; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SUBUNIT: Monomer. CC -!- INDUCTION: Is weakly repressed by THZ and not at all by thiamine. CC -!- MISCELLANEOUS: Thiamine phosphate synthase appears to proceed with CC a dissociative mechanism (SN1 like) in which the pyrimidine CC pyrophosphate dissociates to give a reactive pyrimidine CC intermediate which is then trapped by the thiazole moiety. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X73124; CAA51582.1; -; Genomic_DNA. DR EMBL; AL009126; CAB15855.1; -; Genomic_DNA. DR PIR; S39681; S39681. DR RefSeq; NP_391708.1; NC_000964.3. DR PDB; 1G4E; X-ray; 1.60 A; A/B=1-222. DR PDB; 1G4P; X-ray; 2.50 A; A/B=1-222. DR PDB; 1G4S; X-ray; 1.70 A; A/B=1-222. DR PDB; 1G4T; X-ray; 1.55 A; A/B=1-222. DR PDB; 1G67; X-ray; 1.40 A; A/B=1-222. DR PDB; 1G69; X-ray; 1.50 A; A/B=1-222. DR PDB; 1G6C; X-ray; 1.40 A; A/B=1-222. DR PDB; 2TPS; X-ray; 1.25 A; A/B=1-222. DR PDB; 3O15; X-ray; 1.95 A; A=1-222. DR PDB; 3O16; X-ray; 2.10 A; A=1-222. DR PDBsum; 1G4E; -. DR PDBsum; 1G4P; -. DR PDBsum; 1G4S; -. DR PDBsum; 1G4T; -. DR PDBsum; 1G67; -. DR PDBsum; 1G69; -. DR PDBsum; 1G6C; -. DR PDBsum; 2TPS; -. DR PDBsum; 3O15; -. DR PDBsum; 3O16; -. DR ProteinModelPortal; P39594; -. DR SMR; P39594; 1-222. DR STRING; 224308.BSU38290; -. DR PaxDb; P39594; -. DR EnsemblBacteria; CAB15855; CAB15855; BSU38290. DR GeneID; 937316; -. DR KEGG; bsu:BSU38290; -. DR PATRIC; 18979704; VBIBacSub10457_4014. DR GenoList; BSU38290; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BSUB:BSU38290-MONOMER; -. DR BioCyc; MetaCyc:BSU38290-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR EvolutionaryTrace; P39594; -. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Magnesium; Metal-binding; KW Reference proteome; Thiamine biosynthesis; Transferase. FT CHAIN 1 222 Thiamine-phosphate synthase. FT /FTId=PRO_0000156995. FT REGION 44 48 HMP-PP binding. FT REGION 143 145 THZ-P binding. FT REGION 195 196 THZ-P binding. FT METAL 80 80 Magnesium. FT METAL 99 99 Magnesium. FT BINDING 79 79 HMP-PP. FT BINDING 117 117 HMP-PP. FT BINDING 146 146 HMP-PP. FT BINDING 175 175 THZ-P; via amide nitrogen. FT MUTAGEN 117 117 S->A: 8000-fold reduction in catalytic FT activity. FT HELIX 6 12 FT STRAND 15 19 FT HELIX 21 23 FT HELIX 28 38 FT STRAND 41 45 FT HELIX 55 72 FT STRAND 76 80 FT HELIX 82 88 FT STRAND 91 95 FT STRAND 97 99 FT HELIX 102 109 FT STRAND 112 118 FT HELIX 121 130 FT STRAND 133 137 FT STRAND 145 148 FT HELIX 156 163 FT STRAND 170 175 FT TURN 178 180 FT HELIX 182 186 FT STRAND 190 195 FT HELIX 196 199 FT STRAND 201 203 FT HELIX 204 221 SQ SEQUENCE 222 AA; 23681 MW; BF09EB73866F4FB4 CRC64; MTRISREMMK ELLSVYFIMG SNNTKADPVT VVQKALKGGA TLYQFREKGG DALTGEARIK FAEKAQAACR EAGVPFIVND DVELALNLKA DGIHIGQEDA NAKEVRAAIG DMILGVSAHT MSEVKQAEED GADYVGLGPI YPTETKKDTR AVQGVSLIEA VRRQGISIPI VGIGGITIDN AAPVIQAGAD GVSMISAISQ AEDPESAARK FREEIQTYKT GR // ID THIE_BACTN Reviewed; 209 AA. AC Q8AA13; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 80. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BT_0652; OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC OS 10582 / E50 / VPI-5482). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=226186; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482; RX PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., RA Chiang H.C., Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015928; AAO75759.1; -; Genomic_DNA. DR RefSeq; NP_809565.1; NC_004663.1. DR ProteinModelPortal; Q8AA13; -. DR STRING; 226186.BT_0652; -. DR EnsemblBacteria; AAO75759; AAO75759; BT_0652. DR GeneID; 1072399; -. DR KEGG; bth:BT_0652; -. DR PATRIC; 21056073; VBIBacThe70966_0663. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; MKEANIE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BTHE226186:GJXV-654-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_0000156996. FT REGION 32 36 HMP-PP binding (By similarity). FT REGION 129 131 THZ-P binding (By similarity). FT METAL 65 65 Magnesium (By similarity). FT METAL 84 84 Magnesium (By similarity). FT BINDING 64 64 HMP-PP (By similarity). FT BINDING 103 103 HMP-PP (By similarity). FT BINDING 132 132 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23050 MW; 26723EDA3597CA8E CRC64; MVSLQFITHQ TDRYTYFESA LMALEGGCKW IQLRMKEAPC EEVEAVALQL KPLCKEKEAI LLLDDHVELA KKLEVDGVHL GKKDMPIDQA RQLLGEAFII GGTANTFEDV VQHYRAGADY LGIGPFRFTT TKKNLSPVLG LEGYTAILSQ MKEANIELPV VAIGGITRED IPAILETGVN GIALSGTILR AEDPAAETRK ILNMKRIIK // ID THIE_BACV8 Reviewed; 208 AA. AC A6L645; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BVU_3541; OS Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=435590; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8482 / DSM 1447 / NCTC 11154; RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156; RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., RA Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., RA Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., RA Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.; RT "Evolution of symbiotic bacteria in the distal human intestine."; RL PLoS Biol. 5:1574-1586(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000139; ABR41159.1; -; Genomic_DNA. DR RefSeq; YP_001300781.1; NC_009614.1. DR ProteinModelPortal; A6L645; -. DR STRING; 435590.BVU_3541; -. DR EnsemblBacteria; ABR41159; ABR41159; BVU_3541. DR GeneID; 5304501; -. DR KEGG; bvu:BVU_3541; -. DR PATRIC; 21072138; VBIBacVul85104_3644. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BVUL435590:GH96-3532-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 208 Thiamine-phosphate synthase. FT /FTId=PRO_0000336376. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 23064 MW; 79EB40A5EE664EDA CRC64; MEDKTVELQF ITHFTDTYSY YDSARMALEG GCRWIQLRMK DTPVDEVERE AIRLQGLCKD YGATFVIDDH VELVKKIHAD GVHLGKKDMP VAEARGILGK EFIIGGTANT FDDVKMHYKA GADYIGCGPF RFTTTKKDLS PVLGLEGYRS IILQMKEANI HLPIVAIGGI TLEDIPSIME TGITGIALSG TILRAKDPVA ETKRIMNL // ID THIE_BACWK Reviewed; 219 AA. AC A9VRN4; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BcerKBAB4_0358; OS Bacillus weihenstephanensis (strain KBAB4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KBAB4; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., RA Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., RA Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., RA Weissenbach J., Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000903; ABY41624.1; -; Genomic_DNA. DR RefSeq; YP_001643252.1; NC_010184.1. DR ProteinModelPortal; A9VRN4; -. DR SMR; A9VRN4; 1-215. DR STRING; 315730.BcerKBAB4_0358; -. DR EnsemblBacteria; ABY41624; ABY41624; BcerKBAB4_0358. DR GeneID; 5840528; -. DR KEGG; bwe:BcerKBAB4_0358; -. DR PATRIC; 19005120; VBIBacWei55973_0924. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BWEI315730:GHRU-431-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000093660. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23481 MW; FD9A0C103BE9AC34 CRC64; MPRITKAEMS RLLPVYFIMG SNNCTKEPLQ VLRDALEGGI TIFQLREKGE GALTGEKRID FAKELQALCK EYGVPFIVND DVELALELDA DGVHVGQDDE GITSVREKMG DKIIGVSAHT IEEARFAIEN GADYLGVGPI FPTSTKKDTK AVQGTKGLAH FREQGITMPI VGIGGITIEN TAAVIEAGAD GVSVISAISL AESAYESTRK LAEEVNKSL // ID THIE_BORA1 Reviewed; 216 AA. AC Q2KUS6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 57. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BAV3015; OS Bordetella avium (strain 197N). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=360910; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=197N; RX PubMed=16885469; DOI=10.1128/JB.01927-05; RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., RA King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., RA Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., RA Squares S., Woodward J., Parkhill J., Temple L.M.; RT "Comparison of the genome sequence of the poultry pathogen Bordetella RT avium with those of B. bronchiseptica, B. pertussis, and B. RT parapertussis reveals extensive diversity in surface structures RT associated with host interaction."; RL J. Bacteriol. 188:6002-6015(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM167904; CAJ50625.1; -; Genomic_DNA. DR RefSeq; YP_787510.1; NC_010645.1. DR ProteinModelPortal; Q2KUS6; -. DR STRING; 360910.BAV3015; -. DR GeneID; 6267799; -. DR KEGG; bav:BAV3015; -. DR PATRIC; 21132341; VBIBorAvi43433_3049. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BAVI360910:GCKI-3089-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 216 Thiamine-phosphate synthase. FT /FTId=PRO_1000008130. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22339 MW; 4D954AD12F5B7161 CRC64; MNTLRFPAGL YGVTPEWDDT SRLLAAVRDA AAGGMRALQL RRKHLSREQR LLQARALAPL CRELGVTFIV NDDWRTALEA GADGAHIGRD DATLAEVRAA APGLLLGVSC YADLNRAREL LAQGADYIAF GAVFPSPTKP QAAHAPLALL GEAAAQVRAC GEPRPAVVAI GGITPANAGL VAAAGADSIA VITGLFEAPD IRAAAQACAA PFPLTD // ID THIE_BORBR Reviewed; 217 AA. AC Q7WF72; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BB4408; OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) OS (Alcaligenes bronchisepticus). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX640450; CAE34771.1; -; Genomic_DNA. DR RefSeq; NP_890942.1; NC_002927.3. DR ProteinModelPortal; Q7WF72; -. DR STRING; 257310.BB4408; -. DR EnsemblBacteria; CAE34771; CAE34771; BB4408. DR GeneID; 2660526; -. DR KEGG; bbr:BB4408; -. DR PATRIC; 21142275; VBIBorBro124907_4483. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BBRO257310:BB4408-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_0000156997. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22357 MW; 71DD7E467DE564AB CRC64; MKTLRFPAGL YGITPEWDDT DRLLAAVRAA AAGGMTALQL RRKLADERLR AAQARALAPL CRELGVVFLV NDHWKLALDV GADGAHLGRD DADPATVRAQ AGAGLLLGVS CYNDLRRADA LLAAGADYVA FGTVFASPTK PEAVHAPLQT LTEARARLLA CPAPRPAVVA IGGITPANVS QVAQAGADSA AVISGLFEAP DIQAAARACA AAFSVNP // ID THIE_BORPA Reviewed; 217 AA. AC Q7W3U2; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BPP3935; OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257311; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX640435; CAE39218.1; -; Genomic_DNA. DR RefSeq; NP_886085.1; NC_002928.3. DR ProteinModelPortal; Q7W3U2; -. DR STRING; 257311.BPP3935; -. DR EnsemblBacteria; CAE39218; CAE39218; BPP3935. DR GeneID; 1666452; -. DR KEGG; bpa:BPP3935; -. DR PATRIC; 21151944; VBIBorPar43418_4130. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPAR257311:BPP3935-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_0000156998. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22343 MW; 71DD7E5C67E57EB1 CRC64; MKTLRFPAGL YGITPEWDDT DRLLAAVRAA AAGGMTALQL RRKLADERLR AAQARALAPL CRELGVVFLV NDHWKLALDV GADGAHLGRD DADPATVRAQ AGAGLLLGVS CYNDLRRADA LLAAGADYVA FGTVFASPTK PEAVHAPLQT LTEARARVLA CPAPRPAVVA IGGITPANVS QVAQAGADSA AVISGLFEAP DIQAAARACA AAFSVNP // ID THIE_BORPE Reviewed; 217 AA. AC Q7W049; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 14-MAY-2014, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BP0316; OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257313; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX640411; CAE40693.1; -; Genomic_DNA. DR RefSeq; NP_879191.1; NC_002929.2. DR ProteinModelPortal; Q7W049; -. DR STRING; 257313.BP0316; -. DR EnsemblBacteria; CAE40693; CAE40693; BP0316. DR GeneID; 2664389; -. DR KEGG; bpe:BP0316; -. DR PATRIC; 21153670; VBIBorPer7866_0342. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BPER257313:BP0316-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_0000156999. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22343 MW; 71DD7E5C67E57EB1 CRC64; MKTLRFPAGL YGITPEWDDT DRLLAAVRAA AAGGMTALQL RRKLADERLR AAQARALAPL CRELGVVFLV NDHWKLALDV GADGAHLGRD DADPATVRAQ AGAGLLLGVS CYNDLRRADA LLAAGADYVA FGTVFASPTK PEAVHAPLQT LTEARARVLA CPAPRPAVVA IGGITPANVS QVAQAGADSA AVISGLFEAP DIQAAARACA AAFSVNP // ID THIE_CALMQ Reviewed; 205 AA. AC A8M9N4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Cmaq_0061; OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 OS / IC-167). OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Caldivirga. OX NCBI_TaxID=397948; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., RA Lowe T.M., Saltikov C., House C.H., Richardson P.; RT "Complete sequence of Caldivirga maquilingensis IC-167."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000852; ABW00915.1; -; Genomic_DNA. DR RefSeq; YP_001539905.1; NC_009954.1. DR ProteinModelPortal; A8M9N4; -. DR STRING; 397948.Cmaq_0061; -. DR EnsemblBacteria; ABW00915; ABW00915; Cmaq_0061. DR GeneID; 5710154; -. DR KEGG; cma:Cmaq_0061; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; CMAQ397948:GH9M-61-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_1000075570. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22057 MW; 1090E97CEC897DDF CRC64; MRLPKGIYGI TDDSYNVKNH VDAAKVFLEG GVRIIQYRRK EGSIRQMLNE AKEIRKLCNQ YGAVMIVDDR VDIAVLSDAD GVHVGLEDAP VDEVKRRFSG IIIGASASTV DEAKEGEKAG ADYLGAGSIF PSPTKPDYRI LGLEGLRRVV QSVSIPVYAI GGVTLESIPA IKATGAWGAA VISGILAAKD PLEMAKRFVK AWDEA // ID THIE_CALS8 Reviewed; 221 AA. AC A4XG66; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2012, sequence version 2. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Csac_0254; OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=351627; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43494 / DSM 8903; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., RA van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., RA Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., RA Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., RA Richardson P.; RT "Genome sequence of the thermophilic hydrogen-producing bacterium RT Caldicellulosiruptor saccharolyticus DSM 8903."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000679; ABP65901.2; -; Genomic_DNA. DR RefSeq; YP_001179092.2; NC_009437.1. DR STRING; 351627.Csac_0254; -. DR EnsemblBacteria; ABP65901; ABP65901; Csac_0254. DR GeneID; 5087019; -. DR KEGG; csc:Csac_0254; -. DR PATRIC; 21249912; VBICalSac56748_0295. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR BioCyc; CSAC351627:GJ17-259-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 221 Thiamine-phosphate synthase. FT /FTId=PRO_0000336377. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 24930 MW; 78E73DF672749C97 CRC64; MSLSKEEKLQ LFKSYNIYGL TAEKFSNGRS NIEVVKAMLE SGIKIIQYRE KHKSLKEKYE ECLQIRELTK QYGALLIVND HVDLCQMVGA DGVHLGQEDY PAKEVRKILG EDFIIGVTTH TKEQVEKAVE DGADYIGLGP VFQSFTKDKP HPPIGLEMVR WAATYCKIPF VAIGGIKEHN LKDVLKAGAK CVSLVTEIVG SDDISQKIKK LWDIIKEFER S // ID THIE_CAMJ8 Reviewed; 210 AA. AC A8FMD4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=C8J_1022; OS Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC OS 11828). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=407148; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=81116 / NCTC 11828; RX PubMed=17873037; DOI=10.1128/JB.01404-07; RA Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., RA Nuijten P.J.M., van Vliet A.H.M.; RT "The complete genome sequence of Campylobacter jejuni strain 81116 RT (NCTC11828)."; RL J. Bacteriol. 189:8402-8403(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000814; ABV52621.1; -; Genomic_DNA. DR RefSeq; YP_001482598.1; NC_009839.1. DR ProteinModelPortal; A8FMD4; -. DR STRING; 407148.C8J_1022; -. DR EnsemblBacteria; ABV52621; ABV52621; C8J_1022. DR GeneID; 5617642; -. DR KEGG; cju:C8J_1022; -. DR PATRIC; 20055676; VBICamJej119085_1032. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CJEJ407148:GHCS-1057-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_1000071283. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22980 MW; 25138187D1AAA731 CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKAVLD ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLPLK // ID THIE_CAMJE Reviewed; 210 AA. AC Q9PNL3; Q0P9H3; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 14-MAY-2014, entry version 87. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Cj1081c; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., RA Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., RA Whitehead S., Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL111168; CAL35198.1; -; Genomic_DNA. DR PIR; D81311; D81311. DR RefSeq; YP_002344474.1; NC_002163.1. DR ProteinModelPortal; Q9PNL3; -. DR IntAct; Q9PNL3; 40. DR STRING; 192222.Cj1081c; -. DR EnsemblBacteria; CAL35198; CAL35198; Cj1081c. DR GeneID; 905372; -. DR KEGG; cje:Cj1081c; -. DR PATRIC; 20059120; VBICamJej33762_1063. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CJEJ192222:GJTS-1054-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_0000157000. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23001 MW; 753C83D43B0EB44A CRC64; MKNKLDLSLY LVATKGSKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID THIE_CAMJJ Reviewed; 210 AA. AC A1W068; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CJJ81176_1099; OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=354242; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=81-176; RA Fouts D.E., Nelson K.E., Sebastian Y.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000538; EAQ72046.1; -; Genomic_DNA. DR RefSeq; YP_001000759.1; NC_008787.1. DR ProteinModelPortal; A1W068; -. DR STRING; 354242.CJJ81176_1099; -. DR EnsemblBacteria; EAQ72046; EAQ72046; CJJ81176_1099. DR GeneID; 4683371; -. DR KEGG; cjj:CJJ81176_1099; -. DR PATRIC; 20052171; VBICamJej103413_1098. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CJEJ354242:GC51-1075-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_1000008131. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22980 MW; 25138187D1AAA731 CRC64; MKNKLDLSLY LVASQGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKAYKIPFLI NDRVDIALAL DADGVHLGQE DLEVKLARKL LGDEKIIGLS LKKLEQLEFI QGANYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGVDKAVLD ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLPLK // ID THIE_CAMJR Reviewed; 210 AA. AC Q5HU23; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CJE1224; OS Campylobacter jejuni (strain RM1221). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=195099; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM1221; RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015; RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., RA Nelson K.E.; RT "Major structural differences and novel potential virulence mechanisms RT from the genomes of multiple Campylobacter species."; RL PLoS Biol. 3:72-85(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000025; AAW35546.1; -; Genomic_DNA. DR RefSeq; YP_179212.1; NC_003912.7. DR ProteinModelPortal; Q5HU23; -. DR STRING; 195099.CJE1224; -. DR EnsemblBacteria; AAW35546; AAW35546; CJE1224. DR GeneID; 3231731; -. DR KEGG; cjr:CJE1224; -. DR PATRIC; 20044244; VBICamJej134361_1240. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VTDRTLC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CJEJ195099:GJC0-1250-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_0000157001. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23028 MW; 6F1E4B2FF82C7CBA CRC64; MKNKLDLSLY LVATKGNKSE ECFLNTLENA IKGGVSIIQL REKELNAREF YKLGLKVQKL CKSYKIPFLI NDRVDIALAL DADGVHLGQE DLEAKLARKL LGDEKIIGLS LKKLEQLEFI QGVNYLGCGA IKATPTKESS LLSLELLSQI CDKSPIGVVA IGGIDKEALV ELKGINLSGV AVVRAIMDAK DAFLAAKELK RKIYENLSLK // ID THIE_CAUSK Reviewed; 219 AA. AC B0SUK3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Caul_0750; OS Caulobacter sp. (strain K31). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=366602; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K31; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., RA Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Stephens C., Richardson P.; RT "Complete sequence of chromosome of Caulobacter sp. K31."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000927; ABZ69881.1; -; Genomic_DNA. DR RefSeq; YP_001682379.1; NC_010338.1. DR ProteinModelPortal; B0SUK3; -. DR STRING; 366602.Caul_0750; -. DR EnsemblBacteria; ABZ69881; ABZ69881; Caul_0750. DR GeneID; 5898204; -. DR KEGG; cak:Caul_0750; -. DR PATRIC; 21314480; VBICauSp18104_1111. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CSP366602:GH0Y-751-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000117298. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 22280 MW; A4AF597E421E1420 CRC64; MTDCRLYLIT PPALDDLAAF GHDLAAALDG GDVAALQIRL KDAPDDIIAA AVQVLSPIAR ARDVAVILND RPDLAARLGC DGVHLGQDDM PLAQARKLMG PGAMIGVTCH DSRHLAMEAA EAGADYVAFG AFFPTTTKDA PTTADPEILS IWQETMEIPS VAIGGITADN AAGLAAAGAD FLAVSAGVWK HPQGPAAGVA AINAAIAQGL EARLAARGG // ID THIE_CHLAA Reviewed; 216 AA. AC A9WDL8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Caur_0374; OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl). OC Bacteria; Chloroflexi; Chloroflexales; Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=324602; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl; RX PubMed=21714912; DOI=10.1186/1471-2164-12-334; RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J., RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W., RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.; RT "Complete genome sequence of the filamentous anoxygenic phototrophic RT bacterium Chloroflexus aurantiacus."; RL BMC Genomics 12:334-334(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000909; ABY33624.1; -; Genomic_DNA. DR RefSeq; YP_001634013.1; NC_010175.1. DR ProteinModelPortal; A9WDL8; -. DR STRING; 324602.Caur_0374; -. DR EnsemblBacteria; ABY33624; ABY33624; Caur_0374. DR GeneID; 5825777; -. DR KEGG; cau:Caur_0374; -. DR PATRIC; 21411284; VBIChlAur28763_0426. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CAUR324602:GIXU-378-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 216 Thiamine-phosphate synthase. FT /FTId=PRO_0000336379. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22596 MW; 28BE1FA1C780A5FE CRC64; MSIAHIVDWR LYVVTDAGLS RGRSHRAVIE AAIVGGATVV QYREKHASTR QMIEEALELR DLTRRAGVPL IVNDRVDVAL AVDADGVHVG QDDMPVALAR RLIGNKLLGV SAHNLSEALQ AVRDGADYLG VGPIFATTTK PDAAAPIGLD GLRAIRQHVS IPIVAIGGIN QANAADVMRA GADGIAVVSA VVAADDVTAA ARQLRALVSV TQEKAL // ID THIE_CHLAB Reviewed; 212 AA. AC Q5L6R5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 1. DT 14-MAY-2014, entry version 59. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CAB198; OS Chlamydophila abortus (strain DSM 27085 / S26/3). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydophila. OX NCBI_TaxID=218497; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 27085 / S26/3; RX PubMed=15837807; DOI=10.1101/gr.3684805; RA Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D., RA Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., RA Ormond D., Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., RA Quail M.A., Price C., Barrell B.G., Parkhill J., Longbottom D.; RT "The Chlamydophila abortus genome sequence reveals an array of RT variable proteins that contribute to interspecies variation."; RL Genome Res. 15:629-640(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR848038; CAH63656.1; -; Genomic_DNA. DR RefSeq; YP_219627.1; NC_004552.2. DR ProteinModelPortal; Q5L6R5; -. DR STRING; 218497.CAB198; -. DR EnsemblBacteria; CAH63656; CAH63656; CAB198. DR GeneID; 3338215; -. DR KEGG; cab:CAB198; -. DR PATRIC; 20201804; VBIChlAbo21869_0221. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FVCACVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CABO218497:GJB0-213-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_1000008132. FT REGION 38 42 HMP-PP binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22791 MW; 7210C1C72D168DFC CRC64; MEENFFKLIL ITNKQQISVE EYLDFVCACV QSGVTSVQLR EKELSYRELL GFGEALKSIL DPLEIPLIVS DSVSVCLDLD ATGVHLGQTD GDVIEARELL GSDKIIGWNV NTLDQLLNAN TLPIDYLGLS AMFATQNKPD ATNLWGFSGL EQAVSLCEHP IVAIGGIDES NASKVIDAGA AGIAAIGVFH SAQNPSSVTK ALREIVDRGL RC // ID THIE_CHLCV Reviewed; 212 AA. AC Q824E9; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 75. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CCA_00203; OS Chlamydophila caviae (strain GPIC). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydophila. OX NCBI_TaxID=227941; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GPIC; RX PubMed=12682364; DOI=10.1093/nar/gkg321; RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., RA Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., RA White O., Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., RA Bavoil P.M., Fraser C.M.; RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): RT examining the role of niche-specific genes in the evolution of the RT Chlamydiaceae."; RL Nucleic Acids Res. 31:2134-2147(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015925; AAP04954.1; -; Genomic_DNA. DR RefSeq; NP_829076.1; NC_003361.3. DR ProteinModelPortal; Q824E9; -. DR STRING; 227941.CCA00203; -. DR PRIDE; Q824E9; -. DR EnsemblBacteria; AAP04954; AAP04954; CCA_00203. DR GeneID; 1217888; -. DR KEGG; cca:CCA00203; -. DR PATRIC; 20269428; VBIChlCav107360_0213. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CCAV227941:GH8L-217-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_0000157002. FT REGION 38 42 HMP-PP binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22571 MW; 10F9019B3D93D2DC CRC64; MEEDFFKLIL ITDRQNIPME EYLDFVSACV QSGVTAVQLR EKGLSHRELL SFGGALKSIL DPLDIPLIVS DSVSVCLDLD ASGVHLGQTD GDVIEARELL GPDKIIGWNV HTLDQLLNAN TLPIDYLGLS ALFATENKPE ATDLWGFSGL EQAVSLCEHP IVAVGGIDES NAGNVVEAGA AGIAAIGAFH SAHNPGLATK ALREIVDRGL RC // ID THIE_CHLL2 Reviewed; 210 AA. AC B3ED41; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Clim_1406; OS Chlorobium limicola (strain DSM 245 / NBRC 103803). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290315; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 245 / NBRC 103803; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., RA Liu Z., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobium limicola DSM 245."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001097; ACD90466.1; -; Genomic_DNA. DR RefSeq; YP_001943445.1; NC_010803.1. DR ProteinModelPortal; B3ED41; -. DR STRING; 290315.Clim_1406; -. DR EnsemblBacteria; ACD90466; ACD90466; Clim_1406. DR GeneID; 6356177; -. DR KEGG; cli:Clim_1406; -. DR PATRIC; 21374929; VBIChlLim118737_1500. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CLIM290315:GHUH-1439-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_1000093661. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22111 MW; 990CF7A9F08660BF CRC64; MIPSSPFLCF ITDESRSPII LARKALEGGA SMIQLRHKSA DGDQLYHWSV AIQALCRKHK AIFIVNDRVD IALAAGADGV HLGQQDLPAD AARKLLGKDR IMGISVSSPL EALAAEKNGA DYVGFGHIFP TSSKDKKNTP VGPESIADIK AIITIPIIAI GGITGCNAQL PIRAGAAGIA VIAAVSRAAD PEIAARELVG ILQKNIEHNR // ID THIE_CHLP8 Reviewed; 204 AA. AC B3QNM2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Cpar_1118; OS Chlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. OS thiosulfatophilum (strain DSM 263 / NCIB 8327)). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=517417; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIB 8327; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., RA Liu Z., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobaculum parvum NCIB 8327."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001099; ACF11525.1; -; Genomic_DNA. DR RefSeq; YP_001998725.1; NC_011027.1. DR ProteinModelPortal; B3QNM2; -. DR STRING; 517417.Cpar_1118; -. DR EnsemblBacteria; ACF11525; ACF11525; Cpar_1118. DR GeneID; 6420049; -. DR KEGG; cpc:Cpar_1118; -. DR PATRIC; 21365487; VBIChlPar72705_1109. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CIGGINE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPAR517417:GH95-1150-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 204 Thiamine-phosphate synthase. FT /FTId=PRO_1000093662. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21448 MW; 263B6340CC83A1B0 CRC64; MTIPRRLLCV ITDQQSNPVE LARMALEGGA RMVQLRRKSA SGRDLFEWAV RIQALCREYE ALFIVNDRVD IALAAHADGV HLGQQDIPVA SARALLGPET LIGVSVSTPS EAAKAAEEGA DYLGVGHIFP TSSKEKPMPP IGTSAIRPII EASGLPVIAI GGIELQNVAE VIKAGASGVA VISAVSGSAD PVAATRELVK RIRQ // ID THIE_CHLPD Reviewed; 206 AA. AC A1BGM7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Cpha266_1532; OS Chlorobium phaeobacteroides (strain DSM 266). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290317; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 266; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., RA Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobium phaeobacteroides DSM 266."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000492; ABL65554.1; -; Genomic_DNA. DR RefSeq; YP_911978.1; NC_008639.1. DR ProteinModelPortal; A1BGM7; -. DR STRING; 290317.Cpha266_1532; -. DR EnsemblBacteria; ABL65554; ABL65554; Cpha266_1532. DR GeneID; 4569582; -. DR KEGG; cph:Cpha266_1532; -. DR PATRIC; 21391269; VBIChlPha122104_1804. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CIGGINE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPHA290317:GHX4-1562-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 206 Thiamine-phosphate synthase. FT /FTId=PRO_0000336378. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21737 MW; 89CD4FF5726DCC3E CRC64; MIPAKPFLCV ITDEQCSSPV DLALMALEGG AEMIQLRHKS ASGKQLFQWA LDIQRLCRIH HAQFIVNDRV DIALAMNADG VHLGQQDLQP GEARKLLGTD KIIGVSTSSL TEALNAERAG ADYIGFGHIF QTGSKNKLSA PLGSAAISAV VQRISIPLVA IGGINKMNMM ETIAAGASGI AMIAAISRTA DPEGATRAIT ELLKGH // ID THIE_CHLTE Reviewed; 204 AA. AC Q8KD79; DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 14-MAY-2014, entry version 77. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CT1175; OS Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=194439; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49652 / DSM 12025 / TLS; RX PubMed=12093901; DOI=10.1073/pnas.132181499; RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., RA Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., RA Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., RA Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P., RA Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., RA Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., RA Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.; RT "The complete genome sequence of Chlorobium tepidum TLS, a RT photosynthetic, anaerobic, green-sulfur bacterium."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE006470; AAM72408.1; -; Genomic_DNA. DR RefSeq; NP_662066.1; NC_002932.3. DR ProteinModelPortal; Q8KD79; -. DR STRING; 194439.CT1175; -. DR EnsemblBacteria; AAM72408; AAM72408; CT1175. DR GeneID; 1006539; -. DR KEGG; cte:CT1175; -. DR PATRIC; 21400317; VBIChlTep116050_1070. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CTEP194439:GHN0-1207-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 204 Thiamine-phosphate synthase. FT /FTId=PRO_0000157003. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21475 MW; A845747ACBAEE09C CRC64; MTLPRRVLCV ITDEHSNPVE LARMALQGGA GMVQLRRKTA SGQELYEWAI RIQALCSEQQ ALFIVNDRVD IAMAVHADGV HLGQQDLPAS AARALLAPDA IIGVSVSNAT EAIKAAEEGA SYIGVGHIFP TFSKDKPSEP LGTASIRPIG RAAQLPVIAI GGIGHDNAAE VIRAGASGIA VISAVSDSDD PETATRELVR RIRQ // ID THIE_CHRVO Reviewed; 207 AA. AC Q7P1R3; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 14-MAY-2014, entry version 79. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CV_0150; OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / OS NBRC 12614 / NCIMB 9131 / NCTC 9757). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Chromobacterium. OX NCBI_TaxID=243365; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / RC NCTC 9757; RX PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., RA Batista J.S., Belo A., van den Berg C., Bogo M., Bonatto S., RA Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., RA Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., RA Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., RA Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., RA Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., RA Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., RA Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., RA di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., RA Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., RA Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., RA Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., RA Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., RA Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., RA Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., RA Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., RA Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., RA Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016825; AAQ57829.1; -; Genomic_DNA. DR RefSeq; NP_899820.1; NC_005085.1. DR ProteinModelPortal; Q7P1R3; -. DR STRING; 243365.CV_0150; -. DR EnsemblBacteria; AAQ57829; AAQ57829; CV_0150. DR GeneID; 2551056; -. DR KEGG; cvi:CV_0150; -. DR PATRIC; 21435056; VBIChrVio67196_0139. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CVIO243365:GHUD-150-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_0000157004. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 20832 MW; 42C09B0F53422B46 CRC64; MPPRVEGLYA VTPDGLDDAR LFALAAAALA GGARALQYRD KSGDAGRRLR QAAELQRLCR AHGALFIVND DVELAERIGA DGVHLGRDDG DIAAARRRLG ADAVIGASCY DRIELARAAL AAGASYVAFG AVFPSRTKPH AAAAPLSLFA DAAALGANAV AIGGIAAGNA GRAVEAGADA IAVIGGLFDA DDTAAAARAL AGWFGAR // ID THIE_CITK8 Reviewed; 211 AA. AC A8AKT0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CKO_02993; OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=290338; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696; RG The Citrobacter koseri Genome Sequencing Project; RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., RA Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000822; ABV14093.1; -; Genomic_DNA. DR RefSeq; YP_001454529.1; NC_009792.1. DR ProteinModelPortal; A8AKT0; -. DR STRING; 290338.CKO_02993; -. DR EnsemblBacteria; ABV14093; ABV14093; CKO_02993. DR GeneID; 5582667; -. DR KEGG; cko:CKO_02993; -. DR PATRIC; 20388636; VBICitKos71230_2510. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CKOS290338:GJ8L-2985-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000008133. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23197 MW; A7A6F868A3C061B2 CRC64; MYQPDFPAVP FRLGLYPVVD SVQWIERLLE AGVRTLQLRI KDKRDEEVED DVSAAIALGR RYNARLFIND YWRLAIKHNA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIERLGDYP TVAIGGISLE RASPVLKTGV GSIAVVSAIT RAEDWREATA QLLAIAGAGD E // ID THIE_CLOAB Reviewed; 211 AA. AC Q97LQ9; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 14-MAY-2014, entry version 85. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CA_C0495; OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG OS 5710 / VKM B-1787). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., RA Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., RA Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., RA Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE001437; AAK78475.1; -; Genomic_DNA. DR PIR; H96960; H96960. DR RefSeq; NP_347135.1; NC_003030.1. DR ProteinModelPortal; Q97LQ9; -. DR STRING; 272562.CA_C0495; -. DR EnsemblBacteria; AAK78475; AAK78475; CA_C0495. DR GeneID; 1116678; -. DR KEGG; cac:CA_C0495; -. DR PATRIC; 32035345; VBICloAce74127_0694. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CACE272562:GJIH-536-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000157005. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23159 MW; 8857F93D17AAFCA6 CRC64; MKNVDYKLYL VTDRKVLKER DLYKSIEEAI KGGVTLVQLR EKEMSTLDFY ESALKLKKIT ETYKIPLIIN DRIDIALAIN ADGVHIGQSD MPLIKARELL GKDKIIGVSA HSIEEALEAE RNGATYLGVG AIYNTSTKGD AQAVSLEELK NIKNSVKIPV VGIGGINEEN ANKVIETGVD GISVISGILS AQKIKDKARV MFDIVKKNST K // ID THIE_CLOB1 Reviewed; 205 AA. AC A7FPT0; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CLB_0490; OS Clostridium botulinum (strain ATCC 19397 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441770; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19397 / Type A; RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1- RT A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000726; ABS33773.1; -; Genomic_DNA. DR RefSeq; YP_001382841.1; NC_009697.1. DR ProteinModelPortal; A7FPT0; -. DR STRING; 441770.CLB_0490; -. DR EnsemblBacteria; ABS33773; ABS33773; CLB_0490. DR GeneID; 5394837; -. DR KEGG; cba:CLB_0490; -. DR PATRIC; 19355598; VBICloBot110701_0435. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CBOT441770:GH1E-476-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_0000336381. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22406 MW; 26EC80739A450727 CRC64; MEINYELYLI TDRRFLKGRQ LKKVVEDAIL GGVTIVQVRE KDVSTREFYN VAKEVKEVTD YYKVPIIIND RLDIAQAIDA SGVHLGQKDM HLNIAREILG KDKIIGISVG NVKEALQAQN NGADYLGIGT IFPTGSKKDV DAIIGIDGLS KIKDSISIPS VAIGGINKTN FKDVLKTGIE GISVISAILD EDDIKLAANN LLINK // ID THIE_CLOB6 Reviewed; 205 AA. AC C3L061; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CLJ_B0521; OS Clostridium botulinum (strain 657 / Type Ba4). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=515621; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=657 / Type Ba4; RA Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., RA Smith T.J., Sutton G., Brettin T.S.; RT "Genome sequence of Clostridium botulinum Ba4 strain 657."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001083; ACQ53399.1; -; Genomic_DNA. DR RefSeq; YP_002861327.1; NC_012658.1. DR ProteinModelPortal; C3L061; -. DR STRING; 515621.CLJ_B0521; -. DR EnsemblBacteria; ACQ53399; ACQ53399; CLJ_B0521. DR GeneID; 7881114; -. DR KEGG; cbi:CLJ_B0521; -. DR PATRIC; 19409472; VBICloBot19908_0768. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CBOT515621:GCP3-507-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_1000202748. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22434 MW; 3841EBA6E001F1C7 CRC64; MEINYELYLI TDRRFLKGRQ LKKVVEDAIL GGVTIVQVRE KDVSTKEFYN VAKEVKEVTD YYRVPIIIND RLDIAQAIDA NGVHLGQKDM HLNIAREILG KDKIIGISVG NVKEALEAQN NGADYLGIGT IFPTGSKKDV DAIIGIDGLS KIKDSISIPS VAIGGINKTN FKDVLKTGIE GISVISAILD EDDIKLAANN LLINK // ID THIE_CLOB8 Reviewed; 209 AA. AC A6M1W6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Cbei_4487; OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium OS acetobutylicum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=290402; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51743 / NCIMB 8052; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Tapia R., Brainard J., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Bennet G., Cann I., Chen J.-S., Contreras A.L., RA Jones D., Kashket E., Mitchell W., Stoddard S., Schwarz W., RA Qureshi N., Young M., Shi Z., Ezeji T., White B., Blaschek H., RA Richardson P.; RT "Complete sequence of Clostridium beijerinckii NCIMB 8052."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000721; ABR36596.1; -; Genomic_DNA. DR RefSeq; YP_001311552.1; NC_009617.1. DR ProteinModelPortal; A6M1W6; -. DR STRING; 290402.Cbei_4487; -. DR EnsemblBacteria; ABR36596; ABR36596; Cbei_4487. DR GeneID; 5295642; -. DR KEGG; cbe:Cbei_4487; -. DR PATRIC; 19353290; VBICloBei69853_4660. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CBEI290402:GHL5-4589-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_0000336380. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22576 MW; 5F80674A59C312BC CRC64; MKPKIDYSIY LVTDRDLMST ETLEEAVEKA IIGGCTLIQL REKDCSSLDF YNTAVRVKEI TDKHNIPLII NDRVDIALAV DAAGVHVGQS DIPAAIVRKV IGNDKILGVS TGSVNEALEA EKNGADYLGV GAMYSTGTKK DADSTSMNEL RKIRENVSIP IVVIGGINKD RVKDFKGIGI DGLAIVSAII AKEDITTAAK ELKNEFIKI // ID THIE_CLOBA Reviewed; 210 AA. AC B2UY65; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CLH_2855; OS Clostridium botulinum (strain Alaska E43 / Type E3). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=508767; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Alaska E43 / Type E3; RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., RA Smith T.J., Sutton G., Brettin T.S.; RT "Complete genome sequence of Clostridium botulinum E3 str. Alaska RT E43."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001078; ACD51788.1; -; Genomic_DNA. DR RefSeq; YP_001922232.1; NC_010723.1. DR ProteinModelPortal; B2UY65; -. DR STRING; 508767.CLH_2855; -. DR EnsemblBacteria; ACD51788; ACD51788; CLH_2855. DR GeneID; 6317874; -. DR KEGG; cbt:CLH_2855; -. DR PATRIC; 19421955; VBICloBot115804_2767. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CBOT508767:GHKO-2846-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_1000093663. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23237 MW; FFFFEC02A228D796 CRC64; MKNKIDYSIY LVTDRDLMST NTLEEAVEKS ILGGATLIQL REKECSSHDF YETALKIKKI TQKYNIPLII NDRVDIALAV DADGIHIGQS DLPATVVRNI IGEDKILGVS AGNLDEALKA QKDRADYIGV GAMYSTGTKK DATSTTMSEL KEITQKVSMP VVVIGGINKE RIKDFKEINI DGLAIVSAII AQKDIEKATR ELKEEFYKIK // ID THIE_CLOBB Reviewed; 213 AA. AC B2TQ13; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CLL_A3104; OS Clostridium botulinum (strain Eklund 17B / Type B). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=508765; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Eklund 17B / Type B; RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., RA Smith T.J., Sutton G., Brettin T.S.; RT "Complete sequence of Clostridium botulinum strain Eklund."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001056; ACD22548.1; -; Genomic_DNA. DR RefSeq; YP_001887290.1; NC_010674.1. DR ProteinModelPortal; B2TQ13; -. DR STRING; 508765.CLL_A3104; -. DR EnsemblBacteria; ACD22548; ACD22548; CLL_A3104. DR GeneID; 6293448; -. DR KEGG; cbk:CLL_A3104; -. DR PATRIC; 19399020; VBICloBot123574_3012. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CBOT508765:GJ4H-3092-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_1000093664. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23388 MW; 6D1AA3EF2AC03B32 CRC64; MKNKIDYSIY LVTDRDLMST NTLEEAVEKS ILGGTTLVQL REKECSSHDF YETALNVKKI TQKYNIPLII NDRVDIALAV DADGIHIGQS DLPATVVRNI IGEDKILGVS AGNLDEALKA QKDGADYIGV GAMYSTGTKK DATSTTMNEL REIMKKVSIP VVVIGGINKE RIKDFNGINI DGLAIVSAII AQENIEKSTR ELKEEFDKLN TLI // ID THIE_CLOBH Reviewed; 205 AA. AC A5HYZ3; A7G0Y9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CBO0449, CLC_0523; OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441771; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A; RX PubMed=17519437; DOI=10.1101/gr.6282807; RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., RA Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T., RA Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., RA Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., RA Sanders M., Simmonds M., White B., Whithead S., Parkhill J.; RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum RT strain Hall A and comparative analysis of the clostridial genomes."; RL Genome Res. 17:1082-1092(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A; RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1- RT A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000727; ABS39118.1; -; Genomic_DNA. DR EMBL; AM412317; CAL82002.1; -; Genomic_DNA. DR RefSeq; YP_001252993.1; NC_009495.1. DR RefSeq; YP_001386408.1; NC_009698.1. DR ProteinModelPortal; A5HYZ3; -. DR STRING; 413999.CBO0449; -. DR EnsemblBacteria; ABS39118; ABS39118; CLC_0523. DR GeneID; 5184704; -. DR GeneID; 5400418; -. DR KEGG; cbh:CLC_0523; -. DR KEGG; cbo:CBO0449; -. DR PATRIC; 19363015; VBICloBot22612_0452. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CBOT413999:GJ72-509-MONOMER; -. DR BioCyc; CBOT441771:GIWX-494-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_0000336382. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22406 MW; 26EC80739A450727 CRC64; MEINYELYLI TDRRFLKGRQ LKKVVEDAIL GGVTIVQVRE KDVSTREFYN VAKEVKEVTD YYKVPIIIND RLDIAQAIDA SGVHLGQKDM HLNIAREILG KDKIIGISVG NVKEALQAQN NGADYLGIGT IFPTGSKKDV DAIIGIDGLS KIKDSISIPS VAIGGINKTN FKDVLKTGIE GISVISAILD EDDIKLAANN LLINK // ID THIE_CLOBJ Reviewed; 205 AA. AC C1FSC1; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 34. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CLM_0531; OS Clostridium botulinum (strain Kyoto / Type A2). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=536232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kyoto / Type A2; RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C., RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., RA Brettin T.S.; RT "Genome sequence of Clostridium botulinum A2 Kyoto."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001581; ACO85552.1; -; Genomic_DNA. DR RefSeq; YP_002802776.1; NC_012563.1. DR ProteinModelPortal; C1FSC1; -. DR STRING; 536232.CLM_0531; -. DR EnsemblBacteria; ACO85552; ACO85552; CLM_0531. DR GeneID; 7767215; -. DR KEGG; cby:CLM_0531; -. DR PATRIC; 19377677; VBICloBot91161_0465. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CBOT536232:GCO3-509-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_1000198075. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22421 MW; C1251A32D1585842 CRC64; MEINYELYLI TDRRFLKGRQ LKKIVEDAIL GGVTIVQVRE KDVSTREFYN VAKEVKEVTD YYKVPIIIND RLDIAQAIDA SGVHLGQKDM HLNIAREILG KDKIIGISVG NVKEALEAQN NGADYLGIGT IFPTGSKKDV DAIIGIDGLS KIKDSISIPS VAIGGINKTN FKDVLKTGIE GISVISAILD EDDIKLAANN LLINK // ID THIE_CLOBK Reviewed; 205 AA. AC B1IEG6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CLD_0293; OS Clostridium botulinum (strain Okra / Type B1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=498213; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Okra / Type B1; RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1- RT A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000939; ACA43312.1; -; Genomic_DNA. DR RefSeq; YP_001780104.1; NC_010516.1. DR ProteinModelPortal; B1IEG6; -. DR STRING; 498213.CLD_0293; -. DR EnsemblBacteria; ACA43312; ACA43312; CLD_0293. DR GeneID; 6148632; -. DR KEGG; cbb:CLD_0293; -. DR PATRIC; 19401457; VBICloBot127283_0634. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CBOT498213:GCNI-524-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_0000336385. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22421 MW; 2000A3EB0431BC27 CRC64; MEINYELYLI TDRRFLKGRQ LKKVVEDAIL GGVTIVQVRE KDVSTREFYN IAKEVKEVTD YYKVPIIIND RLDIAQAIDA SGVHLGQKDM HLNIAREILG KDKIIGISVG NVKEALEAQN NGADYLGIGT IFPTGSKKDV DAIIGIDGLS KIKDSISIPS VAIGGINKTN FKDVLKTGIE GISVISAILD EDDIKLAANN LLINK // ID THIE_CLOBL Reviewed; 205 AA. AC A7GAL0; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CLI_0534; OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441772; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Langeland / NCTC 10281 / Type F; RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., RA Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., White O., RA Brettin T.S.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000728; ABS42158.1; -; Genomic_DNA. DR RefSeq; YP_001389820.1; NC_009699.1. DR ProteinModelPortal; A7GAL0; -. DR STRING; 441772.CLI_0534; -. DR EnsemblBacteria; ABS42158; ABS42158; CLI_0534. DR GeneID; 5402412; -. DR KEGG; cbf:CLI_0534; -. DR PATRIC; 19424030; VBICloBot15611_0458. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CBOT441772:GJIE-513-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_0000336383. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22407 MW; 33B89532CE505327 CRC64; MEINYELYLI TDRRFLKGRQ LKKVVEDAIL GGVTIVQVRE KDVSTREFYN VAKEVKEVTD YYKVPIIIND RLDIAQAIDA SGVHLGQKDM HLNIAREILG KDKIIGISVG NVKEALEAQN NGADYLGIGT IFPTGSKKDV DAIIGIDGLS KIKDSISIPS VAIGGINKTN FKDVLKTGIE GISVISAILD EDDIKLAANN LLINK // ID THIE_CLOBM Reviewed; 205 AA. AC B1KV12; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CLK_3652; OS Clostridium botulinum (strain Loch Maree / Type A3). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=498214; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Loch Maree / Type A3; RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1- RT A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000962; ACA56025.1; -; Genomic_DNA. DR RefSeq; YP_001785790.1; NC_010520.1. DR ProteinModelPortal; B1KV12; -. DR STRING; 498214.CLK_3652; -. DR EnsemblBacteria; ACA56025; ACA56025; CLK_3652. DR GeneID; 6154572; -. DR KEGG; cbl:CLK_3652; -. DR PATRIC; 19386313; VBICloBot822_0771. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MEASHIS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CBOT498214:GH05-500-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_0000336384. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22362 MW; BDD3BB951CCA4CAC CRC64; MEINYGLYLI TDRRFLKGRQ LKKVVEDAIL GGVTIVQVRE KDVSTREFYN VAKEVKEVTD YYKVPIIIND RLDIAQAIDA NGVHLGQKDM HLNIAREILG KDKIIGISVG NVKEALEAQN NGADYLGIGT IFPTGSKKDV DAIIGIDGLS KIKDSISIPS VAIGGINKTN FKDVLKTGIE GISVISAILD EDDIKLAANN LLINK // ID THIE_CLOCE Reviewed; 210 AA. AC B8I3J4; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Ccel_1989; OS Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / OS H10). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=394503; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., RA Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., RA Kyrpides N., Ivanova N., Zhou J., Richardson P.; RT "Complete sequence of Clostridium cellulolyticum H10."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001348; ACL76337.1; -; Genomic_DNA. DR RefSeq; YP_002506317.1; NC_011898.1. DR ProteinModelPortal; B8I3J4; -. DR STRING; 394503.Ccel_1989; -. DR EnsemblBacteria; ACL76337; ACL76337; Ccel_1989. DR GeneID; 7310700; -. DR KEGG; cce:Ccel_1989; -. DR PATRIC; 19434891; VBICloCel57783_2047. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CCEL394503:GJET-2035-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_1000198076. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22311 MW; 16FCA6731DAA5471 CRC64; MKSKIDYTLY LVTDHQLMST KTLEEAVEQA IAGGCTLVQL REKTASSRDF YQNAINVKTI TDKYNVPLII NDRIDIALAV GADGVHVGQS DLPAAVVRKI IGNDKILGVS AGSVEKAIEA QKIGADYIGV GALFSTSTKT DAKAVSIETL MKIVREVSIP VVGIGGINAE NAVQLKNTGI RGIAVVSAII SQKDIKSSAE KLLEIFVNKA // ID THIE_CLOD6 Reviewed; 210 AA. AC Q186F8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 55. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CD630_16010; OS Clostridium difficile (strain 630). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=272563; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=630; RX PubMed=16804543; DOI=10.1038/ng1830; RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A., RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., RA Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.; RT "The multidrug-resistant human pathogen Clostridium difficile has a RT highly mobile, mosaic genome."; RL Nat. Genet. 38:779-786(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM180355; CAJ68466.1; -; Genomic_DNA. DR RefSeq; YP_001088102.1; NC_009089.1. DR ProteinModelPortal; Q186F8; -. DR STRING; 272563.CD1601; -. DR EnsemblBacteria; CAJ68466; CAJ68466; CD630_16010. DR GeneID; 4913386; -. DR KEGG; cdf:CD630_16010; -. DR PATRIC; 19441581; VBICloDif38397_1678. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CDIF272563:GJFE-1777-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_0000336386. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 23414 MW; F50956BE21E60D7E CRC64; MIDKESLKKC LKLYLVTDSE MLKGRDFYKC LEDAISSGIT TVQLREKNAS GREFLRKAMK LREITKRYGV KFIINDRVDI ALICDADGVH VGQSDIDVRE VRKLIGNNKI LGVSARTLEE AICAKNDGAD YLGVGSIFTT STKLDAKSAS FETVKEIKEK VDMPFVLIGG INLDNIDKLK CLESDGYAII SAILKAEDIS KEVEKWTLKI // ID THIE_CLONN Reviewed; 204 AA. AC A0Q2A0; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=NT01CX_0248; OS Clostridium novyi (strain NT). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=386415; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NT; RX PubMed=17115055; DOI=10.1038/nbt1256; RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., RA Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., RA Vogelstein B., Zhou S.; RT "The genome and transcriptomes of the anti-tumor agent Clostridium RT novyi-NT."; RL Nat. Biotechnol. 24:1573-1580(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000382; ABK61946.1; -; Genomic_DNA. DR RefSeq; YP_878752.1; NC_008593.1. DR ProteinModelPortal; A0Q2A0; -. DR STRING; 386415.NT01CX_0248; -. DR EnsemblBacteria; ABK61946; ABK61946; NT01CX_0248. DR GeneID; 4539740; -. DR KEGG; cno:NT01CX_0248; -. DR PATRIC; 19481046; VBICloNov112828_1788. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CNOV386415:GH98-1815-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 204 Thiamine-phosphate synthase. FT /FTId=PRO_1000093665. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21802 MW; 64F2C806CC3095DC CRC64; MDINYKLYLI TDRSFLNGRS LAECVEDAIK GGATLVQVRE KNISTRDFYN IAREVQEVTT KYNVPLLIND RIDIALAINA DGVHLGQSDM PIELARKILG DDKVIGISAG NVKEAIEAEK AGADYVGLGT VFFTGTKKDI DEPIGLAGLK EITEKITIPS VAIGGINKEN AKSVLATGVD GISVISAILK NDDIQGASKT LANI // ID THIE_CLOP1 Reviewed; 207 AA. AC Q0TQV4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 14-MAY-2014, entry version 54. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CPF_1543; OS Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13124 / NCTC 8237 / Type A; RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., RA DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., RA Melville S.B., Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial RT pathogen, Clostridium perfringens."; RL Genome Res. 16:1031-1040(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000246; ABG83983.1; -; Genomic_DNA. DR RefSeq; YP_695986.1; NC_008261.1. DR ProteinModelPortal; Q0TQV4; -. DR STRING; 195103.CPF_1543; -. DR EnsemblBacteria; ABG83983; ABG83983; CPF_1543. DR GeneID; 4202016; -. DR KEGG; cpf:CPF_1543; -. DR PATRIC; 19485346; VBICloPer106549_1493. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPER195103:GHAW-1561-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000008134. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 23005 MW; 8C1138BEB1EF9AD6 CRC64; MINKDYKKLY LVTDYRIPFN ELLEKTKEAL IGGVSIVQYR AKNKKTKEMC KEAKELKKLC DEFGALFLVN DRIDVALAVK ANGVHIGQDD MEVFIAREIM PKDAVIGVTV HNKEEALKAI KEGADNLGVG ALFSTNSKDD ATLMTLETLR EIKSVSNIPL YGIGGITPYN LNKDILENLD GVAVISALLN SDNIREKSKE FLNILSK // ID THIE_CLOPE Reviewed; 207 AA. AC Q8XKQ8; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 14-MAY-2014, entry version 79. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CPE1336; OS Clostridium perfringens (strain 13 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195102; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13 / Type A; RX PubMed=11792842; DOI=10.1073/pnas.022493799; RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., RA Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.; RT "Complete genome sequence of Clostridium perfringens, an anaerobic RT flesh-eater."; RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000016; BAB81042.1; -; Genomic_DNA. DR RefSeq; NP_562252.1; NC_003366.1. DR ProteinModelPortal; Q8XKQ8; -. DR STRING; 195102.CPE1336; -. DR EnsemblBacteria; BAB81042; BAB81042; BAB81042. DR GeneID; 989645; -. DR KEGG; cpe:CPE1336; -. DR PATRIC; 19496618; VBICloPer59675_1406. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPER195102:GJFM-1381-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_0000157006. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22919 MW; 4C6E430EC139CE52 CRC64; MSNKDYKKLY LVTDYRIPFN ELLEKTKEAL IGGVSIVQYR AKNKKTKEMC KEAKELKKLC DEFGALFLVN DRIDVALAVK ANGVHIGQDD MEVSIAREIM PKDAVIGVTV HNKEEALKAI KEGADNLGVG ALFSTNSKDD ATLMTLETLR EIKSVSNIPL YGIGGITPYN LNKDILENLD GVAVISALLN SDNIREKSKE FLNILSK // ID THIE_CLOPS Reviewed; 207 AA. AC Q0STA1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 14-MAY-2014, entry version 54. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CPR_1336; OS Clostridium perfringens (strain SM101 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=289380; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM101 / Type A; RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., RA DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., RA Melville S.B., Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial RT pathogen, Clostridium perfringens."; RL Genome Res. 16:1031-1040(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000312; ABG85325.1; -; Genomic_DNA. DR RefSeq; YP_698656.1; NC_008262.1. DR ProteinModelPortal; Q0STA1; -. DR STRING; 289380.CPR_1336; -. DR EnsemblBacteria; ABG85325; ABG85325; CPR_1336. DR GeneID; 4204047; -. DR KEGG; cpr:CPR_1336; -. DR PATRIC; 19490963; VBICloPer122123_1312. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPER289380:GI76-1349-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000008135. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22898 MW; 217D9AFC46689FF7 CRC64; MSNKDYKKLY LVTDYRIPFN ELLEKTKEAL IGGVSIVQYR AKNKETKEMC KEARALKKLC DEFGALFLVN DRIDVALAVK AHGVHIGQDD MDVSIAREIM PKDAIIGVTV HNKEEALKAI KDGADNLGVG ALFSTNSKDD ATLMTLETLR EIKSVSNIPL YGIGGITPYN LNKDILENLD GVAVISALLN SDNIREKSKE FLNILSK // ID THIE_CLOTE Reviewed; 209 AA. AC Q893R0; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 14-MAY-2014, entry version 74. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CTC_01751; OS Clostridium tetani (strain Massachusetts / E88). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=212717; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Massachusetts / E88; RX PubMed=12552129; DOI=10.1073/pnas.0335853100; RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., RA Gottschalk G.; RT "The genome sequence of Clostridium tetani, the causative agent of RT tetanus disease."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAO36282.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015927; AAO36282.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_782345.1; NC_004557.1. DR ProteinModelPortal; Q893R0; -. DR STRING; 212717.CTC01751; -. DR EnsemblBacteria; AAO36282; AAO36282; CTC_01751. DR GeneID; 1060934; -. DR KEGG; ctc:CTC01751; -. DR PATRIC; 19511557; VBICloTet101274_1826. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CTET212717:GJAM-1612-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_0000157007. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22899 MW; BC91305F1D16634E CRC64; MHNKNLDCTL YLVTDRDILK GRDLKKVLEE AILGGTTLVQ LREKNVSSKE FYEIAKDIKV ITDKYNIPLI INDRVDIALA VNAEGIHIGQ KDLPANIVRK IIGEDKILGV SANTIEDALK AQRDGADYLG VGAIFPTNSK KDAESTSIET LKEIKNAVNI PIVAIGGINE NNVQKLKETN IDGIAVISTI LGKEDVKKAC EELTGFFNE // ID THIE_COPPD Reviewed; 211 AA. AC B5Y6I1; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=COPRO5265_0006; OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermodesulfobiaceae; Coprothermobacter. OX NCBI_TaxID=309798; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35245 / DSM 5265 / BT; RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.; RT "The complete genome sequence of Coprothermobacter proteolyticus RT strain ATCC 5245 / DSM 5265 / BT."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001145; ACI17434.1; -; Genomic_DNA. DR RefSeq; YP_002246378.1; NC_011295.1. DR ProteinModelPortal; B5Y6I1; -. DR STRING; 309798.COPRO5265_0006; -. DR EnsemblBacteria; ACI17434; ACI17434; COPRO5265_0006. DR GeneID; 6943385; -. DR KEGG; cpo:COPRO5265_0006; -. DR PATRIC; 21472900; VBICopPro72829_0006. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPRO309798:GH7M-6-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000198077. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22194 MW; 168CDB16AE8BEE74 CRC64; MVTKEQLKEK LKLYVILDRK LGNGVPLRQQ AQLAIAGGAT AIQLRDKEMK GRDYYQAALV IKDVCKENNV LFIVNDRLDV ALAAEADGVH LGQEDLPLHA AKKLAPPGFI IGISAVNVEQ AKLAEKGGAD YLGVGDVFGT ASKPDAKLTG VDMLKMICQS TSLPCVAIGG INVNNAKIVL DAGAIGIAVI SAVVSQKDIT GAAKALRELI P // ID THIE_COREF Reviewed; 216 AA. AC Q8FP55; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 72. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CE1933; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM OS 11189 / NBRC 100395). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., RA Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., RA Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- MISCELLANEOUS: There is also a thiED fusion protein in this CC bacteria (AC Q8FTH8). CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000035; BAC18743.1; -; Genomic_DNA. DR RefSeq; NP_738543.1; NC_004369.1. DR ProteinModelPortal; Q8FP55; -. DR STRING; 196164.CE1933; -. DR EnsemblBacteria; BAC18743; BAC18743; BAC18743. DR GeneID; 1034647; -. DR KEGG; cef:CE1933; -. DR PATRIC; 21490011; VBICorEff9312_1919. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6PZXB0; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 216 Thiamine-phosphate synthase. FT /FTId=PRO_0000157008. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). SQ SEQUENCE 216 AA; 22925 MW; B64A9E583BC15659 CRC64; MRPTPDLRCY FITGHGSHEH IVDVARRAVA GGARTVQVRS KPITARELYA LTEAVALAVG ETAHVLVDDR VDIALALRHR GLPVHGVHVG QDDLPVRDVR ALLGEEAIIG LTTGTRELVE AANEHAEVLD YIGAGPFRPT PTKDSGRPPL GVEGYRELVE LSRLPVVAIG DVTADDAPAL ADTGVAGLAV VRGLMESADP TGYARRLITG FGEGRQ // ID THIE_CORJK Reviewed; 218 AA. AC Q4JVZ1; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 14-MAY-2014, entry version 54. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=jk0854; OS Corynebacterium jeikeium (strain K411). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=306537; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K411; RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005; RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., RA Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., RA Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., RA Puehler A.; RT "Complete genome sequence and analysis of the multiresistant RT nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring RT bacterium of the human skin flora."; RL J. Bacteriol. 187:4671-4682(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR931997; CAI37016.1; -; Genomic_DNA. DR RefSeq; YP_250634.1; NC_007164.1. DR ProteinModelPortal; Q4JVZ1; -. DR STRING; 306537.jk0854; -. DR EnsemblBacteria; CAI37016; CAI37016; jk0854. DR GeneID; 3433255; -. DR KEGG; cjk:jk0854; -. DR PATRIC; 21512608; VBICorJei31838_0865. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6PZXB0; -. DR BioCyc; CJEI306537:GJ8V-884-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 218 Thiamine-phosphate synthase. FT /FTId=PRO_0000336387. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). SQ SEQUENCE 218 AA; 22597 MW; 891B856F0D89A6E9 CRC64; MSASLDLRCY LVTGAPHEKV VDVAAAAAAG GAGVVQVRSK PISVRDLTAL AVEVAAAVQK ANPATRVLID DRVDVAAALM PEHNIHGVHI GQDDLDPRLA RQLLGKDAII GLTTGTLPLV QQANEYADVI DYIGAGPFRP TPTKDSGREP LGLEGYPALV EASRVPVVAI GDVHAEDAAD LAATGVAGLA IVRGIMQAEN PKAYAESVVS QFSEANER // ID THIE_CROS8 Reviewed; 210 AA. AC A7MJ80; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=ESA_03680; OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=290339; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-894; RX PubMed=20221447; DOI=10.1371/journal.pone.0009556; RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., RA Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., RA Wilson R.K., McClelland M., Forsythe S.J.; RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative RT genomic hybridization analysis with other Cronobacter species."; RL PLoS ONE 5:E9556-E9556(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000783; ABU78884.1; -; Genomic_DNA. DR RefSeq; YP_001439720.1; NC_009778.1. DR ProteinModelPortal; A7MJ80; -. DR STRING; 290339.ESA_03680; -. DR EnsemblBacteria; ABU78884; ABU78884; ESA_03680. DR GeneID; 5550601; -. DR KEGG; esa:ESA_03680; -. DR PATRIC; 20399049; VBICroSak107175_3277. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; CSAK290339:GJ80-3669-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_0000336391. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22754 MW; F0F8D76340FCA4DF CRC64; MTPLFAPVPH RLGLYPVVDS VEWVTRLLDA GVRTLQLRIK DKTDAEVETD IAAAIALGQR YHARLFINDY WRLAIKHQAY GVHLGQEDLE TADPDAIRRA GLRLGVSTHD DMEIDVALAV RPSYIALGHV FPTQTKQMPS APQGLAQLAA HVKRLGDYPT VAIGGISLER APAVLETGVG SIAVVSAITQ APDWRGATQR LLELAGVGDE // ID THIE_DECAR Reviewed; 211 AA. AC Q478V2; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Daro_3901; OS Dechloromonas aromatica (strain RCB). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Dechloromonas. OX NCBI_TaxID=159087; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCB; RX PubMed=19650930; DOI=10.1186/1471-2164-10-351; RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., RA Lapidus A.; RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RT RCB: indications of a surprisingly complex life-style and cryptic RT anaerobic pathways for aromatic degradation."; RL BMC Genomics 10:351-351(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000089; AAZ48629.1; -; Genomic_DNA. DR RefSeq; YP_287099.1; NC_007298.1. DR ProteinModelPortal; Q478V2; -. DR STRING; 159087.Daro_3901; -. DR EnsemblBacteria; AAZ48629; AAZ48629; Daro_3901. DR GeneID; 3567689; -. DR KEGG; dar:Daro_3901; -. DR PATRIC; 21606496; VBIDecAro89105_3888. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DARO159087:GI5B-3979-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000336388. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21979 MW; CCA7412B6E2D9E61 CRC64; MATNKLRGLY AITPDRADGA RLLADVEAAL AGGCRVVQYR DKLSTMPEQV ARAQALRELT RRFAATLLIN DDLALAALVQ ADGVHLGKDD GNLVVARAIL GPDKILGASC YADFAAAEAA SRAGADYVAF GAVYPSPTKP QAANATTELF VRAKAELPAA TCAIGGITLD NAPPLIVAGA DLLAVITDLF SAPDIMARAA AYQRLFEEAH S // ID THIE_DEIGD Reviewed; 221 AA. AC Q1IX16; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 1. DT 14-MAY-2014, entry version 59. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Dgeo_1923; OS Deinococcus geothermalis (strain DSM 11300). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=319795; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11300; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., RA Zhai M., Richardson P.; RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM RT 11300."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000359; ABF46218.1; -; Genomic_DNA. DR RefSeq; YP_605387.1; NC_008025.1. DR ProteinModelPortal; Q1IX16; -. DR STRING; 319795.Dgeo_1923; -. DR EnsemblBacteria; ABF46218; ABF46218; Dgeo_1923. DR GeneID; 4057671; -. DR KEGG; dge:Dgeo_1923; -. DR PATRIC; 21625799; VBIDeiGeo41128_2518. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DGEO319795:GHMU-1961-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 221 Thiamine-phosphate synthase. FT /FTId=PRO_0000336389. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23290 MW; 801317B5BB431715 CRC64; MSRSLGRLYL VATPRPDQPE AEFLARVEAA LDGGVDTLQL RCKAGSPQYG EARPYIALAR RVGALAQARD VPFFVNDRVD VALASGADGV HLGQDDLPAE WARRLAPGLQ IGLSTHSPEQ AARAQAEHPT YFAVGPVYAT PTKPGRAAAG LAYVRHVAAL CPAVPWYAIG GVDLSTVDDV VAAGATRVAV VRAVLDAPDP ARAAADLLAR LPDAWEARVC R // ID THIE_DEIRA Reviewed; 280 AA. AC Q9RYX9; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 14-MAY-2014, entry version 85. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=DR_A0174; OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / OS LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=243230; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / RC NCIMB 9279 / R1 / VKM B-1422; RX PubMed=10567266; DOI=10.1126/science.286.5444.1571; RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C., RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., RA Fraser C.M.; RT "Genome sequence of the radioresistant bacterium Deinococcus RT radiodurans R1."; RL Science 286:1571-1577(1999). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE001825; AAF12197.1; -; Genomic_DNA. DR PIR; A75614; A75614. DR RefSeq; NP_285498.1; NC_001264.1. DR ProteinModelPortal; Q9RYX9; -. DR STRING; 243230.DR_A0174; -. DR EnsemblBacteria; AAF12197; AAF12197; DR_A0174. DR GeneID; 1798009; -. DR KEGG; dra:DR_A0174; -. DR PATRIC; 21633386; VBIDeiRad64572_3062. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MLARYFI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DRAD243230:GH46-2865-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 280 Thiamine-phosphate synthase. FT /FTId=PRO_0000157009. FT REGION 104 108 HMP-PP binding (By similarity). FT REGION 205 207 THZ-P binding (By similarity). FT METAL 142 142 Magnesium (By similarity). FT METAL 161 161 Magnesium (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 179 179 HMP-PP (By similarity). FT BINDING 208 208 HMP-PP (By similarity). FT BINDING 236 236 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 280 AA; 29811 MW; AE655C7BEF93D703 CRC64; MGWSGSPLTL PPLRGSPPLP QVERDRTQPQ LLAFADAFPS EGRGELRSRE RRGEATGRGG LRMTAPTRPL GHLYLVATPR PGQSEAEFLR RVEDALAGGV DTLQLRCKAD SGQYGEARPY IALAERLRDL AHARNVPFFV NDRVDVALAA GADGVHLGQN DLPVEWARLM APGLRVGRST HRPEDAARAL AEAPAYFATG PVHATPTKPG RVAAGLGYVR HIAALRPTLP WYAIGGIDLG NVQAVLDAGA TRIAVVRAVL DADDCAAAAH ALREALMVNG // ID THIE_DESHD Reviewed; 207 AA. AC B8FUD4; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Dhaf_2520; OS Desulfitobacterium hafniense (strain DCB-2 / DSM 10664). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=272564; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DCB-2 / DSM 10664; RX PubMed=22316246; DOI=10.1186/1471-2180-12-21; RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., RA Marsh T.L., Tiedje J.M.; RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram- RT positive anaerobe capable of dehalogenation and metal reduction."; RL BMC Microbiol. 12:21-21(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001336; ACL20548.1; -; Genomic_DNA. DR RefSeq; YP_002458984.1; NC_011830.1. DR ProteinModelPortal; B8FUD4; -. DR STRING; 272564.Dhaf_2520; -. DR EnsemblBacteria; ACL20548; ACL20548; Dhaf_2520. DR GeneID; 7259491; -. DR KEGG; dhd:Dhaf_2520; -. DR PATRIC; 21662841; VBIDesHaf15223_2622. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DHAF272564:GCV8-2547-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000198078. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21878 MW; 78E74095095D3D62 CRC64; MAVDYSLYLV TDRILVGPKD FLLSIRKALE GGVTLLQLRE KETNSREFYD IGVKVKELAA EFGVPLIIND RVDLALALDA DGVHVGQQDL PLAKVRNIIG PDKILGYSVS SLEEALQGER MGADYLGAGP VFPTGSKKDA AEAIGLAKLK EIKAGVSLPV VGIGGIGAAN LRVVKETGID GVSVISAILS QEDPCAAAKG LVDLWRN // ID THIE_DESHY Reviewed; 207 AA. AC Q24XQ0; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 14-MAY-2014, entry version 57. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=DSY1403; OS Desulfitobacterium hafniense (strain Y51). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=138119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y51; RX PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006; RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K., RA Inatomi K., Furukawa K., Inui M., Yukawa H.; RT "Complete genome sequence of the dehalorespiring bacterium RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides RT ethenogenes 195."; RL J. Bacteriol. 188:2262-2274(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008230; BAE83192.1; -; Genomic_DNA. DR RefSeq; YP_517636.1; NC_007907.1. DR ProteinModelPortal; Q24XQ0; -. DR STRING; 138119.DSY1403; -. DR EnsemblBacteria; BAE83192; BAE83192; DSY1403. DR GeneID; 3954053; -. DR KEGG; dsy:DSY1403; -. DR PATRIC; 21671193; VBIDesHaf65307_1561. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DHAF138119:GHT5-1432-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_0000336390. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21882 MW; 78E75E75E7596D62 CRC64; MAVDYSLYLV TDRILVGPKD FLLSIRKALE GGVTLLQLRE KETNSREFYD IGVKVKELAA EFGVPLIIND RVDLALALDA DGVHVGQQDL PLAKVRNIIG PDKILGYSVS SLEEALQGER MGADYLGAGP VFPTGSKKDA AEAIGLAKLK EIKAGVSLPV VGIGGIGAAN LRAVKETGID GVSVISAILS QEDPCAAAKG LMDLWRN // ID THIE_DESMR Reviewed; 211 AA. AC C4XIJ2; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 14-MAY-2014, entry version 33. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=DMR_30760; OS Desulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=573370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700980 / DSM 13731 / RS-1; RX PubMed=19675025; DOI=10.1101/gr.088906.108; RA Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., RA Aoki N., Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., RA Takeyama H., Matsunaga T.; RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 RT revealed common gene clusters in magnetotactic bacteria."; RL Genome Res. 19:1801-1808(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010904; BAH76567.1; -; Genomic_DNA. DR RefSeq; YP_002954453.1; NC_012796.1. DR ProteinModelPortal; C4XIJ2; -. DR STRING; 573370.DMR_30760; -. DR EnsemblBacteria; BAH76567; BAH76567; DMR_30760. DR GeneID; 7980532; -. DR KEGG; dma:DMR_30760; -. DR PATRIC; 21752377; VBIDesMag26496_2944. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VQVRSKP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DMAG573370:GHJL-3113-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000202749. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21639 MW; AA7EA1EA5FCD6E30 CRC64; MKPNFDPTLY LVTDRGCLAG RDLLDVVGRA VAGGAKLVQL REKNACTREF VELARALVGL VRPLGARLVI NDRVDVALAC DADGVHVGQD DMRPADVRAL IGPDRLLGLS VTGEDEARAA RGEPVDYLGA GPVFATATKK DAGAPQGIEG LIRMIALAEV PVVAIGAVTA ANAAAVMAAG AAGLAMVSAI CAAPDPEAAA RELRVIAEQG R // ID THIE_DICT6 Reviewed; 223 AA. AC B5YA97; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=DICTH_1552; OS Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12). OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus. OX NCBI_TaxID=309799; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35947 / DSM 3960 / H-6-12; RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.; RT "The complete genome sequence of Dictyoglomus thermophilum strain ATCC RT 35947 / DSM 3960 / H-6-12."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001146; ACI19897.1; -; Genomic_DNA. DR RefSeq; YP_002251367.1; NC_011297.1. DR ProteinModelPortal; B5YA97; -. DR STRING; 309799.DICTH_1552; -. DR EnsemblBacteria; ACI19897; ACI19897; DICTH_1552. DR GeneID; 6945984; -. DR KEGG; dth:DICTH_1552; -. DR PATRIC; 21807726; VBIDicThe33784_1492. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CIGGINE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DTHE309799:GHF9-1537-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 223 Thiamine-phosphate synthase. FT /FTId=PRO_1000093666. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 25389 MW; 5B62ED041CF7B213 CRC64; MNKGEKLSLF KDYNLYCLTC EDYSLGRRNI DVVREILNAG VRIIQYREKK KTMREKYQEA KKIRELTAQY NALLIINDHL DLAKIVEADG VHIGQEDYPI EVAKEYLGDE FIIGLTTHTK TQVIEAFQKG ADYIGLGPIF PSYTKEKPHP PIGLEIIEWA VNHVHIPIVA IGGIKESNIY EVLKHGAKCI AMVTEIVSSQ DIYEKTKNII RILEGYKNGK NLA // ID THIE_DICTD Reviewed; 223 AA. AC B8E358; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Dtur_1660; OS Dictyoglomus turgidum (strain Z-1310 / DSM 6724). OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus. OX NCBI_TaxID=515635; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Z-1310 / DSM 6724; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Mead D.; RT "Complete sequence of Dictyoglomus turgidum DSM 6724."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001251; ACK42932.1; -; Genomic_DNA. DR RefSeq; YP_002353546.1; NC_011661.1. DR ProteinModelPortal; B8E358; -. DR STRING; 515635.Dtur_1660; -. DR EnsemblBacteria; ACK42932; ACK42932; Dtur_1660. DR GeneID; 7082179; -. DR KEGG; dtu:Dtur_1660; -. DR PATRIC; 21812130; VBIDicTur93964_1710. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GAKWIQY; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; DTUR515635:GH4F-1711-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 223 Thiamine-phosphate synthase. FT /FTId=PRO_1000117299. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 25386 MW; E46FDB43723EF7CC CRC64; MNKKEKLELL KDFNLYCLTC EEYSIGRKNI DVVREILEAG VKIIQYREKK KPMREKYHEV VKIRDLTAKY NALLIVNDHL DLTKIVEADG VHIGQEDYPI EVAKEFLGEN FIIGLTTHTK EQVMEALRKG ADYIGLGPIF PSYTKEKPHP PIGIEILDWA IKNISIPVVA IGGIKESNIH EILNLGAKCI AMVTEIVSSP NIYEKTRKII HILEGYKNGK YIA // ID THIE_ECO24 Reviewed; 211 AA. AC A7ZUK8; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=EcE24377A_4535; OS Escherichia coli O139:H28 (strain E24377A / ETEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=331111; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E24377A / ETEC; RX PubMed=18676672; DOI=10.1128/JB.00619-08; RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., RA Henderson I.R., Sperandio V., Ravel J.; RT "The pangenome structure of Escherichia coli: comparative genomic RT analysis of E. coli commensal and pathogenic isolates."; RL J. Bacteriol. 190:6881-6893(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000800; ABV16469.1; -; Genomic_DNA. DR RefSeq; YP_001465487.1; NC_009801.1. DR ProteinModelPortal; A7ZUK8; -. DR SMR; A7ZUK8; 20-202. DR STRING; 331111.EcE24377A_4535; -. DR EnsemblBacteria; ABV16469; ABV16469; EcE24377A_4535. DR GeneID; 5589036; -. DR KEGG; ecw:EcE24377A_4535; -. DR PATRIC; 18298336; VBIEscCol31211_4748. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL331111:GH7P-4516-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000057641. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_ECO57 Reviewed; 211 AA. AC Q8X6Y0; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 14-MAY-2014, entry version 79. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Z5568, ECs4916; OS Escherichia coli O157:H7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., RA Welch R.A., Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli RT O157:H7 and genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE005174; AAG59190.1; -; Genomic_DNA. DR EMBL; BA000007; BAB38339.1; -; Genomic_DNA. DR PIR; B86091; B86091. DR PIR; D91243; D91243. DR RefSeq; NP_290625.1; NC_002655.2. DR RefSeq; NP_312943.1; NC_002695.1. DR ProteinModelPortal; Q8X6Y0; -. DR SMR; Q8X6Y0; 10-209. DR STRING; 155864.Z5568; -. DR EnsemblBacteria; AAG59190; AAG59190; Z5568. DR EnsemblBacteria; BAB38339; BAB38339; BAB38339. DR GeneID; 914936; -. DR GeneID; 960136; -. DR KEGG; ece:Z5568; -. DR KEGG; ecs:ECs4916; -. DR PATRIC; 18359525; VBIEscCol44059_4903. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL386585:GJFA-4916-MONOMER; -. DR BioCyc; ECOO157:THIE-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000157012. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_ECO5E Reviewed; 211 AA. AC B5Z089; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=ECH74115_5461; OS Escherichia coli O157:H7 (strain EC4115 / EHEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=444450; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EC4115 / EHEC; RA Eppinger M., Sebastian Y., Ravel J.; RT "Complete genome sequence of Escherichia coli O157:H7 str. EC4115."; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001164; ACI37440.1; -; Genomic_DNA. DR RefSeq; YP_002273509.1; NC_011353.1. DR ProteinModelPortal; B5Z089; -. DR SMR; B5Z089; 10-209. DR STRING; 444450.ECH74115_5461; -. DR EnsemblBacteria; ACI37440; ACI37440; ECH74115_5461. DR GeneID; 6969054; -. DR KEGG; ecf:ECH74115_5461; -. DR PATRIC; 18371457; VBIEscCol74651_5316. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL444450:GHOB-5438-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000093667. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23057 MW; 0AFA353935A48520 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLSDYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_ECOHS Reviewed; 211 AA. AC A8A793; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=EcHS_A4227; OS Escherichia coli O9:H4 (strain HS). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=331112; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HS; RX PubMed=18676672; DOI=10.1128/JB.00619-08; RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., RA Henderson I.R., Sperandio V., Ravel J.; RT "The pangenome structure of Escherichia coli: comparative genomic RT analysis of E. coli commensal and pathogenic isolates."; RL J. Bacteriol. 190:6881-6893(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000802; ABV08397.1; -; Genomic_DNA. DR RefSeq; YP_001460780.1; NC_009800.1. DR ProteinModelPortal; A8A793; -. DR SMR; A8A793; 11-208. DR STRING; 331112.EcHS_A4227; -. DR EnsemblBacteria; ABV08397; ABV08397; EcHS_A4227. DR GeneID; 5591987; -. DR KEGG; ecx:EcHS_A4227; -. DR PATRIC; 18318420; VBIEscCol77814_4112. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL331112:GHHI-4221-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000057642. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23027 MW; 0AE827392C8C3853 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGVSLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_ECOK1 Reviewed; 211 AA. AC A1AIG4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Ecok1_39600; ORFNames=APECO1_24812; OS Escherichia coli O1:K1 / APEC. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=405955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17293413; DOI=10.1128/JB.01726-06; RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., RA Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., RA Nolan L.K.; RT "The genome sequence of avian pathogenic Escherichia coli strain RT O1:K1:H7 shares strong similarities with human extraintestinal RT pathogenic E. coli genomes."; RL J. Bacteriol. 189:3228-3236(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000468; ABJ03454.1; -; Genomic_DNA. DR RefSeq; YP_859578.1; NC_008563.1. DR ProteinModelPortal; A1AIG4; -. DR SMR; A1AIG4; 9-208. DR STRING; 405955.APECO1_24812; -. DR EnsemblBacteria; ABJ03454; ABJ03454; APECO1_24812. DR GeneID; 4493800; -. DR KEGG; ecv:APECO1_24812; -. DR PATRIC; 18220521; VBIEscCol127180_4462. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000008136. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_ECOL5 Reviewed; 211 AA. AC Q0TA72; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 14-MAY-2014, entry version 55. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=ECP_4206; OS Escherichia coli O6:K15:H31 (strain 536 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=362663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=536 / UPEC; RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x; RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.; RT "Role of pathogenicity island-associated integrases in the genome RT plasticity of uropathogenic Escherichia coli strain 536."; RL Mol. Microbiol. 61:584-595(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000247; ABG72157.1; -; Genomic_DNA. DR RefSeq; YP_672058.1; NC_008253.1. DR ProteinModelPortal; Q0TA72; -. DR SMR; Q0TA72; 10-208. DR STRING; 362663.ECP_4206; -. DR EnsemblBacteria; ABG72157; ABG72157; ECP_4206. DR GeneID; 4188259; -. DR KEGG; ecp:ECP_4206; -. DR PATRIC; 18199335; VBIEscCol77757_4252. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR PhylomeDB; Q0TA72; -. DR BioCyc; ECOL362663:GIY5-4244-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000008137. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23086 MW; 1A8F52AF19C8B3F0 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ERPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_ECOL6 Reviewed; 211 AA. AC Q8FB78; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 23-APR-2003, sequence version 2. DT 14-MAY-2014, entry version 81. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=c4950; OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=199310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFT073 / ATCC 700928 / UPEC; RX PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence RT of uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAN83378.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014075; AAN83378.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_756804.1; NC_004431.1. DR ProteinModelPortal; Q8FB78; -. DR SMR; Q8FB78; 9-208. DR STRING; 199310.c4950; -. DR EnsemblBacteria; AAN83378; AAN83378; c4950. DR GeneID; 1039862; -. DR KEGG; ecc:c4950; -. DR PATRIC; 18287598; VBIEscCol75197_4649. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000157011. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23030 MW; D9436839F2B7F407 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDQRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSTIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_ECOLC Reviewed; 211 AA. AC B1IUQ4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=EcolC_4032; OS Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=481805; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8739 / DSM 1576 / Crooks; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Ingram L., Richardson P.; RT "Complete sequence of Escherichia coli C str. ATCC 8739."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000946; ACA79631.1; -; Genomic_DNA. DR RefSeq; YP_001726958.1; NC_010468.1. DR ProteinModelPortal; B1IUQ4; -. DR SMR; B1IUQ4; 20-202. DR STRING; 481805.EcolC_4032; -. DR EnsemblBacteria; ACA79631; ACA79631; EcolC_4032. DR GeneID; 6064671; -. DR KEGG; ecl:EcolC_4032; -. DR PATRIC; 18231277; VBIEscCol82905_4320. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL481805:GI3G-4125-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000075571. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_ECOLI Reviewed; 211 AA. AC P30137; Q2M8T0; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 14-MAY-2014, entry version 123. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=b3993, JW3957; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=8432721; RA Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P.; RT "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in RT Escherichia coli K-12."; RL J. Bacteriol. 175:982-992(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8265357; DOI=10.1093/nar/21.23.5408; RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., RA Daniels D.L.; RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the RT region from 89.2 to 92.8 minutes."; RL Nucleic Acids Res. 21:5408-5417(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, AND KINETIC PARAMETERS. RA Backstrom A.D., Austin R., McMordie S., Begley T.P.; RT "Biosynthesis of thiamin I: the function of the thiE gene product."; RL J. Am. Chem. Soc. 117:2351-2352(1995). RN [6] RP MASS SPECTROMETRY. RX PubMed=10082377; RA Kelleher N.L., Taylor S.V., Grannis D., Kinsland C., Chiu H.-J., RA Begley T.P., McLafferty F.W.; RT "Efficient sequence analysis of the six gene products (7-74 kDa) from RT the Escherichia coli thiamin biosynthetic operon by tandem high- RT resolution mass spectrometry."; RL Protein Sci. 7:1796-1801(1998). RN [7] RP FUNCTION IN THIAMINE METABOLISM. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15292217; DOI=10.1074/jbc.M404284200; RA Lawhorn B.G., Gerdes S.Y., Begley T.P.; RT "A genetic screen for the identification of thiamin metabolic genes."; RL J. Biol. Chem. 279:43555-43559(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1 uM for HMP-PP; CC KM=2 uM for THZ-P; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- MASS SPECTROMETRY: Mass=23014.8; Method=Electrospray; Range=1-211; CC Source=PubMed:10082377; CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M88701; AAB95617.1; -; Genomic_DNA. DR EMBL; U00006; AAC43091.1; -; Genomic_DNA. DR EMBL; U00096; AAC76967.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77326.1; -; Genomic_DNA. DR PIR; S35118; S35118. DR RefSeq; NP_418421.1; NC_000913.3. DR RefSeq; YP_491467.1; NC_007779.1. DR ProteinModelPortal; P30137; -. DR SMR; P30137; 20-202. DR DIP; DIP-10983N; -. DR IntAct; P30137; 4. DR MINT; MINT-1247897; -. DR STRING; 511145.b3993; -. DR SWISS-2DPAGE; P30137; -. DR EnsemblBacteria; AAC76967; AAC76967; b3993. DR EnsemblBacteria; BAE77326; BAE77326; BAE77326. DR GeneID; 12930339; -. DR GeneID; 948491; -. DR KEGG; ecj:Y75_p3203; -. DR KEGG; eco:b3993; -. DR PATRIC; 32123509; VBIEscCol129921_4107. DR EchoBASE; EB1545; -. DR EcoGene; EG11586; thiE. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR PhylomeDB; P30137; -. DR BioCyc; EcoCyc:THIE-MONOMER; -. DR BioCyc; ECOL316407:JW3957-MONOMER; -. DR BioCyc; MetaCyc:THIE-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR PRO; PR:P30137; -. DR Genevestigator; P30137; -. DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc. DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IDA:EcoCyc. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 1: Evidence at protein level; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000157010. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64; MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_ECOSE Reviewed; 211 AA. AC B6I5K4; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=ECSE_4281; OS Escherichia coli (strain SE11). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=409438; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SE11; RX PubMed=18931093; DOI=10.1093/dnares/dsn026; RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., RA Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.; RT "Complete genome sequence and comparative analysis of the wild-type RT commensal Escherichia coli strain SE11 isolated from a healthy RT adult."; RL DNA Res. 15:375-386(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009240; BAG79805.1; -; Genomic_DNA. DR RefSeq; YP_002295556.1; NC_011415.1. DR ProteinModelPortal; B6I5K4; -. DR SMR; B6I5K4; 10-208. DR STRING; 409438.ECSE_4281; -. DR EnsemblBacteria; BAG79805; BAG79805; ECSE_4281. DR GeneID; 7002666; -. DR KEGG; ecy:ECSE_4281; -. DR PATRIC; 18427268; VBIEscCol83070_4460. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL409438:GHUU-4372-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000093668. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_ECOUT Reviewed; 211 AA. AC Q1R5V9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=UTI89_C3826; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UTI89 / UPEC; RX PubMed=16585510; DOI=10.1073/pnas.0600938103; RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., RA Hultgren S.J., Gordon J.I.; RT "Identification of genes subject to positive selection in RT uropathogenic strains of Escherichia coli: a comparative genomics RT approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=ABE09255.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000243; ABE09255.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_542786.1; NC_007946.1. DR ProteinModelPortal; Q1R5V9; -. DR SMR; Q1R5V9; 9-208. DR STRING; 364106.UTI89_C3826; -. DR EnsemblBacteria; ABE09255; ABE09255; UTI89_C3826. DR GeneID; 3990799; -. DR KEGG; eci:UTI89_C3826; -. DR PATRIC; 18457098; VBIEscCol42261_3748. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ECOL364106:GHPQ-3789-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000336394. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23028 MW; 704F56EB1D88F7F4 CRC64; MYQPEFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_ENT38 Reviewed; 211 AA. AC A4W5B6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Ent638_0206; OS Enterobacter sp. (strain 638). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=399742; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=638; RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943; RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D., RA Vangronsveld J., Newman L., Monchy S.; RT "Genome sequence of the plant growth promoting endophytic bacterium RT Enterobacter sp. 638."; RL PLoS Genet. 6:E1000943-E1000943(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000653; ABP58896.1; -; Genomic_DNA. DR RefSeq; YP_001174947.1; NC_009436.1. DR ProteinModelPortal; A4W5B6; -. DR STRING; 399742.Ent638_0206; -. DR EnsemblBacteria; ABP58896; ABP58896; Ent638_0206. DR GeneID; 5110707; -. DR KEGG; ent:Ent638_0206; -. DR PATRIC; 20409930; VBIEntSp101211_0334. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; ESP399742:GJ0E-212-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000057643. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23064 MW; 0211A44A59418480 CRC64; MYQPDFPPVP FRLGLYPVVD SVVWIERLLQ AGVKTLQLRI KDKCDEDVEP DVANAIKLGR RYGARLFIND YWQLAIQHQA YGVHLGQEDL ETTDLSAIRN AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLT RHIERLADYP TVAIGGISLE RVPAVLKTGV GSVAVVSAIT QAADWQVATA QLLQLAGAGD E // ID THIE_ENTFA Reviewed; 211 AA. AC Q830K5; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 75. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=EF_2776; OS Enterococcus faecalis (strain ATCC 700802 / V583). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=226185; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700802 / V583; RX PubMed=12663927; DOI=10.1126/science.1080613; RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., RA Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., RA Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., RA Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., RA Fraser C.M.; RT "Role of mobile DNA in the evolution of vancomycin-resistant RT Enterococcus faecalis."; RL Science 299:2071-2074(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016830; AAO82473.1; -; Genomic_DNA. DR RefSeq; NP_816403.1; NC_004668.1. DR ProteinModelPortal; Q830K5; -. DR STRING; 226185.EF2776; -. DR EnsemblBacteria; AAO82473; AAO82473; EF_2776. DR GeneID; 1201626; -. DR KEGG; efa:EF2776; -. DR PATRIC; 21855735; VBIEntFae7065_2587. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; IESENSH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; EFAE226185:GHI1-2710-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000157013. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22909 MW; 8B29A97E305C6782 CRC64; MREKLKVYLV TGRYDFSDTE FLKRIETACR SGVTLVQLRE KEVSTRRFYE LAVKVKVVTD AYQIPLIIND RVDICLAVDA AGVHIGDDEL PVALVRKLVG STKIVGVSAK TVARGVEAEN EGADYLGVGA IFPTTTKDSP LTSLQTLSEI AAAVTIPVVA IGGIKEENIE QLMGTGVAGV SLVSEIMLAE QITEKVQGLM RVTERMLEAR K // ID THIE_PECAS Reviewed; 213 AA. AC Q6DAM1; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 14-MAY-2014, entry version 69. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=ECA0231; OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia OS carotovora subsp. atroseptica). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pectobacterium. OX NCBI_TaxID=218491; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCRI 1043 / ATCC BAA-672; RX PubMed=15263089; DOI=10.1073/pnas.0402424101; RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H., RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.; RT "Genome sequence of the enterobacterial phytopathogen Erwinia RT carotovora subsp. atroseptica and characterization of virulence RT factors."; RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX950851; CAG73151.1; -; Genomic_DNA. DR RefSeq; YP_048359.1; NC_004547.2. DR ProteinModelPortal; Q6DAM1; -. DR STRING; 218491.ECA0231; -. DR EnsemblBacteria; CAG73151; CAG73151; ECA0231. DR GeneID; 2884295; -. DR KEGG; eca:ECA0231; -. DR PATRIC; 20475629; VBIPecAtr54885_0233. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PATR218491:GJNB-242-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000336392. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23067 MW; 042A93638E4520C9 CRC64; MTDSTPFAPT AQRLGLYPVV DSVEWIERLL GVGVKTIQLR IKDRSDEQAE TDVIQAIALG SRYQAQLFIN DYWTLAVKHQ AYGVHLGQED LDTADLAAIK KAGLRLGVST HYDRELARAV AINPSYIALG HIFPTQTKDM PSAPQGLAEL TRHIADLQGR FPTVAIGGIS IDRVPAVLAT GVGSIAVVSA ITQAPDWRQA TATLLKMIEG REA // ID THIE_ERYLH Reviewed; 213 AA. AC Q2NB00; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 14-MAY-2014, entry version 57. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=ELI_05245; OS Erythrobacter litoralis (strain HTCC2594). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=314225; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2594; RX PubMed=19168610; DOI=10.1128/JB.00026-09; RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.; RT "Complete genome sequence of Erythrobacter litoralis HTCC2594."; RL J. Bacteriol. 191:2419-2420(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000157; ABC63141.1; -; Genomic_DNA. DR RefSeq; YP_457938.1; NC_007722.1. DR ProteinModelPortal; Q2NB00; -. DR STRING; 314225.ELI_05245; -. DR EnsemblBacteria; ABC63141; ABC63141; ELI_05245. DR GeneID; 3869146; -. DR KEGG; eli:ELI_05245; -. DR PATRIC; 21859216; VBIEryLit102657_1039. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; FQFRVKG; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; ELIT314225:GHLE-1074-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000336393. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22700 MW; 9128A83AD2165146 CRC64; MAETEIPTQL YLISPLDVRG GFPQRLERAL EAGRGVVTAF QFRVKGIDQH EAARLAEPLQ AICAAHDVAF VVNDSIALAK RLKADGVHLG QDDGSPKEAR EQLGREAQIG VTCHASRHLA MEAGEAGADY VAFGAFFDSA TKDKGDAEQP TLELLEWWSQ VFEIPCVAIG GITPDNCQPL IEAGADFLAV SGAVWSGDER AAVQAFAEQI AAA // ID THIE_FLAJ1 Reviewed; 212 AA. AC A5FJJ1; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Fjoh_1600; OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) OS (Cytophaga johnsonae). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=376686; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17061 / DSM 2064 / UW101; RX PubMed=19717629; DOI=10.1128/AEM.01495-09; RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., RA Rhodes R.G., Goltsman E., Wang W., Xu J., Hunnicutt D.W., RA Staroscik A.M., Hoover T.R., Cheng Y.Q., Stein J.L.; RT "Novel features of the polysaccharide-digesting gliding bacterium RT Flavobacterium johnsoniae as revealed by genome sequence analysis."; RL Appl. Environ. Microbiol. 75:6864-6875(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000685; ABQ04632.1; -; Genomic_DNA. DR RefSeq; YP_001193951.1; NC_009441.1. DR ProteinModelPortal; A5FJJ1; -. DR STRING; 376686.Fjoh_1600; -. DR EnsemblBacteria; ABQ04632; ABQ04632; Fjoh_1600. DR GeneID; 5090951; -. DR KEGG; fjo:Fjoh_1600; -. DR PATRIC; 21897539; VBIFlaJoh53613_1645. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; FJOH376686:GIXN-1631-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_0000336395. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23824 MW; 807E714B364CC649 CRC64; MYNKLQYISQ GNTIEDQVRN IHQALDSGCD WIQMRFKNQT EKDSFILAEE IKLLCEKYLA SFIINDNLYL AQQINADGVH LGLSDMKIDE ARTILGAEKI IGGTANTFED IQNHVKNGCN YIGLGPFRFT NTKEKLSPIL GLSGYFEILQ KMKKNKIEVP VYAIGGITLK DINPLMETGI HGIAVSGIIT ESDEKKILIQ QLNEKLYANV IV // ID THIE_FLAPJ Reviewed; 206 AA. AC A6GWR9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=FP0431; OS Flavobacterium psychrophilum (strain JIP02/86 / ATCC 49511). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=402612; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JIP02/86 / ATCC 49511; RX PubMed=17592475; DOI=10.1038/nbt1313; RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., RA Kerouault B., Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., RA Gibrat J.-F., Claverol S., Dumetz F., Le Henaff M., Benmansour A.; RT "Complete genome sequence of the fish pathogen Flavobacterium RT psychrophilum."; RL Nat. Biotechnol. 25:763-769(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM398681; CAL42542.1; -; Genomic_DNA. DR RefSeq; YP_001295360.1; NC_009613.3. DR ProteinModelPortal; A6GWR9; -. DR STRING; 402612.FP0431; -. DR EnsemblBacteria; CAL42542; CAL42542; FP0431. DR GeneID; 5299666; -. DR KEGG; fps:FP0431; -. DR PATRIC; 21905718; VBIFlaPsy4505_0445. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; FPSY402612:GJEP-752-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 206 Thiamine-phosphate synthase. FT /FTId=PRO_0000336396. FT REGION 33 37 HMP-PP binding (By similarity). FT REGION 130 132 THZ-P binding (By similarity). FT METAL 66 66 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT BINDING 65 65 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 23148 MW; 7F73B12BADE3F75A CRC64; MYNKLQYISQ GKTIEEQLLN IRKALENGCQ WIQMRFKDTH SDNVFTLAEA VKRMCQEYTA TFIINDNVYL AKKINADGVH LGLNDMNIAE ARTILGEAKI IGGTANTFEE VLQRTAENCN YIGLGPFQFT ATKEKLSPVL GLEGYHLIIQ QMKTKKNKIP IYAIGGIQLE NVDDIMKTGI YGIAVSGLIT QSENPFQLIT QLNKKL // ID THIE_FUSNN Reviewed; 206 AA. AC Q8RI59; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 14-MAY-2014, entry version 79. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=FN1758; OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP OS 101130 / JCM 8532 / LMG 13131). OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=190304; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131; RX PubMed=11889109; DOI=10.1128/JB.184.7.2005-2018.2002; RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A., RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., RA Vasieva O., Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., RA Larsen N., D'Souza M., Walunas T., Pusch G., Haselkorn R., RA Fonstein M., Kyrpides N.C., Overbeek R.; RT "Genome sequence and analysis of the oral bacterium Fusobacterium RT nucleatum strain ATCC 25586."; RL J. Bacteriol. 184:2005-2018(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE009951; AAL93873.1; -; Genomic_DNA. DR RefSeq; NP_602574.1; NC_003454.1. DR ProteinModelPortal; Q8RI59; -. DR STRING; 190304.FN1758; -. DR EnsemblBacteria; AAL93873; AAL93873; FN1758. DR GeneID; 992623; -. DR KEGG; fnu:FN1758; -. DR PATRIC; 21949035; VBIFusNuc122357_0248. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 206 Thiamine-phosphate synthase. FT /FTId=PRO_0000157014. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22966 MW; 0BB82B5F632778CA CRC64; MDLKDCKIYL VTDEKACNGK DFYKCIEESI KGGVKIVQLR EKNISTKDFY KKALKVKEIC KNYEVLFIIN DRLDITQAVE ADGVHLGQSD MPIEKAREIL KDKFLIGATA RNIEEAEKAQ LLGADYIGSG AIFGTSTKDN AKRLEMEDLK KIVNSVKIPV FAIGGININN VWMLKNIGLQ GVCSVSGILS EKDCKKAVEN ILKNFN // ID THIE_GEOKA Reviewed; 221 AA. AC Q5KZU0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=GK1511; OS Geobacillus kaustophilus (strain HTA426). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=235909; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTA426; RX PubMed=15576355; DOI=10.1093/nar/gkh970; RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., RA Matsui S., Uchiyama I.; RT "Thermoadaptation trait revealed by the genome sequence of RT thermophilic Geobacillus kaustophilus."; RL Nucleic Acids Res. 32:6292-6303(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000043; BAD75796.1; -; Genomic_DNA. DR RefSeq; YP_147364.1; NC_006510.1. DR ProteinModelPortal; Q5KZU0; -. DR SMR; Q5KZU0; 1-220. DR STRING; 235909.GK1511; -. DR EnsemblBacteria; BAD75796; BAD75796; GK1511. DR GeneID; 3184797; -. DR KEGG; gka:GK1511; -. DR PATRIC; 21964317; VBIGeoKau81518_1626. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GKAU235909:GJO7-1587-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 221 Thiamine-phosphate synthase. FT /FTId=PRO_1000008138. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23044 MW; FCC8031FF0737252 CRC64; MVRIASGEMK ERLAVYFIMG SQNSERPAAD VLKEALDGGV TLFQFREKGP GALKGADKEA LARQLQRLCR AYGVPFIVND DVELALAIDA DGVHVGQDDE DARRVREKIG DKILGVSAHN VEEAMAAVEA GADYLGVGPI YPTSSKEDAK EAQGPDVLRR LREAGITIPI VAIGGITAAN AKTVVEAGAD GVSVISAIAS APSPKAAAAA LAEAVRAART R // ID THIE_GEOSL Reviewed; 213 AA. AC P61411; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 1. DT 14-MAY-2014, entry version 73. DE RecName: Full=Putative thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=GSU0587; OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=243231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51573 / DSM 12127 / PCA; RX PubMed=14671304; DOI=10.1126/science.1088727; RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C., RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J., RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A., RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., RA Van Aken S.E., Lovley D.R., Fraser C.M.; RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface RT environments."; RL Science 302:1967-1969(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017180; AAR33918.1; -; Genomic_DNA. DR RefSeq; NP_951645.1; NC_002939.5. DR ProteinModelPortal; P61411; -. DR STRING; 243231.GSU0587; -. DR EnsemblBacteria; AAR33918; AAR33918; GSU0587. DR GeneID; 2685827; -. DR KEGG; gsu:GSU0587; -. DR PATRIC; 22023923; VBIGeoSul17553_0585. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; SCHSEAD; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GSUL243231:GH27-592-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 213 Putative thiamine-phosphate synthase. FT /FTId=PRO_0000157015. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22139 MW; 0F2B52608A092621 CRC64; MAKVDFSLYL ITDRHQAGGR DLLAVVEGAL AGGVRCVQLR EKDLPARTLL ELARAMRRLT DRFGARLLIN DRVDIALAAG ADGVHLGEEG MPAAVARELL GSGRLIGVSC HGRGGAAAAV AQGADFITFG PVYPTPSKAA YGEPVGIDQL AATTKEIHIP VFALGGIKEA NIPEALAAGA AGVALISAII ADPDPRERAR ALLALLPPRT RDE // ID THIE_GEOTN Reviewed; 221 AA. AC A4IN28; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=GTNG_1362; OS Geobacillus thermodenitrificans (strain NG80-2). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=420246; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NG80-2; RX PubMed=17372208; DOI=10.1073/pnas.0609650104; RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., RA Han W., Peng X., Liu R., Wang L.; RT "Genome and proteome of long-chain alkane degrading Geobacillus RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil RT reservoir."; RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000557; ABO66732.1; -; Genomic_DNA. DR RefSeq; YP_001125477.1; NC_009328.1. DR ProteinModelPortal; A4IN28; -. DR SMR; A4IN28; 1-218. DR STRING; 420246.GTNG_1362; -. DR EnsemblBacteria; ABO66732; ABO66732; GTNG_1362. DR GeneID; 4966301; -. DR KEGG; gtn:GTNG_1362; -. DR PATRIC; 21979103; VBIGeoThe136879_1431. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GTHE420246:GIXT-1434-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 221 Thiamine-phosphate synthase. FT /FTId=PRO_1000008139. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23485 MW; 86F1A7724AD4291D CRC64; MARITSEEMK ERLAVYFIMG SQNSERPAED VLKEALDGGV TLFQFREKGS AALEGEEKEA LARQLQRLCR TYGVPFIVND DVELAIAIDA DGVHVGQDDE DARRVREKIG DKILGVSAHN VEEARAAIEA GADYIGVGPI YPTRSKDDAN EAQGPGILRH LREQGITIPI VAIGGITADN TRAVIEAGAD GVSVISAIAS APEPKAAAAA LATAVREANL R // ID THIE_GLOVI Reviewed; 341 AA. AC Q7NNK8; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 14-MAY-2014, entry version 75. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=gll0403; OS Gloeobacter violaceus (strain PCC 7421). OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacter. OX NCBI_TaxID=251221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7421; RX PubMed=14621292; DOI=10.1093/dnares/10.4.137; RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a RT cyanobacterium that lacks thylakoids."; RL DNA Res. 10:137-145(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAC88344.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000045; BAC88344.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_923349.1; NC_005125.1. DR ProteinModelPortal; Q7NNK8; -. DR STRING; 251221.gvip037; -. DR PRIDE; Q7NNK8; -. DR EnsemblBacteria; BAC88344; BAC88344; BAC88344. DR GeneID; 2599707; -. DR KEGG; gvi:gvip037; -. DR PATRIC; 22040167; VBIGloVio86258_0409. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; GVIO251221:GH9A-406-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 341 Thiamine-phosphate synthase. FT /FTId=PRO_0000157079. FT REGION 1 123 Unknown. FT REGION 124 341 Thiamine-phosphate synthase. FT REGION 171 175 HMP-PP binding (By similarity). FT REGION 268 270 THZ-P binding (By similarity). FT METAL 204 204 Magnesium (By similarity). FT METAL 223 223 Magnesium (By similarity). FT BINDING 203 203 HMP-PP (By similarity). FT BINDING 242 242 HMP-PP (By similarity). FT BINDING 271 271 HMP-PP (By similarity). FT BINDING 298 298 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 341 AA; 37236 MW; AFE66A6883CB4F14 CRC64; MAVVEEQVVL RILDANLDRA REGVRVVEEW LRFGGGPGES LAECKALRQQ LGRFHTERLR AARDTPHDPG TGLEHPDEGV RSSPLDVVRV NFARIQEALR VLEEYAKLVQ PDLAAAAKEW RYRVYTLEST ATGGDLRTRL AAARLYLVTS PHPELIEIVE HALAVGLPLV QLREKEAPAR AVLDIALRLR DVTLRHGALF IVNDRVDLAL ACGADGVHLG QEDLPLARAR ALMGPRLLIG QSTHAPAEAQ QAVADGADYL GVGPVYATPT KQGRTPVGLE YVRHCRESIE RPGFAIGGID RSNLEAVIAA GAERIAVVRA IMAAEDPGRT TAWFLERLNR G // ID THIE_HAEI8 Reviewed; 226 AA. AC Q4QNC6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 14-MAY-2014, entry version 56. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=NTHI0542; OS Haemophilus influenzae (strain 86-028NP). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=281310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=86-028NP; RX PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005; RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., RA Munson R.S. Jr.; RT "Genomic sequence of an otitis media isolate of nontypeable RT Haemophilus influenzae: comparative study with H. influenzae serotype RT d, strain KW20."; RL J. Bacteriol. 187:4627-4636(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000057; AAX87471.1; -; Genomic_DNA. DR RefSeq; YP_248131.1; NC_007146.2. DR ProteinModelPortal; Q4QNC6; -. DR STRING; 281310.NTHI0542; -. DR EnsemblBacteria; AAX87471; AAX87471; NTHI0542. DR GeneID; 3429856; -. DR KEGG; hit:NTHI0542; -. DR PATRIC; 20181249; VBIHaeInf100748_0499. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HINF281310:GJ89-508-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 226 Thiamine-phosphate synthase. FT /FTId=PRO_1000008140. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24750 MW; 4923365317694040 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNV GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID THIE_HAEIE Reviewed; 226 AA. AC A5UA71; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CGSHiEE_00910; OS Haemophilus influenzae (strain PittEE). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=374930; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PittEE; RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103; RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., RA Post J.C., Ehrlich G.D.; RT "Characterization and modeling of the Haemophilus influenzae core and RT supragenomes based on the complete genomic sequences of Rd and 12 RT clinical nontypeable strains."; RL Genome Biol. 8:R103.1-R103.18(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000671; ABQ97672.1; -; Genomic_DNA. DR RefSeq; YP_001290055.1; NC_009566.1. DR ProteinModelPortal; A5UA71; -. DR STRING; 374930.CGSHiEE_00910; -. DR EnsemblBacteria; ABQ97672; ABQ97672; CGSHiEE_00910. DR GeneID; 5225337; -. DR KEGG; hip:CGSHiEE_00910; -. DR PATRIC; 20276361; VBIHaeInf81350_0181. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HINF374930:GJDD-170-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 226 Thiamine-phosphate synthase. FT /FTId=PRO_1000008141. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24750 MW; 4923365317694040 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAMSCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNV GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID THIE_HAEIG Reviewed; 226 AA. AC A5UGT0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=CGSHiGG_05275; OS Haemophilus influenzae (strain PittGG). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=374931; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PittGG; RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103; RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., RA Post J.C., Ehrlich G.D.; RT "Characterization and modeling of the Haemophilus influenzae core and RT supragenomes based on the complete genomic sequences of Rd and 12 RT clinical nontypeable strains."; RL Genome Biol. 8:R103.1-R103.18(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000672; ABQ99985.1; -; Genomic_DNA. DR RefSeq; YP_001292369.1; NC_009567.1. DR ProteinModelPortal; A5UGT0; -. DR STRING; 374931.CGSHiGG_05275; -. DR EnsemblBacteria; ABQ99985; ABQ99985; CGSHiGG_05275. DR GeneID; 5226388; -. DR KEGG; hiq:CGSHiGG_05275; -. DR PATRIC; 20186360; VBIHaeInf102487_1063. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HINF374931:GJA4-912-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 226 Thiamine-phosphate synthase. FT /FTId=PRO_1000008142. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24672 MW; 6C2E14DED084FAE4 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAINCR DLCREYGVPF IVDDNVDLAL AIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID THIE_HAEIN Reviewed; 226 AA. AC P71350; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 14-MAY-2014, entry version 100. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=HI_0417; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.3.CO;2-W; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22075.1; -; Genomic_DNA. DR PIR; A64152; A64152. DR RefSeq; NP_438579.1; NC_000907.1. DR ProteinModelPortal; P71350; -. DR STRING; 71421.HI0417; -. DR EnsemblBacteria; AAC22075; AAC22075; HI_0417. DR GeneID; 949518; -. DR KEGG; hin:HI0417; -. DR PATRIC; 20189387; VBIHaeInf48452_0437. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 1: Evidence at protein level; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 226 Thiamine-phosphate synthase. FT /FTId=PRO_0000157016. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 24730 MW; C5EB00DED081EEE7 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAINCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID THIE_HISS1 Reviewed; 221 AA. AC Q0I131; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=HS_0090; OS Histophilus somni (strain 129Pt) (Haemophilus somnus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Histophilus. OX NCBI_TaxID=205914; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=129Pt; RX PubMed=17172329; DOI=10.1128/JB.01422-06; RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., RA Xie G., Inzana T.J.; RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) RT strain 129Pt and comparison to Haemophilus ducreyi 35000HP and RT Haemophilus influenzae Rd."; RL J. Bacteriol. 189:1890-1898(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000436; ABI24371.1; -; Genomic_DNA. DR RefSeq; YP_718297.1; NC_008309.1. DR ProteinModelPortal; Q0I131; -. DR STRING; 205914.HS_0090; -. DR EnsemblBacteria; ABI24371; ABI24371; HS_0090. DR GeneID; 4239599; -. DR KEGG; hso:HS_0090; -. DR PATRIC; 20280082; VBIHaeSom53361_0099. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HSOM205914:GJ7V-94-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 221 Thiamine-phosphate synthase. FT /FTId=PRO_0000336397. FT REGION 49 53 HMP-PP binding (By similarity). FT REGION 151 153 THZ-P binding (By similarity). FT REGION 203 204 THZ-P binding (By similarity). FT METAL 86 86 Magnesium (By similarity). FT METAL 105 105 Magnesium (By similarity). FT BINDING 85 85 HMP-PP (By similarity). FT BINDING 124 124 HMP-PP (By similarity). FT BINDING 154 154 HMP-PP (By similarity). FT BINDING 183 183 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 24035 MW; 2FD266A2E9690560 CRC64; MQHKYDIATA MRLYFIAGSQ DVTHFASDPA DNLLSVLEQA LQAGITCYQF REKGKRALQN PIAYKALAIA CRNLCRKYKV PFVVNDDVAL AVEIGADGIH VGQTDMPPHQ VKRLCTGKCF VGTSVNTIEQ GLIAQNDPNV DYFGVGPIFP TQSKEDAEPV LSPAFITQIR ANHIDKPMVA IGGIKVKDVA MLMAKGANGV AVISAITQSN HIEKTVKELL R // ID THIE_HALHL Reviewed; 209 AA. AC A1WYL4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Hhal_2012; OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira OS halophila (strain DSM 244 / SL1)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Halorhodospira. OX NCBI_TaxID=349124; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 244 / SL1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Hoff W., Richardson P.; RT "Complete sequence of Halorhodospira halophila SL1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000544; ABM62776.1; -; Genomic_DNA. DR RefSeq; YP_001003578.1; NC_008789.1. DR ProteinModelPortal; A1WYL4; -. DR STRING; 349124.Hhal_2012; -. DR EnsemblBacteria; ABM62776; ABM62776; Hhal_2012. DR GeneID; 4710409; -. DR KEGG; hha:Hhal_2012; -. DR PATRIC; 22098319; VBIHalHal112047_1987. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HHAL349124:GI3I-2061-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_0000336398. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21913 MW; ACE9F0D12CC292BE CRC64; MNKQPSQLAG VYAVTQPRPD LQEAVAAVLR GGVGIVQYRD KSEDADRRRE EAGALCRLCE EYGALFLVND DVDLAAAVAA HGVHLGRDDG AVVAARQQLG DTAWIGVSCY DDLDRARRLV AEGADYVAFG SIFPSPTKPE SGLAPMELLR SGREATGCPT VAIGGIDAGN IHEVAAAGAD AAAVVSALFA AEDPEAAARQ LVAQWQRSR // ID THIE_HALMA Reviewed; 211 AA. AC Q5V0G6; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=rrnAC2143; OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM OS B-1809) (Halobacterium marismortui). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Haloarcula. OX NCBI_TaxID=272569; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809; RX PubMed=15520287; DOI=10.1101/gr.2700304; RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., RA Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., RA Date S.V., Marcotte E., Hood L., Ng W.V.; RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from RT the Dead Sea."; RL Genome Res. 14:2221-2234(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY596297; AAV46987.1; -; Genomic_DNA. DR RefSeq; YP_136693.1; NC_006396.1. DR ProteinModelPortal; Q5V0G6; -. DR STRING; 272569.rrnAC2143; -. DR EnsemblBacteria; AAV46987; AAV46987; rrnAC2143. DR GeneID; 3128916; -. DR KEGG; hma:rrnAC2143; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; EKNRTAR; -. DR BioCyc; HMAR272569:GJDH-1931-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000157068. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21897 MW; A50351BF3C7F8005 CRC64; MVDWDVYLVT QASLSAGRTT DEIVAEAIES GVGVVQLREK NRTARERYEL GQKLRELTRE ADVTFVVNDR IDLAQAIDAD GVHLGDDDLP VSVARDILGD DAVIGRSVST VEDAREAATA GADYLGVGAV FATGSKDDID DEEYAVGTDR VAAIAEAVDI PFVGIGGITA GNATAVVDAG ADGVAVITEI TKADDPAAAA EALHSAVEQG R // ID THIE_HALWD Reviewed; 223 AA. AC Q18GX9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=HQ_2655A; OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Haloquadratum. OX NCBI_TaxID=362976; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16790 / HBSQ001; RX PubMed=16820047; DOI=10.1186/1471-2164-7-169; RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., RA Pfeiffer F., Oesterhelt D.; RT "The genome of the square archaeon Haloquadratum walsbyi: life at the RT limits of water activity."; RL BMC Genomics 7:169-169(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM180088; CAJ52766.1; -; Genomic_DNA. DR RefSeq; YP_658372.1; NC_008212.1. DR ProteinModelPortal; Q18GX9; -. DR STRING; 362976.HQ2655A; -. DR EnsemblBacteria; CAJ52766; CAJ52766; HQ_2655A. DR GeneID; 4194763; -. DR KEGG; hwa:HQ2655A; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; RPTPTKN; -. DR BioCyc; HWAL362976:GJSR-1756-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 223 Thiamine-phosphate synthase. FT /FTId=PRO_0000336434. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 22907 MW; F19828A011C6323C CRC64; MNTSMQTYLV TQEDRSAGRS TTEIVEAAID GGIDIVQLRE KETTARRRYE IGQTVRTQTA QAGVTFLVND RVDLAAAVNA DGVHLGDDDL PVTAAREVLG QDAIIGRSVS TPAAAQRAED IGADYLGVGA VYPTGTKDVT AESAEIGPKT VTAITDAVSI PVIGIGGITP SNTTEVIRAG ADGVAVVSAI TTADDPAAAT RKLQGSVDTA SVESQLPSEE PSA // ID THIE_HELPH Reviewed; 219 AA. AC Q1CT27; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 55. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=HPAG1_0828; OS Helicobacter pylori (strain HPAG1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=357544; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HPAG1; RX PubMed=16788065; DOI=10.1073/pnas.0603784103; RA Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., RA Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., RA Mardis E.R., Engstrand L.G., Gordon J.I.; RT "The complete genome sequence of a chronic atrophic gastritis RT Helicobacter pylori strain: evolution during disease progression."; RL Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000241; ABF84895.1; -; Genomic_DNA. DR RefSeq; YP_627569.1; NC_008086.1. DR ProteinModelPortal; Q1CT27; -. DR STRING; 357544.HPAG1_0828; -. DR EnsemblBacteria; ABF84895; ABF84895; HPAG1_0828. DR GeneID; 4098194; -. DR KEGG; hpa:HPAG1_0828; -. DR PATRIC; 20603025; VBIHelPyl56048_0859. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HPYL357544:GH1F-840-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000008143. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 24052 MW; 6A1C4D90672446B5 CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDTLELAL QSQITAFQFR QKGDLALQDP VEIKQLALKC QKLCQKYGTP FIINDEVRLA LELKADGVHV GQEDMAIEEV IALCKKHQFI GLSVNTLEQA LKARHLDAVA YFGVGPIFPT PSKKDKQVVG VELLKKIRDS GVKKPLIAIG GITTHNASKL REYGGIAVIS AITQARDKAL AIEKLLNNA // ID THIE_HELPJ Reviewed; 217 AA. AC Q9ZL01; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 14-MAY-2014, entry version 92. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=jhp_0781; OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori OS J99). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J99 / ATCC 700824; RX PubMed=9923682; DOI=10.1038/16495; RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., RA Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., RA Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., RA Trust T.J.; RT "Genomic sequence comparison of two unrelated isolates of the human RT gastric pathogen Helicobacter pylori."; RL Nature 397:176-180(1999). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE001439; AAD06361.1; -; Genomic_DNA. DR PIR; G71889; G71889. DR RefSeq; NP_223499.1; NC_000921.1. DR ProteinModelPortal; Q9ZL01; -. DR STRING; 85963.jhp0781; -. DR EnsemblBacteria; AAD06361; AAD06361; jhp_0781. DR GeneID; 890113; -. DR KEGG; hpj:jhp0781; -. DR PATRIC; 20606295; VBIHelPyl98156_0852. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HPYL85963:GJB9-794-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_0000157018. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 197 198 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23810 MW; 817416264C1AA210 CRC64; MFDANCLKLM FVAGSQDFYH IKGDRTNALL DTLELALQSK ITAFQFRQKG DLALQDPVEI KRLALECQKL CKKYGTPFII NDEVRLALEL KADGVHVGQE DMAIEEVVTL CQKRLFIGLS VNTLEQALKA RHLDHIAYLG VGPIFPTPSK KDAKEVVGVN LLKKIHDSGV EKPLIAIGGI TTDNASKLQK FSGIAVISAI TQAKDKALAV EKLLKNA // ID THIE_HELPS Reviewed; 219 AA. AC B2USY5; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=HPSH_02585; OS Helicobacter pylori (strain Shi470). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=512562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Shi470; RA Kersulyte D., Kalia A., Gilman R.H., Berg D.E.; RT "Genome sequence of Helicobacter pylori from the remote Amazon: traces RT of Asian ancestry of the first Americans."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001072; ACD47967.1; -; Genomic_DNA. DR RefSeq; YP_001909997.1; NC_010698.2. DR ProteinModelPortal; B2USY5; -. DR STRING; 512562.HPSH_02585; -. DR EnsemblBacteria; ACD47967; ACD47967; HPSH_02585. DR GeneID; 6296133; -. DR KEGG; hps:HPSH_02585; -. DR PATRIC; 20612383; VBIHelPyl23559_0504. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HPYL512562:GHHZ-518-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_1000093669. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23888 MW; 94E7CE1332F9EDF6 CRC64; MFDANCLKLM FVAGSQDFYH IKGGKNDRIN ALLDALELAL QSKITAFQFR QKGDLALQDP IEIKQLALEC QKLCQKYGAP FIVNDEVQLA LELKADGVHV GQEDMAIEEV MALCKKRLFI GLSVNTLEQA LKVRHLDGVA YFGVGPIFPT QSKKDKQVVG VELLKKIKDS GIKKPLIAIG GITAHNASKL REYGGIAVIS AITQAKDKAL AVGKLLKNA // ID THIE_HELPY Reviewed; 219 AA. AC O25514; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 14-MAY-2014, entry version 94. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=HP_0843; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter OS pylori). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., RA Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., RA Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., RA Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., RA Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., RA Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., RA Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., RA Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000511; AAD07889.1; -; Genomic_DNA. DR PIR; C64625; C64625. DR RefSeq; NP_207636.1; NC_000915.1. DR RefSeq; YP_006934757.1; NC_018939.1. DR ProteinModelPortal; O25514; -. DR STRING; 85962.HP0843; -. DR PRIDE; O25514; -. DR EnsemblBacteria; AAD07889; AAD07889; HP_0843. DR GeneID; 13870027; -. DR GeneID; 899372; -. DR KEGG; heo:C694_04320; -. DR KEGG; hpy:HP0843; -. DR PATRIC; 20592979; VBIHelPyl33062_0877. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HPY:HP0843-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_0000157017. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23897 MW; 033E0191999238BD CRC64; MFDADCLKLM FVAGSQDFYH IKGGKNDRIN ALLDTLELAL QSKITAFQFR QKGDLALQDP TQIKQLAMKC QKLCQKYGAP FIVNDEVQLA LELKADGVHV GQEDMAIEEV ITLCKKRQFI GLSVNTLEQA LKARHLDAVA YLGVGPIFPT PSKKDKQVVG VELLKKIKDS GIKKPLIAIG GITMHNAPKL REYGGIAVIS AIAQAKDKAL AVGKLLNNA // ID THIE_HERA2 Reviewed; 206 AA. AC A9AZD9; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Haur_2443; OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785). OC Bacteria; Chloroflexi; Herpetosiphonales; Herpetosiphonaceae; OC Herpetosiphon. OX NCBI_TaxID=316274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23779 / DSM 785; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Bryant D.A., Richardson P.; RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC RT 23779."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000875; ABX05083.1; -; Genomic_DNA. DR RefSeq; YP_001545211.1; NC_009972.1. DR ProteinModelPortal; A9AZD9; -. DR STRING; 316274.Haur_2443; -. DR EnsemblBacteria; ABX05083; ABX05083; Haur_2443. DR GeneID; 5734324; -. DR KEGG; hau:Haur_2443; -. DR PATRIC; 22121959; VBIHerAur93466_2508. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HAUR316274:GHYA-2471-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 206 Thiamine-phosphate synthase. FT /FTId=PRO_1000198079. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21240 MW; A9951F75578BC86E CRC64; MMQIDWRLYA VLDTATLGSR DPLAMTAALL AGGIGVLQLR AKNLSVRQTA QLAQAILPLT KIAQIPLIIN DDLGLALAVG ADGVHLGVDD LPLDLARASF KGLIGYSPEG VADAQRAEKL GVDYLGVGPF AATTTKLDAG APLGQAGLRA IVEAVDCPVV AIGGIAQHNV AEVRACGVAG IVVVSALLNA TNPTQACREF LAHYKE // ID THIE_HYDS0 Reviewed; 214 AA. AC B4U6B2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=HY04AAS1_1566; OS Hydrogenobaculum sp. (strain Y04AAS1). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum. OX NCBI_TaxID=380749; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y04AAS1; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the RT Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001130; ACG58248.1; -; Genomic_DNA. DR RefSeq; YP_002122226.1; NC_011126.1. DR ProteinModelPortal; B4U6B2; -. DR STRING; 380749.HY04AAS1_1566; -. DR EnsemblBacteria; ACG58248; ACG58248; HY04AAS1_1566. DR GeneID; 6744397; -. DR KEGG; hya:HY04AAS1_1566; -. DR PATRIC; 22137854; VBIHydSp64203_1571. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HSP380749:GH30-1619-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 214 Thiamine-phosphate synthase. FT /FTId=PRO_1000093670. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 24052 MW; 8FD050C3537DD758 CRC64; MFKDFNFSIY LVTDDAFFVD RDVVRTIEQA IEGGITAVQY RFKNKPSRKM YEELLVLRDI TKQNKVALIV NDRVDLAIAV KADGVHVGQE DLPPDVCKKI IPEDMIVGYS VNNLEQLKDA MTMPIDYIGF GSVFHTKTKK DYKYVGLEAL CKATNITSIP IIAIGGITHY NLKDVLKCKV KGVAVVSAIL GFEDVKRAAS DFKQMYKESL SMQI // ID THIE_HYPNA Reviewed; 221 AA. AC Q0BXD3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 54. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=HNE_3185; OS Hyphomonas neptunium (strain ATCC 15444). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hyphomonas. OX NCBI_TaxID=228405; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15444; RX PubMed=16980487; DOI=10.1128/JB.00111-06; RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., RA Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., RA Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A., RA Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C., RA Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D., RA Davidsen T.M., Yang Q., Zafar N., Ward N.L.; RT "Comparative genomic evidence for a close relationship between the RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter RT crescentus."; RL J. Bacteriol. 188:6841-6850(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000158; ABI75590.1; -; Genomic_DNA. DR RefSeq; YP_761860.1; NC_008358.1. DR ProteinModelPortal; Q0BXD3; -. DR STRING; 228405.HNE_3185; -. DR EnsemblBacteria; ABI75590; ABI75590; HNE_3185. DR GeneID; 4289215; -. DR KEGG; hne:HNE_3185; -. DR PATRIC; 32219247; VBIHypNep17450_3190. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; HNEP228405:GI69-3186-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 221 Thiamine-phosphate synthase. FT /FTId=PRO_0000336399. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23083 MW; B3E75DD9AF15B278 CRC64; MTDTAQPRPR TRLYLITPPQ IGDVSAFRKS LEETLSAGDV ASLQLRLKGQ DGMIDMQATQ EVGAAVTAMA QEAGVAVLIN DAAELSRQLG ADGVHLGWDD MPVKTARALL GPDAIIGATA KNSYHRAMQA GEDGADYVAF GAFYPTTTKE GTIPAELELL EVWQSAMILP CVAIGGITVS NAAPLVTAGA DFLAVSSGVW NHEDGPAAAV RAFNALFESL A // ID THIE_JANMA Reviewed; 207 AA. AC A6SUR1; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=mma_0318; OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Janthinobacterium. OX NCBI_TaxID=375286; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Marseille; RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138; RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., RA Raoult D., Drancourt M.; RT "Genome analysis of Minibacterium massiliensis highlights the RT convergent evolution of water-living bacteria."; RL PLoS Genet. 3:1454-1463(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000269; ABR89197.1; -; Genomic_DNA. DR RefSeq; YP_001352008.1; NC_009659.1. DR ProteinModelPortal; A6SUR1; -. DR STRING; 375286.mma_0318; -. DR EnsemblBacteria; ABR89197; ABR89197; mma_0318. DR GeneID; 5350680; -. DR KEGG; mms:mma_0318; -. DR PATRIC; 22153059; VBIJanSp106498_0328. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; JSP375286:GJ8U-325-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000093671. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21882 MW; 1E75373E3E4E36D8 CRC64; MKSNLHGLYL VTPDWDDTRK LLEITELALK GGVSLLQYRH KTADAALRQE QAECLQALCR SYEVPFIIND HIDLCLGINA DGIHVGGTDK SVAEVRAIIG PDKILGSSCY GDLALAHAAE AAGASYVAFG GFYPSKVKKY PVTTAPTIVS DWKAQGKVPS CVIGGMTRDN SAPLVANGAD MVAAISSVYL AGDPQAAARA FVSLFAK // ID THIE_KINRD Reviewed; 213 AA. AC A6W6A2; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Krad_0853; OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / OS SRS30216). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Kineosporiineae; Kineosporiaceae; Kineococcus. OX NCBI_TaxID=266940; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., RA Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Lykidis A., Bagwell C.E., RA Shimkets L., Berry C.J., Fliermans C., Richardson P.; RT "Complete sequence of chromosome of Kineococcus radiotolerans RT SRS30216."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000750; ABS02341.1; -; Genomic_DNA. DR RefSeq; YP_001360605.1; NC_009664.2. DR ProteinModelPortal; A6W6A2; -. DR STRING; 266940.Krad_0853; -. DR EnsemblBacteria; ABS02341; ABS02341; Krad_0853. DR GeneID; 5337172; -. DR KEGG; kra:Krad_0853; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; KRAD266940:GI4N-1381-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000336400. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 21276 MW; 8AE9542A23B63B2B CRC64; MSPRPAFDPT LYLVTDTGLC GPRGVPAVVR AAVAGGVSAV QVRAKDGGDR ERLALVRAVQ DVLRGTGVAL IVDDAVDIAL IAGADGVHLG QSDLPAAEVR RLAPDLLLGL SVSTPAQAAA VDPAVVDYLG VGPVRATATK PDAAAPLGPE GLRAVVAAAP VPCVAIGGIH PDNLDALRGS GIAGFCVVSE VCAAADPEAA ARALRTQWHG RAS // ID THIE_KLEP7 Reviewed; 211 AA. AC A6TGQ0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=KPN78578_43100; ORFNames=KPN_04375; OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH OS 78578). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=272620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700721 / MGH 78578; RG The Klebsiella pneumonia Genome Sequencing Project; RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000647; ABR79734.1; -; Genomic_DNA. DR RefSeq; YP_001338001.1; NC_009648.1. DR ProteinModelPortal; A6TGQ0; -. DR STRING; 272620.KPN_04375; -. DR EnsemblBacteria; ABR79734; ABR79734; KPN_04375. DR GeneID; 5340622; -. DR KEGG; kpn:KPN_04375; -. DR PATRIC; 20463210; VBIKlePne13394_4423. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; KPNE272620:GKDC-4412-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000008144. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23015 MW; 21B54D01518D3CB0 CRC64; MYQPDFPPVP FRLGLYPVVD SVAWIERLLE AGVRTLQLRI KDRRDSEVED DVIAAIALGR RYHARLFIND YWQLAIKHQA YGVHLGQEDL ETTDLSAIRQ AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIQRLADYP TVAIGGISLE KAPGVLATGV GSIAVVSAIT QAADWRAATD QLLALAGAGD E // ID THIE_KORVE Reviewed; 211 AA. AC Q1ILG3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Acid345_3286; OS Koribacter versatilis (strain Ellin345). OC Bacteria; Acidobacteria; Candidatus Koribacter. OX NCBI_TaxID=204669; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin345; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., RA Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., RA Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., RA Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C., RA Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., RA Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., RA Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., RA Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., RA Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000360; ABF42287.1; -; Genomic_DNA. DR RefSeq; YP_592361.1; NC_008009.1. DR ProteinModelPortal; Q1ILG3; -. DR STRING; 204669.Acid345_3286; -. DR EnsemblBacteria; ABF42287; ABF42287; Acid345_3286. DR GeneID; 4072698; -. DR KEGG; aba:Acid345_3286; -. DR PATRIC; 31983742; VBICanKor57425_3503. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; KVER204669:GHL8-3312-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000336367. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22598 MW; 313BA59617357CEF CRC64; MASGLKLPRL YAIVDADCFG PEPSLATLTH FAKELVAGGV TLLQYRNKQG SAREILSHAR ELKRALPPEV TLLLNDRADL AIAAGFHGVH VGQDDLSPEG ARLVVGPEMF VGTSTHNPEQ LQIADKATVD YLAIGPIFAT KSKINPDPVV GLDRLRAVRK LTSKPLVAIG GITRENCRSV IDAGADSVAV IADLLVDPRQ RASEFLQILH S // ID THIE_LACBA Reviewed; 217 AA. AC Q03NS1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LVIS_2097; OS Lactobacillus brevis (strain ATCC 367 / JCM 1170). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=387344; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 367 / JCM 1170; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., RA Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., RA Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., RA Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J., RA Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., RA Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., RA Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., RA Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., RA Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., RA Weimer B.C., Mills D.A.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000416; ABJ65151.1; -; Genomic_DNA. DR RefSeq; YP_796182.1; NC_008497.1. DR ProteinModelPortal; Q03NS1; -. DR STRING; 387344.LVIS_2097; -. DR EnsemblBacteria; ABJ65151; ABJ65151; LVIS_2097. DR GeneID; 4413106; -. DR KEGG; lbr:LVIS_2097; -. DR PATRIC; 22203128; VBILacBre134470_2003. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LBRE387344:GJ8S-2097-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_1000008145. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 144 146 THZ-P binding (By similarity). FT REGION 195 196 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 147 147 HMP-PP (By similarity). FT BINDING 175 175 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22513 MW; 9431633BF03EBD84 CRC64; MSVTFEPGLL RAYFVAGSQD VPGQDLRDVL AKMLAAGITA FQFRDKATST LTPEQRLALG RDLRAQCRVA NVPFIVDDDV ELALALDADG IHVGQSDQRV QQVIQAVAGR NIFVGLSCST MAEVTAANAI AGIDYIGSGP IFPTISKADA DPVVGTAGLQ KLVAQSRVPV VAIGGVTVDS LPAIAETGAA GVAVITLLTH SHDVDADTAA MRQAFSK // ID THIE_LACC3 Reviewed; 213 AA. AC Q03CB2; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 55. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LSEI_0300; OS Lactobacillus casei (strain ATCC 334). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=321967; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 334; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., RA Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., RA Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., RA Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J., RA Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., RA Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., RA Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., RA Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., RA Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., RA Weimer B.C., Mills D.A.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000423; ABJ69160.1; -; Genomic_DNA. DR RefSeq; YP_805602.1; NC_008526.1. DR ProteinModelPortal; Q03CB2; -. DR STRING; 321967.LSEI_0300; -. DR EnsemblBacteria; ABJ69160; ABJ69160; LSEI_0300. DR GeneID; 4419767; -. DR KEGG; lca:LSEI_0300; -. DR PATRIC; 22204326; VBILacCas62221_0324. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LCAS321967:GH4S-300-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000336401. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22637 MW; 15A5895958E715C1 CRC64; MNATDLKLYL VTHRYDDNEA TFLAKIAAAC ENSVTMVQLR EKMLSTRAYF ELAQRVKLIT DRYQIPLIID DRVDICLAVD AAGVHIGDDE LPVAMTRQLI GPDKVLGVST KTVETAVAAV AAGADYLGVG AIFPTQTKAN AAVTPIATLK AITAQVAVPV VAIGGVKEAN LATFKDTGIA GVAIVSEIMQ APDIAHKVQA LRTKLKAVLP NDR // ID THIE_LACCB Reviewed; 213 AA. AC B3W783; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LCABL_03160; OS Lactobacillus casei (strain BL23). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=543734; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BL23; RA Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., RA Hartke A., Deutscher J.; RT "Lactobacillus casei BL23 complete genome sequence."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM177140; CAQ65442.1; -; Genomic_DNA. DR RefSeq; YP_001986300.1; NC_010999.1. DR ProteinModelPortal; B3W783; -. DR STRING; 543734.LCABL_03160; -. DR EnsemblBacteria; CAQ65442; CAQ65442; LCABL_03160. DR GeneID; 6406912; -. DR KEGG; lcb:LCABL_03160; -. DR PATRIC; 22210141; VBILacCas89204_0302. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LCAS543734:GCHL-308-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_1000093672. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22633 MW; 09637BD33C906AD5 CRC64; MNATDLKLYL VTHRYDDNEA TFLAKIAAAC ENGVTMVQLR EKMLSTRAYF ELAQRVKLIT DRYQIPLIID DRVDICLAVD AAGVHIGDDE LPVAMTRQLI GPDKVLGVST KTVETAVAAV AAGADYLGVG AIFPTQTKAN APVTPIATLK AITAQVAVPV VAIGGVKEAN LGTFKETGIA GVAIVSEIMQ APDIAHKVQA LRTKLKAVLP NDR // ID THIE_LACF3 Reviewed; 213 AA. AC B2GBV5; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LAF_0801; OS Lactobacillus fermentum (strain NBRC 3956 / LMG 18251). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=334390; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 3956 / LMG 18251; RX PubMed=18487258; DOI=10.1093/dnares/dsn009; RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., RA Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., RA Kikuchi J., Masaoka T., Hattori M.; RT "Comparative genome analysis of Lactobacillus reuteri and RT Lactobacillus fermentum reveal a genomic island for reuterin and RT cobalamin production."; RL DNA Res. 15:151-161(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008937; BAG27137.1; -; Genomic_DNA. DR RefSeq; YP_001843617.1; NC_010610.1. DR ProteinModelPortal; B2GBV5; -. DR STRING; 334390.LAF_0801; -. DR EnsemblBacteria; BAG27137; BAG27137; LAF_0801. DR GeneID; 6233309; -. DR KEGG; lfe:LAF_0801; -. DR PATRIC; 22225794; VBILacFer15497_0883. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LFER334390:GJ2S-846-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_1000093673. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22416 MW; C5F1FDE4EE087316 CRC64; MLFKNEILRC YLIGGSQDTH HDPDEFLTKV EAAMQAGITA FQYREKGTST LSKAETLALG QQVRELATKY GVPLFVDDDL ELAAAIKADG IHVGQKDQRI EEVLAAVSDQ LMVGYSCNTA AQVAHANQLN VDYIGTGPVF PTISKDDAGS ALGVDGLADF VEQSAHPVVA IGGISLDNVG ATLTSGCAGL SMISMVLGAD DVAGTVKKIL ELY // ID THIE_LACLA Reviewed; 215 AA. AC Q9CG48; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 1. DT 14-MAY-2014, entry version 93. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LL1262; ORFNames=L0201; OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus OS lactis). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=272623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IL1403; RX PubMed=11337471; DOI=10.1101/gr.GR-1697R; RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., RA Weissenbach J., Ehrlich S.D., Sorokin A.; RT "The complete genome sequence of the lactic acid bacterium Lactococcus RT lactis ssp. lactis IL1403."; RL Genome Res. 11:731-753(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE005176; AAK05360.1; -; Genomic_DNA. DR PIR; F86782; F86782. DR RefSeq; NP_267418.1; NC_002662.1. DR ProteinModelPortal; Q9CG48; -. DR STRING; 272623.L0201; -. DR EnsemblBacteria; AAK05360; AAK05360; L0201. DR GeneID; 1114911; -. DR KEGG; lla:L0201; -. DR PATRIC; 22294912; VBILacLac136773_1364. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LLAC272623:GHSH-1350-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 215 Thiamine-phosphate synthase. FT /FTId=PRO_0000157019. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23657 MW; 824D01C7F484806A CRC64; MKNKILDLRA YFIAGPQDFP KLSIDDAIDK ISVIIKSGVT VYQFRDKGTI YKNKNQRLEV AKRLQEVAQK AAVSFIVNDD VELARELSAD GIHVGQDDDS VSKIRELIGQ EMWVGLSVSN DMELESAQKS GADYLGIGPI YPTNSKSDAA EPIGVDHLRK MLEHNQLPTV GIGGITENSL TELSKIGLGG VAVISLLTES ENYKNMVQKI KQNIR // ID THIE_LACLM Reviewed; 218 AA. AC A2RKJ7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=llmg_1218; OS Lactococcus lactis subsp. cremoris (strain MG1363). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=416870; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MG1363; RX PubMed=17307855; DOI=10.1128/JB.01768-06; RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., RA van Sinderen D., Kok J.; RT "The complete genome sequence of the lactic acid bacterial paradigm RT Lactococcus lactis subsp. cremoris MG1363."; RL J. Bacteriol. 189:3256-3270(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM406671; CAL97809.1; -; Genomic_DNA. DR RefSeq; YP_001032527.1; NC_009004.1. DR ProteinModelPortal; A2RKJ7; -. DR STRING; 416870.llmg_1218; -. DR EnsemblBacteria; CAL97809; CAL97809; llmg_1218. DR GeneID; 4797017; -. DR KEGG; llm:llmg_1218; -. DR PATRIC; 22283591; VBILacLac4574_1252. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LLAC416870:GCDT-1241-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 218 Thiamine-phosphate synthase. FT /FTId=PRO_1000008146. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23698 MW; F5BA2C42AECE10EB CRC64; MTKKTLDLSV YFIAGSQNFS ECSLDEATQK IALIIKSGVT VYQFRDKGTI YKEQKQRLSI AQKLQKVSEE AGVSFIVNDD VELARELNAD GIHIGQTDES VSKVREKVGQ EMWLGLSVTN ADELKTAQSS GADYLGIGPI YPTNSKNDAA KPIGIKDLRL MLLENQLPIV GIGGITQDSL TELSAIGLDG LAVISLLTEA ENPKKVAQMI RQKITKNG // ID THIE_LACLS Reviewed; 218 AA. AC Q02YS6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LACR_1375; OS Lactococcus lactis subsp. cremoris (strain SK11). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=272622; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK11; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., RA Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., RA Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., RA Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J., RA Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., RA Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., RA Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., RA Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., RA Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., RA Weimer B.C., Mills D.A.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000425; ABJ72896.1; -; Genomic_DNA. DR RefSeq; YP_809318.1; NC_008527.1. DR ProteinModelPortal; Q02YS6; -. DR STRING; 272622.LACR_1375; -. DR EnsemblBacteria; ABJ72896; ABJ72896; LACR_1375. DR GeneID; 4432564; -. DR KEGG; llc:LACR_1375; -. DR PATRIC; 22289597; VBILacLac38071_1545. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LLAC272622:GJUG-1375-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 218 Thiamine-phosphate synthase. FT /FTId=PRO_1000008147. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23610 MW; 7FEB36A732E0C9E1 CRC64; MTNKTLDLSV YFIAGAQNFS ECSLDGATQK IALIIKSGVT VYQFRDKGTI YKEQKQRLSI AQKLQKVSEE AGVSFIVNDD VELARELNAD GIHIGQTDES VSKVREKVGQ EMWLGLSVTK ADELKTAQSS GADYLGIGPI YPTNSKNDAA KPIGIKDLRL MLLENQLPIV GIGGITQDSL TELSAIGLDG LAVISLLTEA ENPKKVAQMI RQKITKNG // ID THIE_LACPL Reviewed; 217 AA. AC Q890C0; F9UST8; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 73. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=lp_0115; OS Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=220668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., RA Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., RA Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., RA Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., RA De Vos W.M., Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL935263; CCC77669.1; -; Genomic_DNA. DR RefSeq; YP_004888183.1; NC_004567.2. DR ProteinModelPortal; Q890C0; -. DR STRING; 220668.lp_0115; -. DR EnsemblBacteria; CCC77669; CCC77669; lp_0115. DR GeneID; 1061356; -. DR KEGG; lpl:lp_0115; -. DR PATRIC; 22246813; VBILacPla27411_0093. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_0000157020. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22845 MW; 83E413079D570282 CRC64; MTLKFEPTQL RAYFVCGTQD VPGQDLNMVV QTALDAGVTA FQYRDKGNSQ LTTVERFALG QQLRERCAQA HVPFIVDDDV ELALALQADG IHVGQKDDWV TQVIQRVANQ MFVGLSCSTL AEVQIANQLE GIAYLGSGPI FPTTSKADAD PVVGLTGLRQ LVMTASCPVV AIGGITVAQL PAIAATGAAG AAVISMLTRS PDMAATVKAM LTATEGH // ID THIE_LACRD Reviewed; 215 AA. AC A5VKA1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Lreu_1015; OS Lactobacillus reuteri (strain DSM 20016). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=557436; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20016; RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314; RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M., RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M., RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., RA Ivanova N., Kyrpides N.C., Walter J.; RT "The evolution of host specialization in the vertebrate gut symbiont RT Lactobacillus reuteri."; RL PLoS Genet. 7:E1001314-E1001314(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000705; ABQ83275.1; -; Genomic_DNA. DR RefSeq; YP_001271612.1; NC_009513.1. DR ProteinModelPortal; A5VKA1; -. DR STRING; 557436.Lreu_1015; -. DR EnsemblBacteria; ABQ83275; ABQ83275; Lreu_1015. DR GeneID; 5188285; -. DR KEGG; lre:Lreu_1015; -. DR PATRIC; 22255214; VBILacReu87937_1023. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LREU557436:GC7Y-1072-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 215 Thiamine-phosphate synthase. FT /FTId=PRO_1000057644. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23849 MW; BE51CB250D92566D CRC64; MIFDPKMLQV YLVGGTQDVH NDVVKFLEKV ELAMKSGITA FQYREKGNSK LRPNERVDLG LELRTLCTHY GIPLIVDDDY ELAQQINADG VHVGQNDTKI EQVSVAVGHQ MFIGYSCNTP EQVERANTMD FIDYIGCGPV FPTKSKSDAD TAIGINRLER LNMISERPVV AIGGIDEENM KVVHDTGVAG LAVISLVFDS KDLVATVKKM KNLYK // ID THIE_LACRJ Reviewed; 215 AA. AC B2G7Q4; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LAR_0970; OS Lactobacillus reuteri (strain JCM 1112). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=557433; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 1112; RX PubMed=18487258; DOI=10.1093/dnares/dsn009; RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., RA Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., RA Kikuchi J., Masaoka T., Hattori M.; RT "Comparative genome analysis of Lactobacillus reuteri and RT Lactobacillus fermentum reveal a genomic island for reuterin and RT cobalamin production."; RL DNA Res. 15:151-161(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP007281; BAG25486.1; -; Genomic_DNA. DR RefSeq; YP_001841966.1; NC_010609.1. DR ProteinModelPortal; B2G7Q4; -. DR STRING; 557433.LAR_0970; -. DR EnsemblBacteria; BAG25486; BAG25486; LAR_0970. DR GeneID; 6230631; -. DR KEGG; lrf:LAR_0970; -. DR PATRIC; 22259400; VBILacReu111271_1060. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GAKWIQY; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LREU557433:GHNR-1027-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 215 Thiamine-phosphate synthase. FT /FTId=PRO_1000093674. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23849 MW; BE51CB250D92566D CRC64; MIFDPKMLQV YLVGGTQDVH NDVVKFLEKV ELAMKSGITA FQYREKGNSK LRPNERVDLG LELRTLCTHY GIPLIVDDDY ELAQQINADG VHVGQNDTKI EQVSVAVGHQ MFIGYSCNTP EQVERANTMD FIDYIGCGPV FPTKSKSDAD TAIGINRLER LNMISERPVV AIGGIDEENM KVVHDTGVAG LAVISLVFDS KDLVATVKKM KNLYK // ID THIE_LACSS Reviewed; 224 AA. AC Q38ZM1; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LCA_0057; OS Lactobacillus sakei subsp. sakei (strain 23K). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=314315; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=23K; RX PubMed=16273110; DOI=10.1038/nbt1160; RA Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M., RA Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., RA Loux V., Zagorec M.; RT "The complete genome sequence of the meat-borne lactic acid bacterium RT Lactobacillus sakei 23K."; RL Nat. Biotechnol. 23:1527-1533(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR936503; CAI54356.1; -; Genomic_DNA. DR RefSeq; YP_394668.1; NC_007576.1. DR ProteinModelPortal; Q38ZM1; -. DR STRING; 314315.LSA0057; -. DR EnsemblBacteria; CAI54356; CAI54356; LCA_0057. DR GeneID; 3778055; -. DR KEGG; lsa:LSA0057; -. DR PATRIC; 22272882; VBILacSak116432_0055. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LSAK314315:GCKE-88-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 224 Thiamine-phosphate synthase. FT /FTId=PRO_0000336402. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 24191 MW; DA3E890EEC5B9564 CRC64; MTNIAQEILQ TYLVAGTQDT GRENFLPILD QALQAGITCF QFRDKGPNSL PTDAMRSDYA KKAQALCRTY HVPFIIDDRL ELALDLQADG LHVGQSDQPW PKIEVAKQHG LITGLSCHTA QEILSSHQQP ALDYIGVGPI FPTNSKEDAK TPLGLAQLKA FTQLSQLPVV AIGGISLKNC QQVAETGVAG AAVISAITQA KNIPQAIQLL NQPWQSSEGN NHES // ID THIE_LARHH Reviewed; 211 AA. AC C1DCM3; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LHK_02661; OS Laribacter hongkongensis (strain HLHK9). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Laribacter. OX NCBI_TaxID=557598; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLHK9; RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416; RA Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., RA Tsang A.K.L., Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., RA Snyder L.A.S., Cai J.J., Huang J.-D., Mak W., Pallen M.J., Lok S., RA Yuen K.-Y.; RT "The complete genome and proteome of Laribacter hongkongensis reveal RT potential mechanisms for adaptations to different temperatures and RT habitats."; RL PLoS Genet. 5:E1000416-E1000416(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001154; ACO75642.1; -; Genomic_DNA. DR RefSeq; YP_002796651.1; NC_012559.1. DR ProteinModelPortal; C1DCM3; -. DR STRING; 557598.LHK_02661; -. DR EnsemblBacteria; ACO75642; ACO75642; LHK_02661. DR GeneID; 7758271; -. DR KEGG; lhk:LHK_02661; -. DR PATRIC; 22302111; VBILarHon49832_2426. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LHON557598:GHO5-2706-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000198080. FT REGION 40 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21258 MW; 624D7C4E41DF9BF3 CRC64; MKKMIDYSVY LVLDPELCGG LDGMLRVTEA AMAGGAGVVQ LRAPQWKKRQ WLDAARALQP LCRQGGAVFV VNDQVDVALA VGADGVHVGQ QDLPVAVVRE LMGPQALIGL SVNHAGQLAA VPSEADYLGL GPVFATSTKK DAAPVLGLAQ LAGLAAATSL PTVGIGGIAP ANAGAVFAAG VDGVAVVSAI CTAADPAAVT RELYALKGHT A // ID THIE_LAWIP Reviewed; 217 AA. AC Q1MRJ6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 1. DT 14-MAY-2014, entry version 55. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LI0324; OS Lawsonia intracellularis (strain PHE/MN1-00). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Lawsonia. OX NCBI_TaxID=363253; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PHE/MN1-00; RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L., RA Peterson A., May B., Singh S., Gebhart C., Kapur V.; RT "The complete genome sequence of Lawsonia intracellularis: the RT causative agent of proliferative enteropathy."; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM180252; CAJ54380.1; -; Genomic_DNA. DR RefSeq; YP_594701.1; NC_008011.1. DR ProteinModelPortal; Q1MRJ6; -. DR STRING; 363253.LI0324; -. DR GeneID; 4059818; -. DR KEGG; lip:LI0324; -. DR PATRIC; 22304031; VBILawInt40445_0360. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LINT363253:GH6E-334-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_0000336403. FT REGION 44 48 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 115 115 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23780 MW; 02D37AFDB58BCA7B CRC64; MAYILPGSSL DADLYAITDD ALSFNRSVIE VVKQLLDAGI RIIQYREKNK SSNSMLKDCI TIKKLTEEAN ACFIVNDHVD IAVLCNADGV HLGQDDLPVD KVRELIGKEK IIGLSTHSPQ QAQKAIEMGA DYIGVGPLYP TKTKKDVCEP VTISYLDWVV SHIAIPFVAI GGIKQHNIQE VIQHGAKCCA LVSEILSAPN IPLRIQELRQ AILLAHT // ID THIE_LEPBA Reviewed; 210 AA. AC B0SE83; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LBF_2631; OS Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=355278; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Patoc 1 / Ames; RX PubMed=18270594; DOI=10.1371/journal.pone.0001607; RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., RA McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., RA Coppel R.L., Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.; RT "Genome sequence of the saprophyte Leptospira biflexa provides RT insights into the evolution of Leptospira and the pathogenesis of RT leptospirosis."; RL PLoS ONE 3:E1607-E1607(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000777; ABZ95114.1; -; Genomic_DNA. DR RefSeq; YP_001963692.1; NC_010842.1. DR ProteinModelPortal; B0SE83; -. DR STRING; 355278.LBF_2631; -. DR EnsemblBacteria; ABZ95114; ABZ95114; LBF_2631. DR GeneID; 6387379; -. DR KEGG; lbf:LBF_2631; -. DR PATRIC; 22344415; VBILepBif95142_2752. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HGSTREM; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LBIF355278:GHTJ-2626-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_1000093675. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22794 MW; CCDFFAA255B35D6F CRC64; MQNKIQGVYL VTDRPLCLHH KLEEVVQMAA SGGVSLVQLR EKDSTSREFL ELAIHLKFIL SPFQVPLLIN DRVDLCLASG ADGVHLGQTD LPWLEARRIL GKDAIIGLSI ETKEDFATLT KEDPNPQLEY LAVSPVFDTP TKTNTKEALG LAGVRWLKEK TDIPVVAIGG INISNAKDVI GAGADMIAVV SAICSAKNPK EATVALRNQF // ID THIE_LEPBP Reviewed; 210 AA. AC B0SMR9; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LEPBI_I2715; OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / OS Paris). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=456481; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Patoc 1 / ATCC 23582 / Paris; RX PubMed=18270594; DOI=10.1371/journal.pone.0001607; RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., RA McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., RA Coppel R.L., Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.; RT "Genome sequence of the saprophyte Leptospira biflexa provides RT insights into the evolution of Leptospira and the pathogenesis of RT leptospirosis."; RL PLoS ONE 3:E1607-E1607(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000786; ABZ98793.1; -; Genomic_DNA. DR RefSeq; YP_001840069.1; NC_010602.1. DR ProteinModelPortal; B0SMR9; -. DR STRING; 456481.LEPBI_I2715; -. DR EnsemblBacteria; ABZ98793; ABZ98793; LEPBI_I2715. DR GeneID; 6223191; -. DR KEGG; lbi:LEPBI_I2715; -. DR PATRIC; 22352241; VBILepBif123590_2740. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LBIF456481:GCM0-2687-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_1000093676. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 22794 MW; CCDFFAA255B35D6F CRC64; MQNKIQGVYL VTDRPLCLHH KLEEVVQMAA SGGVSLVQLR EKDSTSREFL ELAIHLKFIL SPFQVPLLIN DRVDLCLASG ADGVHLGQTD LPWLEARRIL GKDAIIGLSI ETKEDFATLT KEDPNPQLEY LAVSPVFDTP TKTNTKEALG LAGVRWLKEK TDIPVVAIGG INISNAKDVI GAGADMIAVV SAICSAKNPK EATVALRNQF // ID THIE_LEUCK Reviewed; 212 AA. AC B1MX63; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LCK_00282; OS Leuconostoc citreum (strain KM20). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostoc. OX NCBI_TaxID=349519; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KM20; RX PubMed=18281406; DOI=10.1128/JB.01862-07; RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., RA Kim J.-S., Lee S., Park H.-S., Park Y.-H., Oh T.K.; RT "Complete genome sequence of Leuconostoc citreum KM20."; RL J. Bacteriol. 190:3093-3094(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ489736; ACA82115.1; -; Genomic_DNA. DR RefSeq; YP_001727559.1; NC_010471.1. DR ProteinModelPortal; B1MX63; -. DR STRING; 349519.LCK_00282; -. DR EnsemblBacteria; ACA82115; ACA82115; LCK_00282. DR GeneID; 6063848; -. DR KEGG; lci:LCK_00282; -. DR PATRIC; 32613823; VBILeuCit37309_0401. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MLARYFI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LCIT349519:GHNF-298-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_1000093677. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT REGION 192 193 THZ-P binding (By similarity). FT METAL 77 77 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT BINDING 76 76 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22953 MW; 7A894A6C27EF6B46 CRC64; MIFDKTMLAR YFIMGTQDVA DEAEFLRILN QALRSGITLF QYREKGQGAL VGQKKLQLAK QVRALTAQYH VPLVIDDDMA LAHAIAADGI HFGQDDGRPV DNIKQSGNLF VGVSVSNQQE YQRIAHVAGI DHIGVGPIFA TTSKSDAKPP IGISGLSQLI RIAHHPIVAI GGIQRDNLSK VLSTGVDGAA VISMISQSGD IQKTLADWRN RT // ID THIE_LISIN Reviewed; 214 AA. AC Q92EW5; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 14-MAY-2014, entry version 79. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=lin0343; OS Listeria innocua serovar 6a (strain CLIP 11262). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=272626; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIP 11262; RX PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., RA Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., RA Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., RA Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., RA Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., RA Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., RA Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., RA Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL596164; CAC95576.1; -; Genomic_DNA. DR PIR; AH1475; AH1475. DR RefSeq; NP_469688.1; NC_003212.1. DR ProteinModelPortal; Q92EW5; -. DR STRING; 272626.lin0343; -. DR EnsemblBacteria; CAC95576; CAC95576; CAC95576. DR GeneID; 1128771; -. DR KEGG; lin:lin0343; -. DR PATRIC; 20297368; VBILisInn102668_0358. DR GenoList; LIN0343; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 214 Thiamine-phosphate synthase. FT /FTId=PRO_0000157021. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22528 MW; 5AE82E4B5B373EDD CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK AGITCFQYRE KGAGALQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAE EAERLGSVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSEDC QSVIKQLKNP GSPS // ID THIE_LISMC Reviewed; 214 AA. AC C1KZ34; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Lm4b_00337; OS Listeria monocytogenes serotype 4b (strain CLIP80459). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=568819; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIP80459; RX PubMed=22530965; DOI=10.1186/1471-2164-13-144; RA Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B., RA Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., RA Goesmann A., Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., RA Garrido P., Rusniok C., Buchrieser C., Goebel W., Chakraborty T.; RT "Comparative genomics and transcriptomics of lineages I, II, and III RT strains of Listeria monocytogenes."; RL BMC Genomics 13:144-144(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM242711; CAS04104.1; -; Genomic_DNA. DR RefSeq; YP_002757052.1; NC_012488.1. DR ProteinModelPortal; C1KZ34; -. DR STRING; 634178.Lm4b_00337; -. DR EnsemblBacteria; CAS04104; CAS04104; Lm4b_00337. DR GeneID; 7703731; -. DR KEGG; lmc:Lm4b_00337; -. DR PATRIC; 20303778; VBILisMon88360_0325. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LMON568819:GJF9-489-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 214 Thiamine-phosphate synthase. FT /FTId=PRO_1000202750. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22595 MW; 10E4ADFD02F4711D CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAE EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GYPS // ID THIE_LISMF Reviewed; 214 AA. AC Q723Y9; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 69. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LMOf2365_0336; OS Listeria monocytogenes serotype 4b (strain F2365). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=265669; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F2365; RX PubMed=15115801; DOI=10.1093/nar/gkh562; RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., RA Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., RA Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., RA Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., RA Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., RA Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., RA Bayles D.O., Luchansky J.B., Fraser C.M.; RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food- RT borne pathogen Listeria monocytogenes reveal new insights into the RT core genome components of this species."; RL Nucleic Acids Res. 32:2386-2395(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017262; AAT03122.1; -; Genomic_DNA. DR RefSeq; YP_012945.1; NC_002973.6. DR ProteinModelPortal; Q723Y9; -. DR STRING; 265669.LMOf2365_0336; -. DR EnsemblBacteria; AAT03122; AAT03122; LMOf2365_0336. DR GeneID; 2799134; -. DR KEGG; lmf:LMOf2365_0336; -. DR PATRIC; 20321879; VBILisMon105049_0338. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 214 Thiamine-phosphate synthase. FT /FTId=PRO_0000157022. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22615 MW; 35C5E8FFC475399F CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGAGSLQTAS ERKEMALECQ QLCTKYQVPF IINDDVALAL EIGADGIHVG QNDEEIRQVI ASCAGKMKIG LSVHSVSEAE EAERLGAVDY IGVGPIFPTI SKADAESVSG TAILEEIRRA GIKLPIVGIG GINETNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GYPS // ID THIE_LISMH Reviewed; 214 AA. AC B8DET0; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=LMHCC_2315; OS Listeria monocytogenes serotype 4a (strain HCC23). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=552536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HCC23; RX PubMed=21602330; DOI=10.1128/JB.05236-11; RA Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., RA Bridges S.M., Lawrence M.L.; RT "Genome sequence of lineage III Listeria monocytogenes strain HCC23."; RL J. Bacteriol. 193:3679-3680(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001175; ACK40652.1; -; Genomic_DNA. DR RefSeq; YP_002351266.1; NC_011660.1. DR ProteinModelPortal; B8DET0; -. DR STRING; 552536.LMHCC_2315; -. DR EnsemblBacteria; ACK40652; ACK40652; LMHCC_2315. DR GeneID; 7078769; -. DR KEGG; lmh:LMHCC_2315; -. DR PATRIC; 20319754; VBILisMon86872_2300. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LMON552536:GIW4-2347-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 214 Thiamine-phosphate synthase. FT /FTId=PRO_1000198081. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22444 MW; 1CA16767F5492E91 CRC64; MRAELAVYFI AGTQDIVRGT LPGVLEEALK AGITCFQYRE KGVGSLQTAS ERKEMALECQ QLCAKYQVPF IINDDVALAL EIGADGIHVG QNDEGIRQVI ASCAGKMKIG LSVHSVSEAA EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GIKLPIVGIG GINEKNSAEV LTAGADGVSV ISAITRSDDC YSVIKQLKNP GSPS // ID THIE_LISMO Reviewed; 214 AA. AC Q8YA44; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 14-MAY-2014, entry version 78. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=lmo0318; OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=169963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-679 / EGD-e; RX PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., RA Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., RA Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., RA Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., RA Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., RA Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., RA Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., RA Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL591974; CAD00845.1; -; Genomic_DNA. DR PIR; AG1114; AG1114. DR RefSeq; NP_463848.1; NC_003210.1. DR ProteinModelPortal; Q8YA44; -. DR STRING; 169963.lmo0318; -. DR EnsemblBacteria; CAD00845; CAD00845; CAD00845. DR GeneID; 987536; -. DR KEGG; lmo:lmo0318; -. DR PATRIC; 20309683; VBILisMon69206_0327. DR GenoList; LMO0318; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LMON169963:LMO0318-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 214 Thiamine-phosphate synthase. FT /FTId=PRO_0000157023. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22398 MW; CD29EC73FEF09751 CRC64; MRAELAVYFI AGTQDIVRGT LPSVLEEALK GGITCFQYRE KGAGSLQTAS ERKEMALECQ KLCAKYQVPF IINDDVALAL EIGADGIHVG QTDEAIRQVI ASCSGKMKIG LSVHSVSEAK EAERLGAVDY IGVGPIFPTI SKADAEPVSG TAILEEIRRA GITIPIVGIG GINETNSAEV LTAGADGVSV ISAITQSDDC HSVIKQLKNP GSPS // ID THIE_LISW6 Reviewed; 208 AA. AC A0AFC5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=lwe0289; OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / OS SLCC5334). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=386043; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35897 / DSM 20650 / SLCC5334; RX PubMed=16936040; DOI=10.1128/JB.00758-06; RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., RA Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., RA Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., RA Liang C., Dandekar T., Lampidis R., Kreft J., Goebel W., RA Chakraborty T.; RT "Whole-genome sequence of Listeria welshimeri reveals common steps in RT genome reduction with Listeria innocua as compared to Listeria RT monocytogenes."; RL J. Bacteriol. 188:7405-7415(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM263198; CAK19707.1; -; Genomic_DNA. DR RefSeq; YP_848490.1; NC_008555.1. DR ProteinModelPortal; A0AFC5; -. DR STRING; 386043.lwe0289; -. DR EnsemblBacteria; CAK19707; CAK19707; lwe0289. DR GeneID; 4465686; -. DR KEGG; lwe:lwe0289; -. DR PATRIC; 20327703; VBILisWel39304_0292. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LWEL386043:GI5X-305-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 208 Thiamine-phosphate synthase. FT /FTId=PRO_1000008148. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 22066 MW; 7BDFE7C85262901F CRC64; MKEELAVYFI AGTQDIVRGT LPSVLEEALK GGITCFQYRE KGAGSLQTAS ERKEMALECQ KLCAKYQVPF IINDDVVLAL EIGADGIHVG QNDEEIHQVI TSCAGKMKIG LSVHSVSEAE EAERLGAVDY IGVGPIFPTI SKADAEPESG TEILKEIRRA GIKLPIVGIG GINEANIAEV LAAGADGVSV ISAITRADDY QLVIANLI // ID THIE_LYSSC Reviewed; 213 AA. AC B1HX34; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Bsph_4149; OS Lysinibacillus sphaericus (strain C3-41). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=444177; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C3-41; RX PubMed=18296527; DOI=10.1128/JB.01652-07; RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., RA Gao M., Berry C., Yuan Z.; RT "Complete genome sequence of the mosquitocidal bacterium Bacillus RT sphaericus C3-41 and comparison with those of closely related Bacillus RT species."; RL J. Bacteriol. 190:2892-2902(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000817; ACA41610.1; -; Genomic_DNA. DR RefSeq; YP_001699740.1; NC_010382.1. DR ProteinModelPortal; B1HX34; -. DR STRING; 444177.Bsph_4149; -. DR EnsemblBacteria; ACA41610; ACA41610; Bsph_4149. DR GeneID; 6022361; -. DR KEGG; lsp:Bsph_4149; -. DR PATRIC; 22420741; VBILysSph89750_4227. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; LSPH444177:GJEL-4119-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_1000093678. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23338 MW; 1313E97C7F5869B8 CRC64; MKREDLQLYF IMGTSNVSHQ EPLVVLEKAL RAGITMFQLR EKGPYALTGL AYEQFARQCQ QLCQHYHVPF IVNDDVDLAV RLGADGVHIG QDDEQIAIAR KKMANRILGV SVHSQEELQI AIDHHADYVG IGPIFATTSK SDAQPPCGTN FLQQASKLQP NLPIVAIGGI NGINADIVFQ AGADGVAVIS ALCESEDIEQ TVSIFKSLNR IKR // ID THIE_MANSM Reviewed; 220 AA. AC Q65US7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MS0676; OS Mannheimia succiniciproducens (strain MBEL55E). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Basfia. OX NCBI_TaxID=221988; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBEL55E; RX PubMed=15378067; DOI=10.1038/nbt1010; RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., RA Kim C.H., Jeong H., Hur C.G., Kim J.J.; RT "The genome sequence of the capnophilic rumen bacterium Mannheimia RT succiniciproducens."; RL Nat. Biotechnol. 22:1275-1281(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016827; AAU37283.1; -; Genomic_DNA. DR RefSeq; YP_087868.1; NC_006300.1. DR ProteinModelPortal; Q65US7; -. DR STRING; 221988.MS0676; -. DR EnsemblBacteria; AAU37283; AAU37283; MS0676. DR GeneID; 3075648; -. DR KEGG; msu:MS0676; -. DR PATRIC; 22444743; VBIManSuc86752_0619. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; BMAN221988:GHGM-698-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 220 Thiamine-phosphate synthase. FT /FTId=PRO_1000008149. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 149 151 THZ-P binding (By similarity). FT REGION 201 202 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 152 152 HMP-PP (By similarity). FT BINDING 181 181 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24104 MW; 85A6AF050241539A CRC64; MNKIKSMLSV YFIAGSQDCR HLPGEPTENL LTILQRALEA GITCFQFREK GEQSLACDLQ LKRRLALKCL QLCRQFQVPF IVNDDVELAL SIQADGIHVG QKDTAVETIL RNTRNKPIIG LSINTLAQAL ANKDRQDIDY FGVGPIFPTN SKADHSPLVG MNFIRQIRQL GIDKPCVAIG GIKEESAAIL RRLGADGVAV ISAISHSVNI ANTVKTLAQK // ID THIE_MARAV Reviewed; 222 AA. AC A1TYG6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Maqu_0687; OS Marinobacter aquaeolei (strain ATCC 700491 / DSM 11845 / VT8) OS (Marinobacter hydrocarbonoclasticus (strain DSM 11845)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=351348; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700491 / DSM 11845 / VT8; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Edwards K., Richardson P.; RT "Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000514; ABM17785.1; -; Genomic_DNA. DR RefSeq; YP_957972.1; NC_008740.1. DR ProteinModelPortal; A1TYG6; -. DR STRING; 351348.Maqu_0687; -. DR EnsemblBacteria; ABM17785; ABM17785; Maqu_0687. DR GeneID; 4657514; -. DR KEGG; maq:Maqu_0687; -. DR PATRIC; 22456576; VBIMarAqu65105_1084. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MHYD351348:GHYZ-691-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 222 Thiamine-phosphate synthase. FT /FTId=PRO_0000336404. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23171 MW; 866BB6A6D20953DC CRC64; MGTVRSQIRP GLYAITDNRL TPADTLIVSV EAALAGGARL VQYRDKGSTA SERLVQARNL NSLCQGFDVP LLINDDPELA ARVGAAGVHL GQDDCSLVDA RRLLGEHAII GITCHHSLNL AQTAVDGGAD YLAFGRFYDS ATKPGAPPAS PDVLTEAKAL GLPITAIGGI TGNNAEPLIR AGADLVAVVG GLFGGQPSDI EARAKAFNRQ FARHHPLFSL SE // ID THIE_METAC Reviewed; 228 AA. AC Q8TMD6; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 14-MAY-2014, entry version 81. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MA_2722; OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / OS C2A). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=188937; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A; RX PubMed=11932238; DOI=10.1101/gr.223902; RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., RA FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., RA Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., RA Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W., RA Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., RA Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., RA Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., RA Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., RA Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., RA Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., RA Metcalf W.W., Birren B.; RT "The genome of Methanosarcina acetivorans reveals extensive metabolic RT and physiological diversity."; RL Genome Res. 12:532-542(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE010299; AAM06101.1; -; Genomic_DNA. DR RefSeq; NP_617621.1; NC_003552.1. DR ProteinModelPortal; Q8TMD6; -. DR STRING; 188937.MA2722; -. DR EnsemblBacteria; AAM06101; AAM06101; MA_2722. DR GeneID; 1474615; -. DR KEGG; mac:MA2722; -. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR PhylomeDB; Q8TMD6; -. DR BioCyc; MACE188937:GI2O-2752-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 228 Thiamine-phosphate synthase. FT /FTId=PRO_0000157069. FT REGION 52 56 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 199 200 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 24829 MW; FAFD36294DB6AACE CRC64; MNQKNSNPKN PPRKISLLKQ IDFYLVTDSG LSKKGTLSDV REAVDAGCKI VQYREKNKST KEMIDEASEI KRICGDRAIF LVNDRIDVAL AVDADGVHIG QDDMPIEIAK KLLGPEKIIG LTVHNVEEAL EAERNGADYV GLGSIFDTST KKDAGKGIGP ASIKEVKNAI KIPVVAIGGI NRENCIPVVE NGADSFVAIS AVVCSDDVKR ETRKFIEIIR EIKNSGRQ // ID THIE_METB6 Reviewed; 216 AA. AC A7IA09; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Mboo_2056; OS Methanoregula boonei (strain 6A8). OC Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales; OC Methanoregulaceae; Methanoregula. OX NCBI_TaxID=456442; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=6A8; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., RA Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Zinder S., Richardson P.; RT "Complete sequence of Candidatus Methanoregula boonei 6A8."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000780; ABS56570.1; -; Genomic_DNA. DR RefSeq; YP_001405213.1; NC_009712.1. DR ProteinModelPortal; A7IA09; -. DR STRING; 456442.Mboo_2056; -. DR EnsemblBacteria; ABS56570; ABS56570; Mboo_2056. DR GeneID; 5410689; -. DR KEGG; mbn:Mboo_2056; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; MBOO456442:GH2T-2100-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 216 Thiamine-phosphate synthase. FT /FTId=PRO_0000336436. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 22249 MW; A6AEFAE431F9BE36 CRC64; MRLDLYVITD GAIGGGRSHA EIARFACAGG ADAIQLRDKA CGPDALCRIG REIRAITRDT GTLFIVNDRL DVALACGADG VHLGQGDLRV DTARRLAPRP FMIGVSVGNA EEAISAVVAG ADYVAASPIF ATSSKDDAGP GCGISGLREI RAAVAVPVVA IGGITRDNVA EVIAGGADSI AVISAVVGQP DIVAAARDLR ERITTAKEQY REKRDA // ID THIE_METBF Reviewed; 220 AA. AC Q466J5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 63. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Mbar_A3318; OS Methanosarcina barkeri (strain Fusaro / DSM 804). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=269797; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fusaro / DSM 804; RX PubMed=16980466; DOI=10.1128/JB.00810-06; RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., RA Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., RA Sowers K.R.; RT "The Methanosarcina barkeri genome: comparative analysis with RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive RT rearrangement within methanosarcinal genomes."; RL J. Bacteriol. 188:7922-7931(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000099; AAZ72197.1; -; Genomic_DNA. DR RefSeq; YP_306777.1; NC_007355.1. DR ProteinModelPortal; Q466J5; -. DR STRING; 269797.Mbar_A3318; -. DR EnsemblBacteria; AAZ72197; AAZ72197; Mbar_A3318. DR GeneID; 3626097; -. DR KEGG; mba:Mbar_A3318; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; MBAR269797:GHUW-3373-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 220 Thiamine-phosphate synthase. FT /FTId=PRO_0000336437. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 79 79 Magnesium (By similarity). FT METAL 98 98 Magnesium (By similarity). FT BINDING 78 78 HMP-PP (By similarity). FT BINDING 117 117 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 24007 MW; 36E31DA2E28B10E4 CRC64; MKQKGFSRKS SLLKEIDFYL VTDSGLSMKG TLSDVRDAVE SGCRIVQYRE KDKSTKEMVE EASEIKRICS GRAIFLVNDR IDVALAVDAD GVHIGQDDMP VETARKLLGE DKIIGLSVND REEAVLAEKL GADYVGLGPI FDTATKKDAG EGIGPLKIRE VKDAIKLPVV AIGGINKENC ESVIQNGADS LVAISAVVCS NDVKREAKYF IDMIRRTRKA // ID THIE_METCA Reviewed; 224 AA. AC Q602R3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 14-MAY-2014, entry version 67. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MCA2999; OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath). OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylococcus. OX NCBI_TaxID=243233; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath; RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303; RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., RA Ravel J., Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., RA Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., RA Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S., RA Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R., RA Eisen J.A.; RT "Genomic insights into methanotrophy: the complete genome sequence of RT Methylococcus capsulatus (Bath)."; RL PLoS Biol. 2:1616-1628(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017282; AAU90980.1; -; Genomic_DNA. DR RefSeq; YP_115387.1; NC_002977.6. DR ProteinModelPortal; Q602R3; -. DR STRING; 243233.MCA2999; -. DR EnsemblBacteria; AAU90980; AAU90980; MCA2999. DR GeneID; 3103993; -. DR KEGG; mca:MCA2999; -. DR PATRIC; 22609892; VBIMetCap22254_3038. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 224 Thiamine-phosphate synthase. FT /FTId=PRO_0000336406. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 224 AA; 23261 MW; AF7ED6BDBB8346B0 CRC64; MKNSMYLPFP SKGLYAITPD RLQGDALLAA AESAILGGAA VVQYRPKSGP ASDRLSDGIR LQELCRTAGI PLIVNDSPRL AAEIGADGVH LGKNDGSVAA ARHVLGDRAI VGISCYDSLE RALRAEAEGA NYVAFGALFP SATKPCASRA RLETLREAGT RLQIPIAAIG GIDTTNAGQV IGAGADLVAA VEAVFGAADV ARAARELCSL FHAPRKRRPR CDDA // ID THIE_METFK Reviewed; 209 AA. AC Q1GXW1; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 1. DT 14-MAY-2014, entry version 55. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Mfla_2663; OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylobacillus. OX NCBI_TaxID=265072; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT / ATCC 51484 / DSM 6875; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., RA Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N., Anderson I., RA Richardson P.; RT "Complete sequence of Methylobacillus flagellatus KT."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000284; ABE50926.1; -; Genomic_DNA. DR RefSeq; YP_546767.1; NC_007947.1. DR ProteinModelPortal; Q1GXW1; -. DR STRING; 265072.Mfla_2663; -. DR EnsemblBacteria; ABE50926; ABE50926; Mfla_2663. DR GeneID; 4001761; -. DR KEGG; mfa:Mfla_2663; -. DR PATRIC; 32271177; VBIMetFla97085_2796. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MFLA265072:GHWJ-2724-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_0000336405. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21534 MW; 0F3F3D88EE1C7DF2 CRC64; MTRHSLPPIQ GLYAITPDET DTSRLVTISE AVLAGGAGAL QYRNKRVSGT QASNQAGALL DLCRRFQTPL IINDDVQLAA ALDADGVHLG IDDGDIAAAR AALGPDKIIG ASCYNNLALA RQAASLGADY VAFGACFPSS TKPDAPRADI ALFAKARELG LPIVAIGGIT LDNAAGIISA GADAVAVIGA LWTAADIEAR ARQFHQLFN // ID THIE_METHJ Reviewed; 206 AA. AC Q2FM63; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Mhun_1934; OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC OS 100397 / JF-1). OC Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales; OC Methanospirillaceae; Methanospirillum. OX NCBI_TaxID=323259; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., RA Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., RA Stams A.J.M., Boone D.R., Richardson P.; RT "Complete sequence of Methanospirillum hungatei JF-1."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000254; ABD41645.1; -; Genomic_DNA. DR RefSeq; YP_503364.1; NC_007796.1. DR ProteinModelPortal; Q2FM63; -. DR STRING; 323259.Mhun_1934; -. DR EnsemblBacteria; ABD41645; ABD41645; Mhun_1934. DR GeneID; 3924131; -. DR KEGG; mhu:Mhun_1934; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; MHUN323259:GH0L-1956-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 206 Thiamine-phosphate synthase. FT /FTId=PRO_0000336438. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 21361 MW; 52E8EEAE5C525095 CRC64; MDCGLYIITD EILAPGCSHI QIAKESLSGG AKIIQLRDKR RNAAELYAIA QEIRSLCTQH HARFIVNDRL DIALAVQADG VHLGQDDLPL SAARLLAPRP FIIGVSVGTV EEAVLAEKGG ADYLGVGPVY PTGTKADAGP AVGPGLIRSI RERVAIPIIA IGGINLTNAG DVLAAGADGI AVISAVICSP DIAAASRKFA DLMIHS // ID THIE_METM5 Reviewed; 207 AA. AC A4FX32; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MmarC5_0446; OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=402880; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C5 / ATCC BAA-1333; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., RA Han C., Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., RA Richardson P.; RT "Complete sequence of chromosome of Methanococcus maripaludis C5."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000609; ABO34761.1; -; Genomic_DNA. DR RefSeq; YP_001096976.1; NC_009135.1. DR ProteinModelPortal; A4FX32; -. DR SMR; A4FX32; 3-206. DR STRING; 402880.MmarC5_0446; -. DR EnsemblBacteria; ABO34761; ABO34761; MmarC5_0446. DR GeneID; 4928433; -. DR KEGG; mmq:MmarC5_0446; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GGINKER; -. DR BioCyc; MMAR402880:GJ2R-457-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000008150. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22375 MW; A695BD6550CA3D7E CRC64; MKFKDKLKFY VITDSNYSDE VSSVEKALKG GASSIQLRMK TSSTRKMIEV GNKLRTLTSE YDALFFVNDR LDVAQAVNAD GIHVGIDDMP VSKIKEIAPN LIIGASAYNI DEMKTAEYEG ADYLGVGAVY STNTKLDARN LGLDGLKDIS KIANLPIVAI GGINHSNVEN VLECGVSGVA VVSAIVGAEN ILKSAENMHE LIKKYIK // ID THIE_METM6 Reviewed; 207 AA. AC A9AAG9; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MmarC6_1529; OS Methanococcus maripaludis (strain C6 / ATCC BAA-1332). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=444158; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C6 / ATCC BAA-1332; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., RA Whitman W.B., Richardson P.; RT "Complete sequence of Methanococcus maripaludis C6."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000867; ABX02342.1; -; Genomic_DNA. DR RefSeq; YP_001549574.1; NC_009975.1. DR ProteinModelPortal; A9AAG9; -. DR SMR; A9AAG9; 3-206. DR STRING; 444158.MmarC6_1529; -. DR EnsemblBacteria; ABX02342; ABX02342; MmarC6_1529. DR GeneID; 5737382; -. DR KEGG; mmx:MmarC6_1529; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; MMAR444158:GHN2-1575-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000093679. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22302 MW; E62B97F8B1B21DE0 CRC64; MKFKDKLKFY VITDSNYSDE VISVEEALKG GASSIQLRMK TSSTRKMIEV GNKLRKLTSE YDALFFVNDR LDVAQAVNAD GIHVGIDDMP ISKIKEIAPN LIIGASAYNT DEMKTAEMGG ADYLGVGAVY STNTKLDARN LGLDGLKNIS KIASIPIVAI GGINHLNVEN VLECGVSGVA VVSAIVGAEN ILKSAENMNE LIKKYIK // ID THIE_METM7 Reviewed; 207 AA. AC A6VG83; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MmarC7_0390; OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=426368; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C7 / ATCC BAA-1331; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Anderson I., Sieprawska-Lupa M., RA Whitman W.B., Richardson P.; RT "Complete sequence of Methanococcus maripaludis C7."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000745; ABR65459.1; -; Genomic_DNA. DR RefSeq; YP_001329610.1; NC_009637.1. DR ProteinModelPortal; A6VG83; -. DR SMR; A6VG83; 3-206. DR STRING; 426368.MmarC7_0390; -. DR EnsemblBacteria; ABR65459; ABR65459; MmarC7_0390. DR GeneID; 5328208; -. DR KEGG; mmz:MmarC7_0390; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; MMAR426368:GHHL-392-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000008151. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22458 MW; 5229DFF91FFFD597 CRC64; MKFKDKLKFY VITDNNYSNE VVSVEEALKG GASSIQLRMK NSTTREMIEV GNELRKLTLE YDALFFVNDR LDVAQVVNAD GIHVGIDDMP VSKIKEIAPN LIIGASAYNM EEMKTAESEG ADYLGVGAVY STNTKLDARN LGIDGLKSIS KLSKLPIVAI GGINHSNVQN VLECGVSGVA VVSAIVGAEN ILKSAENMNE LIKKYIK // ID THIE_METMA Reviewed; 240 AA. AC Q8PS49; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2002, sequence version 1. DT 14-MAY-2014, entry version 85. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MM_3235; OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / OS JCM 11833 / OCM 88) (Methanosarcina frisia). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=192952; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88; RX PubMed=12125824; RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., RA Fritz H.-J., Gottschalk G.; RT "The genome of Methanosarcina mazei: evidence for lateral gene RT transfer between Bacteria and Archaea."; RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008384; AAM32931.1; -; Genomic_DNA. DR RefSeq; NP_635259.1; NC_003901.1. DR ProteinModelPortal; Q8PS49; -. DR STRING; 192952.MM_3235; -. DR EnsemblBacteria; AAM32931; AAM32931; MM_3235. DR GeneID; 1481577; -. DR KEGG; mma:MM_3235; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR BioCyc; MMAZ192952:GCK2-3300-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 240 Thiamine-phosphate synthase. FT /FTId=PRO_0000157070. FT REGION 63 67 HMP-PP binding (By similarity). FT REGION 159 161 THZ-P binding (By similarity). FT REGION 210 211 THZ-P binding (By similarity). FT METAL 95 95 Magnesium (By similarity). FT METAL 114 114 Magnesium (By similarity). FT BINDING 94 94 HMP-PP (By similarity). FT BINDING 133 133 HMP-PP (By similarity). FT BINDING 162 162 HMP-PP (By similarity). FT BINDING 190 190 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 240 AA; 25817 MW; AD2F6432E5946705 CRC64; MEKKNCNPKE TSSQKASDKN HLTLKNSLLK DIDFYLVTDS GLSKKGTLSD VKESVEAGCK IVQYREKCKS TGEMIDEAAE IKKICSGRAI FLINDRIDVA LVVDADGVHI GQDDMPIETA RKILGANKII GLTVHNADEA IEAEKSGADY VGLGSIFDTF TKKDAGKGIG PASIREVRNA IKISVVAIGG INKENCRSVI ENGADSLVAI SAVVCSDDVK KETREFIDII REIKGTGSSK // ID THIE_METMJ Reviewed; 211 AA. AC A3CS45; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Memar_0261; OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1). OC Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales; OC Methanomicrobiaceae; Methanoculleus. OX NCBI_TaxID=368407; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35101 / DSM 1498 / JR1; RX PubMed=21304656; DOI=10.4056/sigs.32535; RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A., RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C., RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., RA Hauser L., Land M., Lucas S., Richardson P., Whitman W.B., RA Kyrpides N.C.; RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. RT 1981 type strain JR1."; RL Stand. Genomic Sci. 1:189-196(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000562; ABN56195.1; -; Genomic_DNA. DR RefSeq; YP_001046177.1; NC_009051.1. DR ProteinModelPortal; A3CS45; -. DR STRING; 368407.Memar_0261; -. DR EnsemblBacteria; ABN56195; ABN56195; Memar_0261. DR GeneID; 4846234; -. DR KEGG; mem:Memar_0261; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; MMAR368407:GH7L-262-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000336435. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 20929 MW; 5B44FA0E19E179C5 CRC64; MGYDLYVVTD ETIGRGRTHT DLARLAAAGG ADVIQLRDKR LPGRDLLSAA VAIREITTDA GALFIVNDRL DVAIAAGADG VHLGANDLPV GEARRIVPPG FLIGASVGSV AAAVRAAAEG ADYVALSPTF ATGSKDDAGP GCGLAALKEI RAAVSLPLVA IGGITAANVA DVIAAGADGV AVISAVVGEG DVTAAARSLR DRIAAAKAEG R // ID THIE_METMP Reviewed; 207 AA. AC P61413; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MMP1139; OS Methanococcus maripaludis (strain S2 / LL). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=267377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S2 / LL; RX PubMed=15466049; DOI=10.1128/JB.186.20.6956-6969.2004; RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J., RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., RA Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., RA Major T.A., Moore B.C., Porat I., Palmeiri A., Rouse G., RA Saenphimmachak C., Soell D., Van Dien S., Wang T., Whitman W.B., RA Xia Q., Zhang Y., Larimer F.W., Olson M.V., Leigh J.A.; RT "Complete genome sequence of the genetically tractable RT hydrogenotrophic methanogen Methanococcus maripaludis."; RL J. Bacteriol. 186:6956-6969(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX950229; CAF30695.1; -; Genomic_DNA. DR RefSeq; NP_988259.1; NC_005791.1. DR ProteinModelPortal; P61413; -. DR SMR; P61413; 3-206. DR STRING; 267377.MMP1139; -. DR EnsemblBacteria; CAF30695; CAF30695; MMP1139. DR GeneID; 2762052; -. DR KEGG; mmp:MMP1139; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; MMAR267377:GJ77-1170-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_0000157071. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22358 MW; 17B283A0ADE5E1D7 CRC64; MKFKDKLKFY VITDSNYSDE VISVEESLKG GATSIQLRMK TSSTRKMIEV GNKLRKLTSE YDALFFVNDR LDVAQAVNAD GIHVGIDDMP VSKIKEIAPN LIIGASAYNL DEMKTAESEG ADYLGVGAVY STNTKLDARD LGINGLKNIS KIANLPIVAI GGINHSNVEN VLKCGVSGVA VVSAIVGAEN ILKSAENMNE LIKKYIK // ID THIE_METS3 Reviewed; 209 AA. AC A5ULP4; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Msm_0917; OS Methanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861). OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanobrevibacter. OX NCBI_TaxID=420247; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PS / ATCC 35061 / DSM 861; RX PubMed=17563350; DOI=10.1073/pnas.0704189104; RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., RA Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K., RA Gordon J.I.; RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to RT the human gut."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000678; ABQ87122.1; -; Genomic_DNA. DR RefSeq; YP_001273490.1; NC_009515.1. DR ProteinModelPortal; A5ULP4; -. DR STRING; 420247.Msm_0917; -. DR EnsemblBacteria; ABQ87122; ABQ87122; Msm_0917. DR GeneID; 5217370; -. DR KEGG; msi:Msm_0917; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; MSMI420247:GHWZ-942-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_1000057645. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22713 MW; 5B9A05467142E296 CRC64; MNNLDLSLYL VTNNSEDEEK FLNIIEESLK GGVSVVQLRE KKAETLDFYN LALKVKEITQ KYNVPLIIND RIDIALAIDA DGVHVGQSDM PAKTARSMIG EDKILGVSAA NIKEAKKAQR ESADYIGVGA VYPTNTKDDA TSVPKKELKE IVKSVDIPVV AIGGITQENA HELNDCGIDG LSVVSAIMEA KNPKIASENL LKEFKAKNS // ID THIE_METVS Reviewed; 206 AA. AC A6UPE6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Mevan_0461; OS Methanococcus vannielii (strain SB / ATCC 35089 / DSM 1224). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=406327; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB / ATCC 35089 / DSM 1224; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.; RT "Complete sequence of Methanococcus vannielii SB."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000742; ABR54368.1; -; Genomic_DNA. DR RefSeq; YP_001322980.1; NC_009634.1. DR ProteinModelPortal; A6UPE6; -. DR SMR; A6UPE6; 3-206. DR STRING; 406327.Mevan_0461; -. DR EnsemblBacteria; ABR54368; ABR54368; Mevan_0461. DR GeneID; 5325364; -. DR KEGG; mvn:Mevan_0461; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; MVAN406327:GI04-466-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 206 Thiamine-phosphate synthase. FT /FTId=PRO_1000008152. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22516 MW; 32D35A8D9CD6D2E5 CRC64; MTFKNKLKFY VITDRKYSCE VYSVEQALKG GATAVQLRMK SSNTREMVEV GQKIRKLTLE YDALFFVNDR LDIAQAVKSD GIHVGIDDIS ISKIKEIAPE LIIGASAYNI NEMKIAESEG ADYLGVGSVY PTNTKLDARY LGLNGLKELS NCSNLPVVAI GGINHENVKE VLMCGVSGVA VVSAIVGAND IIFSAKKMNE IIKKYI // ID THIE_MOOTA Reviewed; 210 AA. AC Q2RGI8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Moth_2162; OS Moorella thermoacetica (strain ATCC 39073). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Moorella group; Moorella. OX NCBI_TaxID=264732; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39073; RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x; RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.; RT "The complete genome sequence of Moorella thermoacetica (f. RT Clostridium thermoaceticum)."; RL Environ. Microbiol. 10:2550-2573(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000232; ABC20451.1; -; Genomic_DNA. DR RefSeq; YP_430994.1; NC_007644.1. DR ProteinModelPortal; Q2RGI8; -. DR STRING; 264732.Moth_2162; -. DR EnsemblBacteria; ABC20451; ABC20451; Moth_2162. DR GeneID; 3833011; -. DR KEGG; mta:Moth_2162; -. DR PATRIC; 22641774; VBIMooThe6753_2355. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MTHE264732:GH0A-2241-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 210 Thiamine-phosphate synthase. FT /FTId=PRO_1000008153. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 184 185 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 210 AA; 21409 MW; 07F95C0103D6CFF1 CRC64; MPQWDLYVVI TTKLGGGRPT LELVRGALAG GATAIQLREK ELPARELVEL GRAIRELTRD AGATFIVNDR LDIALAVEAD GLHIGQEDLP APVARKLLGP EKILGVSAGT TDEARQAEVD GADYLGVGSI FATGSKGDAG SPIGLEGLRA IRAAVKIPIV GIGGINPDNA AGVIAAGADG VSVISAVIGA ADVAAAARRL REVVTRARGK // ID THIE_MYCA1 Reviewed; 223 AA. AC A0QLT6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MAV_4748; OS Mycobacterium avium (strain 104). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=243243; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=104; RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., RA Fraser C.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000479; ABK67563.1; -; Genomic_DNA. DR RefSeq; YP_883874.1; NC_008595.1. DR ProteinModelPortal; A0QLT6; -. DR STRING; 243243.MAV_4748; -. DR EnsemblBacteria; ABK67563; ABK67563; MAV_4748. DR GeneID; 4529670; -. DR KEGG; mav:MAV_4748; -. DR PATRIC; 17991195; VBIMycAvi38287_4666. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MAVI243243:GH3Y-4747-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 223 Thiamine-phosphate synthase. FT /FTId=PRO_1000008154. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23241 MW; 6CBFB820FCEFD41B CRC64; MHQRLATLAA ARLYLCTDAR RERGDLAEFA DAALAGGVDV IQLRDKGSPG EQRFGPLEAR DELAACEILA DAARRHGALF AVNDRADIAR AAGADVLHLG QGDLPLDVAR AFVGPDVLLG LSSHDRDQMT AAAAGPADYF CVGPCWPTPT KPGRAAPGLA LVRAAAELRT GKPWFAIGGI DAQRLPEVLD AGARRVVVVR AITAADDPAA AARRLSSALA AAR // ID THIE_MYCBO Reviewed; 222 AA. AC P66917; P96260; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 62. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Mb0422c; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., RA Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., RA Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., RA Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX248335; CAD93285.1; -; Genomic_DNA. DR RefSeq; NP_854085.1; NC_002945.3. DR ProteinModelPortal; P66917; -. DR SMR; P66917; 1-221. DR STRING; 233413.Mb0422c; -. DR EnsemblBacteria; CAD93285; CAD93285; Mb0422c. DR GeneID; 1091426; -. DR KEGG; mbo:Mb0422c; -. DR PATRIC; 18002583; VBIMycBov88188_0460. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 222 Thiamine-phosphate synthase. FT /FTId=PRO_0000157027. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID THIE_MYCBP Reviewed; 222 AA. AC A1KFN6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=BCG_0453c; OS Mycobacterium bovis (strain BCG / Pasteur 1173P2). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=410289; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCG / Pasteur 1173P2; RX PubMed=17372194; DOI=10.1073/pnas.0700869104; RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., RA Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., RA Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., RA Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T.; RT "Genome plasticity of BCG and impact on vaccine efficacy."; RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM408590; CAL70438.1; -; Genomic_DNA. DR RefSeq; YP_976551.1; NC_008769.1. DR ProteinModelPortal; A1KFN6; -. DR SMR; A1KFN6; 1-221. DR STRING; 410289.BCG_0453c; -. DR EnsemblBacteria; CAL70438; CAL70438; BCG_0453c. DR GeneID; 4695711; -. DR KEGG; mbb:BCG_0453c; -. DR PATRIC; 18011421; VBIMycBov80988_0490. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MBOV410289:GJW7-459-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 222 Thiamine-phosphate synthase. FT /FTId=PRO_1000008155. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID THIE_MYCGI Reviewed; 237 AA. AC A4T2R5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Mflv_0198; OS Mycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens OS (strain ATCC 700033 / PYR-GCK)). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=350054; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PYR-GCK; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C., RA Richardson P.; RT "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000656; ABP42693.1; -; Genomic_DNA. DR RefSeq; YP_001131481.1; NC_009338.1. DR ProteinModelPortal; A4T2R5; -. DR STRING; 350054.Mflv_0198; -. DR EnsemblBacteria; ABP42693; ABP42693; Mflv_0198. DR GeneID; 4971820; -. DR KEGG; mgi:Mflv_0198; -. DR PATRIC; 18028378; VBIMycGil17082_0203. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MGIL350054:GHK8-198-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 237 Thiamine-phosphate synthase. FT /FTId=PRO_0000336407. FT REGION 57 61 HMP-PP binding (By similarity). FT REGION 162 164 THZ-P binding (By similarity). FT METAL 99 99 Magnesium (By similarity). FT METAL 118 118 Magnesium (By similarity). FT BINDING 98 98 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 165 165 HMP-PP (By similarity). FT BINDING 193 193 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 237 AA; 25081 MW; 5E23CA4FCC6C6A3F CRC64; MWSRSSLRRL TATVSTVPES PSLQGARLYL CTDARRERGD LADFADAALA GGVDIIQLRD KGSPGEKAFG PLEARAEIDA LHVLAEAARR HNALVAVNDR ADIARASGAE VLHLGQDDLP LTVARQIVGD RVIGRSTHDL AQAEAAIAED VDYFCVGPCW PTPTKPGRAA PGLDLVREVA ALNTTKPWFA IGGIDAQRLP DVLDAGARRV VVVRAITAAE DPRAAAEQLA GMLDSAV // ID THIE_MYCLB Reviewed; 235 AA. AC B8ZU95; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 36. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MLBr00300; OS Mycobacterium leprae (strain Br4923). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=561304; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Br4923; RX PubMed=19881526; DOI=10.1038/ng.477; RA Monot M., Honore N., Garnier T., Zidane N., Sherafi D., RA Paniz-Mondolfi A., Matsuoka M., Taylor G.M., Donoghue H.D., RA Bouwman A., Mays S., Watson C., Lockwood D., Khamispour A., RA Dowlati Y., Jianping S., Rea T.H., Vera-Cabrera L., Stefani M.M., RA Banu S., Macdonald M., Sapkota B.R., Spencer J.S., Thomas J., RA Harshman K., Singh P., Busso P., Gattiker A., Rougemont J., RA Brennan P.J., Cole S.T.; RT "Comparative genomic and phylogeographic analysis of Mycobacterium RT leprae."; RL Nat. Genet. 41:1282-1289(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM211192; CAR70393.1; -; Genomic_DNA. DR RefSeq; YP_002502967.1; NC_011896.1. DR ProteinModelPortal; B8ZU95; -. DR STRING; 561304.MLBr_00300; -. DR EnsemblBacteria; CAR70393; CAR70393; MLBr00300. DR GeneID; 7326365; -. DR KEGG; mlb:MLBr_00300; -. DR PATRIC; 18040460; VBIMycLep121698_0463. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MLEP561304:GJP6-310-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 235 Thiamine-phosphate synthase. FT /FTId=PRO_1000198082. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 160 162 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 163 163 HMP-PP (By similarity). FT BINDING 191 191 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 235 AA; 24846 MW; 3447784202D3DD1C CRC64; MQEPHRQPAI CLSTRLAKAR LYLCTDARRE RGDLAQFVNA ALAGGVDIVQ LRDKGSVGEQ QFGPLEARDA LAACEIFTDA TGRHDALFAV NDRADIARAA GADVLHLGQG DLPPGVARQI VCRQMLIGLS THDRHQVAAA VAALDAGLVD YFCVGPCWPT PTKPDRPAPG LELVRAAAEL AGDKPWFAIG GIDAQRLPDV LHAGARRIVV VRAITAAADP RAAAEQLIST LTATS // ID THIE_MYCLE Reviewed; 235 AA. AC Q9ZBL5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 14-MAY-2014, entry version 87. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=ML0300; ORFNames=MLCB1450.23c; OS Mycobacterium leprae (strain TN). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=272631; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TN; RX PubMed=11234002; DOI=10.1038/35059006; RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., RA Barrell B.G.; RT "Massive gene decay in the leprosy bacillus."; RL Nature 409:1007-1011(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL035159; CAA22707.1; -; Genomic_DNA. DR EMBL; AL583918; CAC29808.1; -; Genomic_DNA. DR PIR; T44738; T44738. DR RefSeq; NP_301336.1; NC_002677.1. DR ProteinModelPortal; Q9ZBL5; -. DR STRING; 272631.ML0300; -. DR EnsemblBacteria; CAC29808; CAC29808; CAC29808. DR GeneID; 908861; -. DR KEGG; mle:ML0300; -. DR PATRIC; 18051036; VBIMycLep78757_0467. DR Leproma; ML0300; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 235 Thiamine-phosphate synthase. FT /FTId=PRO_0000157024. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 160 162 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 163 163 HMP-PP (By similarity). FT BINDING 191 191 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 235 AA; 24846 MW; 3447784202D3DD1C CRC64; MQEPHRQPAI CLSTRLAKAR LYLCTDARRE RGDLAQFVNA ALAGGVDIVQ LRDKGSVGEQ QFGPLEARDA LAACEIFTDA TGRHDALFAV NDRADIARAA GADVLHLGQG DLPPGVARQI VCRQMLIGLS THDRHQVAAA VAALDAGLVD YFCVGPCWPT PTKPDRPAPG LELVRAAAEL AGDKPWFAIG GIDAQRLPDV LHAGARRIVV VRAITAAADP RAAAEQLIST LTATS // ID THIE_MYCMM Reviewed; 220 AA. AC B2HPZ9; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MMAR_0717; OS Mycobacterium marinum (strain ATCC BAA-535 / M). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=216594; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-535 / M; RX PubMed=18403782; DOI=10.1101/gr.075069.107; RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., RA Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., RA Jagels K., Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A., RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., RA Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.; RT "Insights from the complete genome sequence of Mycobacterium marinum RT on the evolution of Mycobacterium tuberculosis."; RL Genome Res. 18:729-741(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000854; ACC39176.1; -; Genomic_DNA. DR RefSeq; YP_001849031.1; NC_010612.1. DR ProteinModelPortal; B2HPZ9; -. DR STRING; 216594.MMAR_0717; -. DR EnsemblBacteria; ACC39176; ACC39176; MMAR_0717. DR GeneID; 6224966; -. DR KEGG; mmi:MMAR_0717; -. DR PATRIC; 18062151; VBIMycMar75906_0768. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MMAR216594:GJOB-717-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 220 Thiamine-phosphate synthase. FT /FTId=PRO_1000093680. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23065 MW; 378197B21B48683D CRC64; MHSRLATARL YLCTDARRER GDLADFADAA LAGGVDIIQL RDKGSAGEQR FGPLEARDEL AACEILADAA ARHAAMFAVN DRADIARAAR ADVLHLGQRD LPVDVARAIT GPATLIGQST HDRDQVSAAA IGAVDYFCVG PCWPTPTKPG RTAPGLDLVR FAADVAGAKP WFAIGGIDGV RLPEVLAAGA RRIVVVRAIT AADDPREAAA KLKSELLAAI // ID THIE_MYCPA Reviewed; 223 AA. AC P61412; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 1. DT 14-MAY-2014, entry version 73. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MAP_3897c; OS Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=262316; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-968 / K-10; RX PubMed=16116077; DOI=10.1073/pnas.0505662102; RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., RA Banerji N., Kanjilal S., Kapur V.; RT "The complete genome sequence of Mycobacterium avium subspecies RT paratuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016958; AAS06447.1; -; Genomic_DNA. DR RefSeq; NP_962831.1; NC_002944.2. DR ProteinModelPortal; P61412; -. DR STRING; 262316.MAP3897c; -. DR EnsemblBacteria; AAS06447; AAS06447; MAP_3897c. DR GeneID; 2720829; -. DR KEGG; mpa:MAP3897c; -. DR PATRIC; 18000684; VBIMycAvi108102_4148. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MAVI262316:GCQR-3942-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 223 Thiamine-phosphate synthase. FT /FTId=PRO_0000157025. FT REGION 42 46 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT METAL 84 84 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT BINDING 83 83 HMP-PP (By similarity). FT BINDING 122 122 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 179 179 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23206 MW; 1A7ECE8B8C3C9D6F CRC64; MHQRLATLAA ARLYLCTDAR RERGDLAEFA DAALAGGVDV IQLRDKGSPG EQRFGPLEAR DELAACEILA DAARRHGALF AVNDRADIAR AAGADVLHLG QGDLPLEVAR AFVGPDVLLG LSSHDRDQMA AAAAGPADYF CVGPCWPTPT KPGRAAPGLA LVRAAAELHT GKPWFAIGGI DAQRLPEVLD AGARRVVVVR AITAADDPAA AARRLSSALA AAR // ID THIE_MYCS2 Reviewed; 227 AA. AC A0QQK7; I7G410; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 54. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MSMEG_0789, MSMEI_0774; OS Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=246196; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., RA Fraser C.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20; RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.; RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic RT mutations or sequencing errors?"; RL Genome Biol. 8:R20.1-R20.9(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RX PubMed=18955433; DOI=10.1101/gr.081901.108; RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.; RT "Ortho-proteogenomics: multiple proteomes investigation through RT orthology and a new MS-based protocol."; RL Genome Res. 19:128-135(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=AFP37254.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000480; ABK70128.1; -; Genomic_DNA. DR EMBL; CP001663; AFP37254.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_006565549.1; NC_018289.1. DR RefSeq; YP_885195.1; NC_008596.1. DR ProteinModelPortal; A0QQK7; -. DR STRING; 246196.MSMEG_0789; -. DR EnsemblBacteria; ABK70128; ABK70128; MSMEG_0789. DR EnsemblBacteria; AFP37254; AFP37254; MSMEI_0774. DR GeneID; 13427944; -. DR GeneID; 4533425; -. DR KEGG; msg:MSMEI_0774; -. DR KEGG; msm:MSMEG_0789; -. DR PATRIC; 18074048; VBIMycSme59918_0785. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MSME246196:GJ4Y-790-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 227 Thiamine-phosphate synthase. FT /FTId=PRO_0000336408. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT METAL 88 88 Magnesium (By similarity). FT METAL 107 107 Magnesium (By similarity). FT BINDING 87 87 HMP-PP (By similarity). FT BINDING 126 126 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 183 183 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 23939 MW; 3AEA0B5DFD7E6CBB CRC64; MDQAVELPVQ RLQRASLYLC TDARRERGDL AEFADAALAG GVDLIQLRDK GSAGEKQFGP LEARQELEAL EILADAARRH GALLAVNDRA DIALAAGADV LHLGQDDLPL DVARGIIGRR PVIGRSTHDA AQMAVAIEER VDYFCVGPCW PTPTKPGRPA PGLDLVRATA AHSPGKPWFA IGGIDQERLP EVLAAGARRV VVVRAITAAD DPKAAAEDLK AAISAAG // ID THIE_MYCSJ Reviewed; 226 AA. AC A3PTW9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Mjls_0534; OS Mycobacterium sp. (strain JLS). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=164757; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JLS; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Miller C.D., Anderson A.J., Sims R.C., Richardson P.; RT "Complete sequence of Mycobacterium sp. JLS."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000580; ABN96346.1; -; Genomic_DNA. DR RefSeq; YP_001068837.1; NC_009077.1. DR ProteinModelPortal; A3PTW9; -. DR STRING; 164757.Mjls_0534; -. DR EnsemblBacteria; ABN96346; ABN96346; Mjls_0534. DR GeneID; 4876279; -. DR KEGG; mjl:Mjls_0534; -. DR PATRIC; 18087187; VBIMycSp51234_0542. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MSP164757:GHV3-538-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 226 Thiamine-phosphate synthase. FT /FTId=PRO_0000336409. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT METAL 88 88 Magnesium (By similarity). FT METAL 107 107 Magnesium (By similarity). FT BINDING 87 87 HMP-PP (By similarity). FT BINDING 126 126 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 183 183 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23999 MW; A7125C7FA05EFA15 CRC64; MREPLDPLGP ALAQASLYLC TDARRERGDL AEFADAALAG GVDLIQLRDK GSAGERRFGP LEAREELAAL EILAEAARRR GALLAVNDRA DIALAAGADV LHLGQDDLPL PVARRIIGPR PLIGRSTHDS AQVSAAVAEE VDYFCVGPCW PTPTKPGREA PGLGLVREVA SRATEKPWFA IGGIDEARLP EVLDAGARRI VVVRAITAAD DPKAAARRLK DALVSR // ID THIE_MYCSK Reviewed; 226 AA. AC A1UAB4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 53. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Mkms_0556; OS Mycobacterium sp. (strain KMS). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=189918; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KMS; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Miller C.D., Richardson P.; RT "Complete sequence of chromosome of Mycobacterium sp. KMS."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000518; ABL89772.1; -; Genomic_DNA. DR RefSeq; YP_936562.1; NC_008705.1. DR ProteinModelPortal; A1UAB4; -. DR STRING; 189918.Mkms_0556; -. DR EnsemblBacteria; ABL89772; ABL89772; Mkms_0556. DR GeneID; 4615100; -. DR KEGG; mkm:Mkms_0556; -. DR PATRIC; 18100064; VBIMycSp70743_1083. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTLLQYR; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MSP189918:GH4X-560-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 226 Thiamine-phosphate synthase. FT /FTId=PRO_0000336410. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT METAL 88 88 Magnesium (By similarity). FT METAL 107 107 Magnesium (By similarity). FT BINDING 87 87 HMP-PP (By similarity). FT BINDING 126 126 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 183 183 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23895 MW; E5D662346DE7CC20 CRC64; MREPLDPLGP ALAQASLYLC TDARRERGDL AEFADAALAG GVDLIQLRDK GSAGERRFGP LEAREELAAL EILAEAARRH GALLAVNDRA DIALAAGADV LHLGQDDLPL PVARRIIGPS PLIGRSTHDS AQVAAAVAEE VDYFCVGPCW PTPTKPGREA PGLGLVREVA SRATEKPWFA IGGIDEARLP EVLDAGARRI VVVRAITAAD DPKAAARRLK DALVSR // ID THIE_MYCSS Reviewed; 226 AA. AC Q1BEL9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Mmcs_0544; OS Mycobacterium sp. (strain MCS). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=164756; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCS; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Miller C.D., Hughes J.E., Anderson A.J., RA Sims R.C., Richardson P.; RT "Complete sequence of chromosome of Mycobacterium sp. MCS."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000384; ABG06665.1; -; Genomic_DNA. DR RefSeq; YP_637721.1; NC_008146.1. DR ProteinModelPortal; Q1BEL9; -. DR STRING; 164756.Mmcs_0544; -. DR EnsemblBacteria; ABG06665; ABG06665; Mmcs_0544. DR GeneID; 4109390; -. DR KEGG; mmc:Mmcs_0544; -. DR PATRIC; 18111193; VBIMycSp106721_0559. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MSP164756:GHQ8-548-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 226 Thiamine-phosphate synthase. FT /FTId=PRO_0000336411. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 152 154 THZ-P binding (By similarity). FT METAL 88 88 Magnesium (By similarity). FT METAL 107 107 Magnesium (By similarity). FT BINDING 87 87 HMP-PP (By similarity). FT BINDING 126 126 HMP-PP (By similarity). FT BINDING 155 155 HMP-PP (By similarity). FT BINDING 183 183 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 226 AA; 23895 MW; E5D662346DE7CC20 CRC64; MREPLDPLGP ALAQASLYLC TDARRERGDL AEFADAALAG GVDLIQLRDK GSAGERRFGP LEAREELAAL EILAEAARRH GALLAVNDRA DIALAAGADV LHLGQDDLPL PVARRIIGPS PLIGRSTHDS AQVAAAVAEE VDYFCVGPCW PTPTKPGREA PGLGLVREVA SRATEKPWFA IGGIDEARLP EVLDAGARRI VVVRAITAAD DPKAAARRLK DALVSR // ID THIE_MYCTA Reviewed; 222 AA. AC A5TZE0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 45. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MRA_0420; OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=419947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25177 / H37Ra; RA Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y., RA Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.; RT "Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra, RT a non-pathogenic variant closely related to the well-characterized RT pathogenic strain H37Rv."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000611; ABQ72140.1; -; Genomic_DNA. DR RefSeq; YP_001281702.1; NC_009525.1. DR ProteinModelPortal; A5TZE0; -. DR SMR; A5TZE0; 1-221. DR STRING; 419947.MRA_0420; -. DR EnsemblBacteria; ABQ72140; ABQ72140; MRA_0420. DR GeneID; 5214254; -. DR KEGG; mra:MRA_0420; -. DR PATRIC; 18140466; VBIMycTub106795_0454. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MTUB419947:GJ8N-426-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 222 Thiamine-phosphate synthase. FT /FTId=PRO_1000008156. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID THIE_MYCTO Reviewed; 222 AA. AC P9WG74; L0T3H3; P66916; P96260; DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2014, sequence version 1. DT 14-MAY-2014, entry version 2. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MT0427; OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=83331; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., RA Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000516; AAK44651.1; -; Genomic_DNA. DR PIR; D70629; D70629. DR RefSeq; NP_334837.1; NC_002755.2. DR GeneID; 923706; -. DR UniPathway; UPA00060; UER00141. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 222 Thiamine-phosphate synthase. FT /FTId=PRO_0000428411. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID THIE_MYCTU Reviewed; 222 AA. AC P9WG75; L0T3H3; P66916; P96260; DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2014, sequence version 1. DT 14-MAY-2014, entry version 2. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Rv0414c; ORFNames=MTCY22G10.11c; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [2] RP DISRUPTION PHENOTYPE. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=14569030; DOI=10.1073/pnas.2134250100; RA Sassetti C.M., Rubin E.J.; RT "Genetic requirements for mycobacterial survival during infection."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12989-12994(2003). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, ENZYME REGULATION, RP IDENTIFICATION OF INHIBITORS, AND IDENTIFICATION AS A DRUG TARGET. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=21818324; DOI=10.1371/journal.pone.0022441; RA Khare G., Kar R., Tyagi A.K.; RT "Identification of inhibitors against Mycobacterium tuberculosis RT thiamin phosphate synthase, an important target for the development of RT anti-TB drugs."; RL PLoS ONE 6:E22441-E22441(2011). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH PHOSPHATE. RC STRAIN=ATCC 25618 / H37Rv; RA McCulloch K.M., Ramamoorthy D., Ishida K., Guida W.C., Begley T.P., RA Ealick S.E.; RT "Crystal structure and identification of potential inhibitor compounds RT for Mycobacterium tuberculosis thiamin phosphate synthase."; RL Submitted (JUL-2011) to the PDB data bank. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- ENZYME REGULATION: TPS activity is potently inhibited by several CC molecules such as 4-{[(2-hydroxy-5-nitrophenyl)methylidene]amino}- CC 5-methyl-2-(propan-2-yl)phenol (NSC compound 33472) and 2-{5- CC [2,4,6-(trinitrophenyl)amino]-1H-tetrazol-1-yl}ethanol (NSC CC compound 116720). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=5 uM for HMP-PP; CC KM=14 uM for THZ-P; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene are shown to be CC attenuated in a mouse tuberculosis model. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL123456; CCP43145.1; -; Genomic_DNA. DR PIR; D70629; D70629. DR RefSeq; NP_214928.1; NC_000962.3. DR RefSeq; YP_006513740.1; NC_018143.2. DR PDB; 3O63; X-ray; 2.35 A; A/B=1-222. DR PDBsum; 3O63; -. DR GeneID; 13318281; -. DR GeneID; 886391; -. DR TubercuList; Rv0414c; -. DR UniPathway; UPA00060; UER00141. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Magnesium; Metal-binding; KW Reference proteome; Thiamine biosynthesis; Transferase. FT CHAIN 1 222 Thiamine-phosphate synthase. FT /FTId=PRO_0000157026. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 82 82 Magnesium (By similarity). FT METAL 101 101 Magnesium (By similarity). FT BINDING 81 81 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). FT HELIX 1 8 FT STRAND 11 15 FT TURN 19 21 FT HELIX 24 33 FT STRAND 37 41 FT HELIX 47 52 FT HELIX 57 73 FT STRAND 77 82 FT HELIX 84 90 FT STRAND 93 97 FT HELIX 104 110 FT STRAND 116 121 FT HELIX 124 132 FT STRAND 136 140 FT HELIX 157 164 FT STRAND 173 178 FT TURN 181 183 FT HELIX 184 189 FT STRAND 195 198 FT HELIX 199 202 FT HELIX 207 219 SQ SEQUENCE 222 AA; 23271 MW; 2A9A32898F666C21 CRC64; MHESRLASAR LYLCTDARRE RGDLAQFAEA ALAGGVDIIQ LRDKGSPGEL RFGPLQARDE LAACEILADA AHRYGALFAV NDRADIARAA GADVLHLGQR DLPVNVARQI LAPDTLIGRS THDPDQVAAA AAGDADYFCV GPCWPTPTKP GRAAPGLGLV RVAAELGGDD KPWFAIGGIN AQRLPAVLDA GARRIVVVRA ITSADDPRAA AEQLRSALTA AN // ID THIE_MYCUA Reviewed; 220 AA. AC A0PRY2; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MUL_2806; OS Mycobacterium ulcerans (strain Agy99). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=362242; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Agy99; RX PubMed=17210928; DOI=10.1101/gr.5942807; RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., RA Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., RA Jones L.M., Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.; RT "Reductive evolution and niche adaptation inferred from the genome of RT Mycobacterium ulcerans, the causative agent of Buruli ulcer."; RL Genome Res. 17:192-200(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000325; ABL05101.1; -; Genomic_DNA. DR RefSeq; YP_906572.1; NC_008611.1. DR ProteinModelPortal; A0PRY2; -. DR STRING; 362242.MUL_2806; -. DR EnsemblBacteria; ABL05101; ABL05101; MUL_2806. DR GeneID; 4552974; -. DR KEGG; mul:MUL_2806; -. DR PATRIC; 18172874; VBIMycUlc37413_3274. DR GenoList; MUL_2806; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 220 Thiamine-phosphate synthase. FT /FTId=PRO_0000336412. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 220 AA; 23079 MW; 2ABD64601B48683D CRC64; MHSRLATARL YLCTDARRER GDLADFADAA LAGGVDIIQL RDKGSAGEQR FGPLEARDEL AACEILADAA ARHAAMFAVN DRADIARAAR ADVLHLGQRD LPVDVARAIT GPATLIGQST HDRDQVSAAA IGAVDYFCVG PCWPTPTKPG RTAPGLDLVR FAADVAGAKP WFAIGGIDGL RLPEVLAAGA RRIVVVRAIT AADDPREAAA KLKSELLAAI // ID THIE_MYCVP Reviewed; 221 AA. AC A1T2Z5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Mvan_0707; OS Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=350058; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 7251 / PYR-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Anderson I.J., Miller C., Richardson P.; RT "Complete sequence of Mycobacterium vanbaalenii PYR-1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000511; ABM11545.1; -; Genomic_DNA. DR RefSeq; YP_951551.1; NC_008726.1. DR ProteinModelPortal; A1T2Z5; -. DR STRING; 350058.Mvan_0707; -. DR EnsemblBacteria; ABM11545; ABM11545; Mvan_0707. DR GeneID; 4643650; -. DR KEGG; mva:Mvan_0707; -. DR PATRIC; 18179589; VBIMycVan31953_0728. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MVAN350058:GIWR-712-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 221 Thiamine-phosphate synthase. FT /FTId=PRO_0000336413. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 146 148 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 120 120 HMP-PP (By similarity). FT BINDING 149 149 HMP-PP (By similarity). FT BINDING 177 177 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23323 MW; 53BE51168B979C10 CRC64; MRESRKLDSA ALYLCTDARR ERGDLAEFAD AALAGGVDII QLRDKGSAGE QRFGPLEARE EIEVLATLAD AARRHGALFA VNDRADIALA ADADVLHLGQ DDLPLTVARR IVGDRIVGRS THDLDQVRAA VGEDVNYFCV GPCWPTPTKP GRPAPGLDLI RATAALGTDK PWFAIGGIDA ERLPEVLDAG ARRVVVVRAI TAADDPGAAA QRLAGMLSAA G // ID THIE_MYXXD Reviewed; 218 AA. AC Q1D282; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MXAN_5087; OS Myxococcus xanthus (strain DK 1622). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Myxococcus. OX NCBI_TaxID=246197; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DK 1622; RX PubMed=17015832; DOI=10.1073/pnas.0607335103; RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., RA Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C., RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R., RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R., RA Kaplan H.B.; RT "Evolution of sensory complexity recorded in a myxobacterial genome."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000113; ABF88204.1; -; Genomic_DNA. DR RefSeq; YP_633241.1; NC_008095.1. DR ProteinModelPortal; Q1D282; -. DR STRING; 246197.MXAN_5087; -. DR EnsemblBacteria; ABF88204; ABF88204; MXAN_5087. DR GeneID; 4102751; -. DR KEGG; mxa:MXAN_5087; -. DR PATRIC; 22652703; VBIMyxXan43560_5001. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; MXAN246197:GIWU-5051-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 218 Thiamine-phosphate synthase. FT /FTId=PRO_0000336414. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 140 142 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 143 143 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 22471 MW; 3D292D8805BA609C CRC64; MNAPSRPHLP RGPYLLCDDS VLPEISLVDK AARLVAGGAR LVQLRMKRTP IREALAATRQ VVALCRREGA LCLVNDRVDL ALLADADGVH VGDEDVPAED ARALLGPGRL VGVTVRDVVG ARAAQAAGAD YVGLGPVFPT STKQVPAPVL GLEAFASVVR DSPLPVVGIG GVGLVNIASV AAAGAHCAAV VSDALLAADI TERVRRLVEA FEQGRFGA // ID THIE_NATPD Reviewed; 214 AA. AC Q3IP34; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 62. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=NP_4054A; OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160) (Halobacterium OS pharaonis). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Natronomonas. OX NCBI_TaxID=348780; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35678 / DSM 2160; RX PubMed=16169924; DOI=10.1101/gr.3952905; RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., RA Oesterhelt D.; RT "Living with two extremes: conclusions from the genome sequence of RT Natronomonas pharaonis."; RL Genome Res. 15:1336-1343(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR936257; CAI50118.1; -; Genomic_DNA. DR RefSeq; YP_330756.1; NC_007426.1. DR ProteinModelPortal; Q3IP34; -. DR STRING; 348780.NP4054A; -. DR PRIDE; Q3IP34; -. DR EnsemblBacteria; CAI50118; CAI50118; NP_4054A. DR GeneID; 3703246; -. DR KEGG; nph:NP4054A; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; NPHA348780:GJX0-2058-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 214 Thiamine-phosphate synthase. FT /FTId=PRO_0000336439. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22083 MW; CA07FE2EB5590BA3 CRC64; MTQDFGVYLV TGAEHSAGRS TAEVVEAAIR GGVDIVQLRD KTATARERYE VGTELRTLTR DAGVPLVVND RLDLAAAIDA DGVHLGDDDL PIEVAREQLG SDAIVGRSVS TPDAAREAEQ AGADYLGVGA IYGTDSKDTD PEQSNIGLDR IRAVRDATSL PFVGIGGVTP DNAAPVVEAG ADGVAVISAI TAADDPEHAT RRLADAVEGV APNV // ID THIE_NEIG1 Reviewed; 205 AA. AC Q5F5C2; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 14-MAY-2014, entry version 62. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=NGO2007; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90615.1; -; Genomic_DNA. DR RefSeq; YP_209027.1; NC_002946.2. DR ProteinModelPortal; Q5F5C2; -. DR STRING; 242231.NGO2007; -. DR EnsemblBacteria; AAW90615; AAW90615; NGO2007. DR GeneID; 3282617; -. DR KEGG; ngo:NGO2007; -. DR PATRIC; 20337795; VBINeiGon24812_2421. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NGON242231:GI2G-1908-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_0000157028. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21839 MW; 0716637E2F6CD2A9 CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALFVHP GYIASGAIFQ TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID THIE_NEIMA Reviewed; 205 AA. AC Q9JWI2; A1IPJ0; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 14-MAY-2014, entry version 82. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=NMA0363; OS Neisseria meningitidis serogroup A / serotype 4A (strain Z2491). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122587; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Z2491; RX PubMed=10761919; DOI=10.1038/35006655; RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., RA Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., RA Jagels K., Leather S., Moule S., Mungall K.L., Quail M.A., RA Rajandream M.A., Rutherford K.M., Simmonds M., Skelton J., RA Whitehead S., Spratt B.G., Barrell B.G.; RT "Complete DNA sequence of a serogroup A strain of Neisseria RT meningitidis Z2491."; RL Nature 404:502-506(2000). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL157959; CAM07659.1; -; Genomic_DNA. DR PIR; E82032; E82032. DR RefSeq; YP_002341872.1; NC_003116.1. DR ProteinModelPortal; Q9JWI2; -. DR STRING; 122587.NMA0363; -. DR EnsemblBacteria; CAM07659; CAM07659; NMA0363. DR GeneID; 906366; -. DR KEGG; nma:NMA0363; -. DR PATRIC; 20361400; VBINeiMen132687_0422. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IVAGAKH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NMEN122587:GI3Q-348-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_0000157029. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21702 MW; 8FF53D111925A2EC CRC64; MTFLPLKSPL KFYAVVPTAD WVERMVEAGA DTVQLRCKAL HGDELKREIA RCVAACQGSH TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYIASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTKAA NPEAVVKAFQ ALWDG // ID THIE_NEIMB Reviewed; 205 AA. AC Q9JXF7; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 14-MAY-2014, entry version 82. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=NMB2069; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42388.1; -; Genomic_DNA. DR PIR; A81011; A81011. DR RefSeq; NP_275059.1; NC_003112.2. DR ProteinModelPortal; Q9JXF7; -. DR STRING; 122586.NMB2069; -. DR EnsemblBacteria; AAF42388; AAF42388; NMB2069. DR GeneID; 904001; -. DR KEGG; nme:NMB2069; -. DR PATRIC; 20360298; VBINeiMen85645_2649. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NMEN122586:GHGG-2132-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_0000157030. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21605 MW; 7DAC8AFBD9AD2D26 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKAL HGDELKREIA RCAAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYIASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID THIE_NITEC Reviewed; 212 AA. AC Q0AFV0; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Neut_1538; OS Nitrosomonas eutropha (strain C91). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=335283; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C91; RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x; RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., RA Wei X.; RT "Whole-genome analysis of the ammonia-oxidizing bacterium, RT Nitrosomonas eutropha C91: implications for niche adaptation."; RL Environ. Microbiol. 9:2993-3007(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000450; ABI59782.1; -; Genomic_DNA. DR RefSeq; YP_747747.1; NC_008344.1. DR ProteinModelPortal; Q0AFV0; -. DR STRING; 335283.Neut_1538; -. DR EnsemblBacteria; ABI59782; ABI59782; Neut_1538. DR GeneID; 4273619; -. DR KEGG; net:Neut_1538; -. DR PATRIC; 22720472; VBINitEut7577_1893. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NEUT335283:GHT6-1567-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_0000336416. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23225 MW; 2F932E118AA235ED CRC64; MIDPPMDRIK VSGLYAITPD IENIDRLCEM AYHVLAGGVS WLQYRNKKAN SRLRLMQALE IHLLCKQFQV PLIINDHMDL VMEIDAEGLH VGGEDTSVAA ARHYLGRNKI IGVSCYNQLS HAIEAEKAGA DYVAFGAFYP SMTKVDAYQA PIHLLDAAKK TLNIPIVAIG GINLDNAEAL IARGCDAVAV SQALFSAQDI QSAARHFSKL FC // ID THIE_NITEU Reviewed; 214 AA. AC Q82UQ7; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 69. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=NE1424; OS Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=228410; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19718 / NBRC 14298; RX PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003; RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.; RT "Complete genome sequence of the ammonia-oxidizing bacterium and RT obligate chemolithoautotroph Nitrosomonas europaea."; RL J. Bacteriol. 185:2759-2773(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL954747; CAD85335.1; -; Genomic_DNA. DR RefSeq; NP_841465.1; NC_004757.1. DR ProteinModelPortal; Q82UQ7; -. DR STRING; 228410.NE1424; -. DR EnsemblBacteria; CAD85335; CAD85335; NE1424. DR GeneID; 1082374; -. DR KEGG; neu:NE1424; -. DR PATRIC; 22714017; VBINitEur56163_1602. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NEUR228410:GJNO-1454-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 214 Thiamine-phosphate synthase. FT /FTId=PRO_0000157031. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 22715 MW; 89B41DB3856DE4FA CRC64; MVPAAEPMKQ GGVSGLYAIT PDMADTGRLC DAVRQALAGG VSWLQYRNKT ADSRLRLVQA AEIHLLCRQF QVPLIVNDHL DLAMEIDAEG LHVGGDDISP AVARCHLGQD KIIGVSCYNQ LDRAIEAEEA GADYVAFGAF YPSMTKTGTY QAPIELLTAA KKKLGIPVVA IGGIDLDNAG MLIASGCDAV AVSQALFGAQ DIQSAARYFS ELFD // ID THIE_NITMU Reviewed; 234 AA. AC Q2Y5Q6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 60. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Nmul_A2628; OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosospira. OX NCBI_TaxID=323848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25196 / NCIMB 11849; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC RT 25196."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000103; ABB75915.1; -; Genomic_DNA. DR RefSeq; YP_413307.1; NC_007614.1. DR ProteinModelPortal; Q2Y5Q6; -. DR STRING; 323848.Nmul_A2628; -. DR EnsemblBacteria; ABB75915; ABB75915; Nmul_A2628. DR GeneID; 3786331; -. DR KEGG; nmu:Nmul_A2628; -. DR PATRIC; 22729006; VBINitMul110821_3051. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NMUL323848:GKEC-2674-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 234 Thiamine-phosphate synthase. FT /FTId=PRO_0000336417. FT REGION 52 56 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 234 AA; 25453 MW; A91D202E58DEEB20 CRC64; MRTVSRNEIK RCSAAPRREI TGLYAITPDT GDTSHLVAMT WRALAGGARL VQYRSKTLNE ELHREQARSL AHLCRRFDVP LLINDHIDLA LEVGADGVHL GREDAPISQA RLKLGHEKII GISCYNELES AIEAECNGAD YVAFGAFFNS VTKTDTVPAS IDLLRQGNLE IRIPIVAIGG INSDNALELI SAGADAVAVS NALFGARDIR SEAAKFSGLF KRQSFHPSLS RTSQ // ID THIE_NITOC Reviewed; 217 AA. AC Q3JDH3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Noc_0604; OS Nitrosococcus oceani (strain ATCC 19707 / NCIMB 11848). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=323261; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19707 / NCIMB 11848; RX PubMed=16957257; DOI=10.1128/AEM.00463-06; RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., RA Poret-Peterson A.T., Vergez L.M., Ward B.B.; RT "Complete genome sequence of the marine, chemolithoautotrophic, RT ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707."; RL Appl. Environ. Microbiol. 72:6299-6315(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000127; ABA57123.1; -; Genomic_DNA. DR RefSeq; YP_342653.1; NC_007484.1. DR ProteinModelPortal; Q3JDH3; -. DR STRING; 323261.Noc_0604; -. DR EnsemblBacteria; ABA57123; ABA57123; Noc_0604. DR GeneID; 3706836; -. DR KEGG; noc:Noc_0604; -. DR PATRIC; 22705006; VBINitOce57959_0744. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NOCE323261:GCI3-611-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_0000336415. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 23327 MW; F171BA2D2D007049 CRC64; MSSSIRGLYA IADTHLLPRQ DLGNAVALAL QGGASLIQYR DKSQEITRRY KEAESLQRIC HQYQAPLIIN DDALLAAEIG AEGVHLGQDD SSITSARKIL GAKAIIGISC YNDLARAIAA EQAGADYVAF GRLFPSITKP EPIWASLALL REARKNLNLP IVAIGGITPE NALQVIEAGA SAVAVIGGLF KSRDIRAAAA AYRQHFPSWN LPKPRLF // ID THIE_NOCFA Reviewed; 232 AA. AC Q5YNP9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 14-MAY-2014, entry version 68. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=NFA_53400; OS Nocardia farcinica (strain IFM 10152). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Nocardia. OX NCBI_TaxID=247156; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IFM 10152; RX PubMed=15466710; DOI=10.1073/pnas.0406410101; RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K., RA Shiba T., Hattori M.; RT "The complete genomic sequence of Nocardia farcinica IFM 10152."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006618; BAD60192.1; -; Genomic_DNA. DR RefSeq; YP_121556.1; NC_006361.1. DR ProteinModelPortal; Q5YNP9; -. DR STRING; 247156.nfa53400; -. DR EnsemblBacteria; BAD60192; BAD60192; NFA_53400. DR GeneID; 3111587; -. DR KEGG; nfa:nfa53400; -. DR PATRIC; 22740285; VBINocFar94200_5361. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; HRFYFIT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NFAR247156:GJ9T-5411-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 232 Thiamine-phosphate synthase. FT /FTId=PRO_1000008157. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 157 159 THZ-P binding (By similarity). FT METAL 92 92 Magnesium (By similarity). FT METAL 111 111 Magnesium (By similarity). FT BINDING 91 91 HMP-PP (By similarity). FT BINDING 130 130 HMP-PP (By similarity). FT BINDING 160 160 HMP-PP (By similarity). FT BINDING 188 188 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 232 AA; 24610 MW; 6CC715F9607613D3 CRC64; MHPSHPKRPL PPRDRLATAR LYLCTDARRE KGDLAKFAEA AFAGGVDIIQ LRDKGSPGEA KFGPLEAKAE LGALAELKAV ARRHGGLVAV NDRADIALAA GADVLHLGQG DLPPWYARRI VGPDVVIGRS THNRAQAGLA AIDEHIDYFC TGPVWSTPTK PGRQAAGLDL VRSTADSHPT RPWFAIGGID LERLPELLAA GADRIVVVRA ITEARDPEAA ARALKSALLA AS // ID THIE_NOSP7 Reviewed; 351 AA. AC B2J6F7; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Npun_R3982; OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=63737; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29133 / PCC 73102; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Meeks J.C., Elhai J., Campbell E.L., Thiel T., Longmire J., Potts M., RA Atlas R.; RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001037; ACC82362.1; -; Genomic_DNA. DR RefSeq; YP_001867305.1; NC_010628.1. DR ProteinModelPortal; B2J6F7; -. DR STRING; 63737.Npun_R3982; -. DR PRIDE; B2J6F7; -. DR EnsemblBacteria; ACC82362; ACC82362; Npun_R3982. DR GeneID; 6253327; -. DR KEGG; npu:Npun_R3982; -. DR PATRIC; 22761028; VBINosPun48114_4673. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NPUN63737:GJNP-3851-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 351 Thiamine-phosphate synthase. FT /FTId=PRO_1000142060. FT REGION 1 129 Unknown. FT REGION 130 351 Thiamine-phosphate synthase. FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 351 AA; 39527 MW; DFA77413E32FED9A CRC64; MVEPYSQKEQ VQQVVYRILD ANLDRAREGL RIIEEWCRFG LNNAQLALEC KRLRQELAKW HTPELRAARD TPGDPGTELT HPQEEERASI KSVLQANFCR VEEALRVLEE YSKLYQPNIA KACKQMRYQV YTLESNLMGH QRHQLLWRSR LYLVTSPSEN LLNNVEAALK GGLTLLQYRD KTADDSLRLE QARKLRQLCH IYGALFIVND RVDLALAVDA DGVHLGQQDM PIAIARQLLG SQRLIGLSTT NKEEMQAAIA EGVDYIGVGP VYETPTKVGK AATGLEYVSY AAKNCSIPWF AIGGIDANNI NDAIDAGAKR VAVVRSLMQA EQPTLVTQYL LSQLNRIKPE L // ID THIE_NOSS1 Reviewed; 351 AA. AC Q8YX72; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 14-MAY-2014, entry version 78. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=alr1343; OS Nostoc sp. (strain PCC 7120 / UTEX 2576). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=103690; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7120 / UTEX 2576; RX PubMed=11759840; DOI=10.1093/dnares/8.5.205; RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., RA Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M., RA Yasuda M., Tabata S.; RT "Complete genomic sequence of the filamentous nitrogen-fixing RT cyanobacterium Anabaena sp. strain PCC 7120."; RL DNA Res. 8:205-213(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAB73300.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000019; BAB73300.1; ALT_INIT; Genomic_DNA. DR PIR; AD1974; AD1974. DR RefSeq; NP_485386.1; NC_003272.1. DR ProteinModelPortal; Q8YX72; -. DR STRING; 103690.alr1343; -. DR PRIDE; Q8YX72; -. DR EnsemblBacteria; BAB73300; BAB73300; BAB73300. DR GeneID; 1104938; -. DR KEGG; ana:alr1343; -. DR PATRIC; 22772658; VBINosSp37423_1812. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; NFNRARE; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 351 Thiamine-phosphate synthase. FT /FTId=PRO_0000157078. FT REGION 1 129 Unknown. FT REGION 130 351 Thiamine-phosphate synthase. FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 351 AA; 39251 MW; 8F2A372F5F947546 CRC64; MVEPYSQQKQ IQQVVYRILD ANLDRAREGL RIIEEWCRFG LNSGQLAGEC KYLRQEVAVW HTEELRAARD TAGDPGTDLS HPQEEQRSSI KALLQANFCR VEEALRVLEE YGKLYHPKMG QACKQMRYRV YSLETNLMGH QRHQLLRRSR LYLVTSPSES LLPTVEAALK GGLTLLQYRD KDTDDFVRLE LATKLRQLCH SYGALFIIND RVDLALAVDA DGVHLGQQDM PIATARQLLG PQRLIGRSTT NADEMQKAIA EGADYIGVGP VYETPTKIGK AAAGLGYVSY AAQHSSVPWF AIGGIDANNI NDVIDAGAER VAVVRSLMQA EQPTLVTQYL ISQLNRIKPE S // ID THIE_OCEIH Reviewed; 206 AA. AC Q8ESZ3; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 78. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=OB0472; OS Oceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / OS HTE831). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Oceanobacillus. OX NCBI_TaxID=221109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831; RX PubMed=12235376; DOI=10.1093/nar/gkf526; RA Takami H., Takaki Y., Uchiyama I.; RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya RT Ridge and its unexpected adaptive capabilities to extreme RT environments."; RL Nucleic Acids Res. 30:3927-3935(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000028; BAC12428.1; -; Genomic_DNA. DR RefSeq; NP_691393.1; NC_004193.1. DR ProteinModelPortal; Q8ESZ3; -. DR STRING; 221109.OB0472; -. DR EnsemblBacteria; BAC12428; BAC12428; BAC12428. DR GeneID; 1015743; -. DR KEGG; oih:OB0472; -. DR PATRIC; 22791863; VBIOceIhe82024_0485. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; OIHE221109:GI2A-519-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 206 Thiamine-phosphate synthase. FT /FTId=PRO_0000157032. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT REGION 190 191 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 170 170 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22735 MW; FC1404CBB1CE90FF CRC64; MKFDKHMLRK YFIMGSQNCH RDPREILKEA ASAGITAFQY REKGKNSLTG TAKVELAKDL KAICHDFQIP FIINDDVDLA KQLDADGIHI GQDDQPVEVV RKQFPNKIIG LSISTNNELN QSPLDLVDYI GVGPIFDTNT KEDAKTAVGL EWIQSLKKQH PSLPLVAIGG INTTNAQEII QAGADGVSFI SAITETDHIL QAVQRL // ID THIE_PASMU Reviewed; 221 AA. AC P57930; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 1. DT 14-MAY-2014, entry version 89. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PM1260; OS Pasteurella multocida (strain Pm70). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=272843; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pm70; RX PubMed=11248100; DOI=10.1073/pnas.051634598; RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.; RT "Complete genomic sequence of Pasteurella multocida Pm70."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004439; AAK03344.1; -; Genomic_DNA. DR RefSeq; NP_246197.1; NC_002663.1. DR ProteinModelPortal; P57930; -. DR STRING; 272843.PM1260; -. DR EnsemblBacteria; AAK03344; AAK03344; PM1260. DR GeneID; 1244607; -. DR KEGG; pmu:PM1260; -. DR PATRIC; 22871771; VBIPasMul88067_1270. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMUL272843:GC8W-1310-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 221 Thiamine-phosphate synthase. FT /FTId=PRO_0000157033. FT REGION 46 50 HMP-PP binding (By similarity). FT REGION 148 150 THZ-P binding (By similarity). FT REGION 200 201 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 151 151 HMP-PP (By similarity). FT BINDING 180 180 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 221 AA; 23736 MW; 2207E7ECF5E62134 CRC64; MKPVHAFMRL YFIAGTQDCL HLDGDPAQNL LNILQQALQS GITCYQFREK GKKALQDPDK IKALAIQCRD LCRQYQVPFV VNDDVQLAID IGADGIHVGQ TDMAVADVAA LCHSHCFIGT SVNTLEQGIA AQANPLIDYF GTGPIFPTQS KEDPKPVVGV DFVSTIRAHG IDKPIVAIGG VTTQTAEELR RRGANGVAVI SAITQSADIA KTVKELLGNA Q // ID THIE_PEDPA Reviewed; 216 AA. AC Q03GM4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 52. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PEPE_0560; OS Pediococcus pentosaceus (strain ATCC 25745 / 183-1w). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=278197; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25745 / 183-1w; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., RA Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., RA Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., RA Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J., RA Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., RA Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., RA Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., RA Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., RA Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., RA Weimer B.C., Mills D.A.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000422; ABJ67648.1; -; Genomic_DNA. DR RefSeq; YP_804090.1; NC_008525.1. DR ProteinModelPortal; Q03GM4; -. DR STRING; 278197.PEPE_0560; -. DR EnsemblBacteria; ABJ67648; ABJ67648; PEPE_0560. DR GeneID; 4418250; -. DR KEGG; ppe:PEPE_0560; -. DR PATRIC; 22874478; VBIPedPen34213_0551. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MLARYFI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPEN278197:GI4Y-560-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 216 Thiamine-phosphate synthase. FT /FTId=PRO_1000008158. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 143 145 THZ-P binding (By similarity). FT REGION 194 195 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 146 146 HMP-PP (By similarity). FT BINDING 174 174 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23326 MW; EA0646A1A861583F CRC64; MKFNSDMLKI YFVAGTQDVA NKADFLPKVE EILQAGATAF QLREKGYNSI DNPAELTELA EKCHQLTQKY HVPLFIDDDV DLALAIHAEG IHVGQKDEKI ESVLKRVQGS MIVGLSCNTE AQVKQANQLD GIDYLGTGTV FETTSKADAG AALGVAKLQE LVELSHYPIV AIGGITLDNL PQTMATGVKG FAAISMFTQM TAVPTQMQKI KAIVKG // ID THIE_PELLD Reviewed; 212 AA. AC Q3B4B1; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Plut_0958; OS Pelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM OS 273)). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Pelodictyon. OX NCBI_TaxID=319225; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 273; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Pelodictyon luteolum DSM 273."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000096; ABB23820.1; -; Genomic_DNA. DR RefSeq; YP_374863.1; NC_007512.1. DR ProteinModelPortal; Q3B4B1; -. DR STRING; 319225.Plut_0958; -. DR EnsemblBacteria; ABB23820; ABB23820; Plut_0958. DR GeneID; 3745370; -. DR KEGG; plt:Plut_0958; -. DR PATRIC; 21379484; VBIChlLut1287_1007. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PLUT319225:GHDM-964-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_1000075572. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 21895 MW; 35005D33524422DC CRC64; MNSPHSPILC VITDEDTSPL DMVPRALRGG ANMIQLRRKT ASGRELCRLA EALIPFCRQA GALFIINDRA DIALATDADG VHLGQDDLPV AAARQLFGPG KIIGASTSSV DEALKAERNG ADYAGFGHIF PTGSKAKGYK PLGPEAISLA AAALRIPLIA IGGITRENAG PLISRGAAGI AVISAVTKAE SPEEAARSLM AIMNTTRAGE GT // ID THIE_PELTS Reviewed; 218 AA. AC A5D4K4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PTH_0643; OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Pelotomaculum. OX NCBI_TaxID=370438; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13744 / JCM 10971 / SI; RX PubMed=18218977; DOI=10.1101/gr.7136508; RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.; RT "The genome of Pelotomaculum thermopropionicum reveals niche- RT associated evolution in anaerobic microbiota."; RL Genome Res. 18:442-448(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009389; BAF58824.1; -; Genomic_DNA. DR RefSeq; YP_001211193.1; NC_009454.1. DR ProteinModelPortal; A5D4K4; -. DR STRING; 370438.PTH_0643; -. DR EnsemblBacteria; BAF58824; BAF58824; PTH_0643. DR GeneID; 5138434; -. DR KEGG; pth:PTH_0643; -. DR PATRIC; 22908214; VBIPelThe8413_0729. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PTHE370438:GCGQ-661-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 218 Thiamine-phosphate synthase. FT /FTId=PRO_0000336418. FT REGION 45 49 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 78 78 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 77 77 HMP-PP (By similarity). FT BINDING 116 116 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 24015 MW; B7D02E8F24CFA7E8 CRC64; MVRRRGLSGL LEADIYGITA WEYSLGRSNI EVVAQMIEAG IKVIQYREKE RPARQKYEEC LKIREMTREA GVTFIVNDHV DLALLVDADG VHLGQDDLPA DRVRELVGDK MIIGLSTHSP AQARAAEKMG VDYIGVGPIF ATKTKKDVCD PVGLEYLEFV VKNISLPFVA IGGIKEHNIA EVSSRGAKCI ALVTEIVGAE DIKAKVRALR AIISRKED // ID THIE_PELUB Reviewed; 207 AA. AC Q4FN35; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SAR11_0583; OS Pelagibacter ubique (strain HTCC1062). OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=335992; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC1062; RX PubMed=16109880; DOI=10.1126/science.1114057; RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., RA Baptista D., Bibbs L., Eads J., Richardson T.H., Noordewier M., RA Rappe M.S., Short J.M., Carrington J.C., Mathur E.J.; RT "Genome streamlining in a cosmopolitan oceanic bacterium."; RL Science 309:1242-1245(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000084; AAZ21404.1; -; Genomic_DNA. DR RefSeq; YP_266007.1; NC_007205.1. DR ProteinModelPortal; Q4FN35; -. DR STRING; 335992.SAR11_0583; -. DR EnsemblBacteria; AAZ21404; AAZ21404; SAR11_0583. DR GeneID; 3517132; -. DR KEGG; pub:SAR11_0583; -. DR PATRIC; 31990651; VBICanPel5618_0583. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CIGGINE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPEL335992:GH3Z-596-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000117300. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 138 140 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 141 141 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 23506 MW; 764CBC8AA43DD44D CRC64; MKQNKINKKF VYLISPNKIP DINFYDDLAL VLSSKKISFF QLRLKKETNL NKLIIGKKIK KICNKHKVKF LINDDPLLAK KLNADGCHLG QKDMDLIKAR KILKNKIIGV TCHNSINLAK KAINDGADYL AFGAFYATKT KTVKYRASLT VLKSIKKITS LPIVAIGGIK LSNYKKLLLN KANFLAISGY IWNNKKYKPL EAIRKLK // ID THIE_PERMH Reviewed; 209 AA. AC C0QR82; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PERMA_1410; OS Persephonella marina (strain DSM 14350 / EX-H1). OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; Persephonella. OX NCBI_TaxID=123214; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14350 / EX-H1; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the RT Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001230; ACO04508.1; -; Genomic_DNA. DR RefSeq; YP_002731178.1; NC_012440.1. DR ProteinModelPortal; C0QR82; -. DR STRING; 123214.PERMA_1410; -. DR PRIDE; C0QR82; -. DR EnsemblBacteria; ACO04508; ACO04508; PERMA_1410. DR GeneID; 7674707; -. DR KEGG; pmx:PERMA_1410; -. DR PATRIC; 22916273; VBIPerMar119911_1425. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR123214:GIZP-1409-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_1000202751. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 23252 MW; 3F93626506A40A3E CRC64; MERMDLSLYV ITDEKLLEGK DIYSCIEQAI SGGATVIQYR AKNKSSKKMY EEAVVIKKVC RKYDIPFIVN DRIDIAIAVD ADGVHLGQDD LDVEVARRIL GFEKIIGLST KKIEDVIKAN SLPVDYIGFG SVFPTSTKED AVYAGLEKLK EVMKISVQPV VAIGGINEKN LTDLLKTGCR NVAVVSAVFK DDNIKENTER LKNIMENFT // ID THIE_PHOLL Reviewed; 216 AA. AC Q7N964; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 14-MAY-2014, entry version 72. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=plu0485; OS Photorhabdus luminescens subsp. laumondii (strain TT01). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Photorhabdus. OX NCBI_TaxID=243265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TT01; RX PubMed=14528314; DOI=10.1038/nbt886; RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., RA Medigue C., Lanois A., Powell K., Siguier P., Vincent R., Wingate V., RA Zouine M., Glaser P., Boemare N., Danchin A., Kunst F.; RT "The genome sequence of the entomopathogenic bacterium Photorhabdus RT luminescens."; RL Nat. Biotechnol. 21:1307-1313(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571860; CAE12780.1; -; Genomic_DNA. DR RefSeq; NP_927838.1; NC_005126.1. DR ProteinModelPortal; Q7N964; -. DR STRING; 243265.plu0485; -. DR EnsemblBacteria; CAE12780; CAE12780; plu0485. DR GeneID; 2800435; -. DR KEGG; plu:plu0485; -. DR PATRIC; 20504479; VBIPhoLum48522_0525. DR GenoList; plu0485; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 216 Thiamine-phosphate synthase. FT /FTId=PRO_0000157034. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 216 AA; 23761 MW; 08E3925E9B9D267B CRC64; MNNLPNAPFA PTEHRLGLYP VVDSLAWISR LLQTGVTTIQ LRIKDLPEDQ VEEEIQQAIM LGRQYNARLF INDYWRLAIK HGAYGVHLGQ EDLVIADLNA IQKTGLRLGI STHDEQELAR AKSLRPSYIA LGHIFPTTTK AMPSSPQGVE ALKRQVENTP DYSTVAIGGI SLERVPDVIA TGVGSVALVS AITKAKDWRQ ATAQLLYLVE GIELKG // ID THIE_PICTO Reviewed; 204 AA. AC Q6KZH9; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 71. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PTO1288; OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC OS 100828). OC Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales; OC Picrophilaceae; Picrophilus. OX NCBI_TaxID=263820; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828; RX PubMed=15184674; DOI=10.1073/pnas.0401356101; RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C., RA Schepers B., Dock C., Antranikian G., Liebl W.; RT "Genome sequence of Picrophilus torridus and its implications for life RT around pH 0."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017261; AAT43873.1; -; Genomic_DNA. DR RefSeq; YP_024066.1; NC_005877.1. DR ProteinModelPortal; Q6KZH9; -. DR STRING; 263820.PTO1288; -. DR EnsemblBacteria; AAT43873; AAT43873; PTO1288. DR GeneID; 2844411; -. DR KEGG; pto:PTO1288; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HVAANIA; -. DR BioCyc; PTOR263820:GHA3-1336-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 204 Thiamine-phosphate synthase. FT /FTId=PRO_0000157072. FT REGION 34 38 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT REGION 180 181 THZ-P binding (By similarity). FT METAL 67 67 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 66 66 HMP-PP (By similarity). FT BINDING 104 104 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 160 160 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22854 MW; 8C1142BC41F1D6A1 CRC64; MKLSGLYLVT KDYYNGNFFN IVEESLSAGV NILQYRDKTN PYNIKIEAGR RLKNLAYKYN VPFIVDDSPV LLDILDADGI HIGKDDPPFE YIKERFPGKI IGVSTYGDIN LGIKYERLGA DYIAFGSFFK TSTKDDAEMC DINILNNASK FNIPVFAIGG INTRNVDELL KYKISGIAVV SAIFDAANPG EATRTFLEKL RKIL // ID THIE_PROM3 Reviewed; 353 AA. AC A2CB21; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=P9303_19391; OS Prochlorococcus marinus (strain MIT 9303). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=59922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9303; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., RA Steglich C., Church G.M., Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000554; ABM78681.1; -; Genomic_DNA. DR RefSeq; YP_001017946.1; NC_008820.1. DR ProteinModelPortal; A2CB21; -. DR STRING; 59922.P9303_19391; -. DR EnsemblBacteria; ABM78681; ABM78681; P9303_19391. DR GeneID; 4777528; -. DR KEGG; pmf:P9303_19391; -. DR PATRIC; 23001381; VBIProMar17757_1998. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR59922:GH54-2041-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 353 Thiamine-phosphate synthase. FT /FTId=PRO_1000052340. FT REGION 1 128 Unknown. FT REGION 129 353 Thiamine-phosphate synthase. FT REGION 185 189 HMP-PP binding (By similarity). FT REGION 282 284 THZ-P binding (By similarity). FT METAL 218 218 Magnesium (By similarity). FT METAL 237 237 Magnesium (By similarity). FT BINDING 217 217 HMP-PP (By similarity). FT BINDING 256 256 HMP-PP (By similarity). FT BINDING 285 285 HMP-PP (By similarity). FT BINDING 312 312 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 353 AA; 38726 MW; 3C5F36F5C32EC399 CRC64; MKSMPVAPIA DLRVAQLIDA NLDRAREGLR VVEDWCRFGL DREDLVVTLK DWRQRLGRHH HDSYKQARST ATDQGIGLSH PAQQERHEPW HVVAANCARV QEALRVLEEF ARQPDPQLAA SAAAIRYGLY DLEVTVLQAN AGKKRRQQLQ ACHLCLITTS QSDLANNDLF RTVSAALVAG IDMVQYRNKE ASDLQRLTQA KELASLCRKH GALFIVNDRI DLALAVDADG VHLGQDDLPT DVARGLIGSE RLLGRSTQFL AQLQKAEAEG CDYLGVGPVN STATKPERQP IGLAYVKEAS KATQLPWFAI GGINISNLEA VRQAGAKRIA VIGAIMNSKD PAATSLQLLE ALR // ID THIE_PROMA Reviewed; 346 AA. AC Q7VAV5; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 14-MAY-2014, entry version 70. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Pro_1348; OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=167539; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SARG / CCMP1375 / SS120; RX PubMed=12917486; DOI=10.1073/pnas.1733211100; RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., RA Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., RA Scanlan D.J., Tandeau de Marsac N., Weissenbach J., Wincker P., RA Wolf Y.I., Hess W.R.; RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, RT a nearly minimal oxyphototrophic genome."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017126; AAQ00392.1; -; Genomic_DNA. DR RefSeq; NP_875739.1; NC_005042.1. DR ProteinModelPortal; Q7VAV5; -. DR STRING; 167539.Pro1348; -. DR EnsemblBacteria; AAQ00392; AAQ00392; Pro_1348. DR GeneID; 1462729; -. DR KEGG; pma:Pro_1348; -. DR PATRIC; 23029455; VBIProMar8617_1414. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR167539:GJN2-1378-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 346 Thiamine-phosphate synthase. FT /FTId=PRO_0000157080. FT REGION 1 125 Unknown. FT REGION 126 346 Thiamine-phosphate synthase. FT REGION 177 181 HMP-PP binding (By similarity). FT REGION 274 276 THZ-P binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 346 AA; 38944 MW; 57B620FC6274564D CRC64; MSVTPNPDQH VAQLIDANLD RAREGLRVIE DWCRFSLKNK DMVITLKNWR QQLGKEHYEI YKNARSSSSD QSAGLSHPAQ KERILPQQIL SANFARIQEA LRVIEEFSRI SHPKLSKISA QIRYEIYDLE VIILKISNLN MLDEKLKSCK LCLITRTHPE LIKTVLLALK AGVTMIQYRC KETPDNQMIA EAKELASICK SYNSLFLIND RADIALAVDA DGVHLGQKDM PIQTARKIIG HQKIIGLSTH SLEEIQNATS QGCNYIGIGP IFKTKSKQND LSLGIDFFSK INLKTNLPWF AIGGINKDNI DKIKEVGIKR VAVINAIMGA EDPYLASKEL LGKLKK // ID THIE_PROMH Reviewed; 215 AA. AC B4EYU2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PMI2778; OS Proteus mirabilis (strain HI4320). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Proteus. OX NCBI_TaxID=529507; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI4320; RX PubMed=18375554; DOI=10.1128/JB.01981-07; RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N., RA Parkhill J., Mobley H.L.T.; RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master RT of both adherence and motility."; RL J. Bacteriol. 190:4027-4037(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM942759; CAR45483.1; -; Genomic_DNA. DR RefSeq; YP_002152479.1; NC_010554.1. DR ProteinModelPortal; B4EYU2; -. DR STRING; 529507.PMI2778; -. DR EnsemblBacteria; CAR45483; CAR45483; PMI2778. DR GeneID; 6803448; -. DR KEGG; pmr:PMI2778; -. DR PATRIC; 20520230; VBIProMir120933_2709. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; PMIR529507:GJIW-2833-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 215 Thiamine-phosphate synthase. FT /FTId=PRO_1000093681. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23730 MW; 25CEC84A69E37C31 CRC64; MNRSSNSAFA PTEKKLGLYP VVDSIEWVER LLKIGVTTIQ LRIKDKQPKD VEQDIITAIK LGRKYNARLF INDYWQLAIK HHAYGVHLGQ EDLDIADLDA IKQSGLCLGI STHNDTELQR AKRLLPSYIA LGHIFPTTTK DMPSKPQGLR ALKHQVEQTH DFPTVAIGGI SLEKVSDVVA TGVGGVALVS AITKASDWQQ VTLKLLELVE GKPSC // ID THIE_PROMM Reviewed; 353 AA. AC Q7V8I3; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 14-MAY-2014, entry version 70. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PMT_0363; OS Prochlorococcus marinus (strain MIT 9313). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=74547; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9313; RX PubMed=12917642; DOI=10.1038/nature01947; RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., RA Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., RA Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., RA Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A., RA Webb E.A., Zinser E.R., Chisholm S.W.; RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic RT niche differentiation."; RL Nature 424:1042-1047(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX548175; CAE20538.1; -; Genomic_DNA. DR RefSeq; NP_894196.1; NC_005071.1. DR ProteinModelPortal; Q7V8I3; -. DR STRING; 74547.PMT0363; -. DR EnsemblBacteria; CAE20538; CAE20538; PMT_0363. DR GeneID; 1728075; -. DR KEGG; pmt:PMT0363; -. DR PATRIC; 23008547; VBIProMar135351_0432. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 353 Thiamine-phosphate synthase. FT /FTId=PRO_0000157081. FT REGION 1 128 Unknown. FT REGION 129 353 Thiamine-phosphate synthase. FT REGION 185 189 HMP-PP binding (By similarity). FT REGION 282 284 THZ-P binding (By similarity). FT METAL 218 218 Magnesium (By similarity). FT METAL 237 237 Magnesium (By similarity). FT BINDING 217 217 HMP-PP (By similarity). FT BINDING 256 256 HMP-PP (By similarity). FT BINDING 285 285 HMP-PP (By similarity). FT BINDING 312 312 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 353 AA; 38986 MW; 89076DBE88D51524 CRC64; MKSMPFAPIA DLRVAQLIDA NLDRAREGLR VVEDWCRFGL DREELVMTLK DWRQRLGRHH HDSYKQARST ATDQGIGLSH PAQQERHEPW HVVAANCARV QEALRVLEEF ARQPDPQLAA SAAAIRYGLY DLEVTVLQAN AGKKRRQQLQ DCHLCLITTS QSDLNSNDLL RTVNAALVAG IDMVQYRNKE ASDLQRLTQA KELASLCRKH GALFIVNDRI DLALAVDADG VHLGQDDLPT DVARRLIGSE RLLGRSTQFL AQLQKAEAEG CDYLGVGPVN STATKPERQP IGLAYVKEAS KATQLPWFAI GGINISNLEA LRQAGAKRIA VIGAIMNSKD PAATSLQLLE ALR // ID THIE_PROMP Reviewed; 351 AA. AC Q7V0I3; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 14-MAY-2014, entry version 72. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PMM1274; OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=59919; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1986 / MED4; RX PubMed=12917642; DOI=10.1038/nature01947; RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., RA Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., RA Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., RA Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A., RA Webb E.A., Zinser E.R., Chisholm S.W.; RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic RT niche differentiation."; RL Nature 424:1042-1047(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- CAUTION: Asn-213 is present instead of the conserved Asp which is CC expected to be a metal binding residue. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX548174; CAE19733.1; -; Genomic_DNA. DR RefSeq; NP_893391.1; NC_005072.1. DR ProteinModelPortal; Q7V0I3; -. DR STRING; 59919.PMM1274; -. DR EnsemblBacteria; CAE19733; CAE19733; PMM1274. DR GeneID; 1726932; -. DR KEGG; pmm:PMM1274; -. DR PATRIC; 23033606; VBIProMar68066_1460. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR59919:GJMQ-1309-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 351 Thiamine-phosphate synthase. FT /FTId=PRO_0000157082. FT REGION 1 128 Unknown. FT REGION 129 351 Thiamine-phosphate synthase. FT REGION 180 184 HMP-PP binding (By similarity). FT REGION 277 279 THZ-P binding (By similarity). FT REGION 327 328 THZ-P binding (By similarity). FT METAL 213 213 Magnesium (By similarity). FT METAL 232 232 Magnesium (By similarity). FT BINDING 212 212 HMP-PP (By similarity). FT BINDING 251 251 HMP-PP (By similarity). FT BINDING 280 280 HMP-PP (By similarity). FT BINDING 307 307 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 351 AA; 39600 MW; F9DA4CEEFA3502B4 CRC64; MKNPNIIQPE DLRISQIIDA NLDRAREGLR VLEDWARFGL GNEDFVIRIK NFRQILGKNH LEIYKLSRNH IEDQCKGLSH VEQINRNSSS KIISSNSARV QEALRVIEEF SRIHNSKLSK IASEIRYEIY TLEIEILNFN TRKRAQSIIS KNNLYSITDP RENLLEIIEK ILLGGVKIIQ HRFKEGNDKD HLKEAIEINK LCKKYNSLFI VNNRLDIALA SKADGVHLGQ DDLDIKTVRK LLGASKIIGV SANNSTDINK AVKDGCDYIG VGPVFPTLTK KNKEPLGEEK IKALTKELNI PCFAIGGINK LNISSLKNHG ISKVAIVSGL LNSEDPKDEA MIIIKELSHE N // ID THIE_PROMS Reviewed; 351 AA. AC A2BSJ5; DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=A9601_14731; OS Prochlorococcus marinus (strain AS9601). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=146891; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AS9601; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., RA Steglich C., Church G.M., Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000551; ABM70756.1; -; Genomic_DNA. DR RefSeq; YP_001009863.1; NC_008816.1. DR ProteinModelPortal; A2BSJ5; -. DR STRING; 146891.A9601_14731; -. DR EnsemblBacteria; ABM70756; ABM70756; A9601_14731. DR GeneID; 4718194; -. DR KEGG; pmb:A9601_14731; -. DR PATRIC; 22984465; VBIProMar75723_1480. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMAR146891:GH90-1499-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 351 Thiamine-phosphate synthase. FT /FTId=PRO_0000415380. FT REGION 1 128 Unknown. FT REGION 129 351 Thiamine-phosphate synthase. FT REGION 180 184 HMP-PP binding (By similarity). FT REGION 277 279 THZ-P binding (By similarity). FT METAL 213 213 Magnesium (By similarity). FT METAL 232 232 Magnesium (By similarity). FT BINDING 212 212 HMP-PP (By similarity). FT BINDING 251 251 HMP-PP (By similarity). FT BINDING 280 280 HMP-PP (By similarity). FT BINDING 307 307 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 351 AA; 40310 MW; 71D1ACB8A9C0EA3E CRC64; MLNSNTKDHE DLRIYQIIDA NLDRAREGLR VLEDWARFGL GKEKYVEKIK NFRQILGKNH LEVYKQSRNQ IEDNCKGLTH QEQLNRKTSE QIISSNSARV QEALRVIEEF SRLHNNELSK IASEIRYEIY TVEIDLLSFS KFKKSEKILK ENDLYVITDQ KDNLLEIIEE ILIAGVKIIQ HRFKTGTDQD HLQEAIEIKN LCKRYNSLFI VNDRLDIALA SNADGIHLGQ DDLDLKTTRK LFGYSKIIGI SANNAIDISN ALDEGCDYIG IGPVFETTTK KNKKPLGIEN IKTLTKDLNI PWFAIGGIKS NNISYLKRNG FKKVALVSEL MNSEDPKEDA MMILKELSHE N // ID THIE_PROVI Reviewed; 209 AA. AC A4SEP8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Cvib_0943; OS Prosthecochloris vibrioformis (strain DSM 265) (Chlorobium vibrioforme OS subsp. thiosulfatophilum (strain DSM 265)) (Chlorobium phaeovibrioides OS (strain DSM 265)). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290318; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 265; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., RA Schuster S.C., Bryant D.A., Richardson P.; RT "Complete sequence of Prosthecochloris vibrioformis DSM 265."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000607; ABP36957.1; -; Genomic_DNA. DR RefSeq; YP_001130459.1; NC_009337.1. DR ProteinModelPortal; A4SEP8; -. DR STRING; 290318.Cvib_0943; -. DR EnsemblBacteria; ABP36957; ABP36957; Cvib_0943. DR GeneID; 4970596; -. DR KEGG; pvi:Cvib_0943; -. DR PATRIC; 21396302; VBIChlPha132153_0996. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; CPHA290318:GHNQ-961-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_1000075573. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22334 MW; 2B37D73C382721FB CRC64; MMFPSRPMLC VITDEELPPV TFARQALWGG ATILQLRNKT ASGRDLCRWS EAILPLTRQH NALFIVNDRL DIALATGADG VHLGQDDLPA TVARKLLGPD RIIGVSTGTR EEALQAEKEG ADYVGFGHIF PTGSKDKPLP PVGTLALQDT ASLLSIPLIA IGGIQLENAR RVISCGASGI AVISAVSRHP DPRIAAEALV REMEEGMLL // ID THIE_PSE14 Reviewed; 205 AA. AC Q48DP2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PSPPH_4383; OS Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=264730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1448A / Race 6; RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005; RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., RA Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., RA Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., RA Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., RA Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., RA Mansfield J.W., Collmer A., Buell R.; RT "Whole-genome sequence analysis of Pseudomonas syringae pv. RT phaseolicola 1448A reveals divergence among pathovars in genes RT involved in virulence and transposition."; RL J. Bacteriol. 187:6488-6498(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000058; AAZ35143.1; -; Genomic_DNA. DR RefSeq; YP_276499.1; NC_005773.3. DR ProteinModelPortal; Q48DP2; -. DR STRING; 264730.PSPPH_4383; -. DR EnsemblBacteria; AAZ35143; AAZ35143; PSPPH_4383. DR GeneID; 3557718; -. DR KEGG; psp:PSPPH_4383; -. DR PATRIC; 19978253; VBIPseSyr78478_4583. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PSAV264730:GKDE-4387-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_1000008159. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 21968 MW; 8D8113EA1D6B9C94 CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKT SDESRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGSL ELAEQAKADG ATYVAFGRFF NSLTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN AQEVTRRAKA FMALL // ID THIE_PSEA7 Reviewed; 209 AA. AC A6V0D3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PSPA7_1132; OS Pseudomonas aeruginosa (strain PA7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=381754; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PA7; RA Dodson R.J., Harkins D., Paulsen I.T.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000744; ABR83884.1; -; Genomic_DNA. DR RefSeq; YP_001346518.1; NC_009656.1. DR ProteinModelPortal; A6V0D3; -. DR STRING; 381754.PSPA7_1132; -. DR EnsemblBacteria; ABR83884; ABR83884; PSPA7_1132. DR GeneID; 5359164; -. DR KEGG; pap:PSPA7_1132; -. DR PATRIC; 19824078; VBIPseAer80442_1077. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PAER381754:GHMY-1132-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_1000008160. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22039 MW; D9BAAB51F3D39FE1 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SCDQARRLRE AASLRELCER HGAQLIVNDD AELAARLGVG VHLGQTDGSL SAARALLGRQ ALVGATCHAS LELAEQAVAD GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLI AVIHALFAAA SAAEVERRAR AFSALFETA // ID THIE_PSEA8 Reviewed; 209 AA. AC B7V9E0; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PLES_09991; OS Pseudomonas aeruginosa (strain LESB58). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=557722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LESB58; RX PubMed=19047519; DOI=10.1101/gr.086082.108; RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I., RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., RA Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., RA Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L., RA Levesque R.C.; RT "Newly introduced genomic prophage islands are critical determinants RT of in vivo competitiveness in the Liverpool epidemic strain of RT Pseudomonas aeruginosa."; RL Genome Res. 19:12-23(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM209186; CAW25726.1; -; Genomic_DNA. DR RefSeq; YP_002438605.1; NC_011770.1. DR ProteinModelPortal; B7V9E0; -. DR STRING; 557722.PLES_09991; -. DR EnsemblBacteria; CAW25726; CAW25726; PLES_09991. DR GeneID; 7180123; -. DR KEGG; pag:PLES_09991; -. DR PATRIC; 19811554; VBIPseAer113719_1038. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PAER557722:GHJW-1014-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_1000117301. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22132 MW; 9895AA70DDD2DD52 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER YGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAQ LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLPLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID THIE_PSEAB Reviewed; 209 AA. AC Q02SE4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PA14_12400; OS Pseudomonas aeruginosa (strain UCBPP-PA14). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCBPP-PA14; RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90; RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., RA Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.; RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is RT combinatorial."; RL Genome Biol. 7:R90.1-R90.14(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000438; ABJ13251.1; -; Genomic_DNA. DR RefSeq; YP_789142.1; NC_008463.1. DR ProteinModelPortal; Q02SE4; -. DR STRING; 208963.PA14_12400; -. DR EnsemblBacteria; ABJ13251; ABJ13251; PA14_12400. DR GeneID; 4382006; -. DR KEGG; pau:PA14_12400; -. DR PATRIC; 19848080; VBIPseAer79785_1013. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PAER208963:GI5K-999-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_1000008161. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22200 MW; 647D8D7222003226 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER YGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAR LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID THIE_PSEAE Reviewed; 209 AA. AC Q9HX40; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 14-MAY-2014, entry version 80. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PA3976; OS Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG OS 12228). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004091; AAG07363.1; -; Genomic_DNA. DR PIR; F83149; F83149. DR RefSeq; NP_252665.1; NC_002516.2. DR ProteinModelPortal; Q9HX40; -. DR SMR; Q9HX40; 24-200. DR STRING; 208964.PA3976; -. DR DNASU; 880858; -. DR GeneID; 880858; -. DR KEGG; pae:PA3976; -. DR PATRIC; 19842623; VBIPseAer58763_4168. DR PseudoCAP; PA3976; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_0000157035. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22146 MW; 898DA261D0AFA265 CRC64; MKLRGLYAIT DSQLLDDGRL LPYVEAALRG GARLLQYRDK SSDQARRLRE AESLRELCER HGAQLIVNDD AELAARLGVG LHLGQTDGSL SAARALLGRQ AIIGATCHAQ LELAEQAVAE GASYVAFGRF FNSSTKPGAP AASVELLDQA RPRLHLPITA IGGISLDTAP GLIARGVDLV AVIHALFAAA SAAEVERRAR AFSALFEPA // ID THIE_PSEE4 Reviewed; 207 AA. AC Q1I4H6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 1. DT 14-MAY-2014, entry version 54. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PSEEN4803; OS Pseudomonas entomophila (strain L48). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=384676; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L48; RX PubMed=16699499; DOI=10.1038/nbt1212; RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C., RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., RA Wincker P., Weissenbach J., Lemaitre B., Medigue C., Boccard F.; RT "Complete genome sequence of the entomopathogenic and metabolically RT versatile soil bacterium Pseudomonas entomophila."; RL Nat. Biotechnol. 24:673-679(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT573326; CAK17460.1; -; Genomic_DNA. DR RefSeq; YP_610243.1; NC_008027.1. DR ProteinModelPortal; Q1I4H6; -. DR STRING; 384676.PSEEN4803; -. DR EnsemblBacteria; CAK17460; CAK17460; PSEEN4803. DR GeneID; 4090633; -. DR KEGG; pen:PSEEN4803; -. DR PATRIC; 19867616; VBIPseEnt83862_4605. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PENT384676:GJB8-4566-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000008162. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21789 MW; B24CF8DF8516DE73 CRC64; MTLRGLYAIT DSQLLAGRFL SHVEAALEGG VCLLQYRDKS DDAGRRLREA EGLKKLCERY GTQLIINDDA ELAARLGVGV HLGQTDGPLT PARALLGRQA IIGSTCHASL ELAEQAASEG ASYVAFGRFF NSVTKPGAPA ASLELLEQAR ARVKLPIAVI GGITLDNAAP LVAHGADLLA VIHGLFGADS AQEVTRRARA FNALFAS // ID THIE_PSEF5 Reviewed; 207 AA. AC Q4K5I7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PFL_5428; OS Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=220664; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pf-5 / ATCC BAA-477; RX PubMed=15980861; DOI=10.1038/nbt1110; RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A., RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J., RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., RA Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., RA Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., RA Pierson L.S. III, Thomashow L.S., Loper J.E.; RT "Complete genome sequence of the plant commensal Pseudomonas RT fluorescens Pf-5."; RL Nat. Biotechnol. 23:873-878(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000076; AAY94638.1; -; Genomic_DNA. DR RefSeq; YP_262496.1; NC_004129.6. DR ProteinModelPortal; Q4K5I7; -. DR STRING; 220664.PFL_5428; -. DR EnsemblBacteria; AAY94638; AAY94638; PFL_5428. DR GeneID; 3479820; -. DR KEGG; pfl:PFL_5428; -. DR PATRIC; 19880341; VBIPseFlu72549_5541. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PFLU220664:GIX8-5465-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000008163. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22078 MW; 0350EB9055663740 CRC64; MKLRGLYAIT DSQLLAGKFL KYVEAALEGG VTLLQYRDKS DDQARRLREA ETLLALCERY KTRLIINDDA ELAARIGAGV HLGQTDGPLT PARALLGRQA IIGATCHSQL PLAEQAAKEG ASYVAFGRFF NSTTKPGAPA ASLELLDQAR ASLHLPICVI GGITLDNAAP LVNHGADLLA VVHGLFGAES AEEVTRRARA FNALFNS // ID THIE_PSEFS Reviewed; 209 AA. AC C3K2K2; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 14-MAY-2014, entry version 35. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PFLU_5400; OS Pseudomonas fluorescens (strain SBW25). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=216595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBW25; RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51; RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R., RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M., RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J., RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L., RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K., RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M., RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.; RT "Genomic and genetic analyses of diversity and plant interactions of RT Pseudomonas fluorescens."; RL Genome Biol. 10:R51.1-R51.16(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM181176; CAY52565.1; -; Genomic_DNA. DR RefSeq; YP_002874898.1; NC_012660.1. DR ProteinModelPortal; C3K2K2; -. DR STRING; 216595.PFLU5400; -. DR EnsemblBacteria; CAY52565; CAY52565; PFLU_5400. DR GeneID; 7817527; -. DR KEGG; pfs:PFLU5400; -. DR PATRIC; 19904898; VBIPseFlu98510_5521. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_1000202752. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22359 MW; 5E0C11B72B9C7500 CRC64; MKLRGLYAIT DSQLLAGKFL AYVEAALDGG VTLLQYRDKS SDEARRLREA EKLRELCSRY KTQLIINDDA ELAARLGVGV HLGQTDGPLT PARALLGSKA IIGSTCHSQI ELAEQAAKEG ASYVAFGRFF NSNTKPGAPA ATVEMLAQAR ARVQLPICVI GGITLENAEP LVAHGADLLA VVHGLFGADS TQEVTRRARA FNDLLKISV // ID THIE_PSEMY Reviewed; 209 AA. AC A4XYV5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Pmen_3773; OS Pseudomonas mendocina (strain ymp). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=399739; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ymp; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., RA Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Hersman L., Dubois J., Maurice P., RA Richardson P.; RT "Complete sequence of Pseudomonas mendocina ymp."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000680; ABP86521.1; -; Genomic_DNA. DR RefSeq; YP_001189253.1; NC_009439.1. DR ProteinModelPortal; A4XYV5; -. DR STRING; 399739.Pmen_3773; -. DR EnsemblBacteria; ABP86521; ABP86521; Pmen_3773. DR GeneID; 5105768; -. DR KEGG; pmy:Pmen_3773; -. DR PATRIC; 19914182; VBIPseMen131592_3826. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PMEN399739:GHR6-3836-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_0000336419. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 21668 MW; FA6A07698A7DF97F CRC64; MTAALRGLYA ITDTPLLAGG KLLPYAEAAL IGGARLLQYR DKSGDAVRRL DEAQALAELC QRHGATLIIN DDLELAAHLG VGLHLGQTDG SLAAARARLG ADVVIGGTCH AQLELAERAV AEGASYIAFG RFFNSNTKPG APAATVELLD QARTRFAQPI VAIGGVTLDN APGLIARGAS MVAVIHALFA ADSALEVQDR ARAFAALFD // ID THIE_PSEP1 Reviewed; 207 AA. AC A5W9G9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Pput_4659; OS Pseudomonas putida (strain F1 / ATCC 700007). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=351746; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F1 / ATCC 700007; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Parales R., RA Richardson P.; RT "Complete sequence of Pseudomonas putida F1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000712; ABQ80779.1; -; Genomic_DNA. DR RefSeq; YP_001269963.1; NC_009512.1. DR ProteinModelPortal; A5W9G9; -. DR STRING; 351746.Pput_4659; -. DR EnsemblBacteria; ABQ80779; ABQ80779; Pput_4659. DR GeneID; 5194445; -. DR KEGG; ppf:Pput_4659; -. DR PATRIC; 19925560; VBIPsePut56420_4722. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPUT351746:GI26-4750-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000008164. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21688 MW; 4F893600A265FBB4 CRC64; MKLRGLYAIT DSQLLAGRFL SHVEAALEGG VCLLQYRDKS DDAARRLREA EGLMKLCERY GTQLLINDDA ELAARLGVGV HLGQTDGPLT PARALLGRQA IIGSTCHASL ELAAQAASEG ASYVAFGRFF NSVTKPGAPA ANVGLLEQAR AQVKLPIAVI GGITLDNAAP LVAHGADLLA VIHGLFGADS AQEVTRRARA FNALFAS // ID THIE_PSEPF Reviewed; 207 AA. AC Q3K6C1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Pfl01_4946; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pf0-1; RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51; RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R., RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M., RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J., RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L., RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K., RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M., RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.; RT "Genomic and genetic analyses of diversity and plant interactions of RT Pseudomonas fluorescens."; RL Genome Biol. 10:R51.1-R51.16(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000094; ABA76683.1; -; Genomic_DNA. DR RefSeq; YP_350674.1; NC_007492.2. DR ProteinModelPortal; Q3K6C1; -. DR STRING; 205922.Pfl01_4946; -. DR EnsemblBacteria; ABA76683; ABA76683; Pfl01_4946. DR GeneID; 3714029; -. DR KEGG; pfo:Pfl01_4946; -. DR PATRIC; 19892090; VBIPseFlu44242_4960. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PFLU205922:GJBD-5025-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000008165. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22290 MW; AA58BEDCF4D9B565 CRC64; MKLRGLYAIT DSQLLAGKFL SYVEAALEGG VTLLQYRDKS SDEARRLREA EALRDLCERY KTQLIINDDA ELAARLNVGV HLGQTDGPLS PTRALLGYKA IIGSTCHAQL ELAEQAAREG ASYVAFGRFF NSNTKPGAPS CSLDLLDEAK RTLHLPICAI GGITLDNAAP LVAHGVDLLA VVHGLFGANS TAEVTRRARA FNELLKV // ID THIE_PSEPG Reviewed; 207 AA. AC B0KJV8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PputGB1_4837; OS Pseudomonas putida (strain GB-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=76869; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.; RT "Complete sequence of Pseudomonas putida GB-1."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000926; ABZ00722.1; -; Genomic_DNA. DR RefSeq; YP_001671057.1; NC_010322.1. DR ProteinModelPortal; B0KJV8; -. DR STRING; 76869.PputGB1_4837; -. DR EnsemblBacteria; ABZ00722; ABZ00722; PputGB1_4837. DR GeneID; 5872650; -. DR KEGG; ppg:PputGB1_4837; -. DR PATRIC; 19936745; VBIPsePut76638_4834. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPUT76869:GIXB-4920-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000075574. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21762 MW; FC569F62B4BE5007 CRC64; MKLRGLYAIT DSQLLAGRFL SHVEAALDGG VCLLQYRDKS DDAARRLREA EGLMKLCERY GTQLLINDDA ELAARLGVGV HLGQTDGPLT PARTLLGRQA IIGSTCHASL ELAAQAASEG ASYVAFGRFF NSVTKPGAPA ANVDLLEQAR AQVKLPIAVI GGITLDNAAP LVAHGADLLA VIHGLFGADS AQEVTRRARA FNALFAS // ID THIE_PSEPK Reviewed; 207 AA. AC Q88DP1; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 71. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PP_4783; OS Pseudomonas putida (strain KT2440). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=160488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT2440; RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x; RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M., RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F., RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., RA Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., RA Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., RA Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., RA Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., RA Fraser C.M.; RT "Complete genome sequence and comparative analysis of the RT metabolically versatile Pseudomonas putida KT2440."; RL Environ. Microbiol. 4:799-808(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015451; AAN70352.1; -; Genomic_DNA. DR RefSeq; NP_746888.1; NC_002947.3. DR ProteinModelPortal; Q88DP1; -. DR STRING; 160488.PP_4783; -. DR EnsemblBacteria; AAN70352; AAN70352; PP_4783. DR GeneID; 1042405; -. DR KEGG; ppu:PP_4783; -. DR PATRIC; 19948344; VBIPsePut30601_5102. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPUT160488:GIXO-4877-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_0000157036. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21702 MW; 9C04EE8BC9634D6D CRC64; MKLRGLYAIT DSQLLAGRFL SHVEAALEGG VCLLQYRDKT DDAARRLREA EGLMKLCERY GTQLLINDDA ELAARLGVGV HLGQTDGPLT PARALLGRQA IIGSTCHASL ELAAQAASEG ASYVAFGRFF NSVTKPGAPA ANVGLLEQAR AQVKLPIAVI GGITLDNAAP LVAHGADLLA VIHGLFGADS AQEVTRRARA FNALFAS // ID THIE_PSEPW Reviewed; 207 AA. AC B1J1Y7; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 14-MAY-2014, entry version 42. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PputW619_0637; OS Pseudomonas putida (strain W619). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=390235; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W619; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Taghavi S., Vangronsveld D., RA van der Lelie D., Richardson P.; RT "Complete sequence of Pseudomonas putida W619."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000949; ACA71142.1; -; Genomic_DNA. DR RefSeq; YP_001747511.1; NC_010501.1. DR ProteinModelPortal; B1J1Y7; -. DR STRING; 390235.PputW619_0637; -. DR EnsemblBacteria; ACA71142; ACA71142; PputW619_0637. DR GeneID; 6109546; -. DR KEGG; ppw:PputW619_0637; -. DR PATRIC; 19951005; VBIPsePut93764_0643. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPUT390235:GHHJ-639-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000093682. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21667 MW; 1012A718BFE23F7B CRC64; MKLRGLYAIT DSQLLAGRFL THVEAALEGG VRLLQYRDKS DDAARRLREA QALQKLCERY GTELVINDDA ELAARLGVGV HLGQTDGPLT PARALLGRQA IIGSTCHASL DLAAQAASEG ASYVAFGRFF NSVTKPGAPA ADVGLLAQAR GQVKLPIAVI GGITLDNAAP LVAHGADLLA VIHGLFGADS AQEVTRRARA FNALFAS // ID THIE_PSESM Reviewed; 205 AA. AC Q87VY6; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 76. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PSPTO_4799; OS Pseudomonas syringae pv. tomato (strain DC3000). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=223283; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DC3000; RX PubMed=12928499; DOI=10.1073/pnas.1731982100; RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T., RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., RA Madupu R., Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., RA Nelson W.C., Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., RA Khouri H.M., Fedorova N.B., Tran B., Russell D., Berry K.J., RA Utterback T.R., Van Aken S.E., Feldblyum T.V., D'Ascenzo M., RA Deng W.-L., Ramos A.R., Alfano J.R., Cartinhour S., Chatterjee A.K., RA Delaney T.P., Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X., RA Bender C.L., White O., Fraser C.M., Collmer A.; RT "The complete genome sequence of the Arabidopsis and tomato pathogen RT Pseudomonas syringae pv. tomato DC3000."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016853; AAO58228.1; -; Genomic_DNA. DR RefSeq; NP_794533.1; NC_004578.1. DR ProteinModelPortal; Q87VY6; -. DR STRING; 223283.PSPTO_4799; -. DR EnsemblBacteria; AAO58228; AAO58228; PSPTO_4799. DR GeneID; 1186482; -. DR KEGG; pst:PSPTO_4799; -. DR PATRIC; 20001104; VBIPseSyr93040_4910. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PSYR223283:GJIX-4865-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_0000157037. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22007 MW; A70BC30808744997 CRC64; MKLRGLYAIT DSQLLTGKFL SYVEAALDGG VTLLQYRDKT GDDSRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQTDGSLP DARALLGHKA IVGATCHGQL ELAEQAKADG ATYVAFGRFF NSQTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAET PQEVTRRAKA FMALL // ID THIE_PSEU2 Reviewed; 205 AA. AC Q4ZNA1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 1. DT 14-MAY-2014, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Psyr_4341; OS Pseudomonas syringae pv. syringae (strain B728a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=205918; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B728a; RX PubMed=16043691; DOI=10.1073/pnas.0504930102; RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A., RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S., RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M., RA Kyrpides N.C., Ivanova N., Lindow S.E.; RT "Comparison of the complete genome sequences of Pseudomonas syringae RT pv. syringae B728a and pv. tomato DC3000."; RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000075; AAY39371.1; -; Genomic_DNA. DR RefSeq; YP_237409.1; NC_007005.1. DR ProteinModelPortal; Q4ZNA1; -. DR STRING; 205918.Psyr_4341; -. DR EnsemblBacteria; AAY39371; AAY39371; Psyr_4341. DR GeneID; 3369881; -. DR KEGG; psb:Psyr_4341; -. DR PATRIC; 19989469; VBIPseSyr42314_4480. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PSYR205918:GJ94-4406-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_1000008166. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 86 86 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 205 AA; 22022 MW; A65CC800FF8B9092 CRC64; MKLRGLYAIT DSQLLSGKFL SYVEAALDGG VTLLQYRDKN SDESRRLREA TELLKLCERY KTRLIINDDA ELAARLGVGV HLGQSDGSLP DARALLGHKA IVGATCHGRV ELAEQAKADG ATYVAFGRFF NSLTKPGAPA VPLDLIAQVR ARVHLPIAVI GGITLENAPQ LVEHGADLLA VVHGLFGAEN TQEVTRRAKA FTALL // ID THIE_PSEU5 Reviewed; 213 AA. AC A4VQX9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PST_3757; OS Pseudomonas stutzeri (strain A1501). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=379731; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A1501; RA Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., RA Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., RA Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.; RT "Complete genome sequence of the metabolically versatile and root- RT associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000304; ABP81380.1; -; Genomic_DNA. DR RefSeq; YP_001174222.1; NC_009434.1. DR ProteinModelPortal; A4VQX9; -. DR STRING; 379731.PST_3757; -. DR EnsemblBacteria; ABP81380; ABP81380; PST_3757. DR GeneID; 5096718; -. DR KEGG; psa:PST_3757; -. DR PATRIC; 19968012; VBIPseStu31643_3735. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PSTU379731:GJER-3752-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000336420. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22683 MW; 99A5EB7B84E94725 CRC64; MKESSRLRGL YAITDSKLLA DGRLLPYVEA ALKGGARLLQ YRDKTSDEAR RLREADALQE LCARHGAQLI INDDAELAAR LGVGLHLGQE DGSLAAARAL LGRQAIIGAT CHAQLPLAEQ AARDGASYVA FGRFFQSHTK PGAPAANHEL LREARARIGL PIVAIGGITL DTAPSLIAEG VQMIAVIHAL FAADSAAEVE RRAQAFSQLF NTP // ID THIE_PSYWF Reviewed; 213 AA. AC A5WDP0; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PsycPRwf_0829; OS Psychrobacter sp. (strain PRwf-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=349106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRwf-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., RA Richardson P.; RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000713; ABQ93781.1; -; Genomic_DNA. DR RefSeq; YP_001279731.1; NC_009524.1. DR ProteinModelPortal; A5WDP0; -. DR STRING; 349106.PsycPRwf_0829; -. DR EnsemblBacteria; ABQ93781; ABQ93781; PsycPRwf_0829. DR GeneID; 5206590; -. DR KEGG; prw:PsycPRwf_0829; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; PPRW349106:GHZF-848-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000336421. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 142 144 THZ-P binding (By similarity). FT REGION 193 194 THZ-P binding (By similarity). FT METAL 75 75 Magnesium (By similarity). FT METAL 94 94 Magnesium (By similarity). FT BINDING 74 74 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 145 145 HMP-PP (By similarity). FT BINDING 173 173 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 22462 MW; FA1CD5EF15B4375C CRC64; MNKHNKSADA LSLYLVTDSA LCADKGLIET VLAAIDGGVT LVQLRDKHAS DEALYTTACE LKEAIAGRVP LVINDKVQIA HKAKLDGAHI GQGDLSVKQA RNILGHDAWL GLSINTLAQL QQTHHHHLDL LDYVGLGPVF ATATKQDHAE PIGLEGLSTL SKASVLPTVA IGGINHANAR QVYQTGCHGI AVVSAICAAD DPKQAAELLI AQR // ID THIE_PYRAB Reviewed; 207 AA. AC Q9UZQ5; G8ZJP4; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 14-MAY-2014, entry version 96. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PYRAB10900; ORFNames=PAB1645; OS Pyrococcus abyssi (strain GE5 / Orsay). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=272844; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GE5 / Orsay; RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x; RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., RA Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.; RT "An integrated analysis of the genome of the hyperthermophilic RT archaeon Pyrococcus abyssi."; RL Mol. Microbiol. 47:1495-1512(2003). RN [2] RP GENOME REANNOTATION. RC STRAIN=GE5 / Orsay; RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x; RA Gao J., Wang J.; RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 RT and Pyrococcus furiosus DSM 3638."; RL Curr. Microbiol. 64:118-129(2012). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ248286; CAB50001.1; -; Genomic_DNA. DR EMBL; HE613800; CCE70503.1; -; Genomic_DNA. DR PIR; D75087; D75087. DR RefSeq; NP_126770.1; NC_000868.1. DR ProteinModelPortal; Q9UZQ5; -. DR SMR; Q9UZQ5; 3-207. DR STRING; 272844.PAB1645; -. DR EnsemblBacteria; CAB50001; CAB50001; PAB1645. DR GeneID; 1496448; -. DR KEGG; pab:PAB1645; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_0000157073. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22537 MW; F53ACEEF7F8A82D4 CRC64; MGFREKLKLY VITDRRLKPE VKSVRQALEG GATSIQLRIK DASTKEMYEV GKEIRRLTQE YDALFFVDDR IDVALAVNAD GVQLGPEDMP IEVAREIAPN LIIGASVYSL EEALEAEKKG ADYLGAGSVF PTKTKRDVRV IRIEGLREIV EAVSIPVVAI GGINVENVKQ VLSAGVDGIA VVSAVMGASD VKKATEELRK IIEEVLG // ID THIE_PYRFU Reviewed; 207 AA. AC Q8U192; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 14-MAY-2014, entry version 81. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PF1334; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=186497; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=10430560; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and RT P. horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE009950; AAL81458.1; -; Genomic_DNA. DR RefSeq; NP_579063.1; NC_003413.1. DR PDB; 1XI3; X-ray; 1.70 A; A/B=2-207. DR PDBsum; 1XI3; -. DR ProteinModelPortal; Q8U192; -. DR SMR; Q8U192; 2-207. DR STRING; 186497.PF1334; -. DR PRIDE; Q8U192; -. DR EnsemblBacteria; AAL81458; AAL81458; PF1334. DR GeneID; 1469209; -. DR KEGG; pfu:PF1334; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ISTHNEE; -. DR UniPathway; UPA00060; UER00141. DR EvolutionaryTrace; Q8U192; -. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Magnesium; Metal-binding; KW Reference proteome; Thiamine biosynthesis; Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_0000157074. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). FT HELIX 3 6 FT STRAND 8 12 FT TURN 15 17 FT HELIX 20 29 FT STRAND 33 37 FT HELIX 44 60 FT STRAND 64 69 FT HELIX 71 77 FT STRAND 80 84 FT HELIX 91 97 FT STRAND 101 109 FT HELIX 110 119 FT STRAND 122 127 FT HELIX 142 152 FT STRAND 157 162 FT TURN 165 167 FT HELIX 168 172 FT TURN 173 175 FT STRAND 177 182 FT HELIX 183 186 FT STRAND 188 190 FT HELIX 191 206 SQ SEQUENCE 207 AA; 22590 MW; 7776F777009AE858 CRC64; MNLRNKLKLY VITDRRLKPE VESVREALEG GATAIQMRIK NAPTREMYEI GKTLRQLTRE YDALFFVDDR VDVALAVDAD GVQLGPEDMP IEVAKEIAPN LIIGASVYSL EEALEAEKKG ADYLGAGSVF PTKTKEDARV IGLEGLRKIV ESVKIPVVAI GGINKDNARE VLKTGVDGIA VISAVMGAED VRKATEELRK IVEEVLG // ID THIE_PYRHO Reviewed; 207 AA. AC O58878; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 14-MAY-2014, entry version 97. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PH1156; OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / OS NBRC 100139 / OT-3). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=70601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3; RX PubMed=9679194; DOI=10.1093/dnares/5.2.55; RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., RA Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., RA Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., RA Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., RA Masuchi Y., Shizuya H., Kikuchi H.; RT "Complete sequence and gene organization of the genome of a hyper- RT thermophilic archaebacterium, Pyrococcus horikoshii OT3."; RL DNA Res. 5:55-76(1998). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000001; BAA30256.1; -; Genomic_DNA. DR PIR; F71057; F71057. DR RefSeq; NP_143058.2; NC_000961.1. DR ProteinModelPortal; O58878; -. DR SMR; O58878; 2-207. DR STRING; 70601.PH1156; -. DR EnsemblBacteria; BAA30256; BAA30256; BAA30256. DR GeneID; 1443476; -. DR KEGG; pho:PH1156; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; PHOR70601:GJWR-1148-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_0000157075. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 182 183 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 22489 MW; AB89345245A3A379 CRC64; MNFKEKLKLY IITDRRLKPE IASVKQALEG GATSIQLRIK NAPTREMYEI GKEIRKLTNE YGALFFVDDR IDVALAVNAD GVQLGPDDMP IEIAREIAPN LIIGASVYSL EEALEAEMKG ADYLGAGSVF PTQTKKDVKV IGIEGLREIV NAVKIPVVAI GGINLENVRE VLLTGVDGIA VVSAVMGTED VKRATEGLRR IIEEVLG // ID THIE_RHIEC Reviewed; 204 AA. AC O34294; Q2K202; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 14-MAY-2014, entry version 85. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=RHE_PB00079; OS Rhizobium etli (strain CFN 42 / ATCC 51251). OG Plasmid p42b. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=347834; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CE3; RX PubMed=9371431; RA Miranda-Rios J., Morera C., Taboada H., Davalos A., Encarnacion S., RA Mora J., Soberon M.; RT "Expression of thiamin biosynthetic genes (thiCOGE) and production of RT symbiotic terminal oxidase cbb3 in Rhizobium etli."; RL J. Bacteriol. 179:6887-6893(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFN 42 / ATCC 51251; RX PubMed=16505379; DOI=10.1073/pnas.0508502103; RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., RA Jimenez-Jacinto V., Collado-Vides J., Davila G.; RT "The partitioned Rhizobium etli genome: genetic and metabolic RT redundancy in seven interacting replicons."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF004408; AAC45975.1; -; Genomic_DNA. DR EMBL; CP000135; ABC93121.1; -; Genomic_DNA. DR PIR; T44257; T44257. DR RefSeq; YP_471848.1; NC_007763.1. DR ProteinModelPortal; O34294; -. DR STRING; 347834.RHE_PB00079; -. DR EnsemblBacteria; ABC93121; ABC93121; RHE_PB00079. DR GeneID; 3895021; -. DR KEGG; ret:RHE_PB00079; -. DR PATRIC; 23090560; VBIRhiEtl108884_4911. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QWIEVTR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; RETL347834:GJJ0-6078-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Plasmid; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 204 Thiamine-phosphate synthase. FT /FTId=PRO_0000157038. FT REGION 28 32 HMP-PP binding (By similarity). FT REGION 177 178 THZ-P binding (By similarity). FT COMPBIAS 46 54 Poly-Ala. FT METAL 61 61 Magnesium (By similarity). FT METAL 80 80 Magnesium (By similarity). FT BINDING 60 60 HMP-PP (By similarity). FT BINDING 99 99 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22488 MW; 81BA95165880628A CRC64; MRLDPFYLIV DSADWVERLV PLGVKLVQLR IKDRPEPVLR EEIRRAKAAC AAAACQLIIN DYWRLAIDEG CDFIHLGQED LMAADLAAIR RAGLKLGLST HDPSELETAL AAAPDYVALG PVWPTILKEM KWAPQGVERL ADWRRRVGPM PLVAIGGITA ERAPLVLENG ADSAAVVTDI TRNPDPEART RQWLAATAPW RSVG // ID THIE_RHOBA Reviewed; 375 AA. AC Q7UQH1; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=RB6331; OS Rhodopirellula baltica (strain SH1). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Rhodopirellula. OX NCBI_TaxID=243090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH1; RX PubMed=12835416; DOI=10.1073/pnas.1431443100; RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., RA Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., RA Schlesner H., Amann R., Reinhardt R.; RT "Complete genome sequence of the marine planctomycete Pirellula sp. RT strain 1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX294143; CAD74732.1; -; Genomic_DNA. DR RefSeq; NP_867187.1; NC_005027.1. DR ProteinModelPortal; Q7UQH1; -. DR STRING; 243090.RB6331; -. DR EnsemblBacteria; CAD74732; CAD74732; RB6331. DR GeneID; 1792452; -. DR KEGG; rba:RB6331; -. DR PATRIC; 23247553; VBIRhoBal59814_3052. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 375 Thiamine-phosphate synthase. FT /FTId=PRO_0000157083. FT REGION 1 127 Unknown. FT REGION 128 375 Thiamine-phosphate synthase. FT REGION 183 185 HMP-PP binding (By similarity). FT METAL 216 216 Magnesium (By similarity). FT METAL 235 235 Magnesium (By similarity). FT BINDING 215 215 HMP-PP (By similarity). FT BINDING 254 254 HMP-PP (By similarity). FT BINDING 283 283 HMP-PP (By similarity). FT BINDING 315 315 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 375 AA; 40704 MW; 140DC875C253AB92 CRC64; MTNAESRTVL RILDANANRA GEGLRTLEES ARFILNDLSL TERLKTHRHD LAVAMRRWNR FQLIGSRDTP GDVGTGVQTA SEQSRADLSS VIAAATTRTQ QALRCLEEYG KTADSEFAAC IESIRYQCYA TFRELELKMA GLNARSRKLV EARLYALIAC EPNADYLKAR IAELVDAGVD VIQLRDSSVD DRTLFEQAKL GAAIAAERDV LWIINDRADI AVASGADGVH VGQEELPVDA VREVVGPERL IGLSTHSIEQ VRLATRTTAN YIGCGPTFPG KTKSFDRYPG CEFLTQVSDA ERSGELTLPA FAIGGIGLGN VEQVAQSGIG RVAVTGALAP HDGLHQTAMG MREILERVPL RITPDSSDVC PLPND // ID THIE_RHOCS Reviewed; 207 AA. AC B6INN5; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=RC1_1824; OS Rhodospirillum centenum (strain ATCC 51521 / SW). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=414684; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51521 / SW; RA Touchman J.W., Bauer C., Blankenship R.E.; RT "Genome sequence of Rhodospirillum centenum."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000613; ACI99219.1; -; Genomic_DNA. DR RefSeq; YP_002298032.1; NC_011420.2. DR ProteinModelPortal; B6INN5; -. DR STRING; 414684.RC1_1824; -. DR EnsemblBacteria; ACI99219; ACI99219; RC1_1824. DR GeneID; 7006591; -. DR KEGG; rce:RC1_1824; -. DR PATRIC; 23318840; VBIRhoCen1465_1759. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PEILTIW; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RCEN414684:GHCM-1803-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000117302. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 107 107 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 164 164 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21998 MW; CEB4E1649A5C10C5 CRC64; MTDCRLYLIT PPAFDPQAFA PTLAAALDAG DVACVQLRLK DAPDEAILRA VEVLRPLVQA RDVAFILNDR PDLAARSGCD GVHVGQEDTP YREARRLVGA DAIVGVTCHD SRHLAMVAGE EGADYVAFGA FFPTGTKEPK TTADPEILTW WQEMMEVPCV AIGGITVETA PLLVQAGADF LAVCGGVWNH PAGPAAAVAD FNRVMRG // ID THIE_RHOFD Reviewed; 219 AA. AC Q21VL5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 14-MAY-2014, entry version 56. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Rfer_2471; OS Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Albidiferax. OX NCBI_TaxID=338969; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15236 / ATCC BAA-621 / T118; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM RT 15236."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000267; ABD70188.1; -; Genomic_DNA. DR RefSeq; YP_523719.1; NC_007908.1. DR ProteinModelPortal; Q21VL5; -. DR STRING; 338969.Rfer_2471; -. DR EnsemblBacteria; ABD70188; ABD70188; Rfer_2471. DR GeneID; 3960286; -. DR KEGG; rfr:Rfer_2471; -. DR PATRIC; 23237639; VBIRhoFer131161_2822. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; AFER338969:GHU9-2499-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 219 Thiamine-phosphate synthase. FT /FTId=PRO_0000336422. FT REGION 48 52 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT REGION 196 197 THZ-P binding (By similarity). FT METAL 81 81 Magnesium (By similarity). FT METAL 100 100 Magnesium (By similarity). FT BINDING 80 80 HMP-PP (By similarity). FT BINDING 119 119 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 219 AA; 23091 MW; C32F26590507C3A5 CRC64; MVGASTLAHD VRLQALRLYL VTDQFCAGGR TLADVVAAAV QGGVTCVQLR EKQLNTRDFL AQALALKDLL APHGIPLVIN DRIDVALACG AQGVHLGQSD MPVTQARRLL PPEVFIGWSV ETLEDVARSA ELPVDYLGVS PIFATPTKTD TLPPWGLEGL RQVRRATTVP LVAIGGIHVG NAREVLLAGA DGLAVVSALC AAQDPCVAAL RLRQLIDAV // ID THIE_ROSCS Reviewed; 228 AA. AC A7NRF7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 1. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Rcas_4121; OS Roseiflexus castenholzii (strain DSM 13941 / HLO8). OC Bacteria; Chloroflexi; Chloroflexales; Chloroflexaceae; Roseiflexus. OX NCBI_TaxID=383372; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13941 / HLO8; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., RA Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Hanada S., RA Tsukatani Y., Richardson P.; RT "Complete sequence of Roseiflexus castenholzii DSM 13941."; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000804; ABU60153.1; -; Genomic_DNA. DR RefSeq; YP_001434171.1; NC_009767.1. DR ProteinModelPortal; A7NRF7; -. DR STRING; 383372.Rcas_4121; -. DR EnsemblBacteria; ABU60153; ABU60153; Rcas_4121. DR GeneID; 5541632; -. DR KEGG; rca:Rcas_4121; -. DR PATRIC; 23347112; VBIRosCas91182_4591. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RCAS383372:GH89-4176-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 228 Thiamine-phosphate synthase. FT /FTId=PRO_0000336423. FT REGION 57 61 HMP-PP binding (By similarity). FT REGION 154 156 THZ-P binding (By similarity). FT REGION 205 206 THZ-P binding (By similarity). FT METAL 90 90 Magnesium (By similarity). FT METAL 109 109 Magnesium (By similarity). FT BINDING 89 89 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 HMP-PP (By similarity). FT BINDING 185 185 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 228 AA; 23171 MW; 4EBB8CF54A071043 CRC64; MAWSTLVDPS PSVLTNPIPF PSGRGIVYVI TDRRAAGERS LIDIVHAALR GGANAIQLRD KDVPARAMIA LGEALLPLTR AAGVPLIVND RVDVALALDA DGVHVGQDDI PADMVRRIIG PARILGVSVA TVEQAQQAAR DGATYVSVGD LFGTPSKPDA GPPIGLTPLT EIARAVDLPV LGIGGITVAN AASVVRAGAV GVAVISAVIG APDPEAATRA LCDVAAQR // ID THIE_ROSS1 Reviewed; 236 AA. AC A5UUL3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=RoseRS_1927; OS Roseiflexus sp. (strain RS-1). OC Bacteria; Chloroflexi; Chloroflexales; Chloroflexaceae; Roseiflexus. OX NCBI_TaxID=357808; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RS-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Bryant D.A., Richardson P.; RT "Complete sequence of Roseiflexus sp. RS-1."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000686; ABQ90316.1; -; Genomic_DNA. DR RefSeq; YP_001276266.1; NC_009523.1. DR ProteinModelPortal; A5UUL3; -. DR STRING; 357808.RoseRS_1927; -. DR EnsemblBacteria; ABQ90316; ABQ90316; RoseRS_1927. DR GeneID; 5208888; -. DR KEGG; rrs:RoseRS_1927; -. DR PATRIC; 23352144; VBIRosSp109359_2125. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; RSP357808:GH5Z-1955-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 236 Thiamine-phosphate synthase. FT /FTId=PRO_0000336424. FT REGION 57 61 HMP-PP binding (By similarity). FT REGION 154 156 THZ-P binding (By similarity). FT REGION 205 206 THZ-P binding (By similarity). FT METAL 90 90 Magnesium (By similarity). FT METAL 109 109 Magnesium (By similarity). FT BINDING 89 89 HMP-PP (By similarity). FT BINDING 128 128 HMP-PP (By similarity). FT BINDING 157 157 HMP-PP (By similarity). FT BINDING 185 185 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 236 AA; 24047 MW; B9B8710E39446ABA CRC64; MVLSTLIEPL PSVQSDPIPF PSGGGIVYVI TDRRAAGERA LTDIVSAALR GGAHVIQLRD KDVPARDMVA LGQALLPLTR DAGVPLIVND RVDVALALDA DGVHVGQDDI PAEMVRRIIG PERILGVSVA TVEQAQRAMD AGATYVSVGD LFGTPSKPDA GPPIGLEPLA EIARTVNLPV LGIGGINLAN AASVIRAGAV GVAVISAVIG APDPEAATRA LHAVIASALD ERARAG // ID THIE_SACD2 Reviewed; 217 AA. AC Q21MI9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Sde_0828; OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Saccharophagus. OX NCBI_TaxID=203122; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2-40 / ATCC 43961 / DSM 17024; RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087; RA Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M., RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., RA Lamed R., Richardson P.M., Borovok I., Hutcheson S.; RT "Complete genome sequence of the complex carbohydrate-degrading marine RT bacterium, Saccharophagus degradans strain 2-40 T."; RL PLoS Genet. 4:E1000087-E1000087(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000282; ABD80090.1; -; Genomic_DNA. DR RefSeq; YP_526302.1; NC_007912.1. DR ProteinModelPortal; Q21MI9; -. DR STRING; 203122.Sde_0828; -. DR EnsemblBacteria; ABD80090; ABD80090; Sde_0828. DR GeneID; 3967726; -. DR KEGG; sde:Sde_0828; -. DR PATRIC; 23400415; VBISacDeg56404_0911. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SDEG203122:GI2M-833-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 217 Thiamine-phosphate synthase. FT /FTId=PRO_0000336425. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 217 AA; 22930 MW; F2C370172D9B4C6B CRC64; MPHNKHTVYA ITDATLMPTT ASLCHRVELA LRSGVTWLQY RDKSSNTSKR SEQAQALKAL CQTYNAKLII NDDTALAKQV GADGVHLGQT DGCIVSAREL LGPQAIIGST CHASLELAER ALAQGSSYVA FGRFFASNTK PNAAPAQLSL LAHAQQKFTC PIVAIGGITP SNGAQLLHAG ATTLAVCHSL FADDNVEYRA KCLLGLTPNA EDALVTS // ID THIE_SACEN Reviewed; 223 AA. AC A4F727; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SACE_0505; OS Saccharopolyspora erythraea (strain NRRL 23338). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharopolyspora. OX NCBI_TaxID=405948; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL 23338; RX PubMed=17369815; DOI=10.1038/nbt1297; RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., RA Dickens S., Haydock S.F., Leadlay P.F.; RT "Complete genome sequence of the erythromycin-producing bacterium RT Saccharopolyspora erythraea NRRL23338."; RL Nat. Biotechnol. 25:447-453(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM420293; CAL99851.1; -; Genomic_DNA. DR RefSeq; YP_001102777.1; NC_009142.1. DR ProteinModelPortal; A4F727; -. DR STRING; 405948.SACE_0505; -. DR EnsemblBacteria; CAL99851; CAL99851; SACE_0505. DR GeneID; 4940371; -. DR KEGG; sen:SACE_0505; -. DR PATRIC; 23408388; VBISacEry28377_0514. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 223 Thiamine-phosphate synthase. FT /FTId=PRO_1000008167. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 150 152 THZ-P binding (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT BINDING 84 84 HMP-PP (By similarity). FT BINDING 123 123 HMP-PP (By similarity). FT BINDING 153 153 HMP-PP (By similarity). FT BINDING 182 182 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23581 MW; AF55067072FB1440 CRC64; MPGLDGFGIR ARLEEALLYL CTDARTERGD LAEFADAALD GGVDIIQLRD KSAGGAPLEA RHELAALEVL AEACVRHGAL LAVNDRADVA MAADADVLHL GQDDLPVELA RRIVGDQVVV GRSTHDVVQA DSAATEQGVD YFCTGPVWTT PTKPGREAAG LELVRHTAEH RGHGRPWFAI GGIGMDNIDE VVQAGARRVV VVRAITEAED PRAAAAALRT KLG // ID THIE_SALA4 Reviewed; 211 AA. AC B5F1H6; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SeAg_B4406; OS Salmonella agona (strain SL483). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=454166; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SL483; RA Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., RA Leclerc J., Cebula T., Sebastian Y.; RT "Complete genome of Salmonella agona strain SL483."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001138; ACH50920.1; -; Genomic_DNA. DR RefSeq; YP_002149071.1; NC_011149.1. DR ProteinModelPortal; B5F1H6; -. DR STRING; 454166.SeAg_B4406; -. DR EnsemblBacteria; ACH50920; ACH50920; SeAg_B4406. DR PATRIC; 18487026; VBISalEnt65316_4263. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT454166:GHBA-4372-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000093683. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22925 MW; 62F1334ED6435438 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVES DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSVAVVSAIT QAADWREATA QLLAIAGVGD E // ID THIE_SALAI Reviewed; 208 AA. AC A8M4E6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Sare_4280; OS Salinispora arenicola (strain CNS-205). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Salinispora. OX NCBI_TaxID=391037; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNS-205; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., RA Penn K., Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.; RT "Complete sequence of Salinispora arenicola CNS-205."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000850; ABW00062.1; -; Genomic_DNA. DR RefSeq; YP_001539052.1; NC_009953.1. DR ProteinModelPortal; A8M4E6; -. DR STRING; 391037.Sare_4280; -. DR EnsemblBacteria; ABW00062; ABW00062; Sare_4280. DR GeneID; 5706992; -. DR KEGG; saq:Sare_4280; -. DR PATRIC; 23437145; VBISalAre38676_4321. DR eggNOG; NOG133055; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AICHAED; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SARE391037:GH66-4330-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 208 Thiamine-phosphate synthase. FT /FTId=PRO_0000336427. FT REGION 37 39 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 20611 MW; 0A8E1C9F42908852 CRC64; MSSLGRLHLI TDNRPGQDPL AVVRAALSVA RAELVVQVRV TDETTDRQAY DLARRVTVLC ARYGATCLVN DRLHVALAVG ADGGHVGADD LPVGAARAVL GSAAVLGATA READTAVEAV AAGASYLGVG SVHPTTSKDG LPPPIGAAGL RAVAAAVSVP VIAIGGVTAA DVPDLRAAGA YGVAVIAALS HAADPARATA AFVEALTC // ID THIE_SALAR Reviewed; 211 AA. AC A9MHD7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SARI_03495; OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=41514; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980; RG The Salmonella enterica serovar Arizonae Genome Sequencing Project; RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., RA Nash W., Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000880; ABX23320.1; -; Genomic_DNA. DR ProteinModelPortal; A9MHD7; -. DR STRING; 41514.SARI_03495; -. DR EnsemblBacteria; ABX23320; ABX23320; SARI_03495. DR PATRIC; 18475973; VBISalEnt13497_3322. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT882884:GJ8H-3491-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000075575. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22829 MW; 5F460978D5F7D1F9 CRC64; MYQPDFPPVP LRLGLYPVVD SVAWIECLLA AGVRTIQLRI KDKRDAEVEA DVVAAITLGR RYDARLFVND YWRLAIKHQA YGVHLGQEDL KTTDLNAIRT AGLRLGVSTH DDMEIDIALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHIERLADYP TVAIGGISLK RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLAIAGVGD E // ID THIE_SALCH Reviewed; 211 AA. AC Q57H62; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SCH_4044; OS Salmonella choleraesuis (strain SC-B67). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=321314; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC-B67; RX PubMed=15781495; DOI=10.1093/nar/gki297; RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., RA Wang H.-S., Lee Y.-S.; RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a RT highly invasive and resistant zoonotic pathogen."; RL Nucleic Acids Res. 33:1690-1698(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017220; AAX67950.1; -; Genomic_DNA. DR RefSeq; YP_219031.1; NC_006905.1. DR ProteinModelPortal; Q57H62; -. DR STRING; 321314.SC4044; -. DR EnsemblBacteria; AAX67950; AAX67950; SCH_4044. DR PATRIC; 32329481; VBISalEnt136302_4658. DR eggNOG; COG0352; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT321314:GJCS-4234-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000008168. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22950 MW; 088AE10486472682 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE VGVRTIQLRI KDKRNEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSVAVVSAIT QAADWREATA QLLAIVGVGD E // ID THIE_SALDC Reviewed; 211 AA. AC B5FQK8; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SeD_A4569; OS Salmonella dublin (strain CT_02021853). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=439851; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT_02021853; RA Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., RA Leclerc J., Cebula T., Sebastian Y.; RT "Complete genome of Salmonella dublin strain CT_02021853."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001144; ACH77093.1; -; Genomic_DNA. DR RefSeq; YP_002218079.1; NC_011205.1. DR ProteinModelPortal; B5FQK8; -. DR STRING; 439851.SeD_A4569; -. DR EnsemblBacteria; ACH77093; ACH77093; SeD_A4569. DR PATRIC; 18497182; VBISalEnt111443_4469. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT439851:GH2Z-4513-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000093684. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22898 MW; B8C829313371011C CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RATAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID THIE_SALEP Reviewed; 211 AA. AC B5QYE8; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 40. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SEN3949; OS Salmonella enteritidis PT4 (strain P125109). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=550537; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P125109; RX PubMed=18583645; DOI=10.1101/gr.077404.108; RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T., RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., RA Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., RA Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., RA Parkhill J.; RT "Comparative genome analysis of Salmonella enteritidis PT4 and RT Salmonella gallinarum 287/91 provides insights into evolutionary and RT host adaptation pathways."; RL Genome Res. 18:1624-1637(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM933172; CAR35518.1; -; Genomic_DNA. DR RefSeq; YP_002245992.1; NC_011294.1. DR ProteinModelPortal; B5QYE8; -. DR STRING; 550537.SEN3949; -. DR PATRIC; 32338625; VBISalEnt14964_4032. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT550537:GJFI-4017-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000093685. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22898 MW; B8C829313371011C CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RATAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID THIE_SALG2 Reviewed; 211 AA. AC B5RFJ1; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SG3443; OS Salmonella gallinarum (strain 287/91 / NCTC 13346). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=550538; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=287/91 / NCTC 13346; RX PubMed=18583645; DOI=10.1101/gr.077404.108; RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T., RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., RA Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., RA Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., RA Parkhill J.; RT "Comparative genome analysis of Salmonella enteritidis PT4 and RT Salmonella gallinarum 287/91 provides insights into evolutionary and RT host adaptation pathways."; RL Genome Res. 18:1624-1637(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM933173; CAR39234.1; -; Genomic_DNA. DR RefSeq; YP_002228236.1; NC_011274.1. DR ProteinModelPortal; B5RFJ1; -. DR STRING; 550538.SG3443; -. DR PATRIC; 18505544; VBISalEnt1629_3653. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT550538:GJ93-3389-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000093686. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22898 MW; B8C829313371011C CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RATAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID THIE_SALHS Reviewed; 211 AA. AC B4TCT2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 38. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SeHA_C4493; OS Salmonella heidelberg (strain SL476). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=454169; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SL476; RA Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., RA Leclerc J., Cebula T., Sebastian Y.; RT "Complete genome of Salmonella heidelberg strain SL476."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001120; ACF67589.1; -; Genomic_DNA. DR RefSeq; YP_002048148.1; NC_011083.1. DR ProteinModelPortal; B4TCT2; -. DR STRING; 454169.SeHA_C4493; -. DR EnsemblBacteria; ACF67589; ACF67589; SeHA_C4493. DR PATRIC; 18516425; VBISalEnt43179_4257. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT454169:GHYG-4463-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000093687. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22950 MW; A495042EC6FEDE33 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIDRLADYP TVAIGGISVE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID THIE_SALNS Reviewed; 211 AA. AC B4T0Z5; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SNSL254_A4495; OS Salmonella newport (strain SL254). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=423368; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SL254; RA Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., RA Leclerc J., Cebula T., Sebastian Y.; RT "Complete genome of Salmonella newport strain SL254."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001113; ACF61562.1; -; Genomic_DNA. DR RefSeq; YP_002043411.1; NC_011080.1. DR ProteinModelPortal; B4T0Z5; -. DR STRING; 423368.SNSL254_A4495; -. DR EnsemblBacteria; ACF61562; ACF61562; SNSL254_A4495. DR PATRIC; 18527290; VBISalEnt114557_4476. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT423368:GHJB-4452-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000093688. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22936 MW; B72D3FAD6D6EC0DC CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIDRLADYP TVAIGGISVE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID THIE_SALPA Reviewed; 211 AA. AC Q5PKA7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 14-MAY-2014, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SPA4000; OS Salmonella paratyphi A (strain ATCC 9150 / SARB42). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=295319; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9150 / SARB42; RX PubMed=15531882; DOI=10.1038/ng1470; RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., RA Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., RA Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., RA Kohlberg S., Strong C., Du F., Carter J., Kremizki C., Layman D., RA Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., RA Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., RA Spieth J., Wilson R.K.; RT "Comparison of genome degradation in Paratyphi A and Typhi, human- RT restricted serovars of Salmonella enterica that cause typhoid."; RL Nat. Genet. 36:1268-1274(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000026; AAV79752.1; -; Genomic_DNA. DR RefSeq; YP_153064.1; NC_006511.1. DR ProteinModelPortal; Q5PKA7; -. DR STRING; 295319.SPA4000; -. DR EnsemblBacteria; AAV79752; AAV79752; SPA4000. DR PATRIC; 32357773; VBISalEnt134188_4242. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT295319:GJBZ-3995-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000008169. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23021 MW; F9B034AAFDD7CBE0 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAMKHNA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLV RHIERLADYP TVAIGGISLE HAPAVLATGV GSIAVVSAIT QAADWRDATA QLLAIAGVGD E // ID THIE_SALPB Reviewed; 211 AA. AC A9N0K5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SPAB_05153; OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1016998; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1250 / SPB7; RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project; RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., RA Nash W., Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000886; ABX70434.1; -; Genomic_DNA. DR RefSeq; YP_001591267.1; NC_010102.1. DR ProteinModelPortal; A9N0K5; -. DR STRING; 272994.SPAB_05153; -. DR EnsemblBacteria; ABX70434; ABX70434; SPAB_05153. DR PATRIC; 18536725; VBISalEnt120821_4167. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT28901:GH9O-5142-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000075576. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22908 MW; 2F1618F73D71ECAD CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH NDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID THIE_SALPK Reviewed; 211 AA. AC B5BJR2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SSPA3715; OS Salmonella paratyphi A (strain AKU_12601). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=554290; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AKU_12601; RX PubMed=19159446; DOI=10.1186/1471-2164-10-36; RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., RA Bhutta Z.A., Quail M.A., Norbertczak H., Walker D., Simmonds M., RA White B., Bason N., Mungall K., Dougan G., Parkhill J.; RT "Pseudogene accumulation in the evolutionary histories of Salmonella RT enterica serovars Paratyphi A and Typhi."; RL BMC Genomics 10:36-36(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM200053; CAR61998.1; -; Genomic_DNA. DR RefSeq; YP_002144553.1; NC_011147.1. DR ProteinModelPortal; B5BJR2; -. DR STRING; 554290.SSPA3715; -. DR EnsemblBacteria; CAR61998; CAR61998; SSPA3715. DR PATRIC; 32348167; VBISalEnt134303_4247. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT554290:GJDA-4005-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000093689. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23021 MW; F9B034AAFDD7CBE0 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYDARLFIND YWRLAMKHNA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLV RHIERLADYP TVAIGGISLE HAPAVLATGV GSIAVVSAIT QAADWRDATA QLLAIAGVGD E // ID THIE_SALRD Reviewed; 227 AA. AC Q2S2A8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 14-MAY-2014, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SRU_1552; OS Salinibacter ruber (strain DSM 13855 / M31). OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Salinibacter. OX NCBI_TaxID=309807; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13855 / M31; RX PubMed=16330755; DOI=10.1073/pnas.0509073102; RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., RA Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., RA Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., RA Charlebois R.L., Legault B., Rodriguez-Valera F.; RT "The genome of Salinibacter ruber: convergence and gene exchange among RT hyperhalophilic bacteria and archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000159; ABC43834.1; -; Genomic_DNA. DR RefSeq; YP_445673.1; NC_007677.1. DR ProteinModelPortal; Q2S2A8; -. DR STRING; 309807.SRU_1552; -. DR EnsemblBacteria; ABC43834; ABC43834; SRU_1552. DR GeneID; 3851530; -. DR KEGG; sru:SRU_1552; -. DR PATRIC; 23425539; VBISalRub86502_1606. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR PhylomeDB; Q2S2A8; -. DR BioCyc; SRUB309807:GJJD-1549-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 227 Thiamine-phosphate synthase. FT /FTId=PRO_0000336426. FT REGION 50 54 HMP-PP binding (By similarity). FT REGION 147 149 THZ-P binding (By similarity). FT REGION 198 199 THZ-P binding (By similarity). FT METAL 83 83 Magnesium (By similarity). FT METAL 102 102 Magnesium (By similarity). FT BINDING 82 82 HMP-PP (By similarity). FT BINDING 121 121 HMP-PP (By similarity). FT BINDING 150 150 HMP-PP (By similarity). FT BINDING 178 178 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 227 AA; 23859 MW; E8482CC22966A42A CRC64; MENTSTNGEP ARAEKSIGRL HVLTDFHLQQ DRSHAELARL AIRGGADTIQ FRQKHGGIQN KLLEARKVAT VCADASTPLL IDDHLDIAQA TDADGVHLGQ DDFPIDAARS VLGPSPIIGG TASKPHEAAE AYEQGADYIG FGPVFPTTSK RNPKSVKGPD GLADACEAVP IPVIAIGGIT HDRVRSVLEA GAHGVAVLSA VDTARNPEQA TARFRAAIDG VLREADS // ID THIE_SALSV Reviewed; 211 AA. AC B4TQK3; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 14-MAY-2014, entry version 37. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SeSA_A4373; OS Salmonella schwarzengrund (strain CVM19633). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=439843; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CVM19633; RA Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., RA Leclerc J., Cebula T., Sebastian Y.; RT "Complete genome of Salmonella schwarzengrund strain CVM19633."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001127; ACF88670.1; -; Genomic_DNA. DR RefSeq; YP_002117064.1; NC_011094.1. DR ProteinModelPortal; B4TQK3; -. DR STRING; 439843.SeSA_A4373; -. DR EnsemblBacteria; ACF88670; ACF88670; SeSA_A4373. DR PATRIC; 32377303; VBISalEnt87589_4335. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT439843:GHHR-46-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000093690. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22997 MW; 53EBA33604968A81 CRC64; MYQPDFPTVP FRLGLYPVVD SVQWIERLLE AGVRTIQLRI KDKRDEEVEA DIIAAIALGR RYDARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLEAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPSVLATGV GSIAVVSAIT QAADWRAATA QLLDIAGVGD E // ID THIE_SALTI Reviewed; 211 AA. AC Q8Z325; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 14-MAY-2014, entry version 85. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=STY3722, t3468; OS Salmonella typhi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT18; RX PubMed=11677608; DOI=10.1038/35101607; RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., RA Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J., RA Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., RA Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., RA Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., RA Whitehead S., Barrell B.G.; RT "Complete genome sequence of a multiple drug resistant Salmonella RT enterica serovar Typhi CT18."; RL Nature 413:848-852(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700931 / Ty2; RX PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003; RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., RA Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.; RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 RT and CT18."; RL J. Bacteriol. 185:2330-2337(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL513382; CAD09481.1; -; Genomic_DNA. DR EMBL; AE014613; AAO70984.1; -; Genomic_DNA. DR RefSeq; NP_457911.1; NC_003198.1. DR RefSeq; NP_807124.1; NC_004631.1. DR ProteinModelPortal; Q8Z325; -. DR STRING; 220341.STY3722; -. DR EnsemblBacteria; AAO70984; AAO70984; t3468. DR EnsemblBacteria; CAD09481; CAD09481; CAD09481. DR GeneID; 1249978; -. DR KEGG; sty:STY3722; -. DR PATRIC; 18545580; VBISalEnt120419_3794. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000157039. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22839 MW; B535027E2F10C309 CRC64; MYQPDFPTVP FRLGLYPVVD SVAWIERLLE AGVRTIQLRI KDKRDEEVEA DVIAAIALGR CYDARLFIND YWRLAIKHNA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDIALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA RHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWRAATA QLLAIAGVGD E // ID THIE_SALTO Reviewed; 208 AA. AC A4XBL2; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 48. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Strop_3889; OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Salinispora. OX NCBI_TaxID=369723; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., RA Udwary D.W., Richardson P.; RT "Complete sequence of Salinispora tropica CNB-440."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000667; ABP56319.1; -; Genomic_DNA. DR RefSeq; YP_001160697.1; NC_009380.1. DR ProteinModelPortal; A4XBL2; -. DR STRING; 369723.Strop_3889; -. DR EnsemblBacteria; ABP56319; ABP56319; Strop_3889. DR GeneID; 5060367; -. DR KEGG; stp:Strop_3889; -. DR PATRIC; 23446972; VBISalTro43511_4014. DR eggNOG; actNOG01985; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; PRLHVIT; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; STRO369723:GI49-3938-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 208 Thiamine-phosphate synthase. FT /FTId=PRO_0000336428. FT REGION 37 39 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 208 AA; 20427 MW; 83E7E45614050890 CRC64; MSSLGRLHLI TDARAGRNPL TVVQAALSVA RTELVVQVRV ADDATDRQAY DLARRVIALC ARYDATCLVN DRLHVALAVG AAGGHVGADD LPVGAARAVL GSAAVLGVTA RDADTAVEAV AAGASYLGVG PVHPTTSKEG LPPAIGVAGV GVVAAAVSVP VIAIGAVTAA DVPVLRAAGA YGVAVIGALS HAADPAGATA ALLEALTW // ID THIE_SALTY Reviewed; 211 AA. AC Q9L9I8; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 14-MAY-2014, entry version 89. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=STM4163; ORFNames=STMF1.34; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., RA Waterston R., Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium RT LT2."; RL Nature 413:852-856(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF170176; AAF33508.1; -; Genomic_DNA. DR EMBL; AE006468; AAL22991.1; -; Genomic_DNA. DR RefSeq; NP_463032.1; NC_003197.1. DR ProteinModelPortal; Q9L9I8; -. DR STRING; 99287.STM4163; -. DR EnsemblBacteria; AAL22991; AAL22991; STM4163. DR GeneID; 1255689; -. DR KEGG; stm:STM4163; -. DR PATRIC; 32387211; VBISalEnt20916_4377. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SENT99287:GCTI-4193-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000157040. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22983 MW; 803CF861FC550D88 CRC64; MYQPDFPTVP FRLGLYPVVD SVEWIERLLE SGVRTIQLRI KDKRDEEVEA DVIAAIALGR RYNARLFIND YWRLAIKHRA YGVHLGQEDL ETTDLKAIQA AGLRLGVSTH DDMEIDVALA AKPSYIALGH VFPTQTKQMP SAPQGLAQLA SHIERLADYP TVAIGGISLE RAPAVLATGV GSIAVVSAIT QAADWREATA ELLAIAGVGD E // ID THIE_SERP5 Reviewed; 212 AA. AC A8G8F3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Spro_0283; OS Serratia proteamaculans (strain 568). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=399741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=568; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D., RA Richardson P.; RT "Complete sequence of chromosome of Serratia proteamaculans 568."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000826; ABV39393.1; -; Genomic_DNA. DR RefSeq; YP_001476521.1; NC_009832.1. DR ProteinModelPortal; A8G8F3; -. DR STRING; 399741.Spro_0283; -. DR EnsemblBacteria; ABV39393; ABV39393; Spro_0283. DR GeneID; 5607050; -. DR KEGG; spe:Spro_0283; -. DR PATRIC; 32413202; VBISerPro44537_0324. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SPRO399741:GI55-297-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_0000336429. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22793 MW; E9C00141BFA7FE01 CRC64; MTDITTPFPA TPHKLGLYPV VDSVEWIARL LDAGVTTLQL RIKDLPDEQV EDDIAAAIAL GKRYDARLFI NDYWQLAIKH GAYGVHLGQE DLDTTDLAAI HRAGLRLGVS THDDSELARA IAVKPSYIAL GHIFPTQTKD MPSAPQGLVE LKRHIAGLSD YPTVAIGGIS IDRVAAVLDC GVGSVAVVSA ITQAPDWRAA TAQLLQLIEG KE // ID THIE_SHIB3 Reviewed; 211 AA. AC B2TWI0; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 14-MAY-2014, entry version 41. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SbBS512_E4484; OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=344609; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 3083-94 / BS512; RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R., RA Jiang L., Ravel J., Sebastian Y.; RT "Complete sequence of Shigella boydii serotype 18 strain BS512."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001063; ACD07041.1; -; Genomic_DNA. DR RefSeq; YP_001882679.1; NC_010658.1. DR ProteinModelPortal; B2TWI0; -. DR SMR; B2TWI0; 10-208. DR STRING; 344609.SbBS512_E4484; -. DR EnsemblBacteria; ACD07041; ACD07041; SbBS512_E4484. DR GeneID; 6271707; -. DR KEGG; sbc:SbBS512_E4484; -. DR PATRIC; 18676394; VBIShiBoy129590_4886. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SBOY344609:GI0O-4481-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000093691. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_SHIBS Reviewed; 211 AA. AC Q31U04; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SBO_4014; OS Shigella boydii serotype 4 (strain Sb227). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300268; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sb227; RX PubMed=16275786; DOI=10.1093/nar/gki954; RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., RA Qiang B., Hou Y., Yu J., Jin Q.; RT "Genome dynamics and diversity of Shigella species, the etiologic RT agents of bacillary dysentery."; RL Nucleic Acids Res. 33:6445-6458(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000036; ABB68454.1; -; Genomic_DNA. DR RefSeq; YP_410282.1; NC_007613.1. DR ProteinModelPortal; Q31U04; -. DR STRING; 300268.SBO_4014; -. DR EnsemblBacteria; ABB68454; ABB68454; SBO_4014. DR GeneID; 3782997; -. DR KEGG; sbo:SBO_4014; -. DR PATRIC; 18687888; VBIShiBoy33460_4796. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SBOY300268:GJFL-4011-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000008170. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23055 MW; 0AF6D6D635A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVISAIT QAADWRLATA QLLEIAGVGD E // ID THIE_SHIDS Reviewed; 211 AA. AC Q32AG6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 59. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SDY_3733; OS Shigella dysenteriae serotype 1 (strain Sd197). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300267; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sd197; RX PubMed=16275786; DOI=10.1093/nar/gki954; RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., RA Qiang B., Hou Y., Yu J., Jin Q.; RT "Genome dynamics and diversity of Shigella species, the etiologic RT agents of bacillary dysentery."; RL Nucleic Acids Res. 33:6445-6458(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000034; ABB63689.1; -; Genomic_DNA. DR RefSeq; YP_405180.1; NC_007606.1. DR ProteinModelPortal; Q32AG6; -. DR STRING; 300267.SDY_3733; -. DR EnsemblBacteria; ABB63689; ABB63689; SDY_3733. DR GeneID; 3798277; -. DR KEGG; sdy:SDY_3733; -. DR PATRIC; 18698088; VBIShiDys99784_4425. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SDYS300267:GJEW-3729-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000008171. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23014 MW; BAF46224F8539C01 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLSAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAAQGLEQLA RHVERLADYP TVAIGGISLP RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_SHIF8 Reviewed; 211 AA. AC Q0SY07; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 14-MAY-2014, entry version 54. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SFV_4065; OS Shigella flexneri serotype 5b (strain 8401). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=373384; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8401; RX PubMed=16822325; DOI=10.1186/1471-2164-7-173; RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., RA Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., RA Jin Q.; RT "Complete genome sequence of Shigella flexneri 5b and comparison with RT Shigella flexneri 2a."; RL BMC Genomics 7:173-173(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000266; ABF06058.1; -; Genomic_DNA. DR RefSeq; YP_691363.1; NC_008258.1. DR ProteinModelPortal; Q0SY07; -. DR SMR; Q0SY07; 10-208. DR STRING; 373384.SFV_4065; -. DR EnsemblBacteria; ABF06058; ABF06058; SFV_4065. DR GeneID; 4209199; -. DR KEGG; sfv:SFV_4065; -. DR PATRIC; 18732367; VBIShiFle33408_4613. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SFLE373384:GHZM-4061-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000008172. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_SHIFL Reviewed; 211 AA. AC Q83PB9; Q7UBA1; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 14-MAY-2014, entry version 78. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SF4065, S3670; OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE005674; AAN45494.2; -; Genomic_DNA. DR EMBL; AE014073; AAP18707.1; -; Genomic_DNA. DR RefSeq; NP_709787.2; NC_004337.2. DR RefSeq; NP_838896.1; NC_004741.1. DR ProteinModelPortal; Q83PB9; -. DR SMR; Q83PB9; 10-208. DR STRING; 198214.SF4065; -. DR EnsemblBacteria; AAN45494; AAN45494; SF4065. DR EnsemblBacteria; AAP18707; AAP18707; S3670. DR GeneID; 1027414; -. DR GeneID; 1079890; -. DR KEGG; sfl:SF4065; -. DR KEGG; sfx:S3670; -. DR PATRIC; 18709162; VBIShiFle31049_4015. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000157041. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23041 MW; 0AE8273935A49AC0 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_SHISS Reviewed; 211 AA. AC Q3YUZ1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 60. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SSON_4166; OS Shigella sonnei (strain Ss046). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300269; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ss046; RX PubMed=16275786; DOI=10.1093/nar/gki954; RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., RA Qiang B., Hou Y., Yu J., Jin Q.; RT "Genome dynamics and diversity of Shigella species, the etiologic RT agents of bacillary dysentery."; RL Nucleic Acids Res. 33:6445-6458(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000038; AAZ90671.1; -; Genomic_DNA. DR RefSeq; YP_312906.1; NC_007384.1. DR ProteinModelPortal; Q3YUZ1; -. DR STRING; 300269.SSON_4166; -. DR EnsemblBacteria; AAZ90671; AAZ90671; SSON_4166. DR GeneID; 3669082; -. DR KEGG; ssn:SSON_4166; -. DR PATRIC; 18743329; VBIShiSon107113_4931. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; AVRPSYI; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; SSON300269:GJJF-4161-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000008173. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23040 MW; 6DF9E5BB3D8C3E64 CRC64; MYQPDFPPVP FRLGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRNEEVEA DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA QLLEIAGVGD E // ID THIE_STAA1 Reviewed; 213 AA. AC A7X4S8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SAHV_2076; OS Staphylococcus aureus (strain Mu3 / ATCC 700698). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=418127; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mu3 / ATCC 700698; RX PubMed=17954695; DOI=10.1128/AAC.00534-07; RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.; RT "Mutated response regulator graR is responsible for phenotypic RT conversion of Staphylococcus aureus from heterogeneous vancomycin- RT intermediate resistance to vancomycin-intermediate resistance."; RL Antimicrob. Agents Chemother. 52:45-53(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009324; BAF78959.1; -; Genomic_DNA. DR RefSeq; YP_001442666.1; NC_009782.1. DR ProteinModelPortal; A7X4S8; -. DR SMR; A7X4S8; 4-209. DR STRING; 418127.SAHV_2076; -. DR PRIDE; A7X4S8; -. DR EnsemblBacteria; BAF78959; BAF78959; SAHV_2076. DR GeneID; 5560378; -. DR KEGG; saw:SAHV_2076; -. DR PATRIC; 19559318; VBIStaAur127830_2134. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR418127:GJP9-2137-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_1000008174. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID THIE_STAA2 Reviewed; 213 AA. AC A6U3H7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SaurJH1_2166; OS Staphylococcus aureus (strain JH1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=359787; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JH1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Tomasz A., RA Richardson P.; RT "Complete sequence of chromosome of Staphylococcus aureus subsp. RT aureus JH1."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000736; ABR52995.1; -; Genomic_DNA. DR RefSeq; YP_001317282.1; NC_009632.1. DR ProteinModelPortal; A6U3H7; -. DR SMR; A6U3H7; 4-209. DR STRING; 359787.SaurJH1_2166; -. DR PRIDE; A6U3H7; -. DR EnsemblBacteria; ABR52995; ABR52995; SaurJH1_2166. DR GeneID; 5317007; -. DR KEGG; sah:SaurJH1_2166; -. DR PATRIC; 19536292; VBIStaAur98826_2213. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR359787:GCG4-2235-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_1000075577. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID THIE_STAA3 Reviewed; 213 AA. AC Q2FF35; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SAUSA300_2047; OS Staphylococcus aureus (strain USA300). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USA300; RX PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000255; ABD22374.1; -; Genomic_DNA. DR RefSeq; YP_494693.1; NC_007793.1. DR ProteinModelPortal; Q2FF35; -. DR SMR; Q2FF35; 4-209. DR STRING; 451515.SAUSA300_2047; -. DR PRIDE; Q2FF35; -. DR EnsemblBacteria; ABD22374; ABD22374; SAUSA300_2047. DR GeneID; 3914397; -. DR KEGG; saa:SAUSA300_2047; -. DR PATRIC; 19593601; VBIStaAur129981_2186. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR451515:GH3C-2047-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_1000008175. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID THIE_STAA8 Reviewed; 213 AA. AC Q2FWG3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 14-MAY-2014, entry version 57. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SAOUHSC_02328; OS Staphylococcus aureus (strain NCTC 8325). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=93061; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 8325; RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., RA Iandolo J.J.; RT "The Staphylococcus aureus NCTC8325 genome."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000253; ABD31362.1; -; Genomic_DNA. DR RefSeq; YP_500807.1; NC_007795.1. DR ProteinModelPortal; Q2FWG3; -. DR SMR; Q2FWG3; 4-209. DR STRING; 93061.SAOUHSC_02328; -. DR PRIDE; Q2FWG3; -. DR EnsemblBacteria; ABD31362; ABD31362; SAOUHSC_02328. DR GeneID; 3920953; -. DR KEGG; sao:SAOUHSC_02328; -. DR PATRIC; 19581985; VBIStaAur99865_2109. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR93061:GIWJ-2265-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_1000008176. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID THIE_STAA9 Reviewed; 213 AA. AC A5IUN7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 50. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SaurJH9_2128; OS Staphylococcus aureus (strain JH9). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=359786; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JH9; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Tomasz A., Richardson P.; RT "Complete sequence of chromosome of Staphylococcus aureus subsp. RT aureus JH9."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000703; ABQ49910.1; -; Genomic_DNA. DR RefSeq; YP_001247486.1; NC_009487.1. DR ProteinModelPortal; A5IUN7; -. DR SMR; A5IUN7; 4-209. DR STRING; 359786.SaurJH9_2128; -. DR PRIDE; A5IUN7; -. DR EnsemblBacteria; ABQ49910; ABQ49910; SaurJH9_2128. DR GeneID; 5169783; -. DR KEGG; saj:SaurJH9_2128; -. DR PATRIC; 19542195; VBIStaAur42398_2245. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR359786:GJEM-2202-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_1000075578. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID THIE_STAAB Reviewed; 213 AA. AC Q2YUL2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 60. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SAB1975c; OS Staphylococcus aureus (strain bovine RF122 / ET3-1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=273036; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=bovine RF122 / ET3-1; RX PubMed=17971880; DOI=10.1371/journal.pone.0001120; RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.; RT "Molecular correlates of host specialization in Staphylococcus RT aureus."; RL PLoS ONE 2:E1120-E1120(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ938182; CAI81664.1; -; Genomic_DNA. DR RefSeq; YP_417434.1; NC_007622.1. DR ProteinModelPortal; Q2YUL2; -. DR STRING; 273036.SAB1975c; -. DR EnsemblBacteria; CAI81664; CAI81664; SAB1975c. DR GeneID; 3794324; -. DR KEGG; sab:SAB1975c; -. DR PATRIC; 19524953; VBIStaAur92441_2081. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR273036:GJVS-2040-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_1000008177. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23299 MW; 1DEE5A36885AE5AE CRC64; MFNQSYLNVY FICGTSNVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYNV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLGEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID THIE_STAAC Reviewed; 213 AA. AC Q5HEA8; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 14-MAY-2014, entry version 68. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SACOL2083; OS Staphylococcus aureus (strain COL). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=93062; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COL; RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., RA Hance I.R., Nelson K.E., Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete RT genome analysis of an early methicillin-resistant Staphylococcus RT aureus strain and a biofilm-producing methicillin-resistant RT Staphylococcus epidermidis strain."; RL J. Bacteriol. 187:2426-2438(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000046; AAW37045.1; -; Genomic_DNA. DR RefSeq; YP_186899.1; NC_002951.2. DR ProteinModelPortal; Q5HEA8; -. DR SMR; Q5HEA8; 4-209. DR STRING; 93062.SACOL2083; -. DR PRIDE; Q5HEA8; -. DR EnsemblBacteria; AAW37045; AAW37045; SACOL2083. DR GeneID; 3238111; -. DR KEGG; sac:SACOL2083; -. DR PATRIC; 19530435; VBIStaAur112458_2029. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR93062:GCEP-2077-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000157042. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID THIE_STAAE Reviewed; 213 AA. AC A6QIT5; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=NWMN_1995; OS Staphylococcus aureus (strain Newman). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=426430; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Newman; RX PubMed=17951380; DOI=10.1128/JB.01000-07; RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.; RT "Genome sequence of Staphylococcus aureus strain Newman and RT comparative analysis of staphylococcal genomes: polymorphism and RT evolution of two major pathogenicity islands."; RL J. Bacteriol. 190:300-310(2008). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009351; BAF68267.1; -; Genomic_DNA. DR RefSeq; YP_001333029.1; NC_009641.1. DR ProteinModelPortal; A6QIT5; -. DR SMR; A6QIT5; 4-209. DR STRING; 426430.NWMN_1995; -. DR PRIDE; A6QIT5; -. DR EnsemblBacteria; BAF68267; BAF68267; NWMN_1995. DR GeneID; 5332232; -. DR KEGG; sae:NWMN_1995; -. DR PATRIC; 19587794; VBIStaAur133992_2182. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR426430:GIXC-2059-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_1000071284. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID THIE_STAAM Reviewed; 213 AA. AC P66918; Q99SG6; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SAV2091; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mu50 / ATCC 700699; RX PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., RA Ogasawara N., Hayashi H., Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus RT aureus."; RL Lancet 357:1225-1240(2001). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000017; BAB58253.1; -; Genomic_DNA. DR RefSeq; NP_372615.1; NC_002758.2. DR ProteinModelPortal; P66918; -. DR SMR; P66918; 4-209. DR STRING; 158878.SAV2091; -. DR PRIDE; P66918; -. DR EnsemblBacteria; BAB58253; BAB58253; SAV2091. DR GeneID; 1122108; -. DR KEGG; sav:SAV2091; -. DR PATRIC; 19565060; VBIStaAur52173_2165. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR158878:GJJ5-2151-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000157043. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID THIE_STAAN Reviewed; 213 AA. AC P66919; Q99SG6; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 68. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SA1894; OS Staphylococcus aureus (strain N315). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=158879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N315; RX PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., RA Ogasawara N., Hayashi H., Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus RT aureus."; RL Lancet 357:1225-1240(2001). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=N315; RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.; RT "Shotgun proteomic analysis of total and membrane protein extracts of RT S. aureus strain N315."; RL Submitted (OCT-2007) to UniProtKB. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000018; BAB43178.1; -; Genomic_DNA. DR PIR; A99902; A99902. DR RefSeq; NP_375199.1; NC_002745.2. DR ProteinModelPortal; P66919; -. DR SMR; P66919; 4-209. DR STRING; 158879.SA1894; -. DR PRIDE; P66919; -. DR EnsemblBacteria; BAB43178; BAB43178; BAB43178. DR GeneID; 1124795; -. DR KEGG; sau:SA1894; -. DR PATRIC; 19576244; VBIStaAur116463_2049. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR158879:GJCB-2027-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 1: Evidence at protein level; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000157044. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23399 MW; 8FEFB39D6EF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID THIE_STAAR Reviewed; 213 AA. AC Q6GEY4; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SAR2180; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=282458; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MRSA252; RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571856; CAG41160.1; -; Genomic_DNA. DR RefSeq; YP_041539.1; NC_002952.2. DR ProteinModelPortal; Q6GEY4; -. DR STRING; 282458.SAR2180; -. DR EnsemblBacteria; CAG41160; CAG41160; SAR2180. DR GeneID; 2859526; -. DR KEGG; sar:SAR2180; -. DR PATRIC; 19547997; VBIStaAur71814_2184. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR282458:GJA5-2212-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000157045. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23393 MW; 8FF4285C1CE7DE64 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GFSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHTPVG PEMIATFKEM NPQLPIVAIG GINTSNVAPI VEAGANGISV ISAISKSENI EKTVNRFKDF FNN // ID THIE_STAAS Reviewed; 213 AA. AC Q6G7L9; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SAS1995; OS Staphylococcus aureus (strain MSSA476). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=282459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSSA476; RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571857; CAG43802.1; -; Genomic_DNA. DR RefSeq; YP_044105.1; NC_002953.3. DR ProteinModelPortal; Q6G7L9; -. DR STRING; 282459.SAS1995; -. DR GeneID; 2863653; -. DR KEGG; sas:SAS1995; -. DR PATRIC; 19553599; VBIStaAur96780_2076. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000157046. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23384 MW; 8FEFB3993FF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI ENTVNRFKDF FNN // ID THIE_STAAW Reviewed; 213 AA. AC Q8NVH5; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2002, sequence version 1. DT 14-MAY-2014, entry version 76. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=MW2014; OS Staphylococcus aureus (strain MW2). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=196620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MW2; RX PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5; RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., RA Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., RA Yamamoto K., Hiramatsu K.; RT "Genome and virulence determinants of high virulence community- RT acquired MRSA."; RL Lancet 359:1819-1827(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000033; BAB95879.1; -; Genomic_DNA. DR RefSeq; NP_646831.1; NC_003923.1. DR ProteinModelPortal; Q8NVH5; -. DR STRING; 196620.MW2014; -. DR EnsemblBacteria; BAB95879; BAB95879; BAB95879. DR GeneID; 1004130; -. DR KEGG; sam:MW2014; -. DR PATRIC; 19570744; VBIStaAur44266_2090. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAUR196620:GJ9Z-2083-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000157047. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 23384 MW; 8FEFB3993FF82F94 CRC64; MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI ENTVNRFKDF FNN // ID THIE_STACT Reviewed; 212 AA. AC Q9RGS5; B9DMF5; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 14-MAY-2014, entry version 74. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Sca_1593; OS Staphylococcus carnosus (strain TM300). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=396513; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Krismer B., Goetz F.; RT "Identification of an operon involved in thiamin biosynthesis in RT Staphylococcus carnosus TM300."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TM300; RX PubMed=19060169; DOI=10.1128/AEM.01982-08; RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., RA Schuster S.C., Goetz F.; RT "Genome analysis of the meat starter culture bacterium Staphylococcus RT carnosus TM300."; RL Appl. Environ. Microbiol. 75:811-822(2009). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF109218; AAF25544.1; -; Genomic_DNA. DR EMBL; AM295250; CAL28498.1; -; Genomic_DNA. DR RefSeq; YP_002634683.1; NC_012121.1. DR ProteinModelPortal; Q9RGS5; -. DR STRING; 396513.Sca_1593; -. DR GeneID; 7550725; -. DR KEGG; sca:Sca_1593; -. DR PATRIC; 19604035; VBIStaCar105558_1590. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SCAR396513:GJ9G-1644-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_0000157050. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22993 MW; 03B94A80C2CB969A CRC64; MFQSKDLNVY FICGTQDIPE GRTIQEVLKE ALEGGITLYQ FREKGNGAKT GQDKVALAKE LQALCKSYNV PFIVNDDVAL AEEIDADGIH VGQDDEAVDD FNNRFEGKII GLSIGNLEEL NASDLTYVDY IGVGPIFATP SKDDASEPVG PKMIETLRKE VGDLPIVAIG GISLDNVQEV AKTSADGVSV ISAIARSPHV TETVHKFLQY FK // ID THIE_STAEQ Reviewed; 212 AA. AC Q5HMD0; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 2. DT 14-MAY-2014, entry version 70. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SERP1698; OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=176279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35984 / RP62A; RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., RA Hance I.R., Nelson K.E., Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete RT genome analysis of an early methicillin-resistant Staphylococcus RT aureus strain and a biofilm-producing methicillin-resistant RT Staphylococcus epidermidis strain."; RL J. Bacteriol. 187:2426-2438(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAW55076.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000029; AAW55076.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_189263.1; NC_002976.3. DR ProteinModelPortal; Q5HMD0; -. DR STRING; 176279.SERP1698; -. DR EnsemblBacteria; AAW55076; AAW55076; SERP1698. DR GeneID; 3242743; -. DR KEGG; ser:SERP1698; -. DR PATRIC; 19614319; VBIStaEpi130894_1658. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SEPI176279:GJJB-1767-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_0000157049. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23621 MW; 76A5ECC4F52118E9 CRC64; MFDSKQLSVY FICGTQDIPK NKSIEQVLKE ALEAGITLYQ FREKGPNALK GEKKKQLALK LKQLCHSYHV PMIVNDDVQL AQEINADGIH VGQDDMEIQQ FASQFKNKII GLSVGNLKEY QQSDLSKVDY IGVGPMYTTS SKDDASKPVG PSMISQLRLY IHDFPIVAIG GINETNVQPI VDEGADGISV ISAITRSTNI DKTVKYFLRY FT // ID THIE_STAES Reviewed; 212 AA. AC Q8CNK2; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 83. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SE_1690; OS Staphylococcus epidermidis (strain ATCC 12228). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=176280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12228; RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x; RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., RA Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., RA Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.; RT "Genome-based analysis of virulence genes in a non-biofilm-forming RT Staphylococcus epidermidis strain (ATCC 12228)."; RL Mol. Microbiol. 49:1577-1593(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015929; AAO05289.1; -; Genomic_DNA. DR RefSeq; NP_765245.1; NC_004461.1. DR ProteinModelPortal; Q8CNK2; -. DR STRING; 176280.SE1690; -. DR EnsemblBacteria; AAO05289; AAO05289; SE_1690. DR GeneID; 1056989; -. DR KEGG; sep:SE1690; -. DR PATRIC; 19609242; VBIStaEpi113981_1650. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SEPI176280:GCDG-1740-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_0000157048. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23621 MW; 76A5ECC4F52118E9 CRC64; MFDSKQLSVY FICGTQDIPK NKSIEQVLKE ALEAGITLYQ FREKGPNALK GEKKKQLALK LKQLCHSYHV PMIVNDDVQL AQEINADGIH VGQDDMEIQQ FASQFKNKII GLSVGNLKEY QQSDLSKVDY IGVGPMYTTS SKDDASKPVG PSMISQLRLY IHDFPIVAIG GINETNVQPI VDEGADGISV ISAITRSTNI DKTVKYFLRY FT // ID THIE_STAHJ Reviewed; 212 AA. AC Q4L7X3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SH0943; OS Staphylococcus haemolyticus (strain JCSC1435). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=279808; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC1435; RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005; RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., RA Lee J.C., Hiramatsu K.; RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the RT extreme plasticity of its genome and the evolution of human-colonizing RT staphylococcal species."; RL J. Bacteriol. 187:7292-7308(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006716; BAE04252.1; -; Genomic_DNA. DR RefSeq; YP_252858.1; NC_007168.1. DR ProteinModelPortal; Q4L7X3; -. DR STRING; 279808.SH0943; -. DR EnsemblBacteria; BAE04252; BAE04252; SH0943. DR GeneID; 3481776; -. DR KEGG; sha:SH0943; -. DR PATRIC; 19617927; VBIStaHae67511_0930. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SHAE279808:GJX7-954-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_1000008178. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23255 MW; BE29659DF38E3D76 CRC64; MFNSSSLNVY FICGTQDVPE GKDIREILKQ ALEAGITLFQ FREKGPTSLD GVEKEHLAID LLKLCHDYQV PFIVNDDVDL AEKINADGIH VGQDDENVKS FAERFKDKII GLSIGNEKEY YHSDLEHVDY IGVGPMFATI SKNDANAPVG PSMIATLKNI NPSLPMVAIG GITEDNIEPI AQNGADGVSV ISAIARSHNI DKTVTKMKSY FK // ID THIE_STAS1 Reviewed; 212 AA. AC Q49Z39; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SSP0792; OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / OS DSM 20229). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=342451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15305 / DSM 20229; RX PubMed=16135568; DOI=10.1073/pnas.0502950102; RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., RA Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., RA Hattori M., Ohta T.; RT "Whole genome sequence of Staphylococcus saprophyticus reveals the RT pathogenesis of uncomplicated urinary tract infection."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008934; BAE17937.1; -; Genomic_DNA. DR RefSeq; YP_300882.1; NC_007350.1. DR ProteinModelPortal; Q49Z39; -. DR STRING; 342451.SSP0792; -. DR EnsemblBacteria; BAE17937; BAE17937; SSP0792. DR GeneID; 3615759; -. DR KEGG; ssp:SSP0792; -. DR PATRIC; 19623086; VBIStaSap90642_0794. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; MLARYFI; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSAP342451:GKFA-804-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_1000008179. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 191 192 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 113 113 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 171 171 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 23107 MW; 1BCEAF3A9404A3B9 CRC64; MFDKNNLKLY FICGTQDIES KTTIIDVVTE ALESGITMFQ FREKGNGALI GDEKEDLARK LLALCHDYAV PFIVNDDVAL ANKIGADGIH VGQDDMDVKV FAEQFKGKII GLSISNIDEY KTSNLAHVDY IGVGPMYATT SKDDANLPVG PEMITKLRAH VNHFPIVAIG GINVENTREV MQAGADGISI ISAITKSENI SNTISQFLQN VE // ID THIE_STRA1 Reviewed; 223 AA. AC Q3K1L6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 57. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SAK_0965; OS Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC OS SS700). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=205921; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27591 / A909 / CDC SS700; RX PubMed=16172379; DOI=10.1073/pnas.0506758102; RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D., RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., RA DeBoy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., RA Peterson J.D., Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A., RA Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N., RA Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J., RA Smith S., Utterback T.R., White O., Rubens C.E., Grandi G., RA Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R., RA Fraser C.M.; RT "Genome analysis of multiple pathogenic isolates of Streptococcus RT agalactiae: implications for the microbial 'pan-genome'."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000114; ABA44825.1; -; Genomic_DNA. DR RefSeq; YP_329587.1; NC_007432.1. DR ProteinModelPortal; Q3K1L6; -. DR STRING; 205921.SAK_0965; -. DR EnsemblBacteria; ABA44825; ABA44825; SAK_0965. DR GeneID; 3686717; -. DR KEGG; sak:SAK_0965; -. DR PATRIC; 19633195; VBIStrAga82541_0907. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAGA205921:GHD7-966-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 223 Thiamine-phosphate synthase. FT /FTId=PRO_1000008180. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24635 MW; C8592610981AB9B1 CRC64; MKDTLKLYFV CGTVDCSRKN ILTVVEEALQ AGITLFQFRE KGFTALQGKE KIAMAKQLQI LCKQYQVPFI IDDDIDLVEL IDADGLHIGQ NDLPVDEARR RLPDKIIGLS VSTMDEYQKS QLSVVDYIGI GPFNPTQSKA DAKPAVGNRT TKAVREINQD IPIVAIGGIT SDFVHDIIES GADGIAVISA ISKANHIVDA TRQLRYEVEK ALVNRQKHSD VIK // ID THIE_STRA3 Reviewed; 223 AA. AC Q8E5W9; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 73. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=gbs0860; OS Streptococcus agalactiae serotype III (strain NEM316). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=211110; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NEM316; RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x; RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., RA Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., RA Kunst F.; RT "Genome sequence of Streptococcus agalactiae, a pathogen causing RT invasive neonatal disease."; RL Mol. Microbiol. 45:1499-1513(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL766847; CAD46504.1; -; Genomic_DNA. DR RefSeq; NP_735310.1; NC_004368.1. DR ProteinModelPortal; Q8E5W9; -. DR STRING; 211110.gbs0860; -. DR EnsemblBacteria; CAD46504; CAD46504; CAD46504. DR GeneID; 1029839; -. DR KEGG; san:gbs0860; -. DR PATRIC; 19637582; VBIStrAga3577_0883. DR GenoList; gbs0860; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 223 Thiamine-phosphate synthase. FT /FTId=PRO_0000157051. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24610 MW; BE824D7D2C1F1CA5 CRC64; MKDTLKLYFV CGTVDCSRKN ILTVVEEALQ AGITLFQFRE KGFTALQGKE KIAMAKQLQI LCKQYQVPFI IDDDIDLVEL IDADGLHIGQ NDLPVDEARR RLPDKIIGLS VSTMAEYQKS QLSVVDYIGI GPFNPTQSKA DAKPAVGNRT TKAVREINQD IPIVAIGGIT SDFVHDIIES GADGIAVISA ISKANHIVDA TRQLRYEVEK ALVNRQKRSD VIK // ID THIE_STRA5 Reviewed; 223 AA. AC Q8E092; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 14-MAY-2014, entry version 76. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SAG0842; OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=208435; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-611 / 2603 V/R; RX PubMed=12200547; DOI=10.1073/pnas.182380799; RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N., RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D., RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C., RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., RA Radune D., Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., RA Carty H.A., Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., RA Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D., RA Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G., RA Fraser C.M.; RT "Complete genome sequence and comparative genomic analysis of an RT emerging human pathogen, serotype V Streptococcus agalactiae."; RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE009948; AAM99729.1; -; Genomic_DNA. DR RefSeq; NP_687857.1; NC_004116.1. DR ProteinModelPortal; Q8E092; -. DR STRING; 208435.SAG0842; -. DR EnsemblBacteria; AAM99729; AAM99729; SAG0842. DR GeneID; 1013646; -. DR KEGG; sag:SAG0842; -. DR PATRIC; 19628514; VBIStrAga72745_0848. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAGA208435:GHVY-933-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 223 Thiamine-phosphate synthase. FT /FTId=PRO_0000157052. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 188 189 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 168 168 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 24635 MW; C8592610981AB9B1 CRC64; MKDTLKLYFV CGTVDCSRKN ILTVVEEALQ AGITLFQFRE KGFTALQGKE KIAMAKQLQI LCKQYQVPFI IDDDIDLVEL IDADGLHIGQ NDLPVDEARR RLPDKIIGLS VSTMDEYQKS QLSVVDYIGI GPFNPTQSKA DAKPAVGNRT TKAVREINQD IPIVAIGGIT SDFVHDIIES GADGIAVISA ISKANHIVDA TRQLRYEVEK ALVNRQKHSD VIK // ID THIE_STRAW Reviewed; 215 AA. AC Q82AF9; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 14-MAY-2014, entry version 76. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SAV_6099; OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / OS NCIMB 12804 / NRRL 8165 / MA-4680). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=227882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / RC MA-4680; RX PubMed=11572948; DOI=10.1073/pnas.211433198; RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., RA Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., RA Kikuchi H., Shiba T., Sakaki Y., Hattori M.; RT "Genome sequence of an industrial microorganism Streptomyces RT avermitilis: deducing the ability of producing secondary RT metabolites."; RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / RC MA-4680; RX PubMed=12692562; DOI=10.1038/nbt820; RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., RA Sakaki Y., Hattori M., Omura S.; RT "Complete genome sequence and comparative analysis of the industrial RT microorganism Streptomyces avermitilis."; RL Nat. Biotechnol. 21:526-531(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAC73810.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000030; BAC73810.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_827275.1; NC_003155.4. DR ProteinModelPortal; Q82AF9; -. DR STRING; 227882.SAV_6099; -. DR EnsemblBacteria; BAC73810; BAC73810; SAV_6099. DR GeneID; 1211401; -. DR KEGG; sma:SAV_6099; -. DR PATRIC; 23726230; VBIStrAve112782_6468. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SAVE227882:GJU1-6179-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 215 Thiamine-phosphate synthase. FT /FTId=PRO_0000157053. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23005 MW; AA7E7B52BD3D7A57 CRC64; MPDTARDRLA DARVYLCTDA RRRQGDLAEF LDAALAGGVD IVQLRDKGME AAEELEHLQV FADACRRHGK LLAVNDRADV AHAVDSDVLH LGQGDLPVPA ARAILGADVL IGRSTHAEAE AEAAAVQEGV DYFCTGPCWP TPTKPGRHAP GLDLVRHTAA LGTDRPWFAI GGIDLGNLDE VLEAGARRVV VVRAITEADD PKAAAEEFAK RLRHA // ID THIE_STRCO Reviewed; 223 AA. AC Q9S2V2; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 14-MAY-2014, entry version 84. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SCO2104; ORFNames=SC4A10.37c; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces; OC Streptomyces albidoflavus group. OX NCBI_TaxID=100226; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145; RX PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., RA Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., RA Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., RA Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., RA Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces RT coelicolor A3(2)."; RL Nature 417:141-147(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL939111; CAB52013.1; -; Genomic_DNA. DR PIR; T34974; T34974. DR RefSeq; NP_626363.1; NC_003888.3. DR ProteinModelPortal; Q9S2V2; -. DR STRING; 100226.SCO2104; -. DR EnsemblBacteria; CAB52013; CAB52013; CAB52013. DR GeneID; 1097538; -. DR KEGG; sco:SCO2104; -. DR PATRIC; 23733858; VBIStrCoe124346_2138. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR PhylomeDB; Q9S2V2; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 223 Thiamine-phosphate synthase. FT /FTId=PRO_0000157054. FT REGION 47 51 HMP-PP binding (By similarity). FT REGION 145 147 THZ-P binding (By similarity). FT METAL 80 80 Magnesium (By similarity). FT METAL 99 99 Magnesium (By similarity). FT BINDING 79 79 HMP-PP (By similarity). FT BINDING 118 118 HMP-PP (By similarity). FT BINDING 148 148 HMP-PP (By similarity). FT BINDING 176 176 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 223 AA; 23356 MW; 468C1FD3163723A8 CRC64; MPDTAPTAAR ARLADARLYL CTDARRSQGD LPEFLDAVLA GGVDIVQLRD KGMEAAEELE HLAVFADACA RHGKLLAVND RADVAHAARA DVLHLGQGDL PVPAARAILG DDVLIGRSTH AESEAAAAAA QEGVDYFCTG PCWPTPTKPG RHAPGLDLVR RTAALGTDRP WFAIGGIDLG NLDEVLEAGA RRVVVVRAIT AAEDPGAAAA EFARRLRQAP AHG // ID THIE_STRS2 Reviewed; 229 AA. AC A4W0K4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 14-MAY-2014, entry version 51. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SSU98_0735; OS Streptococcus suis (strain 98HAH33). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=391296; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=98HAH33; RX PubMed=17375201; DOI=10.1371/journal.pone.0000315; RA Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., RA Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., RA Ju A., Ge J., Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., RA Wang X., Gao G.F., Yang R., Wang J., Yu J.; RT "A glimpse of streptococcal toxic shock syndrome from comparative RT genomics of S. suis 2 Chinese isolates."; RL PLoS ONE 2:E315-E315(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000408; ABP91893.1; -; Genomic_DNA. DR RefSeq; YP_001200293.1; NC_009443.1. DR ProteinModelPortal; A4W0K4; -. DR STRING; 391296.SSU98_0735; -. DR EnsemblBacteria; ABP91893; ABP91893; SSU98_0735. DR GeneID; 5101885; -. DR KEGG; ssv:SSU98_0735; -. DR PATRIC; 19777709; VBIStrSui72275_0722. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSUI391296:GI2E-785-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 229 Thiamine-phosphate synthase. FT /FTId=PRO_0000336430. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 111 111 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 229 AA; 24866 MW; 13EC09C5B3734B31 CRC64; MNRKMLQVYF ICGTSDCPKG KFLDVLEKAL QAGITCFQFR EKGEQGLTGA DKLLLAKQVQ HLCHRYQVPL IINDDVELAR AIDADGIHLG QEDLSVVEAR QLFPGKIIGL SVGTKEEYLN SPIDLVDYIG SGPVFPTLSK DDASPAIGMD GLKQLRKLNS DIPMVAIGGL SAKDCKEVLQ AGADGIAVIS AISHAEDPYK ATKILVDGMQ AMILKFNQVE SNKQILKNP // ID THIE_SYNPW Reviewed; 353 AA. AC A5GMH7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 14-MAY-2014, entry version 43. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SynWH7803_1716; OS Synechococcus sp. (strain WH7803). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=32051; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH7803; RG Genoscope; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT971583; CAK24142.1; -; Genomic_DNA. DR RefSeq; YP_001225439.1; NC_009481.1. DR ProteinModelPortal; A5GMH7; -. DR STRING; 32051.SynWH7803_1716; -. DR PRIDE; A5GMH7; -. DR EnsemblBacteria; CAK24142; CAK24142; SynWH7803_1716. DR GeneID; 5146421; -. DR KEGG; syx:SynWH7803_1716; -. DR PATRIC; 23829611; VBISynSp43824_1760. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; NFNRARE; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 353 Thiamine-phosphate synthase. FT /FTId=PRO_1000052341. FT REGION 1 128 Unknown. FT REGION 129 353 Thiamine-phosphate synthase. FT REGION 185 189 HMP-PP binding (By similarity). FT REGION 282 284 THZ-P binding (By similarity). FT REGION 332 333 THZ-P binding (By similarity). FT METAL 218 218 Magnesium (By similarity). FT METAL 237 237 Magnesium (By similarity). FT BINDING 217 217 HMP-PP (By similarity). FT BINDING 256 256 HMP-PP (By similarity). FT BINDING 285 285 HMP-PP (By similarity). FT BINDING 312 312 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 353 AA; 38820 MW; 0FB296A767D93919 CRC64; MESMPVAPST DPRVARLIDA NLDRAREGLR VIEDWCRFGL DRQDLVVPLK DWRQQLGQLH HDRYRQARST ATDSAAGLGH PAQDTRTDSV AIVKANASRV QEALRVIEEF ARNGDAVLAR TAAAVRYALY DHEVRILEAC GHSRRKQQLE DARLCLITDP GADDGCERLV QRVEAALQSG VSLVQYRRKH GSDGLRLQEA QQLAQLCHEH NALFIVNDRI DLALLVNADG VHLGQEDLPY REARRLLGSA KLIGRSTHKL AQLHEAQEQG ADYVGVGPVF ATATKADRHP AGLSWVKEAC EAARIPWFAI GGITATTLPR VREAGAQRVA VVSAIMASED PASASRQLLD LLT // ID THIE_SYNPX Reviewed; 349 AA. AC Q7U5U1; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 14-MAY-2014, entry version 68. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=SYNW1604; OS Synechococcus sp. (strain WH8102). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=84588; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH8102; RX PubMed=12917641; DOI=10.1038/nature01943; RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., RA Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J., RA Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.; RT "The genome of a motile marine Synechococcus."; RL Nature 424:1037-1042(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX569693; CAE08119.1; -; Genomic_DNA. DR RefSeq; NP_897697.1; NC_005070.1. DR ProteinModelPortal; Q7U5U1; -. DR STRING; 84588.SYNW1604; -. DR EnsemblBacteria; CAE08119; CAE08119; SYNW1604. DR GeneID; 1732029; -. DR KEGG; syw:SYNW1604; -. DR PATRIC; 23834863; VBISynSp27240_1730. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 349 Thiamine-phosphate synthase. FT /FTId=PRO_0000157085. FT REGION 1 125 Unknown. FT REGION 126 349 Thiamine-phosphate synthase. FT REGION 177 181 HMP-PP binding (By similarity). FT METAL 210 210 Magnesium (By similarity). FT METAL 229 229 Magnesium (By similarity). FT BINDING 209 209 HMP-PP (By similarity). FT BINDING 248 248 HMP-PP (By similarity). FT BINDING 277 277 HMP-PP (By similarity). FT BINDING 304 304 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 349 AA; 37875 MW; 7D532A6B253CB9E4 CRC64; MGCESSLDPR VARLIDANLD RAREGLRVVE DWCRFGLERD DLVISLKDWR QRLGKLHQER YKRARSTVTD PGAGMEHPAQ LDRHSPRQVV EANCGRVQEA LRVLEEYGRN VDAPLSAEAA AIRYGLYDLE VTCLTATSGN NRRNRLQDCQ LCLITSPCPD LVDRVKTALR SGVAMVQHRC KSGSDLERLA EARTLAALCR DHGALLIIND RIDLALAVDA DGVHLGQDDL PTDVARGLIG PGRLLGRSTH SLNQVAEAHR EDCDYLGLGP VNNTAVKPER PAIGAALVGE ALAITHKPVF AIGGISQANL DALMAVGCRR VAVIGAIMGS DNPEKASQNL LSSLSRPTL // ID THIE_SYNS3 Reviewed; 353 AA. AC Q0IC17; DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot. DT 25-JAN-2012, sequence version 2. DT 14-MAY-2014, entry version 55. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=sync_0791; OS Synechococcus sp. (strain CC9311). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=64471; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC9311; RX PubMed=16938853; DOI=10.1073/pnas.0602963103; RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., RA Badger J.H., Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., RA Durkin A.S., Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., RA Halpin R., Paulsen I.T.; RT "Genome sequence of Synechococcus CC9311: insights into adaptation to RT a coastal environment."; RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=ABI45071.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000435; ABI45071.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_730005.1; NC_008319.1. DR STRING; 64471.sync_0791; -. DR EnsemblBacteria; ABI45071; ABI45071; sync_0791. DR GeneID; 4261304; -. DR KEGG; syg:sync_0791; -. DR PATRIC; 23792492; VBISynSp88089_0811. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSP64471:GIVP-791-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 353 Thiamine-phosphate synthase. FT /FTId=PRO_0000415379. FT REGION 1 128 Unknown. FT REGION 129 353 Thiamine-phosphate synthase. FT REGION 185 189 HMP-PP binding (By similarity). FT REGION 282 284 THZ-P binding (By similarity). FT METAL 218 218 Magnesium (By similarity). FT METAL 237 237 Magnesium (By similarity). FT BINDING 217 217 HMP-PP (By similarity). FT BINDING 256 256 HMP-PP (By similarity). FT BINDING 285 285 HMP-PP (By similarity). FT BINDING 312 312 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 353 AA; 39116 MW; B47DC1A90AD05BCA CRC64; MELMVVEADA KLRVARLIDA NLDRAREGLR VIEDWCRFGL DRDDLVLPLK DWRQRLGQQH HDRYRRARST ATDVAAGLGH PAQTSRCSAP AIIKANASRV QEALRVLEEF GRNLDPDLAS TAAEIRYGLY DLEVRILEAC GRQHRQERLE GAKLCLITDP DRDNNLERLL HGVEAALMAG VSLVQYRRKQ GNDKQRLLEA QALKTLCSRF EALFIVNDRI DLALLVDADG VHLGQDDLPL SEARQLLGPE RLLGRSTHRL EHLLEAQQAG ADYLGVGPVF ATKTKRDLSP AGLSWVTEAS RHAAVPWFAI GGIDIETIPS VRAAGAQRVA VVSAIMSSND PEEASRTLLQ TLA // ID THIE_SYNSC Reviewed; 352 AA. AC Q3AL68; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 14-MAY-2014, entry version 57. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Syncc9605_0896; OS Synechococcus sp. (strain CC9605). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=110662; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC9605; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Synechococcus sp. CC9605."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000110; ABB34664.1; -; Genomic_DNA. DR RefSeq; YP_381219.1; NC_007516.1. DR ProteinModelPortal; Q3AL68; -. DR STRING; 110662.Syncc9605_0896; -. DR EnsemblBacteria; ABB34664; ABB34664; Syncc9605_0896. DR GeneID; 3736365; -. DR KEGG; syd:Syncc9605_0896; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; NFNRARE; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SSP110662:GJ7R-929-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 352 Thiamine-phosphate synthase. FT /FTId=PRO_1000052342. FT REGION 1 128 Unknown. FT REGION 129 352 Thiamine-phosphate synthase. FT REGION 180 184 HMP-PP binding (By similarity). FT METAL 213 213 Magnesium (By similarity). FT METAL 232 232 Magnesium (By similarity). FT BINDING 212 212 HMP-PP (By similarity). FT BINDING 251 251 HMP-PP (By similarity). FT BINDING 280 280 HMP-PP (By similarity). FT BINDING 307 307 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 352 AA; 38642 MW; 0DAEE1F3C039B27C CRC64; MNPTPSETSL DPRVARLIDA NLDRAREGLR VVEDWCRFGL EQQDLVVRLK DWRQRLGRLH HDSYKQARST STDTGAGLKH PAQLDRHSPD RVVAANCARA QEALRVLEEY GRTIDPALAA EAAAIRYGLY DLEVTCLNAT LGARRRNKLK DACLCLITTP CDDLTDRVEA ALRNGVGMVQ YRCKAGNDRE RLQEAQQLRQ LCNKFGALLL INDRVDLALA VDADGVHLGQ EDMPSEVARD LLGVDRLLGR STHSIDQVHQ AQQEPIDYLG FGPIHSTAVK PERNPVGVEL LAKATAISQR PVFAIGGITP ANLPALLMAG GQRAAVIGAI MHSEDSGQAT RHLLQQLDQA TI // ID THIE_SYNWW Reviewed; 209 AA. AC Q0AZ86; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 14-MAY-2014, entry version 54. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Swol_0641; OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae; OC Syntrophomonas. OX NCBI_TaxID=335541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2245B / Goettingen; RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x; RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L., RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.; RT "The genome of Syntrophomonas wolfei: new insights into syntrophic RT metabolism and biohydrogen production."; RL Environ. Microbiol. 12:2289-2301(2010). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000448; ABI67968.1; -; Genomic_DNA. DR RefSeq; YP_753339.1; NC_008346.1. DR ProteinModelPortal; Q0AZ86; -. DR STRING; 335541.Swol_0641; -. DR EnsemblBacteria; ABI67968; ABI67968; Swol_0641. DR GeneID; 4281499; -. DR KEGG; swo:Swol_0641; -. DR PATRIC; 23856017; VBISynWol51738_0676. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; SWOL335541:GHL1-660-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 209 Thiamine-phosphate synthase. FT /FTId=PRO_1000057646. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 209 AA; 22766 MW; 0EC8E1C2506C5480 CRC64; MVNSDYSLYL VTDRSLLQGR SLLEEVRKAV KGGVSMVQLR EKEAGSREFY ELAQTLQTEL RELGVPLLIN DRLDIALAVD ADGLHLGQDD LPLPVARSLL GKEKIIGLSI NKREEAREGE KMGADYLGVS PVFSTPTKAD APPATGLEFL ASLRQEIKIP LVAIGGINKE NLKMIKETGA DGAAVISALM GASDIEGEAR KLRQIWERN // ID THIE_SYNY3 Reviewed; 343 AA. AC P72965; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 14-MAY-2014, entry version 95. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=sll0635; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the RT entire genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000022; BAA16983.1; -; Genomic_DNA. DR PIR; S74943; S74943. DR RefSeq; NP_440303.1; NC_000911.1. DR RefSeq; YP_005650360.1; NC_017277.1. DR RefSeq; YP_007450186.1; NC_020286.1. DR ProteinModelPortal; P72965; -. DR STRING; 1148.sll0635; -. DR PaxDb; P72965; -. DR EnsemblBacteria; BAA16983; BAA16983; BAA16983. DR GeneID; 12256049; -. DR GeneID; 14615833; -. DR GeneID; 953602; -. DR KEGG; syn:sll0635; -. DR KEGG; syy:SYNGTS_0407; -. DR KEGG; syz:MYO_14110; -. DR PATRIC; 23837742; VBISynSp132158_0441. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR PhylomeDB; P72965; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 343 Thiamine-phosphate synthase. FT /FTId=PRO_0000157086. FT REGION 1 123 Unknown. FT REGION 124 343 Thiamine-phosphate synthase. FT REGION 171 175 HMP-PP binding (By similarity). FT REGION 268 270 THZ-P binding (By similarity). FT METAL 204 204 Magnesium (By similarity). FT METAL 223 223 Magnesium (By similarity). FT BINDING 203 203 HMP-PP (By similarity). FT BINDING 242 242 HMP-PP (By similarity). FT BINDING 271 271 HMP-PP (By similarity). FT BINDING 298 298 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 343 AA; 37883 MW; 84BE7074EC082056 CRC64; MQQASPTAIA RILDANLNRA REGLRTVEEW CRFALENREL AEECKQLRQA LAPWHQDDLR AARDTPNDVG TQLTHAQEAL RTDVRALLQA NLCRVEEALR VLEEYGKLRD PAMGACCKQL RYRVYALESG LLGSKLVQRL QQCSLYLVTS PQENLLATVE AALQGGLKLV QYRDKDAEDQ LRWQRAKDLR ELCRQYEALF LVNDRVDLAL AVDADGVHLG QQDLPIAVAR QLLGPDKIIG RSTTNPEEMA KAIAEGADYI GVGPVYATPT KAGKKPAGLE YVQYAVTNSP VPWFAIGGID GENLGEVMEA GATQVAIVRA IMETTNPTQA TAQLLTQLSR INP // ID THIE_THEAC Reviewed; 213 AA. AC Q9HIQ4; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 14-MAY-2014, entry version 84. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Ta1277; OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / OS NBRC 15155 / AMRC-C165). OC Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales; OC Thermoplasmataceae; Thermoplasma. OX NCBI_TaxID=273075; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165; RX PubMed=11029001; DOI=10.1038/35035069; RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.; RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma RT acidophilum."; RL Nature 407:508-513(2000). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL445067; CAC12401.1; -; Genomic_DNA. DR RefSeq; NP_394734.1; NC_002578.1. DR ProteinModelPortal; Q9HIQ4; -. DR STRING; 273075.Ta1277; -. DR EnsemblBacteria; CAC12401; CAC12401; CAC12401. DR GeneID; 1456763; -. DR KEGG; tac:Ta1277; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 213 Thiamine-phosphate synthase. FT /FTId=PRO_0000157076. FT REGION 39 43 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 213 AA; 24009 MW; CFF4F00D69A9AE2A CRC64; MKLEGRRIKG LYLVTEDYSR KNFFNIIEEA IIGGVDIVQY RDKSNPRSVR LDVARKVKQI CNRYDILFFI DDDVQLAIEV QADGVHIGKD DMPLPDARRI FDGLIGYSTY GDREMAIFAE KNGADYVAFG PFFHTDTKKD ADVYDIHVLE GIHKYIRIPV FVIGGINISN IRTFSGYGID GVAVVSAIFS DPDPERAARE LKAALYNYVL SSA // ID THIE_THEEB Reviewed; 351 AA. AC Q8DHK2; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 14-MAY-2014, entry version 74. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=tlr1947; OS Thermosynechococcus elongatus (strain BP-1). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Thermosynechococcus. OX NCBI_TaxID=197221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BP-1; RX PubMed=12240834; DOI=10.1093/dnares/9.4.123; RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., RA Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the thermophilic cyanobacterium RT Thermosynechococcus elongatus BP-1."; RL DNA Res. 9:123-130(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAC09499.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000039; BAC09499.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_682737.1; NC_004113.1. DR ProteinModelPortal; Q8DHK2; -. DR STRING; 197221.tlr1947; -. DR PRIDE; Q8DHK2; -. DR EnsemblBacteria; BAC09499; BAC09499; BAC09499. DR GeneID; 1012088; -. DR KEGG; tel:tlr1947; -. DR PATRIC; 23929298; VBITheElo119873_2037. DR eggNOG; COG0352; -. DR HOGENOM; HOG000233097; -. DR KO; K00788; -. DR OMA; ANCARVQ; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR InterPro; IPR016229; TMP_synthase_cyanobac_bac. DR Pfam; PF02581; TMP-TENI; 1. DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 351 Thiamine-phosphate synthase. FT /FTId=PRO_0000157084. FT REGION 1 127 Unknown. FT REGION 128 351 Thiamine-phosphate synthase. FT REGION 178 182 HMP-PP binding (By similarity). FT REGION 275 277 THZ-P binding (By similarity). FT METAL 211 211 Magnesium (By similarity). FT METAL 230 230 Magnesium (By similarity). FT BINDING 210 210 HMP-PP (By similarity). FT BINDING 249 249 HMP-PP (By similarity). FT BINDING 278 278 HMP-PP (By similarity). FT BINDING 305 305 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 351 AA; 38829 MW; 50E8E21BBD12AEF4 CRC64; MQNLAPASEG QRLRRILDAN LDRAREGLRV IEEWCRFGRE DAALSAECKD LRQTLGRYHT EELRAARQTD QDPGTALSHP QERDRPTLNA VLTANFARVQ EALRVIEEYG KLTDTELSET AKALRYRVYI LEQALTLNPL QARLRQLQGA KLYLVTAPSD RLLEIVEAAL KGGLPLVQYR DKTSDDHTRL TTARQLQALC QRYGALFLVN DRVDIALGAN ADGVHLGQMD IPMELARQIL GRDRLVGRST TNAQELERAI AEGADYVGVG PIFATPTKPG KAAVGFDYLQ YARKHAPMPQ FAIGGIDLSN IEEVIKAGAT QVAVVRAIMA AADPEATTRE LLRRLSQGEP S // ID THIE_THEFY Reviewed; 218 AA. AC Q47R33; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 14-MAY-2014, entry version 63. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Tfu_1046; OS Thermobifida fusca (strain YX). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptosporangineae; Nocardiopsaceae; Thermobifida. OX NCBI_TaxID=269800; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YX; RX PubMed=17209016; DOI=10.1128/JB.01899-06; RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., RA DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A., RA Richardson P., Wilson D.B., Kyrpides N.; RT "Genome sequence and analysis of the soil cellulolytic actinomycete RT Thermobifida fusca YX."; RL J. Bacteriol. 189:2477-2486(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000088; AAZ55084.1; -; Genomic_DNA. DR RefSeq; YP_289107.1; NC_007333.1. DR ProteinModelPortal; Q47R33; -. DR STRING; 269800.Tfu_1046; -. DR EnsemblBacteria; AAZ55084; AAZ55084; Tfu_1046. DR GeneID; 3579598; -. DR KEGG; tfu:Tfu_1046; -. DR PATRIC; 23902582; VBITheFus33945_1091. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TFUS269800:GI42-1064-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 218 Thiamine-phosphate synthase. FT /FTId=PRO_1000008181. FT REGION 43 47 HMP-PP binding (By similarity). FT REGION 141 143 THZ-P binding (By similarity). FT METAL 76 76 Magnesium (By similarity). FT METAL 95 95 Magnesium (By similarity). FT BINDING 75 75 HMP-PP (By similarity). FT BINDING 114 114 HMP-PP (By similarity). FT BINDING 144 144 HMP-PP (By similarity). FT BINDING 172 172 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 218 AA; 23366 MW; 572900752D77A17C CRC64; MDETLRKRLE SARLYLCTDA RADRGDLAEF LDAALAGGVD IVQLRDKTLD ARDELAALEV VREACDRHGA LLAVNDRADI AHAVNADVLH LGQRDLPVRY ARAILGDRPL IGRSTNAAEL SAAADREEGV DYFCIGPVWA TPTKPGRPAA GLDEVARVAA LHPQRPWFAI GGINEDNLDQ VLAAGARRAV VVRAITEAED PRAAAAELKR RLVAAAAA // ID THIE_THET2 Reviewed; 206 AA. AC Q72KL8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 14-MAY-2014, entry version 66. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=TT_C0315; OS Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=262724; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HB27 / ATCC BAA-163 / DSM 7039; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., RA Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., RA Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., RA Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus RT thermophilus."; RL Nat. Biotechnol. 22:547-553(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017221; AAS80663.1; -; Genomic_DNA. DR RefSeq; YP_004290.1; NC_005835.1. DR ProteinModelPortal; Q72KL8; -. DR STRING; 262724.TTC0315; -. DR EnsemblBacteria; AAS80663; AAS80663; TT_C0315. DR GeneID; 2775542; -. DR KEGG; tth:TTC0315; -. DR PATRIC; 23951027; VBITheThe54392_0313. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; CTLLQYR; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TTHE262724:GCAT-324-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 206 Thiamine-phosphate synthase. FT /FTId=PRO_1000008182. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22529 MW; 7F7E9C6D5D15FC74 CRC64; MLGRLYLVVT PRPGWSLEAT LDRTERALAG GVEVVQLRAK DWEARPTLAL GERMLALARR YGVPFFLNDR PDLAALLGAD GVHLGQNDLT PEEARRFFAG MVGRSTHAPE QALRALEEGV DYLSVGPVWE TPTKPGRPAA GLAYVRWAAE NLGEKPWYAI GGIDLGNLDQ VLEAGARRIV VVRAILDAPD PERAARALRE RLYGVA // ID THIE_THET8 Reviewed; 206 AA. AC Q5SKG9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 14-MAY-2014, entry version 64. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=TTHA0674; OS Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HB8 / ATCC 27634 / DSM 579; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., RA Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008226; BAD70497.1; -; Genomic_DNA. DR RefSeq; YP_143940.1; NC_006461.1. DR ProteinModelPortal; Q5SKG9; -. DR STRING; 300852.TTHA0674; -. DR EnsemblBacteria; BAD70497; BAD70497; BAD70497. DR GeneID; 3169730; -. DR KEGG; ttj:TTHA0674; -. DR PATRIC; 23956325; VBITheThe93045_0668. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TTHE300852:GH8R-704-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 206 Thiamine-phosphate synthase. FT /FTId=PRO_1000008183. FT REGION 36 40 HMP-PP binding (By similarity). FT REGION 131 133 THZ-P binding (By similarity). FT METAL 69 69 Magnesium (By similarity). FT METAL 88 88 Magnesium (By similarity). FT BINDING 68 68 HMP-PP (By similarity). FT BINDING 105 105 HMP-PP (By similarity). FT BINDING 134 134 HMP-PP (By similarity). FT BINDING 162 162 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 206 AA; 22529 MW; 7F7E9C6D5D15FC74 CRC64; MLGRLYLVVT PRPGWSLEAT LDRTERALAG GVEVVQLRAK DWEARPTLAL GERMLALARR YGVPFFLNDR PDLAALLGAD GVHLGQNDLT PEEARRFFAG MVGRSTHAPE QALRALEEGV DYLSVGPVWE TPTKPGRPAA GLAYVRWAAE NLGEKPWYAI GGIDLGNLDQ VLEAGARRIV VVRAILDAPD PERAARALRE RLYGVA // ID THIE_THETN Reviewed; 214 AA. AC Q8R806; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 14-MAY-2014, entry version 75. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=TTE2233; OS Thermoanaerobacter tengcongensis (strain DSM 15242 / JCM 11007 / NBRC OS 100824 / MB4) (Caldanaerobacter subterraneus subsp. tengcongensis). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Caldanaerobacter. OX NCBI_TaxID=273068; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4; RX PubMed=11997336; DOI=10.1101/gr.219302; RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., RA Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., RA Tan H., Chen R., Wang J., Yu J., Yang H.; RT "A complete sequence of the T. tengcongensis genome."; RL Genome Res. 12:689-700(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAM25383.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008691; AAM25383.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_623779.1; NC_003869.1. DR ProteinModelPortal; Q8R806; -. DR STRING; 273068.TTE2233; -. DR EnsemblBacteria; AAM25383; AAM25383; TTE2233. DR GeneID; 997949; -. DR KEGG; tte:TTE2233; -. DR PATRIC; 23899195; VBITheTen82880_2232. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 214 Thiamine-phosphate synthase. FT /FTId=PRO_0000157059. FT REGION 38 42 HMP-PP binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23218 MW; EC629BAA9408D058 CRC64; MKRIDFTLYA ITDRSFIKGM DIAEAVEIAI KNGVTVVQLR EKDISSREFY EIALKVKEVT RKYNVPLIIN DRVDIALAVD AEGVHVGPDD LPVGVVRRIL GPDKIVGGSA YSVEEALKAE KEGADYIGAG SVFAQPVKPE AEVIGIEGVR KIKEAVNIPV VAIGGVNKTN AYEVILHSGV DGISAIAGIF DGDIEANTKD MLREIRRAFK ERGK // ID THIE_THEVO Reviewed; 211 AA. AC Q97BE8; DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 14-MAY-2014, entry version 82. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=TV0508; ORFNames=TVG0496174; OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC OS 15438 / GSS1). OC Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales; OC Thermoplasmataceae; Thermoplasma. OX NCBI_TaxID=273116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1; RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257; RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., RA Kawashima-Ohya Y., Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., RA Nunoshiba T., Yamamoto Y., Aramaki H., Makino K., Suzuki M.; RT "Archaeal adaptation to higher temperatures revealed by genomic RT sequence of Thermoplasma volcanium."; RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000011; BAB59650.1; -; Genomic_DNA. DR RefSeq; NP_111027.1; NC_002689.2. DR ProteinModelPortal; Q97BE8; -. DR STRING; 273116.TVN0508; -. DR EnsemblBacteria; BAB59650; BAB59650; BAB59650. DR GeneID; 1441024; -. DR KEGG; tvo:TVN0508; -. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR BioCyc; TVOL273116:GC31-527-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_0000157077. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 133 135 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 23300 MW; 0A05D787127C5D72 CRC64; MNEKKLRGLY LVTYDYYGAE FYEKIIDAIE GGVDILQYRD KTNAYSVKLQ VARKLTSIAA DYGIPFFVDD DPKLAKEAGA DGVHIGRDDP PIEQVRDVFN GLIGVSTYGN LELATEAEKK GASYVAFGSF FHTDTKKDAG IYDIKILEKA RHFVKIPIFV IGGINLETIT KFCGYSIDGI AVVSAILAAE NVKKAAKELK EKVEDIINGR C // ID THIE_THIDA Reviewed; 211 AA. AC Q3SFU7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 14-MAY-2014, entry version 58. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Tbd_2556; OS Thiobacillus denitrificans (strain ATCC 25259). OC Bacteria; Proteobacteria; Betaproteobacteria; Hydrogenophilales; OC Hydrogenophilaceae; Thiobacillus. OX NCBI_TaxID=292415; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25259; RX PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006; RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.; RT "The genome sequence of the obligately chemolithoautotrophic, RT facultatively anaerobic bacterium Thiobacillus denitrificans."; RL J. Bacteriol. 188:1473-1488(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000116; AAZ98509.1; -; Genomic_DNA. DR RefSeq; YP_316314.1; NC_007404.1. DR ProteinModelPortal; Q3SFU7; -. DR STRING; 292415.Tbd_2556; -. DR EnsemblBacteria; AAZ98509; AAZ98509; Tbd_2556. DR GeneID; 3672532; -. DR KEGG; tbd:Tbd_2556; -. DR PATRIC; 23971309; VBIThiDen82923_2541. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TDEN292415:GHWG-2606-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000008184. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 135 137 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 138 138 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 21891 MW; 6C7229DDBE02093C CRC64; MRTFPGGVYA LTRETPDTER LLAEVEAALA GGVAAVQYRD KSGDVAQRHA QASELAALCR RFGVPLIVND DLRLADLAGA DGVHLGRDDA SIREARIILG PAKFVGASCY QSLDLARAAQ TAGADYVAFG SFYPSPTKPA AARADVALLA RASRHIALPV VAIGGITAAN AAPLIDAGAD SLAVLSALFD APDVRRAAAE LNRLFAAEPE E // ID THIE_THISH Reviewed; 211 AA. AC B8GLE3; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 14-MAY-2014, entry version 39. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Tgr7_2420; OS Thioalkalivibrio sp. (strain HL-EbGR7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thioalkalivibrio. OX NCBI_TaxID=396588; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HL-EbGR7; RX PubMed=21475584; DOI=10.4056/sigs.1483693; RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., RA Ivanova N., Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.; RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL- RT EbGr7."; RL Stand. Genomic Sci. 4:23-35(2011). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001339; ACL73498.1; -; Genomic_DNA. DR RefSeq; YP_002514485.1; NC_011901.1. DR ProteinModelPortal; B8GLE3; -. DR STRING; 396588.Tgr7_2420; -. DR EnsemblBacteria; ACL73498; ACL73498; Tgr7_2420. DR GeneID; 7317122; -. DR KEGG; tgr:Tgr7_2420; -. DR PATRIC; 23964374; VBIThiSp19295_2408. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; QFREKGP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; TSUL396588:GH5B-2464-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000198083. FT REGION 41 45 HMP-PP binding (By similarity). FT REGION 139 141 THZ-P binding (By similarity). FT REGION 189 190 THZ-P binding (By similarity). FT METAL 74 74 Magnesium (By similarity). FT METAL 93 93 Magnesium (By similarity). FT BINDING 73 73 HMP-PP (By similarity). FT BINDING 112 112 HMP-PP (By similarity). FT BINDING 142 142 HMP-PP (By similarity). FT BINDING 169 169 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 22331 MW; 83D99904C6CD270F CRC64; MTETGERLRG LYAVTPDIPT DIEDLRARAE AVLRGGARLL QYRDKSADLP RREQAARALR ALCERHGALF IVNDDVALAL RVGAHGVHLG QQDMPLAEAR AMLGREAIIG ITCHERLDLA LSAQAAGADY VAFGAVYPSP TKPGAVRAPL PLFTEARETL SIPVCAIGGI EADNAAAVIA AGADMVAVVS GVFARPDPEA EARRLAAMFE V // ID THIE_UNCMA Reviewed; 212 AA. AC Q0W1L8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 14-MAY-2014, entry version 59. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=UNCMA_05320; ORFNames=RCIX2678; OS Uncultured methanogenic archaeon RC-I. OC Archaea; Euryarchaeota; Methanomicrobia; Methanocellales; OC Methanocellaceae; Methanocella. OX NCBI_TaxID=351160; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16857943; DOI=10.1126/science.1127062; RA Erkel C., Kube M., Reinhardt R., Liesack W.; RT "Genome of rice cluster I archaea -- the key methane producers in the RT rice rhizosphere."; RL Science 313:370-372(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM114193; CAJ37725.1; -; Genomic_DNA. DR RefSeq; YP_687051.1; NC_009464.1. DR ProteinModelPortal; Q0W1L8; -. DR STRING; 351160.RCIX2678; -. DR EnsemblBacteria; CAJ37725; CAJ37725; RCIX2678. DR GeneID; 5145458; -. DR KEGG; rci:RCIX2678; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR BioCyc; UMET351160:GJT4-546-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_0000336440. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 22551 MW; 6AAE1B4E7934083D CRC64; MQYDLYVVTD EGLSRGLTHP ELARRAIAGS ADVIQLRDKK CDCDYLLRCA MEMREDCNKA GVTFIVNDRL DVALQSQADG VHIGQSDMPL KFARRVAPKG FIIGVSAGTV EEALRAEHDG ADYIGFGPVF PTGSKADAGP VCGLDLLREV RRRVSIPVVA IGGINAANAP EVLAAGADGL AVISAVVSQE DVTAAARNLK AIISQYRLSG RQ // ID THIE_VIBCB Reviewed; 204 AA. AC A7N7S3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 1. DT 14-MAY-2014, entry version 44. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=VIBHAR_06844; OS Vibrio campbellii (strain ATCC BAA-1116 / BB120). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=338187; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1116 / BB120; RG The Vibrio harveyi Genome Sequencing Project; RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C., RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., RA Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., RA Irgon J., Wilson R.K.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000790; ABU74719.1; -; Genomic_DNA. DR RefSeq; YP_001448946.1; NC_009784.1. DR RefSeq; YP_008528249.1; NC_022270.1. DR ProteinModelPortal; A7N7S3; -. DR STRING; 338187.VIBHAR_06844; -. DR EnsemblBacteria; ABU74719; ABU74719; VIBHAR_06844. DR GeneID; 16817798; -. DR GeneID; 5557697; -. DR KEGG; vca:M892_18365; -. DR KEGG; vha:VIBHAR_06844; -. DR PATRIC; 20137743; VBIVibHar24526_5339. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; VHAR338187:GJCH-5830-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 204 Thiamine-phosphate synthase. FT /FTId=PRO_1000008185. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 22004 MW; 5F6063E23742426D CRC64; MNAYRLYLVT DDQQDLATLK RVVRKAVEGG VTMVQVREKH GDVRAFIERA QAVKDILKDT DVPLIINDRV DVALAVDADG VHLGQSDMPA TIARELIGPN KILGLSIENE EQLTEADSLP IDYIGLSAIF ATPTKTNTKK HWGIDGLKMA LETTSLPIVA IGGINESNIP QLSATGVHGL ALVSAICHAE DPKAASEYLL GLMR // ID THIE_VIBPA Reviewed; 204 AA. AC Q87JW8; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 23-MAY-2003, sequence version 1. DT 14-MAY-2014, entry version 77. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=VPA0130; OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=223926; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIMD 2210633; RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1; RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.; RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism RT distinct from that of V. cholerae."; RL Lancet 361:743-749(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000032; BAC61473.1; -; Genomic_DNA. DR RefSeq; NP_799640.1; NC_004605.1. DR ProteinModelPortal; Q87JW8; -. DR STRING; 223926.VPA0130; -. DR EnsemblBacteria; BAC61473; BAC61473; BAC61473. DR GeneID; 1190809; -. DR KEGG; vpa:VPA0130; -. DR PATRIC; 20144695; VBIVibPar50997_3090. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; VTDRTLC; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; VPAR223926:GHK4-3353-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 204 Thiamine-phosphate synthase. FT /FTId=PRO_0000157060. FT REGION 35 39 HMP-PP binding (By similarity). FT REGION 132 134 THZ-P binding (By similarity). FT REGION 183 184 THZ-P binding (By similarity). FT METAL 68 68 Magnesium (By similarity). FT METAL 87 87 Magnesium (By similarity). FT BINDING 67 67 HMP-PP (By similarity). FT BINDING 106 106 HMP-PP (By similarity). FT BINDING 135 135 HMP-PP (By similarity). FT BINDING 163 163 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 204 AA; 21796 MW; 30ED16DCD5F62066 CRC64; MNAYRLYLVT DDQQDLPTLK HVVRKAVEGG VTMVQVREKH GDVREFIERA QAVKTILEGT GVPLIINDRV DVALAVDADG VHLGQSDMPA EIARQLIGPN KILGLSIETE DQLAEADSLP IDYIGLSAIF ATPTKTNTKK HWGIGGLKMA LNTTSLPIVA IGGINETNIP ALSATGVHGL ALVSAICHAE NPTKAAEYLL SLMD // ID THIE_WOLSU Reviewed; 214 AA. AC Q7M9N9; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 14-MAY-2014, entry version 69. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=WS0788; OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC OS 11488 / FDC 602W) (Vibrio succinogenes). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Wolinella. OX NCBI_TaxID=273121; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W; RX PubMed=14500908; DOI=10.1073/pnas.1932838100; RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., RA Meyer F., Lederer H., Schuster S.C.; RT "Complete genome sequence and analysis of Wolinella succinogenes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571659; CAE09902.1; -; Genomic_DNA. DR RefSeq; NP_907002.1; NC_005090.1. DR ProteinModelPortal; Q7M9N9; -. DR STRING; 273121.WS0788; -. DR EnsemblBacteria; CAE09902; CAE09902; WS0788. DR GeneID; 2554647; -. DR KEGG; wsu:WS0788; -. DR PATRIC; 24038626; VBIWolSuc63014_0743. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; ITTHNAS; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 214 Thiamine-phosphate synthase. FT /FTId=PRO_0000157061. FT REGION 40 44 HMP-PP binding (By similarity). FT REGION 137 139 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 73 73 Magnesium (By similarity). FT METAL 92 92 Magnesium (By similarity). FT BINDING 72 72 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 140 140 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 214 AA; 23532 MW; 9C60683F5109BF0F CRC64; MQDMRLQGLY GISESGWYKR PHEAIELLLE AIEGGMKIFQ LREKEGSDEE ILPLARALWN HCRQKGVLFI LNDRLDLALS LGVDGVHLGI DDAEASRARI LLPHGIIGIS CYGDLDRAHK AKEEGASYVA FGSCFPSPTK PASSVIDLTL FKKAQEELAI PLCAIGGIEA QNVGELIHCD MIAVISSLWS GGVAQVRKNA KGLIQSWREN RERV // ID THIE_XANAC Reviewed; 212 AA. AC Q8PH45; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 14-MAY-2014, entry version 77. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=XAC3415; OS Xanthomonas axonopodis pv. citri (strain 306). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190486; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008923; AAM38258.1; -; Genomic_DNA. DR RefSeq; NP_643722.1; NC_003919.1. DR ProteinModelPortal; Q8PH45; -. DR STRING; 190486.XAC3415; -. DR EnsemblBacteria; AAM38258; AAM38258; XAC3415. DR GeneID; 1157486; -. DR KEGG; xac:XAC3415; -. DR PATRIC; 24058969; VBIXanAxo33670_3536. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XAXO190486:GH55-3415-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 212 Thiamine-phosphate synthase. FT /FTId=PRO_0000157062. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 212 AA; 21988 MW; A88AA9C5CC6FA12E CRC64; MPNRPNVRGV YLITPDEPNT QRLLLRTAPL LGSITWLQYR NKQADAALRL RQAGALREAC AAHGVPLIIN DDAQLAAQVG AQGVHLGEDD GDVAAARALL GEQAIIGVSC YDDIERGRAA AASGASYVAF GAFFPTTTKQ TTRRATPALL QQAAELDVPR VAIGGIAPAQ VPALVTAGAD LIAVVSGVYA APDPVAAVQG YRAGFAAQRG KL // ID THIE_XANC8 Reviewed; 207 AA. AC Q4UYA4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 14-MAY-2014, entry version 61. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=XC_0895; OS Xanthomonas campestris pv. campestris (strain 8004). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=314565; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8004; RX PubMed=15899963; DOI=10.1101/gr.3378705; RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., RA Zeng S., Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., RA Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.; RT "Comparative and functional genomic analyses of the pathogenicity of RT phytopathogen Xanthomonas campestris pv. campestris."; RL Genome Res. 15:757-767(2005). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000050; AAY47969.1; -; Genomic_DNA. DR RefSeq; YP_241989.1; NC_007086.1. DR ProteinModelPortal; Q4UYA4; -. DR STRING; 314565.XC_0895; -. DR EnsemblBacteria; AAY47969; AAY47969; XC_0895. DR GeneID; 3382580; -. DR KEGG; xcb:XC_0895; -. DR PATRIC; 24063115; VBIXanCam24967_0967. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XCAM314565:GCQG-893-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_1000008186. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21236 MW; F7B53E5CB4985770 CRC64; MPTLQNARGV YLITPDTRDT AQLLACTLPL LPHITWLQYR NKQADAALRL AQATALRAAC TAHGVPLIIN DDAALAQQVG ADGVHLGEDD GEVAAARALL GASAIIGVSC YDEIERARAA AAAGANYVAF GAFFPTATKV TTRRATPALL HEAAALGLPR VAIGGITPSQ VPELVTAGAD LIAVVSGVYA AADPVAAVQA YRAGFTQ // ID THIE_XANCP Reviewed; 207 AA. AC Q8P5R7; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 14-MAY-2014, entry version 75. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=XCC3269; OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / OS LMG 568). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190485; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / NCPPB 528 / LMG 568; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008922; AAM42539.1; -; Genomic_DNA. DR RefSeq; NP_638615.1; NC_003902.1. DR ProteinModelPortal; Q8P5R7; -. DR STRING; 190485.XCC3269; -. DR EnsemblBacteria; AAM42539; AAM42539; XCC3269. DR GeneID; 999453; -. DR KEGG; xcc:XCC3269; -. DR PATRIC; 24077611; VBIXanCam115730_3492. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; KEDVCAP; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XCAM190485:GIXZ-3267-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 207 Thiamine-phosphate synthase. FT /FTId=PRO_0000157063. FT REGION 38 42 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 185 186 THZ-P binding (By similarity). FT METAL 71 71 Magnesium (By similarity). FT METAL 90 90 Magnesium (By similarity). FT BINDING 70 70 HMP-PP (By similarity). FT BINDING 109 109 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 165 165 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 207 AA; 21236 MW; F7B53E5CB4985770 CRC64; MPTLQNARGV YLITPDTRDT AQLLACTLPL LPHITWLQYR NKQADAALRL AQATALRAAC TAHGVPLIIN DDAALAQQVG ADGVHLGEDD GEVAAARALL GASAIIGVSC YDEIERARAA AAAGANYVAF GAFFPTATKV TTRRATPALL HEAAALGLPR VAIGGITPSQ VPELVTAGAD LIAVVSGVYA AADPVAAVQA YRAGFTQ // ID THIE_XANP2 Reviewed; 211 AA. AC A7IGG9; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 49. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=Xaut_1867; OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Xanthobacter. OX NCBI_TaxID=78245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1158 / Py2; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., RA Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Ensigns S.A., Richardson P.; RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000781; ABS67112.1; -; Genomic_DNA. DR RefSeq; YP_001416769.1; NC_009720.1. DR ProteinModelPortal; A7IGG9; -. DR STRING; 78245.Xaut_1867; -. DR EnsemblBacteria; ABS67112; ABS67112; Xaut_1867. DR GeneID; 5423806; -. DR KEGG; xau:Xaut_1867; -. DR PATRIC; 24045787; VBIXanAut29526_2188. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; CTGPVWA; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XAUT78245:GHS6-1884-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 211 Thiamine-phosphate synthase. FT /FTId=PRO_1000093692. FT REGION 39 41 HMP-PP binding (By similarity). FT REGION 136 138 THZ-P binding (By similarity). FT REGION 187 188 THZ-P binding (By similarity). FT METAL 72 72 Magnesium (By similarity). FT METAL 91 91 Magnesium (By similarity). FT BINDING 71 71 HMP-PP (By similarity). FT BINDING 110 110 HMP-PP (By similarity). FT BINDING 139 139 HMP-PP (By similarity). FT BINDING 167 167 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 211 AA; 20959 MW; 3BDD5F1402E7F7D9 CRC64; MPKPFDLTLY LVTDPRLVAA RGLLTTVDAA VKGGATIVQL RDPDAHGRAL VEQARALKAL LAPLGIPLII NDRVDVAVAA DADGVHLGQD DMTPADARAV LGPQRILGLS VGNPAEYAAS DLSGVDYLGV GPVKATGTKA DAGGAIGAAG VGAVRALTRL PLVGIGGLAT ADVADVIRAG ADGVAVVSSI CAASDPEQAA RALKAAVLAA R // ID THIE_XYLFA Reviewed; 234 AA. AC Q9PGC4; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 14-MAY-2014, entry version 77. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=XF_0378; OS Xylella fastidiosa (strain 9a5c). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=160492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9a5c; RX PubMed=10910347; DOI=10.1038/35018003; RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H., RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., RA Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., RA Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., RA Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., RA Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., RA Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., RA Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., RA Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., RA Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., RA Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., RA Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., RA Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., RA Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., RA de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., RA da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., RA da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., RA de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., RA Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., RA Zago M.A., Zatz M., Meidanis J., Setubal J.C.; RT "The genome sequence of the plant pathogen Xylella fastidiosa."; RL Nature 406:151-159(2000). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE003849; AAF83188.1; -; Genomic_DNA. DR PIR; A82814; A82814. DR RefSeq; NP_297668.1; NC_002488.3. DR ProteinModelPortal; Q9PGC4; -. DR STRING; 160492.XF0378; -. DR EnsemblBacteria; AAF83188; AAF83188; XF_0378. DR GeneID; 1125906; -. DR KEGG; xfa:XF0378; -. DR PATRIC; 24130711; VBIXylFas578_0402. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 234 Thiamine-phosphate synthase. FT /FTId=PRO_0000157064. FT REGION 65 69 HMP-PP binding (By similarity). FT REGION 163 165 THZ-P binding (By similarity). FT REGION 212 213 THZ-P binding (By similarity). FT METAL 98 98 Magnesium (By similarity). FT METAL 117 117 Magnesium (By similarity). FT BINDING 97 97 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 166 166 HMP-PP (By similarity). FT BINDING 192 192 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 234 AA; 25334 MW; 006FDE3ADF0E6A1B CRC64; MEVSRIGSFQ EHIDKTTGIV TPHPLLRKPL MSQPRGIYLI TPDETDTARL IARTAPLLNG IVWLQYRNKL ANTALRTEQA QALLALCRQT GIPLLINDDL ELAQTIGADG VHLGMHDSNP SIARAQLGPH AIIGVSCYNQ IERAKQAIKA GASYVGFGTF YPSHTKTTPY RATPELLRQT THLGVPRVAI GGLTPKNIAP IIEAGAELLA VISGIYSAKN PVTALKAYQS QFNI // ID THIE_XYLFT Reviewed; 234 AA. AC Q87AX6; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 74. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=PD_1687; OS Xylella fastidiosa (strain Temecula1 / ATCC 700964). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=183190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Temecula1 / ATCC 700964; RX PubMed=12533478; DOI=10.1128/JB.185.3.1018-1026.2003; RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., RA Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., RA Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., RA Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., RA Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., RA Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., RA Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., RA Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., RA da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., RA Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., RA de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., RA Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., RA Kitajima J.P.; RT "Comparative analyses of the complete genome sequences of Pierce's RT disease and citrus variegated chlorosis strains of Xylella RT fastidiosa."; RL J. Bacteriol. 185:1018-1026(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE009442; AAO29525.1; -; Genomic_DNA. DR RefSeq; NP_779876.1; NC_004556.1. DR ProteinModelPortal; Q87AX6; -. DR STRING; 183190.PD1687; -. DR EnsemblBacteria; AAO29525; AAO29525; PD_1687. DR GeneID; 1143029; -. DR KEGG; xft:PD1687; -. DR PATRIC; 24151752; VBIXylFas71109_2177. DR eggNOG; COG0352; -. DR KO; K00788; -. DR OMA; IIGVTTH; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; XFAS183190:GIX4-1687-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 234 Thiamine-phosphate synthase. FT /FTId=PRO_0000157065. FT REGION 65 69 HMP-PP binding (By similarity). FT REGION 163 165 THZ-P binding (By similarity). FT REGION 212 213 THZ-P binding (By similarity). FT METAL 98 98 Magnesium (By similarity). FT METAL 117 117 Magnesium (By similarity). FT BINDING 97 97 HMP-PP (By similarity). FT BINDING 136 136 HMP-PP (By similarity). FT BINDING 166 166 HMP-PP (By similarity). FT BINDING 192 192 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 234 AA; 25243 MW; 2A44EAB00D44BC72 CRC64; MEVSSIGSFQ EHIDKTTDIV TLHPLLRNPI MPQPRGIYLI TPDETDTARL IAHTAPLLNG IVWLQYRNKL ANTALRTEQA QALLALCRPT GIPLLINDDL ELAQTIGADG VHLGMHDSNA SIARAQLGPH AIIGVSCYNQ IERAKQAIKA GASYVGFGAF YPSHTKTTPY RATPELLRQT THLGVPRVAI GGLTPKNIAP IIEAGAELLA VISGIYSAKN PITALKAYQS QFNI // ID THIE_YERP3 Reviewed; 215 AA. AC A7FNH7; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 14-MAY-2014, entry version 47. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=YpsIP31758_3854; OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=349747; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP 31758; RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142; RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G., RA Fayolle C., Lindler L.E., Carniel E., Ravel J.; RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, RT the causative agent of Far East scarlet-like fever."; RL PLoS Genet. 3:1508-1523(2007). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000720; ABS47924.1; -; Genomic_DNA. DR RefSeq; YP_001402805.1; NC_009708.1. DR ProteinModelPortal; A7FNH7; -. DR STRING; 349747.YpsIP31758_3854; -. DR EnsemblBacteria; ABS47924; ABS47924; YpsIP31758_3854. DR GeneID; 5386729; -. DR KEGG; ypi:YpsIP31758_3854; -. DR PATRIC; 18636989; VBIYerPse15693_4392. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; YPSE349747:GH71-3953-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 215 Thiamine-phosphate synthase. FT /FTId=PRO_1000057647. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23305 MW; EE4A7D570AA52574 CRC64; MATPGFPSTE QRLGLYPVVD SLLWIERLLA AGVTTLQLRI KNADDAQVEQ DIVAAIELGK RYQARLFIND YWQLAVKHGA YGVHLGQEDL ETADLAAIQQ AGLRLGISTH DEHELAVAKT LRPSYIALGH IFPTQTKQMP SSPQGLASLS RQVKNTPDYP TVAIGGISIE RVPHVLATGV GSVAVVSAIT LASDWQRATA QLLHLIEGKE LADEK // ID THIE_YERPA Reviewed; 215 AA. AC Q1C1U8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 14-MAY-2014, entry version 54. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=YPA_3612; OS Yersinia pestis bv. Antiqua (strain Antiqua). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=360102; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Antiqua; RX PubMed=16740952; DOI=10.1128/JB.00124-06; RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., RA Vergez L.M., Worsham P., Chu M.C., Andersen G.L.; RT "Complete genome sequence of Yersinia pestis strains Antiqua and RT Nepal516: evidence of gene reduction in an emerging pathogen."; RL J. Bacteriol. 188:4453-4463(2006). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=ABG15574.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000308; ABG15574.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_653519.1; NC_008150.1. DR ProteinModelPortal; Q1C1U8; -. DR STRING; 360102.YPA_3612; -. DR EnsemblBacteria; ABG15574; ABG15574; YPA_3612. DR GeneID; 4118386; -. DR KEGG; ypa:YPA_3612; -. DR PATRIC; 18587209; VBIYerPes1796_4386. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; YPES360102:GHZU-3698-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 215 Thiamine-phosphate synthase. FT /FTId=PRO_0000336431. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23275 MW; EE560D5E7AB02574 CRC64; MATPGFPSTE QRLGLYPVVD SLLWIERLLA AGVTTLQLRI KNADDAQVEQ DIVAAIELGK RYQARLFIND YWQLAVKHGA YGVHLGQEDL EAADLAAIQQ AGLRLGISTH DEHELAVAKT LRPSYIALGH IFPTQTKQMP SSPQGLASLS RQVKNTPDYP TVAIGGISIE RVPHVLATGV GSVAVVSAIT LASDWQRATA QLLHLIEGKE LADEK // ID THIE_YERPE Reviewed; 215 AA. AC Q8ZAQ1; Q0WAR8; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 14-MAY-2014, entry version 95. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=YPO3740, y0490, YP_3103; OS Yersinia pestis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=632; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO-92 / Biovar Orientalis; RX PubMed=11586360; DOI=10.1038/35097083; RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., RA Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., RA Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., RA Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.; RT "Genome sequence of Yersinia pestis, the causative agent of plague."; RL Nature 413:523-527(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIM10+ / Biovar Mediaevalis; RX PubMed=12142430; DOI=10.1128/JB.184.16.4601-4611.2002; RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., RA Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., RA Straley S.C., McDonough K.A., Nilles M.L., Matson J.S., Blattner F.R., RA Perry R.D.; RT "Genome sequence of Yersinia pestis KIM."; RL J. Bacteriol. 184:4601-4611(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=91001 / Biovar Mediaevalis; RX PubMed=15368893; DOI=10.1093/dnares/11.3.179; RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., RA Jin L., Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., RA Yang H., Wang J., Huang P., Yang R.; RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate RT avirulent to humans."; RL DNA Res. 11:179-197(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAM84079.1; Type=Erroneous initiation; CC Sequence=AAS63273.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL590842; CAL22327.1; -; Genomic_DNA. DR EMBL; AE009952; AAM84079.1; ALT_INIT; Genomic_DNA. DR EMBL; AE017042; AAS63273.1; ALT_INIT; Genomic_DNA. DR PIR; AD0455; AD0455. DR RefSeq; NP_667828.1; NC_004088.1. DR RefSeq; NP_994396.1; NC_005810.1. DR RefSeq; YP_002348620.1; NC_003143.1. DR ProteinModelPortal; Q8ZAQ1; -. DR IntAct; Q8ZAQ1; 1. DR STRING; 214092.YPO3740; -. DR DNASU; 1145437; -. DR EnsemblBacteria; AAM84079; AAM84079; y0490. DR EnsemblBacteria; AAS63273; AAS63273; YP_3103. DR GeneID; 1145437; -. DR GeneID; 1176566; -. DR GeneID; 2766734; -. DR KEGG; ype:YPO3740; -. DR KEGG; ypk:y0490; -. DR KEGG; ypm:YP_3103; -. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; YPES214092:GKDD-3703-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 215 Thiamine-phosphate synthase. FT /FTId=PRO_0000157066. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23275 MW; EE560D5E7AB02574 CRC64; MATPGFPSTE QRLGLYPVVD SLLWIERLLA AGVTTLQLRI KNADDAQVEQ DIVAAIELGK RYQARLFIND YWQLAVKHGA YGVHLGQEDL EAADLAAIQQ AGLRLGISTH DEHELAVAKT LRPSYIALGH IFPTQTKQMP SSPQGLASLS RQVKNTPDYP TVAIGGISIE RVPHVLATGV GSVAVVSAIT LASDWQRATA QLLHLIEGKE LADEK // ID THIE_YERPN Reviewed; 215 AA. AC Q1CN71; C4GNF3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 14-MAY-2014, entry version 54. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=YPN_0226; ORFNames=YP516_0204; OS Yersinia pestis bv. Antiqua (strain Nepal516). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=377628; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nepal516; RX PubMed=16740952; DOI=10.1128/JB.00124-06; RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., RA Vergez L.M., Worsham P., Chu M.C., Andersen G.L.; RT "Complete genome sequence of Yersinia pestis strains Antiqua and RT Nepal516: evidence of gene reduction in an emerging pathogen."; RL J. Bacteriol. 188:4453-4463(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L., RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., RA Tapia R., Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., RA Brettin T.S.; RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=ABG16559.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000305; ABG16559.1; ALT_INIT; Genomic_DNA. DR EMBL; ACNQ01000004; EEO78477.1; -; Genomic_DNA. DR RefSeq; YP_646159.1; NC_008149.1. DR ProteinModelPortal; Q1CN71; -. DR STRING; 377628.YPN_0226; -. DR EnsemblBacteria; ABG16559; ABG16559; YPN_0226. DR EnsemblBacteria; EEO78477; EEO78477; YP516_0204. DR GeneID; 4124155; -. DR KEGG; ypn:YPN_0226; -. DR PATRIC; 18599399; VBIYerPes46733_0389. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; YPES377628:GIXK-252-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 215 Thiamine-phosphate synthase. FT /FTId=PRO_0000336432. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23275 MW; EE560D5E7AB02574 CRC64; MATPGFPSTE QRLGLYPVVD SLLWIERLLA AGVTTLQLRI KNADDAQVEQ DIVAAIELGK RYQARLFIND YWQLAVKHGA YGVHLGQEDL EAADLAAIQQ AGLRLGISTH DEHELAVAKT LRPSYIALGH IFPTQTKQMP SSPQGLASLS RQVKNTPDYP TVAIGGISIE RVPHVLATGV GSVAVVSAIT LASDWQRATA QLLHLIEGKE LADEK // ID THIE_YERPP Reviewed; 215 AA. AC A4TS25; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 14-MAY-2014, entry version 46. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=YPDSF_3737; OS Yersinia pestis (strain Pestoides F). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=386656; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pestoides F; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., RA Schmutz J., Larimer F., Land M., Hauser L., Worsham P., Chu M., RA Bearden S., Garcia E., Richardson P.; RT "Complete sequence of chromosome of Yersinia pestis Pestoides F."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC -!- SEQUENCE CAUTION: CC Sequence=ABP42087.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000668; ABP42087.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_001165060.1; NC_009381.1. DR ProteinModelPortal; A4TS25; -. DR STRING; 386656.YPDSF_3737; -. DR EnsemblBacteria; ABP42087; ABP42087; YPDSF_3737. DR GeneID; 5063076; -. DR KEGG; ypp:YPDSF_3737; -. DR PATRIC; 18617573; VBIYerPes122972_4638. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; YPES386656:GKD7-3829-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 215 Thiamine-phosphate synthase. FT /FTId=PRO_0000336433. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23275 MW; EE560D5E7AB02574 CRC64; MATPGFPSTE QRLGLYPVVD SLLWIERLLA AGVTTLQLRI KNADDAQVEQ DIVAAIELGK RYQARLFIND YWQLAVKHGA YGVHLGQEDL EAADLAAIQQ AGLRLGISTH DEHELAVAKT LRPSYIALGH IFPTQTKQMP SSPQGLASLS RQVKNTPDYP TVAIGGISIE RVPHVLATGV GSVAVVSAIT LASDWQRATA QLLHLIEGKE LADEK // ID THIE_YERPS Reviewed; 215 AA. AC Q66FP6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 65. DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; OrderedLocusNames=YPTB0289; OS Yersinia pseudotuberculosis serotype I (strain IP32953). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=273123; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP32953; RX PubMed=15358858; DOI=10.1073/pnas.0404012101; RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M., RA Derbise A., Hauser L.J., Garcia E.; RT "Insights into the evolution of Yersinia pestis through whole-genome RT comparison with Yersinia pseudotuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX936398; CAH19529.1; -; Genomic_DNA. DR RefSeq; YP_068835.1; NC_006155.1. DR ProteinModelPortal; Q66FP6; -. DR STRING; 273123.YPTB0289; -. DR EnsemblBacteria; CAH19529; CAH19529; YPTB0289. DR GeneID; 2956690; -. DR KEGG; yps:YPTB0289; -. DR PATRIC; 18638707; VBIYerPse22266_0457. DR eggNOG; COG0352; -. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; GRSTHEP; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; YPSE273123:GI1M-315-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 215 Thiamine-phosphate synthase. FT /FTId=PRO_1000008187. FT REGION 37 41 HMP-PP binding (By similarity). FT REGION 134 136 THZ-P binding (By similarity). FT REGION 186 187 THZ-P binding (By similarity). FT METAL 70 70 Magnesium (By similarity). FT METAL 89 89 Magnesium (By similarity). FT BINDING 69 69 HMP-PP (By similarity). FT BINDING 108 108 HMP-PP (By similarity). FT BINDING 137 137 HMP-PP (By similarity). FT BINDING 166 166 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 215 AA; 23305 MW; EE4A7D570AA52574 CRC64; MATPGFPSTE QRLGLYPVVD SLLWIERLLA AGVTTLQLRI KNADDAQVEQ DIVAAIELGK RYQARLFIND YWQLAVKHGA YGVHLGQEDL ETADLAAIQQ AGLRLGISTH DEHELAVAKT LRPSYIALGH IFPTQTKQMP SSPQGLASLS RQVKNTPDYP TVAIGGISIE RVPHVLATGV GSVAVVSAIT LASDWQRATA QLLHLIEGKE LADEK // ID THIME_SYMTH Reviewed; 480 AA. AC Q67T51; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 14-MAY-2014, entry version 69. DE RecName: Full=Thiamine biosynthesis bifunctional protein ThiM/ThiE; DE Includes: DE RecName: Full=Hydroxyethylthiazole kinase; DE EC=2.7.1.50; DE AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase; DE Short=TH kinase; DE Short=Thz kinase; DE Includes: DE RecName: Full=Thiamine-phosphate synthase; DE Short=TMP-PPase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; GN Name=thiM/thiE; OrderedLocusNames=STH157; OS Symbiobacterium thermophilum (strain T / IAM 14863). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XVIII. Incertae Sedis; Symbiobacterium. OX NCBI_TaxID=292459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T / IAM 14863; RX PubMed=15383646; DOI=10.1093/nar/gkh830; RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., RA Morimura K., Ikeda H., Hattori M., Beppu T.; RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable RT bacterium that depends on microbial commensalism."; RL Nucleic Acids Res. 32:4937-4944(2004). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP) (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- CATALYTIC ACTIVITY: 2-methyl-4-amino-5-hydroxymethylpyrimidine CC diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = CC diphosphate + thiamine phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: In the N-terminal section; belongs to the Thz kinase CC family. CC -!- SIMILARITY: In the C-terminal section; belongs to the thiamine- CC phosphate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006840; BAD39142.1; -; Genomic_DNA. DR RefSeq; YP_073986.1; NC_006177.1. DR ProteinModelPortal; Q67T51; -. DR STRING; 292459.STH157; -. DR EnsemblBacteria; BAD39142; BAD39142; STH157. DR GeneID; 2981020; -. DR KEGG; sth:STH157; -. DR PATRIC; 23778373; VBISymThe116959_0158. DR eggNOG; COG0352; -. DR HOGENOM; HOG000097679; -. DR OMA; RECKEND; -. DR OrthoDB; EOG628F8M; -. DR BioCyc; STHE292459:GJMM-173-MONOMER; -. DR UniPathway; UPA00060; UER00139. DR UniPathway; UPA00060; UER00141. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02110; HK; 1. DR Pfam; PF02581; TMP-TENI; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 480 Thiamine biosynthesis bifunctional FT protein ThiM/ThiE. FT /FTId=PRO_0000383912. FT REGION 1 287 Hydroxyethylthiazole kinase. FT REGION 288 480 Thiamine-phosphate synthase. FT REGION 303 307 HMP-PP binding (By similarity). FT REGION 400 402 THZ-P binding (By similarity). FT REGION 451 452 THZ-P binding (By similarity). FT METAL 336 336 Magnesium (By similarity). FT METAL 355 355 Magnesium (By similarity). FT BINDING 40 40 4-methyl-5-(2-hydroxyethyl)thiazole; via FT amide nitrogen (By similarity). FT BINDING 116 116 ATP (By similarity). FT BINDING 164 164 ATP (By similarity). FT BINDING 191 191 4-methyl-5-(2-hydroxyethyl)thiazole; via FT amide nitrogen (By similarity). FT BINDING 335 335 HMP-PP (By similarity). FT BINDING 374 374 HMP-PP (By similarity). FT BINDING 403 403 HMP-PP (By similarity). FT BINDING 431 431 THZ-P; via amide nitrogen (By FT similarity). SQ SEQUENCE 480 AA; 48683 MW; 0FEC441B02894F29 CRC64; MSTLPERVRE RRPLVHAITN CVTMEWVARG LLAAGARPVM ARDAAEAPVV AAAADALVLN LGTWSPGLQQ AMLEAGQVAA RRGIPVVLDP VGAGGTETRT RAALELLERV RVTAVRGNAG EILALAGRDG LVRGVDGPDG RPGPQTERAA RAVARRFGCL VAVTGATDLV TDGRRTLAVR AGHPLMSQVP GTGCLATALV AAALAAGTGA GPAGRDRPME DVDVVAEALL WAGWAGEQAA SAASGPGTFA AAFLDRLALR GPLPPGRIAP PLSERLSLYV LVSGATPPDV LEAVLQAGCR MIQFREKRLP LPAQLEAAAR VREACRRHGA LLVVNDRVDL ALAVGADGVH LGQEDLPVAA ARRILGPDAV IGATCETAGE ARAARDAGAD YIGAGPVYVT PSKPDAGEPY GPDVVRRVSE AADLPVVGIG GIGPGRAAPV IAAGAAGVAV ISAVLGAPDP GAAARAILDE VRRAKGEVSA //